data_9BY1
# 
_entry.id   9BY1 
# 
_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   9BY1         pdb_00009by1 10.2210/pdb9by1/pdb 
WWPDB D_1000284359 ?            ?                   
EMDB  EMD-45017    ?            ?                   
# 
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                        9BY1 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-23 
_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 product condition of Bacillus subtilis ribonucleotide reductase complex' 
_pdbx_database_related.db_id          EMD-45017 
_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 ?        ? ? ? 
6 non-polymer syn "2'-DEOXYGUANOSINE-5'-DIPHOSPHATE"                   427.201   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 
6 "2'-DEOXYGUANOSINE-5'-DIPHOSPHATE" DGI 
# 
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 
DGI 'DNA linking'       n "2'-DEOXYGUANOSINE-5'-DIPHOSPHATE" ? 'C10 H15 N5 O10 P2' 427.201 
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 330 309 309 LYS LYS C . n 
C 2 331 ALA 331 310 310 ALA ALA 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 330 309 309 LYS LYS D . n 
D 2 331 ALA 331 310 310 ALA ALA 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_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 ATP ? ? ATP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 MG  ? ? MG  ? ? 'SUBJECT OF INVESTIGATION' ? 
3 DGI ? ? DGI ? ? 'SUBJECT OF INVESTIGATION' ? 
4 TTP ? ? TTP ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 6 DGI 1 804 804 DGI DGI A . 
I 3 TTP 1 801 801 TTP TTP B . 
J 4 MG  1 802 802 MG  MG  B . 
K 5 ATP 1 803 803 ATP ATP B . 
L 6 DGI 1 804 804 DGI DGI 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                     9BY1 
_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                         9BY1 
_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                   9BY1 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9BY1 
_refine.pdbx_diffrn_id                           ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            . 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
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' ? 0.003 ? 11776 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.472 ? 15904 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 9.923 ? 1608  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.039 ? 1688  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.003 ? 2032  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9BY1 
_struct.title                        'Consensus model for product 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        9BY1 
_struct_keywords.text            'Ribonucleotide Reductase, 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 6 ? 
I N N 3 ? 
J N N 4 ? 
K N N 5 ? 
L N N 6 ? 
# 
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 9BY1 A 1  ? 700 ? P50620 1 ? 700 ? 1 700 
2 1 9BY1 B 1  ? 700 ? P50620 1 ? 700 ? 1 700 
3 2 9BY1 C 22 ? 350 ? P50621 1 ? 329 ? 1 329 
4 2 9BY1 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 9BY1 MET C 1  ? UNP P50621 ? ? 'initiating methionine' -20 1  
3 9BY1 GLY C 2  ? UNP P50621 ? ? 'expression tag'        -19 2  
3 9BY1 SER C 3  ? UNP P50621 ? ? 'expression tag'        -18 3  
3 9BY1 SER C 4  ? UNP P50621 ? ? 'expression tag'        -17 4  
3 9BY1 HIS C 5  ? UNP P50621 ? ? 'expression tag'        -16 5  
3 9BY1 HIS C 6  ? UNP P50621 ? ? 'expression tag'        -15 6  
3 9BY1 HIS C 7  ? UNP P50621 ? ? 'expression tag'        -14 7  
3 9BY1 HIS C 8  ? UNP P50621 ? ? 'expression tag'        -13 8  
3 9BY1 HIS C 9  ? UNP P50621 ? ? 'expression tag'        -12 9  
3 9BY1 HIS C 10 ? UNP P50621 ? ? 'expression tag'        -11 10 
3 9BY1 SER C 11 ? UNP P50621 ? ? 'expression tag'        -10 11 
3 9BY1 SER C 12 ? UNP P50621 ? ? 'expression tag'        -9  12 
3 9BY1 GLY C 13 ? UNP P50621 ? ? 'expression tag'        -8  13 
3 9BY1 LEU C 14 ? UNP P50621 ? ? 'expression tag'        -7  14 
3 9BY1 VAL C 15 ? UNP P50621 ? ? 'expression tag'        -6  15 
3 9BY1 PRO C 16 ? UNP P50621 ? ? 'expression tag'        -5  16 
3 9BY1 ARG C 17 ? UNP P50621 ? ? 'expression tag'        -4  17 
3 9BY1 GLY C 18 ? UNP P50621 ? ? 'expression tag'        -3  18 
3 9BY1 SER C 19 ? UNP P50621 ? ? 'expression tag'        -2  19 
3 9BY1 HIS C 20 ? UNP P50621 ? ? 'expression tag'        -1  20 
3 9BY1 MET C 21 ? UNP P50621 ? ? 'expression tag'        0   21 
4 9BY1 MET D 1  ? UNP P50621 ? ? 'initiating methionine' -20 22 
4 9BY1 GLY D 2  ? UNP P50621 ? ? 'expression tag'        -19 23 
4 9BY1 SER D 3  ? UNP P50621 ? ? 'expression tag'        -18 24 
4 9BY1 SER D 4  ? UNP P50621 ? ? 'expression tag'        -17 25 
4 9BY1 HIS D 5  ? UNP P50621 ? ? 'expression tag'        -16 26 
4 9BY1 HIS D 6  ? UNP P50621 ? ? 'expression tag'        -15 27 
4 9BY1 HIS D 7  ? UNP P50621 ? ? 'expression tag'        -14 28 
4 9BY1 HIS D 8  ? UNP P50621 ? ? 'expression tag'        -13 29 
4 9BY1 HIS D 9  ? UNP P50621 ? ? 'expression tag'        -12 30 
4 9BY1 HIS D 10 ? UNP P50621 ? ? 'expression tag'        -11 31 
4 9BY1 SER D 11 ? UNP P50621 ? ? 'expression tag'        -10 32 
4 9BY1 SER D 12 ? UNP P50621 ? ? 'expression tag'        -9  33 
4 9BY1 GLY D 13 ? UNP P50621 ? ? 'expression tag'        -8  34 
4 9BY1 LEU D 14 ? UNP P50621 ? ? 'expression tag'        -7  35 
4 9BY1 VAL D 15 ? UNP P50621 ? ? 'expression tag'        -6  36 
4 9BY1 PRO D 16 ? UNP P50621 ? ? 'expression tag'        -5  37 
4 9BY1 ARG D 17 ? UNP P50621 ? ? 'expression tag'        -4  38 
4 9BY1 GLY D 18 ? UNP P50621 ? ? 'expression tag'        -3  39 
4 9BY1 SER D 19 ? UNP P50621 ? ? 'expression tag'        -2  40 
4 9BY1 HIS D 20 ? UNP P50621 ? ? 'expression tag'        -1  41 
4 9BY1 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,K,L 
# 
_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   ? ASN A 14  ? PRO A 7   ASN A 14  1 ? 8  
HELX_P HELX_P2  AA2 GLU A 15  ? MET A 17  ? GLU A 15  MET A 17  5 ? 3  
HELX_P HELX_P3  AA3 ASP A 27  ? TYR A 40  ? ASP A 27  TYR A 40  1 ? 14 
HELX_P HELX_P4  AA4 TYR A 40  ? THR A 45  ? TYR A 40  THR A 45  1 ? 6  
HELX_P HELX_P5  AA5 ASN A 50  ? ASN A 61  ? ASN A 50  ASN A 61  1 ? 12 
HELX_P HELX_P6  AA6 GLU A 65  ? SER A 70  ? GLU A 65  SER A 70  1 ? 6  
HELX_P HELX_P7  AA7 SER A 73  ? LYS A 87  ? SER A 73  LYS A 87  1 ? 15 
HELX_P HELX_P8  AA8 SER A 93  ? TYR A 104 ? SER A 93  TYR A 104 1 ? 12 
HELX_P HELX_P9  AA9 ARG A 117 ? ASN A 131 ? ARG A 117 ASN A 131 1 ? 15 
HELX_P HELX_P10 AB1 ASP A 133 ? ASN A 146 ? ASP A 133 ASN A 146 1 ? 14 
HELX_P HELX_P11 AB2 SER A 152 ? ALA A 159 ? SER A 152 ALA A 159 1 ? 8  
HELX_P HELX_P12 AB3 SER A 178 ? LEU A 195 ? SER A 178 LEU A 195 1 ? 18 
HELX_P HELX_P13 AB4 GLY A 222 ? ALA A 237 ? GLY A 222 ALA A 237 1 ? 16 
HELX_P HELX_P14 AB5 ASP A 238 ? GLN A 242 ? ASP A 238 GLN A 242 5 ? 5  
HELX_P HELX_P15 AB6 ASP A 257 ? THR A 264 ? ASP A 257 THR A 264 1 ? 8  
HELX_P HELX_P16 AB7 PRO A 285 ? GLU A 294 ? PRO A 285 GLU A 294 1 ? 10 
HELX_P HELX_P17 AB8 TYR A 302 ? GLY A 311 ? TYR A 302 GLY A 311 1 ? 10 
HELX_P HELX_P18 AB9 HIS A 313 ? MET A 317 ? HIS A 313 MET A 317 5 ? 5  
HELX_P HELX_P19 AC1 ASP A 318 ? ASN A 329 ? ASP A 318 ASN A 329 1 ? 12 
HELX_P HELX_P20 AC2 ASN A 338 ? GLY A 354 ? ASN A 338 GLY A 354 1 ? 17 
HELX_P HELX_P21 AC3 GLN A 361 ? LYS A 366 ? GLN A 361 LYS A 366 1 ? 6  
HELX_P HELX_P22 AC4 ILE A 416 ? LYS A 423 ? ILE A 416 LYS A 423 1 ? 8  
HELX_P HELX_P23 AC5 SER A 424 ? THR A 443 ? SER A 424 THR A 443 1 ? 20 
HELX_P HELX_P24 AC6 ALA A 448 ? LYS A 459 ? ALA A 448 LYS A 459 1 ? 12 
HELX_P HELX_P25 AC7 ASN A 467 ? GLN A 474 ? ASN A 467 GLN A 474 1 ? 8  
HELX_P HELX_P26 AC8 SER A 481 ? GLY A 511 ? SER A 481 GLY A 511 1 ? 31 
HELX_P HELX_P27 AC9 SER A 520 ? GLY A 525 ? SER A 520 GLY A 525 1 ? 6  
HELX_P HELX_P28 AD1 PHE A 528 ? THR A 534 ? PHE A 528 THR A 534 1 ? 7  
HELX_P HELX_P29 AD2 TYR A 540 ? PHE A 547 ? TYR A 540 PHE A 547 1 ? 8  
HELX_P HELX_P30 AD3 THR A 554 ? GLY A 569 ? THR A 554 GLY A 569 1 ? 16 
HELX_P HELX_P31 AD4 SER A 583 ? GLN A 588 ? SER A 583 GLN A 588 1 ? 6  
HELX_P HELX_P32 AD5 GLU A 628 ? MET A 632 ? GLU A 628 MET A 632 5 ? 5  
HELX_P HELX_P33 AD6 ASP A 633 ? GLN A 646 ? ASP A 633 GLN A 646 1 ? 14 
HELX_P HELX_P34 AD7 THR A 663 ? ARG A 677 ? THR A 663 ARG A 677 1 ? 15 
HELX_P HELX_P35 AD8 PRO B 7   ? GLU B 15  ? PRO B 7   GLU B 15  1 ? 9  
HELX_P HELX_P36 AD9 ASP B 27  ? THR B 45  ? ASP B 27  THR B 45  1 ? 19 
HELX_P HELX_P37 AE1 ASN B 50  ? ASN B 61  ? ASN B 50  ASN B 61  1 ? 12 
HELX_P HELX_P38 AE2 GLU B 65  ? SER B 70  ? GLU B 65  SER B 70  1 ? 6  
HELX_P HELX_P39 AE3 SER B 73  ? LYS B 87  ? SER B 73  LYS B 87  1 ? 15 
HELX_P HELX_P40 AE4 SER B 93  ? TYR B 104 ? SER B 93  TYR B 104 1 ? 12 
HELX_P HELX_P41 AE5 ARG B 117 ? ASN B 131 ? ARG B 117 ASN B 131 1 ? 15 
HELX_P HELX_P42 AE6 ASP B 133 ? ASN B 146 ? ASP B 133 ASN B 146 1 ? 14 
HELX_P HELX_P43 AE7 SER B 152 ? ALA B 159 ? SER B 152 ALA B 159 1 ? 8  
HELX_P HELX_P44 AE8 SER B 178 ? LEU B 195 ? SER B 178 LEU B 195 1 ? 18 
HELX_P HELX_P45 AE9 GLY B 222 ? ALA B 237 ? GLY B 222 ALA B 237 1 ? 16 
HELX_P HELX_P46 AF1 ASP B 257 ? THR B 264 ? ASP B 257 THR B 264 1 ? 8  
HELX_P HELX_P47 AF2 PRO B 285 ? GLU B 294 ? PRO B 285 GLU B 294 1 ? 10 
HELX_P HELX_P48 AF3 TYR B 302 ? GLY B 311 ? TYR B 302 GLY B 311 1 ? 10 
HELX_P HELX_P49 AF4 HIS B 313 ? MET B 317 ? HIS B 313 MET B 317 5 ? 5  
HELX_P HELX_P50 AF5 ASP B 318 ? ASN B 329 ? ASP B 318 ASN B 329 1 ? 12 
HELX_P HELX_P51 AF6 ASN B 338 ? GLY B 354 ? ASN B 338 GLY B 354 1 ? 17 
HELX_P HELX_P52 AF7 GLN B 361 ? LYS B 366 ? GLN B 361 LYS B 366 1 ? 6  
HELX_P HELX_P53 AF8 ILE B 416 ? LYS B 423 ? ILE B 416 LYS B 423 1 ? 8  
HELX_P HELX_P54 AF9 SER B 424 ? THR B 443 ? SER B 424 THR B 443 1 ? 20 
HELX_P HELX_P55 AG1 ALA B 448 ? LYS B 459 ? ALA B 448 LYS B 459 1 ? 12 
HELX_P HELX_P56 AG2 ASN B 467 ? GLN B 474 ? ASN B 467 GLN B 474 1 ? 8  
HELX_P HELX_P57 AG3 SER B 481 ? GLY B 511 ? SER B 481 GLY B 511 1 ? 31 
HELX_P HELX_P58 AG4 SER B 520 ? GLY B 525 ? SER B 520 GLY B 525 1 ? 6  
HELX_P HELX_P59 AG5 PHE B 528 ? THR B 534 ? PHE B 528 THR B 534 1 ? 7  
HELX_P HELX_P60 AG6 TYR B 540 ? PHE B 547 ? TYR B 540 PHE B 547 1 ? 8  
HELX_P HELX_P61 AG7 THR B 554 ? GLY B 569 ? THR B 554 GLY B 569 1 ? 16 
HELX_P HELX_P62 AG8 SER B 583 ? GLN B 588 ? SER B 583 GLN B 588 1 ? 6  
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 ? ? ? ? ? ? ? 2.037 ? ? 
metalc2 metalc ? ? E TTP . O2B ? ? ? 1_555 F MG . MG ? ? A TTP 801 A MG 802 1_555 ? ? ? ? ? ? ? 2.480 ? ? 
metalc3 metalc ? ? E TTP . O1G ? ? ? 1_555 F MG . MG ? ? A TTP 801 A MG 802 1_555 ? ? ? ? ? ? ? 2.509 ? ? 
metalc4 metalc ? ? I TTP . O2A ? ? ? 1_555 J MG . MG ? ? B TTP 801 B MG 802 1_555 ? ? ? ? ? ? ? 2.349 ? ? 
metalc5 metalc ? ? I TTP . O3G ? ? ? 1_555 J MG . MG ? ? B TTP 801 B MG 802 1_555 ? ? ? ? ? ? ? 2.119 ? ? 
# 
_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 O2B ? E TTP . ? A TTP 801 ? 1_555 71.9  ? 
2 O2A ? E TTP . ? A TTP 801 ? 1_555 MG ? F MG . ? A MG 802 ? 1_555 O1G ? E TTP . ? A TTP 801 ? 1_555 88.9  ? 
3 O2B ? E TTP . ? A TTP 801 ? 1_555 MG ? F MG . ? A MG 802 ? 1_555 O1G ? E TTP . ? A TTP 801 ? 1_555 68.0  ? 
4 O2A ? I TTP . ? B TTP 801 ? 1_555 MG ? J MG . ? B MG 802 ? 1_555 O3G ? I TTP . ? B TTP 801 ? 1_555 103.5 ? 
# 
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 1.37  
2 TYR 355 B . ? TYR 355 B PRO 356 B ? PRO 356 B 1 -0.18 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 3 ? 
AA7 ? 6 ? 
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 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? 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 ? parallel      
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA7 4 5 ? parallel      
AA7 5 6 ? 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 ASN A 410 ? ASN A 415 ? ASN A 410 ASN A 415 
AA1 3 ILE A 461 ? MET A 466 ? ILE A 461 MET A 466 
AA2 1 ILE A 407 ? SER A 408 ? ILE A 407 SER A 408 
AA2 2 CYS A 170 ? GLU A 174 ? CYS A 170 GLU A 174 
AA2 3 GLY A 198 ? ASN A 202 ? GLY A 198 ASN A 202 
AA2 4 GLY A 247 ? ASN A 252 ? GLY A 247 ASN A 252 
AA2 5 LEU A 278 ? ILE A 284 ? LEU A 278 ILE A 284 
AA2 6 TYR A 357 ? PHE A 360 ? TYR A 357 PHE A 360 
AA2 7 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 CYS B 170 ? GLU B 174 ? CYS B 170 GLU B 174 
AA7 2 GLY B 198 ? ASN B 202 ? GLY B 198 ASN B 202 
AA7 3 GLY B 247 ? ASN B 252 ? GLY B 247 ASN B 252 
AA7 4 LEU B 278 ? ILE B 284 ? LEU B 278 ILE B 284 
AA7 5 TYR B 357 ? PHE B 360 ? TYR B 357 PHE B 360 
AA7 6 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 ? LEU B 658 ? THR B 655 LEU B 658 
AB1 2 TYR B 684 ? THR B 687 ? TYR B 684 THR B 687 
# 
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 O ILE A 407 ? O ILE A 407 N LEU A 172 ? N LEU A 172 
AA2 2 3 N LEU A 173 ? N LEU A 173 O SER A 200 ? O SER A 200 
AA2 3 4 N LEU A 201 ? N LEU A 201 O ALA A 248 ? O ALA A 248 
AA2 4 5 N GLY A 247 ? N GLY A 247 O SER A 279 ? O SER A 279 
AA2 5 6 N VAL A 282 ? N VAL A 282 O TYR A 357 ? O TYR A 357 
AA2 6 7 N ILE A 358 ? N ILE A 358 O ILE A 682 ? O ILE A 682 
AA3 1 2 N VAL A 300 ? N VAL A 300 O GLU A 335 ? O GLU A 335 
AA4 1 2 N GLU A 602 ? N GLU A 602 O TYR A 613 ? O TYR A 613 
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 N LEU B 173 ? N LEU B 173 O SER B 200 ? O SER B 200 
AA7 2 3 N LEU B 201 ? N LEU B 201 O TYR B 250 ? O TYR B 250 
AA7 3 4 N GLY B 247 ? N GLY B 247 O SER B 279 ? O SER B 279 
AA7 4 5 N VAL B 282 ? N VAL B 282 O TYR B 357 ? O TYR B 357 
AA7 5 6 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 ARG B 604 ? N ARG B 604 O THR B 611 ? O THR B 611 
AB1 1 2 N LEU B 656 ? N LEU B 656 O TYR B 684 ? O TYR B 684 
# 
_pdbx_entry_details.entry_id                   9BY1 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 ? ? 2.13 
2 1 O A CYS 382 ? ? OG A SER 653 ? ? 2.13 
3 1 O A PRO 616 ? ? OH A TYR 626 ? ? 2.14 
4 1 O B CYS 382 ? ? OG B SER 653 ? ? 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 ASN A 61  ? ? -93.41  30.30   
2  1 MET A 240 ? ? 72.25   -7.71   
3  1 SER A 593 ? ? 59.79   -154.94 
4  1 SER A 653 ? ? -68.80  98.80   
5  1 ASP B 215 ? ? 80.07   -0.91   
6  1 ASP B 238 ? ? -95.38  31.16   
7  1 SER B 408 ? ? -160.75 114.82  
8  1 SER B 593 ? ? 58.39   -151.20 
9  1 THR D 311 ? ? -168.69 116.01  
10 1 ASP D 317 ? ? 61.69   167.64  
11 1 ASP D 318 ? ? 67.18   -4.11   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BY1 
_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 predcition 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                    9BY1 
_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                  2.55 
_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               504919 
_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                        9BY1 
_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              9BY1 
_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                9BY1 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
_em_single_particle_entity.entry_id              9BY1 
_em_single_particle_entity.id                    1 
_em_single_particle_entity.image_processing_id   1 
_em_single_particle_entity.point_symmetry        C1 
# 
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 GLU 323 ? C GLU 344 
365 1 Y 1 C ASP 324 ? C ASP 345 
366 1 Y 1 C GLU 325 ? C GLU 346 
367 1 Y 1 C LYS 326 ? C LYS 347 
368 1 Y 1 C GLU 327 ? C GLU 348 
369 1 Y 1 C GLN 328 ? C GLN 349 
370 1 Y 1 C ILE 329 ? C ILE 350 
371 1 Y 1 D MET -20 ? D MET 1   
372 1 Y 1 D GLY -19 ? D GLY 2   
373 1 Y 1 D SER -18 ? D SER 3   
374 1 Y 1 D SER -17 ? D SER 4   
375 1 Y 1 D HIS -16 ? D HIS 5   
376 1 Y 1 D HIS -15 ? D HIS 6   
377 1 Y 1 D HIS -14 ? D HIS 7   
378 1 Y 1 D HIS -13 ? D HIS 8   
379 1 Y 1 D HIS -12 ? D HIS 9   
380 1 Y 1 D HIS -11 ? D HIS 10  
381 1 Y 1 D SER -10 ? D SER 11  
382 1 Y 1 D SER -9  ? D SER 12  
383 1 Y 1 D GLY -8  ? D GLY 13  
384 1 Y 1 D LEU -7  ? D LEU 14  
385 1 Y 1 D VAL -6  ? D VAL 15  
386 1 Y 1 D PRO -5  ? D PRO 16  
387 1 Y 1 D ARG -4  ? D ARG 17  
388 1 Y 1 D GLY -3  ? D GLY 18  
389 1 Y 1 D SER -2  ? D SER 19  
390 1 Y 1 D HIS -1  ? D HIS 20  
391 1 Y 1 D MET 0   ? D MET 21  
392 1 Y 1 D MET 1   ? D MET 22  
393 1 Y 1 D THR 2   ? D THR 23  
394 1 Y 1 D LYS 3   ? D LYS 24  
395 1 Y 1 D ILE 4   ? D ILE 25  
396 1 Y 1 D TYR 5   ? D TYR 26  
397 1 Y 1 D ASP 6   ? D ASP 27  
398 1 Y 1 D ALA 7   ? D ALA 28  
399 1 Y 1 D ALA 8   ? D ALA 29  
400 1 Y 1 D ASN 9   ? D ASN 30  
401 1 Y 1 D TRP 10  ? D TRP 31  
402 1 Y 1 D SER 11  ? D SER 32  
403 1 Y 1 D LYS 12  ? D LYS 33  
404 1 Y 1 D HIS 13  ? D HIS 34  
405 1 Y 1 D GLU 14  ? D GLU 35  
406 1 Y 1 D ASP 15  ? D ASP 36  
407 1 Y 1 D ASP 16  ? D ASP 37  
408 1 Y 1 D PHE 17  ? D PHE 38  
409 1 Y 1 D THR 18  ? D THR 39  
410 1 Y 1 D GLN 19  ? D GLN 40  
411 1 Y 1 D MET 20  ? D MET 41  
412 1 Y 1 D PHE 21  ? D PHE 42  
413 1 Y 1 D TYR 22  ? D TYR 43  
414 1 Y 1 D ASN 23  ? D ASN 44  
415 1 Y 1 D GLN 24  ? D GLN 45  
416 1 Y 1 D ASN 25  ? D ASN 46  
417 1 Y 1 D VAL 26  ? D VAL 47  
418 1 Y 1 D LYS 27  ? D LYS 48  
419 1 Y 1 D GLN 28  ? D GLN 49  
420 1 Y 1 D PHE 29  ? D PHE 50  
421 1 Y 1 D TRP 30  ? D TRP 51  
422 1 Y 1 D LEU 31  ? D LEU 52  
423 1 Y 1 D PRO 32  ? D PRO 53  
424 1 Y 1 D GLU 33  ? D GLU 54  
425 1 Y 1 D GLU 34  ? D GLU 55  
426 1 Y 1 D ILE 35  ? D ILE 56  
427 1 Y 1 D ALA 36  ? D ALA 57  
428 1 Y 1 D LEU 37  ? D LEU 58  
429 1 Y 1 D ASN 38  ? D ASN 59  
430 1 Y 1 D GLY 39  ? D GLY 60  
431 1 Y 1 D ASP 40  ? D ASP 61  
432 1 Y 1 D LEU 41  ? D LEU 62  
433 1 Y 1 D LEU 42  ? D LEU 63  
434 1 Y 1 D THR 43  ? D THR 64  
435 1 Y 1 D TRP 44  ? D TRP 65  
436 1 Y 1 D LYS 45  ? D LYS 66  
437 1 Y 1 D TYR 46  ? D TYR 67  
438 1 Y 1 D LEU 47  ? D LEU 68  
439 1 Y 1 D GLY 48  ? D GLY 69  
440 1 Y 1 D LYS 49  ? D LYS 70  
441 1 Y 1 D ASN 50  ? D ASN 71  
442 1 Y 1 D GLU 51  ? D GLU 72  
443 1 Y 1 D GLN 52  ? D GLN 73  
444 1 Y 1 D ASP 53  ? D ASP 74  
445 1 Y 1 D THR 54  ? D THR 75  
446 1 Y 1 D TYR 55  ? D TYR 76  
447 1 Y 1 D MET 56  ? D MET 77  
448 1 Y 1 D LYS 57  ? D LYS 78  
449 1 Y 1 D VAL 58  ? D VAL 79  
450 1 Y 1 D LEU 59  ? D LEU 80  
451 1 Y 1 D ALA 60  ? D ALA 81  
452 1 Y 1 D GLY 61  ? D GLY 82  
453 1 Y 1 D LEU 62  ? D LEU 83  
454 1 Y 1 D THR 63  ? D THR 84  
455 1 Y 1 D LEU 64  ? D LEU 85  
456 1 Y 1 D LEU 65  ? D LEU 86  
457 1 Y 1 D ASP 66  ? D ASP 87  
458 1 Y 1 D THR 67  ? D THR 88  
459 1 Y 1 D GLU 68  ? D GLU 89  
460 1 Y 1 D GLN 69  ? D GLN 90  
461 1 Y 1 D GLY 70  ? D GLY 91  
462 1 Y 1 D ASN 71  ? D ASN 92  
463 1 Y 1 D THR 72  ? D THR 93  
464 1 Y 1 D GLY 73  ? D GLY 94  
465 1 Y 1 D MET 74  ? D MET 95  
466 1 Y 1 D PRO 75  ? D PRO 96  
467 1 Y 1 D ILE 76  ? D ILE 97  
468 1 Y 1 D VAL 77  ? D VAL 98  
469 1 Y 1 D ALA 78  ? D ALA 99  
470 1 Y 1 D GLU 79  ? D GLU 100 
471 1 Y 1 D HIS 80  ? D HIS 101 
472 1 Y 1 D VAL 81  ? D VAL 102 
473 1 Y 1 D ASP 82  ? D ASP 103 
474 1 Y 1 D GLY 83  ? D GLY 104 
475 1 Y 1 D HIS 84  ? D HIS 105 
476 1 Y 1 D GLN 85  ? D GLN 106 
477 1 Y 1 D ARG 86  ? D ARG 107 
478 1 Y 1 D LYS 87  ? D LYS 108 
479 1 Y 1 D ALA 88  ? D ALA 109 
480 1 Y 1 D VAL 89  ? D VAL 110 
481 1 Y 1 D LEU 90  ? D LEU 111 
482 1 Y 1 D ASN 91  ? D ASN 112 
483 1 Y 1 D PHE 92  ? D PHE 113 
484 1 Y 1 D MET 93  ? D MET 114 
485 1 Y 1 D ALA 94  ? D ALA 115 
486 1 Y 1 D MET 95  ? D MET 116 
487 1 Y 1 D MET 96  ? D MET 117 
488 1 Y 1 D GLU 97  ? D GLU 118 
489 1 Y 1 D ASN 98  ? D ASN 119 
490 1 Y 1 D ALA 99  ? D ALA 120 
491 1 Y 1 D VAL 100 ? D VAL 121 
492 1 Y 1 D HIS 101 ? D HIS 122 
493 1 Y 1 D ALA 102 ? D ALA 123 
494 1 Y 1 D LYS 103 ? D LYS 124 
495 1 Y 1 D SER 104 ? D SER 125 
496 1 Y 1 D TYR 105 ? D TYR 126 
497 1 Y 1 D SER 106 ? D SER 127 
498 1 Y 1 D ASN 107 ? D ASN 128 
499 1 Y 1 D ILE 108 ? D ILE 129 
500 1 Y 1 D PHE 109 ? D PHE 130 
501 1 Y 1 D MET 110 ? D MET 131 
502 1 Y 1 D THR 111 ? D THR 132 
503 1 Y 1 D LEU 112 ? D LEU 133 
504 1 Y 1 D ALA 113 ? D ALA 134 
505 1 Y 1 D PRO 114 ? D PRO 135 
506 1 Y 1 D THR 115 ? D THR 136 
507 1 Y 1 D GLU 116 ? D GLU 137 
508 1 Y 1 D THR 117 ? D THR 138 
509 1 Y 1 D ILE 118 ? D ILE 139 
510 1 Y 1 D ASN 119 ? D ASN 140 
511 1 Y 1 D GLU 120 ? D GLU 141 
512 1 Y 1 D VAL 121 ? D VAL 142 
513 1 Y 1 D PHE 122 ? D PHE 143 
514 1 Y 1 D GLU 123 ? D GLU 144 
515 1 Y 1 D TRP 124 ? D TRP 145 
516 1 Y 1 D VAL 125 ? D VAL 146 
517 1 Y 1 D LYS 126 ? D LYS 147 
518 1 Y 1 D GLN 127 ? D GLN 148 
519 1 Y 1 D ASN 128 ? D ASN 149 
520 1 Y 1 D LYS 129 ? D LYS 150 
521 1 Y 1 D TYR 130 ? D TYR 151 
522 1 Y 1 D LEU 131 ? D LEU 152 
523 1 Y 1 D GLN 132 ? D GLN 153 
524 1 Y 1 D LYS 133 ? D LYS 154 
525 1 Y 1 D LYS 134 ? D LYS 155 
526 1 Y 1 D ALA 135 ? D ALA 156 
527 1 Y 1 D GLN 136 ? D GLN 157 
528 1 Y 1 D MET 137 ? D MET 158 
529 1 Y 1 D ILE 138 ? D ILE 159 
530 1 Y 1 D VAL 139 ? D VAL 160 
531 1 Y 1 D GLY 140 ? D GLY 161 
532 1 Y 1 D LEU 141 ? D LEU 162 
533 1 Y 1 D TYR 142 ? D TYR 163 
534 1 Y 1 D LYS 143 ? D LYS 164 
535 1 Y 1 D ALA 144 ? D ALA 165 
536 1 Y 1 D ILE 145 ? D ILE 166 
537 1 Y 1 D GLN 146 ? D GLN 167 
538 1 Y 1 D LYS 147 ? D LYS 168 
539 1 Y 1 D ASP 148 ? D ASP 169 
540 1 Y 1 D ASP 149 ? D ASP 170 
541 1 Y 1 D GLU 150 ? D GLU 171 
542 1 Y 1 D ILE 151 ? D ILE 172 
543 1 Y 1 D SER 152 ? D SER 173 
544 1 Y 1 D LEU 153 ? D LEU 174 
545 1 Y 1 D PHE 154 ? D PHE 175 
546 1 Y 1 D LYS 155 ? D LYS 176 
547 1 Y 1 D ALA 156 ? D ALA 177 
548 1 Y 1 D MET 157 ? D MET 178 
549 1 Y 1 D VAL 158 ? D VAL 179 
550 1 Y 1 D ALA 159 ? D ALA 180 
551 1 Y 1 D SER 160 ? D SER 181 
552 1 Y 1 D VAL 161 ? D VAL 182 
553 1 Y 1 D TYR 162 ? D TYR 183 
554 1 Y 1 D LEU 163 ? D LEU 184 
555 1 Y 1 D GLU 164 ? D GLU 185 
556 1 Y 1 D SER 165 ? D SER 186 
557 1 Y 1 D PHE 166 ? D PHE 187 
558 1 Y 1 D LEU 167 ? D LEU 188 
559 1 Y 1 D PHE 168 ? D PHE 189 
560 1 Y 1 D TYR 169 ? D TYR 190 
561 1 Y 1 D SER 170 ? D SER 191 
562 1 Y 1 D GLY 171 ? D GLY 192 
563 1 Y 1 D PHE 172 ? D PHE 193 
564 1 Y 1 D TYR 173 ? D TYR 194 
565 1 Y 1 D TYR 174 ? D TYR 195 
566 1 Y 1 D PRO 175 ? D PRO 196 
567 1 Y 1 D LEU 176 ? D LEU 197 
568 1 Y 1 D TYR 177 ? D TYR 198 
569 1 Y 1 D PHE 178 ? D PHE 199 
570 1 Y 1 D TYR 179 ? D TYR 200 
571 1 Y 1 D GLY 180 ? D GLY 201 
572 1 Y 1 D GLN 181 ? D GLN 202 
573 1 Y 1 D GLY 182 ? D GLY 203 
574 1 Y 1 D LYS 183 ? D LYS 204 
575 1 Y 1 D LEU 184 ? D LEU 205 
576 1 Y 1 D MET 185 ? D MET 206 
577 1 Y 1 D GLN 186 ? D GLN 207 
578 1 Y 1 D SER 187 ? D SER 208 
579 1 Y 1 D GLY 188 ? D GLY 209 
580 1 Y 1 D GLU 189 ? D GLU 210 
581 1 Y 1 D ILE 190 ? D ILE 211 
582 1 Y 1 D ILE 191 ? D ILE 212 
583 1 Y 1 D ASN 192 ? D ASN 213 
584 1 Y 1 D LEU 193 ? D LEU 214 
585 1 Y 1 D ILE 194 ? D ILE 215 
586 1 Y 1 D LEU 195 ? D LEU 216 
587 1 Y 1 D ARG 196 ? D ARG 217 
588 1 Y 1 D ASP 197 ? D ASP 218 
589 1 Y 1 D GLU 198 ? D GLU 219 
590 1 Y 1 D ALA 199 ? D ALA 220 
591 1 Y 1 D ILE 200 ? D ILE 221 
592 1 Y 1 D HIS 201 ? D HIS 222 
593 1 Y 1 D GLY 202 ? D GLY 223 
594 1 Y 1 D VAL 203 ? D VAL 224 
595 1 Y 1 D TYR 204 ? D TYR 225 
596 1 Y 1 D VAL 205 ? D VAL 226 
597 1 Y 1 D GLY 206 ? D GLY 227 
598 1 Y 1 D LEU 207 ? D LEU 228 
599 1 Y 1 D LEU 208 ? D LEU 229 
600 1 Y 1 D ALA 209 ? D ALA 230 
601 1 Y 1 D GLN 210 ? D GLN 231 
602 1 Y 1 D GLU 211 ? D GLU 232 
603 1 Y 1 D ILE 212 ? D ILE 233 
604 1 Y 1 D TYR 213 ? D TYR 234 
605 1 Y 1 D ASN 214 ? D ASN 235 
606 1 Y 1 D LYS 215 ? D LYS 236 
607 1 Y 1 D GLN 216 ? D GLN 237 
608 1 Y 1 D THR 217 ? D THR 238 
609 1 Y 1 D GLU 218 ? D GLU 239 
610 1 Y 1 D GLU 219 ? D GLU 240 
611 1 Y 1 D LYS 220 ? D LYS 241 
612 1 Y 1 D LYS 221 ? D LYS 242 
613 1 Y 1 D ALA 222 ? D ALA 243 
614 1 Y 1 D GLU 223 ? D GLU 244 
615 1 Y 1 D LEU 224 ? D LEU 245 
616 1 Y 1 D ARG 225 ? D ARG 246 
617 1 Y 1 D GLU 226 ? D GLU 247 
618 1 Y 1 D PHE 227 ? D PHE 248 
619 1 Y 1 D ALA 228 ? D ALA 249 
620 1 Y 1 D ILE 229 ? D ILE 250 
621 1 Y 1 D ASP 230 ? D ASP 251 
622 1 Y 1 D LEU 231 ? D LEU 252 
623 1 Y 1 D LEU 232 ? D LEU 253 
624 1 Y 1 D ASN 233 ? D ASN 254 
625 1 Y 1 D GLN 234 ? D GLN 255 
626 1 Y 1 D LEU 235 ? D LEU 256 
627 1 Y 1 D TYR 236 ? D TYR 257 
628 1 Y 1 D GLU 237 ? D GLU 258 
629 1 Y 1 D ASN 238 ? D ASN 259 
630 1 Y 1 D GLU 239 ? D GLU 260 
631 1 Y 1 D LEU 240 ? D LEU 261 
632 1 Y 1 D GLU 241 ? D GLU 262 
633 1 Y 1 D TYR 242 ? D TYR 263 
634 1 Y 1 D THR 243 ? D THR 264 
635 1 Y 1 D GLU 244 ? D GLU 265 
636 1 Y 1 D ASP 245 ? D ASP 266 
637 1 Y 1 D LEU 246 ? D LEU 267 
638 1 Y 1 D TYR 247 ? D TYR 268 
639 1 Y 1 D ASP 248 ? D ASP 269 
640 1 Y 1 D GLN 249 ? D GLN 270 
641 1 Y 1 D VAL 250 ? D VAL 271 
642 1 Y 1 D GLY 251 ? D GLY 272 
643 1 Y 1 D LEU 252 ? D LEU 273 
644 1 Y 1 D SER 253 ? D SER 274 
645 1 Y 1 D HIS 254 ? D HIS 275 
646 1 Y 1 D ASP 255 ? D ASP 276 
647 1 Y 1 D VAL 256 ? D VAL 277 
648 1 Y 1 D LYS 257 ? D LYS 278 
649 1 Y 1 D LYS 258 ? D LYS 279 
650 1 Y 1 D PHE 259 ? D PHE 280 
651 1 Y 1 D ILE 260 ? D ILE 281 
652 1 Y 1 D ARG 261 ? D ARG 282 
653 1 Y 1 D TYR 262 ? D TYR 283 
654 1 Y 1 D ASN 263 ? D ASN 284 
655 1 Y 1 D ALA 264 ? D ALA 285 
656 1 Y 1 D ASN 265 ? D ASN 286 
657 1 Y 1 D LYS 266 ? D LYS 287 
658 1 Y 1 D ALA 267 ? D ALA 288 
659 1 Y 1 D LEU 268 ? D LEU 289 
660 1 Y 1 D MET 269 ? D MET 290 
661 1 Y 1 D ASN 270 ? D ASN 291 
662 1 Y 1 D LEU 271 ? D LEU 292 
663 1 Y 1 D GLY 272 ? D GLY 293 
664 1 Y 1 D PHE 273 ? D PHE 294 
665 1 Y 1 D ASP 274 ? D ASP 295 
666 1 Y 1 D PRO 275 ? D PRO 296 
667 1 Y 1 D TYR 276 ? D TYR 297 
668 1 Y 1 D PHE 277 ? D PHE 298 
669 1 Y 1 D GLU 278 ? D GLU 299 
670 1 Y 1 D GLU 279 ? D GLU 300 
671 1 Y 1 D GLU 280 ? D GLU 301 
672 1 Y 1 D ASP 281 ? D ASP 302 
673 1 Y 1 D ILE 282 ? D ILE 303 
674 1 Y 1 D ASN 283 ? D ASN 304 
675 1 Y 1 D PRO 284 ? D PRO 305 
676 1 Y 1 D ILE 285 ? D ILE 306 
677 1 Y 1 D VAL 286 ? D VAL 307 
678 1 Y 1 D LEU 287 ? D LEU 308 
679 1 Y 1 D ASN 288 ? D ASN 309 
680 1 Y 1 D GLY 289 ? D GLY 310 
681 1 Y 1 D LEU 290 ? D LEU 311 
682 1 Y 1 D ASN 291 ? D ASN 312 
683 1 Y 1 D THR 292 ? D THR 313 
684 1 Y 1 D LYS 293 ? D LYS 314 
685 1 Y 1 D THR 294 ? D THR 315 
686 1 Y 1 D LYS 295 ? D LYS 316 
687 1 Y 1 D SER 296 ? D SER 317 
688 1 Y 1 D HIS 297 ? D HIS 318 
689 1 Y 1 D ASP 298 ? D ASP 319 
690 1 Y 1 D PHE 299 ? D PHE 320 
691 1 Y 1 D PHE 300 ? D PHE 321 
692 1 Y 1 D SER 301 ? D SER 322 
693 1 Y 1 D MET 302 ? D MET 323 
694 1 Y 1 D LYS 303 ? D LYS 324 
695 1 Y 1 D GLY 304 ? D GLY 325 
696 1 Y 1 D ASN 305 ? D ASN 326 
697 1 Y 1 D GLY 306 ? D GLY 327 
698 1 Y 1 D TYR 307 ? D TYR 328 
699 1 Y 1 D LYS 308 ? D LYS 329 
700 1 Y 1 D GLU 323 ? D GLU 344 
701 1 Y 1 D ASP 324 ? D ASP 345 
702 1 Y 1 D GLU 325 ? D GLU 346 
703 1 Y 1 D LYS 326 ? D LYS 347 
704 1 Y 1 D GLU 327 ? D GLU 348 
705 1 Y 1 D GLN 328 ? D GLN 349 
706 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 
DGI O1B    O  N N 135 
DGI PB     P  N N 136 
DGI O2B    O  N N 137 
DGI O3B    O  N N 138 
DGI O3A    O  N N 139 
DGI PA     P  N S 140 
DGI O1A    O  N N 141 
DGI O2A    O  N N 142 
DGI "O5'"  O  N N 143 
DGI "C5'"  C  N N 144 
DGI "C4'"  C  N R 145 
DGI "O4'"  O  N N 146 
DGI "C3'"  C  N S 147 
DGI "O3'"  O  N N 148 
DGI "C2'"  C  N N 149 
DGI "C1'"  C  N R 150 
DGI N9     N  Y N 151 
DGI C8     C  Y N 152 
DGI N7     N  Y N 153 
DGI C5     C  Y N 154 
DGI C4     C  Y N 155 
DGI N3     N  N N 156 
DGI C2     C  N N 157 
DGI N2     N  N N 158 
DGI N1     N  N N 159 
DGI C6     C  N N 160 
DGI O6     O  N N 161 
DGI HOB2   H  N N 162 
DGI HOB3   H  N N 163 
DGI HOA2   H  N N 164 
DGI "H5'"  H  N N 165 
DGI "H5''" H  N N 166 
DGI "H4'"  H  N N 167 
DGI "H3'"  H  N N 168 
DGI "HO3'" H  N N 169 
DGI "H2'"  H  N N 170 
DGI "H2''" H  N N 171 
DGI "H1'"  H  N N 172 
DGI H8     H  N N 173 
DGI HN21   H  N N 174 
DGI HN22   H  N N 175 
DGI HN1    H  N N 176 
GLN N      N  N N 177 
GLN CA     C  N S 178 
GLN C      C  N N 179 
GLN O      O  N N 180 
GLN CB     C  N N 181 
GLN CG     C  N N 182 
GLN CD     C  N N 183 
GLN OE1    O  N N 184 
GLN NE2    N  N N 185 
GLN OXT    O  N N 186 
GLN H      H  N N 187 
GLN H2     H  N N 188 
GLN HA     H  N N 189 
GLN HB2    H  N N 190 
GLN HB3    H  N N 191 
GLN HG2    H  N N 192 
GLN HG3    H  N N 193 
GLN HE21   H  N N 194 
GLN HE22   H  N N 195 
GLN HXT    H  N N 196 
GLU N      N  N N 197 
GLU CA     C  N S 198 
GLU C      C  N N 199 
GLU O      O  N N 200 
GLU CB     C  N N 201 
GLU CG     C  N N 202 
GLU CD     C  N N 203 
GLU OE1    O  N N 204 
GLU OE2    O  N N 205 
GLU OXT    O  N N 206 
GLU H      H  N N 207 
GLU H2     H  N N 208 
GLU HA     H  N N 209 
GLU HB2    H  N N 210 
GLU HB3    H  N N 211 
GLU HG2    H  N N 212 
GLU HG3    H  N N 213 
GLU HE2    H  N N 214 
GLU HXT    H  N N 215 
GLY N      N  N N 216 
GLY CA     C  N N 217 
GLY C      C  N N 218 
GLY O      O  N N 219 
GLY OXT    O  N N 220 
GLY H      H  N N 221 
GLY H2     H  N N 222 
GLY HA2    H  N N 223 
GLY HA3    H  N N 224 
GLY HXT    H  N N 225 
HIS N      N  N N 226 
HIS CA     C  N S 227 
HIS C      C  N N 228 
HIS O      O  N N 229 
HIS CB     C  N N 230 
HIS CG     C  Y N 231 
HIS ND1    N  Y N 232 
HIS CD2    C  Y N 233 
HIS CE1    C  Y N 234 
HIS NE2    N  Y N 235 
HIS OXT    O  N N 236 
HIS H      H  N N 237 
HIS H2     H  N N 238 
HIS HA     H  N N 239 
HIS HB2    H  N N 240 
HIS HB3    H  N N 241 
HIS HD1    H  N N 242 
HIS HD2    H  N N 243 
HIS HE1    H  N N 244 
HIS HE2    H  N N 245 
HIS HXT    H  N N 246 
ILE N      N  N N 247 
ILE CA     C  N S 248 
ILE C      C  N N 249 
ILE O      O  N N 250 
ILE CB     C  N S 251 
ILE CG1    C  N N 252 
ILE CG2    C  N N 253 
ILE CD1    C  N N 254 
ILE OXT    O  N N 255 
ILE H      H  N N 256 
ILE H2     H  N N 257 
ILE HA     H  N N 258 
ILE HB     H  N N 259 
ILE HG12   H  N N 260 
ILE HG13   H  N N 261 
ILE HG21   H  N N 262 
ILE HG22   H  N N 263 
ILE HG23   H  N N 264 
ILE HD11   H  N N 265 
ILE HD12   H  N N 266 
ILE HD13   H  N N 267 
ILE HXT    H  N N 268 
LEU N      N  N N 269 
LEU CA     C  N S 270 
LEU C      C  N N 271 
LEU O      O  N N 272 
LEU CB     C  N N 273 
LEU CG     C  N N 274 
LEU CD1    C  N N 275 
LEU CD2    C  N N 276 
LEU OXT    O  N N 277 
LEU H      H  N N 278 
LEU H2     H  N N 279 
LEU HA     H  N N 280 
LEU HB2    H  N N 281 
LEU HB3    H  N N 282 
LEU HG     H  N N 283 
LEU HD11   H  N N 284 
LEU HD12   H  N N 285 
LEU HD13   H  N N 286 
LEU HD21   H  N N 287 
LEU HD22   H  N N 288 
LEU HD23   H  N N 289 
LEU HXT    H  N N 290 
LYS N      N  N N 291 
LYS CA     C  N S 292 
LYS C      C  N N 293 
LYS O      O  N N 294 
LYS CB     C  N N 295 
LYS CG     C  N N 296 
LYS CD     C  N N 297 
LYS CE     C  N N 298 
LYS NZ     N  N N 299 
LYS OXT    O  N N 300 
LYS H      H  N N 301 
LYS H2     H  N N 302 
LYS HA     H  N N 303 
LYS HB2    H  N N 304 
LYS HB3    H  N N 305 
LYS HG2    H  N N 306 
LYS HG3    H  N N 307 
LYS HD2    H  N N 308 
LYS HD3    H  N N 309 
LYS HE2    H  N N 310 
LYS HE3    H  N N 311 
LYS HZ1    H  N N 312 
LYS HZ2    H  N N 313 
LYS HZ3    H  N N 314 
LYS HXT    H  N N 315 
MET N      N  N N 316 
MET CA     C  N S 317 
MET C      C  N N 318 
MET O      O  N N 319 
MET CB     C  N N 320 
MET CG     C  N N 321 
MET SD     S  N N 322 
MET CE     C  N N 323 
MET OXT    O  N N 324 
MET H      H  N N 325 
MET H2     H  N N 326 
MET HA     H  N N 327 
MET HB2    H  N N 328 
MET HB3    H  N N 329 
MET HG2    H  N N 330 
MET HG3    H  N N 331 
MET HE1    H  N N 332 
MET HE2    H  N N 333 
MET HE3    H  N N 334 
MET HXT    H  N N 335 
MG  MG     MG N N 336 
PHE N      N  N N 337 
PHE CA     C  N S 338 
PHE C      C  N N 339 
PHE O      O  N N 340 
PHE CB     C  N N 341 
PHE CG     C  Y N 342 
PHE CD1    C  Y N 343 
PHE CD2    C  Y N 344 
PHE CE1    C  Y N 345 
PHE CE2    C  Y N 346 
PHE CZ     C  Y N 347 
PHE OXT    O  N N 348 
PHE H      H  N N 349 
PHE H2     H  N N 350 
PHE HA     H  N N 351 
PHE HB2    H  N N 352 
PHE HB3    H  N N 353 
PHE HD1    H  N N 354 
PHE HD2    H  N N 355 
PHE HE1    H  N N 356 
PHE HE2    H  N N 357 
PHE HZ     H  N N 358 
PHE HXT    H  N N 359 
PRO N      N  N N 360 
PRO CA     C  N S 361 
PRO C      C  N N 362 
PRO O      O  N N 363 
PRO CB     C  N N 364 
PRO CG     C  N N 365 
PRO CD     C  N N 366 
PRO OXT    O  N N 367 
PRO H      H  N N 368 
PRO HA     H  N N 369 
PRO HB2    H  N N 370 
PRO HB3    H  N N 371 
PRO HG2    H  N N 372 
PRO HG3    H  N N 373 
PRO HD2    H  N N 374 
PRO HD3    H  N N 375 
PRO HXT    H  N N 376 
SER N      N  N N 377 
SER CA     C  N S 378 
SER C      C  N N 379 
SER O      O  N N 380 
SER CB     C  N N 381 
SER OG     O  N N 382 
SER OXT    O  N N 383 
SER H      H  N N 384 
SER H2     H  N N 385 
SER HA     H  N N 386 
SER HB2    H  N N 387 
SER HB3    H  N N 388 
SER HG     H  N N 389 
SER HXT    H  N N 390 
THR N      N  N N 391 
THR CA     C  N S 392 
THR C      C  N N 393 
THR O      O  N N 394 
THR CB     C  N R 395 
THR OG1    O  N N 396 
THR CG2    C  N N 397 
THR OXT    O  N N 398 
THR H      H  N N 399 
THR H2     H  N N 400 
THR HA     H  N N 401 
THR HB     H  N N 402 
THR HG1    H  N N 403 
THR HG21   H  N N 404 
THR HG22   H  N N 405 
THR HG23   H  N N 406 
THR HXT    H  N N 407 
TRP N      N  N N 408 
TRP CA     C  N S 409 
TRP C      C  N N 410 
TRP O      O  N N 411 
TRP CB     C  N N 412 
TRP CG     C  Y N 413 
TRP CD1    C  Y N 414 
TRP CD2    C  Y N 415 
TRP NE1    N  Y N 416 
TRP CE2    C  Y N 417 
TRP CE3    C  Y N 418 
TRP CZ2    C  Y N 419 
TRP CZ3    C  Y N 420 
TRP CH2    C  Y N 421 
TRP OXT    O  N N 422 
TRP H      H  N N 423 
TRP H2     H  N N 424 
TRP HA     H  N N 425 
TRP HB2    H  N N 426 
TRP HB3    H  N N 427 
TRP HD1    H  N N 428 
TRP HE1    H  N N 429 
TRP HE3    H  N N 430 
TRP HZ2    H  N N 431 
TRP HZ3    H  N N 432 
TRP HH2    H  N N 433 
TRP HXT    H  N N 434 
TTP PA     P  N S 435 
TTP O1A    O  N N 436 
TTP O2A    O  N N 437 
TTP O3A    O  N N 438 
TTP PB     P  N S 439 
TTP O1B    O  N N 440 
TTP O2B    O  N N 441 
TTP O3B    O  N N 442 
TTP PG     P  N N 443 
TTP O1G    O  N N 444 
TTP O2G    O  N N 445 
TTP O3G    O  N N 446 
TTP "O5'"  O  N N 447 
TTP "C5'"  C  N N 448 
TTP "C4'"  C  N R 449 
TTP "O4'"  O  N N 450 
TTP "C3'"  C  N S 451 
TTP "O3'"  O  N N 452 
TTP "C2'"  C  N N 453 
TTP "C1'"  C  N R 454 
TTP N1     N  N N 455 
TTP C2     C  N N 456 
TTP O2     O  N N 457 
TTP N3     N  N N 458 
TTP C4     C  N N 459 
TTP O4     O  N N 460 
TTP C5     C  N N 461 
TTP C5M    C  N N 462 
TTP C6     C  N N 463 
TTP HOA2   H  N N 464 
TTP HOB2   H  N N 465 
TTP HOG2   H  N N 466 
TTP HOG3   H  N N 467 
TTP "H5'1" H  N N 468 
TTP "H5'2" H  N N 469 
TTP "H4'"  H  N N 470 
TTP "H3'"  H  N N 471 
TTP "HO3'" H  N N 472 
TTP "H2'1" H  N N 473 
TTP "H2'2" H  N N 474 
TTP "H1'"  H  N N 475 
TTP HN3    H  N N 476 
TTP HM51   H  N N 477 
TTP HM52   H  N N 478 
TTP HM53   H  N N 479 
TTP H6     H  N N 480 
TYR N      N  N N 481 
TYR CA     C  N S 482 
TYR C      C  N N 483 
TYR O      O  N N 484 
TYR CB     C  N N 485 
TYR CG     C  Y N 486 
TYR CD1    C  Y N 487 
TYR CD2    C  Y N 488 
TYR CE1    C  Y N 489 
TYR CE2    C  Y N 490 
TYR CZ     C  Y N 491 
TYR OH     O  N N 492 
TYR OXT    O  N N 493 
TYR H      H  N N 494 
TYR H2     H  N N 495 
TYR HA     H  N N 496 
TYR HB2    H  N N 497 
TYR HB3    H  N N 498 
TYR HD1    H  N N 499 
TYR HD2    H  N N 500 
TYR HE1    H  N N 501 
TYR HE2    H  N N 502 
TYR HH     H  N N 503 
TYR HXT    H  N N 504 
VAL N      N  N N 505 
VAL CA     C  N S 506 
VAL C      C  N N 507 
VAL O      O  N N 508 
VAL CB     C  N N 509 
VAL CG1    C  N N 510 
VAL CG2    C  N N 511 
VAL OXT    O  N N 512 
VAL H      H  N N 513 
VAL H2     H  N N 514 
VAL HA     H  N N 515 
VAL HB     H  N N 516 
VAL HG11   H  N N 517 
VAL HG12   H  N N 518 
VAL HG13   H  N N 519 
VAL HG21   H  N N 520 
VAL HG22   H  N N 521 
VAL HG23   H  N N 522 
VAL HXT    H  N N 523 
# 
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 
DGI O1B   PB     doub N N 132 
DGI PB    O2B    sing N N 133 
DGI PB    O3B    sing N N 134 
DGI PB    O3A    sing N N 135 
DGI O2B   HOB2   sing N N 136 
DGI O3B   HOB3   sing N N 137 
DGI O3A   PA     sing N N 138 
DGI PA    O1A    doub N N 139 
DGI PA    O2A    sing N N 140 
DGI PA    "O5'"  sing N N 141 
DGI O2A   HOA2   sing N N 142 
DGI "O5'" "C5'"  sing N N 143 
DGI "C5'" "C4'"  sing N N 144 
DGI "C5'" "H5'"  sing N N 145 
DGI "C5'" "H5''" sing N N 146 
DGI "C4'" "O4'"  sing N N 147 
DGI "C4'" "C3'"  sing N N 148 
DGI "C4'" "H4'"  sing N N 149 
DGI "O4'" "C1'"  sing N N 150 
DGI "C3'" "O3'"  sing N N 151 
DGI "C3'" "C2'"  sing N N 152 
DGI "C3'" "H3'"  sing N N 153 
DGI "O3'" "HO3'" sing N N 154 
DGI "C2'" "C1'"  sing N N 155 
DGI "C2'" "H2'"  sing N N 156 
DGI "C2'" "H2''" sing N N 157 
DGI "C1'" N9     sing N N 158 
DGI "C1'" "H1'"  sing N N 159 
DGI N9    C8     sing Y N 160 
DGI N9    C4     sing Y N 161 
DGI C8    N7     doub Y N 162 
DGI C8    H8     sing N N 163 
DGI N7    C5     sing Y N 164 
DGI C5    C4     doub Y N 165 
DGI C5    C6     sing N N 166 
DGI C4    N3     sing N N 167 
DGI N3    C2     doub N N 168 
DGI C2    N2     sing N N 169 
DGI C2    N1     sing N N 170 
DGI N2    HN21   sing N N 171 
DGI N2    HN22   sing N N 172 
DGI N1    C6     sing N N 173 
DGI N1    HN1    sing N N 174 
DGI C6    O6     doub N N 175 
GLN N     CA     sing N N 176 
GLN N     H      sing N N 177 
GLN N     H2     sing N N 178 
GLN CA    C      sing N N 179 
GLN CA    CB     sing N N 180 
GLN CA    HA     sing N N 181 
GLN C     O      doub N N 182 
GLN C     OXT    sing N N 183 
GLN CB    CG     sing N N 184 
GLN CB    HB2    sing N N 185 
GLN CB    HB3    sing N N 186 
GLN CG    CD     sing N N 187 
GLN CG    HG2    sing N N 188 
GLN CG    HG3    sing N N 189 
GLN CD    OE1    doub N N 190 
GLN CD    NE2    sing N N 191 
GLN NE2   HE21   sing N N 192 
GLN NE2   HE22   sing N N 193 
GLN OXT   HXT    sing N N 194 
GLU N     CA     sing N N 195 
GLU N     H      sing N N 196 
GLU N     H2     sing N N 197 
GLU CA    C      sing N N 198 
GLU CA    CB     sing N N 199 
GLU CA    HA     sing N N 200 
GLU C     O      doub N N 201 
GLU C     OXT    sing N N 202 
GLU CB    CG     sing N N 203 
GLU CB    HB2    sing N N 204 
GLU CB    HB3    sing N N 205 
GLU CG    CD     sing N N 206 
GLU CG    HG2    sing N N 207 
GLU CG    HG3    sing N N 208 
GLU CD    OE1    doub N N 209 
GLU CD    OE2    sing N N 210 
GLU OE2   HE2    sing N N 211 
GLU OXT   HXT    sing N N 212 
GLY N     CA     sing N N 213 
GLY N     H      sing N N 214 
GLY N     H2     sing N N 215 
GLY CA    C      sing N N 216 
GLY CA    HA2    sing N N 217 
GLY CA    HA3    sing N N 218 
GLY C     O      doub N N 219 
GLY C     OXT    sing N N 220 
GLY OXT   HXT    sing N N 221 
HIS N     CA     sing N N 222 
HIS N     H      sing N N 223 
HIS N     H2     sing N N 224 
HIS CA    C      sing N N 225 
HIS CA    CB     sing N N 226 
HIS CA    HA     sing N N 227 
HIS C     O      doub N N 228 
HIS C     OXT    sing N N 229 
HIS CB    CG     sing N N 230 
HIS CB    HB2    sing N N 231 
HIS CB    HB3    sing N N 232 
HIS CG    ND1    sing Y N 233 
HIS CG    CD2    doub Y N 234 
HIS ND1   CE1    doub Y N 235 
HIS ND1   HD1    sing N N 236 
HIS CD2   NE2    sing Y N 237 
HIS CD2   HD2    sing N N 238 
HIS CE1   NE2    sing Y N 239 
HIS CE1   HE1    sing N N 240 
HIS NE2   HE2    sing N N 241 
HIS OXT   HXT    sing N N 242 
ILE N     CA     sing N N 243 
ILE N     H      sing N N 244 
ILE N     H2     sing N N 245 
ILE CA    C      sing N N 246 
ILE CA    CB     sing N N 247 
ILE CA    HA     sing N N 248 
ILE C     O      doub N N 249 
ILE C     OXT    sing N N 250 
ILE CB    CG1    sing N N 251 
ILE CB    CG2    sing N N 252 
ILE CB    HB     sing N N 253 
ILE CG1   CD1    sing N N 254 
ILE CG1   HG12   sing N N 255 
ILE CG1   HG13   sing N N 256 
ILE CG2   HG21   sing N N 257 
ILE CG2   HG22   sing N N 258 
ILE CG2   HG23   sing N N 259 
ILE CD1   HD11   sing N N 260 
ILE CD1   HD12   sing N N 261 
ILE CD1   HD13   sing N N 262 
ILE OXT   HXT    sing N N 263 
LEU N     CA     sing N N 264 
LEU N     H      sing N N 265 
LEU N     H2     sing N N 266 
LEU CA    C      sing N N 267 
LEU CA    CB     sing N N 268 
LEU CA    HA     sing N N 269 
LEU C     O      doub N N 270 
LEU C     OXT    sing N N 271 
LEU CB    CG     sing N N 272 
LEU CB    HB2    sing N N 273 
LEU CB    HB3    sing N N 274 
LEU CG    CD1    sing N N 275 
LEU CG    CD2    sing N N 276 
LEU CG    HG     sing N N 277 
LEU CD1   HD11   sing N N 278 
LEU CD1   HD12   sing N N 279 
LEU CD1   HD13   sing N N 280 
LEU CD2   HD21   sing N N 281 
LEU CD2   HD22   sing N N 282 
LEU CD2   HD23   sing N N 283 
LEU OXT   HXT    sing N N 284 
LYS N     CA     sing N N 285 
LYS N     H      sing N N 286 
LYS N     H2     sing N N 287 
LYS CA    C      sing N N 288 
LYS CA    CB     sing N N 289 
LYS CA    HA     sing N N 290 
LYS C     O      doub N N 291 
LYS C     OXT    sing N N 292 
LYS CB    CG     sing N N 293 
LYS CB    HB2    sing N N 294 
LYS CB    HB3    sing N N 295 
LYS CG    CD     sing N N 296 
LYS CG    HG2    sing N N 297 
LYS CG    HG3    sing N N 298 
LYS CD    CE     sing N N 299 
LYS CD    HD2    sing N N 300 
LYS CD    HD3    sing N N 301 
LYS CE    NZ     sing N N 302 
LYS CE    HE2    sing N N 303 
LYS CE    HE3    sing N N 304 
LYS NZ    HZ1    sing N N 305 
LYS NZ    HZ2    sing N N 306 
LYS NZ    HZ3    sing N N 307 
LYS OXT   HXT    sing N N 308 
MET N     CA     sing N N 309 
MET N     H      sing N N 310 
MET N     H2     sing N N 311 
MET CA    C      sing N N 312 
MET CA    CB     sing N N 313 
MET CA    HA     sing N N 314 
MET C     O      doub N N 315 
MET C     OXT    sing N N 316 
MET CB    CG     sing N N 317 
MET CB    HB2    sing N N 318 
MET CB    HB3    sing N N 319 
MET CG    SD     sing N N 320 
MET CG    HG2    sing N N 321 
MET CG    HG3    sing N N 322 
MET SD    CE     sing N N 323 
MET CE    HE1    sing N N 324 
MET CE    HE2    sing N N 325 
MET CE    HE3    sing N N 326 
MET OXT   HXT    sing N N 327 
PHE N     CA     sing N N 328 
PHE N     H      sing N N 329 
PHE N     H2     sing N N 330 
PHE CA    C      sing N N 331 
PHE CA    CB     sing N N 332 
PHE CA    HA     sing N N 333 
PHE C     O      doub N N 334 
PHE C     OXT    sing N N 335 
PHE CB    CG     sing N N 336 
PHE CB    HB2    sing N N 337 
PHE CB    HB3    sing N N 338 
PHE CG    CD1    doub Y N 339 
PHE CG    CD2    sing Y N 340 
PHE CD1   CE1    sing Y N 341 
PHE CD1   HD1    sing N N 342 
PHE CD2   CE2    doub Y N 343 
PHE CD2   HD2    sing N N 344 
PHE CE1   CZ     doub Y N 345 
PHE CE1   HE1    sing N N 346 
PHE CE2   CZ     sing Y N 347 
PHE CE2   HE2    sing N N 348 
PHE CZ    HZ     sing N N 349 
PHE OXT   HXT    sing N N 350 
PRO N     CA     sing N N 351 
PRO N     CD     sing N N 352 
PRO N     H      sing N N 353 
PRO CA    C      sing N N 354 
PRO CA    CB     sing N N 355 
PRO CA    HA     sing N N 356 
PRO C     O      doub N N 357 
PRO C     OXT    sing N N 358 
PRO CB    CG     sing N N 359 
PRO CB    HB2    sing N N 360 
PRO CB    HB3    sing N N 361 
PRO CG    CD     sing N N 362 
PRO CG    HG2    sing N N 363 
PRO CG    HG3    sing N N 364 
PRO CD    HD2    sing N N 365 
PRO CD    HD3    sing N N 366 
PRO OXT   HXT    sing N N 367 
SER N     CA     sing N N 368 
SER N     H      sing N N 369 
SER N     H2     sing N N 370 
SER CA    C      sing N N 371 
SER CA    CB     sing N N 372 
SER CA    HA     sing N N 373 
SER C     O      doub N N 374 
SER C     OXT    sing N N 375 
SER CB    OG     sing N N 376 
SER CB    HB2    sing N N 377 
SER CB    HB3    sing N N 378 
SER OG    HG     sing N N 379 
SER OXT   HXT    sing N N 380 
THR N     CA     sing N N 381 
THR N     H      sing N N 382 
THR N     H2     sing N N 383 
THR CA    C      sing N N 384 
THR CA    CB     sing N N 385 
THR CA    HA     sing N N 386 
THR C     O      doub N N 387 
THR C     OXT    sing N N 388 
THR CB    OG1    sing N N 389 
THR CB    CG2    sing N N 390 
THR CB    HB     sing N N 391 
THR OG1   HG1    sing N N 392 
THR CG2   HG21   sing N N 393 
THR CG2   HG22   sing N N 394 
THR CG2   HG23   sing N N 395 
THR OXT   HXT    sing N N 396 
TRP N     CA     sing N N 397 
TRP N     H      sing N N 398 
TRP N     H2     sing N N 399 
TRP CA    C      sing N N 400 
TRP CA    CB     sing N N 401 
TRP CA    HA     sing N N 402 
TRP C     O      doub N N 403 
TRP C     OXT    sing N N 404 
TRP CB    CG     sing N N 405 
TRP CB    HB2    sing N N 406 
TRP CB    HB3    sing N N 407 
TRP CG    CD1    doub Y N 408 
TRP CG    CD2    sing Y N 409 
TRP CD1   NE1    sing Y N 410 
TRP CD1   HD1    sing N N 411 
TRP CD2   CE2    doub Y N 412 
TRP CD2   CE3    sing Y N 413 
TRP NE1   CE2    sing Y N 414 
TRP NE1   HE1    sing N N 415 
TRP CE2   CZ2    sing Y N 416 
TRP CE3   CZ3    doub Y N 417 
TRP CE3   HE3    sing N N 418 
TRP CZ2   CH2    doub Y N 419 
TRP CZ2   HZ2    sing N N 420 
TRP CZ3   CH2    sing Y N 421 
TRP CZ3   HZ3    sing N N 422 
TRP CH2   HH2    sing N N 423 
TRP OXT   HXT    sing N N 424 
TTP PA    O1A    doub N N 425 
TTP PA    O2A    sing N N 426 
TTP PA    O3A    sing N N 427 
TTP PA    "O5'"  sing N N 428 
TTP O2A   HOA2   sing N N 429 
TTP O3A   PB     sing N N 430 
TTP PB    O1B    doub N N 431 
TTP PB    O2B    sing N N 432 
TTP PB    O3B    sing N N 433 
TTP O2B   HOB2   sing N N 434 
TTP O3B   PG     sing N N 435 
TTP PG    O1G    doub N N 436 
TTP PG    O2G    sing N N 437 
TTP PG    O3G    sing N N 438 
TTP O2G   HOG2   sing N N 439 
TTP O3G   HOG3   sing N N 440 
TTP "O5'" "C5'"  sing N N 441 
TTP "C5'" "C4'"  sing N N 442 
TTP "C5'" "H5'1" sing N N 443 
TTP "C5'" "H5'2" sing N N 444 
TTP "C4'" "O4'"  sing N N 445 
TTP "C4'" "C3'"  sing N N 446 
TTP "C4'" "H4'"  sing N N 447 
TTP "O4'" "C1'"  sing N N 448 
TTP "C3'" "O3'"  sing N N 449 
TTP "C3'" "C2'"  sing N N 450 
TTP "C3'" "H3'"  sing N N 451 
TTP "O3'" "HO3'" sing N N 452 
TTP "C2'" "C1'"  sing N N 453 
TTP "C2'" "H2'1" sing N N 454 
TTP "C2'" "H2'2" sing N N 455 
TTP "C1'" N1     sing N N 456 
TTP "C1'" "H1'"  sing N N 457 
TTP N1    C2     sing N N 458 
TTP N1    C6     sing N N 459 
TTP C2    O2     doub N N 460 
TTP C2    N3     sing N N 461 
TTP N3    C4     sing N N 462 
TTP N3    HN3    sing N N 463 
TTP C4    O4     doub N N 464 
TTP C4    C5     sing N N 465 
TTP C5    C5M    sing N N 466 
TTP C5    C6     doub N N 467 
TTP C5M   HM51   sing N N 468 
TTP C5M   HM52   sing N N 469 
TTP C5M   HM53   sing N N 470 
TTP C6    H6     sing N N 471 
TYR N     CA     sing N N 472 
TYR N     H      sing N N 473 
TYR N     H2     sing N N 474 
TYR CA    C      sing N N 475 
TYR CA    CB     sing N N 476 
TYR CA    HA     sing N N 477 
TYR C     O      doub N N 478 
TYR C     OXT    sing N N 479 
TYR CB    CG     sing N N 480 
TYR CB    HB2    sing N N 481 
TYR CB    HB3    sing N N 482 
TYR CG    CD1    doub Y N 483 
TYR CG    CD2    sing Y N 484 
TYR CD1   CE1    sing Y N 485 
TYR CD1   HD1    sing N N 486 
TYR CD2   CE2    doub Y N 487 
TYR CD2   HD2    sing N N 488 
TYR CE1   CZ     doub Y N 489 
TYR CE1   HE1    sing N N 490 
TYR CE2   CZ     sing Y N 491 
TYR CE2   HE2    sing N N 492 
TYR CZ    OH     sing N N 493 
TYR OH    HH     sing N N 494 
TYR OXT   HXT    sing N N 495 
VAL N     CA     sing N N 496 
VAL N     H      sing N N 497 
VAL N     H2     sing N N 498 
VAL CA    C      sing N N 499 
VAL CA    CB     sing N N 500 
VAL CA    HA     sing N N 501 
VAL C     O      doub N N 502 
VAL C     OXT    sing N N 503 
VAL CB    CG1    sing N N 504 
VAL CB    CG2    sing N N 505 
VAL CB    HB     sing N N 506 
VAL CG1   HG11   sing N N 507 
VAL CG1   HG12   sing N N 508 
VAL CG1   HG13   sing N N 509 
VAL CG2   HG21   sing N N 510 
VAL CG2   HG22   sing N N 511 
VAL CG2   HG23   sing N N 512 
VAL OXT   HXT    sing N N 513 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-05-23 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9BY1 
_em_admin.last_update        2025-03-26 
_em_admin.map_release_date   2025-03-19 
_em_admin.title              'Consensus model for product 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 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 ? ? cryoSPARC ?            
'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                    9BY1 
_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   ? 103.943 117.072 98.011  1.00 62.08 ? 6   VAL A N     1 
ATOM   2     C  CA    . VAL A 1 6   ? 105.266 117.556 97.640  1.00 62.36 ? 6   VAL A CA    1 
ATOM   3     C  C     . VAL A 1 6   ? 105.127 118.718 96.656  1.00 62.94 ? 6   VAL A C     1 
ATOM   4     O  O     . VAL A 1 6   ? 104.239 118.713 95.800  1.00 63.15 ? 6   VAL A O     1 
ATOM   5     C  CB    . VAL A 1 6   ? 106.136 116.405 97.063  1.00 63.87 ? 6   VAL A CB    1 
ATOM   6     C  CG1   . VAL A 1 6   ? 105.897 116.212 95.570  1.00 62.06 ? 6   VAL A CG1   1 
ATOM   7     C  CG2   . VAL A 1 6   ? 107.608 116.643 97.350  1.00 61.45 ? 6   VAL A CG2   1 
ATOM   8     N  N     . PRO A 1 7   ? 105.967 119.742 96.811  1.00 59.20 ? 7   PRO A N     1 
ATOM   9     C  CA    . PRO A 1 7   ? 105.956 120.849 95.849  1.00 54.41 ? 7   PRO A CA    1 
ATOM   10    C  C     . PRO A 1 7   ? 106.323 120.367 94.455  1.00 56.89 ? 7   PRO A C     1 
ATOM   11    O  O     . PRO A 1 7   ? 107.140 119.461 94.281  1.00 60.99 ? 7   PRO A O     1 
ATOM   12    C  CB    . PRO A 1 7   ? 107.009 121.812 96.405  1.00 55.67 ? 7   PRO A CB    1 
ATOM   13    C  CG    . PRO A 1 7   ? 107.045 121.517 97.862  1.00 57.38 ? 7   PRO A CG    1 
ATOM   14    C  CD    . PRO A 1 7   ? 106.821 120.037 97.975  1.00 58.01 ? 7   PRO A CD    1 
ATOM   15    N  N     . LYS A 1 8   ? 105.699 120.986 93.452  1.00 57.74 ? 8   LYS A N     1 
ATOM   16    C  CA    . LYS A 1 8   ? 105.953 120.586 92.073  1.00 55.83 ? 8   LYS A CA    1 
ATOM   17    C  C     . LYS A 1 8   ? 107.387 120.891 91.663  1.00 56.92 ? 8   LYS A C     1 
ATOM   18    O  O     . LYS A 1 8   ? 108.013 120.110 90.936  1.00 58.10 ? 8   LYS A O     1 
ATOM   19    C  CB    . LYS A 1 8   ? 104.971 121.281 91.132  1.00 55.85 ? 8   LYS A CB    1 
ATOM   20    C  CG    . LYS A 1 8   ? 104.821 120.588 89.789  1.00 56.87 ? 8   LYS A CG    1 
ATOM   21    C  CD    . LYS A 1 8   ? 104.589 121.585 88.671  1.00 57.93 ? 8   LYS A CD    1 
ATOM   22    C  CE    . LYS A 1 8   ? 104.798 120.940 87.312  1.00 57.24 ? 8   LYS A CE    1 
ATOM   23    N  NZ    . LYS A 1 8   ? 105.331 121.910 86.317  1.00 59.26 ? 8   LYS A NZ    1 
ATOM   24    N  N     . TRP A 1 9   ? 107.923 122.026 92.117  1.00 57.42 ? 9   TRP A N     1 
ATOM   25    C  CA    . TRP A 1 9   ? 109.256 122.430 91.684  1.00 52.20 ? 9   TRP A CA    1 
ATOM   26    C  C     . TRP A 1 9   ? 110.335 121.526 92.267  1.00 54.07 ? 9   TRP A C     1 
ATOM   27    O  O     . TRP A 1 9   ? 111.297 121.184 91.572  1.00 58.26 ? 9   TRP A O     1 
ATOM   28    C  CB    . TRP A 1 9   ? 109.512 123.891 92.046  1.00 53.76 ? 9   TRP A CB    1 
ATOM   29    C  CG    . TRP A 1 9   ? 109.192 124.259 93.456  1.00 50.62 ? 9   TRP A CG    1 
ATOM   30    C  CD1   . TRP A 1 9   ? 110.020 124.170 94.529  1.00 51.26 ? 9   TRP A CD1   1 
ATOM   31    C  CD2   . TRP A 1 9   ? 107.958 124.794 93.945  1.00 51.19 ? 9   TRP A CD2   1 
ATOM   32    N  NE1   . TRP A 1 9   ? 109.380 124.605 95.663  1.00 52.80 ? 9   TRP A NE1   1 
ATOM   33    C  CE2   . TRP A 1 9   ? 108.111 124.996 95.329  1.00 52.42 ? 9   TRP A CE2   1 
ATOM   34    C  CE3   . TRP A 1 9   ? 106.738 125.117 93.347  1.00 51.40 ? 9   TRP A CE3   1 
ATOM   35    C  CZ2   . TRP A 1 9   ? 107.091 125.505 96.126  1.00 52.69 ? 9   TRP A CZ2   1 
ATOM   36    C  CZ3   . TRP A 1 9   ? 105.728 125.623 94.138  1.00 55.36 ? 9   TRP A CZ3   1 
ATOM   37    C  CH2   . TRP A 1 9   ? 105.909 125.812 95.512  1.00 54.79 ? 9   TRP A CH2   1 
ATOM   38    N  N     . ILE A 1 10  ? 110.202 121.122 93.533  1.00 54.83 ? 10  ILE A N     1 
ATOM   39    C  CA    . ILE A 1 10  ? 111.186 120.193 94.083  1.00 57.30 ? 10  ILE A CA    1 
ATOM   40    C  C     . ILE A 1 10  ? 110.983 118.782 93.553  1.00 56.17 ? 10  ILE A C     1 
ATOM   41    O  O     . ILE A 1 10  ? 111.934 117.991 93.543  1.00 59.88 ? 10  ILE A O     1 
ATOM   42    C  CB    . ILE A 1 10  ? 111.187 120.166 95.624  1.00 56.74 ? 10  ILE A CB    1 
ATOM   43    C  CG1   . ILE A 1 10  ? 110.197 119.136 96.164  1.00 58.20 ? 10  ILE A CG1   1 
ATOM   44    C  CG2   . ILE A 1 10  ? 110.903 121.534 96.200  1.00 56.16 ? 10  ILE A CG2   1 
ATOM   45    C  CD1   . ILE A 1 10  ? 110.393 118.838 97.629  1.00 58.86 ? 10  ILE A CD1   1 
ATOM   46    N  N     . GLN A 1 11  ? 109.771 118.437 93.115  1.00 57.56 ? 11  GLN A N     1 
ATOM   47    C  CA    . GLN A 1 11  ? 109.574 117.161 92.439  1.00 57.71 ? 11  GLN A CA    1 
ATOM   48    C  C     . GLN A 1 11  ? 110.276 117.150 91.088  1.00 57.23 ? 11  GLN A C     1 
ATOM   49    O  O     . GLN A 1 11  ? 110.916 116.159 90.722  1.00 59.27 ? 11  GLN A O     1 
ATOM   50    C  CB    . GLN A 1 11  ? 108.081 116.876 92.284  1.00 59.21 ? 11  GLN A CB    1 
ATOM   51    C  CG    . GLN A 1 11  ? 107.754 115.760 91.312  1.00 60.40 ? 11  GLN A CG    1 
ATOM   52    C  CD    . GLN A 1 11  ? 106.970 116.253 90.114  1.00 62.14 ? 11  GLN A CD    1 
ATOM   53    O  OE1   . GLN A 1 11  ? 105.994 116.988 90.258  1.00 60.81 ? 11  GLN A OE1   1 
ATOM   54    N  NE2   . GLN A 1 11  ? 107.395 115.853 88.922  1.00 60.87 ? 11  GLN A NE2   1 
ATOM   55    N  N     . LEU A 1 12  ? 110.172 118.250 90.338  1.00 56.86 ? 12  LEU A N     1 
ATOM   56    C  CA    . LEU A 1 12  ? 110.907 118.372 89.082  1.00 55.64 ? 12  LEU A CA    1 
ATOM   57    C  C     . LEU A 1 12  ? 112.411 118.396 89.323  1.00 57.82 ? 12  LEU A C     1 
ATOM   58    O  O     . LEU A 1 12  ? 113.182 117.833 88.537  1.00 60.33 ? 12  LEU A O     1 
ATOM   59    C  CB    . LEU A 1 12  ? 110.466 119.631 88.339  1.00 56.21 ? 12  LEU A CB    1 
ATOM   60    C  CG    . LEU A 1 12  ? 109.362 119.480 87.294  1.00 56.95 ? 12  LEU A CG    1 
ATOM   61    C  CD1   . LEU A 1 12  ? 108.622 120.794 87.116  1.00 55.54 ? 12  LEU A CD1   1 
ATOM   62    C  CD2   . LEU A 1 12  ? 109.941 119.004 85.973  1.00 57.80 ? 12  LEU A CD2   1 
ATOM   63    N  N     . ASN A 1 13  ? 112.846 119.056 90.398  1.00 56.01 ? 13  ASN A N     1 
ATOM   64    C  CA    . ASN A 1 13  ? 114.268 119.139 90.706  1.00 53.25 ? 13  ASN A CA    1 
ATOM   65    C  C     . ASN A 1 13  ? 114.842 117.782 91.089  1.00 55.37 ? 13  ASN A C     1 
ATOM   66    O  O     . ASN A 1 13  ? 116.037 117.539 90.893  1.00 60.87 ? 13  ASN A O     1 
ATOM   67    C  CB    . ASN A 1 13  ? 114.495 120.154 91.828  1.00 56.47 ? 13  ASN A CB    1 
ATOM   68    C  CG    . ASN A 1 13  ? 115.941 120.226 92.269  1.00 56.88 ? 13  ASN A CG    1 
ATOM   69    O  OD1   . ASN A 1 13  ? 116.314 119.676 93.304  1.00 55.70 ? 13  ASN A OD1   1 
ATOM   70    N  ND2   . ASN A 1 13  ? 116.765 120.910 91.485  1.00 56.67 ? 13  ASN A ND2   1 
ATOM   71    N  N     . ASN A 1 14  ? 114.014 116.890 91.631  1.00 58.64 ? 14  ASN A N     1 
ATOM   72    C  CA    . ASN A 1 14  ? 114.468 115.550 91.978  1.00 59.26 ? 14  ASN A CA    1 
ATOM   73    C  C     . ASN A 1 14  ? 114.542 114.621 90.775  1.00 58.44 ? 14  ASN A C     1 
ATOM   74    O  O     . ASN A 1 14  ? 115.083 113.518 90.901  1.00 60.97 ? 14  ASN A O     1 
ATOM   75    C  CB    . ASN A 1 14  ? 113.552 114.944 93.044  1.00 57.34 ? 14  ASN A CB    1 
ATOM   76    C  CG    . ASN A 1 14  ? 113.817 115.505 94.426  1.00 59.55 ? 14  ASN A CG    1 
ATOM   77    O  OD1   . ASN A 1 14  ? 114.181 116.670 94.576  1.00 61.58 ? 14  ASN A OD1   1 
ATOM   78    N  ND2   . ASN A 1 14  ? 113.634 114.676 95.446  1.00 59.86 ? 14  ASN A ND2   1 
ATOM   79    N  N     . GLU A 1 15  ? 114.022 115.034 89.621  1.00 58.78 ? 15  GLU A N     1 
ATOM   80    C  CA    . GLU A 1 15  ? 114.135 114.244 88.402  1.00 59.98 ? 15  GLU A CA    1 
ATOM   81    C  C     . GLU A 1 15  ? 115.503 114.370 87.748  1.00 62.82 ? 15  GLU A C     1 
ATOM   82    O  O     . GLU A 1 15  ? 115.754 113.697 86.742  1.00 64.95 ? 15  GLU A O     1 
ATOM   83    C  CB    . GLU A 1 15  ? 113.046 114.646 87.404  1.00 59.81 ? 15  GLU A CB    1 
ATOM   84    C  CG    . GLU A 1 15  ? 111.668 114.796 88.020  1.00 60.71 ? 15  GLU A CG    1 
ATOM   85    C  CD    . GLU A 1 15  ? 110.557 114.788 86.988  1.00 64.69 ? 15  GLU A CD    1 
ATOM   86    O  OE1   . GLU A 1 15  ? 110.864 114.870 85.782  1.00 64.54 ? 15  GLU A OE1   1 
ATOM   87    O  OE2   . GLU A 1 15  ? 109.376 114.700 87.386  1.00 65.10 ? 15  GLU A OE2   1 
ATOM   88    N  N     . ILE A 1 16  ? 116.381 115.220 88.282  1.00 60.12 ? 16  ILE A N     1 
ATOM   89    C  CA    . ILE A 1 16  ? 117.749 115.294 87.779  1.00 59.81 ? 16  ILE A CA    1 
ATOM   90    C  C     . ILE A 1 16  ? 118.473 113.978 88.023  1.00 60.22 ? 16  ILE A C     1 
ATOM   91    O  O     . ILE A 1 16  ? 119.191 113.473 87.151  1.00 61.32 ? 16  ILE A O     1 
ATOM   92    C  CB    . ILE A 1 16  ? 118.494 116.478 88.424  1.00 59.71 ? 16  ILE A CB    1 
ATOM   93    C  CG1   . ILE A 1 16  ? 117.782 117.795 88.113  1.00 57.94 ? 16  ILE A CG1   1 
ATOM   94    C  CG2   . ILE A 1 16  ? 119.939 116.529 87.949  1.00 60.14 ? 16  ILE A CG2   1 
ATOM   95    C  CD1   . ILE A 1 16  ? 118.282 118.963 88.931  1.00 57.42 ? 16  ILE A CD1   1 
ATOM   96    N  N     . MET A 1 17  ? 118.291 113.398 89.210  1.00 61.96 ? 17  MET A N     1 
ATOM   97    C  CA    . MET A 1 17  ? 118.985 112.169 89.569  1.00 63.31 ? 17  MET A CA    1 
ATOM   98    C  C     . MET A 1 17  ? 118.398 110.936 88.898  1.00 63.95 ? 17  MET A C     1 
ATOM   99    O  O     . MET A 1 17  ? 119.080 109.909 88.823  1.00 65.07 ? 17  MET A O     1 
ATOM   100   C  CB    . MET A 1 17  ? 118.966 111.986 91.085  1.00 62.46 ? 17  MET A CB    1 
ATOM   101   C  CG    . MET A 1 17  ? 119.433 113.210 91.839  1.00 63.05 ? 17  MET A CG    1 
ATOM   102   S  SD    . MET A 1 17  ? 120.982 113.876 91.202  1.00 68.49 ? 17  MET A SD    1 
ATOM   103   C  CE    . MET A 1 17  ? 122.171 112.869 92.083  1.00 62.35 ? 17  MET A CE    1 
ATOM   104   N  N     . ILE A 1 18  ? 117.160 111.007 88.415  1.00 64.18 ? 18  ILE A N     1 
ATOM   105   C  CA    . ILE A 1 18  ? 116.585 109.894 87.665  1.00 65.89 ? 18  ILE A CA    1 
ATOM   106   C  C     . ILE A 1 18  ? 117.328 109.811 86.335  1.00 66.86 ? 18  ILE A C     1 
ATOM   107   O  O     . ILE A 1 18  ? 117.162 110.669 85.464  1.00 67.73 ? 18  ILE A O     1 
ATOM   108   C  CB    . ILE A 1 18  ? 115.071 110.050 87.456  1.00 66.91 ? 18  ILE A CB    1 
ATOM   109   C  CG1   . ILE A 1 18  ? 114.252 109.790 88.737  1.00 66.13 ? 18  ILE A CG1   1 
ATOM   110   C  CG2   . ILE A 1 18  ? 114.584 109.113 86.358  1.00 66.27 ? 18  ILE A CG2   1 
ATOM   111   C  CD1   . ILE A 1 18  ? 114.707 110.460 90.019  1.00 65.53 ? 18  ILE A CD1   1 
ATOM   112   N  N     . GLN A 1 19  ? 118.163 108.787 86.185  1.00 71.05 ? 19  GLN A N     1 
ATOM   113   C  CA    . GLN A 1 19  ? 119.034 108.677 85.024  1.00 71.87 ? 19  GLN A CA    1 
ATOM   114   C  C     . GLN A 1 19  ? 118.251 108.116 83.846  1.00 71.30 ? 19  GLN A C     1 
ATOM   115   O  O     . GLN A 1 19  ? 117.816 106.960 83.873  1.00 73.51 ? 19  GLN A O     1 
ATOM   116   C  CB    . GLN A 1 19  ? 120.238 107.795 85.347  1.00 73.09 ? 19  GLN A CB    1 
ATOM   117   C  CG    . GLN A 1 19  ? 121.206 108.415 86.343  1.00 71.71 ? 19  GLN A CG    1 
ATOM   118   C  CD    . GLN A 1 19  ? 122.419 107.543 86.602  1.00 73.20 ? 19  GLN A CD    1 
ATOM   119   O  OE1   . GLN A 1 19  ? 122.544 106.453 86.045  1.00 72.86 ? 19  GLN A OE1   1 
ATOM   120   N  NE2   . GLN A 1 19  ? 123.318 108.020 87.454  1.00 72.98 ? 19  GLN A NE2   1 
ATOM   121   N  N     . LYS A 1 20  ? 118.074 108.934 82.814  1.00 72.06 ? 20  LYS A N     1 
ATOM   122   C  CA    . LYS A 1 20  ? 117.392 108.535 81.591  1.00 74.28 ? 20  LYS A CA    1 
ATOM   123   C  C     . LYS A 1 20  ? 118.434 108.370 80.494  1.00 74.99 ? 20  LYS A C     1 
ATOM   124   O  O     . LYS A 1 20  ? 119.194 109.304 80.212  1.00 74.94 ? 20  LYS A O     1 
ATOM   125   C  CB    . LYS A 1 20  ? 116.336 109.564 81.191  1.00 73.59 ? 20  LYS A CB    1 
ATOM   126   C  CG    . LYS A 1 20  ? 115.740 109.338 79.813  1.00 73.75 ? 20  LYS A CG    1 
ATOM   127   C  CD    . LYS A 1 20  ? 115.574 110.647 79.062  1.00 74.93 ? 20  LYS A CD    1 
ATOM   128   C  CE    . LYS A 1 20  ? 116.853 111.468 79.096  1.00 75.21 ? 20  LYS A CE    1 
ATOM   129   N  NZ    . LYS A 1 20  ? 117.990 110.754 78.455  1.00 75.02 ? 20  LYS A NZ    1 
ATOM   130   N  N     . ASP A 1 21  ? 118.466 107.184 79.884  1.00 73.95 ? 21  ASP A N     1 
ATOM   131   C  CA    . ASP A 1 21  ? 119.450 106.845 78.854  1.00 74.93 ? 21  ASP A CA    1 
ATOM   132   C  C     . ASP A 1 21  ? 120.877 106.976 79.385  1.00 75.37 ? 21  ASP A C     1 
ATOM   133   O  O     . ASP A 1 21  ? 121.792 107.383 78.668  1.00 73.35 ? 21  ASP A O     1 
ATOM   134   C  CB    . ASP A 1 21  ? 119.255 107.697 77.598  1.00 75.14 ? 21  ASP A CB    1 
ATOM   135   C  CG    . ASP A 1 21  ? 117.802 107.790 77.177  1.00 76.00 ? 21  ASP A CG    1 
ATOM   136   O  OD1   . ASP A 1 21  ? 117.082 106.775 77.292  1.00 74.51 ? 21  ASP A OD1   1 
ATOM   137   O  OD2   . ASP A 1 21  ? 117.380 108.877 76.731  1.00 75.49 ? 21  ASP A OD2   1 
ATOM   138   N  N     . GLY A 1 22  ? 121.067 106.626 80.656  1.00 75.34 ? 22  GLY A N     1 
ATOM   139   C  CA    . GLY A 1 22  ? 122.384 106.631 81.258  1.00 75.44 ? 22  GLY A CA    1 
ATOM   140   C  C     . GLY A 1 22  ? 122.942 107.992 81.601  1.00 75.59 ? 22  GLY A C     1 
ATOM   141   O  O     . GLY A 1 22  ? 124.134 108.090 81.915  1.00 74.31 ? 22  GLY A O     1 
ATOM   142   N  N     . LYS A 1 23  ? 122.129 109.045 81.554  1.00 72.10 ? 23  LYS A N     1 
ATOM   143   C  CA    . LYS A 1 23  ? 122.590 110.396 81.830  1.00 69.79 ? 23  LYS A CA    1 
ATOM   144   C  C     . LYS A 1 23  ? 121.658 111.074 82.822  1.00 70.60 ? 23  LYS A C     1 
ATOM   145   O  O     . LYS A 1 23  ? 120.454 110.805 82.853  1.00 71.94 ? 23  LYS A O     1 
ATOM   146   C  CB    . LYS A 1 23  ? 122.666 111.239 80.550  1.00 69.81 ? 23  LYS A CB    1 
ATOM   147   C  CG    . LYS A 1 23  ? 123.748 110.815 79.575  1.00 69.94 ? 23  LYS A CG    1 
ATOM   148   C  CD    . LYS A 1 23  ? 123.793 111.759 78.385  1.00 70.00 ? 23  LYS A CD    1 
ATOM   149   C  CE    . LYS A 1 23  ? 124.789 111.296 77.340  1.00 70.12 ? 23  LYS A CE    1 
ATOM   150   N  NZ    . LYS A 1 23  ? 124.780 112.185 76.146  1.00 68.96 ? 23  LYS A NZ    1 
ATOM   151   N  N     . PHE A 1 24  ? 122.230 111.959 83.634  1.00 63.59 ? 24  PHE A N     1 
ATOM   152   C  CA    . PHE A 1 24  ? 121.425 112.792 84.516  1.00 60.70 ? 24  PHE A CA    1 
ATOM   153   C  C     . PHE A 1 24  ? 120.572 113.750 83.695  1.00 60.99 ? 24  PHE A C     1 
ATOM   154   O  O     . PHE A 1 24  ? 121.017 114.288 82.678  1.00 59.82 ? 24  PHE A O     1 
ATOM   155   C  CB    . PHE A 1 24  ? 122.318 113.582 85.471  1.00 59.57 ? 24  PHE A CB    1 
ATOM   156   C  CG    . PHE A 1 24  ? 122.960 112.746 86.537  1.00 60.31 ? 24  PHE A CG    1 
ATOM   157   C  CD1   . PHE A 1 24  ? 122.273 112.434 87.697  1.00 60.91 ? 24  PHE A CD1   1 
ATOM   158   C  CD2   . PHE A 1 24  ? 124.252 112.277 86.383  1.00 60.12 ? 24  PHE A CD2   1 
ATOM   159   C  CE1   . PHE A 1 24  ? 122.862 111.666 88.681  1.00 60.97 ? 24  PHE A CE1   1 
ATOM   160   C  CE2   . PHE A 1 24  ? 124.846 111.509 87.364  1.00 59.58 ? 24  PHE A CE2   1 
ATOM   161   C  CZ    . PHE A 1 24  ? 124.150 111.203 88.514  1.00 60.68 ? 24  PHE A CZ    1 
ATOM   162   N  N     . GLN A 1 25  ? 119.335 113.960 84.142  1.00 62.04 ? 25  GLN A N     1 
ATOM   163   C  CA    . GLN A 1 25  ? 118.417 114.877 83.468  1.00 60.23 ? 25  GLN A CA    1 
ATOM   164   C  C     . GLN A 1 25  ? 118.670 116.282 84.006  1.00 61.10 ? 25  GLN A C     1 
ATOM   165   O  O     . GLN A 1 25  ? 117.961 116.794 84.875  1.00 61.60 ? 25  GLN A O     1 
ATOM   166   C  CB    . GLN A 1 25  ? 116.974 114.437 83.668  1.00 61.35 ? 25  GLN A CB    1 
ATOM   167   C  CG    . GLN A 1 25  ? 116.682 113.035 83.163  1.00 61.72 ? 25  GLN A CG    1 
ATOM   168   C  CD    . GLN A 1 25  ? 115.224 112.655 83.314  1.00 62.94 ? 25  GLN A CD    1 
ATOM   169   O  OE1   . GLN A 1 25  ? 114.409 112.915 82.430  1.00 62.62 ? 25  GLN A OE1   1 
ATOM   170   N  NE2   . GLN A 1 25  ? 114.888 112.034 84.438  1.00 61.33 ? 25  GLN A NE2   1 
ATOM   171   N  N     . PHE A 1 26  ? 119.716 116.912 83.469  1.00 56.99 ? 26  PHE A N     1 
ATOM   172   C  CA    . PHE A 1 26  ? 120.110 118.234 83.944  1.00 56.24 ? 26  PHE A CA    1 
ATOM   173   C  C     . PHE A 1 26  ? 119.104 119.304 83.541  1.00 57.79 ? 26  PHE A C     1 
ATOM   174   O  O     . PHE A 1 26  ? 118.962 120.311 84.243  1.00 57.02 ? 26  PHE A O     1 
ATOM   175   C  CB    . PHE A 1 26  ? 121.501 118.586 83.418  1.00 53.89 ? 26  PHE A CB    1 
ATOM   176   C  CG    . PHE A 1 26  ? 122.602 117.771 84.030  1.00 54.46 ? 26  PHE A CG    1 
ATOM   177   C  CD1   . PHE A 1 26  ? 122.771 117.732 85.403  1.00 54.79 ? 26  PHE A CD1   1 
ATOM   178   C  CD2   . PHE A 1 26  ? 123.466 117.041 83.234  1.00 55.62 ? 26  PHE A CD2   1 
ATOM   179   C  CE1   . PHE A 1 26  ? 123.783 116.981 85.969  1.00 53.74 ? 26  PHE A CE1   1 
ATOM   180   C  CE2   . PHE A 1 26  ? 124.479 116.289 83.795  1.00 54.22 ? 26  PHE A CE2   1 
ATOM   181   C  CZ    . PHE A 1 26  ? 124.637 116.261 85.164  1.00 51.86 ? 26  PHE A CZ    1 
ATOM   182   N  N     . ASP A 1 27  ? 118.401 119.108 82.424  1.00 62.94 ? 27  ASP A N     1 
ATOM   183   C  CA    . ASP A 1 27  ? 117.420 120.085 81.967  1.00 62.05 ? 27  ASP A CA    1 
ATOM   184   C  C     . ASP A 1 27  ? 116.208 120.183 82.883  1.00 62.72 ? 27  ASP A C     1 
ATOM   185   O  O     . ASP A 1 27  ? 115.417 121.120 82.731  1.00 63.39 ? 27  ASP A O     1 
ATOM   186   C  CB    . ASP A 1 27  ? 116.962 119.746 80.548  1.00 61.99 ? 27  ASP A CB    1 
ATOM   187   C  CG    . ASP A 1 27  ? 116.959 120.955 79.633  1.00 65.87 ? 27  ASP A CG    1 
ATOM   188   O  OD1   . ASP A 1 27  ? 116.956 120.769 78.398  1.00 67.54 ? 27  ASP A OD1   1 
ATOM   189   O  OD2   . ASP A 1 27  ? 116.960 122.092 80.148  1.00 65.89 ? 27  ASP A OD2   1 
ATOM   190   N  N     . LYS A 1 28  ? 116.039 119.245 83.817  1.00 58.95 ? 28  LYS A N     1 
ATOM   191   C  CA    . LYS A 1 28  ? 114.916 119.319 84.743  1.00 59.29 ? 28  LYS A CA    1 
ATOM   192   C  C     . LYS A 1 28  ? 115.026 120.522 85.669  1.00 60.24 ? 28  LYS A C     1 
ATOM   193   O  O     . LYS A 1 28  ? 114.005 121.031 86.143  1.00 62.62 ? 28  LYS A O     1 
ATOM   194   C  CB    . LYS A 1 28  ? 114.823 118.031 85.561  1.00 59.19 ? 28  LYS A CB    1 
ATOM   195   C  CG    . LYS A 1 28  ? 114.463 116.809 84.741  1.00 60.79 ? 28  LYS A CG    1 
ATOM   196   C  CD    . LYS A 1 28  ? 113.007 116.838 84.317  1.00 61.67 ? 28  LYS A CD    1 
ATOM   197   C  CE    . LYS A 1 28  ? 112.718 115.770 83.277  1.00 61.08 ? 28  LYS A CE    1 
ATOM   198   N  NZ    . LYS A 1 28  ? 111.268 115.694 82.952  1.00 62.13 ? 28  LYS A NZ    1 
ATOM   199   N  N     . ASP A 1 29  ? 116.248 120.988 85.939  1.00 56.67 ? 29  ASP A N     1 
ATOM   200   C  CA    . ASP A 1 29  ? 116.422 122.125 86.837  1.00 54.62 ? 29  ASP A CA    1 
ATOM   201   C  C     . ASP A 1 29  ? 115.889 123.413 86.226  1.00 53.85 ? 29  ASP A C     1 
ATOM   202   O  O     . ASP A 1 29  ? 115.435 124.300 86.957  1.00 55.46 ? 29  ASP A O     1 
ATOM   203   C  CB    . ASP A 1 29  ? 117.895 122.280 87.209  1.00 53.50 ? 29  ASP A CB    1 
ATOM   204   C  CG    . ASP A 1 29  ? 118.097 122.494 88.694  1.00 56.62 ? 29  ASP A CG    1 
ATOM   205   O  OD1   . ASP A 1 29  ? 117.212 122.092 89.477  1.00 56.53 ? 29  ASP A OD1   1 
ATOM   206   O  OD2   . ASP A 1 29  ? 119.142 123.057 89.080  1.00 55.51 ? 29  ASP A OD2   1 
ATOM   207   N  N     . LYS A 1 30  ? 115.943 123.543 84.899  1.00 53.96 ? 30  LYS A N     1 
ATOM   208   C  CA    . LYS A 1 30  ? 115.295 124.673 84.243  1.00 56.53 ? 30  LYS A CA    1 
ATOM   209   C  C     . LYS A 1 30  ? 113.782 124.595 84.408  1.00 55.08 ? 30  LYS A C     1 
ATOM   210   O  O     . LYS A 1 30  ? 113.127 125.590 84.744  1.00 59.19 ? 30  LYS A O     1 
ATOM   211   C  CB    . LYS A 1 30  ? 115.680 124.711 82.765  1.00 55.73 ? 30  LYS A CB    1 
ATOM   212   C  CG    . LYS A 1 30  ? 115.097 125.884 81.999  1.00 57.13 ? 30  LYS A CG    1 
ATOM   213   C  CD    . LYS A 1 30  ? 116.103 126.448 81.010  1.00 57.38 ? 30  LYS A CD    1 
ATOM   214   C  CE    . LYS A 1 30  ? 115.544 127.659 80.283  1.00 57.36 ? 30  LYS A CE    1 
ATOM   215   N  NZ    . LYS A 1 30  ? 115.038 127.305 78.928  1.00 55.86 ? 30  LYS A NZ    1 
ATOM   216   N  N     . GLU A 1 31  ? 113.212 123.409 84.192  1.00 53.14 ? 31  GLU A N     1 
ATOM   217   C  CA    . GLU A 1 31  ? 111.794 123.213 84.469  1.00 53.63 ? 31  GLU A CA    1 
ATOM   218   C  C     . GLU A 1 31  ? 111.506 123.377 85.954  1.00 54.84 ? 31  GLU A C     1 
ATOM   219   O  O     . GLU A 1 31  ? 110.454 123.902 86.336  1.00 56.85 ? 31  GLU A O     1 
ATOM   220   C  CB    . GLU A 1 31  ? 111.347 121.835 83.984  1.00 55.58 ? 31  GLU A CB    1 
ATOM   221   C  CG    . GLU A 1 31  ? 110.888 121.805 82.538  1.00 57.10 ? 31  GLU A CG    1 
ATOM   222   C  CD    . GLU A 1 31  ? 111.169 120.478 81.865  1.00 60.81 ? 31  GLU A CD    1 
ATOM   223   O  OE1   . GLU A 1 31  ? 111.872 119.641 82.468  1.00 61.34 ? 31  GLU A OE1   1 
ATOM   224   O  OE2   . GLU A 1 31  ? 110.687 120.270 80.731  1.00 57.68 ? 31  GLU A OE2   1 
ATOM   225   N  N     . ALA A 1 32  ? 112.437 122.943 86.808  1.00 50.21 ? 32  ALA A N     1 
ATOM   226   C  CA    . ALA A 1 32  ? 112.244 123.088 88.246  1.00 49.74 ? 32  ALA A CA    1 
ATOM   227   C  C     . ALA A 1 32  ? 112.150 124.553 88.647  1.00 52.52 ? 32  ALA A C     1 
ATOM   228   O  O     . ALA A 1 32  ? 111.261 124.933 89.414  1.00 52.64 ? 32  ALA A O     1 
ATOM   229   C  CB    . ALA A 1 32  ? 113.378 122.399 89.003  1.00 49.37 ? 32  ALA A CB    1 
ATOM   230   N  N     . VAL A 1 33  ? 113.043 125.398 88.125  1.00 53.89 ? 33  VAL A N     1 
ATOM   231   C  CA    . VAL A 1 33  ? 113.010 126.812 88.489  1.00 52.11 ? 33  VAL A CA    1 
ATOM   232   C  C     . VAL A 1 33  ? 111.815 127.508 87.844  1.00 52.88 ? 33  VAL A C     1 
ATOM   233   O  O     . VAL A 1 33  ? 111.212 128.410 88.440  1.00 54.45 ? 33  VAL A O     1 
ATOM   234   C  CB    . VAL A 1 33  ? 114.346 127.497 88.137  1.00 49.65 ? 33  VAL A CB    1 
ATOM   235   C  CG1   . VAL A 1 33  ? 114.510 127.676 86.639  1.00 50.94 ? 33  VAL A CG1   1 
ATOM   236   C  CG2   . VAL A 1 33  ? 114.457 128.835 88.850  1.00 49.63 ? 33  VAL A CG2   1 
ATOM   237   N  N     . HIS A 1 34  ? 111.443 127.100 86.627  1.00 51.21 ? 34  HIS A N     1 
ATOM   238   C  CA    . HIS A 1 34  ? 110.265 127.677 85.986  1.00 50.61 ? 34  HIS A CA    1 
ATOM   239   C  C     . HIS A 1 34  ? 109.011 127.390 86.804  1.00 52.91 ? 34  HIS A C     1 
ATOM   240   O  O     . HIS A 1 34  ? 108.192 128.286 87.052  1.00 53.52 ? 34  HIS A O     1 
ATOM   241   C  CB    . HIS A 1 34  ? 110.142 127.128 84.561  1.00 52.99 ? 34  HIS A CB    1 
ATOM   242   C  CG    . HIS A 1 34  ? 109.076 127.782 83.734  1.00 54.53 ? 34  HIS A CG    1 
ATOM   243   N  ND1   . HIS A 1 34  ? 107.845 128.142 84.237  1.00 54.99 ? 34  HIS A ND1   1 
ATOM   244   C  CD2   . HIS A 1 34  ? 109.066 128.142 82.428  1.00 54.31 ? 34  HIS A CD2   1 
ATOM   245   C  CE1   . HIS A 1 34  ? 107.121 128.691 83.278  1.00 55.53 ? 34  HIS A CE1   1 
ATOM   246   N  NE2   . HIS A 1 34  ? 107.840 128.704 82.171  1.00 55.75 ? 34  HIS A NE2   1 
ATOM   247   N  N     . SER A 1 35  ? 108.853 126.138 87.244  1.00 54.52 ? 35  SER A N     1 
ATOM   248   C  CA    . SER A 1 35  ? 107.725 125.782 88.095  1.00 51.71 ? 35  SER A CA    1 
ATOM   249   C  C     . SER A 1 35  ? 107.802 126.494 89.437  1.00 52.17 ? 35  SER A C     1 
ATOM   250   O  O     . SER A 1 35  ? 106.783 126.965 89.953  1.00 54.95 ? 35  SER A O     1 
ATOM   251   C  CB    . SER A 1 35  ? 107.675 124.268 88.294  1.00 52.04 ? 35  SER A CB    1 
ATOM   252   O  OG    . SER A 1 35  ? 106.876 123.932 89.414  1.00 53.94 ? 35  SER A OG    1 
ATOM   253   N  N     . TYR A 1 36  ? 109.002 126.581 90.016  1.00 51.96 ? 36  TYR A N     1 
ATOM   254   C  CA    . TYR A 1 36  ? 109.179 127.293 91.276  1.00 51.28 ? 36  TYR A CA    1 
ATOM   255   C  C     . TYR A 1 36  ? 108.646 128.709 91.169  1.00 48.05 ? 36  TYR A C     1 
ATOM   256   O  O     . TYR A 1 36  ? 107.837 129.145 91.993  1.00 48.40 ? 36  TYR A O     1 
ATOM   257   C  CB    . TYR A 1 36  ? 110.657 127.303 91.665  1.00 48.18 ? 36  TYR A CB    1 
ATOM   258   C  CG    . TYR A 1 36  ? 110.969 128.102 92.908  1.00 49.55 ? 36  TYR A CG    1 
ATOM   259   C  CD1   . TYR A 1 36  ? 110.401 127.773 94.131  1.00 47.79 ? 36  TYR A CD1   1 
ATOM   260   C  CD2   . TYR A 1 36  ? 111.840 129.182 92.860  1.00 48.72 ? 36  TYR A CD2   1 
ATOM   261   C  CE1   . TYR A 1 36  ? 110.689 128.497 95.269  1.00 46.21 ? 36  TYR A CE1   1 
ATOM   262   C  CE2   . TYR A 1 36  ? 112.133 129.913 93.992  1.00 47.00 ? 36  TYR A CE2   1 
ATOM   263   C  CZ    . TYR A 1 36  ? 111.556 129.566 95.194  1.00 48.20 ? 36  TYR A CZ    1 
ATOM   264   O  OH    . TYR A 1 36  ? 111.845 130.292 96.324  1.00 49.93 ? 36  TYR A OH    1 
ATOM   265   N  N     . PHE A 1 37  ? 109.046 129.422 90.119  1.00 52.33 ? 37  PHE A N     1 
ATOM   266   C  CA    . PHE A 1 37  ? 108.562 130.783 89.939  1.00 52.03 ? 37  PHE A CA    1 
ATOM   267   C  C     . PHE A 1 37  ? 107.053 130.801 89.749  1.00 53.00 ? 37  PHE A C     1 
ATOM   268   O  O     . PHE A 1 37  ? 106.326 131.308 90.610  1.00 56.08 ? 37  PHE A O     1 
ATOM   269   C  CB    . PHE A 1 37  ? 109.280 131.451 88.771  1.00 54.27 ? 37  PHE A CB    1 
ATOM   270   C  CG    . PHE A 1 37  ? 110.554 132.120 89.173  1.00 53.33 ? 37  PHE A CG    1 
ATOM   271   C  CD1   . PHE A 1 37  ? 110.534 133.384 89.733  1.00 50.94 ? 37  PHE A CD1   1 
ATOM   272   C  CD2   . PHE A 1 37  ? 111.767 131.476 89.027  1.00 52.97 ? 37  PHE A CD2   1 
ATOM   273   C  CE1   . PHE A 1 37  ? 111.701 134.000 90.120  1.00 52.14 ? 37  PHE A CE1   1 
ATOM   274   C  CE2   . PHE A 1 37  ? 112.935 132.089 89.411  1.00 52.60 ? 37  PHE A CE2   1 
ATOM   275   C  CZ    . PHE A 1 37  ? 112.903 133.351 89.962  1.00 53.07 ? 37  PHE A CZ    1 
ATOM   276   N  N     . VAL A 1 38  ? 106.560 130.166 88.681  1.00 56.29 ? 38  VAL A N     1 
ATOM   277   C  CA    . VAL A 1 38  ? 105.152 130.298 88.319  1.00 55.98 ? 38  VAL A CA    1 
ATOM   278   C  C     . VAL A 1 38  ? 104.199 129.611 89.286  1.00 55.09 ? 38  VAL A C     1 
ATOM   279   O  O     . VAL A 1 38  ? 102.982 129.691 89.089  1.00 57.17 ? 38  VAL A O     1 
ATOM   280   C  CB    . VAL A 1 38  ? 104.889 129.760 86.898  1.00 54.17 ? 38  VAL A CB    1 
ATOM   281   C  CG1   . VAL A 1 38  ? 105.841 130.402 85.907  1.00 54.99 ? 38  VAL A CG1   1 
ATOM   282   C  CG2   . VAL A 1 38  ? 105.000 128.244 86.871  1.00 52.11 ? 38  VAL A CG2   1 
ATOM   283   N  N     . ASP A 1 39  ? 104.702 128.941 90.325  1.00 54.44 ? 39  ASP A N     1 
ATOM   284   C  CA    . ASP A 1 39  ? 103.825 128.336 91.314  1.00 53.35 ? 39  ASP A CA    1 
ATOM   285   C  C     . ASP A 1 39  ? 104.018 128.856 92.730  1.00 57.86 ? 39  ASP A C     1 
ATOM   286   O  O     . ASP A 1 39  ? 103.105 128.696 93.547  1.00 62.07 ? 39  ASP A O     1 
ATOM   287   C  CB    . ASP A 1 39  ? 104.003 126.809 91.326  1.00 55.43 ? 39  ASP A CB    1 
ATOM   288   C  CG    . ASP A 1 39  ? 103.728 126.179 89.974  1.00 59.11 ? 39  ASP A CG    1 
ATOM   289   O  OD1   . ASP A 1 39  ? 102.896 126.725 89.220  1.00 59.45 ? 39  ASP A OD1   1 
ATOM   290   O  OD2   . ASP A 1 39  ? 104.343 125.137 89.665  1.00 59.18 ? 39  ASP A OD2   1 
ATOM   291   N  N     . TYR A 1 40  ? 105.160 129.460 93.053  1.00 55.84 ? 40  TYR A N     1 
ATOM   292   C  CA    . TYR A 1 40  ? 105.381 130.027 94.375  1.00 54.78 ? 40  TYR A CA    1 
ATOM   293   C  C     . TYR A 1 40  ? 105.696 131.513 94.331  1.00 58.84 ? 40  TYR A C     1 
ATOM   294   O  O     . TYR A 1 40  ? 105.101 132.290 95.085  1.00 61.31 ? 40  TYR A O     1 
ATOM   295   C  CB    . TYR A 1 40  ? 106.520 129.273 95.080  1.00 53.50 ? 40  TYR A CB    1 
ATOM   296   C  CG    . TYR A 1 40  ? 106.653 129.595 96.548  1.00 54.49 ? 40  TYR A CG    1 
ATOM   297   C  CD1   . TYR A 1 40  ? 105.617 129.330 97.433  1.00 55.50 ? 40  TYR A CD1   1 
ATOM   298   C  CD2   . TYR A 1 40  ? 107.814 130.165 97.049  1.00 55.19 ? 40  TYR A CD2   1 
ATOM   299   C  CE1   . TYR A 1 40  ? 105.735 129.624 98.776  1.00 57.83 ? 40  TYR A CE1   1 
ATOM   300   C  CE2   . TYR A 1 40  ? 107.941 130.462 98.390  1.00 57.88 ? 40  TYR A CE2   1 
ATOM   301   C  CZ    . TYR A 1 40  ? 106.899 130.190 99.249  1.00 60.48 ? 40  TYR A CZ    1 
ATOM   302   O  OH    . TYR A 1 40  ? 107.021 130.485 100.588 1.00 60.61 ? 40  TYR A OH    1 
ATOM   303   N  N     . ILE A 1 41  ? 106.604 131.934 93.451  1.00 54.90 ? 41  ILE A N     1 
ATOM   304   C  CA    . ILE A 1 41  ? 107.197 133.259 93.580  1.00 53.59 ? 41  ILE A CA    1 
ATOM   305   C  C     . ILE A 1 41  ? 106.246 134.329 93.065  1.00 53.32 ? 41  ILE A C     1 
ATOM   306   O  O     . ILE A 1 41  ? 105.964 135.311 93.759  1.00 55.78 ? 41  ILE A O     1 
ATOM   307   C  CB    . ILE A 1 41  ? 108.553 133.309 92.851  1.00 52.66 ? 41  ILE A CB    1 
ATOM   308   C  CG1   . ILE A 1 41  ? 109.554 132.368 93.523  1.00 51.31 ? 41  ILE A CG1   1 
ATOM   309   C  CG2   . ILE A 1 41  ? 109.094 134.727 92.828  1.00 52.11 ? 41  ILE A CG2   1 
ATOM   310   C  CD1   . ILE A 1 41  ? 109.835 132.707 94.963  1.00 48.48 ? 41  ILE A CD1   1 
ATOM   311   N  N     . ASN A 1 42  ? 105.736 134.154 91.844  1.00 54.78 ? 42  ASN A N     1 
ATOM   312   C  CA    . ASN A 1 42  ? 104.787 135.118 91.301  1.00 56.27 ? 42  ASN A CA    1 
ATOM   313   C  C     . ASN A 1 42  ? 103.507 135.163 92.123  1.00 60.05 ? 42  ASN A C     1 
ATOM   314   O  O     . ASN A 1 42  ? 102.847 136.206 92.190  1.00 60.07 ? 42  ASN A O     1 
ATOM   315   C  CB    . ASN A 1 42  ? 104.477 134.781 89.843  1.00 55.74 ? 42  ASN A CB    1 
ATOM   316   C  CG    . ASN A 1 42  ? 105.718 134.766 88.973  1.00 57.04 ? 42  ASN A CG    1 
ATOM   317   O  OD1   . ASN A 1 42  ? 106.769 135.269 89.365  1.00 60.62 ? 42  ASN A OD1   1 
ATOM   318   N  ND2   . ASN A 1 42  ? 105.602 134.187 87.785  1.00 57.10 ? 42  ASN A ND2   1 
ATOM   319   N  N     . GLN A 1 43  ? 103.139 134.044 92.752  1.00 62.73 ? 43  GLN A N     1 
ATOM   320   C  CA    . GLN A 1 43  ? 101.965 134.034 93.617  1.00 61.00 ? 43  GLN A CA    1 
ATOM   321   C  C     . GLN A 1 43  ? 102.226 134.791 94.915  1.00 58.96 ? 43  GLN A C     1 
ATOM   322   O  O     . GLN A 1 43  ? 101.367 135.546 95.382  1.00 62.57 ? 43  GLN A O     1 
ATOM   323   C  CB    . GLN A 1 43  ? 101.544 132.594 93.910  1.00 60.19 ? 43  GLN A CB    1 
ATOM   324   C  CG    . GLN A 1 43  ? 101.703 131.637 92.735  1.00 61.00 ? 43  GLN A CG    1 
ATOM   325   C  CD    . GLN A 1 43  ? 100.672 131.858 91.643  1.00 63.44 ? 43  GLN A CD    1 
ATOM   326   O  OE1   . GLN A 1 43  ? 100.676 132.885 90.963  1.00 61.83 ? 43  GLN A OE1   1 
ATOM   327   N  NE2   . GLN A 1 43  ? 99.781  130.889 91.469  1.00 62.11 ? 43  GLN A NE2   1 
ATOM   328   N  N     . ASN A 1 44  ? 103.404 134.606 95.507  1.00 54.20 ? 44  ASN A N     1 
ATOM   329   C  CA    . ASN A 1 44  ? 103.738 135.214 96.787  1.00 55.96 ? 44  ASN A CA    1 
ATOM   330   C  C     . ASN A 1 44  ? 104.383 136.587 96.652  1.00 56.20 ? 44  ASN A C     1 
ATOM   331   O  O     . ASN A 1 44  ? 104.753 137.183 97.668  1.00 56.48 ? 44  ASN A O     1 
ATOM   332   C  CB    . ASN A 1 44  ? 104.665 134.288 97.581  1.00 56.20 ? 44  ASN A CB    1 
ATOM   333   C  CG    . ASN A 1 44  ? 103.928 133.115 98.200  1.00 59.17 ? 44  ASN A CG    1 
ATOM   334   O  OD1   . ASN A 1 44  ? 103.530 133.162 99.363  1.00 60.39 ? 44  ASN A OD1   1 
ATOM   335   N  ND2   . ASN A 1 44  ? 103.740 132.057 97.420  1.00 57.82 ? 44  ASN A ND2   1 
ATOM   336   N  N     . THR A 1 45  ? 104.525 137.104 95.435  1.00 58.28 ? 45  THR A N     1 
ATOM   337   C  CA    . THR A 1 45  ? 105.134 138.408 95.217  1.00 58.44 ? 45  THR A CA    1 
ATOM   338   C  C     . THR A 1 45  ? 104.079 139.502 95.313  1.00 58.87 ? 45  THR A C     1 
ATOM   339   O  O     . THR A 1 45  ? 103.042 139.434 94.645  1.00 59.44 ? 45  THR A O     1 
ATOM   340   C  CB    . THR A 1 45  ? 105.818 138.468 93.851  1.00 57.25 ? 45  THR A CB    1 
ATOM   341   O  OG1   . THR A 1 45  ? 106.868 137.494 93.798  1.00 59.62 ? 45  THR A OG1   1 
ATOM   342   C  CG2   . THR A 1 45  ? 106.401 139.850 93.607  1.00 55.08 ? 45  THR A CG2   1 
ATOM   343   N  N     . VAL A 1 46  ? 104.346 140.505 96.146  1.00 59.46 ? 46  VAL A N     1 
ATOM   344   C  CA    . VAL A 1 46  ? 103.484 141.679 96.209  1.00 59.72 ? 46  VAL A CA    1 
ATOM   345   C  C     . VAL A 1 46  ? 103.740 142.530 94.973  1.00 59.65 ? 46  VAL A C     1 
ATOM   346   O  O     . VAL A 1 46  ? 104.876 142.943 94.711  1.00 62.03 ? 46  VAL A O     1 
ATOM   347   C  CB    . VAL A 1 46  ? 103.735 142.476 97.495  1.00 58.80 ? 46  VAL A CB    1 
ATOM   348   C  CG1   . VAL A 1 46  ? 102.695 143.573 97.651  1.00 59.69 ? 46  VAL A CG1   1 
ATOM   349   C  CG2   . VAL A 1 46  ? 103.734 141.555 98.700  1.00 57.63 ? 46  VAL A CG2   1 
ATOM   350   N  N     . PHE A 1 47  ? 102.686 142.800 94.209  1.00 63.21 ? 47  PHE A N     1 
ATOM   351   C  CA    . PHE A 1 47  ? 102.785 143.585 92.986  1.00 65.54 ? 47  PHE A CA    1 
ATOM   352   C  C     . PHE A 1 47  ? 102.000 144.876 93.149  1.00 67.14 ? 47  PHE A C     1 
ATOM   353   O  O     . PHE A 1 47  ? 100.867 144.862 93.641  1.00 67.30 ? 47  PHE A O     1 
ATOM   354   C  CB    . PHE A 1 47  ? 102.278 142.802 91.774  1.00 66.78 ? 47  PHE A CB    1 
ATOM   355   C  CG    . PHE A 1 47  ? 102.429 143.541 90.475  1.00 67.44 ? 47  PHE A CG    1 
ATOM   356   C  CD1   . PHE A 1 47  ? 103.641 143.547 89.805  1.00 66.57 ? 47  PHE A CD1   1 
ATOM   357   C  CD2   . PHE A 1 47  ? 101.359 144.225 89.922  1.00 65.67 ? 47  PHE A CD2   1 
ATOM   358   C  CE1   . PHE A 1 47  ? 103.785 144.227 88.611  1.00 67.09 ? 47  PHE A CE1   1 
ATOM   359   C  CE2   . PHE A 1 47  ? 101.497 144.905 88.727  1.00 66.90 ? 47  PHE A CE2   1 
ATOM   360   C  CZ    . PHE A 1 47  ? 102.712 144.906 88.071  1.00 68.07 ? 47  PHE A CZ    1 
ATOM   361   N  N     . PHE A 1 48  ? 102.608 145.984 92.745  1.00 66.65 ? 48  PHE A N     1 
ATOM   362   C  CA    . PHE A 1 48  ? 102.027 147.309 92.882  1.00 64.30 ? 48  PHE A CA    1 
ATOM   363   C  C     . PHE A 1 48  ? 101.657 147.856 91.510  1.00 65.64 ? 48  PHE A C     1 
ATOM   364   O  O     . PHE A 1 48  ? 102.168 147.408 90.480  1.00 67.23 ? 48  PHE A O     1 
ATOM   365   C  CB    . PHE A 1 48  ? 102.999 148.258 93.592  1.00 63.09 ? 48  PHE A CB    1 
ATOM   366   C  CG    . PHE A 1 48  ? 103.429 147.778 94.951  1.00 63.05 ? 48  PHE A CG    1 
ATOM   367   C  CD1   . PHE A 1 48  ? 104.367 146.768 95.079  1.00 62.69 ? 48  PHE A CD1   1 
ATOM   368   C  CD2   . PHE A 1 48  ? 102.885 148.325 96.098  1.00 63.40 ? 48  PHE A CD2   1 
ATOM   369   C  CE1   . PHE A 1 48  ? 104.759 146.321 96.320  1.00 62.96 ? 48  PHE A CE1   1 
ATOM   370   C  CE2   . PHE A 1 48  ? 103.275 147.880 97.343  1.00 64.54 ? 48  PHE A CE2   1 
ATOM   371   C  CZ    . PHE A 1 48  ? 104.213 146.876 97.451  1.00 63.28 ? 48  PHE A CZ    1 
ATOM   372   N  N     . HIS A 1 49  ? 100.749 148.835 91.508  1.00 68.96 ? 49  HIS A N     1 
ATOM   373   C  CA    . HIS A 1 49  ? 100.298 149.420 90.249  1.00 70.43 ? 49  HIS A CA    1 
ATOM   374   C  C     . HIS A 1 49  ? 101.451 150.077 89.500  1.00 70.41 ? 49  HIS A C     1 
ATOM   375   O  O     . HIS A 1 49  ? 101.579 149.922 88.281  1.00 70.53 ? 49  HIS A O     1 
ATOM   376   C  CB    . HIS A 1 49  ? 99.176  150.426 90.507  1.00 70.21 ? 49  HIS A CB    1 
ATOM   377   C  CG    . HIS A 1 49  ? 98.004  149.849 91.238  1.00 71.96 ? 49  HIS A CG    1 
ATOM   378   N  ND1   . HIS A 1 49  ? 98.033  149.559 92.586  1.00 72.35 ? 49  HIS A ND1   1 
ATOM   379   C  CD2   . HIS A 1 49  ? 96.768  149.502 90.807  1.00 70.95 ? 49  HIS A CD2   1 
ATOM   380   C  CE1   . HIS A 1 49  ? 96.866  149.063 92.953  1.00 70.41 ? 49  HIS A CE1   1 
ATOM   381   N  NE2   . HIS A 1 49  ? 96.080  149.017 91.892  1.00 72.21 ? 49  HIS A NE2   1 
ATOM   382   N  N     . ASN A 1 50  ? 102.301 150.811 90.213  1.00 67.85 ? 50  ASN A N     1 
ATOM   383   C  CA    . ASN A 1 50  ? 103.483 151.420 89.624  1.00 66.90 ? 50  ASN A CA    1 
ATOM   384   C  C     . ASN A 1 50  ? 104.625 151.360 90.628  1.00 65.89 ? 50  ASN A C     1 
ATOM   385   O  O     . ASN A 1 50  ? 104.422 151.092 91.815  1.00 67.84 ? 50  ASN A O     1 
ATOM   386   C  CB    . ASN A 1 50  ? 103.221 152.868 89.182  1.00 65.99 ? 50  ASN A CB    1 
ATOM   387   C  CG    . ASN A 1 50  ? 102.640 153.723 90.289  1.00 66.71 ? 50  ASN A CG    1 
ATOM   388   O  OD1   . ASN A 1 50  ? 102.499 153.279 91.427  1.00 66.38 ? 50  ASN A OD1   1 
ATOM   389   N  ND2   . ASN A 1 50  ? 102.300 154.963 89.959  1.00 66.74 ? 50  ASN A ND2   1 
ATOM   390   N  N     . LEU A 1 51  ? 105.839 151.605 90.129  1.00 60.09 ? 51  LEU A N     1 
ATOM   391   C  CA    . LEU A 1 51  ? 107.015 151.569 90.993  1.00 60.33 ? 51  LEU A CA    1 
ATOM   392   C  C     . LEU A 1 51  ? 106.951 152.638 92.077  1.00 61.89 ? 51  LEU A C     1 
ATOM   393   O  O     . LEU A 1 51  ? 107.523 152.457 93.158  1.00 64.13 ? 51  LEU A O     1 
ATOM   394   C  CB    . LEU A 1 51  ? 108.283 151.734 90.154  1.00 60.88 ? 51  LEU A CB    1 
ATOM   395   C  CG    . LEU A 1 51  ? 109.617 151.749 90.904  1.00 58.70 ? 51  LEU A CG    1 
ATOM   396   C  CD1   . LEU A 1 51  ? 109.864 150.413 91.582  1.00 57.68 ? 51  LEU A CD1   1 
ATOM   397   C  CD2   . LEU A 1 51  ? 110.759 152.106 89.970  1.00 58.29 ? 51  LEU A CD2   1 
ATOM   398   N  N     . LYS A 1 52  ? 106.270 153.755 91.809  1.00 62.70 ? 52  LYS A N     1 
ATOM   399   C  CA    . LYS A 1 52  ? 106.156 154.810 92.811  1.00 60.57 ? 52  LYS A CA    1 
ATOM   400   C  C     . LYS A 1 52  ? 105.416 154.320 94.048  1.00 61.94 ? 52  LYS A C     1 
ATOM   401   O  O     . LYS A 1 52  ? 105.842 154.582 95.179  1.00 61.50 ? 52  LYS A O     1 
ATOM   402   C  CB    . LYS A 1 52  ? 105.454 156.028 92.212  1.00 59.08 ? 52  LYS A CB    1 
ATOM   403   C  CG    . LYS A 1 52  ? 105.750 157.333 92.932  1.00 61.63 ? 52  LYS A CG    1 
ATOM   404   C  CD    . LYS A 1 52  ? 105.654 158.517 91.985  1.00 64.12 ? 52  LYS A CD    1 
ATOM   405   C  CE    . LYS A 1 52  ? 106.556 159.660 92.428  1.00 62.86 ? 52  LYS A CE    1 
ATOM   406   N  NZ    . LYS A 1 52  ? 106.795 159.646 93.897  1.00 61.59 ? 52  LYS A NZ    1 
ATOM   407   N  N     . GLU A 1 53  ? 104.308 153.602 93.850  1.00 65.09 ? 53  GLU A N     1 
ATOM   408   C  CA    . GLU A 1 53  ? 103.571 153.052 94.982  1.00 65.51 ? 53  GLU A CA    1 
ATOM   409   C  C     . GLU A 1 53  ? 104.421 152.048 95.747  1.00 64.44 ? 53  GLU A C     1 
ATOM   410   O  O     . GLU A 1 53  ? 104.403 152.022 96.982  1.00 65.65 ? 53  GLU A O     1 
ATOM   411   C  CB    . GLU A 1 53  ? 102.272 152.408 94.497  1.00 65.49 ? 53  GLU A CB    1 
ATOM   412   C  CG    . GLU A 1 53  ? 101.552 151.564 95.538  1.00 67.01 ? 53  GLU A CG    1 
ATOM   413   C  CD    . GLU A 1 53  ? 100.300 150.906 94.988  1.00 68.91 ? 53  GLU A CD    1 
ATOM   414   O  OE1   . GLU A 1 53  ? 99.854  151.301 93.890  1.00 68.94 ? 53  GLU A OE1   1 
ATOM   415   O  OE2   . GLU A 1 53  ? 99.762  149.995 95.652  1.00 68.52 ? 53  GLU A OE2   1 
ATOM   416   N  N     . LYS A 1 54  ? 105.184 151.222 95.029  1.00 60.07 ? 54  LYS A N     1 
ATOM   417   C  CA    . LYS A 1 54  ? 106.049 150.244 95.680  1.00 61.63 ? 54  LYS A CA    1 
ATOM   418   C  C     . LYS A 1 54  ? 107.099 150.925 96.548  1.00 57.98 ? 54  LYS A C     1 
ATOM   419   O  O     . LYS A 1 54  ? 107.307 150.547 97.707  1.00 60.62 ? 54  LYS A O     1 
ATOM   420   C  CB    . LYS A 1 54  ? 106.716 149.362 94.625  1.00 61.37 ? 54  LYS A CB    1 
ATOM   421   C  CG    . LYS A 1 54  ? 107.792 148.447 95.172  1.00 59.32 ? 54  LYS A CG    1 
ATOM   422   C  CD    . LYS A 1 54  ? 108.107 147.329 94.200  1.00 59.56 ? 54  LYS A CD    1 
ATOM   423   C  CE    . LYS A 1 54  ? 109.017 146.294 94.833  1.00 60.49 ? 54  LYS A CE    1 
ATOM   424   N  NZ    . LYS A 1 54  ? 108.947 144.988 94.125  1.00 61.33 ? 54  LYS A NZ    1 
ATOM   425   N  N     . LEU A 1 55  ? 107.771 151.939 95.999  1.00 56.77 ? 55  LEU A N     1 
ATOM   426   C  CA    . LEU A 1 55  ? 108.810 152.628 96.755  1.00 58.29 ? 55  LEU A CA    1 
ATOM   427   C  C     . LEU A 1 55  ? 108.226 153.376 97.945  1.00 61.71 ? 55  LEU A C     1 
ATOM   428   O  O     . LEU A 1 55  ? 108.816 153.377 99.031  1.00 63.47 ? 55  LEU A O     1 
ATOM   429   C  CB    . LEU A 1 55  ? 109.582 153.578 95.843  1.00 59.56 ? 55  LEU A CB    1 
ATOM   430   C  CG    . LEU A 1 55  ? 110.452 152.891 94.789  1.00 59.91 ? 55  LEU A CG    1 
ATOM   431   C  CD1   . LEU A 1 55  ? 111.101 153.918 93.884  1.00 60.09 ? 55  LEU A CD1   1 
ATOM   432   C  CD2   . LEU A 1 55  ? 111.500 152.009 95.448  1.00 59.59 ? 55  LEU A CD2   1 
ATOM   433   N  N     . ASP A 1 56  ? 107.067 154.017 97.764  1.00 65.85 ? 56  ASP A N     1 
ATOM   434   C  CA    . ASP A 1 56  ? 106.426 154.702 98.880  1.00 64.57 ? 56  ASP A CA    1 
ATOM   435   C  C     . ASP A 1 56  ? 106.033 153.719 99.975  1.00 63.80 ? 56  ASP A C     1 
ATOM   436   O  O     . ASP A 1 56  ? 106.231 153.992 101.165 1.00 64.88 ? 56  ASP A O     1 
ATOM   437   C  CB    . ASP A 1 56  ? 105.206 155.478 98.386  1.00 65.27 ? 56  ASP A CB    1 
ATOM   438   C  CG    . ASP A 1 56  ? 105.584 156.705 97.581  1.00 68.32 ? 56  ASP A CG    1 
ATOM   439   O  OD1   . ASP A 1 56  ? 106.718 157.202 97.747  1.00 67.27 ? 56  ASP A OD1   1 
ATOM   440   O  OD2   . ASP A 1 56  ? 104.745 157.176 96.784  1.00 67.74 ? 56  ASP A OD2   1 
ATOM   441   N  N     . TYR A 1 57  ? 105.489 152.562 99.591  1.00 58.74 ? 57  TYR A N     1 
ATOM   442   C  CA    . TYR A 1 57  ? 105.120 151.543 100.566 1.00 61.82 ? 57  TYR A CA    1 
ATOM   443   C  C     . TYR A 1 57  ? 106.337 151.037 101.325 1.00 61.65 ? 57  TYR A C     1 
ATOM   444   O  O     . TYR A 1 57  ? 106.274 150.818 102.541 1.00 63.32 ? 57  TYR A O     1 
ATOM   445   C  CB    . TYR A 1 57  ? 104.426 150.381 99.859  1.00 60.99 ? 57  TYR A CB    1 
ATOM   446   C  CG    . TYR A 1 57  ? 104.158 149.190 100.746 1.00 61.87 ? 57  TYR A CG    1 
ATOM   447   C  CD1   . TYR A 1 57  ? 103.371 149.303 101.880 1.00 61.79 ? 57  TYR A CD1   1 
ATOM   448   C  CD2   . TYR A 1 57  ? 104.729 147.960 100.470 1.00 62.72 ? 57  TYR A CD2   1 
ATOM   449   C  CE1   . TYR A 1 57  ? 103.129 148.209 102.687 1.00 62.57 ? 57  TYR A CE1   1 
ATOM   450   C  CE2   . TYR A 1 57  ? 104.499 146.868 101.276 1.00 63.73 ? 57  TYR A CE2   1 
ATOM   451   C  CZ    . TYR A 1 57  ? 103.701 146.997 102.385 1.00 62.88 ? 57  TYR A CZ    1 
ATOM   452   O  OH    . TYR A 1 57  ? 103.470 145.910 103.196 1.00 61.20 ? 57  TYR A OH    1 
ATOM   453   N  N     . LEU A 1 58  ? 107.453 150.829 100.624 1.00 55.74 ? 58  LEU A N     1 
ATOM   454   C  CA    . LEU A 1 58  ? 108.638 150.290 101.283 1.00 54.34 ? 58  LEU A CA    1 
ATOM   455   C  C     . LEU A 1 58  ? 109.290 151.323 102.194 1.00 54.82 ? 58  LEU A C     1 
ATOM   456   O  O     . LEU A 1 58  ? 109.787 150.978 103.272 1.00 57.24 ? 58  LEU A O     1 
ATOM   457   C  CB    . LEU A 1 58  ? 109.629 149.778 100.240 1.00 55.65 ? 58  LEU A CB    1 
ATOM   458   C  CG    . LEU A 1 58  ? 109.148 148.555 99.458  1.00 55.74 ? 58  LEU A CG    1 
ATOM   459   C  CD1   . LEU A 1 58  ? 109.925 148.405 98.167  1.00 54.92 ? 58  LEU A CD1   1 
ATOM   460   C  CD2   . LEU A 1 58  ? 109.265 147.301 100.304 1.00 55.96 ? 58  LEU A CD2   1 
ATOM   461   N  N     . VAL A 1 59  ? 109.299 152.592 101.785 1.00 60.17 ? 59  VAL A N     1 
ATOM   462   C  CA    . VAL A 1 59  ? 109.892 153.630 102.623 1.00 62.32 ? 59  VAL A CA    1 
ATOM   463   C  C     . VAL A 1 59  ? 109.028 153.883 103.854 1.00 64.21 ? 59  VAL A C     1 
ATOM   464   O  O     . VAL A 1 59  ? 109.535 153.986 104.977 1.00 63.48 ? 59  VAL A O     1 
ATOM   465   C  CB    . VAL A 1 59  ? 110.111 154.919 101.810 1.00 62.94 ? 59  VAL A CB    1 
ATOM   466   C  CG1   . VAL A 1 59  ? 110.531 156.057 102.722 1.00 60.50 ? 59  VAL A CG1   1 
ATOM   467   C  CG2   . VAL A 1 59  ? 111.163 154.693 100.733 1.00 62.37 ? 59  VAL A CG2   1 
ATOM   468   N  N     . GLU A 1 60  ? 107.708 153.976 103.663 1.00 65.05 ? 60  GLU A N     1 
ATOM   469   C  CA    . GLU A 1 60  ? 106.819 154.345 104.762 1.00 64.30 ? 60  GLU A CA    1 
ATOM   470   C  C     . GLU A 1 60  ? 106.795 153.285 105.857 1.00 65.31 ? 60  GLU A C     1 
ATOM   471   O  O     . GLU A 1 60  ? 106.767 153.619 107.047 1.00 67.81 ? 60  GLU A O     1 
ATOM   472   C  CB    . GLU A 1 60  ? 105.410 154.603 104.230 1.00 64.18 ? 60  GLU A CB    1 
ATOM   473   C  CG    . GLU A 1 60  ? 105.274 155.901 103.447 1.00 65.63 ? 60  GLU A CG    1 
ATOM   474   C  CD    . GLU A 1 60  ? 104.084 155.897 102.504 1.00 69.09 ? 60  GLU A CD    1 
ATOM   475   O  OE1   . GLU A 1 60  ? 103.246 154.976 102.603 1.00 68.44 ? 60  GLU A OE1   1 
ATOM   476   O  OE2   . GLU A 1 60  ? 103.981 156.821 101.670 1.00 67.26 ? 60  GLU A OE2   1 
ATOM   477   N  N     . ASN A 1 61  ? 106.800 152.007 105.484 1.00 60.27 ? 61  ASN A N     1 
ATOM   478   C  CA    . ASN A 1 61  ? 106.730 150.936 106.469 1.00 61.25 ? 61  ASN A CA    1 
ATOM   479   C  C     . ASN A 1 61  ? 108.093 150.419 106.895 1.00 61.97 ? 61  ASN A C     1 
ATOM   480   O  O     . ASN A 1 61  ? 108.212 149.231 107.223 1.00 65.50 ? 61  ASN A O     1 
ATOM   481   C  CB    . ASN A 1 61  ? 105.867 149.786 105.951 1.00 62.04 ? 61  ASN A CB    1 
ATOM   482   C  CG    . ASN A 1 61  ? 104.486 150.241 105.542 1.00 63.78 ? 61  ASN A CG    1 
ATOM   483   O  OD1   . ASN A 1 61  ? 104.230 151.436 105.402 1.00 64.86 ? 61  ASN A OD1   1 
ATOM   484   N  ND2   . ASN A 1 61  ? 103.573 149.296 105.406 1.00 62.87 ? 61  ASN A ND2   1 
ATOM   485   N  N     . GLN A 1 62  ? 109.115 151.276 106.881 1.00 57.47 ? 62  GLN A N     1 
ATOM   486   C  CA    . GLN A 1 62  ? 110.408 150.983 107.496 1.00 58.50 ? 62  GLN A CA    1 
ATOM   487   C  C     . GLN A 1 62  ? 111.114 149.805 106.829 1.00 58.22 ? 62  GLN A C     1 
ATOM   488   O  O     . GLN A 1 62  ? 111.854 149.066 107.480 1.00 58.58 ? 62  GLN A O     1 
ATOM   489   C  CB    . GLN A 1 62  ? 110.254 150.724 108.998 1.00 58.34 ? 62  GLN A CB    1 
ATOM   490   C  CG    . GLN A 1 62  ? 109.579 151.848 109.777 1.00 57.52 ? 62  GLN A CG    1 
ATOM   491   C  CD    . GLN A 1 62  ? 110.208 153.205 109.531 1.00 60.36 ? 62  GLN A CD    1 
ATOM   492   O  OE1   . GLN A 1 62  ? 111.192 153.566 110.174 1.00 59.79 ? 62  GLN A OE1   1 
ATOM   493   N  NE2   . GLN A 1 62  ? 109.632 153.971 108.612 1.00 58.72 ? 62  GLN A NE2   1 
ATOM   494   N  N     . TYR A 1 63  ? 110.891 149.615 105.530 1.00 55.43 ? 63  TYR A N     1 
ATOM   495   C  CA    . TYR A 1 63  ? 111.614 148.583 104.799 1.00 53.39 ? 63  TYR A CA    1 
ATOM   496   C  C     . TYR A 1 63  ? 112.880 149.127 104.152 1.00 54.14 ? 63  TYR A C     1 
ATOM   497   O  O     . TYR A 1 63  ? 113.910 148.446 104.135 1.00 53.42 ? 63  TYR A O     1 
ATOM   498   C  CB    . TYR A 1 63  ? 110.714 147.952 103.733 1.00 52.62 ? 63  TYR A CB    1 
ATOM   499   C  CG    . TYR A 1 63  ? 109.658 147.030 104.296 1.00 53.80 ? 63  TYR A CG    1 
ATOM   500   C  CD1   . TYR A 1 63  ? 110.001 145.996 105.154 1.00 52.80 ? 63  TYR A CD1   1 
ATOM   501   C  CD2   . TYR A 1 63  ? 108.321 147.187 103.960 1.00 55.54 ? 63  TYR A CD2   1 
ATOM   502   C  CE1   . TYR A 1 63  ? 109.042 145.150 105.671 1.00 54.37 ? 63  TYR A CE1   1 
ATOM   503   C  CE2   . TYR A 1 63  ? 107.354 146.344 104.471 1.00 55.65 ? 63  TYR A CE2   1 
ATOM   504   C  CZ    . TYR A 1 63  ? 107.721 145.328 105.326 1.00 56.72 ? 63  TYR A CZ    1 
ATOM   505   O  OH    . TYR A 1 63  ? 106.763 144.485 105.838 1.00 55.44 ? 63  TYR A OH    1 
ATOM   506   N  N     . TYR A 1 64  ? 112.823 150.346 103.628 1.00 50.55 ? 64  TYR A N     1 
ATOM   507   C  CA    . TYR A 1 64  ? 113.954 150.986 102.979 1.00 48.55 ? 64  TYR A CA    1 
ATOM   508   C  C     . TYR A 1 64  ? 114.413 152.189 103.790 1.00 51.24 ? 64  TYR A C     1 
ATOM   509   O  O     . TYR A 1 64  ? 113.806 152.566 104.794 1.00 54.25 ? 64  TYR A O     1 
ATOM   510   C  CB    . TYR A 1 64  ? 113.589 151.422 101.556 1.00 48.13 ? 64  TYR A CB    1 
ATOM   511   C  CG    . TYR A 1 64  ? 113.613 150.302 100.545 1.00 49.96 ? 64  TYR A CG    1 
ATOM   512   C  CD1   . TYR A 1 64  ? 114.037 149.029 100.898 1.00 48.70 ? 64  TYR A CD1   1 
ATOM   513   C  CD2   . TYR A 1 64  ? 113.209 150.519 99.237  1.00 50.31 ? 64  TYR A CD2   1 
ATOM   514   C  CE1   . TYR A 1 64  ? 114.056 148.004 99.977  1.00 45.61 ? 64  TYR A CE1   1 
ATOM   515   C  CE2   . TYR A 1 64  ? 113.228 149.504 98.310  1.00 48.57 ? 64  TYR A CE2   1 
ATOM   516   C  CZ    . TYR A 1 64  ? 113.651 148.248 98.684  1.00 48.01 ? 64  TYR A CZ    1 
ATOM   517   O  OH    . TYR A 1 64  ? 113.666 147.236 97.756  1.00 51.50 ? 64  TYR A OH    1 
ATOM   518   N  N     . GLU A 1 65  ? 115.506 152.792 103.336 1.00 54.41 ? 65  GLU A N     1 
ATOM   519   C  CA    . GLU A 1 65  ? 116.009 154.033 103.905 1.00 52.77 ? 65  GLU A CA    1 
ATOM   520   C  C     . GLU A 1 65  ? 115.662 155.183 102.970 1.00 55.50 ? 65  GLU A C     1 
ATOM   521   O  O     . GLU A 1 65  ? 115.887 155.096 101.759 1.00 58.19 ? 65  GLU A O     1 
ATOM   522   C  CB    . GLU A 1 65  ? 117.520 153.966 104.129 1.00 53.38 ? 65  GLU A CB    1 
ATOM   523   C  CG    . GLU A 1 65  ? 117.978 152.743 104.901 1.00 51.75 ? 65  GLU A CG    1 
ATOM   524   C  CD    . GLU A 1 65  ? 119.487 152.652 105.000 1.00 55.94 ? 65  GLU A CD    1 
ATOM   525   O  OE1   . GLU A 1 65  ? 120.173 153.031 104.028 1.00 57.88 ? 65  GLU A OE1   1 
ATOM   526   O  OE2   . GLU A 1 65  ? 119.988 152.203 106.053 1.00 54.94 ? 65  GLU A OE2   1 
ATOM   527   N  N     . GLU A 1 66  ? 115.105 156.254 103.534 1.00 57.66 ? 66  GLU A N     1 
ATOM   528   C  CA    . GLU A 1 66  ? 114.710 157.400 102.726 1.00 56.43 ? 66  GLU A CA    1 
ATOM   529   C  C     . GLU A 1 66  ? 115.905 158.221 102.261 1.00 56.98 ? 66  GLU A C     1 
ATOM   530   O  O     . GLU A 1 66  ? 115.838 158.840 101.194 1.00 57.73 ? 66  GLU A O     1 
ATOM   531   C  CB    . GLU A 1 66  ? 113.737 158.278 103.518 1.00 57.39 ? 66  GLU A CB    1 
ATOM   532   C  CG    . GLU A 1 66  ? 113.322 159.577 102.837 1.00 59.16 ? 66  GLU A CG    1 
ATOM   533   C  CD    . GLU A 1 66  ? 112.407 159.356 101.645 1.00 60.72 ? 66  GLU A CD    1 
ATOM   534   O  OE1   . GLU A 1 66  ? 111.224 159.749 101.726 1.00 58.44 ? 66  GLU A OE1   1 
ATOM   535   O  OE2   . GLU A 1 66  ? 112.870 158.808 100.622 1.00 62.10 ? 66  GLU A OE2   1 
ATOM   536   N  N     . GLU A 1 67  ? 116.999 158.225 103.026 1.00 58.43 ? 67  GLU A N     1 
ATOM   537   C  CA    . GLU A 1 67  ? 118.114 159.122 102.736 1.00 56.39 ? 67  GLU A CA    1 
ATOM   538   C  C     . GLU A 1 67  ? 118.761 158.803 101.392 1.00 57.62 ? 67  GLU A C     1 
ATOM   539   O  O     . GLU A 1 67  ? 119.034 159.709 100.597 1.00 58.26 ? 67  GLU A O     1 
ATOM   540   C  CB    . GLU A 1 67  ? 119.146 159.054 103.861 1.00 57.09 ? 67  GLU A CB    1 
ATOM   541   C  CG    . GLU A 1 67  ? 119.234 157.701 104.547 1.00 58.85 ? 67  GLU A CG    1 
ATOM   542   C  CD    . GLU A 1 67  ? 118.371 157.622 105.791 1.00 59.26 ? 67  GLU A CD    1 
ATOM   543   O  OE1   . GLU A 1 67  ? 117.130 157.649 105.660 1.00 57.56 ? 67  GLU A OE1   1 
ATOM   544   O  OE2   . GLU A 1 67  ? 118.936 157.536 106.902 1.00 62.05 ? 67  GLU A OE2   1 
ATOM   545   N  N     . PHE A 1 68  ? 119.016 157.523 101.117 1.00 54.36 ? 68  PHE A N     1 
ATOM   546   C  CA    . PHE A 1 68  ? 119.701 157.175 99.877  1.00 51.67 ? 68  PHE A CA    1 
ATOM   547   C  C     . PHE A 1 68  ? 118.774 157.253 98.671  1.00 51.43 ? 68  PHE A C     1 
ATOM   548   O  O     . PHE A 1 68  ? 119.232 157.558 97.564  1.00 54.53 ? 68  PHE A O     1 
ATOM   549   C  CB    . PHE A 1 68  ? 120.336 155.785 99.990  1.00 51.34 ? 68  PHE A CB    1 
ATOM   550   C  CG    . PHE A 1 68  ? 119.440 154.657 99.562  1.00 51.07 ? 68  PHE A CG    1 
ATOM   551   C  CD1   . PHE A 1 68  ? 118.516 154.119 100.438 1.00 51.31 ? 68  PHE A CD1   1 
ATOM   552   C  CD2   . PHE A 1 68  ? 119.545 154.114 98.292  1.00 47.64 ? 68  PHE A CD2   1 
ATOM   553   C  CE1   . PHE A 1 68  ? 117.697 153.078 100.048 1.00 48.53 ? 68  PHE A CE1   1 
ATOM   554   C  CE2   . PHE A 1 68  ? 118.731 153.073 97.899  1.00 46.97 ? 68  PHE A CE2   1 
ATOM   555   C  CZ    . PHE A 1 68  ? 117.808 152.552 98.779  1.00 47.65 ? 68  PHE A CZ    1 
ATOM   556   N  N     . LEU A 1 69  ? 117.479 156.989 98.858  1.00 50.50 ? 69  LEU A N     1 
ATOM   557   C  CA    . LEU A 1 69  ? 116.532 157.121 97.759  1.00 53.12 ? 69  LEU A CA    1 
ATOM   558   C  C     . LEU A 1 69  ? 116.196 158.574 97.456  1.00 53.99 ? 69  LEU A C     1 
ATOM   559   O  O     . LEU A 1 69  ? 115.670 158.862 96.376  1.00 54.01 ? 69  LEU A O     1 
ATOM   560   C  CB    . LEU A 1 69  ? 115.250 156.348 98.071  1.00 54.21 ? 69  LEU A CB    1 
ATOM   561   C  CG    . LEU A 1 69  ? 115.304 154.834 97.864  1.00 52.34 ? 69  LEU A CG    1 
ATOM   562   C  CD1   . LEU A 1 69  ? 114.073 154.166 98.450  1.00 51.79 ? 69  LEU A CD1   1 
ATOM   563   C  CD2   . LEU A 1 69  ? 115.449 154.501 96.389  1.00 49.96 ? 69  LEU A CD2   1 
ATOM   564   N  N     . SER A 1 70  ? 116.488 159.492 98.378  1.00 56.43 ? 70  SER A N     1 
ATOM   565   C  CA    . SER A 1 70  ? 116.183 160.902 98.179  1.00 54.27 ? 70  SER A CA    1 
ATOM   566   C  C     . SER A 1 70  ? 117.206 161.619 97.310  1.00 53.76 ? 70  SER A C     1 
ATOM   567   O  O     . SER A 1 70  ? 116.957 162.760 96.907  1.00 57.00 ? 70  SER A O     1 
ATOM   568   C  CB    . SER A 1 70  ? 116.076 161.611 99.531  1.00 54.87 ? 70  SER A CB    1 
ATOM   569   O  OG    . SER A 1 70  ? 117.347 161.730 100.145 1.00 54.49 ? 70  SER A OG    1 
ATOM   570   N  N     . LEU A 1 71  ? 118.341 160.987 97.013  1.00 50.47 ? 71  LEU A N     1 
ATOM   571   C  CA    . LEU A 1 71  ? 119.350 161.602 96.160  1.00 49.91 ? 71  LEU A CA    1 
ATOM   572   C  C     . LEU A 1 71  ? 119.025 161.482 94.679  1.00 50.92 ? 71  LEU A C     1 
ATOM   573   O  O     . LEU A 1 71  ? 119.731 162.077 93.858  1.00 49.94 ? 71  LEU A O     1 
ATOM   574   C  CB    . LEU A 1 71  ? 120.722 160.984 96.436  1.00 48.13 ? 71  LEU A CB    1 
ATOM   575   C  CG    . LEU A 1 71  ? 121.045 160.685 97.900  1.00 50.11 ? 71  LEU A CG    1 
ATOM   576   C  CD1   . LEU A 1 71  ? 122.040 159.544 98.005  1.00 51.35 ? 71  LEU A CD1   1 
ATOM   577   C  CD2   . LEU A 1 71  ? 121.578 161.929 98.589  1.00 51.68 ? 71  LEU A CD2   1 
ATOM   578   N  N     . TYR A 1 72  ? 117.986 160.734 94.320  1.00 48.41 ? 72  TYR A N     1 
ATOM   579   C  CA    . TYR A 1 72  ? 117.566 160.575 92.937  1.00 50.05 ? 72  TYR A CA    1 
ATOM   580   C  C     . TYR A 1 72  ? 116.135 161.061 92.775  1.00 52.52 ? 72  TYR A C     1 
ATOM   581   O  O     . TYR A 1 72  ? 115.280 160.797 93.627  1.00 52.52 ? 72  TYR A O     1 
ATOM   582   C  CB    . TYR A 1 72  ? 117.641 159.112 92.482  1.00 47.76 ? 72  TYR A CB    1 
ATOM   583   C  CG    . TYR A 1 72  ? 118.918 158.387 92.827  1.00 48.25 ? 72  TYR A CG    1 
ATOM   584   C  CD1   . TYR A 1 72  ? 119.082 157.780 94.065  1.00 46.68 ? 72  TYR A CD1   1 
ATOM   585   C  CD2   . TYR A 1 72  ? 119.949 158.282 91.905  1.00 46.38 ? 72  TYR A CD2   1 
ATOM   586   C  CE1   . TYR A 1 72  ? 120.241 157.109 94.381  1.00 44.17 ? 72  TYR A CE1   1 
ATOM   587   C  CE2   . TYR A 1 72  ? 121.111 157.610 92.211  1.00 42.29 ? 72  TYR A CE2   1 
ATOM   588   C  CZ    . TYR A 1 72  ? 121.253 157.026 93.450  1.00 44.23 ? 72  TYR A CZ    1 
ATOM   589   O  OH    . TYR A 1 72  ? 122.410 156.356 93.761  1.00 49.49 ? 72  TYR A OH    1 
ATOM   590   N  N     . SER A 1 73  ? 115.877 161.771 91.681  1.00 54.46 ? 73  SER A N     1 
ATOM   591   C  CA    . SER A 1 73  ? 114.503 162.004 91.269  1.00 55.64 ? 73  SER A CA    1 
ATOM   592   C  C     . SER A 1 73  ? 113.877 160.683 90.842  1.00 56.94 ? 73  SER A C     1 
ATOM   593   O  O     . SER A 1 73  ? 114.564 159.775 90.366  1.00 58.10 ? 73  SER A O     1 
ATOM   594   C  CB    . SER A 1 73  ? 114.445 163.016 90.126  1.00 56.58 ? 73  SER A CB    1 
ATOM   595   O  OG    . SER A 1 73  ? 114.652 162.385 88.875  1.00 56.17 ? 73  SER A OG    1 
ATOM   596   N  N     . PHE A 1 74  ? 112.559 160.569 91.027  1.00 57.55 ? 74  PHE A N     1 
ATOM   597   C  CA    . PHE A 1 74  ? 111.903 159.298 90.745  1.00 55.56 ? 74  PHE A CA    1 
ATOM   598   C  C     . PHE A 1 74  ? 112.037 158.876 89.289  1.00 58.10 ? 74  PHE A C     1 
ATOM   599   O  O     . PHE A 1 74  ? 111.959 157.679 88.998  1.00 60.31 ? 74  PHE A O     1 
ATOM   600   C  CB    . PHE A 1 74  ? 110.424 159.340 91.127  1.00 58.31 ? 74  PHE A CB    1 
ATOM   601   C  CG    . PHE A 1 74  ? 109.711 158.047 90.862  1.00 58.44 ? 74  PHE A CG    1 
ATOM   602   C  CD1   . PHE A 1 74  ? 109.836 156.983 91.736  1.00 57.25 ? 74  PHE A CD1   1 
ATOM   603   C  CD2   . PHE A 1 74  ? 108.932 157.890 89.727  1.00 58.10 ? 74  PHE A CD2   1 
ATOM   604   C  CE1   . PHE A 1 74  ? 109.198 155.788 91.484  1.00 59.03 ? 74  PHE A CE1   1 
ATOM   605   C  CE2   . PHE A 1 74  ? 108.289 156.699 89.473  1.00 59.66 ? 74  PHE A CE2   1 
ATOM   606   C  CZ    . PHE A 1 74  ? 108.422 155.646 90.351  1.00 60.90 ? 74  PHE A CZ    1 
ATOM   607   N  N     . GLU A 1 75  ? 112.241 159.818 88.368  1.00 61.53 ? 75  GLU A N     1 
ATOM   608   C  CA    . GLU A 1 75  ? 112.503 159.431 86.986  1.00 60.87 ? 75  GLU A CA    1 
ATOM   609   C  C     . GLU A 1 75  ? 113.808 158.653 86.879  1.00 62.28 ? 75  GLU A C     1 
ATOM   610   O  O     . GLU A 1 75  ? 113.898 157.672 86.132  1.00 61.74 ? 75  GLU A O     1 
ATOM   611   C  CB    . GLU A 1 75  ? 112.528 160.667 86.088  1.00 60.69 ? 75  GLU A CB    1 
ATOM   612   C  CG    . GLU A 1 75  ? 111.155 161.275 85.854  1.00 62.71 ? 75  GLU A CG    1 
ATOM   613   C  CD    . GLU A 1 75  ? 110.128 160.246 85.419  1.00 65.02 ? 75  GLU A CD    1 
ATOM   614   O  OE1   . GLU A 1 75  ? 110.332 159.610 84.364  1.00 64.94 ? 75  GLU A OE1   1 
ATOM   615   O  OE2   . GLU A 1 75  ? 109.120 160.071 86.134  1.00 64.54 ? 75  GLU A OE2   1 
ATOM   616   N  N     . ASP A 1 76  ? 114.828 159.065 87.636  1.00 57.83 ? 76  ASP A N     1 
ATOM   617   C  CA    . ASP A 1 76  ? 116.098 158.346 87.631  1.00 55.48 ? 76  ASP A CA    1 
ATOM   618   C  C     . ASP A 1 76  ? 115.956 156.954 88.238  1.00 55.04 ? 76  ASP A C     1 
ATOM   619   O  O     . ASP A 1 76  ? 116.528 155.985 87.723  1.00 59.16 ? 76  ASP A O     1 
ATOM   620   C  CB    . ASP A 1 76  ? 117.151 159.155 88.383  1.00 56.81 ? 76  ASP A CB    1 
ATOM   621   C  CG    . ASP A 1 76  ? 117.373 160.524 87.774  1.00 59.57 ? 76  ASP A CG    1 
ATOM   622   O  OD1   . ASP A 1 76  ? 117.366 160.630 86.529  1.00 58.81 ? 76  ASP A OD1   1 
ATOM   623   O  OD2   . ASP A 1 76  ? 117.559 161.494 88.538  1.00 58.56 ? 76  ASP A OD2   1 
ATOM   624   N  N     . ILE A 1 77  ? 115.208 156.834 89.337  1.00 50.95 ? 77  ILE A N     1 
ATOM   625   C  CA    . ILE A 1 77  ? 114.980 155.525 89.943  1.00 51.10 ? 77  ILE A CA    1 
ATOM   626   C  C     . ILE A 1 77  ? 114.209 154.628 88.985  1.00 50.73 ? 77  ILE A C     1 
ATOM   627   O  O     . ILE A 1 77  ? 114.488 153.427 88.868  1.00 52.36 ? 77  ILE A O     1 
ATOM   628   C  CB    . ILE A 1 77  ? 114.245 155.678 91.287  1.00 52.10 ? 77  ILE A CB    1 
ATOM   629   C  CG1   . ILE A 1 77  ? 114.943 156.722 92.158  1.00 52.00 ? 77  ILE A CG1   1 
ATOM   630   C  CG2   . ILE A 1 77  ? 114.172 154.341 92.003  1.00 50.96 ? 77  ILE A CG2   1 
ATOM   631   C  CD1   . ILE A 1 77  ? 114.510 156.702 93.605  1.00 52.22 ? 77  ILE A CD1   1 
ATOM   632   N  N     . LYS A 1 78  ? 113.220 155.196 88.294  1.00 54.43 ? 78  LYS A N     1 
ATOM   633   C  CA    . LYS A 1 78  ? 112.476 154.441 87.295  1.00 54.78 ? 78  LYS A CA    1 
ATOM   634   C  C     . LYS A 1 78  ? 113.390 153.970 86.173  1.00 54.65 ? 78  LYS A C     1 
ATOM   635   O  O     . LYS A 1 78  ? 113.281 152.830 85.718  1.00 57.45 ? 78  LYS A O     1 
ATOM   636   C  CB    . LYS A 1 78  ? 111.338 155.296 86.741  1.00 57.68 ? 78  LYS A CB    1 
ATOM   637   C  CG    . LYS A 1 78  ? 110.096 154.517 86.350  1.00 56.30 ? 78  LYS A CG    1 
ATOM   638   C  CD    . LYS A 1 78  ? 109.086 155.423 85.666  1.00 56.53 ? 78  LYS A CD    1 
ATOM   639   C  CE    . LYS A 1 78  ? 108.293 154.672 84.613  1.00 58.01 ? 78  LYS A CE    1 
ATOM   640   N  NZ    . LYS A 1 78  ? 106.857 154.555 84.985  1.00 57.67 ? 78  LYS A NZ    1 
ATOM   641   N  N     . GLU A 1 79  ? 114.299 154.835 85.717  1.00 55.40 ? 79  GLU A N     1 
ATOM   642   C  CA    . GLU A 1 79  ? 115.250 154.439 84.682  1.00 55.05 ? 79  GLU A CA    1 
ATOM   643   C  C     . GLU A 1 79  ? 116.149 153.307 85.163  1.00 53.13 ? 79  GLU A C     1 
ATOM   644   O  O     . GLU A 1 79  ? 116.441 152.370 84.411  1.00 55.97 ? 79  GLU A O     1 
ATOM   645   C  CB    . GLU A 1 79  ? 116.093 155.641 84.257  1.00 55.66 ? 79  GLU A CB    1 
ATOM   646   C  CG    . GLU A 1 79  ? 115.367 156.637 83.373  1.00 56.47 ? 79  GLU A CG    1 
ATOM   647   C  CD    . GLU A 1 79  ? 116.246 157.809 82.983  1.00 59.82 ? 79  GLU A CD    1 
ATOM   648   O  OE1   . GLU A 1 79  ? 117.281 157.582 82.323  1.00 59.86 ? 79  GLU A OE1   1 
ATOM   649   O  OE2   . GLU A 1 79  ? 115.905 158.956 83.338  1.00 62.05 ? 79  GLU A OE2   1 
ATOM   650   N  N     . VAL A 1 80  ? 116.599 153.380 86.416  1.00 45.17 ? 80  VAL A N     1 
ATOM   651   C  CA    . VAL A 1 80  ? 117.431 152.318 86.977  1.00 43.31 ? 80  VAL A CA    1 
ATOM   652   C  C     . VAL A 1 80  ? 116.667 150.999 87.011  1.00 48.12 ? 80  VAL A C     1 
ATOM   653   O  O     . VAL A 1 80  ? 117.195 149.943 86.634  1.00 49.02 ? 80  VAL A O     1 
ATOM   654   C  CB    . VAL A 1 80  ? 117.930 152.725 88.376  1.00 43.83 ? 80  VAL A CB    1 
ATOM   655   C  CG1   . VAL A 1 80  ? 118.474 151.526 89.126  1.00 45.11 ? 80  VAL A CG1   1 
ATOM   656   C  CG2   . VAL A 1 80  ? 118.989 153.806 88.260  1.00 44.53 ? 80  VAL A CG2   1 
ATOM   657   N  N     . PHE A 1 81  ? 115.408 151.041 87.451  1.00 47.87 ? 81  PHE A N     1 
ATOM   658   C  CA    . PHE A 1 81  ? 114.609 149.821 87.518  1.00 44.55 ? 81  PHE A CA    1 
ATOM   659   C  C     . PHE A 1 81  ? 114.313 149.269 86.126  1.00 47.23 ? 81  PHE A C     1 
ATOM   660   O  O     . PHE A 1 81  ? 114.264 148.049 85.936  1.00 49.26 ? 81  PHE A O     1 
ATOM   661   C  CB    . PHE A 1 81  ? 113.316 150.083 88.287  1.00 45.28 ? 81  PHE A CB    1 
ATOM   662   C  CG    . PHE A 1 81  ? 113.431 149.830 89.763  1.00 44.67 ? 81  PHE A CG    1 
ATOM   663   C  CD1   . PHE A 1 81  ? 114.044 150.753 90.591  1.00 45.70 ? 81  PHE A CD1   1 
ATOM   664   C  CD2   . PHE A 1 81  ? 112.927 148.669 90.321  1.00 47.15 ? 81  PHE A CD2   1 
ATOM   665   C  CE1   . PHE A 1 81  ? 114.152 150.523 91.948  1.00 46.03 ? 81  PHE A CE1   1 
ATOM   666   C  CE2   . PHE A 1 81  ? 113.032 148.435 91.678  1.00 45.55 ? 81  PHE A CE2   1 
ATOM   667   C  CZ    . PHE A 1 81  ? 113.645 149.363 92.492  1.00 43.62 ? 81  PHE A CZ    1 
ATOM   668   N  N     . LYS A 1 82  ? 114.104 150.149 85.142  1.00 47.11 ? 82  LYS A N     1 
ATOM   669   C  CA    . LYS A 1 82  ? 113.965 149.689 83.763  1.00 50.31 ? 82  LYS A CA    1 
ATOM   670   C  C     . LYS A 1 82  ? 115.238 149.006 83.287  1.00 50.32 ? 82  LYS A C     1 
ATOM   671   O  O     . LYS A 1 82  ? 115.183 147.971 82.614  1.00 53.15 ? 82  LYS A O     1 
ATOM   672   C  CB    . LYS A 1 82  ? 113.618 150.852 82.831  1.00 51.84 ? 82  LYS A CB    1 
ATOM   673   C  CG    . LYS A 1 82  ? 112.337 151.598 83.156  1.00 53.66 ? 82  LYS A CG    1 
ATOM   674   C  CD    . LYS A 1 82  ? 111.134 150.680 83.146  1.00 53.83 ? 82  LYS A CD    1 
ATOM   675   C  CE    . LYS A 1 82  ? 110.063 151.195 82.200  1.00 54.49 ? 82  LYS A CE    1 
ATOM   676   N  NZ    . LYS A 1 82  ? 110.608 151.453 80.839  1.00 52.77 ? 82  LYS A NZ    1 
ATOM   677   N  N     . THR A 1 83  ? 116.396 149.575 83.627  1.00 43.31 ? 83  THR A N     1 
ATOM   678   C  CA    . THR A 1 83  ? 117.663 148.960 83.248  1.00 45.01 ? 83  THR A CA    1 
ATOM   679   C  C     . THR A 1 83  ? 117.802 147.574 83.863  1.00 46.39 ? 83  THR A C     1 
ATOM   680   O  O     . THR A 1 83  ? 118.286 146.641 83.211  1.00 47.33 ? 83  THR A O     1 
ATOM   681   C  CB    . THR A 1 83  ? 118.828 149.857 83.668  1.00 46.35 ? 83  THR A CB    1 
ATOM   682   O  OG1   . THR A 1 83  ? 118.634 151.172 83.136  1.00 50.07 ? 83  THR A OG1   1 
ATOM   683   C  CG2   . THR A 1 83  ? 120.143 149.304 83.149  1.00 45.94 ? 83  THR A CG2   1 
ATOM   684   N  N     . ALA A 1 84  ? 117.382 147.418 85.121  1.00 45.10 ? 84  ALA A N     1 
ATOM   685   C  CA    . ALA A 1 84  ? 117.431 146.102 85.752  1.00 40.77 ? 84  ALA A CA    1 
ATOM   686   C  C     . ALA A 1 84  ? 116.498 145.115 85.062  1.00 42.59 ? 84  ALA A C     1 
ATOM   687   O  O     . ALA A 1 84  ? 116.881 143.970 84.797  1.00 47.20 ? 84  ALA A O     1 
ATOM   688   C  CB    . ALA A 1 84  ? 117.085 146.216 87.234  1.00 43.04 ? 84  ALA A CB    1 
ATOM   689   N  N     . TYR A 1 85  ? 115.271 145.539 84.761  1.00 47.90 ? 85  TYR A N     1 
ATOM   690   C  CA    . TYR A 1 85  ? 114.291 144.641 84.164  1.00 47.31 ? 85  TYR A CA    1 
ATOM   691   C  C     . TYR A 1 85  ? 114.471 144.473 82.661  1.00 46.82 ? 85  TYR A C     1 
ATOM   692   O  O     . TYR A 1 85  ? 113.909 143.534 82.089  1.00 49.61 ? 85  TYR A O     1 
ATOM   693   C  CB    . TYR A 1 85  ? 112.874 145.136 84.461  1.00 47.52 ? 85  TYR A CB    1 
ATOM   694   C  CG    . TYR A 1 85  ? 112.386 144.790 85.850  1.00 48.44 ? 85  TYR A CG    1 
ATOM   695   C  CD1   . TYR A 1 85  ? 112.623 145.637 86.923  1.00 47.56 ? 85  TYR A CD1   1 
ATOM   696   C  CD2   . TYR A 1 85  ? 111.690 143.613 86.086  1.00 47.08 ? 85  TYR A CD2   1 
ATOM   697   C  CE1   . TYR A 1 85  ? 112.178 145.323 88.192  1.00 47.10 ? 85  TYR A CE1   1 
ATOM   698   C  CE2   . TYR A 1 85  ? 111.242 143.291 87.351  1.00 46.95 ? 85  TYR A CE2   1 
ATOM   699   C  CZ    . TYR A 1 85  ? 111.489 144.149 88.400  1.00 47.49 ? 85  TYR A CZ    1 
ATOM   700   O  OH    . TYR A 1 85  ? 111.044 143.831 89.660  1.00 49.22 ? 85  TYR A OH    1 
ATOM   701   N  N     . ALA A 1 86  ? 115.236 145.354 82.010  1.00 44.83 ? 86  ALA A N     1 
ATOM   702   C  CA    . ALA A 1 86  ? 115.469 145.207 80.577  1.00 44.55 ? 86  ALA A CA    1 
ATOM   703   C  C     . ALA A 1 86  ? 116.289 143.963 80.267  1.00 46.99 ? 86  ALA A C     1 
ATOM   704   O  O     . ALA A 1 86  ? 116.128 143.368 79.196  1.00 48.71 ? 86  ALA A O     1 
ATOM   705   C  CB    . ALA A 1 86  ? 116.166 146.447 80.022  1.00 44.52 ? 86  ALA A CB    1 
ATOM   706   N  N     . LYS A 1 87  ? 117.174 143.563 81.182  1.00 45.70 ? 87  LYS A N     1 
ATOM   707   C  CA    . LYS A 1 87  ? 117.980 142.368 80.965  1.00 45.53 ? 87  LYS A CA    1 
ATOM   708   C  C     . LYS A 1 87  ? 117.118 141.113 80.910  1.00 45.31 ? 87  LYS A C     1 
ATOM   709   O  O     . LYS A 1 87  ? 117.470 140.149 80.220  1.00 45.51 ? 87  LYS A O     1 
ATOM   710   C  CB    . LYS A 1 87  ? 119.040 142.255 82.064  1.00 42.99 ? 87  LYS A CB    1 
ATOM   711   C  CG    . LYS A 1 87  ? 119.611 140.861 82.274  1.00 43.76 ? 87  LYS A CG    1 
ATOM   712   C  CD    . LYS A 1 87  ? 120.979 140.713 81.631  1.00 45.31 ? 87  LYS A CD    1 
ATOM   713   C  CE    . LYS A 1 87  ? 121.582 139.353 81.936  1.00 44.81 ? 87  LYS A CE    1 
ATOM   714   N  NZ    . LYS A 1 87  ? 122.924 139.184 81.314  1.00 41.81 ? 87  LYS A NZ    1 
ATOM   715   N  N     . LYS A 1 88  ? 115.974 141.123 81.596  1.00 48.29 ? 88  LYS A N     1 
ATOM   716   C  CA    . LYS A 1 88  ? 115.109 139.950 81.716  1.00 47.53 ? 88  LYS A CA    1 
ATOM   717   C  C     . LYS A 1 88  ? 115.897 138.756 82.244  1.00 43.55 ? 88  LYS A C     1 
ATOM   718   O  O     . LYS A 1 88  ? 115.938 137.684 81.639  1.00 46.28 ? 88  LYS A O     1 
ATOM   719   C  CB    . LYS A 1 88  ? 114.431 139.621 80.385  1.00 49.90 ? 88  LYS A CB    1 
ATOM   720   C  CG    . LYS A 1 88  ? 113.136 140.379 80.139  1.00 49.58 ? 88  LYS A CG    1 
ATOM   721   C  CD    . LYS A 1 88  ? 112.723 140.326 78.676  1.00 48.10 ? 88  LYS A CD    1 
ATOM   722   C  CE    . LYS A 1 88  ? 113.927 140.390 77.749  1.00 49.48 ? 88  LYS A CE    1 
ATOM   723   N  NZ    . LYS A 1 88  ? 113.525 140.357 76.316  1.00 48.66 ? 88  LYS A NZ    1 
ATOM   724   N  N     . PHE A 1 89  ? 116.543 138.963 83.389  1.00 42.04 ? 89  PHE A N     1 
ATOM   725   C  CA    . PHE A 1 89  ? 117.367 137.921 83.983  1.00 39.19 ? 89  PHE A CA    1 
ATOM   726   C  C     . PHE A 1 89  ? 116.511 136.734 84.399  1.00 41.58 ? 89  PHE A C     1 
ATOM   727   O  O     . PHE A 1 89  ? 115.428 136.893 84.968  1.00 44.90 ? 89  PHE A O     1 
ATOM   728   C  CB    . PHE A 1 89  ? 118.127 138.474 85.192  1.00 36.60 ? 89  PHE A CB    1 
ATOM   729   C  CG    . PHE A 1 89  ? 118.813 137.419 86.012  1.00 37.60 ? 89  PHE A CG    1 
ATOM   730   C  CD1   . PHE A 1 89  ? 120.075 136.971 85.668  1.00 35.62 ? 89  PHE A CD1   1 
ATOM   731   C  CD2   . PHE A 1 89  ? 118.198 136.876 87.127  1.00 35.76 ? 89  PHE A CD2   1 
ATOM   732   C  CE1   . PHE A 1 89  ? 120.707 136.003 86.418  1.00 38.04 ? 89  PHE A CE1   1 
ATOM   733   C  CE2   . PHE A 1 89  ? 118.826 135.907 87.879  1.00 36.44 ? 89  PHE A CE2   1 
ATOM   734   C  CZ    . PHE A 1 89  ? 120.081 135.470 87.525  1.00 37.89 ? 89  PHE A CZ    1 
ATOM   735   N  N     . ARG A 1 90  ? 117.007 135.534 84.111  1.00 41.17 ? 90  ARG A N     1 
ATOM   736   C  CA    . ARG A 1 90  ? 116.351 134.297 84.504  1.00 41.00 ? 90  ARG A CA    1 
ATOM   737   C  C     . ARG A 1 90  ? 117.346 133.433 85.259  1.00 40.91 ? 90  ARG A C     1 
ATOM   738   O  O     . ARG A 1 90  ? 118.467 133.217 84.789  1.00 43.41 ? 90  ARG A O     1 
ATOM   739   C  CB    . ARG A 1 90  ? 115.806 133.542 83.287  1.00 43.75 ? 90  ARG A CB    1 
ATOM   740   C  CG    . ARG A 1 90  ? 114.856 134.356 82.429  1.00 43.05 ? 90  ARG A CG    1 
ATOM   741   C  CD    . ARG A 1 90  ? 113.440 134.303 82.974  1.00 44.90 ? 90  ARG A CD    1 
ATOM   742   N  NE    . ARG A 1 90  ? 112.568 135.266 82.313  1.00 45.45 ? 90  ARG A NE    1 
ATOM   743   C  CZ    . ARG A 1 90  ? 112.356 136.503 82.740  1.00 47.49 ? 90  ARG A CZ    1 
ATOM   744   N  NH1   . ARG A 1 90  ? 112.920 136.959 83.846  1.00 47.32 ? 90  ARG A NH1   1 
ATOM   745   N  NH2   . ARG A 1 90  ? 111.556 137.302 82.040  1.00 44.69 ? 90  ARG A NH2   1 
ATOM   746   N  N     . PHE A 1 91  ? 116.940 132.953 86.424  1.00 36.89 ? 91  PHE A N     1 
ATOM   747   C  CA    . PHE A 1 91  ? 117.785 132.051 87.191  1.00 36.56 ? 91  PHE A CA    1 
ATOM   748   C  C     . PHE A 1 91  ? 117.945 130.737 86.434  1.00 42.85 ? 91  PHE A C     1 
ATOM   749   O  O     . PHE A 1 91  ? 116.945 130.137 86.026  1.00 44.99 ? 91  PHE A O     1 
ATOM   750   C  CB    . PHE A 1 91  ? 117.181 131.804 88.569  1.00 35.45 ? 91  PHE A CB    1 
ATOM   751   C  CG    . PHE A 1 91  ? 117.287 132.981 89.495  1.00 40.16 ? 91  PHE A CG    1 
ATOM   752   C  CD1   . PHE A 1 91  ? 118.434 133.195 90.238  1.00 42.84 ? 91  PHE A CD1   1 
ATOM   753   C  CD2   . PHE A 1 91  ? 116.240 133.877 89.621  1.00 39.75 ? 91  PHE A CD2   1 
ATOM   754   C  CE1   . PHE A 1 91  ? 118.535 134.274 91.091  1.00 39.25 ? 91  PHE A CE1   1 
ATOM   755   C  CE2   . PHE A 1 91  ? 116.335 134.958 90.472  1.00 39.69 ? 91  PHE A CE2   1 
ATOM   756   C  CZ    . PHE A 1 91  ? 117.483 135.157 91.208  1.00 38.46 ? 91  PHE A CZ    1 
ATOM   757   N  N     . PRO A 1 92  ? 119.175 130.260 86.221  1.00 41.92 ? 92  PRO A N     1 
ATOM   758   C  CA    . PRO A 1 92  ? 119.356 129.035 85.432  1.00 37.61 ? 92  PRO A CA    1 
ATOM   759   C  C     . PRO A 1 92  ? 119.031 127.762 86.188  1.00 38.97 ? 92  PRO A C     1 
ATOM   760   O  O     . PRO A 1 92  ? 118.850 126.715 85.552  1.00 41.36 ? 92  PRO A O     1 
ATOM   761   C  CB    . PRO A 1 92  ? 120.840 129.086 85.055  1.00 39.07 ? 92  PRO A CB    1 
ATOM   762   C  CG    . PRO A 1 92  ? 121.472 129.796 86.204  1.00 39.73 ? 92  PRO A CG    1 
ATOM   763   C  CD    . PRO A 1 92  ? 120.455 130.784 86.730  1.00 41.21 ? 92  PRO A CD    1 
ATOM   764   N  N     . SER A 1 93  ? 118.949 127.815 87.514  1.00 40.68 ? 93  SER A N     1 
ATOM   765   C  CA    . SER A 1 93  ? 118.725 126.630 88.325  1.00 43.92 ? 93  SER A CA    1 
ATOM   766   C  C     . SER A 1 93  ? 117.742 126.963 89.436  1.00 44.25 ? 93  SER A C     1 
ATOM   767   O  O     . SER A 1 93  ? 117.561 128.125 89.806  1.00 46.86 ? 93  SER A O     1 
ATOM   768   C  CB    . SER A 1 93  ? 120.038 126.100 88.915  1.00 41.73 ? 93  SER A CB    1 
ATOM   769   O  OG    . SER A 1 93  ? 120.454 126.883 90.019  1.00 41.28 ? 93  SER A OG    1 
ATOM   770   N  N     . PHE A 1 94  ? 117.098 125.919 89.962  1.00 42.59 ? 94  PHE A N     1 
ATOM   771   C  CA    . PHE A 1 94  ? 116.165 126.114 91.066  1.00 43.68 ? 94  PHE A CA    1 
ATOM   772   C  C     . PHE A 1 94  ? 116.882 126.602 92.317  1.00 44.63 ? 94  PHE A C     1 
ATOM   773   O  O     . PHE A 1 94  ? 116.330 127.401 93.081  1.00 47.29 ? 94  PHE A O     1 
ATOM   774   C  CB    . PHE A 1 94  ? 115.404 124.821 91.355  1.00 42.66 ? 94  PHE A CB    1 
ATOM   775   C  CG    . PHE A 1 94  ? 114.757 124.794 92.710  1.00 44.46 ? 94  PHE A CG    1 
ATOM   776   C  CD1   . PHE A 1 94  ? 113.667 125.600 92.987  1.00 45.04 ? 94  PHE A CD1   1 
ATOM   777   C  CD2   . PHE A 1 94  ? 115.241 123.967 93.707  1.00 46.02 ? 94  PHE A CD2   1 
ATOM   778   C  CE1   . PHE A 1 94  ? 113.075 125.583 94.233  1.00 45.08 ? 94  PHE A CE1   1 
ATOM   779   C  CE2   . PHE A 1 94  ? 114.651 123.944 94.956  1.00 47.49 ? 94  PHE A CE2   1 
ATOM   780   C  CZ    . PHE A 1 94  ? 113.567 124.753 95.218  1.00 45.20 ? 94  PHE A CZ    1 
ATOM   781   N  N     . MET A 1 95  ? 118.106 126.123 92.552  1.00 41.20 ? 95  MET A N     1 
ATOM   782   C  CA    . MET A 1 95  ? 118.822 126.498 93.767  1.00 36.23 ? 95  MET A CA    1 
ATOM   783   C  C     . MET A 1 95  ? 119.137 127.986 93.796  1.00 39.55 ? 95  MET A C     1 
ATOM   784   O  O     . MET A 1 95  ? 119.070 128.614 94.855  1.00 44.80 ? 95  MET A O     1 
ATOM   785   C  CB    . MET A 1 95  ? 120.107 125.682 93.900  1.00 42.89 ? 95  MET A CB    1 
ATOM   786   C  CG    . MET A 1 95  ? 120.505 125.277 95.328  1.00 44.91 ? 95  MET A CG    1 
ATOM   787   S  SD    . MET A 1 95  ? 119.229 124.985 96.579  1.00 53.52 ? 95  MET A SD    1 
ATOM   788   C  CE    . MET A 1 95  ? 118.093 123.883 95.737  1.00 45.45 ? 95  MET A CE    1 
ATOM   789   N  N     . SER A 1 96  ? 119.494 128.567 92.650  1.00 36.11 ? 96  SER A N     1 
ATOM   790   C  CA    . SER A 1 96  ? 119.809 129.992 92.611  1.00 33.14 ? 96  SER A CA    1 
ATOM   791   C  C     . SER A 1 96  ? 118.626 130.829 93.080  1.00 34.37 ? 96  SER A C     1 
ATOM   792   O  O     . SER A 1 96  ? 118.747 131.642 94.009  1.00 34.99 ? 96  SER A O     1 
ATOM   793   C  CB    . SER A 1 96  ? 120.213 130.389 91.192  1.00 35.69 ? 96  SER A CB    1 
ATOM   794   O  OG    . SER A 1 96  ? 120.981 129.370 90.580  1.00 39.83 ? 96  SER A OG    1 
ATOM   795   N  N     . ALA A 1 97  ? 117.463 130.618 92.463  1.00 40.34 ? 97  ALA A N     1 
ATOM   796   C  CA    . ALA A 1 97  ? 116.275 131.380 92.821  1.00 36.55 ? 97  ALA A CA    1 
ATOM   797   C  C     . ALA A 1 97  ? 115.821 131.065 94.237  1.00 36.76 ? 97  ALA A C     1 
ATOM   798   O  O     . ALA A 1 97  ? 115.391 131.962 94.970  1.00 45.12 ? 97  ALA A O     1 
ATOM   799   C  CB    . ALA A 1 97  ? 115.157 131.098 91.823  1.00 36.32 ? 97  ALA A CB    1 
ATOM   800   N  N     . PHE A 1 98  ? 115.895 129.795 94.638  1.00 33.40 ? 98  PHE A N     1 
ATOM   801   C  CA    . PHE A 1 98  ? 115.473 129.420 95.981  1.00 35.30 ? 98  PHE A CA    1 
ATOM   802   C  C     . PHE A 1 98  ? 116.333 130.108 97.031  1.00 37.35 ? 98  PHE A C     1 
ATOM   803   O  O     . PHE A 1 98  ? 115.816 130.679 97.998  1.00 45.04 ? 98  PHE A O     1 
ATOM   804   C  CB    . PHE A 1 98  ? 115.532 127.902 96.145  1.00 40.80 ? 98  PHE A CB    1 
ATOM   805   C  CG    . PHE A 1 98  ? 115.340 127.441 97.560  1.00 42.56 ? 98  PHE A CG    1 
ATOM   806   C  CD1   . PHE A 1 98  ? 114.073 127.373 98.110  1.00 41.79 ? 98  PHE A CD1   1 
ATOM   807   C  CD2   . PHE A 1 98  ? 116.424 127.080 98.341  1.00 42.75 ? 98  PHE A CD2   1 
ATOM   808   C  CE1   . PHE A 1 98  ? 113.889 126.954 99.410  1.00 41.53 ? 98  PHE A CE1   1 
ATOM   809   C  CE2   . PHE A 1 98  ? 116.246 126.661 99.644  1.00 43.12 ? 98  PHE A CE2   1 
ATOM   810   C  CZ    . PHE A 1 98  ? 114.976 126.597 100.178 1.00 43.29 ? 98  PHE A CZ    1 
ATOM   811   N  N     . LYS A 1 99  ? 117.653 130.075 96.847  1.00 38.62 ? 99  LYS A N     1 
ATOM   812   C  CA    . LYS A 1 99  ? 118.551 130.721 97.793  1.00 38.42 ? 99  LYS A CA    1 
ATOM   813   C  C     . LYS A 1 99  ? 118.323 132.222 97.826  1.00 38.30 ? 99  LYS A C     1 
ATOM   814   O  O     . LYS A 1 99  ? 118.296 132.824 98.905  1.00 40.49 ? 99  LYS A O     1 
ATOM   815   C  CB    . LYS A 1 99  ? 120.003 130.400 97.442  1.00 38.88 ? 99  LYS A CB    1 
ATOM   816   C  CG    . LYS A 1 99  ? 120.416 128.976 97.774  1.00 41.49 ? 99  LYS A CG    1 
ATOM   817   C  CD    . LYS A 1 99  ? 120.003 128.593 99.182  1.00 43.01 ? 99  LYS A CD    1 
ATOM   818   C  CE    . LYS A 1 99  ? 121.147 127.938 99.933  1.00 40.66 ? 99  LYS A CE    1 
ATOM   819   N  NZ    . LYS A 1 99  ? 121.025 128.142 101.400 1.00 41.47 ? 99  LYS A NZ    1 
ATOM   820   N  N     . PHE A 1 100 ? 118.133 132.848 96.660  1.00 34.86 ? 100 PHE A N     1 
ATOM   821   C  CA    . PHE A 1 100 ? 117.887 134.286 96.664  1.00 35.47 ? 100 PHE A CA    1 
ATOM   822   C  C     . PHE A 1 100 ? 116.601 134.623 97.407  1.00 37.31 ? 100 PHE A C     1 
ATOM   823   O  O     . PHE A 1 100 ? 116.602 135.448 98.326  1.00 42.26 ? 100 PHE A O     1 
ATOM   824   C  CB    . PHE A 1 100 ? 117.826 134.844 95.245  1.00 36.45 ? 100 PHE A CB    1 
ATOM   825   C  CG    . PHE A 1 100 ? 117.434 136.290 95.206  1.00 36.36 ? 100 PHE A CG    1 
ATOM   826   C  CD1   . PHE A 1 100 ? 118.329 137.268 95.606  1.00 38.00 ? 100 PHE A CD1   1 
ATOM   827   C  CD2   . PHE A 1 100 ? 116.163 136.672 94.818  1.00 36.40 ? 100 PHE A CD2   1 
ATOM   828   C  CE1   . PHE A 1 100 ? 117.972 138.599 95.596  1.00 38.58 ? 100 PHE A CE1   1 
ATOM   829   C  CE2   . PHE A 1 100 ? 115.801 138.003 94.807  1.00 39.62 ? 100 PHE A CE2   1 
ATOM   830   C  CZ    . PHE A 1 100 ? 116.707 138.967 95.197  1.00 39.19 ? 100 PHE A CZ    1 
ATOM   831   N  N     . TYR A 1 101 ? 115.496 133.979 97.040  1.00 40.79 ? 101 TYR A N     1 
ATOM   832   C  CA    . TYR A 1 101 ? 114.206 134.324 97.620  1.00 38.58 ? 101 TYR A CA    1 
ATOM   833   C  C     . TYR A 1 101 ? 114.029 133.796 99.036  1.00 40.46 ? 101 TYR A C     1 
ATOM   834   O  O     . TYR A 1 101 ? 113.032 134.133 99.681  1.00 47.36 ? 101 TYR A O     1 
ATOM   835   C  CB    . TYR A 1 101 ? 113.077 133.824 96.717  1.00 38.44 ? 101 TYR A CB    1 
ATOM   836   C  CG    . TYR A 1 101 ? 112.940 134.643 95.454  1.00 36.68 ? 101 TYR A CG    1 
ATOM   837   C  CD1   . TYR A 1 101 ? 112.434 135.934 95.495  1.00 39.61 ? 101 TYR A CD1   1 
ATOM   838   C  CD2   . TYR A 1 101 ? 113.342 134.137 94.228  1.00 35.56 ? 101 TYR A CD2   1 
ATOM   839   C  CE1   . TYR A 1 101 ? 112.318 136.692 94.347  1.00 39.31 ? 101 TYR A CE1   1 
ATOM   840   C  CE2   . TYR A 1 101 ? 113.232 134.887 93.076  1.00 39.38 ? 101 TYR A CE2   1 
ATOM   841   C  CZ    . TYR A 1 101 ? 112.719 136.164 93.140  1.00 41.06 ? 101 TYR A CZ    1 
ATOM   842   O  OH    . TYR A 1 101 ? 112.607 136.913 91.992  1.00 39.65 ? 101 TYR A OH    1 
ATOM   843   N  N     . ASN A 1 102 ? 114.963 132.987 99.534  1.00 40.06 ? 102 ASN A N     1 
ATOM   844   C  CA    . ASN A 1 102 ? 114.926 132.559 100.923 1.00 41.18 ? 102 ASN A CA    1 
ATOM   845   C  C     . ASN A 1 102 ? 115.897 133.315 101.820 1.00 42.99 ? 102 ASN A C     1 
ATOM   846   O  O     . ASN A 1 102 ? 115.658 133.392 103.030 1.00 44.51 ? 102 ASN A O     1 
ATOM   847   C  CB    . ASN A 1 102 ? 115.223 131.058 101.022 1.00 42.54 ? 102 ASN A CB    1 
ATOM   848   C  CG    . ASN A 1 102 ? 113.967 130.213 101.005 1.00 44.42 ? 102 ASN A CG    1 
ATOM   849   O  OD1   . ASN A 1 102 ? 113.079 130.416 100.177 1.00 45.57 ? 102 ASN A OD1   1 
ATOM   850   N  ND2   . ASN A 1 102 ? 113.885 129.259 101.924 1.00 44.04 ? 102 ASN A ND2   1 
ATOM   851   N  N     . ASP A 1 103 ? 116.978 133.871 101.275 1.00 43.40 ? 103 ASP A N     1 
ATOM   852   C  CA    . ASP A 1 103 ? 117.996 134.522 102.089 1.00 40.57 ? 103 ASP A CA    1 
ATOM   853   C  C     . ASP A 1 103 ? 118.100 136.022 101.871 1.00 41.72 ? 103 ASP A C     1 
ATOM   854   O  O     . ASP A 1 103 ? 118.306 136.762 102.834 1.00 48.23 ? 103 ASP A O     1 
ATOM   855   C  CB    . ASP A 1 103 ? 119.366 133.888 101.821 1.00 44.30 ? 103 ASP A CB    1 
ATOM   856   C  CG    . ASP A 1 103 ? 119.446 132.448 102.287 1.00 46.49 ? 103 ASP A CG    1 
ATOM   857   O  OD1   . ASP A 1 103 ? 118.428 131.922 102.782 1.00 47.53 ? 103 ASP A OD1   1 
ATOM   858   O  OD2   . ASP A 1 103 ? 120.529 131.841 102.158 1.00 48.41 ? 103 ASP A OD2   1 
ATOM   859   N  N     . TYR A 1 104 ? 117.966 136.501 100.632 1.00 31.92 ? 104 TYR A N     1 
ATOM   860   C  CA    . TYR A 1 104 ? 118.252 137.892 100.315 1.00 38.10 ? 104 TYR A CA    1 
ATOM   861   C  C     . TYR A 1 104 ? 117.043 138.693 99.858  1.00 40.63 ? 104 TYR A C     1 
ATOM   862   O  O     . TYR A 1 104 ? 117.059 139.920 99.988  1.00 44.95 ? 104 TYR A O     1 
ATOM   863   C  CB    . TYR A 1 104 ? 119.336 137.973 99.229  1.00 36.22 ? 104 TYR A CB    1 
ATOM   864   C  CG    . TYR A 1 104 ? 120.598 137.226 99.587  1.00 39.70 ? 104 TYR A CG    1 
ATOM   865   C  CD1   . TYR A 1 104 ? 121.586 137.824 100.355 1.00 35.52 ? 104 TYR A CD1   1 
ATOM   866   C  CD2   . TYR A 1 104 ? 120.796 135.918 99.166  1.00 35.63 ? 104 TYR A CD2   1 
ATOM   867   C  CE1   . TYR A 1 104 ? 122.737 137.143 100.689 1.00 36.30 ? 104 TYR A CE1   1 
ATOM   868   C  CE2   . TYR A 1 104 ? 121.945 135.229 99.496  1.00 35.28 ? 104 TYR A CE2   1 
ATOM   869   C  CZ    . TYR A 1 104 ? 122.913 135.847 100.258 1.00 39.94 ? 104 TYR A CZ    1 
ATOM   870   O  OH    . TYR A 1 104 ? 124.060 135.166 100.590 1.00 39.05 ? 104 TYR A OH    1 
ATOM   871   N  N     . ALA A 1 105 ? 116.010 138.047 99.327  1.00 40.22 ? 105 ALA A N     1 
ATOM   872   C  CA    . ALA A 1 105 ? 114.833 138.779 98.882  1.00 39.92 ? 105 ALA A CA    1 
ATOM   873   C  C     . ALA A 1 105 ? 114.095 139.377 100.072 1.00 43.10 ? 105 ALA A C     1 
ATOM   874   O  O     . ALA A 1 105 ? 113.904 138.721 101.100 1.00 42.76 ? 105 ALA A O     1 
ATOM   875   C  CB    . ALA A 1 105 ? 113.899 137.867 98.092  1.00 37.87 ? 105 ALA A CB    1 
ATOM   876   N  N     . LEU A 1 106 ? 113.683 140.633 99.929  1.00 46.22 ? 106 LEU A N     1 
ATOM   877   C  CA    . LEU A 1 106 ? 112.943 141.298 100.990 1.00 45.47 ? 106 LEU A CA    1 
ATOM   878   C  C     . LEU A 1 106 ? 111.558 140.686 101.139 1.00 47.05 ? 106 LEU A C     1 
ATOM   879   O  O     . LEU A 1 106 ? 110.858 140.436 100.153 1.00 45.30 ? 106 LEU A O     1 
ATOM   880   C  CB    . LEU A 1 106 ? 112.829 142.794 100.704 1.00 45.78 ? 106 LEU A CB    1 
ATOM   881   C  CG    . LEU A 1 106 ? 112.202 143.658 101.799 1.00 44.06 ? 106 LEU A CG    1 
ATOM   882   C  CD1   . LEU A 1 106 ? 113.100 143.714 103.021 1.00 43.15 ? 106 LEU A CD1   1 
ATOM   883   C  CD2   . LEU A 1 106 ? 111.928 145.052 101.276 1.00 44.78 ? 106 LEU A CD2   1 
ATOM   884   N  N     . LYS A 1 107 ? 111.164 140.445 102.384 1.00 53.22 ? 107 LYS A N     1 
ATOM   885   C  CA    . LYS A 1 107 ? 109.867 139.879 102.707 1.00 52.77 ? 107 LYS A CA    1 
ATOM   886   C  C     . LYS A 1 107 ? 109.128 140.809 103.659 1.00 53.19 ? 107 LYS A C     1 
ATOM   887   O  O     . LYS A 1 107 ? 109.727 141.667 104.314 1.00 53.49 ? 107 LYS A O     1 
ATOM   888   C  CB    . LYS A 1 107 ? 110.007 138.486 103.333 1.00 50.96 ? 107 LYS A CB    1 
ATOM   889   C  CG    . LYS A 1 107 ? 110.413 137.406 102.348 1.00 50.18 ? 107 LYS A CG    1 
ATOM   890   C  CD    . LYS A 1 107 ? 110.683 136.090 103.054 1.00 54.27 ? 107 LYS A CD    1 
ATOM   891   C  CE    . LYS A 1 107 ? 111.052 135.001 102.062 1.00 53.95 ? 107 LYS A CE    1 
ATOM   892   N  NZ    . LYS A 1 107 ? 111.640 133.809 102.734 1.00 51.18 ? 107 LYS A NZ    1 
ATOM   893   N  N     . THR A 1 108 ? 107.811 140.633 103.723 1.00 60.43 ? 108 THR A N     1 
ATOM   894   C  CA    . THR A 1 108 ? 106.991 141.434 104.615 1.00 60.90 ? 108 THR A CA    1 
ATOM   895   C  C     . THR A 1 108 ? 107.386 141.177 106.070 1.00 61.68 ? 108 THR A C     1 
ATOM   896   O  O     . THR A 1 108 ? 108.117 140.238 106.391 1.00 60.29 ? 108 THR A O     1 
ATOM   897   C  CB    . THR A 1 108 ? 105.510 141.128 104.399 1.00 60.37 ? 108 THR A CB    1 
ATOM   898   O  OG1   . THR A 1 108 ? 105.328 139.715 104.256 1.00 62.46 ? 108 THR A OG1   1 
ATOM   899   C  CG2   . THR A 1 108 ? 105.004 141.825 103.145 1.00 58.65 ? 108 THR A CG2   1 
ATOM   900   N  N     . ASN A 1 109 ? 106.883 142.038 106.959 1.00 63.26 ? 109 ASN A N     1 
ATOM   901   C  CA    . ASN A 1 109 ? 107.296 141.988 108.358 1.00 62.85 ? 109 ASN A CA    1 
ATOM   902   C  C     . ASN A 1 109 ? 106.941 140.659 109.013 1.00 64.16 ? 109 ASN A C     1 
ATOM   903   O  O     . ASN A 1 109 ? 107.603 140.245 109.971 1.00 65.14 ? 109 ASN A O     1 
ATOM   904   C  CB    . ASN A 1 109 ? 106.665 143.146 109.130 1.00 62.97 ? 109 ASN A CB    1 
ATOM   905   C  CG    . ASN A 1 109 ? 107.432 144.440 108.961 1.00 63.07 ? 109 ASN A CG    1 
ATOM   906   O  OD1   . ASN A 1 109 ? 108.655 144.436 108.834 1.00 64.49 ? 109 ASN A OD1   1 
ATOM   907   N  ND2   . ASN A 1 109 ? 106.715 145.557 108.958 1.00 63.35 ? 109 ASN A ND2   1 
ATOM   908   N  N     . ASP A 1 110 ? 105.911 139.978 108.516 1.00 69.12 ? 110 ASP A N     1 
ATOM   909   C  CA    . ASP A 1 110 ? 105.510 138.679 109.035 1.00 68.29 ? 110 ASP A CA    1 
ATOM   910   C  C     . ASP A 1 110 ? 106.143 137.523 108.271 1.00 68.71 ? 110 ASP A C     1 
ATOM   911   O  O     . ASP A 1 110 ? 105.762 136.369 108.491 1.00 69.83 ? 110 ASP A O     1 
ATOM   912   C  CB    . ASP A 1 110 ? 103.986 138.550 109.013 1.00 67.73 ? 110 ASP A CB    1 
ATOM   913   C  CG    . ASP A 1 110 ? 103.372 139.111 107.747 1.00 69.22 ? 110 ASP A CG    1 
ATOM   914   O  OD1   . ASP A 1 110 ? 104.016 139.961 107.099 1.00 69.25 ? 110 ASP A OD1   1 
ATOM   915   O  OD2   . ASP A 1 110 ? 102.244 138.703 107.401 1.00 71.60 ? 110 ASP A OD2   1 
ATOM   916   N  N     . LYS A 1 111 ? 107.100 137.809 107.383 1.00 67.01 ? 111 LYS A N     1 
ATOM   917   C  CA    . LYS A 1 111 ? 107.766 136.789 106.569 1.00 65.67 ? 111 LYS A CA    1 
ATOM   918   C  C     . LYS A 1 111 ? 106.755 135.980 105.761 1.00 66.20 ? 111 LYS A C     1 
ATOM   919   O  O     . LYS A 1 111 ? 106.885 134.764 105.607 1.00 67.81 ? 111 LYS A O     1 
ATOM   920   C  CB    . LYS A 1 111 ? 108.633 135.864 107.429 1.00 65.50 ? 111 LYS A CB    1 
ATOM   921   C  CG    . LYS A 1 111 ? 109.797 136.540 108.147 1.00 65.50 ? 111 LYS A CG    1 
ATOM   922   C  CD    . LYS A 1 111 ? 110.378 137.697 107.351 1.00 66.84 ? 111 LYS A CD    1 
ATOM   923   C  CE    . LYS A 1 111 ? 110.396 138.975 108.173 1.00 67.05 ? 111 LYS A CE    1 
ATOM   924   N  NZ    . LYS A 1 111 ? 110.907 140.134 107.390 1.00 64.50 ? 111 LYS A NZ    1 
ATOM   925   N  N     . LYS A 1 112 ? 105.738 136.661 105.236 1.00 65.19 ? 112 LYS A N     1 
ATOM   926   C  CA    . LYS A 1 112 ? 104.636 136.003 104.545 1.00 67.21 ? 112 LYS A CA    1 
ATOM   927   C  C     . LYS A 1 112 ? 104.747 136.098 103.029 1.00 66.80 ? 112 LYS A C     1 
ATOM   928   O  O     . LYS A 1 112 ? 104.703 135.076 102.340 1.00 68.38 ? 112 LYS A O     1 
ATOM   929   C  CB    . LYS A 1 112 ? 103.301 136.598 105.009 1.00 66.64 ? 112 LYS A CB    1 
ATOM   930   C  CG    . LYS A 1 112 ? 102.086 135.762 104.640 1.00 68.30 ? 112 LYS A CG    1 
ATOM   931   C  CD    . LYS A 1 112 ? 102.052 134.456 105.420 1.00 68.79 ? 112 LYS A CD    1 
ATOM   932   C  CE    . LYS A 1 112 ? 102.190 134.694 106.917 1.00 68.99 ? 112 LYS A CE    1 
ATOM   933   N  NZ    . LYS A 1 112 ? 101.184 135.667 107.425 1.00 66.88 ? 112 LYS A NZ    1 
ATOM   934   N  N     . LYS A 1 113 ? 104.891 137.305 102.497 1.00 59.44 ? 113 LYS A N     1 
ATOM   935   C  CA    . LYS A 1 113 ? 104.959 137.540 101.064 1.00 57.71 ? 113 LYS A CA    1 
ATOM   936   C  C     . LYS A 1 113 ? 106.345 138.053 100.687 1.00 57.01 ? 113 LYS A C     1 
ATOM   937   O  O     . LYS A 1 113 ? 107.213 138.262 101.538 1.00 58.33 ? 113 LYS A O     1 
ATOM   938   C  CB    . LYS A 1 113 ? 103.866 138.519 100.631 1.00 57.89 ? 113 LYS A CB    1 
ATOM   939   C  CG    . LYS A 1 113 ? 102.456 137.964 100.744 1.00 58.07 ? 113 LYS A CG    1 
ATOM   940   C  CD    . LYS A 1 113 ? 102.168 136.960 99.642  1.00 61.03 ? 113 LYS A CD    1 
ATOM   941   C  CE    . LYS A 1 113 ? 100.741 136.446 99.716  1.00 59.78 ? 113 LYS A CE    1 
ATOM   942   N  NZ    . LYS A 1 113 ? 100.473 135.410 98.682  1.00 58.38 ? 113 LYS A NZ    1 
ATOM   943   N  N     . ILE A 1 114 ? 106.546 138.259 99.389  1.00 53.05 ? 114 ILE A N     1 
ATOM   944   C  CA    . ILE A 1 114 ? 107.832 138.667 98.835  1.00 51.46 ? 114 ILE A CA    1 
ATOM   945   C  C     . ILE A 1 114 ? 107.678 140.069 98.265  1.00 49.81 ? 114 ILE A C     1 
ATOM   946   O  O     . ILE A 1 114 ? 106.796 140.316 97.432  1.00 52.14 ? 114 ILE A O     1 
ATOM   947   C  CB    . ILE A 1 114 ? 108.323 137.683 97.762  1.00 52.38 ? 114 ILE A CB    1 
ATOM   948   C  CG1   . ILE A 1 114 ? 108.818 136.391 98.410  1.00 50.93 ? 114 ILE A CG1   1 
ATOM   949   C  CG2   . ILE A 1 114 ? 109.421 138.309 96.920  1.00 52.21 ? 114 ILE A CG2   1 
ATOM   950   C  CD1   . ILE A 1 114 ? 108.890 135.225 97.457  1.00 51.04 ? 114 ILE A CD1   1 
ATOM   951   N  N     . LEU A 1 115 ? 108.531 140.987 98.714  1.00 49.08 ? 115 LEU A N     1 
ATOM   952   C  CA    . LEU A 1 115 ? 108.502 142.371 98.257  1.00 50.55 ? 115 LEU A CA    1 
ATOM   953   C  C     . LEU A 1 115 ? 109.490 142.652 97.136  1.00 51.28 ? 115 LEU A C     1 
ATOM   954   O  O     . LEU A 1 115 ? 109.172 143.407 96.213  1.00 51.53 ? 115 LEU A O     1 
ATOM   955   C  CB    . LEU A 1 115 ? 108.783 143.320 99.426  1.00 50.10 ? 115 LEU A CB    1 
ATOM   956   C  CG    . LEU A 1 115 ? 107.726 143.355 100.528 1.00 48.92 ? 115 LEU A CG    1 
ATOM   957   C  CD1   . LEU A 1 115 ? 108.349 143.762 101.851 1.00 50.16 ? 115 LEU A CD1   1 
ATOM   958   C  CD2   . LEU A 1 115 ? 106.603 144.297 100.145 1.00 50.74 ? 115 LEU A CD2   1 
ATOM   959   N  N     . GLU A 1 116 ? 110.678 142.059 97.189  1.00 49.01 ? 116 GLU A N     1 
ATOM   960   C  CA    . GLU A 1 116 ? 111.741 142.330 96.232  1.00 45.96 ? 116 GLU A CA    1 
ATOM   961   C  C     . GLU A 1 116 ? 111.935 141.138 95.309  1.00 46.68 ? 116 GLU A C     1 
ATOM   962   O  O     . GLU A 1 116 ? 111.984 139.993 95.768  1.00 50.47 ? 116 GLU A O     1 
ATOM   963   C  CB    . GLU A 1 116 ? 113.056 142.640 96.949  1.00 44.86 ? 116 GLU A CB    1 
ATOM   964   C  CG    . GLU A 1 116 ? 113.360 144.114 97.098  1.00 44.72 ? 116 GLU A CG    1 
ATOM   965   C  CD    . GLU A 1 116 ? 114.598 144.361 97.931  1.00 46.78 ? 116 GLU A CD    1 
ATOM   966   O  OE1   . GLU A 1 116 ? 115.082 143.405 98.570  1.00 45.69 ? 116 GLU A OE1   1 
ATOM   967   O  OE2   . GLU A 1 116 ? 115.090 145.508 97.945  1.00 48.03 ? 116 GLU A OE2   1 
ATOM   968   N  N     . ARG A 1 117 ? 112.044 141.412 94.014  1.00 40.98 ? 117 ARG A N     1 
ATOM   969   C  CA    . ARG A 1 117 ? 112.541 140.434 93.063  1.00 41.68 ? 117 ARG A CA    1 
ATOM   970   C  C     . ARG A 1 117 ? 114.061 140.568 92.991  1.00 43.36 ? 117 ARG A C     1 
ATOM   971   O  O     . ARG A 1 117 ? 114.671 141.339 93.736  1.00 47.12 ? 117 ARG A O     1 
ATOM   972   C  CB    . ARG A 1 117 ? 111.877 140.625 91.701  1.00 42.75 ? 117 ARG A CB    1 
ATOM   973   C  CG    . ARG A 1 117 ? 110.357 140.641 91.740  1.00 44.89 ? 117 ARG A CG    1 
ATOM   974   C  CD    . ARG A 1 117 ? 109.806 139.434 92.483  1.00 49.34 ? 117 ARG A CD    1 
ATOM   975   N  NE    . ARG A 1 117 ? 109.897 138.209 91.697  1.00 47.15 ? 117 ARG A NE    1 
ATOM   976   C  CZ    . ARG A 1 117 ? 109.081 137.892 90.702  1.00 47.08 ? 117 ARG A CZ    1 
ATOM   977   N  NH1   . ARG A 1 117 ? 108.087 138.688 90.342  1.00 47.61 ? 117 ARG A NH1   1 
ATOM   978   N  NH2   . ARG A 1 117 ? 109.263 136.746 90.053  1.00 47.96 ? 117 ARG A NH2   1 
ATOM   979   N  N     . TYR A 1 118 ? 114.697 139.808 92.100  1.00 42.12 ? 118 TYR A N     1 
ATOM   980   C  CA    . TYR A 1 118 ? 116.134 139.962 91.906  1.00 35.59 ? 118 TYR A CA    1 
ATOM   981   C  C     . TYR A 1 118 ? 116.460 141.334 91.333  1.00 37.03 ? 118 TYR A C     1 
ATOM   982   O  O     . TYR A 1 118 ? 117.415 141.991 91.766  1.00 40.89 ? 118 TYR A O     1 
ATOM   983   C  CB    . TYR A 1 118 ? 116.656 138.852 90.995  1.00 36.62 ? 118 TYR A CB    1 
ATOM   984   C  CG    . TYR A 1 118 ? 118.155 138.678 91.022  1.00 36.41 ? 118 TYR A CG    1 
ATOM   985   C  CD1   . TYR A 1 118 ? 118.827 138.476 92.218  1.00 35.98 ? 118 TYR A CD1   1 
ATOM   986   C  CD2   . TYR A 1 118 ? 118.896 138.710 89.852  1.00 36.33 ? 118 TYR A CD2   1 
ATOM   987   C  CE1   . TYR A 1 118 ? 120.195 138.313 92.247  1.00 35.26 ? 118 TYR A CE1   1 
ATOM   988   C  CE2   . TYR A 1 118 ? 120.263 138.543 89.870  1.00 30.88 ? 118 TYR A CE2   1 
ATOM   989   C  CZ    . TYR A 1 118 ? 120.908 138.347 91.069  1.00 35.16 ? 118 TYR A CZ    1 
ATOM   990   O  OH    . TYR A 1 118 ? 122.273 138.186 91.090  1.00 45.63 ? 118 TYR A OH    1 
ATOM   991   N  N     . GLU A 1 119 ? 115.659 141.789 90.367  1.00 40.87 ? 119 GLU A N     1 
ATOM   992   C  CA    . GLU A 1 119 ? 115.882 143.098 89.765  1.00 38.65 ? 119 GLU A CA    1 
ATOM   993   C  C     . GLU A 1 119 ? 115.678 144.219 90.775  1.00 40.09 ? 119 GLU A C     1 
ATOM   994   O  O     . GLU A 1 119 ? 116.419 145.205 90.767  1.00 43.18 ? 119 GLU A O     1 
ATOM   995   C  CB    . GLU A 1 119 ? 114.960 143.282 88.561  1.00 40.78 ? 119 GLU A CB    1 
ATOM   996   C  CG    . GLU A 1 119 ? 115.413 142.538 87.319  1.00 40.58 ? 119 GLU A CG    1 
ATOM   997   C  CD    . GLU A 1 119 ? 114.826 141.144 87.222  1.00 43.83 ? 119 GLU A CD    1 
ATOM   998   O  OE1   . GLU A 1 119 ? 114.398 140.600 88.261  1.00 43.15 ? 119 GLU A OE1   1 
ATOM   999   O  OE2   . GLU A 1 119 ? 114.798 140.590 86.103  1.00 45.69 ? 119 GLU A OE2   1 
ATOM   1000  N  N     . ASP A 1 120 ? 114.678 144.090 91.650  1.00 42.18 ? 120 ASP A N     1 
ATOM   1001  C  CA    . ASP A 1 120 ? 114.441 145.121 92.657  1.00 38.43 ? 120 ASP A CA    1 
ATOM   1002  C  C     . ASP A 1 120 ? 115.612 145.224 93.626  1.00 38.47 ? 120 ASP A C     1 
ATOM   1003  O  O     . ASP A 1 120 ? 116.086 146.326 93.930  1.00 45.11 ? 120 ASP A O     1 
ATOM   1004  C  CB    . ASP A 1 120 ? 113.145 144.829 93.413  1.00 42.56 ? 120 ASP A CB    1 
ATOM   1005  C  CG    . ASP A 1 120 ? 111.972 144.595 92.488  1.00 47.65 ? 120 ASP A CG    1 
ATOM   1006  O  OD1   . ASP A 1 120 ? 111.901 145.266 91.437  1.00 46.65 ? 120 ASP A OD1   1 
ATOM   1007  O  OD2   . ASP A 1 120 ? 111.119 143.742 92.809  1.00 50.84 ? 120 ASP A OD2   1 
ATOM   1008  N  N     . ARG A 1 121 ? 116.092 144.081 94.120  1.00 33.30 ? 121 ARG A N     1 
ATOM   1009  C  CA    . ARG A 1 121 ? 117.231 144.086 95.030  1.00 32.93 ? 121 ARG A CA    1 
ATOM   1010  C  C     . ARG A 1 121 ? 118.471 144.653 94.355  1.00 34.08 ? 121 ARG A C     1 
ATOM   1011  O  O     . ARG A 1 121 ? 119.202 145.452 94.952  1.00 41.40 ? 121 ARG A O     1 
ATOM   1012  C  CB    . ARG A 1 121 ? 117.500 142.671 95.542  1.00 34.66 ? 121 ARG A CB    1 
ATOM   1013  C  CG    . ARG A 1 121 ? 118.651 142.569 96.526  1.00 32.58 ? 121 ARG A CG    1 
ATOM   1014  C  CD    . ARG A 1 121 ? 118.165 142.705 97.956  1.00 33.22 ? 121 ARG A CD    1 
ATOM   1015  N  NE    . ARG A 1 121 ? 119.035 143.560 98.752  1.00 37.87 ? 121 ARG A NE    1 
ATOM   1016  C  CZ    . ARG A 1 121 ? 118.767 144.820 99.065  1.00 37.53 ? 121 ARG A CZ    1 
ATOM   1017  N  NH1   . ARG A 1 121 ? 117.660 145.415 98.652  1.00 36.92 ? 121 ARG A NH1   1 
ATOM   1018  N  NH2   . ARG A 1 121 ? 119.632 145.501 99.809  1.00 34.10 ? 121 ARG A NH2   1 
ATOM   1019  N  N     . ILE A 1 122 ? 118.719 144.260 93.104  1.00 33.10 ? 122 ILE A N     1 
ATOM   1020  C  CA    . ILE A 1 122 ? 119.892 144.756 92.394  1.00 28.81 ? 122 ILE A CA    1 
ATOM   1021  C  C     . ILE A 1 122 ? 119.789 146.259 92.166  1.00 30.73 ? 122 ILE A C     1 
ATOM   1022  O  O     . ILE A 1 122 ? 120.772 146.989 92.327  1.00 36.98 ? 122 ILE A O     1 
ATOM   1023  C  CB    . ILE A 1 122 ? 120.081 143.983 91.077  1.00 32.22 ? 122 ILE A CB    1 
ATOM   1024  C  CG1   . ILE A 1 122 ? 120.810 142.668 91.350  1.00 26.90 ? 122 ILE A CG1   1 
ATOM   1025  C  CG2   . ILE A 1 122 ? 120.848 144.814 90.059  1.00 33.16 ? 122 ILE A CG2   1 
ATOM   1026  C  CD1   . ILE A 1 122 ? 121.129 141.888 90.115  1.00 33.14 ? 122 ILE A CD1   1 
ATOM   1027  N  N     . SER A 1 123 ? 118.602 146.748 91.800  1.00 34.61 ? 123 SER A N     1 
ATOM   1028  C  CA    . SER A 1 123 ? 118.421 148.180 91.588  1.00 32.15 ? 123 SER A CA    1 
ATOM   1029  C  C     . SER A 1 123 ? 118.627 148.961 92.877  1.00 31.87 ? 123 SER A C     1 
ATOM   1030  O  O     . SER A 1 123 ? 119.237 150.036 92.868  1.00 39.48 ? 123 SER A O     1 
ATOM   1031  C  CB    . SER A 1 123 ? 117.029 148.455 91.021  1.00 35.29 ? 123 SER A CB    1 
ATOM   1032  O  OG    . SER A 1 123 ? 116.673 147.487 90.056  1.00 40.06 ? 123 SER A OG    1 
ATOM   1033  N  N     . ILE A 1 124 ? 118.113 148.447 93.994  1.00 32.18 ? 124 ILE A N     1 
ATOM   1034  C  CA    . ILE A 1 124 ? 118.295 149.134 95.268  1.00 35.25 ? 124 ILE A CA    1 
ATOM   1035  C  C     . ILE A 1 124 ? 119.768 149.161 95.658  1.00 36.32 ? 124 ILE A C     1 
ATOM   1036  O  O     . ILE A 1 124 ? 120.286 150.192 96.105  1.00 39.45 ? 124 ILE A O     1 
ATOM   1037  C  CB    . ILE A 1 124 ? 117.423 148.482 96.355  1.00 38.31 ? 124 ILE A CB    1 
ATOM   1038  C  CG1   . ILE A 1 124 ? 115.946 148.755 96.069  1.00 39.34 ? 124 ILE A CG1   1 
ATOM   1039  C  CG2   . ILE A 1 124 ? 117.800 149.000 97.731  1.00 33.50 ? 124 ILE A CG2   1 
ATOM   1040  C  CD1   . ILE A 1 124 ? 115.647 150.203 95.738  1.00 37.60 ? 124 ILE A CD1   1 
ATOM   1041  N  N     . VAL A 1 125 ? 120.470 148.039 95.483  1.00 31.80 ? 125 VAL A N     1 
ATOM   1042  C  CA    . VAL A 1 125 ? 121.895 147.996 95.800  1.00 28.65 ? 125 VAL A CA    1 
ATOM   1043  C  C     . VAL A 1 125 ? 122.672 148.955 94.904  1.00 28.03 ? 125 VAL A C     1 
ATOM   1044  O  O     . VAL A 1 125 ? 123.607 149.628 95.352  1.00 39.45 ? 125 VAL A O     1 
ATOM   1045  C  CB    . VAL A 1 125 ? 122.421 146.552 95.688  1.00 32.81 ? 125 VAL A CB    1 
ATOM   1046  C  CG1   . VAL A 1 125 ? 123.925 146.517 95.834  1.00 30.62 ? 125 VAL A CG1   1 
ATOM   1047  C  CG2   . VAL A 1 125 ? 121.779 145.675 96.747  1.00 28.54 ? 125 VAL A CG2   1 
ATOM   1048  N  N     . ALA A 1 126 ? 122.284 149.051 93.632  1.00 26.97 ? 126 ALA A N     1 
ATOM   1049  C  CA    . ALA A 1 126 ? 122.978 149.940 92.706  1.00 26.90 ? 126 ALA A CA    1 
ATOM   1050  C  C     . ALA A 1 126 ? 122.741 151.404 93.049  1.00 33.59 ? 126 ALA A C     1 
ATOM   1051  O  O     . ALA A 1 126 ? 123.669 152.219 92.989  1.00 38.89 ? 126 ALA A O     1 
ATOM   1052  C  CB    . ALA A 1 126 ? 122.529 149.651 91.278  1.00 29.71 ? 126 ALA A CB    1 
ATOM   1053  N  N     . LEU A 1 127 ? 121.502 151.760 93.396  1.00 35.66 ? 127 LEU A N     1 
ATOM   1054  C  CA    . LEU A 1 127 ? 121.214 153.131 93.799  1.00 32.33 ? 127 LEU A CA    1 
ATOM   1055  C  C     . LEU A 1 127 ? 121.909 153.479 95.107  1.00 30.70 ? 127 LEU A C     1 
ATOM   1056  O  O     . LEU A 1 127 ? 122.304 154.632 95.310  1.00 35.41 ? 127 LEU A O     1 
ATOM   1057  C  CB    . LEU A 1 127 ? 119.705 153.338 93.920  1.00 33.66 ? 127 LEU A CB    1 
ATOM   1058  C  CG    . LEU A 1 127 ? 118.914 153.303 92.610  1.00 34.32 ? 127 LEU A CG    1 
ATOM   1059  C  CD1   . LEU A 1 127 ? 117.472 152.906 92.865  1.00 36.17 ? 127 LEU A CD1   1 
ATOM   1060  C  CD2   . LEU A 1 127 ? 118.985 154.641 91.897  1.00 35.11 ? 127 LEU A CD2   1 
ATOM   1061  N  N     . PHE A 1 128 ? 122.056 152.504 96.005  1.00 33.58 ? 128 PHE A N     1 
ATOM   1062  C  CA    . PHE A 1 128 ? 122.843 152.719 97.213  1.00 32.95 ? 128 PHE A CA    1 
ATOM   1063  C  C     . PHE A 1 128 ? 124.312 152.953 96.879  1.00 31.27 ? 128 PHE A C     1 
ATOM   1064  O  O     . PHE A 1 128 ? 124.952 153.841 97.453  1.00 39.12 ? 128 PHE A O     1 
ATOM   1065  C  CB    . PHE A 1 128 ? 122.679 151.524 98.151  1.00 30.22 ? 128 PHE A CB    1 
ATOM   1066  C  CG    . PHE A 1 128 ? 123.544 151.584 99.375  1.00 36.04 ? 128 PHE A CG    1 
ATOM   1067  C  CD1   . PHE A 1 128 ? 123.122 152.264 100.503 1.00 38.18 ? 128 PHE A CD1   1 
ATOM   1068  C  CD2   . PHE A 1 128 ? 124.774 150.949 99.404  1.00 34.01 ? 128 PHE A CD2   1 
ATOM   1069  C  CE1   . PHE A 1 128 ? 123.913 152.318 101.631 1.00 38.90 ? 128 PHE A CE1   1 
ATOM   1070  C  CE2   . PHE A 1 128 ? 125.569 151.004 100.527 1.00 33.65 ? 128 PHE A CE2   1 
ATOM   1071  C  CZ    . PHE A 1 128 ? 125.137 151.686 101.643 1.00 36.22 ? 128 PHE A CZ    1 
ATOM   1072  N  N     . PHE A 1 129 ? 124.863 152.163 95.954  1.00 27.91 ? 129 PHE A N     1 
ATOM   1073  C  CA    . PHE A 1 129 ? 126.269 152.306 95.587  1.00 25.18 ? 129 PHE A CA    1 
ATOM   1074  C  C     . PHE A 1 129 ? 126.544 153.646 94.917  1.00 29.83 ? 129 PHE A C     1 
ATOM   1075  O  O     . PHE A 1 129 ? 127.550 154.299 95.214  1.00 33.63 ? 129 PHE A O     1 
ATOM   1076  C  CB    . PHE A 1 129 ? 126.692 151.169 94.658  1.00 25.64 ? 129 PHE A CB    1 
ATOM   1077  C  CG    . PHE A 1 129 ? 126.905 149.859 95.351  1.00 24.72 ? 129 PHE A CG    1 
ATOM   1078  C  CD1   . PHE A 1 129 ? 127.048 149.798 96.724  1.00 27.43 ? 129 PHE A CD1   1 
ATOM   1079  C  CD2   . PHE A 1 129 ? 126.976 148.685 94.622  1.00 26.43 ? 129 PHE A CD2   1 
ATOM   1080  C  CE1   . PHE A 1 129 ? 127.245 148.591 97.357  1.00 24.66 ? 129 PHE A CE1   1 
ATOM   1081  C  CE2   . PHE A 1 129 ? 127.179 147.477 95.251  1.00 25.99 ? 129 PHE A CE2   1 
ATOM   1082  C  CZ    . PHE A 1 129 ? 127.312 147.430 96.620  1.00 27.44 ? 129 PHE A CZ    1 
ATOM   1083  N  N     . ALA A 1 130 ? 125.666 154.068 94.006  1.00 35.17 ? 130 ALA A N     1 
ATOM   1084  C  CA    . ALA A 1 130 ? 125.958 155.233 93.179  1.00 34.69 ? 130 ALA A CA    1 
ATOM   1085  C  C     . ALA A 1 130 ? 125.934 156.528 93.979  1.00 41.95 ? 130 ALA A C     1 
ATOM   1086  O  O     . ALA A 1 130 ? 126.660 157.471 93.643  1.00 46.83 ? 130 ALA A O     1 
ATOM   1087  C  CB    . ALA A 1 130 ? 124.972 155.309 92.020  1.00 34.39 ? 130 ALA A CB    1 
ATOM   1088  N  N     . ASN A 1 131 ? 125.105 156.597 95.022  1.00 42.75 ? 131 ASN A N     1 
ATOM   1089  C  CA    . ASN A 1 131 ? 125.042 157.757 95.913  1.00 44.01 ? 131 ASN A CA    1 
ATOM   1090  C  C     . ASN A 1 131 ? 124.688 159.033 95.148  1.00 43.25 ? 131 ASN A C     1 
ATOM   1091  O  O     . ASN A 1 131 ? 125.386 160.047 95.223  1.00 47.81 ? 131 ASN A O     1 
ATOM   1092  C  CB    . ASN A 1 131 ? 126.355 157.923 96.685  1.00 43.37 ? 131 ASN A CB    1 
ATOM   1093  C  CG    . ASN A 1 131 ? 126.202 158.791 97.916  1.00 48.23 ? 131 ASN A CG    1 
ATOM   1094  O  OD1   . ASN A 1 131 ? 125.242 158.652 98.674  1.00 45.45 ? 131 ASN A OD1   1 
ATOM   1095  N  ND2   . ASN A 1 131 ? 127.152 159.693 98.124  1.00 46.74 ? 131 ASN A ND2   1 
ATOM   1096  N  N     . GLY A 1 132 ? 123.586 158.976 94.402  1.00 41.70 ? 132 GLY A N     1 
ATOM   1097  C  CA    . GLY A 1 132 ? 123.053 160.123 93.704  1.00 42.53 ? 132 GLY A CA    1 
ATOM   1098  C  C     . GLY A 1 132 ? 123.321 160.155 92.213  1.00 45.52 ? 132 GLY A C     1 
ATOM   1099  O  O     . GLY A 1 132 ? 122.677 160.935 91.503  1.00 49.13 ? 132 GLY A O     1 
ATOM   1100  N  N     . ASP A 1 133 ? 124.242 159.333 91.718  1.00 47.90 ? 133 ASP A N     1 
ATOM   1101  C  CA    . ASP A 1 133 ? 124.596 159.327 90.304  1.00 46.09 ? 133 ASP A CA    1 
ATOM   1102  C  C     . ASP A 1 133 ? 123.698 158.346 89.557  1.00 50.21 ? 133 ASP A C     1 
ATOM   1103  O  O     . ASP A 1 133 ? 123.664 157.156 89.883  1.00 50.99 ? 133 ASP A O     1 
ATOM   1104  C  CB    . ASP A 1 133 ? 126.068 158.958 90.121  1.00 48.59 ? 133 ASP A CB    1 
ATOM   1105  C  CG    . ASP A 1 133 ? 126.645 159.483 88.821  1.00 53.76 ? 133 ASP A CG    1 
ATOM   1106  O  OD1   . ASP A 1 133 ? 125.871 159.697 87.864  1.00 52.67 ? 133 ASP A OD1   1 
ATOM   1107  O  OD2   . ASP A 1 133 ? 127.876 159.681 88.755  1.00 53.53 ? 133 ASP A OD2   1 
ATOM   1108  N  N     . THR A 1 134 ? 122.970 158.848 88.558  1.00 49.40 ? 134 THR A N     1 
ATOM   1109  C  CA    . THR A 1 134 ? 122.066 157.986 87.803  1.00 48.30 ? 134 THR A CA    1 
ATOM   1110  C  C     . THR A 1 134 ? 122.832 157.073 86.852  1.00 50.37 ? 134 THR A C     1 
ATOM   1111  O  O     . THR A 1 134 ? 122.537 155.874 86.759  1.00 52.18 ? 134 THR A O     1 
ATOM   1112  C  CB    . THR A 1 134 ? 121.061 158.839 87.033  1.00 53.34 ? 134 THR A CB    1 
ATOM   1113  O  OG1   . THR A 1 134 ? 120.220 159.530 87.963  1.00 54.72 ? 134 THR A OG1   1 
ATOM   1114  C  CG2   . THR A 1 134 ? 120.195 157.968 86.135  1.00 52.08 ? 134 THR A CG2   1 
ATOM   1115  N  N     . GLU A 1 135 ? 123.819 157.620 86.139  1.00 48.31 ? 135 GLU A N     1 
ATOM   1116  C  CA    . GLU A 1 135 ? 124.599 156.811 85.208  1.00 48.70 ? 135 GLU A CA    1 
ATOM   1117  C  C     . GLU A 1 135 ? 125.406 155.748 85.942  1.00 49.08 ? 135 GLU A C     1 
ATOM   1118  O  O     . GLU A 1 135 ? 125.512 154.609 85.475  1.00 51.59 ? 135 GLU A O     1 
ATOM   1119  C  CB    . GLU A 1 135 ? 125.516 157.707 84.378  1.00 49.97 ? 135 GLU A CB    1 
ATOM   1120  C  CG    . GLU A 1 135 ? 124.776 158.722 83.529  1.00 49.36 ? 135 GLU A CG    1 
ATOM   1121  C  CD    . GLU A 1 135 ? 123.670 158.094 82.707  1.00 54.66 ? 135 GLU A CD    1 
ATOM   1122  O  OE1   . GLU A 1 135 ? 123.970 157.196 81.892  1.00 55.15 ? 135 GLU A OE1   1 
ATOM   1123  O  OE2   . GLU A 1 135 ? 122.500 158.496 82.876  1.00 55.55 ? 135 GLU A OE2   1 
ATOM   1124  N  N     . LYS A 1 136 ? 125.984 156.104 87.090  1.00 40.46 ? 136 LYS A N     1 
ATOM   1125  C  CA    . LYS A 1 136 ? 126.706 155.119 87.887  1.00 40.66 ? 136 LYS A CA    1 
ATOM   1126  C  C     . LYS A 1 136 ? 125.764 154.044 88.413  1.00 41.65 ? 136 LYS A C     1 
ATOM   1127  O  O     . LYS A 1 136 ? 126.131 152.866 88.483  1.00 44.73 ? 136 LYS A O     1 
ATOM   1128  C  CB    . LYS A 1 136 ? 127.435 155.811 89.038  1.00 45.06 ? 136 LYS A CB    1 
ATOM   1129  C  CG    . LYS A 1 136 ? 128.582 155.010 89.622  1.00 42.70 ? 136 LYS A CG    1 
ATOM   1130  C  CD    . LYS A 1 136 ? 129.798 155.054 88.716  1.00 44.03 ? 136 LYS A CD    1 
ATOM   1131  C  CE    . LYS A 1 136 ? 131.070 154.747 89.484  1.00 46.39 ? 136 LYS A CE    1 
ATOM   1132  N  NZ    . LYS A 1 136 ? 132.280 154.949 88.642  1.00 48.18 ? 136 LYS A NZ    1 
ATOM   1133  N  N     . ALA A 1 137 ? 124.543 154.431 88.790  1.00 39.74 ? 137 ALA A N     1 
ATOM   1134  C  CA    . ALA A 1 137 ? 123.560 153.446 89.227  1.00 34.48 ? 137 ALA A CA    1 
ATOM   1135  C  C     . ALA A 1 137 ? 123.205 152.486 88.100  1.00 36.91 ? 137 ALA A C     1 
ATOM   1136  O  O     . ALA A 1 137 ? 123.071 151.278 88.322  1.00 40.21 ? 137 ALA A O     1 
ATOM   1137  C  CB    . ALA A 1 137 ? 122.308 154.148 89.752  1.00 36.01 ? 137 ALA A CB    1 
ATOM   1138  N  N     . LYS A 1 138 ? 123.053 153.006 86.879  1.00 41.09 ? 138 LYS A N     1 
ATOM   1139  C  CA    . LYS A 1 138 ? 122.794 152.138 85.735  1.00 41.12 ? 138 LYS A CA    1 
ATOM   1140  C  C     . LYS A 1 138 ? 123.978 151.219 85.457  1.00 41.16 ? 138 LYS A C     1 
ATOM   1141  O  O     . LYS A 1 138 ? 123.793 150.051 85.096  1.00 43.14 ? 138 LYS A O     1 
ATOM   1142  C  CB    . LYS A 1 138 ? 122.461 152.977 84.502  1.00 45.55 ? 138 LYS A CB    1 
ATOM   1143  C  CG    . LYS A 1 138 ? 121.051 153.542 84.501  1.00 44.20 ? 138 LYS A CG    1 
ATOM   1144  C  CD    . LYS A 1 138 ? 120.965 154.803 83.662  1.00 44.20 ? 138 LYS A CD    1 
ATOM   1145  C  CE    . LYS A 1 138 ? 120.706 154.474 82.202  1.00 46.85 ? 138 LYS A CE    1 
ATOM   1146  N  NZ    . LYS A 1 138 ? 120.745 155.690 81.346  1.00 48.35 ? 138 LYS A NZ    1 
ATOM   1147  N  N     . GLU A 1 139 ? 125.201 151.731 85.611  1.00 40.15 ? 139 GLU A N     1 
ATOM   1148  C  CA    . GLU A 1 139 ? 126.384 150.893 85.434  1.00 36.95 ? 139 GLU A CA    1 
ATOM   1149  C  C     . GLU A 1 139 ? 126.423 149.766 86.460  1.00 35.71 ? 139 GLU A C     1 
ATOM   1150  O  O     . GLU A 1 139 ? 126.739 148.620 86.124  1.00 40.74 ? 139 GLU A O     1 
ATOM   1151  C  CB    . GLU A 1 139 ? 127.648 151.748 85.528  1.00 38.12 ? 139 GLU A CB    1 
ATOM   1152  C  CG    . GLU A 1 139 ? 128.031 152.441 84.234  1.00 41.43 ? 139 GLU A CG    1 
ATOM   1153  C  CD    . GLU A 1 139 ? 129.166 153.429 84.416  1.00 48.66 ? 139 GLU A CD    1 
ATOM   1154  O  OE1   . GLU A 1 139 ? 129.228 154.076 85.482  1.00 45.91 ? 139 GLU A OE1   1 
ATOM   1155  O  OE2   . GLU A 1 139 ? 129.997 153.562 83.493  1.00 48.54 ? 139 GLU A OE2   1 
ATOM   1156  N  N     . TYR A 1 140 ? 126.107 150.075 87.719  1.00 33.04 ? 140 TYR A N     1 
ATOM   1157  C  CA    . TYR A 1 140 ? 126.057 149.042 88.751  1.00 29.82 ? 140 TYR A CA    1 
ATOM   1158  C  C     . TYR A 1 140 ? 124.957 148.029 88.463  1.00 33.60 ? 140 TYR A C     1 
ATOM   1159  O  O     . TYR A 1 140 ? 125.129 146.826 88.699  1.00 34.25 ? 140 TYR A O     1 
ATOM   1160  C  CB    . TYR A 1 140 ? 125.839 149.676 90.122  1.00 32.17 ? 140 TYR A CB    1 
ATOM   1161  C  CG    . TYR A 1 140 ? 127.061 150.317 90.730  1.00 32.33 ? 140 TYR A CG    1 
ATOM   1162  C  CD1   . TYR A 1 140 ? 128.223 149.589 90.938  1.00 34.78 ? 140 TYR A CD1   1 
ATOM   1163  C  CD2   . TYR A 1 140 ? 127.042 151.647 91.117  1.00 33.12 ? 140 TYR A CD2   1 
ATOM   1164  C  CE1   . TYR A 1 140 ? 129.336 150.177 91.502  1.00 34.25 ? 140 TYR A CE1   1 
ATOM   1165  C  CE2   . TYR A 1 140 ? 128.147 152.241 91.677  1.00 35.59 ? 140 TYR A CE2   1 
ATOM   1166  C  CZ    . TYR A 1 140 ? 129.290 151.505 91.869  1.00 30.72 ? 140 TYR A CZ    1 
ATOM   1167  O  OH    . TYR A 1 140 ? 130.388 152.105 92.433  1.00 34.29 ? 140 TYR A OH    1 
ATOM   1168  N  N     . VAL A 1 141 ? 123.808 148.502 87.973  1.00 34.56 ? 141 VAL A N     1 
ATOM   1169  C  CA    . VAL A 1 141 ? 122.724 147.600 87.599  1.00 33.82 ? 141 VAL A CA    1 
ATOM   1170  C  C     . VAL A 1 141 ? 123.178 146.651 86.502  1.00 35.36 ? 141 VAL A C     1 
ATOM   1171  O  O     . VAL A 1 141 ? 122.923 145.445 86.562  1.00 39.01 ? 141 VAL A O     1 
ATOM   1172  C  CB    . VAL A 1 141 ? 121.483 148.402 87.171  1.00 35.90 ? 141 VAL A CB    1 
ATOM   1173  C  CG1   . VAL A 1 141 ? 120.583 147.549 86.312  1.00 36.13 ? 141 VAL A CG1   1 
ATOM   1174  C  CG2   . VAL A 1 141 ? 120.724 148.875 88.382  1.00 35.60 ? 141 VAL A CG2   1 
ATOM   1175  N  N     . ASN A 1 142 ? 123.855 147.179 85.483  1.00 36.31 ? 142 ASN A N     1 
ATOM   1176  C  CA    . ASN A 1 142 ? 124.363 146.323 84.417  1.00 32.35 ? 142 ASN A CA    1 
ATOM   1177  C  C     . ASN A 1 142 ? 125.387 145.332 84.953  1.00 34.33 ? 142 ASN A C     1 
ATOM   1178  O  O     . ASN A 1 142 ? 125.413 144.168 84.541  1.00 40.02 ? 142 ASN A O     1 
ATOM   1179  C  CB    . ASN A 1 142 ? 124.970 147.175 83.305  1.00 32.70 ? 142 ASN A CB    1 
ATOM   1180  C  CG    . ASN A 1 142 ? 123.924 147.742 82.375  1.00 38.39 ? 142 ASN A CG    1 
ATOM   1181  O  OD1   . ASN A 1 142 ? 123.030 147.029 81.921  1.00 37.15 ? 142 ASN A OD1   1 
ATOM   1182  N  ND2   . ASN A 1 142 ? 124.027 149.033 82.085  1.00 37.49 ? 142 ASN A ND2   1 
ATOM   1183  N  N     . LEU A 1 143 ? 126.242 145.780 85.873  1.00 34.53 ? 143 LEU A N     1 
ATOM   1184  C  CA    . LEU A 1 143 ? 127.274 144.909 86.423  1.00 28.49 ? 143 LEU A CA    1 
ATOM   1185  C  C     . LEU A 1 143 ? 126.674 143.754 87.216  1.00 29.89 ? 143 LEU A C     1 
ATOM   1186  O  O     . LEU A 1 143 ? 127.142 142.615 87.116  1.00 29.53 ? 143 LEU A O     1 
ATOM   1187  C  CB    . LEU A 1 143 ? 128.220 145.725 87.300  1.00 28.43 ? 143 LEU A CB    1 
ATOM   1188  C  CG    . LEU A 1 143 ? 129.638 145.191 87.469  1.00 33.16 ? 143 LEU A CG    1 
ATOM   1189  C  CD1   . LEU A 1 143 ? 130.427 145.415 86.197  1.00 34.14 ? 143 LEU A CD1   1 
ATOM   1190  C  CD2   . LEU A 1 143 ? 130.305 145.875 88.642  1.00 30.09 ? 143 LEU A CD2   1 
ATOM   1191  N  N     . MET A 1 144 ? 125.641 144.026 88.015  1.00 33.30 ? 144 MET A N     1 
ATOM   1192  C  CA    . MET A 1 144 ? 125.097 142.980 88.876  1.00 27.10 ? 144 MET A CA    1 
ATOM   1193  C  C     . MET A 1 144 ? 124.061 142.117 88.160  1.00 28.23 ? 144 MET A C     1 
ATOM   1194  O  O     . MET A 1 144 ? 123.960 140.918 88.437  1.00 32.60 ? 144 MET A O     1 
ATOM   1195  C  CB    . MET A 1 144 ? 124.501 143.589 90.143  1.00 28.34 ? 144 MET A CB    1 
ATOM   1196  C  CG    . MET A 1 144 ? 125.510 144.328 91.003  1.00 29.97 ? 144 MET A CG    1 
ATOM   1197  S  SD    . MET A 1 144 ? 124.812 144.871 92.570  1.00 43.83 ? 144 MET A SD    1 
ATOM   1198  C  CE    . MET A 1 144 ? 124.102 146.440 92.094  1.00 33.08 ? 144 MET A CE    1 
ATOM   1199  N  N     . ILE A 1 145 ? 123.271 142.702 87.256  1.00 28.92 ? 145 ILE A N     1 
ATOM   1200  C  CA    . ILE A 1 145 ? 122.285 141.915 86.522  1.00 31.04 ? 145 ILE A CA    1 
ATOM   1201  C  C     . ILE A 1 145 ? 122.970 140.994 85.520  1.00 34.11 ? 145 ILE A C     1 
ATOM   1202  O  O     . ILE A 1 145 ? 122.479 139.894 85.242  1.00 38.15 ? 145 ILE A O     1 
ATOM   1203  C  CB    . ILE A 1 145 ? 121.240 142.833 85.854  1.00 31.15 ? 145 ILE A CB    1 
ATOM   1204  C  CG1   . ILE A 1 145 ? 119.907 142.099 85.702  1.00 29.94 ? 145 ILE A CG1   1 
ATOM   1205  C  CG2   . ILE A 1 145 ? 121.716 143.341 84.499  1.00 31.42 ? 145 ILE A CG2   1 
ATOM   1206  C  CD1   . ILE A 1 145 ? 119.228 141.777 87.012  1.00 28.60 ? 145 ILE A CD1   1 
ATOM   1207  N  N     . ASN A 1 146 ? 124.108 141.416 84.962  1.00 28.37 ? 146 ASN A N     1 
ATOM   1208  C  CA    . ASN A 1 146 ? 124.948 140.501 84.205  1.00 28.04 ? 146 ASN A CA    1 
ATOM   1209  C  C     . ASN A 1 146 ? 125.682 139.528 85.111  1.00 29.80 ? 146 ASN A C     1 
ATOM   1210  O  O     . ASN A 1 146 ? 126.319 138.597 84.609  1.00 36.17 ? 146 ASN A O     1 
ATOM   1211  C  CB    . ASN A 1 146 ? 125.957 141.275 83.357  1.00 30.57 ? 146 ASN A CB    1 
ATOM   1212  C  CG    . ASN A 1 146 ? 125.293 142.133 82.301  1.00 33.10 ? 146 ASN A CG    1 
ATOM   1213  O  OD1   . ASN A 1 146 ? 124.125 141.939 81.971  1.00 34.72 ? 146 ASN A OD1   1 
ATOM   1214  N  ND2   . ASN A 1 146 ? 126.038 143.091 81.765  1.00 34.45 ? 146 ASN A ND2   1 
ATOM   1215  N  N     . GLN A 1 147 ? 125.606 139.736 86.427  1.00 28.51 ? 147 GLN A N     1 
ATOM   1216  C  CA    . GLN A 1 147 ? 126.256 138.889 87.422  1.00 24.20 ? 147 GLN A CA    1 
ATOM   1217  C  C     . GLN A 1 147 ? 127.765 138.845 87.220  1.00 27.45 ? 147 GLN A C     1 
ATOM   1218  O  O     . GLN A 1 147 ? 128.402 137.823 87.462  1.00 34.41 ? 147 GLN A O     1 
ATOM   1219  C  CB    . GLN A 1 147 ? 125.660 137.479 87.424  1.00 24.35 ? 147 GLN A CB    1 
ATOM   1220  C  CG    . GLN A 1 147 ? 124.216 137.439 87.895  1.00 23.59 ? 147 GLN A CG    1 
ATOM   1221  C  CD    . GLN A 1 147 ? 123.765 136.052 88.291  1.00 26.90 ? 147 GLN A CD    1 
ATOM   1222  O  OE1   . GLN A 1 147 ? 123.101 135.871 89.310  1.00 30.64 ? 147 GLN A OE1   1 
ATOM   1223  N  NE2   . GLN A 1 147 ? 124.118 135.063 87.482  1.00 35.27 ? 147 GLN A NE2   1 
ATOM   1224  N  N     . GLU A 1 148 ? 128.342 139.957 86.760  1.00 26.79 ? 148 GLU A N     1 
ATOM   1225  C  CA    . GLU A 1 148 ? 129.792 140.074 86.678  1.00 23.96 ? 148 GLU A CA    1 
ATOM   1226  C  C     . GLU A 1 148 ? 130.413 140.345 88.041  1.00 25.94 ? 148 GLU A C     1 
ATOM   1227  O  O     . GLU A 1 148 ? 131.526 139.886 88.314  1.00 29.13 ? 148 GLU A O     1 
ATOM   1228  C  CB    . GLU A 1 148 ? 130.173 141.184 85.699  1.00 22.49 ? 148 GLU A CB    1 
ATOM   1229  C  CG    . GLU A 1 148 ? 129.656 140.965 84.293  1.00 26.48 ? 148 GLU A CG    1 
ATOM   1230  C  CD    . GLU A 1 148 ? 129.817 142.189 83.418  1.00 33.32 ? 148 GLU A CD    1 
ATOM   1231  O  OE1   . GLU A 1 148 ? 128.896 143.031 83.394  1.00 34.40 ? 148 GLU A OE1   1 
ATOM   1232  O  OE2   . GLU A 1 148 ? 130.868 142.311 82.755  1.00 37.40 ? 148 GLU A OE2   1 
ATOM   1233  N  N     . TYR A 1 149 ? 129.716 141.084 88.898  1.00 25.20 ? 149 TYR A N     1 
ATOM   1234  C  CA    . TYR A 1 149 ? 130.173 141.375 90.247  1.00 19.77 ? 149 TYR A CA    1 
ATOM   1235  C  C     . TYR A 1 149 ? 129.045 141.096 91.225  1.00 23.13 ? 149 TYR A C     1 
ATOM   1236  O  O     . TYR A 1 149 ? 127.882 141.406 90.951  1.00 28.24 ? 149 TYR A O     1 
ATOM   1237  C  CB    . TYR A 1 149 ? 130.636 142.828 90.376  1.00 19.90 ? 149 TYR A CB    1 
ATOM   1238  C  CG    . TYR A 1 149 ? 130.831 143.294 91.800  1.00 25.28 ? 149 TYR A CG    1 
ATOM   1239  C  CD1   . TYR A 1 149 ? 131.824 142.749 92.600  1.00 16.80 ? 149 TYR A CD1   1 
ATOM   1240  C  CD2   . TYR A 1 149 ? 130.020 144.280 92.343  1.00 23.25 ? 149 TYR A CD2   1 
ATOM   1241  C  CE1   . TYR A 1 149 ? 132.006 143.175 93.899  1.00 16.91 ? 149 TYR A CE1   1 
ATOM   1242  C  CE2   . TYR A 1 149 ? 130.193 144.709 93.640  1.00 22.73 ? 149 TYR A CE2   1 
ATOM   1243  C  CZ    . TYR A 1 149 ? 131.188 144.154 94.414  1.00 19.41 ? 149 TYR A CZ    1 
ATOM   1244  O  OH    . TYR A 1 149 ? 131.363 144.579 95.709  1.00 21.65 ? 149 TYR A OH    1 
ATOM   1245  N  N     . GLN A 1 150 ? 129.391 140.505 92.360  1.00 18.66 ? 150 GLN A N     1 
ATOM   1246  C  CA    . GLN A 1 150 ? 128.418 140.194 93.404  1.00 14.02 ? 150 GLN A CA    1 
ATOM   1247  C  C     . GLN A 1 150 ? 128.865 140.805 94.722  1.00 16.16 ? 150 GLN A C     1 
ATOM   1248  O  O     . GLN A 1 150 ? 129.899 140.387 95.276  1.00 23.68 ? 150 GLN A O     1 
ATOM   1249  C  CB    . GLN A 1 150 ? 128.248 138.683 93.547  1.00 20.17 ? 150 GLN A CB    1 
ATOM   1250  C  CG    . GLN A 1 150 ? 127.482 138.241 94.780  1.00 21.57 ? 150 GLN A CG    1 
ATOM   1251  C  CD    . GLN A 1 150 ? 126.055 138.745 94.798  1.00 17.44 ? 150 GLN A CD    1 
ATOM   1252  O  OE1   . GLN A 1 150 ? 125.232 138.343 93.979  1.00 29.68 ? 150 GLN A OE1   1 
ATOM   1253  N  NE2   . GLN A 1 150 ? 125.753 139.627 95.740  1.00 14.53 ? 150 GLN A NE2   1 
ATOM   1254  N  N     . PRO A 1 151 ? 128.145 141.791 95.255  1.00 25.02 ? 151 PRO A N     1 
ATOM   1255  C  CA    . PRO A 1 151 ? 128.452 142.278 96.602  1.00 16.34 ? 151 PRO A CA    1 
ATOM   1256  C  C     . PRO A 1 151 ? 128.266 141.174 97.631  1.00 18.34 ? 151 PRO A C     1 
ATOM   1257  O  O     . PRO A 1 151 ? 127.466 140.254 97.451  1.00 25.89 ? 151 PRO A O     1 
ATOM   1258  C  CB    . PRO A 1 151 ? 127.446 143.415 96.810  1.00 15.82 ? 151 PRO A CB    1 
ATOM   1259  C  CG    . PRO A 1 151 ? 127.028 143.814 95.434  1.00 20.61 ? 151 PRO A CG    1 
ATOM   1260  C  CD    . PRO A 1 151 ? 127.072 142.567 94.614  1.00 23.71 ? 151 PRO A CD    1 
ATOM   1261  N  N     . SER A 1 152 ? 129.032 141.267 98.714  1.00 20.64 ? 152 SER A N     1 
ATOM   1262  C  CA    . SER A 1 152 ? 129.000 140.242 99.745  1.00 17.08 ? 152 SER A CA    1 
ATOM   1263  C  C     . SER A 1 152 ? 127.604 140.120 100.349 1.00 23.98 ? 152 SER A C     1 
ATOM   1264  O  O     . SER A 1 152 ? 126.737 140.978 100.166 1.00 27.76 ? 152 SER A O     1 
ATOM   1265  C  CB    . SER A 1 152 ? 130.016 140.555 100.840 1.00 26.47 ? 152 SER A CB    1 
ATOM   1266  O  OG    . SER A 1 152 ? 129.620 141.687 101.593 1.00 29.58 ? 152 SER A OG    1 
ATOM   1267  N  N     . THR A 1 153 ? 127.394 139.022 101.074 1.00 29.74 ? 153 THR A N     1 
ATOM   1268  C  CA    . THR A 1 153 ? 126.110 138.773 101.727 1.00 24.10 ? 153 THR A CA    1 
ATOM   1269  C  C     . THR A 1 153 ? 125.648 139.926 102.611 1.00 30.17 ? 153 THR A C     1 
ATOM   1270  O  O     . THR A 1 153 ? 124.473 140.310 102.509 1.00 27.01 ? 153 THR A O     1 
ATOM   1271  C  CB    . THR A 1 153 ? 126.191 137.459 102.518 1.00 23.27 ? 153 THR A CB    1 
ATOM   1272  O  OG1   . THR A 1 153 ? 126.227 136.354 101.608 1.00 35.36 ? 153 THR A OG1   1 
ATOM   1273  C  CG2   . THR A 1 153 ? 124.995 137.306 103.444 1.00 24.80 ? 153 THR A CG2   1 
ATOM   1274  N  N     . PRO A 1 154 ? 126.484 140.527 103.469 1.00 30.21 ? 154 PRO A N     1 
ATOM   1275  C  CA    . PRO A 1 154 ? 125.997 141.689 104.238 1.00 21.67 ? 154 PRO A CA    1 
ATOM   1276  C  C     . PRO A 1 154 ? 125.574 142.853 103.360 1.00 23.74 ? 154 PRO A C     1 
ATOM   1277  O  O     . PRO A 1 154 ? 124.486 143.410 103.553 1.00 30.80 ? 154 PRO A O     1 
ATOM   1278  C  CB    . PRO A 1 154 ? 127.198 142.046 105.124 1.00 23.53 ? 154 PRO A CB    1 
ATOM   1279  C  CG    . PRO A 1 154 ? 127.999 140.813 105.192 1.00 21.87 ? 154 PRO A CG    1 
ATOM   1280  C  CD    . PRO A 1 154 ? 127.852 140.156 103.870 1.00 23.36 ? 154 PRO A CD    1 
ATOM   1281  N  N     . THR A 1 155 ? 126.408 143.235 102.391 1.00 22.72 ? 155 THR A N     1 
ATOM   1282  C  CA    . THR A 1 155 ? 126.076 144.365 101.531 1.00 23.39 ? 155 THR A CA    1 
ATOM   1283  C  C     . THR A 1 155 ? 124.863 144.061 100.663 1.00 25.73 ? 155 THR A C     1 
ATOM   1284  O  O     . THR A 1 155 ? 123.916 144.850 100.607 1.00 25.46 ? 155 THR A O     1 
ATOM   1285  C  CB    . THR A 1 155 ? 127.278 144.735 100.663 1.00 21.85 ? 155 THR A CB    1 
ATOM   1286  O  OG1   . THR A 1 155 ? 128.403 145.025 101.501 1.00 26.98 ? 155 THR A OG1   1 
ATOM   1287  C  CG2   . THR A 1 155 ? 126.965 145.950 99.814  1.00 16.77 ? 155 THR A CG2   1 
ATOM   1288  N  N     . PHE A 1 156 ? 124.869 142.911 99.985  1.00 27.99 ? 156 PHE A N     1 
ATOM   1289  C  CA    . PHE A 1 156 ? 123.757 142.567 99.103  1.00 25.75 ? 156 PHE A CA    1 
ATOM   1290  C  C     . PHE A 1 156 ? 122.457 142.415 99.883  1.00 28.61 ? 156 PHE A C     1 
ATOM   1291  O  O     . PHE A 1 156 ? 121.377 142.727 99.370  1.00 29.80 ? 156 PHE A O     1 
ATOM   1292  C  CB    . PHE A 1 156 ? 124.077 141.284 98.338  1.00 26.27 ? 156 PHE A CB    1 
ATOM   1293  C  CG    . PHE A 1 156 ? 123.207 141.061 97.137  1.00 28.30 ? 156 PHE A CG    1 
ATOM   1294  C  CD1   . PHE A 1 156 ? 123.134 142.011 96.133  1.00 25.21 ? 156 PHE A CD1   1 
ATOM   1295  C  CD2   . PHE A 1 156 ? 122.467 139.899 97.008  1.00 26.21 ? 156 PHE A CD2   1 
ATOM   1296  C  CE1   . PHE A 1 156 ? 122.336 141.807 95.026  1.00 29.10 ? 156 PHE A CE1   1 
ATOM   1297  C  CE2   . PHE A 1 156 ? 121.668 139.691 95.904  1.00 25.35 ? 156 PHE A CE2   1 
ATOM   1298  C  CZ    . PHE A 1 156 ? 121.603 140.646 94.912  1.00 30.61 ? 156 PHE A CZ    1 
ATOM   1299  N  N     . LEU A 1 157 ? 122.542 141.936 101.123 1.00 32.58 ? 157 LEU A N     1 
ATOM   1300  C  CA    . LEU A 1 157 ? 121.352 141.716 101.933 1.00 29.43 ? 157 LEU A CA    1 
ATOM   1301  C  C     . LEU A 1 157 ? 120.822 142.999 102.560 1.00 30.13 ? 157 LEU A C     1 
ATOM   1302  O  O     . LEU A 1 157 ? 119.607 143.143 102.720 1.00 38.33 ? 157 LEU A O     1 
ATOM   1303  C  CB    . LEU A 1 157 ? 121.655 140.685 103.023 1.00 31.95 ? 157 LEU A CB    1 
ATOM   1304  C  CG    . LEU A 1 157 ? 120.547 140.356 104.024 1.00 30.78 ? 157 LEU A CG    1 
ATOM   1305  C  CD1   . LEU A 1 157 ? 119.342 139.774 103.315 1.00 30.57 ? 157 LEU A CD1   1 
ATOM   1306  C  CD2   . LEU A 1 157 ? 121.057 139.400 105.088 1.00 28.78 ? 157 LEU A CD2   1 
ATOM   1307  N  N     . ASN A 1 158 ? 121.696 143.939 102.913 1.00 32.24 ? 158 ASN A N     1 
ATOM   1308  C  CA    . ASN A 1 158 ? 121.301 145.077 103.730 1.00 26.06 ? 158 ASN A CA    1 
ATOM   1309  C  C     . ASN A 1 158 ? 121.393 146.419 103.016 1.00 30.83 ? 158 ASN A C     1 
ATOM   1310  O  O     . ASN A 1 158 ? 121.003 147.434 103.600 1.00 38.29 ? 158 ASN A O     1 
ATOM   1311  C  CB    . ASN A 1 158 ? 122.150 145.118 105.005 1.00 29.10 ? 158 ASN A CB    1 
ATOM   1312  C  CG    . ASN A 1 158 ? 122.106 143.814 105.774 1.00 35.91 ? 158 ASN A CG    1 
ATOM   1313  O  OD1   . ASN A 1 158 ? 121.060 143.174 105.875 1.00 37.93 ? 158 ASN A OD1   1 
ATOM   1314  N  ND2   . ASN A 1 158 ? 123.246 143.410 106.318 1.00 32.92 ? 158 ASN A ND2   1 
ATOM   1315  N  N     . ALA A 1 159 ? 121.890 146.464 101.781 1.00 33.23 ? 159 ALA A N     1 
ATOM   1316  C  CA    . ALA A 1 159 ? 122.035 147.740 101.089 1.00 29.54 ? 159 ALA A CA    1 
ATOM   1317  C  C     . ALA A 1 159 ? 120.682 148.403 100.862 1.00 35.78 ? 159 ALA A C     1 
ATOM   1318  O  O     . ALA A 1 159 ? 119.853 147.895 100.101 1.00 41.95 ? 159 ALA A O     1 
ATOM   1319  C  CB    . ALA A 1 159 ? 122.756 147.559 99.753  1.00 34.01 ? 159 ALA A CB    1 
ATOM   1320  N  N     . GLY A 1 160 ? 120.455 149.536 101.518 1.00 42.57 ? 160 GLY A N     1 
ATOM   1321  C  CA    . GLY A 1 160 ? 119.228 150.283 101.353 1.00 40.62 ? 160 GLY A CA    1 
ATOM   1322  C  C     . GLY A 1 160 ? 118.080 149.873 102.246 1.00 43.84 ? 160 GLY A C     1 
ATOM   1323  O  O     . GLY A 1 160 ? 116.968 150.380 102.061 1.00 44.79 ? 160 GLY A O     1 
ATOM   1324  N  N     . ARG A 1 161 ? 118.303 148.976 103.200 1.00 44.43 ? 161 ARG A N     1 
ATOM   1325  C  CA    . ARG A 1 161 ? 117.265 148.538 104.121 1.00 44.17 ? 161 ARG A CA    1 
ATOM   1326  C  C     . ARG A 1 161 ? 117.376 149.301 105.434 1.00 45.79 ? 161 ARG A C     1 
ATOM   1327  O  O     . ARG A 1 161 ? 118.479 149.575 105.913 1.00 48.35 ? 161 ARG A O     1 
ATOM   1328  C  CB    . ARG A 1 161 ? 117.360 147.033 104.377 1.00 41.70 ? 161 ARG A CB    1 
ATOM   1329  C  CG    . ARG A 1 161 ? 117.102 146.190 103.143 1.00 41.97 ? 161 ARG A CG    1 
ATOM   1330  C  CD    . ARG A 1 161 ? 116.848 144.739 103.499 1.00 41.50 ? 161 ARG A CD    1 
ATOM   1331  N  NE    . ARG A 1 161 ? 116.857 143.887 102.316 1.00 44.85 ? 161 ARG A NE    1 
ATOM   1332  C  CZ    . ARG A 1 161 ? 116.711 142.569 102.337 1.00 44.97 ? 161 ARG A CZ    1 
ATOM   1333  N  NH1   . ARG A 1 161 ? 116.536 141.911 103.471 1.00 43.85 ? 161 ARG A NH1   1 
ATOM   1334  N  NH2   . ARG A 1 161 ? 116.747 141.895 101.192 1.00 43.18 ? 161 ARG A NH2   1 
ATOM   1335  N  N     . LYS A 1 162 ? 116.222 149.650 106.008 1.00 54.32 ? 162 LYS A N     1 
ATOM   1336  C  CA    . LYS A 1 162 ? 116.215 150.430 107.242 1.00 53.52 ? 162 LYS A CA    1 
ATOM   1337  C  C     . LYS A 1 162 ? 116.666 149.589 108.430 1.00 55.37 ? 162 LYS A C     1 
ATOM   1338  O  O     . LYS A 1 162 ? 117.684 149.888 109.065 1.00 56.15 ? 162 LYS A O     1 
ATOM   1339  C  CB    . LYS A 1 162 ? 114.820 151.003 107.490 1.00 53.38 ? 162 LYS A CB    1 
ATOM   1340  C  CG    . LYS A 1 162 ? 114.818 152.366 108.157 1.00 55.79 ? 162 LYS A CG    1 
ATOM   1341  C  CD    . LYS A 1 162 ? 113.503 153.093 107.925 1.00 56.08 ? 162 LYS A CD    1 
ATOM   1342  C  CE    . LYS A 1 162 ? 113.691 154.600 107.962 1.00 55.43 ? 162 LYS A CE    1 
ATOM   1343  N  NZ    . LYS A 1 162 ? 114.867 154.992 108.786 1.00 56.51 ? 162 LYS A NZ    1 
ATOM   1344  N  N     . ARG A 1 163 ? 115.922 148.532 108.743 1.00 58.17 ? 163 ARG A N     1 
ATOM   1345  C  CA    . ARG A 1 163 ? 116.252 147.654 109.863 1.00 58.27 ? 163 ARG A CA    1 
ATOM   1346  C  C     . ARG A 1 163 ? 117.248 146.596 109.394 1.00 59.31 ? 163 ARG A C     1 
ATOM   1347  O  O     . ARG A 1 163 ? 116.910 145.449 109.096 1.00 58.44 ? 163 ARG A O     1 
ATOM   1348  C  CB    . ARG A 1 163 ? 114.984 147.033 110.439 1.00 60.96 ? 163 ARG A CB    1 
ATOM   1349  C  CG    . ARG A 1 163 ? 114.021 148.053 111.025 1.00 58.76 ? 163 ARG A CG    1 
ATOM   1350  C  CD    . ARG A 1 163 ? 112.661 147.439 111.298 1.00 58.77 ? 163 ARG A CD    1 
ATOM   1351  N  NE    . ARG A 1 163 ? 111.996 147.034 110.066 1.00 61.36 ? 163 ARG A NE    1 
ATOM   1352  C  CZ    . ARG A 1 163 ? 110.882 146.316 110.018 1.00 63.31 ? 163 ARG A CZ    1 
ATOM   1353  N  NH1   . ARG A 1 163 ? 110.270 145.915 111.121 1.00 62.22 ? 163 ARG A NH1   1 
ATOM   1354  N  NH2   . ARG A 1 163 ? 110.369 145.994 108.834 1.00 60.06 ? 163 ARG A NH2   1 
ATOM   1355  N  N     . ARG A 1 164 ? 118.505 147.020 109.334 1.00 53.99 ? 164 ARG A N     1 
ATOM   1356  C  CA    . ARG A 1 164 ? 119.580 146.240 108.746 1.00 51.53 ? 164 ARG A CA    1 
ATOM   1357  C  C     . ARG A 1 164 ? 120.760 146.153 109.703 1.00 51.81 ? 164 ARG A C     1 
ATOM   1358  O  O     . ARG A 1 164 ? 120.917 146.973 110.612 1.00 53.25 ? 164 ARG A O     1 
ATOM   1359  C  CB    . ARG A 1 164 ? 120.047 146.860 107.425 1.00 50.76 ? 164 ARG A CB    1 
ATOM   1360  C  CG    . ARG A 1 164 ? 120.818 148.161 107.610 1.00 47.11 ? 164 ARG A CG    1 
ATOM   1361  C  CD    . ARG A 1 164 ? 121.729 148.438 106.432 1.00 49.56 ? 164 ARG A CD    1 
ATOM   1362  N  NE    . ARG A 1 164 ? 122.534 149.639 106.614 1.00 51.45 ? 164 ARG A NE    1 
ATOM   1363  C  CZ    . ARG A 1 164 ? 122.776 150.528 105.660 1.00 53.05 ? 164 ARG A CZ    1 
ATOM   1364  N  NH1   . ARG A 1 164 ? 122.274 150.388 104.443 1.00 48.42 ? 164 ARG A NH1   1 
ATOM   1365  N  NH2   . ARG A 1 164 ? 123.539 151.582 105.932 1.00 50.88 ? 164 ARG A NH2   1 
ATOM   1366  N  N     . GLY A 1 165 ? 121.589 145.137 109.486 1.00 45.89 ? 165 GLY A N     1 
ATOM   1367  C  CA    . GLY A 1 165 ? 122.886 145.064 110.117 1.00 43.78 ? 165 GLY A CA    1 
ATOM   1368  C  C     . GLY A 1 165 ? 123.910 145.867 109.339 1.00 48.64 ? 165 GLY A C     1 
ATOM   1369  O  O     . GLY A 1 165 ? 123.592 146.618 108.415 1.00 45.89 ? 165 GLY A O     1 
ATOM   1370  N  N     . GLU A 1 166 ? 125.168 145.701 109.726 1.00 46.79 ? 166 GLU A N     1 
ATOM   1371  C  CA    . GLU A 1 166 ? 126.235 146.394 109.026 1.00 40.56 ? 166 GLU A CA    1 
ATOM   1372  C  C     . GLU A 1 166 ? 126.533 145.714 107.693 1.00 38.71 ? 166 GLU A C     1 
ATOM   1373  O  O     . GLU A 1 166 ? 126.239 144.535 107.485 1.00 39.47 ? 166 GLU A O     1 
ATOM   1374  C  CB    . GLU A 1 166 ? 127.499 146.449 109.883 1.00 38.89 ? 166 GLU A CB    1 
ATOM   1375  C  CG    . GLU A 1 166 ? 127.442 147.477 111.001 1.00 42.79 ? 166 GLU A CG    1 
ATOM   1376  C  CD    . GLU A 1 166 ? 127.243 148.894 110.493 1.00 48.14 ? 166 GLU A CD    1 
ATOM   1377  O  OE1   . GLU A 1 166 ? 127.691 149.199 109.367 1.00 46.30 ? 166 GLU A OE1   1 
ATOM   1378  O  OE2   . GLU A 1 166 ? 126.636 149.705 111.223 1.00 45.81 ? 166 GLU A OE2   1 
ATOM   1379  N  N     . LEU A 1 167 ? 127.121 146.485 106.779 1.00 32.89 ? 167 LEU A N     1 
ATOM   1380  C  CA    . LEU A 1 167 ? 127.533 145.954 105.488 1.00 25.95 ? 167 LEU A CA    1 
ATOM   1381  C  C     . LEU A 1 167 ? 128.861 145.215 105.555 1.00 30.06 ? 167 LEU A C     1 
ATOM   1382  O  O     . LEU A 1 167 ? 129.254 144.588 104.567 1.00 32.57 ? 167 LEU A O     1 
ATOM   1383  C  CB    . LEU A 1 167 ? 127.625 147.081 104.458 1.00 28.05 ? 167 LEU A CB    1 
ATOM   1384  C  CG    . LEU A 1 167 ? 126.348 147.862 104.140 1.00 27.55 ? 167 LEU A CG    1 
ATOM   1385  C  CD1   . LEU A 1 167 ? 126.465 148.513 102.779 1.00 31.36 ? 167 LEU A CD1   1 
ATOM   1386  C  CD2   . LEU A 1 167 ? 125.130 146.963 104.187 1.00 27.58 ? 167 LEU A CD2   1 
ATOM   1387  N  N     . VAL A 1 168 ? 129.554 145.277 106.687 1.00 32.68 ? 168 VAL A N     1 
ATOM   1388  C  CA    . VAL A 1 168 ? 130.799 144.555 106.908 1.00 26.48 ? 168 VAL A CA    1 
ATOM   1389  C  C     . VAL A 1 168 ? 130.544 143.483 107.956 1.00 30.89 ? 168 VAL A C     1 
ATOM   1390  O  O     . VAL A 1 168 ? 129.903 143.745 108.980 1.00 37.58 ? 168 VAL A O     1 
ATOM   1391  C  CB    . VAL A 1 168 ? 131.928 145.505 107.354 1.00 26.63 ? 168 VAL A CB    1 
ATOM   1392  C  CG1   . VAL A 1 168 ? 133.228 144.741 107.531 1.00 29.01 ? 168 VAL A CG1   1 
ATOM   1393  C  CG2   . VAL A 1 168 ? 132.100 146.630 106.350 1.00 30.64 ? 168 VAL A CG2   1 
ATOM   1394  N  N     . SER A 1 169 ? 131.038 142.274 107.699 1.00 29.20 ? 169 SER A N     1 
ATOM   1395  C  CA    . SER A 1 169 ? 130.845 141.164 108.619 1.00 29.66 ? 169 SER A CA    1 
ATOM   1396  C  C     . SER A 1 169 ? 132.142 140.539 109.108 1.00 26.61 ? 169 SER A C     1 
ATOM   1397  O  O     . SER A 1 169 ? 132.092 139.627 109.939 1.00 32.70 ? 169 SER A O     1 
ATOM   1398  C  CB    . SER A 1 169 ? 129.975 140.077 107.976 1.00 33.45 ? 169 SER A CB    1 
ATOM   1399  O  OG    . SER A 1 169 ? 128.608 140.273 108.294 1.00 37.99 ? 169 SER A OG    1 
ATOM   1400  N  N     . CYS A 1 170 ? 133.294 140.987 108.624 1.00 28.37 ? 170 CYS A N     1 
ATOM   1401  C  CA    . CYS A 1 170 ? 134.579 140.491 109.096 1.00 25.94 ? 170 CYS A CA    1 
ATOM   1402  C  C     . CYS A 1 170 ? 135.262 141.594 109.891 1.00 24.37 ? 170 CYS A C     1 
ATOM   1403  O  O     . CYS A 1 170 ? 135.457 142.704 109.384 1.00 27.74 ? 170 CYS A O     1 
ATOM   1404  C  CB    . CYS A 1 170 ? 135.454 140.014 107.933 1.00 32.82 ? 170 CYS A CB    1 
ATOM   1405  S  SG    . CYS A 1 170 ? 136.026 141.282 106.776 1.00 51.08 ? 170 CYS A SG    1 
ATOM   1406  N  N     . PHE A 1 171 ? 135.597 141.294 111.142 1.00 22.54 ? 171 PHE A N     1 
ATOM   1407  C  CA    . PHE A 1 171 ? 136.298 142.218 112.018 1.00 16.45 ? 171 PHE A CA    1 
ATOM   1408  C  C     . PHE A 1 171 ? 137.446 141.489 112.695 1.00 16.92 ? 171 PHE A C     1 
ATOM   1409  O  O     . PHE A 1 171 ? 137.317 140.321 113.069 1.00 26.98 ? 171 PHE A O     1 
ATOM   1410  C  CB    . PHE A 1 171 ? 135.361 142.817 113.073 1.00 17.81 ? 171 PHE A CB    1 
ATOM   1411  C  CG    . PHE A 1 171 ? 134.147 143.481 112.496 1.00 17.04 ? 171 PHE A CG    1 
ATOM   1412  C  CD1   . PHE A 1 171 ? 134.220 144.768 111.996 1.00 16.46 ? 171 PHE A CD1   1 
ATOM   1413  C  CD2   . PHE A 1 171 ? 132.932 142.820 112.455 1.00 16.17 ? 171 PHE A CD2   1 
ATOM   1414  C  CE1   . PHE A 1 171 ? 133.108 145.382 111.463 1.00 15.25 ? 171 PHE A CE1   1 
ATOM   1415  C  CE2   . PHE A 1 171 ? 131.817 143.430 111.922 1.00 16.12 ? 171 PHE A CE2   1 
ATOM   1416  C  CZ    . PHE A 1 171 ? 131.905 144.712 111.427 1.00 14.43 ? 171 PHE A CZ    1 
ATOM   1417  N  N     . LEU A 1 172 ? 138.571 142.184 112.841 1.00 18.50 ? 172 LEU A N     1 
ATOM   1418  C  CA    . LEU A 1 172 ? 139.763 141.636 113.470 1.00 8.23  ? 172 LEU A CA    1 
ATOM   1419  C  C     . LEU A 1 172 ? 140.163 142.556 114.611 1.00 13.48 ? 172 LEU A C     1 
ATOM   1420  O  O     . LEU A 1 172 ? 140.347 143.758 114.402 1.00 18.61 ? 172 LEU A O     1 
ATOM   1421  C  CB    . LEU A 1 172 ? 140.913 141.499 112.467 1.00 13.58 ? 172 LEU A CB    1 
ATOM   1422  C  CG    . LEU A 1 172 ? 140.813 140.444 111.365 1.00 7.83  ? 172 LEU A CG    1 
ATOM   1423  C  CD1   . LEU A 1 172 ? 139.935 140.929 110.224 1.00 11.58 ? 172 LEU A CD1   1 
ATOM   1424  C  CD2   . LEU A 1 172 ? 142.196 140.094 110.857 1.00 11.37 ? 172 LEU A CD2   1 
ATOM   1425  N  N     . LEU A 1 173 ? 140.299 141.995 115.809 1.00 21.52 ? 173 LEU A N     1 
ATOM   1426  C  CA    . LEU A 1 173 ? 140.585 142.770 117.007 1.00 9.24  ? 173 LEU A CA    1 
ATOM   1427  C  C     . LEU A 1 173 ? 141.912 142.341 117.611 1.00 17.43 ? 173 LEU A C     1 
ATOM   1428  O  O     . LEU A 1 173 ? 142.200 141.146 117.721 1.00 27.23 ? 173 LEU A O     1 
ATOM   1429  C  CB    . LEU A 1 173 ? 139.481 142.609 118.056 1.00 15.23 ? 173 LEU A CB    1 
ATOM   1430  C  CG    . LEU A 1 173 ? 138.029 142.850 117.648 1.00 17.18 ? 173 LEU A CG    1 
ATOM   1431  C  CD1   . LEU A 1 173 ? 137.134 142.722 118.866 1.00 21.06 ? 173 LEU A CD1   1 
ATOM   1432  C  CD2   . LEU A 1 173 ? 137.857 144.205 116.988 1.00 16.36 ? 173 LEU A CD2   1 
ATOM   1433  N  N     . GLU A 1 174 ? 142.715 143.323 118.006 1.00 23.95 ? 174 GLU A N     1 
ATOM   1434  C  CA    . GLU A 1 174 ? 143.940 143.085 118.757 1.00 19.68 ? 174 GLU A CA    1 
ATOM   1435  C  C     . GLU A 1 174 ? 143.649 143.312 120.235 1.00 17.61 ? 174 GLU A C     1 
ATOM   1436  O  O     . GLU A 1 174 ? 143.136 144.370 120.613 1.00 30.13 ? 174 GLU A O     1 
ATOM   1437  C  CB    . GLU A 1 174 ? 145.063 144.005 118.282 1.00 22.48 ? 174 GLU A CB    1 
ATOM   1438  C  CG    . GLU A 1 174 ? 145.609 143.671 116.911 1.00 20.70 ? 174 GLU A CG    1 
ATOM   1439  C  CD    . GLU A 1 174 ? 147.082 143.331 116.946 1.00 21.47 ? 174 GLU A CD    1 
ATOM   1440  O  OE1   . GLU A 1 174 ? 147.908 144.267 116.952 1.00 22.44 ? 174 GLU A OE1   1 
ATOM   1441  O  OE2   . GLU A 1 174 ? 147.417 142.130 116.965 1.00 33.14 ? 174 GLU A OE2   1 
ATOM   1442  N  N     . VAL A 1 175 ? 143.974 142.326 121.063 1.00 17.96 ? 175 VAL A N     1 
ATOM   1443  C  CA    . VAL A 1 175 ? 143.720 142.385 122.497 1.00 22.43 ? 175 VAL A CA    1 
ATOM   1444  C  C     . VAL A 1 175 ? 145.043 142.629 123.208 1.00 19.82 ? 175 VAL A C     1 
ATOM   1445  O  O     . VAL A 1 175 ? 145.992 141.851 123.057 1.00 21.39 ? 175 VAL A O     1 
ATOM   1446  C  CB    . VAL A 1 175 ? 143.052 141.098 123.004 1.00 22.38 ? 175 VAL A CB    1 
ATOM   1447  C  CG1   . VAL A 1 175 ? 142.395 141.337 124.354 1.00 14.95 ? 175 VAL A CG1   1 
ATOM   1448  C  CG2   . VAL A 1 175 ? 142.040 140.591 121.991 1.00 17.77 ? 175 VAL A CG2   1 
ATOM   1449  N  N     . ASN A 1 176 ? 145.108 143.708 123.983 1.00 15.51 ? 176 ASN A N     1 
ATOM   1450  C  CA    . ASN A 1 176 ? 146.296 144.006 124.764 1.00 18.88 ? 176 ASN A CA    1 
ATOM   1451  C  C     . ASN A 1 176 ? 146.293 143.208 126.064 1.00 22.90 ? 176 ASN A C     1 
ATOM   1452  O  O     . ASN A 1 176 ? 145.265 142.689 126.505 1.00 22.00 ? 176 ASN A O     1 
ATOM   1453  C  CB    . ASN A 1 176 ? 146.385 145.502 125.062 1.00 17.90 ? 176 ASN A CB    1 
ATOM   1454  C  CG    . ASN A 1 176 ? 147.794 146.031 124.964 1.00 24.26 ? 176 ASN A CG    1 
ATOM   1455  O  OD1   . ASN A 1 176 ? 148.761 145.283 125.090 1.00 27.32 ? 176 ASN A OD1   1 
ATOM   1456  N  ND2   . ASN A 1 176 ? 147.921 147.331 124.732 1.00 22.65 ? 176 ASN A ND2   1 
ATOM   1457  N  N     . ASP A 1 177 ? 147.469 143.122 126.683 1.00 29.71 ? 177 ASP A N     1 
ATOM   1458  C  CA    . ASP A 1 177 ? 147.668 142.291 127.871 1.00 21.81 ? 177 ASP A CA    1 
ATOM   1459  C  C     . ASP A 1 177 ? 147.257 143.063 129.126 1.00 22.62 ? 177 ASP A C     1 
ATOM   1460  O  O     . ASP A 1 177 ? 148.075 143.471 129.952 1.00 27.50 ? 177 ASP A O     1 
ATOM   1461  C  CB    . ASP A 1 177 ? 149.114 141.822 127.947 1.00 22.02 ? 177 ASP A CB    1 
ATOM   1462  C  CG    . ASP A 1 177 ? 149.332 140.776 129.017 1.00 29.31 ? 177 ASP A CG    1 
ATOM   1463  O  OD1   . ASP A 1 177 ? 148.420 139.953 129.238 1.00 31.92 ? 177 ASP A OD1   1 
ATOM   1464  O  OD2   . ASP A 1 177 ? 150.417 140.772 129.632 1.00 29.54 ? 177 ASP A OD2   1 
ATOM   1465  N  N     . SER A 1 178 ? 145.948 143.256 129.259 1.00 21.97 ? 178 SER A N     1 
ATOM   1466  C  CA    . SER A 1 178 ? 145.399 143.923 130.430 1.00 18.38 ? 178 SER A CA    1 
ATOM   1467  C  C     . SER A 1 178 ? 143.951 143.494 130.608 1.00 20.64 ? 178 SER A C     1 
ATOM   1468  O  O     . SER A 1 178 ? 143.291 143.066 129.659 1.00 29.24 ? 178 SER A O     1 
ATOM   1469  C  CB    . SER A 1 178 ? 145.503 145.446 130.311 1.00 18.75 ? 178 SER A CB    1 
ATOM   1470  O  OG    . SER A 1 178 ? 144.296 146.008 129.835 1.00 26.18 ? 178 SER A OG    1 
ATOM   1471  N  N     . LEU A 1 179 ? 143.467 143.612 131.846 1.00 27.85 ? 179 LEU A N     1 
ATOM   1472  C  CA    . LEU A 1 179 ? 142.073 143.283 132.129 1.00 20.53 ? 179 LEU A CA    1 
ATOM   1473  C  C     . LEU A 1 179 ? 141.129 144.305 131.513 1.00 23.62 ? 179 LEU A C     1 
ATOM   1474  O  O     . LEU A 1 179 ? 140.032 143.953 131.067 1.00 27.43 ? 179 LEU A O     1 
ATOM   1475  C  CB    . LEU A 1 179 ? 141.848 143.188 133.637 1.00 23.79 ? 179 LEU A CB    1 
ATOM   1476  C  CG    . LEU A 1 179 ? 140.488 142.645 134.081 1.00 21.95 ? 179 LEU A CG    1 
ATOM   1477  C  CD1   . LEU A 1 179 ? 140.378 141.160 133.776 1.00 24.99 ? 179 LEU A CD1   1 
ATOM   1478  C  CD2   . LEU A 1 179 ? 140.258 142.916 135.556 1.00 21.90 ? 179 LEU A CD2   1 
ATOM   1479  N  N     . ASN A 1 180 ? 141.530 145.578 131.494 1.00 23.72 ? 180 ASN A N     1 
ATOM   1480  C  CA    . ASN A 1 180 ? 140.729 146.593 130.818 1.00 21.77 ? 180 ASN A CA    1 
ATOM   1481  C  C     . ASN A 1 180 ? 140.598 146.281 129.336 1.00 27.45 ? 180 ASN A C     1 
ATOM   1482  O  O     . ASN A 1 180 ? 139.505 146.378 128.763 1.00 30.11 ? 180 ASN A O     1 
ATOM   1483  C  CB    . ASN A 1 180 ? 141.355 147.974 131.017 1.00 21.73 ? 180 ASN A CB    1 
ATOM   1484  C  CG    . ASN A 1 180 ? 140.992 148.593 132.348 1.00 27.17 ? 180 ASN A CG    1 
ATOM   1485  O  OD1   . ASN A 1 180 ? 139.959 148.272 132.934 1.00 33.96 ? 180 ASN A OD1   1 
ATOM   1486  N  ND2   . ASN A 1 180 ? 141.841 149.490 132.832 1.00 28.52 ? 180 ASN A ND2   1 
ATOM   1487  N  N     . ASP A 1 181 ? 141.701 145.880 128.703 1.00 26.01 ? 181 ASP A N     1 
ATOM   1488  C  CA    . ASP A 1 181 ? 141.666 145.548 127.286 1.00 17.15 ? 181 ASP A CA    1 
ATOM   1489  C  C     . ASP A 1 181 ? 140.897 144.260 127.025 1.00 21.45 ? 181 ASP A C     1 
ATOM   1490  O  O     . ASP A 1 181 ? 140.230 144.145 125.996 1.00 25.27 ? 181 ASP A O     1 
ATOM   1491  C  CB    . ASP A 1 181 ? 143.087 145.451 126.742 1.00 19.88 ? 181 ASP A CB    1 
ATOM   1492  C  CG    . ASP A 1 181 ? 143.732 146.811 126.568 1.00 32.65 ? 181 ASP A CG    1 
ATOM   1493  O  OD1   . ASP A 1 181 ? 143.407 147.500 125.579 1.00 36.01 ? 181 ASP A OD1   1 
ATOM   1494  O  OD2   . ASP A 1 181 ? 144.562 147.193 127.418 1.00 30.57 ? 181 ASP A OD2   1 
ATOM   1495  N  N     . ILE A 1 182 ? 140.958 143.293 127.941 1.00 22.08 ? 182 ILE A N     1 
ATOM   1496  C  CA    . ILE A 1 182 ? 140.184 142.066 127.769 1.00 21.35 ? 182 ILE A CA    1 
ATOM   1497  C  C     . ILE A 1 182 ? 138.691 142.352 127.899 1.00 19.80 ? 182 ILE A C     1 
ATOM   1498  O  O     . ILE A 1 182 ? 137.874 141.833 127.127 1.00 25.64 ? 182 ILE A O     1 
ATOM   1499  C  CB    . ILE A 1 182 ? 140.656 140.999 128.773 1.00 24.30 ? 182 ILE A CB    1 
ATOM   1500  C  CG1   . ILE A 1 182 ? 142.009 140.436 128.342 1.00 20.87 ? 182 ILE A CG1   1 
ATOM   1501  C  CG2   . ILE A 1 182 ? 139.631 139.881 128.899 1.00 26.91 ? 182 ILE A CG2   1 
ATOM   1502  C  CD1   . ILE A 1 182 ? 142.682 139.601 129.395 1.00 21.76 ? 182 ILE A CD1   1 
ATOM   1503  N  N     . SER A 1 183 ? 138.312 143.185 128.871 1.00 23.62 ? 183 SER A N     1 
ATOM   1504  C  CA    . SER A 1 183 ? 136.914 143.575 129.012 1.00 21.92 ? 183 SER A CA    1 
ATOM   1505  C  C     . SER A 1 183 ? 136.430 144.338 127.786 1.00 23.98 ? 183 SER A C     1 
ATOM   1506  O  O     . SER A 1 183 ? 135.321 144.100 127.293 1.00 30.29 ? 183 SER A O     1 
ATOM   1507  C  CB    . SER A 1 183 ? 136.731 144.422 130.270 1.00 21.67 ? 183 SER A CB    1 
ATOM   1508  O  OG    . SER A 1 183 ? 137.335 143.809 131.393 1.00 32.70 ? 183 SER A OG    1 
ATOM   1509  N  N     . ARG A 1 184 ? 137.251 145.260 127.278 1.00 24.07 ? 184 ARG A N     1 
ATOM   1510  C  CA    . ARG A 1 184 ? 136.878 145.981 126.069 1.00 24.62 ? 184 ARG A CA    1 
ATOM   1511  C  C     . ARG A 1 184 ? 136.790 145.054 124.867 1.00 28.61 ? 184 ARG A C     1 
ATOM   1512  O  O     . ARG A 1 184 ? 135.934 145.251 124.003 1.00 33.28 ? 184 ARG A O     1 
ATOM   1513  C  CB    . ARG A 1 184 ? 137.869 147.109 125.797 1.00 23.34 ? 184 ARG A CB    1 
ATOM   1514  C  CG    . ARG A 1 184 ? 137.287 148.231 124.963 1.00 27.57 ? 184 ARG A CG    1 
ATOM   1515  C  CD    . ARG A 1 184 ? 136.727 149.332 125.839 1.00 31.41 ? 184 ARG A CD    1 
ATOM   1516  N  NE    . ARG A 1 184 ? 135.292 149.501 125.649 1.00 31.54 ? 184 ARG A NE    1 
ATOM   1517  C  CZ    . ARG A 1 184 ? 134.561 150.420 126.264 1.00 35.38 ? 184 ARG A CZ    1 
ATOM   1518  N  NH1   . ARG A 1 184 ? 135.101 151.274 127.118 1.00 33.25 ? 184 ARG A NH1   1 
ATOM   1519  N  NH2   . ARG A 1 184 ? 133.256 150.485 126.015 1.00 28.82 ? 184 ARG A NH2   1 
ATOM   1520  N  N     . ALA A 1 185 ? 137.661 144.047 124.789 1.00 29.88 ? 185 ALA A N     1 
ATOM   1521  C  CA    . ALA A 1 185 ? 137.581 143.080 123.703 1.00 16.34 ? 185 ALA A CA    1 
ATOM   1522  C  C     . ALA A 1 185 ? 136.285 142.287 123.769 1.00 21.44 ? 185 ALA A C     1 
ATOM   1523  O  O     . ALA A 1 185 ? 135.641 142.057 122.743 1.00 25.25 ? 185 ALA A O     1 
ATOM   1524  C  CB    . ALA A 1 185 ? 138.787 142.143 123.742 1.00 18.19 ? 185 ALA A CB    1 
ATOM   1525  N  N     . ILE A 1 186 ? 135.884 141.868 124.971 1.00 24.13 ? 186 ILE A N     1 
ATOM   1526  C  CA    . ILE A 1 186 ? 134.615 141.158 125.125 1.00 20.11 ? 186 ILE A CA    1 
ATOM   1527  C  C     . ILE A 1 186 ? 133.452 142.053 124.716 1.00 22.48 ? 186 ILE A C     1 
ATOM   1528  O  O     . ILE A 1 186 ? 132.539 141.628 123.993 1.00 27.64 ? 186 ILE A O     1 
ATOM   1529  C  CB    . ILE A 1 186 ? 134.456 140.655 126.571 1.00 28.49 ? 186 ILE A CB    1 
ATOM   1530  C  CG1   . ILE A 1 186 ? 135.438 139.523 126.862 1.00 24.96 ? 186 ILE A CG1   1 
ATOM   1531  C  CG2   . ILE A 1 186 ? 133.028 140.199 126.830 1.00 27.61 ? 186 ILE A CG2   1 
ATOM   1532  C  CD1   . ILE A 1 186 ? 135.635 139.268 128.338 1.00 25.24 ? 186 ILE A CD1   1 
ATOM   1533  N  N     . ASP A 1 187 ? 133.471 143.309 125.167 1.00 28.48 ? 187 ASP A N     1 
ATOM   1534  C  CA    . ASP A 1 187 ? 132.398 144.240 124.837 1.00 23.22 ? 187 ASP A CA    1 
ATOM   1535  C  C     . ASP A 1 187 ? 132.312 144.473 123.334 1.00 27.41 ? 187 ASP A C     1 
ATOM   1536  O  O     . ASP A 1 187 ? 131.226 144.426 122.749 1.00 34.08 ? 187 ASP A O     1 
ATOM   1537  C  CB    . ASP A 1 187 ? 132.611 145.562 125.576 1.00 21.88 ? 187 ASP A CB    1 
ATOM   1538  C  CG    . ASP A 1 187 ? 131.779 146.693 125.006 1.00 35.75 ? 187 ASP A CG    1 
ATOM   1539  O  OD1   . ASP A 1 187 ? 130.549 146.523 124.873 1.00 37.80 ? 187 ASP A OD1   1 
ATOM   1540  O  OD2   . ASP A 1 187 ? 132.355 147.754 124.687 1.00 38.33 ? 187 ASP A OD2   1 
ATOM   1541  N  N     . ILE A 1 188 ? 133.456 144.715 122.690 1.00 25.64 ? 188 ILE A N     1 
ATOM   1542  C  CA    . ILE A 1 188 ? 133.472 144.989 121.257 1.00 22.64 ? 188 ILE A CA    1 
ATOM   1543  C  C     . ILE A 1 188 ? 133.073 143.748 120.472 1.00 23.06 ? 188 ILE A C     1 
ATOM   1544  O  O     . ILE A 1 188 ? 132.386 143.841 119.449 1.00 28.85 ? 188 ILE A O     1 
ATOM   1545  C  CB    . ILE A 1 188 ? 134.857 145.514 120.834 1.00 25.68 ? 188 ILE A CB    1 
ATOM   1546  C  CG1   . ILE A 1 188 ? 135.104 146.901 121.426 1.00 24.54 ? 188 ILE A CG1   1 
ATOM   1547  C  CG2   . ILE A 1 188 ? 134.974 145.579 119.325 1.00 21.84 ? 188 ILE A CG2   1 
ATOM   1548  C  CD1   . ILE A 1 188 ? 136.467 147.459 121.109 1.00 25.14 ? 188 ILE A CD1   1 
ATOM   1549  N  N     . SER A 1 189 ? 133.489 142.568 120.935 1.00 25.93 ? 189 SER A N     1 
ATOM   1550  C  CA    . SER A 1 189 ? 133.087 141.333 120.276 1.00 16.16 ? 189 SER A CA    1 
ATOM   1551  C  C     . SER A 1 189 ? 131.579 141.151 120.332 1.00 22.27 ? 189 SER A C     1 
ATOM   1552  O  O     . SER A 1 189 ? 130.956 140.784 119.331 1.00 28.07 ? 189 SER A O     1 
ATOM   1553  C  CB    . SER A 1 189 ? 133.794 140.142 120.921 1.00 20.74 ? 189 SER A CB    1 
ATOM   1554  O  OG    . SER A 1 189 ? 135.190 140.360 121.002 1.00 25.78 ? 189 SER A OG    1 
ATOM   1555  N  N     . MET A 1 190 ? 130.970 141.415 121.491 1.00 26.25 ? 190 MET A N     1 
ATOM   1556  C  CA    . MET A 1 190 ? 129.517 141.317 121.584 1.00 25.94 ? 190 MET A CA    1 
ATOM   1557  C  C     . MET A 1 190 ? 128.828 142.376 120.729 1.00 24.50 ? 190 MET A C     1 
ATOM   1558  O  O     . MET A 1 190 ? 127.804 142.095 120.098 1.00 26.54 ? 190 MET A O     1 
ATOM   1559  C  CB    . MET A 1 190 ? 129.067 141.417 123.040 1.00 25.04 ? 190 MET A CB    1 
ATOM   1560  C  CG    . MET A 1 190 ? 129.238 140.123 123.816 1.00 26.57 ? 190 MET A CG    1 
ATOM   1561  S  SD    . MET A 1 190 ? 129.018 140.281 125.597 1.00 39.23 ? 190 MET A SD    1 
ATOM   1562  C  CE    . MET A 1 190 ? 129.157 142.049 125.806 1.00 30.80 ? 190 MET A CE    1 
ATOM   1563  N  N     . GLN A 1 191 ? 129.372 143.595 120.692 1.00 20.97 ? 191 GLN A N     1 
ATOM   1564  C  CA    . GLN A 1 191 ? 128.775 144.646 119.872 1.00 27.23 ? 191 GLN A CA    1 
ATOM   1565  C  C     . GLN A 1 191 ? 128.820 144.293 118.391 1.00 27.45 ? 191 GLN A C     1 
ATOM   1566  O  O     . GLN A 1 191 ? 127.845 144.513 117.664 1.00 30.86 ? 191 GLN A O     1 
ATOM   1567  C  CB    . GLN A 1 191 ? 129.478 145.980 120.121 1.00 27.84 ? 191 GLN A CB    1 
ATOM   1568  C  CG    . GLN A 1 191 ? 129.325 146.521 121.530 1.00 26.89 ? 191 GLN A CG    1 
ATOM   1569  C  CD    . GLN A 1 191 ? 127.907 146.944 121.850 1.00 29.63 ? 191 GLN A CD    1 
ATOM   1570  O  OE1   . GLN A 1 191 ? 127.483 146.895 123.003 1.00 30.07 ? 191 GLN A OE1   1 
ATOM   1571  N  NE2   . GLN A 1 191 ? 127.170 147.374 120.834 1.00 30.31 ? 191 GLN A NE2   1 
ATOM   1572  N  N     . LEU A 1 192 ? 129.945 143.750 117.923 1.00 27.08 ? 192 LEU A N     1 
ATOM   1573  C  CA    . LEU A 1 192 ? 130.083 143.420 116.510 1.00 21.70 ? 192 LEU A CA    1 
ATOM   1574  C  C     . LEU A 1 192 ? 129.320 142.156 116.139 1.00 24.39 ? 192 LEU A C     1 
ATOM   1575  O  O     . LEU A 1 192 ? 128.807 142.058 115.019 1.00 33.97 ? 192 LEU A O     1 
ATOM   1576  C  CB    . LEU A 1 192 ? 131.561 143.275 116.147 1.00 21.61 ? 192 LEU A CB    1 
ATOM   1577  C  CG    . LEU A 1 192 ? 132.402 144.551 116.210 1.00 20.23 ? 192 LEU A CG    1 
ATOM   1578  C  CD1   . LEU A 1 192 ? 133.880 144.224 116.102 1.00 20.19 ? 192 LEU A CD1   1 
ATOM   1579  C  CD2   . LEU A 1 192 ? 131.988 145.532 115.128 1.00 18.57 ? 192 LEU A CD2   1 
ATOM   1580  N  N     . SER A 1 193 ? 129.235 141.183 117.050 1.00 28.30 ? 193 SER A N     1 
ATOM   1581  C  CA    . SER A 1 193 ? 128.401 140.013 116.811 1.00 26.65 ? 193 SER A CA    1 
ATOM   1582  C  C     . SER A 1 193 ? 126.927 140.391 116.788 1.00 31.49 ? 193 SER A C     1 
ATOM   1583  O  O     . SER A 1 193 ? 126.137 139.794 116.050 1.00 35.03 ? 193 SER A O     1 
ATOM   1584  C  CB    . SER A 1 193 ? 128.672 138.954 117.878 1.00 28.01 ? 193 SER A CB    1 
ATOM   1585  O  OG    . SER A 1 193 ? 127.901 137.789 117.652 1.00 38.29 ? 193 SER A OG    1 
ATOM   1586  N  N     . LYS A 1 194 ? 126.540 141.380 117.597 1.00 33.26 ? 194 LYS A N     1 
ATOM   1587  C  CA    . LYS A 1 194 ? 125.176 141.891 117.557 1.00 31.74 ? 194 LYS A CA    1 
ATOM   1588  C  C     . LYS A 1 194 ? 124.858 142.493 116.194 1.00 35.67 ? 194 LYS A C     1 
ATOM   1589  O  O     . LYS A 1 194 ? 123.741 142.347 115.685 1.00 38.84 ? 194 LYS A O     1 
ATOM   1590  C  CB    . LYS A 1 194 ? 124.983 142.921 118.670 1.00 29.43 ? 194 LYS A CB    1 
ATOM   1591  C  CG    . LYS A 1 194 ? 123.795 143.842 118.491 1.00 33.40 ? 194 LYS A CG    1 
ATOM   1592  C  CD    . LYS A 1 194 ? 123.896 145.036 119.423 1.00 36.14 ? 194 LYS A CD    1 
ATOM   1593  C  CE    . LYS A 1 194 ? 122.575 145.780 119.518 1.00 33.61 ? 194 LYS A CE    1 
ATOM   1594  N  NZ    . LYS A 1 194 ? 122.660 146.934 120.454 1.00 33.44 ? 194 LYS A NZ    1 
ATOM   1595  N  N     . LEU A 1 195 ? 125.834 143.168 115.583 1.00 34.28 ? 195 LEU A N     1 
ATOM   1596  C  CA    . LEU A 1 195 ? 125.665 143.705 114.240 1.00 31.90 ? 195 LEU A CA    1 
ATOM   1597  C  C     . LEU A 1 195 ? 125.636 142.621 113.172 1.00 34.86 ? 195 LEU A C     1 
ATOM   1598  O  O     . LEU A 1 195 ? 125.326 142.925 112.016 1.00 38.44 ? 195 LEU A O     1 
ATOM   1599  C  CB    . LEU A 1 195 ? 126.785 144.698 113.929 1.00 34.27 ? 195 LEU A CB    1 
ATOM   1600  C  CG    . LEU A 1 195 ? 126.858 145.929 114.830 1.00 34.11 ? 195 LEU A CG    1 
ATOM   1601  C  CD1   . LEU A 1 195 ? 128.130 146.712 114.552 1.00 30.85 ? 195 LEU A CD1   1 
ATOM   1602  C  CD2   . LEU A 1 195 ? 125.630 146.802 114.641 1.00 36.15 ? 195 LEU A CD2   1 
ATOM   1603  N  N     . GLY A 1 196 ? 125.953 141.378 113.526 1.00 32.21 ? 196 GLY A N     1 
ATOM   1604  C  CA    . GLY A 1 196 ? 125.953 140.279 112.586 1.00 31.03 ? 196 GLY A CA    1 
ATOM   1605  C  C     . GLY A 1 196 ? 127.309 139.907 112.034 1.00 35.40 ? 196 GLY A C     1 
ATOM   1606  O  O     . GLY A 1 196 ? 127.396 138.960 111.243 1.00 39.35 ? 196 GLY A O     1 
ATOM   1607  N  N     . GLY A 1 197 ? 128.364 140.613 112.422 1.00 30.36 ? 197 GLY A N     1 
ATOM   1608  C  CA    . GLY A 1 197 ? 129.683 140.353 111.890 1.00 24.85 ? 197 GLY A CA    1 
ATOM   1609  C  C     . GLY A 1 197 ? 130.423 139.247 112.620 1.00 24.16 ? 197 GLY A C     1 
ATOM   1610  O  O     . GLY A 1 197 ? 130.187 138.981 113.795 1.00 30.03 ? 197 GLY A O     1 
ATOM   1611  N  N     . GLY A 1 198 ? 131.329 138.596 111.892 1.00 19.75 ? 198 GLY A N     1 
ATOM   1612  C  CA    . GLY A 1 198 ? 132.235 137.633 112.487 1.00 18.17 ? 198 GLY A CA    1 
ATOM   1613  C  C     . GLY A 1 198 ? 133.469 138.345 113.001 1.00 17.70 ? 198 GLY A C     1 
ATOM   1614  O  O     . GLY A 1 198 ? 134.048 139.183 112.305 1.00 23.09 ? 198 GLY A O     1 
ATOM   1615  N  N     . VAL A 1 199 ? 133.867 138.012 114.224 1.00 20.58 ? 199 VAL A N     1 
ATOM   1616  C  CA    . VAL A 1 199 ? 134.930 138.720 114.925 1.00 16.17 ? 199 VAL A CA    1 
ATOM   1617  C  C     . VAL A 1 199 ? 136.100 137.772 115.138 1.00 13.29 ? 199 VAL A C     1 
ATOM   1618  O  O     . VAL A 1 199 ? 135.921 136.658 115.641 1.00 16.08 ? 199 VAL A O     1 
ATOM   1619  C  CB    . VAL A 1 199 ? 134.440 139.288 116.269 1.00 15.56 ? 199 VAL A CB    1 
ATOM   1620  C  CG1   . VAL A 1 199 ? 135.503 140.172 116.888 1.00 15.25 ? 199 VAL A CG1   1 
ATOM   1621  C  CG2   . VAL A 1 199 ? 133.147 140.054 116.076 1.00 19.41 ? 199 VAL A CG2   1 
ATOM   1622  N  N     . SER A 1 200 ? 137.290 138.217 114.757 1.00 17.27 ? 200 SER A N     1 
ATOM   1623  C  CA    . SER A 1 200 ? 138.528 137.504 115.026 1.00 7.54  ? 200 SER A CA    1 
ATOM   1624  C  C     . SER A 1 200 ? 139.355 138.302 116.022 1.00 13.33 ? 200 SER A C     1 
ATOM   1625  O  O     . SER A 1 200 ? 139.429 139.530 115.937 1.00 20.13 ? 200 SER A O     1 
ATOM   1626  C  CB    . SER A 1 200 ? 139.327 137.279 113.744 1.00 14.15 ? 200 SER A CB    1 
ATOM   1627  O  OG    . SER A 1 200 ? 140.254 136.223 113.904 1.00 19.81 ? 200 SER A OG    1 
ATOM   1628  N  N     . LEU A 1 201 ? 139.970 137.602 116.970 1.00 19.52 ? 201 LEU A N     1 
ATOM   1629  C  CA    . LEU A 1 201 ? 140.754 138.240 118.015 1.00 11.21 ? 201 LEU A CA    1 
ATOM   1630  C  C     . LEU A 1 201 ? 142.148 137.636 118.059 1.00 10.05 ? 201 LEU A C     1 
ATOM   1631  O  O     . LEU A 1 201 ? 142.311 136.416 117.972 1.00 16.59 ? 201 LEU A O     1 
ATOM   1632  C  CB    . LEU A 1 201 ? 140.079 138.094 119.384 1.00 15.21 ? 201 LEU A CB    1 
ATOM   1633  C  CG    . LEU A 1 201 ? 138.685 138.713 119.508 1.00 15.31 ? 201 LEU A CG    1 
ATOM   1634  C  CD1   . LEU A 1 201 ? 137.620 137.631 119.548 1.00 21.22 ? 201 LEU A CD1   1 
ATOM   1635  C  CD2   . LEU A 1 201 ? 138.598 139.605 120.731 1.00 12.63 ? 201 LEU A CD2   1 
ATOM   1636  N  N     . ASN A 1 202 ? 143.150 138.500 118.189 1.00 10.51 ? 202 ASN A N     1 
ATOM   1637  C  CA    . ASN A 1 202 ? 144.525 138.072 118.399 1.00 8.30  ? 202 ASN A CA    1 
ATOM   1638  C  C     . ASN A 1 202 ? 144.777 137.953 119.896 1.00 18.71 ? 202 ASN A C     1 
ATOM   1639  O  O     . ASN A 1 202 ? 144.632 138.933 120.634 1.00 29.04 ? 202 ASN A O     1 
ATOM   1640  C  CB    . ASN A 1 202 ? 145.505 139.057 117.765 1.00 10.43 ? 202 ASN A CB    1 
ATOM   1641  C  CG    . ASN A 1 202 ? 146.889 138.470 117.593 1.00 12.31 ? 202 ASN A CG    1 
ATOM   1642  O  OD1   . ASN A 1 202 ? 147.050 137.258 117.463 1.00 16.44 ? 202 ASN A OD1   1 
ATOM   1643  N  ND2   . ASN A 1 202 ? 147.899 139.330 117.591 1.00 10.72 ? 202 ASN A ND2   1 
ATOM   1644  N  N     . LEU A 1 203 ? 145.152 136.755 120.342 1.00 13.80 ? 203 LEU A N     1 
ATOM   1645  C  CA    . LEU A 1 203 ? 145.396 136.492 121.753 1.00 11.50 ? 203 LEU A CA    1 
ATOM   1646  C  C     . LEU A 1 203 ? 146.878 136.314 122.060 1.00 13.38 ? 203 LEU A C     1 
ATOM   1647  O  O     . LEU A 1 203 ? 147.232 135.834 123.140 1.00 21.85 ? 203 LEU A O     1 
ATOM   1648  C  CB    . LEU A 1 203 ? 144.607 135.262 122.202 1.00 18.16 ? 203 LEU A CB    1 
ATOM   1649  C  CG    . LEU A 1 203 ? 143.087 135.328 122.044 1.00 17.41 ? 203 LEU A CG    1 
ATOM   1650  C  CD1   . LEU A 1 203 ? 142.426 134.241 122.866 1.00 18.20 ? 203 LEU A CD1   1 
ATOM   1651  C  CD2   . LEU A 1 203 ? 142.549 136.695 122.437 1.00 14.72 ? 203 LEU A CD2   1 
ATOM   1652  N  N     . SER A 1 204 ? 147.753 136.701 121.130 1.00 12.64 ? 204 SER A N     1 
ATOM   1653  C  CA    . SER A 1 204 ? 149.183 136.489 121.316 1.00 14.92 ? 204 SER A CA    1 
ATOM   1654  C  C     . SER A 1 204 ? 149.791 137.464 122.316 1.00 19.73 ? 204 SER A C     1 
ATOM   1655  O  O     . SER A 1 204 ? 150.728 137.099 123.034 1.00 27.35 ? 204 SER A O     1 
ATOM   1656  C  CB    . SER A 1 204 ? 149.905 136.599 119.975 1.00 15.18 ? 204 SER A CB    1 
ATOM   1657  O  OG    . SER A 1 204 ? 149.331 135.728 119.018 1.00 23.52 ? 204 SER A OG    1 
ATOM   1658  N  N     . LYS A 1 205 ? 149.286 138.698 122.377 1.00 19.71 ? 205 LYS A N     1 
ATOM   1659  C  CA    . LYS A 1 205 ? 149.818 139.663 123.332 1.00 16.85 ? 205 LYS A CA    1 
ATOM   1660  C  C     . LYS A 1 205 ? 149.443 139.324 124.766 1.00 18.81 ? 205 LYS A C     1 
ATOM   1661  O  O     . LYS A 1 205 ? 150.106 139.797 125.693 1.00 22.98 ? 205 LYS A O     1 
ATOM   1662  C  CB    . LYS A 1 205 ? 149.335 141.071 122.991 1.00 16.53 ? 205 LYS A CB    1 
ATOM   1663  C  CG    . LYS A 1 205 ? 149.951 141.640 121.734 1.00 18.42 ? 205 LYS A CG    1 
ATOM   1664  C  CD    . LYS A 1 205 ? 149.475 143.053 121.475 1.00 24.01 ? 205 LYS A CD    1 
ATOM   1665  C  CE    . LYS A 1 205 ? 150.242 143.683 120.328 1.00 27.27 ? 205 LYS A CE    1 
ATOM   1666  N  NZ    . LYS A 1 205 ? 150.053 142.936 119.058 1.00 20.04 ? 205 LYS A NZ    1 
ATOM   1667  N  N     . LEU A 1 206 ? 148.402 138.522 124.967 1.00 19.30 ? 206 LEU A N     1 
ATOM   1668  C  CA    . LEU A 1 206 ? 148.014 138.112 126.309 1.00 12.55 ? 206 LEU A CA    1 
ATOM   1669  C  C     . LEU A 1 206 ? 149.081 137.208 126.909 1.00 17.32 ? 206 LEU A C     1 
ATOM   1670  O  O     . LEU A 1 206 ? 149.588 136.301 126.241 1.00 22.15 ? 206 LEU A O     1 
ATOM   1671  C  CB    . LEU A 1 206 ? 146.671 137.391 126.268 1.00 20.66 ? 206 LEU A CB    1 
ATOM   1672  C  CG    . LEU A 1 206 ? 145.478 138.232 125.823 1.00 20.56 ? 206 LEU A CG    1 
ATOM   1673  C  CD1   . LEU A 1 206 ? 144.217 137.394 125.818 1.00 16.57 ? 206 LEU A CD1   1 
ATOM   1674  C  CD2   . LEU A 1 206 ? 145.318 139.444 126.722 1.00 23.52 ? 206 LEU A CD2   1 
ATOM   1675  N  N     . ARG A 1 207 ? 149.420 137.450 128.171 1.00 24.93 ? 207 ARG A N     1 
ATOM   1676  C  CA    . ARG A 1 207 ? 150.445 136.653 128.824 1.00 22.96 ? 207 ARG A CA    1 
ATOM   1677  C  C     . ARG A 1 207 ? 149.925 135.252 129.126 1.00 27.55 ? 207 ARG A C     1 
ATOM   1678  O  O     . ARG A 1 207 ? 148.724 135.029 129.294 1.00 28.29 ? 207 ARG A O     1 
ATOM   1679  C  CB    . ARG A 1 207 ? 150.929 137.335 130.102 1.00 23.39 ? 207 ARG A CB    1 
ATOM   1680  C  CG    . ARG A 1 207 ? 149.905 137.443 131.207 1.00 23.39 ? 207 ARG A CG    1 
ATOM   1681  C  CD    . ARG A 1 207 ? 150.430 138.325 132.322 1.00 26.66 ? 207 ARG A CD    1 
ATOM   1682  N  NE    . ARG A 1 207 ? 150.500 139.723 131.916 1.00 30.47 ? 207 ARG A NE    1 
ATOM   1683  C  CZ    . ARG A 1 207 ? 150.523 140.747 132.756 1.00 24.97 ? 207 ARG A CZ    1 
ATOM   1684  N  NH1   . ARG A 1 207 ? 150.516 140.567 134.066 1.00 29.09 ? 207 ARG A NH1   1 
ATOM   1685  N  NH2   . ARG A 1 207 ? 150.554 141.984 132.270 1.00 20.78 ? 207 ARG A NH2   1 
ATOM   1686  N  N     . ALA A 1 208 ? 150.853 134.303 129.187 1.00 33.16 ? 208 ALA A N     1 
ATOM   1687  C  CA    . ALA A 1 208 ? 150.515 132.894 129.263 1.00 25.47 ? 208 ALA A CA    1 
ATOM   1688  C  C     . ALA A 1 208 ? 150.048 132.511 130.666 1.00 31.96 ? 208 ALA A C     1 
ATOM   1689  O  O     . ALA A 1 208 ? 150.064 133.312 131.603 1.00 36.92 ? 208 ALA A O     1 
ATOM   1690  C  CB    . ALA A 1 208 ? 151.711 132.043 128.848 1.00 26.45 ? 208 ALA A CB    1 
ATOM   1691  N  N     . LYS A 1 209 ? 149.611 131.262 130.794 1.00 32.37 ? 209 LYS A N     1 
ATOM   1692  C  CA    . LYS A 1 209 ? 149.190 130.738 132.085 1.00 29.99 ? 209 LYS A CA    1 
ATOM   1693  C  C     . LYS A 1 209 ? 150.383 130.612 133.023 1.00 34.83 ? 209 LYS A C     1 
ATOM   1694  O  O     . LYS A 1 209 ? 151.458 130.150 132.631 1.00 35.86 ? 209 LYS A O     1 
ATOM   1695  C  CB    . LYS A 1 209 ? 148.514 129.379 131.909 1.00 30.24 ? 209 LYS A CB    1 
ATOM   1696  C  CG    . LYS A 1 209 ? 147.568 129.001 133.033 1.00 33.17 ? 209 LYS A CG    1 
ATOM   1697  C  CD    . LYS A 1 209 ? 147.232 127.520 132.996 1.00 32.17 ? 209 LYS A CD    1 
ATOM   1698  C  CE    . LYS A 1 209 ? 148.463 126.677 132.703 1.00 36.74 ? 209 LYS A CE    1 
ATOM   1699  N  NZ    . LYS A 1 209 ? 148.104 125.298 132.272 1.00 37.00 ? 209 LYS A NZ    1 
ATOM   1700  N  N     . GLY A 1 210 ? 150.185 131.023 134.272 1.00 36.75 ? 210 GLY A N     1 
ATOM   1701  C  CA    . GLY A 1 210 ? 151.256 130.983 135.245 1.00 34.86 ? 210 GLY A CA    1 
ATOM   1702  C  C     . GLY A 1 210 ? 152.159 132.192 135.251 1.00 37.26 ? 210 GLY A C     1 
ATOM   1703  O  O     . GLY A 1 210 ? 153.281 132.110 135.758 1.00 39.10 ? 210 GLY A O     1 
ATOM   1704  N  N     . GLU A 1 211 ? 151.711 133.312 134.699 1.00 37.45 ? 211 GLU A N     1 
ATOM   1705  C  CA    . GLU A 1 211 ? 152.466 134.554 134.734 1.00 33.13 ? 211 GLU A CA    1 
ATOM   1706  C  C     . GLU A 1 211 ? 151.946 135.451 135.850 1.00 36.71 ? 211 GLU A C     1 
ATOM   1707  O  O     . GLU A 1 211 ? 150.827 135.292 136.340 1.00 37.39 ? 211 GLU A O     1 
ATOM   1708  C  CB    . GLU A 1 211 ? 152.389 135.278 133.389 1.00 32.43 ? 211 GLU A CB    1 
ATOM   1709  C  CG    . GLU A 1 211 ? 152.941 134.471 132.233 1.00 33.06 ? 211 GLU A CG    1 
ATOM   1710  C  CD    . GLU A 1 211 ? 153.907 135.261 131.378 1.00 37.81 ? 211 GLU A CD    1 
ATOM   1711  O  OE1   . GLU A 1 211 ? 155.017 135.560 131.862 1.00 41.31 ? 211 GLU A OE1   1 
ATOM   1712  O  OE2   . GLU A 1 211 ? 153.566 135.570 130.219 1.00 31.57 ? 211 GLU A OE2   1 
ATOM   1713  N  N     . ALA A 1 212 ? 152.784 136.402 136.250 1.00 36.04 ? 212 ALA A N     1 
ATOM   1714  C  CA    . ALA A 1 212 ? 152.466 137.267 137.375 1.00 32.63 ? 212 ALA A CA    1 
ATOM   1715  C  C     . ALA A 1 212 ? 151.525 138.390 136.963 1.00 37.45 ? 212 ALA A C     1 
ATOM   1716  O  O     . ALA A 1 212 ? 151.611 138.918 135.851 1.00 40.25 ? 212 ALA A O     1 
ATOM   1717  C  CB    . ALA A 1 212 ? 153.745 137.854 137.971 1.00 36.21 ? 212 ALA A CB    1 
ATOM   1718  N  N     . ILE A 1 213 ? 150.622 138.748 137.867 1.00 36.01 ? 213 ILE A N     1 
ATOM   1719  C  CA    . ILE A 1 213 ? 149.771 139.927 137.721 1.00 34.39 ? 213 ILE A CA    1 
ATOM   1720  C  C     . ILE A 1 213 ? 150.130 140.853 138.876 1.00 36.42 ? 213 ILE A C     1 
ATOM   1721  O  O     . ILE A 1 213 ? 149.582 140.737 139.974 1.00 40.53 ? 213 ILE A O     1 
ATOM   1722  C  CB    . ILE A 1 213 ? 148.279 139.588 137.725 1.00 35.73 ? 213 ILE A CB    1 
ATOM   1723  C  CG1   . ILE A 1 213 ? 147.986 138.402 136.811 1.00 37.53 ? 213 ILE A CG1   1 
ATOM   1724  C  CG2   . ILE A 1 213 ? 147.462 140.797 137.305 1.00 33.53 ? 213 ILE A CG2   1 
ATOM   1725  C  CD1   . ILE A 1 213 ? 146.637 137.775 137.062 1.00 31.60 ? 213 ILE A CD1   1 
ATOM   1726  N  N     . LYS A 1 214 ? 151.042 141.794 138.627 1.00 41.55 ? 214 LYS A N     1 
ATOM   1727  C  CA    . LYS A 1 214 ? 151.527 142.726 139.645 1.00 40.57 ? 214 LYS A CA    1 
ATOM   1728  C  C     . LYS A 1 214 ? 152.165 141.968 140.815 1.00 44.25 ? 214 LYS A C     1 
ATOM   1729  O  O     . LYS A 1 214 ? 151.649 141.922 141.934 1.00 45.48 ? 214 LYS A O     1 
ATOM   1730  C  CB    . LYS A 1 214 ? 150.405 143.657 140.122 1.00 39.69 ? 214 LYS A CB    1 
ATOM   1731  C  CG    . LYS A 1 214 ? 150.590 145.104 139.704 1.00 42.50 ? 214 LYS A CG    1 
ATOM   1732  C  CD    . LYS A 1 214 ? 149.441 145.974 140.180 1.00 43.00 ? 214 LYS A CD    1 
ATOM   1733  C  CE    . LYS A 1 214 ? 149.385 147.276 139.397 1.00 44.97 ? 214 LYS A CE    1 
ATOM   1734  N  NZ    . LYS A 1 214 ? 148.027 147.883 139.418 1.00 43.13 ? 214 LYS A NZ    1 
ATOM   1735  N  N     . ASP A 1 215 ? 153.283 141.321 140.487 1.00 45.75 ? 215 ASP A N     1 
ATOM   1736  C  CA    . ASP A 1 215 ? 154.245 140.706 141.402 1.00 50.07 ? 215 ASP A CA    1 
ATOM   1737  C  C     . ASP A 1 215 ? 153.670 139.567 142.241 1.00 49.71 ? 215 ASP A C     1 
ATOM   1738  O  O     . ASP A 1 215 ? 154.311 139.138 143.207 1.00 51.90 ? 215 ASP A O     1 
ATOM   1739  C  CB    . ASP A 1 215 ? 154.923 141.754 142.310 1.00 48.88 ? 215 ASP A CB    1 
ATOM   1740  C  CG    . ASP A 1 215 ? 154.020 142.272 143.421 1.00 52.44 ? 215 ASP A CG    1 
ATOM   1741  O  OD1   . ASP A 1 215 ? 153.752 141.531 144.390 1.00 51.26 ? 215 ASP A OD1   1 
ATOM   1742  O  OD2   . ASP A 1 215 ? 153.583 143.438 143.327 1.00 51.18 ? 215 ASP A OD2   1 
ATOM   1743  N  N     . VAL A 1 216 ? 152.497 139.042 141.899 1.00 43.82 ? 216 VAL A N     1 
ATOM   1744  C  CA    . VAL A 1 216 ? 152.023 137.779 142.458 1.00 46.73 ? 216 VAL A CA    1 
ATOM   1745  C  C     . VAL A 1 216 ? 152.055 136.737 141.348 1.00 48.13 ? 216 VAL A C     1 
ATOM   1746  O  O     . VAL A 1 216 ? 151.387 136.887 140.318 1.00 50.91 ? 216 VAL A O     1 
ATOM   1747  C  CB    . VAL A 1 216 ? 150.625 137.912 143.086 1.00 45.73 ? 216 VAL A CB    1 
ATOM   1748  C  CG1   . VAL A 1 216 ? 149.660 138.599 142.151 1.00 45.56 ? 216 VAL A CG1   1 
ATOM   1749  C  CG2   . VAL A 1 216 ? 150.092 136.543 143.477 1.00 46.09 ? 216 VAL A CG2   1 
ATOM   1750  N  N     . GLU A 1 217 ? 152.838 135.684 141.553 1.00 48.01 ? 217 GLU A N     1 
ATOM   1751  C  CA    . GLU A 1 217 ? 153.189 134.750 140.496 1.00 47.80 ? 217 GLU A CA    1 
ATOM   1752  C  C     . GLU A 1 217 ? 152.136 133.658 140.342 1.00 49.03 ? 217 GLU A C     1 
ATOM   1753  O  O     . GLU A 1 217 ? 151.318 133.415 141.233 1.00 50.27 ? 217 GLU A O     1 
ATOM   1754  C  CB    . GLU A 1 217 ? 154.555 134.125 140.778 1.00 49.39 ? 217 GLU A CB    1 
ATOM   1755  C  CG    . GLU A 1 217 ? 155.560 135.104 141.359 1.00 50.04 ? 217 GLU A CG    1 
ATOM   1756  C  CD    . GLU A 1 217 ? 156.452 135.718 140.300 1.00 51.81 ? 217 GLU A CD    1 
ATOM   1757  O  OE1   . GLU A 1 217 ? 156.943 134.971 139.429 1.00 53.33 ? 217 GLU A OE1   1 
ATOM   1758  O  OE2   . GLU A 1 217 ? 156.656 136.950 140.336 1.00 50.08 ? 217 GLU A OE2   1 
ATOM   1759  N  N     . ASN A 1 218 ? 152.176 132.995 139.184 1.00 46.10 ? 218 ASN A N     1 
ATOM   1760  C  CA    . ASN A 1 218 ? 151.242 131.920 138.844 1.00 45.69 ? 218 ASN A CA    1 
ATOM   1761  C  C     . ASN A 1 218 ? 149.797 132.382 138.993 1.00 48.94 ? 218 ASN A C     1 
ATOM   1762  O  O     . ASN A 1 218 ? 148.922 131.638 139.440 1.00 50.20 ? 218 ASN A O     1 
ATOM   1763  C  CB    . ASN A 1 218 ? 151.510 130.672 139.684 1.00 47.10 ? 218 ASN A CB    1 
ATOM   1764  C  CG    . ASN A 1 218 ? 152.678 129.863 139.164 1.00 49.62 ? 218 ASN A CG    1 
ATOM   1765  O  OD1   . ASN A 1 218 ? 152.511 128.978 138.325 1.00 49.64 ? 218 ASN A OD1   1 
ATOM   1766  N  ND2   . ASN A 1 218 ? 153.874 130.168 139.654 1.00 48.07 ? 218 ASN A ND2   1 
ATOM   1767  N  N     . ALA A 1 219 ? 149.545 133.630 138.608 1.00 40.23 ? 219 ALA A N     1 
ATOM   1768  C  CA    . ALA A 1 219 ? 148.245 134.252 138.798 1.00 38.53 ? 219 ALA A CA    1 
ATOM   1769  C  C     . ALA A 1 219 ? 147.407 134.307 137.531 1.00 41.13 ? 219 ALA A C     1 
ATOM   1770  O  O     . ALA A 1 219 ? 146.177 134.244 137.613 1.00 41.57 ? 219 ALA A O     1 
ATOM   1771  C  CB    . ALA A 1 219 ? 148.423 135.671 139.345 1.00 37.51 ? 219 ALA A CB    1 
ATOM   1772  N  N     . THR A 1 220 ? 148.040 134.415 136.368 1.00 38.15 ? 220 THR A N     1 
ATOM   1773  C  CA    . THR A 1 220 ? 147.310 134.562 135.118 1.00 35.62 ? 220 THR A CA    1 
ATOM   1774  C  C     . THR A 1 220 ? 146.746 133.217 134.677 1.00 37.13 ? 220 THR A C     1 
ATOM   1775  O  O     . THR A 1 220 ? 147.428 132.191 134.738 1.00 38.72 ? 220 THR A O     1 
ATOM   1776  C  CB    . THR A 1 220 ? 148.228 135.139 134.038 1.00 34.47 ? 220 THR A CB    1 
ATOM   1777  O  OG1   . THR A 1 220 ? 148.493 136.516 134.326 1.00 37.31 ? 220 THR A OG1   1 
ATOM   1778  C  CG2   . THR A 1 220 ? 147.572 135.062 132.677 1.00 35.62 ? 220 THR A CG2   1 
ATOM   1779  N  N     . LYS A 1 221 ? 145.488 133.227 134.237 1.00 37.52 ? 221 LYS A N     1 
ATOM   1780  C  CA    . LYS A 1 221 ? 144.822 132.018 133.768 1.00 34.09 ? 221 LYS A CA    1 
ATOM   1781  C  C     . LYS A 1 221 ? 145.184 131.660 132.334 1.00 39.16 ? 221 LYS A C     1 
ATOM   1782  O  O     . LYS A 1 221 ? 144.732 130.621 131.840 1.00 44.49 ? 221 LYS A O     1 
ATOM   1783  C  CB    . LYS A 1 221 ? 143.304 132.170 133.885 1.00 34.58 ? 221 LYS A CB    1 
ATOM   1784  C  CG    . LYS A 1 221 ? 142.836 132.800 135.179 1.00 38.12 ? 221 LYS A CG    1 
ATOM   1785  C  CD    . LYS A 1 221 ? 141.337 132.642 135.348 1.00 37.19 ? 221 LYS A CD    1 
ATOM   1786  C  CE    . LYS A 1 221 ? 140.972 131.251 135.831 1.00 36.15 ? 221 LYS A CE    1 
ATOM   1787  N  NZ    . LYS A 1 221 ? 141.766 130.853 137.022 1.00 38.88 ? 221 LYS A NZ    1 
ATOM   1788  N  N     . GLY A 1 222 ? 145.974 132.484 131.660 1.00 33.82 ? 222 GLY A N     1 
ATOM   1789  C  CA    . GLY A 1 222 ? 146.367 132.211 130.299 1.00 31.76 ? 222 GLY A CA    1 
ATOM   1790  C  C     . GLY A 1 222 ? 145.335 132.672 129.290 1.00 31.54 ? 222 GLY A C     1 
ATOM   1791  O  O     . GLY A 1 222 ? 144.340 133.326 129.612 1.00 32.59 ? 222 GLY A O     1 
ATOM   1792  N  N     . VAL A 1 223 ? 145.591 132.313 128.031 1.00 31.82 ? 223 VAL A N     1 
ATOM   1793  C  CA    . VAL A 1 223 ? 144.678 132.693 126.960 1.00 26.44 ? 223 VAL A CA    1 
ATOM   1794  C  C     . VAL A 1 223 ? 143.415 131.846 126.952 1.00 22.47 ? 223 VAL A C     1 
ATOM   1795  O  O     . VAL A 1 223 ? 142.437 132.226 126.304 1.00 30.14 ? 223 VAL A O     1 
ATOM   1796  C  CB    . VAL A 1 223 ? 145.364 132.612 125.585 1.00 25.55 ? 223 VAL A CB    1 
ATOM   1797  C  CG1   . VAL A 1 223 ? 146.700 133.332 125.614 1.00 25.33 ? 223 VAL A CG1   1 
ATOM   1798  C  CG2   . VAL A 1 223 ? 145.535 131.166 125.152 1.00 26.76 ? 223 VAL A CG2   1 
ATOM   1799  N  N     . VAL A 1 224 ? 143.404 130.710 127.651 1.00 26.12 ? 224 VAL A N     1 
ATOM   1800  C  CA    . VAL A 1 224 ? 142.223 129.851 127.643 1.00 25.13 ? 224 VAL A CA    1 
ATOM   1801  C  C     . VAL A 1 224 ? 141.086 130.458 128.462 1.00 27.35 ? 224 VAL A C     1 
ATOM   1802  O  O     . VAL A 1 224 ? 139.912 130.287 128.119 1.00 30.76 ? 224 VAL A O     1 
ATOM   1803  C  CB    . VAL A 1 224 ? 142.594 128.441 128.133 1.00 32.80 ? 224 VAL A CB    1 
ATOM   1804  C  CG1   . VAL A 1 224 ? 141.372 127.538 128.152 1.00 31.84 ? 224 VAL A CG1   1 
ATOM   1805  C  CG2   . VAL A 1 224 ? 143.674 127.850 127.247 1.00 29.98 ? 224 VAL A CG2   1 
ATOM   1806  N  N     . GLY A 1 225 ? 141.399 131.177 129.542 1.00 24.21 ? 225 GLY A N     1 
ATOM   1807  C  CA    . GLY A 1 225 ? 140.353 131.877 130.271 1.00 21.80 ? 225 GLY A CA    1 
ATOM   1808  C  C     . GLY A 1 225 ? 139.698 132.965 129.442 1.00 22.65 ? 225 GLY A C     1 
ATOM   1809  O  O     . GLY A 1 225 ? 138.469 133.101 129.429 1.00 31.64 ? 225 GLY A O     1 
ATOM   1810  N  N     . VAL A 1 226 ? 140.509 133.752 128.732 1.00 20.02 ? 226 VAL A N     1 
ATOM   1811  C  CA    . VAL A 1 226 ? 139.969 134.743 127.808 1.00 20.67 ? 226 VAL A CA    1 
ATOM   1812  C  C     . VAL A 1 226 ? 139.203 134.060 126.689 1.00 24.67 ? 226 VAL A C     1 
ATOM   1813  O  O     . VAL A 1 226 ? 138.209 134.595 126.188 1.00 27.38 ? 226 VAL A O     1 
ATOM   1814  C  CB    . VAL A 1 226 ? 141.103 135.629 127.260 1.00 19.00 ? 226 VAL A CB    1 
ATOM   1815  C  CG1   . VAL A 1 226 ? 140.535 136.786 126.451 1.00 25.63 ? 226 VAL A CG1   1 
ATOM   1816  C  CG2   . VAL A 1 226 ? 141.966 136.135 128.397 1.00 21.30 ? 226 VAL A CG2   1 
ATOM   1817  N  N     . MET A 1 227 ? 139.652 132.876 126.274 1.00 28.28 ? 227 MET A N     1 
ATOM   1818  C  CA    . MET A 1 227 ? 138.943 132.116 125.253 1.00 22.10 ? 227 MET A CA    1 
ATOM   1819  C  C     . MET A 1 227 ? 137.553 131.718 125.730 1.00 22.77 ? 227 MET A C     1 
ATOM   1820  O  O     . MET A 1 227 ? 136.583 131.808 124.974 1.00 29.89 ? 227 MET A O     1 
ATOM   1821  C  CB    . MET A 1 227 ? 139.757 130.879 124.880 1.00 19.68 ? 227 MET A CB    1 
ATOM   1822  C  CG    . MET A 1 227 ? 140.833 131.132 123.847 1.00 18.07 ? 227 MET A CG    1 
ATOM   1823  S  SD    . MET A 1 227 ? 141.494 129.605 123.169 1.00 33.69 ? 227 MET A SD    1 
ATOM   1824  C  CE    . MET A 1 227 ? 140.193 129.165 122.032 1.00 30.29 ? 227 MET A CE    1 
ATOM   1825  N  N     . LYS A 1 228 ? 137.442 131.269 126.981 1.00 26.86 ? 228 LYS A N     1 
ATOM   1826  C  CA    . LYS A 1 228 ? 136.134 130.937 127.540 1.00 23.88 ? 228 LYS A CA    1 
ATOM   1827  C  C     . LYS A 1 228 ? 135.252 132.174 127.656 1.00 24.44 ? 228 LYS A C     1 
ATOM   1828  O  O     . LYS A 1 228 ? 134.051 132.124 127.352 1.00 26.12 ? 228 LYS A O     1 
ATOM   1829  C  CB    . LYS A 1 228 ? 136.297 130.270 128.904 1.00 23.81 ? 228 LYS A CB    1 
ATOM   1830  C  CG    . LYS A 1 228 ? 137.070 128.966 128.872 1.00 29.50 ? 228 LYS A CG    1 
ATOM   1831  C  CD    . LYS A 1 228 ? 137.116 128.324 130.247 1.00 37.95 ? 228 LYS A CD    1 
ATOM   1832  C  CE    . LYS A 1 228 ? 138.247 128.894 131.090 1.00 36.18 ? 228 LYS A CE    1 
ATOM   1833  N  NZ    . LYS A 1 228 ? 139.395 127.954 131.191 1.00 30.74 ? 228 LYS A NZ    1 
ATOM   1834  N  N     . LEU A 1 229 ? 135.834 133.293 128.097 1.00 24.47 ? 229 LEU A N     1 
ATOM   1835  C  CA    . LEU A 1 229 ? 135.085 134.544 128.160 1.00 21.16 ? 229 LEU A CA    1 
ATOM   1836  C  C     . LEU A 1 229 ? 134.539 134.925 126.790 1.00 21.82 ? 229 LEU A C     1 
ATOM   1837  O  O     . LEU A 1 229 ? 133.363 135.276 126.651 1.00 21.58 ? 229 LEU A O     1 
ATOM   1838  C  CB    . LEU A 1 229 ? 135.976 135.662 128.699 1.00 23.29 ? 229 LEU A CB    1 
ATOM   1839  C  CG    . LEU A 1 229 ? 136.342 135.685 130.180 1.00 22.73 ? 229 LEU A CG    1 
ATOM   1840  C  CD1   . LEU A 1 229 ? 137.486 136.654 130.387 1.00 24.03 ? 229 LEU A CD1   1 
ATOM   1841  C  CD2   . LEU A 1 229 ? 135.146 136.077 131.026 1.00 18.69 ? 229 LEU A CD2   1 
ATOM   1842  N  N     . LEU A 1 230 ? 135.386 134.854 125.762 1.00 27.54 ? 230 LEU A N     1 
ATOM   1843  C  CA    . LEU A 1 230 ? 134.967 135.211 124.412 1.00 18.31 ? 230 LEU A CA    1 
ATOM   1844  C  C     . LEU A 1 230 ? 133.939 134.228 123.870 1.00 18.68 ? 230 LEU A C     1 
ATOM   1845  O  O     . LEU A 1 230 ? 133.009 134.624 123.161 1.00 30.54 ? 230 LEU A O     1 
ATOM   1846  C  CB    . LEU A 1 230 ? 136.181 135.278 123.488 1.00 20.90 ? 230 LEU A CB    1 
ATOM   1847  C  CG    . LEU A 1 230 ? 137.098 136.484 123.682 1.00 27.60 ? 230 LEU A CG    1 
ATOM   1848  C  CD1   . LEU A 1 230 ? 138.440 136.247 123.009 1.00 27.90 ? 230 LEU A CD1   1 
ATOM   1849  C  CD2   . LEU A 1 230 ? 136.436 137.744 123.153 1.00 21.63 ? 230 LEU A CD2   1 
ATOM   1850  N  N     . ASP A 1 231 ? 134.095 132.942 124.183 1.00 21.32 ? 231 ASP A N     1 
ATOM   1851  C  CA    . ASP A 1 231 ? 133.133 131.948 123.727 1.00 24.13 ? 231 ASP A CA    1 
ATOM   1852  C  C     . ASP A 1 231 ? 131.753 132.214 124.310 1.00 29.31 ? 231 ASP A C     1 
ATOM   1853  O  O     . ASP A 1 231 ? 130.746 132.147 123.596 1.00 34.19 ? 231 ASP A O     1 
ATOM   1854  C  CB    . ASP A 1 231 ? 133.621 130.548 124.098 1.00 27.90 ? 231 ASP A CB    1 
ATOM   1855  C  CG    . ASP A 1 231 ? 132.663 129.462 123.663 1.00 37.30 ? 231 ASP A CG    1 
ATOM   1856  O  OD1   . ASP A 1 231 ? 132.512 129.254 122.442 1.00 40.42 ? 231 ASP A OD1   1 
ATOM   1857  O  OD2   . ASP A 1 231 ? 132.065 128.809 124.543 1.00 39.90 ? 231 ASP A OD2   1 
ATOM   1858  N  N     . ASN A 1 232 ? 131.685 132.544 125.601 1.00 30.32 ? 232 ASN A N     1 
ATOM   1859  C  CA    . ASN A 1 232 ? 130.388 132.874 126.184 1.00 28.34 ? 232 ASN A CA    1 
ATOM   1860  C  C     . ASN A 1 232 ? 129.862 134.214 125.689 1.00 28.85 ? 232 ASN A C     1 
ATOM   1861  O  O     . ASN A 1 232 ? 128.645 134.388 125.563 1.00 34.56 ? 232 ASN A O     1 
ATOM   1862  C  CB    . ASN A 1 232 ? 130.468 132.862 127.706 1.00 29.93 ? 232 ASN A CB    1 
ATOM   1863  C  CG    . ASN A 1 232 ? 130.290 131.478 128.274 1.00 37.00 ? 232 ASN A CG    1 
ATOM   1864  O  OD1   . ASN A 1 232 ? 131.162 130.620 128.138 1.00 39.04 ? 232 ASN A OD1   1 
ATOM   1865  N  ND2   . ASN A 1 232 ? 129.149 131.245 128.913 1.00 34.36 ? 232 ASN A ND2   1 
ATOM   1866  N  N     . ALA A 1 233 ? 130.750 135.166 125.399 1.00 27.12 ? 233 ALA A N     1 
ATOM   1867  C  CA    . ALA A 1 233 ? 130.308 136.435 124.833 1.00 18.06 ? 233 ALA A CA    1 
ATOM   1868  C  C     . ALA A 1 233 ? 129.692 136.235 123.455 1.00 31.24 ? 233 ALA A C     1 
ATOM   1869  O  O     . ALA A 1 233 ? 128.706 136.893 123.104 1.00 37.39 ? 233 ALA A O     1 
ATOM   1870  C  CB    . ALA A 1 233 ? 131.479 137.413 124.765 1.00 23.45 ? 233 ALA A CB    1 
ATOM   1871  N  N     . PHE A 1 234 ? 130.265 135.334 122.657 1.00 32.86 ? 234 PHE A N     1 
ATOM   1872  C  CA    . PHE A 1 234 ? 129.719 135.043 121.338 1.00 26.49 ? 234 PHE A CA    1 
ATOM   1873  C  C     . PHE A 1 234 ? 128.461 134.190 121.415 1.00 23.45 ? 234 PHE A C     1 
ATOM   1874  O  O     . PHE A 1 234 ? 127.575 134.325 120.565 1.00 30.17 ? 234 PHE A O     1 
ATOM   1875  C  CB    . PHE A 1 234 ? 130.778 134.362 120.472 1.00 25.73 ? 234 PHE A CB    1 
ATOM   1876  C  CG    . PHE A 1 234 ? 131.806 135.310 119.928 1.00 24.79 ? 234 PHE A CG    1 
ATOM   1877  C  CD1   . PHE A 1 234 ? 131.426 136.389 119.153 1.00 27.44 ? 234 PHE A CD1   1 
ATOM   1878  C  CD2   . PHE A 1 234 ? 133.148 135.133 120.205 1.00 24.50 ? 234 PHE A CD2   1 
ATOM   1879  C  CE1   . PHE A 1 234 ? 132.368 137.267 118.658 1.00 26.47 ? 234 PHE A CE1   1 
ATOM   1880  C  CE2   . PHE A 1 234 ? 134.093 136.009 119.718 1.00 24.69 ? 234 PHE A CE2   1 
ATOM   1881  C  CZ    . PHE A 1 234 ? 133.703 137.076 118.942 1.00 27.24 ? 234 PHE A CZ    1 
ATOM   1882  N  N     . ARG A 1 235 ? 128.363 133.305 122.409 1.00 31.94 ? 235 ARG A N     1 
ATOM   1883  C  CA    . ARG A 1 235 ? 127.108 132.595 122.628 1.00 27.19 ? 235 ARG A CA    1 
ATOM   1884  C  C     . ARG A 1 235 ? 125.992 133.543 123.042 1.00 33.18 ? 235 ARG A C     1 
ATOM   1885  O  O     . ARG A 1 235 ? 124.838 133.345 122.648 1.00 39.94 ? 235 ARG A O     1 
ATOM   1886  C  CB    . ARG A 1 235 ? 127.282 131.503 123.679 1.00 23.83 ? 235 ARG A CB    1 
ATOM   1887  C  CG    . ARG A 1 235 ? 127.182 130.102 123.115 1.00 35.61 ? 235 ARG A CG    1 
ATOM   1888  C  CD    . ARG A 1 235 ? 126.847 129.081 124.194 1.00 38.30 ? 235 ARG A CD    1 
ATOM   1889  N  NE    . ARG A 1 235 ? 127.737 129.133 125.349 1.00 36.57 ? 235 ARG A NE    1 
ATOM   1890  C  CZ    . ARG A 1 235 ? 129.051 128.950 125.311 1.00 36.91 ? 235 ARG A CZ    1 
ATOM   1891  N  NH1   . ARG A 1 235 ? 129.680 128.658 124.184 1.00 35.00 ? 235 ARG A NH1   1 
ATOM   1892  N  NH2   . ARG A 1 235 ? 129.750 129.039 126.438 1.00 34.16 ? 235 ARG A NH2   1 
ATOM   1893  N  N     . TYR A 1 236 ? 126.308 134.562 123.842 1.00 29.53 ? 236 TYR A N     1 
ATOM   1894  C  CA    . TYR A 1 236 ? 125.281 135.507 124.264 1.00 27.32 ? 236 TYR A CA    1 
ATOM   1895  C  C     . TYR A 1 236 ? 124.797 136.354 123.094 1.00 27.65 ? 236 TYR A C     1 
ATOM   1896  O  O     . TYR A 1 236 ? 123.589 136.505 122.882 1.00 32.99 ? 236 TYR A O     1 
ATOM   1897  C  CB    . TYR A 1 236 ? 125.814 136.397 125.384 1.00 27.34 ? 236 TYR A CB    1 
ATOM   1898  C  CG    . TYR A 1 236 ? 124.773 137.336 125.936 1.00 30.58 ? 236 TYR A CG    1 
ATOM   1899  C  CD1   . TYR A 1 236 ? 123.745 136.861 126.734 1.00 27.37 ? 236 TYR A CD1   1 
ATOM   1900  C  CD2   . TYR A 1 236 ? 124.808 138.694 125.650 1.00 30.81 ? 236 TYR A CD2   1 
ATOM   1901  C  CE1   . TYR A 1 236 ? 122.788 137.706 127.238 1.00 30.18 ? 236 TYR A CE1   1 
ATOM   1902  C  CE2   . TYR A 1 236 ? 123.851 139.550 126.152 1.00 24.49 ? 236 TYR A CE2   1 
ATOM   1903  C  CZ    . TYR A 1 236 ? 122.845 139.048 126.947 1.00 25.22 ? 236 TYR A CZ    1 
ATOM   1904  O  OH    . TYR A 1 236 ? 121.884 139.884 127.456 1.00 28.90 ? 236 TYR A OH    1 
ATOM   1905  N  N     . ALA A 1 237 ? 125.726 136.920 122.324 1.00 31.31 ? 237 ALA A N     1 
ATOM   1906  C  CA    . ALA A 1 237 ? 125.379 137.756 121.177 1.00 33.47 ? 237 ALA A CA    1 
ATOM   1907  C  C     . ALA A 1 237 ? 125.247 136.858 119.951 1.00 38.41 ? 237 ALA A C     1 
ATOM   1908  O  O     . ALA A 1 237 ? 126.170 136.695 119.150 1.00 38.45 ? 237 ALA A O     1 
ATOM   1909  C  CB    . ALA A 1 237 ? 126.417 138.852 120.975 1.00 31.50 ? 237 ALA A CB    1 
ATOM   1910  N  N     . ASP A 1 238 ? 124.066 136.260 119.813 1.00 53.76 ? 238 ASP A N     1 
ATOM   1911  C  CA    . ASP A 1 238 ? 123.800 135.294 118.758 1.00 56.57 ? 238 ASP A CA    1 
ATOM   1912  C  C     . ASP A 1 238 ? 122.720 135.741 117.782 1.00 59.45 ? 238 ASP A C     1 
ATOM   1913  O  O     . ASP A 1 238 ? 122.412 134.997 116.846 1.00 61.91 ? 238 ASP A O     1 
ATOM   1914  C  CB    . ASP A 1 238 ? 123.410 133.945 119.371 1.00 55.67 ? 238 ASP A CB    1 
ATOM   1915  C  CG    . ASP A 1 238 ? 122.168 134.035 120.234 1.00 58.85 ? 238 ASP A CG    1 
ATOM   1916  O  OD1   . ASP A 1 238 ? 121.830 135.152 120.678 1.00 58.73 ? 238 ASP A OD1   1 
ATOM   1917  O  OD2   . ASP A 1 238 ? 121.529 132.989 120.467 1.00 61.56 ? 238 ASP A OD2   1 
ATOM   1918  N  N     . GLN A 1 239 ? 122.136 136.927 117.975 1.00 61.25 ? 239 GLN A N     1 
ATOM   1919  C  CA    . GLN A 1 239 ? 121.130 137.488 117.070 1.00 62.46 ? 239 GLN A CA    1 
ATOM   1920  C  C     . GLN A 1 239 ? 119.953 136.523 116.897 1.00 63.56 ? 239 GLN A C     1 
ATOM   1921  O  O     . GLN A 1 239 ? 119.732 135.950 115.827 1.00 64.19 ? 239 GLN A O     1 
ATOM   1922  C  CB    . GLN A 1 239 ? 121.745 137.838 115.709 1.00 61.46 ? 239 GLN A CB    1 
ATOM   1923  C  CG    . GLN A 1 239 ? 123.142 138.418 115.771 1.00 59.51 ? 239 GLN A CG    1 
ATOM   1924  C  CD    . GLN A 1 239 ? 123.895 138.211 114.476 1.00 62.95 ? 239 GLN A CD    1 
ATOM   1925  O  OE1   . GLN A 1 239 ? 125.047 137.777 114.476 1.00 62.17 ? 239 GLN A OE1   1 
ATOM   1926  N  NE2   . GLN A 1 239 ? 123.246 138.519 113.360 1.00 62.14 ? 239 GLN A NE2   1 
ATOM   1927  N  N     . MET A 1 240 ? 119.236 136.324 118.008 1.00 72.59 ? 240 MET A N     1 
ATOM   1928  C  CA    . MET A 1 240 ? 118.054 135.465 118.071 1.00 74.38 ? 240 MET A CA    1 
ATOM   1929  C  C     . MET A 1 240 ? 118.437 133.989 117.991 1.00 74.11 ? 240 MET A C     1 
ATOM   1930  O  O     . MET A 1 240 ? 117.600 133.108 118.210 1.00 76.49 ? 240 MET A O     1 
ATOM   1931  C  CB    . MET A 1 240 ? 117.062 135.828 116.955 1.00 74.52 ? 240 MET A CB    1 
ATOM   1932  C  CG    . MET A 1 240 ? 115.735 135.084 116.988 1.00 73.76 ? 240 MET A CG    1 
ATOM   1933  S  SD    . MET A 1 240 ? 114.292 136.137 116.802 1.00 81.23 ? 240 MET A SD    1 
ATOM   1934  C  CE    . MET A 1 240 ? 112.988 134.910 116.881 1.00 74.57 ? 240 MET A CE    1 
ATOM   1935  N  N     . GLY A 1 241 ? 119.708 133.706 117.723 1.00 72.86 ? 241 GLY A N     1 
ATOM   1936  C  CA    . GLY A 1 241 ? 120.143 132.349 117.485 1.00 72.84 ? 241 GLY A CA    1 
ATOM   1937  C  C     . GLY A 1 241 ? 119.950 131.861 116.067 1.00 75.46 ? 241 GLY A C     1 
ATOM   1938  O  O     . GLY A 1 241 ? 120.331 130.722 115.766 1.00 74.63 ? 241 GLY A O     1 
ATOM   1939  N  N     . GLN A 1 242 ? 119.363 132.680 115.189 1.00 78.67 ? 242 GLN A N     1 
ATOM   1940  C  CA    . GLN A 1 242 ? 119.240 132.302 113.784 1.00 78.03 ? 242 GLN A CA    1 
ATOM   1941  C  C     . GLN A 1 242 ? 120.612 132.064 113.171 1.00 79.99 ? 242 GLN A C     1 
ATOM   1942  O  O     . GLN A 1 242 ? 120.839 131.058 112.488 1.00 79.13 ? 242 GLN A O     1 
ATOM   1943  C  CB    . GLN A 1 242 ? 118.488 133.389 113.015 1.00 77.76 ? 242 GLN A CB    1 
ATOM   1944  C  CG    . GLN A 1 242 ? 116.976 133.336 113.160 1.00 79.20 ? 242 GLN A CG    1 
ATOM   1945  C  CD    . GLN A 1 242 ? 116.266 134.206 112.142 1.00 79.22 ? 242 GLN A CD    1 
ATOM   1946  O  OE1   . GLN A 1 242 ? 116.902 134.836 111.296 1.00 78.36 ? 242 GLN A OE1   1 
ATOM   1947  N  NE2   . GLN A 1 242 ? 114.942 134.247 112.219 1.00 78.97 ? 242 GLN A NE2   1 
ATOM   1948  N  N     . ARG A 1 243 ? 121.542 132.985 113.410 1.00 67.78 ? 243 ARG A N     1 
ATOM   1949  C  CA    . ARG A 1 243 ? 122.954 132.800 113.094 1.00 64.80 ? 243 ARG A CA    1 
ATOM   1950  C  C     . ARG A 1 243 ? 123.733 133.103 114.365 1.00 65.58 ? 243 ARG A C     1 
ATOM   1951  O  O     . ARG A 1 243 ? 123.967 134.273 114.686 1.00 64.80 ? 243 ARG A O     1 
ATOM   1952  C  CB    . ARG A 1 243 ? 123.400 133.707 111.948 1.00 64.07 ? 243 ARG A CB    1 
ATOM   1953  C  CG    . ARG A 1 243 ? 124.812 133.424 111.456 1.00 65.13 ? 243 ARG A CG    1 
ATOM   1954  C  CD    . ARG A 1 243 ? 125.631 134.699 111.341 1.00 64.45 ? 243 ARG A CD    1 
ATOM   1955  N  NE    . ARG A 1 243 ? 125.963 135.249 112.650 1.00 66.50 ? 243 ARG A NE    1 
ATOM   1956  C  CZ    . ARG A 1 243 ? 127.049 135.963 112.911 1.00 63.10 ? 243 ARG A CZ    1 
ATOM   1957  N  NH1   . ARG A 1 243 ? 127.943 136.230 111.973 1.00 61.92 ? 243 ARG A NH1   1 
ATOM   1958  N  NH2   . ARG A 1 243 ? 127.245 136.419 114.145 1.00 59.89 ? 243 ARG A NH2   1 
ATOM   1959  N  N     . GLN A 1 244 ? 124.130 132.056 115.084 1.00 62.15 ? 244 GLN A N     1 
ATOM   1960  C  CA    . GLN A 1 244 ? 124.779 132.237 116.374 1.00 61.07 ? 244 GLN A CA    1 
ATOM   1961  C  C     . GLN A 1 244 ? 126.095 132.990 116.213 1.00 61.80 ? 244 GLN A C     1 
ATOM   1962  O  O     . GLN A 1 244 ? 126.715 132.985 115.145 1.00 59.60 ? 244 GLN A O     1 
ATOM   1963  C  CB    . GLN A 1 244 ? 125.023 130.884 117.047 1.00 59.96 ? 244 GLN A CB    1 
ATOM   1964  C  CG    . GLN A 1 244 ? 126.276 130.159 116.579 1.00 61.24 ? 244 GLN A CG    1 
ATOM   1965  C  CD    . GLN A 1 244 ? 126.172 129.674 115.146 1.00 63.62 ? 244 GLN A CD    1 
ATOM   1966  O  OE1   . GLN A 1 244 ? 125.076 129.463 114.627 1.00 63.03 ? 244 GLN A OE1   1 
ATOM   1967  N  NE2   . GLN A 1 244 ? 127.318 129.496 114.498 1.00 60.62 ? 244 GLN A NE2   1 
ATOM   1968  N  N     . GLY A 1 245 ? 126.506 133.662 117.286 1.00 51.97 ? 245 GLY A N     1 
ATOM   1969  C  CA    . GLY A 1 245 ? 127.721 134.450 117.266 1.00 45.06 ? 245 GLY A CA    1 
ATOM   1970  C  C     . GLY A 1 245 ? 128.943 133.629 116.918 1.00 45.01 ? 245 GLY A C     1 
ATOM   1971  O  O     . GLY A 1 245 ? 129.230 132.618 117.566 1.00 45.50 ? 245 GLY A O     1 
ATOM   1972  N  N     . SER A 1 246 ? 129.668 134.055 115.891 1.00 39.57 ? 246 SER A N     1 
ATOM   1973  C  CA    . SER A 1 246 ? 130.839 133.344 115.402 1.00 34.46 ? 246 SER A CA    1 
ATOM   1974  C  C     . SER A 1 246 ? 132.085 134.161 115.702 1.00 32.15 ? 246 SER A C     1 
ATOM   1975  O  O     . SER A 1 246 ? 132.186 135.324 115.297 1.00 27.19 ? 246 SER A O     1 
ATOM   1976  C  CB    . SER A 1 246 ? 130.730 133.075 113.900 1.00 32.91 ? 246 SER A CB    1 
ATOM   1977  O  OG    . SER A 1 246 ? 129.723 132.118 113.627 1.00 42.35 ? 246 SER A OG    1 
ATOM   1978  N  N     . GLY A 1 247 ? 133.030 133.548 116.410 1.00 25.78 ? 247 GLY A N     1 
ATOM   1979  C  CA    . GLY A 1 247 ? 134.276 134.200 116.728 1.00 12.32 ? 247 GLY A CA    1 
ATOM   1980  C  C     . GLY A 1 247 ? 135.452 133.316 116.365 1.00 16.06 ? 247 GLY A C     1 
ATOM   1981  O  O     . GLY A 1 247 ? 135.332 132.099 116.236 1.00 23.19 ? 247 GLY A O     1 
ATOM   1982  N  N     . ALA A 1 248 ? 136.597 133.962 116.190 1.00 20.06 ? 248 ALA A N     1 
ATOM   1983  C  CA    . ALA A 1 248 ? 137.853 133.275 115.944 1.00 16.64 ? 248 ALA A CA    1 
ATOM   1984  C  C     . ALA A 1 248 ? 138.911 133.834 116.878 1.00 12.74 ? 248 ALA A C     1 
ATOM   1985  O  O     . ALA A 1 248 ? 138.953 135.040 117.133 1.00 21.28 ? 248 ALA A O     1 
ATOM   1986  C  CB    . ALA A 1 248 ? 138.305 133.421 114.487 1.00 9.31  ? 248 ALA A CB    1 
ATOM   1987  N  N     . ALA A 1 249 ? 139.755 132.952 117.396 1.00 17.69 ? 249 ALA A N     1 
ATOM   1988  C  CA    . ALA A 1 249 ? 140.891 133.339 118.215 1.00 10.86 ? 249 ALA A CA    1 
ATOM   1989  C  C     . ALA A 1 249 ? 142.167 132.906 117.514 1.00 8.61  ? 249 ALA A C     1 
ATOM   1990  O  O     . ALA A 1 249 ? 142.235 131.810 116.952 1.00 18.75 ? 249 ALA A O     1 
ATOM   1991  C  CB    . ALA A 1 249 ? 140.814 132.718 119.611 1.00 13.75 ? 249 ALA A CB    1 
ATOM   1992  N  N     . TYR A 1 250 ? 143.170 133.771 117.532 1.00 10.85 ? 250 TYR A N     1 
ATOM   1993  C  CA    . TYR A 1 250 ? 144.447 133.480 116.905 1.00 7.52  ? 250 TYR A CA    1 
ATOM   1994  C  C     . TYR A 1 250 ? 145.554 133.558 117.943 1.00 8.66  ? 250 TYR A C     1 
ATOM   1995  O  O     . TYR A 1 250 ? 145.575 134.466 118.778 1.00 12.58 ? 250 TYR A O     1 
ATOM   1996  C  CB    . TYR A 1 250 ? 144.734 134.444 115.754 1.00 10.55 ? 250 TYR A CB    1 
ATOM   1997  C  CG    . TYR A 1 250 ? 144.109 134.024 114.445 1.00 19.15 ? 250 TYR A CG    1 
ATOM   1998  C  CD1   . TYR A 1 250 ? 142.761 134.237 114.199 1.00 8.69  ? 250 TYR A CD1   1 
ATOM   1999  C  CD2   . TYR A 1 250 ? 144.864 133.399 113.462 1.00 13.37 ? 250 TYR A CD2   1 
ATOM   2000  C  CE1   . TYR A 1 250 ? 142.185 133.850 113.010 1.00 0.00  ? 250 TYR A CE1   1 
ATOM   2001  C  CE2   . TYR A 1 250 ? 144.295 133.010 112.268 1.00 7.88  ? 250 TYR A CE2   1 
ATOM   2002  C  CZ    . TYR A 1 250 ? 142.955 133.236 112.049 1.00 7.01  ? 250 TYR A CZ    1 
ATOM   2003  O  OH    . TYR A 1 250 ? 142.378 132.853 110.862 1.00 22.13 ? 250 TYR A OH    1 
ATOM   2004  N  N     . LEU A 1 251 ? 146.463 132.593 117.889 1.00 10.76 ? 251 LEU A N     1 
ATOM   2005  C  CA    . LEU A 1 251 ? 147.610 132.547 118.778 1.00 13.35 ? 251 LEU A CA    1 
ATOM   2006  C  C     . LEU A 1 251 ? 148.860 132.239 117.972 1.00 12.62 ? 251 LEU A C     1 
ATOM   2007  O  O     . LEU A 1 251 ? 148.848 131.366 117.101 1.00 17.92 ? 251 LEU A O     1 
ATOM   2008  C  CB    . LEU A 1 251 ? 147.428 131.497 119.874 1.00 18.67 ? 251 LEU A CB    1 
ATOM   2009  C  CG    . LEU A 1 251 ? 148.182 131.777 121.172 1.00 14.33 ? 251 LEU A CG    1 
ATOM   2010  C  CD1   . LEU A 1 251 ? 147.466 132.841 121.977 1.00 17.12 ? 251 LEU A CD1   1 
ATOM   2011  C  CD2   . LEU A 1 251 ? 148.344 130.510 121.982 1.00 12.60 ? 251 LEU A CD2   1 
ATOM   2012  N  N     . ASN A 1 252 ? 149.933 132.967 118.261 1.00 13.11 ? 252 ASN A N     1 
ATOM   2013  C  CA    . ASN A 1 252 ? 151.223 132.650 117.671 1.00 13.27 ? 252 ASN A CA    1 
ATOM   2014  C  C     . ASN A 1 252 ? 151.712 131.305 118.191 1.00 18.01 ? 252 ASN A C     1 
ATOM   2015  O  O     . ASN A 1 252 ? 151.525 130.968 119.363 1.00 24.66 ? 252 ASN A O     1 
ATOM   2016  C  CB    . ASN A 1 252 ? 152.237 133.748 117.987 1.00 16.50 ? 252 ASN A CB    1 
ATOM   2017  C  CG    . ASN A 1 252 ? 153.493 133.639 117.152 1.00 20.75 ? 252 ASN A CG    1 
ATOM   2018  O  OD1   . ASN A 1 252 ? 154.446 132.962 117.533 1.00 26.03 ? 252 ASN A OD1   1 
ATOM   2019  N  ND2   . ASN A 1 252 ? 153.501 134.302 116.004 1.00 15.78 ? 252 ASN A ND2   1 
ATOM   2020  N  N     . ILE A 1 253 ? 152.339 130.527 117.305 1.00 15.47 ? 253 ILE A N     1 
ATOM   2021  C  CA    . ILE A 1 253 ? 152.782 129.189 117.670 1.00 14.77 ? 253 ILE A CA    1 
ATOM   2022  C  C     . ILE A 1 253 ? 153.864 129.220 118.743 1.00 20.07 ? 253 ILE A C     1 
ATOM   2023  O  O     . ILE A 1 253 ? 154.086 128.213 119.424 1.00 23.71 ? 253 ILE A O     1 
ATOM   2024  C  CB    . ILE A 1 253 ? 153.260 128.434 116.415 1.00 17.18 ? 253 ILE A CB    1 
ATOM   2025  C  CG1   . ILE A 1 253 ? 153.294 126.927 116.674 1.00 19.60 ? 253 ILE A CG1   1 
ATOM   2026  C  CG2   . ILE A 1 253 ? 154.618 128.944 115.960 1.00 14.28 ? 253 ILE A CG2   1 
ATOM   2027  C  CD1   . ILE A 1 253 ? 152.780 126.101 115.525 1.00 17.40 ? 253 ILE A CD1   1 
ATOM   2028  N  N     . PHE A 1 254 ? 154.538 130.353 118.923 1.00 22.59 ? 254 PHE A N     1 
ATOM   2029  C  CA    . PHE A 1 254 ? 155.571 130.493 119.939 1.00 20.32 ? 254 PHE A CA    1 
ATOM   2030  C  C     . PHE A 1 254 ? 155.028 130.995 121.268 1.00 20.68 ? 254 PHE A C     1 
ATOM   2031  O  O     . PHE A 1 254 ? 155.806 131.192 122.206 1.00 28.07 ? 254 PHE A O     1 
ATOM   2032  C  CB    . PHE A 1 254 ? 156.674 131.426 119.437 1.00 23.64 ? 254 PHE A CB    1 
ATOM   2033  C  CG    . PHE A 1 254 ? 157.635 130.768 118.492 1.00 23.61 ? 254 PHE A CG    1 
ATOM   2034  C  CD1   . PHE A 1 254 ? 158.484 129.771 118.934 1.00 25.48 ? 254 PHE A CD1   1 
ATOM   2035  C  CD2   . PHE A 1 254 ? 157.678 131.134 117.159 1.00 24.39 ? 254 PHE A CD2   1 
ATOM   2036  C  CE1   . PHE A 1 254 ? 159.367 129.159 118.068 1.00 24.03 ? 254 PHE A CE1   1 
ATOM   2037  C  CE2   . PHE A 1 254 ? 158.560 130.523 116.289 1.00 28.24 ? 254 PHE A CE2   1 
ATOM   2038  C  CZ    . PHE A 1 254 ? 159.405 129.535 116.745 1.00 25.82 ? 254 PHE A CZ    1 
ATOM   2039  N  N     . HIS A 1 255 ? 153.722 131.218 121.366 1.00 22.55 ? 255 HIS A N     1 
ATOM   2040  C  CA    . HIS A 1 255 ? 153.097 131.494 122.649 1.00 22.09 ? 255 HIS A CA    1 
ATOM   2041  C  C     . HIS A 1 255 ? 153.167 130.254 123.530 1.00 24.25 ? 255 HIS A C     1 
ATOM   2042  O  O     . HIS A 1 255 ? 153.026 129.127 123.051 1.00 28.09 ? 255 HIS A O     1 
ATOM   2043  C  CB    . HIS A 1 255 ? 151.643 131.919 122.443 1.00 23.41 ? 255 HIS A CB    1 
ATOM   2044  C  CG    . HIS A 1 255 ? 151.051 132.665 123.598 1.00 19.83 ? 255 HIS A CG    1 
ATOM   2045  N  ND1   . HIS A 1 255 ? 150.664 132.045 124.765 1.00 15.32 ? 255 HIS A ND1   1 
ATOM   2046  C  CD2   . HIS A 1 255 ? 150.753 133.976 123.752 1.00 17.54 ? 255 HIS A CD2   1 
ATOM   2047  C  CE1   . HIS A 1 255 ? 150.170 132.945 125.596 1.00 17.30 ? 255 HIS A CE1   1 
ATOM   2048  N  NE2   . HIS A 1 255 ? 150.210 134.124 125.004 1.00 16.91 ? 255 HIS A NE2   1 
ATOM   2049  N  N     . ARG A 1 256 ? 153.400 130.464 124.827 1.00 23.73 ? 256 ARG A N     1 
ATOM   2050  C  CA    . ARG A 1 256 ? 153.505 129.334 125.744 1.00 26.03 ? 256 ARG A CA    1 
ATOM   2051  C  C     . ARG A 1 256 ? 152.196 128.563 125.844 1.00 26.12 ? 256 ARG A C     1 
ATOM   2052  O  O     . ARG A 1 256 ? 152.207 127.339 126.020 1.00 31.71 ? 256 ARG A O     1 
ATOM   2053  C  CB    . ARG A 1 256 ? 153.940 129.818 127.125 1.00 27.84 ? 256 ARG A CB    1 
ATOM   2054  C  CG    . ARG A 1 256 ? 154.184 128.700 128.116 1.00 29.30 ? 256 ARG A CG    1 
ATOM   2055  C  CD    . ARG A 1 256 ? 153.247 128.798 129.305 1.00 29.87 ? 256 ARG A CD    1 
ATOM   2056  N  NE    . ARG A 1 256 ? 151.981 128.118 129.072 1.00 31.02 ? 256 ARG A NE    1 
ATOM   2057  C  CZ    . ARG A 1 256 ? 151.721 126.873 129.447 1.00 34.44 ? 256 ARG A CZ    1 
ATOM   2058  N  NH1   . ARG A 1 256 ? 152.625 126.137 130.072 1.00 33.56 ? 256 ARG A NH1   1 
ATOM   2059  N  NH2   . ARG A 1 256 ? 150.525 126.353 129.187 1.00 30.91 ? 256 ARG A NH2   1 
ATOM   2060  N  N     . ASP A 1 257 ? 151.064 129.251 125.726 1.00 23.08 ? 257 ASP A N     1 
ATOM   2061  C  CA    . ASP A 1 257 ? 149.750 128.635 125.833 1.00 20.36 ? 257 ASP A CA    1 
ATOM   2062  C  C     . ASP A 1 257 ? 149.311 127.930 124.559 1.00 23.94 ? 257 ASP A C     1 
ATOM   2063  O  O     . ASP A 1 257 ? 148.122 127.622 124.436 1.00 29.79 ? 257 ASP A O     1 
ATOM   2064  C  CB    . ASP A 1 257 ? 148.704 129.685 126.211 1.00 25.31 ? 257 ASP A CB    1 
ATOM   2065  C  CG    . ASP A 1 257 ? 148.805 130.118 127.653 1.00 32.30 ? 257 ASP A CG    1 
ATOM   2066  O  OD1   . ASP A 1 257 ? 149.513 129.449 128.434 1.00 33.80 ? 257 ASP A OD1   1 
ATOM   2067  O  OD2   . ASP A 1 257 ? 148.169 131.128 128.006 1.00 33.10 ? 257 ASP A OD2   1 
ATOM   2068  N  N     . ILE A 1 258 ? 150.220 127.668 123.618 1.00 24.80 ? 258 ILE A N     1 
ATOM   2069  C  CA    . ILE A 1 258 ? 149.811 127.127 122.325 1.00 21.78 ? 258 ILE A CA    1 
ATOM   2070  C  C     . ILE A 1 258 ? 149.206 125.736 122.485 1.00 21.25 ? 258 ILE A C     1 
ATOM   2071  O  O     . ILE A 1 258 ? 148.229 125.392 121.812 1.00 27.09 ? 258 ILE A O     1 
ATOM   2072  C  CB    . ILE A 1 258 ? 150.996 127.132 121.338 1.00 24.81 ? 258 ILE A CB    1 
ATOM   2073  C  CG1   . ILE A 1 258 ? 150.539 126.673 119.950 1.00 22.54 ? 258 ILE A CG1   1 
ATOM   2074  C  CG2   . ILE A 1 258 ? 152.150 126.278 121.846 1.00 18.33 ? 258 ILE A CG2   1 
ATOM   2075  C  CD1   . ILE A 1 258 ? 149.536 127.599 119.300 1.00 18.00 ? 258 ILE A CD1   1 
ATOM   2076  N  N     . ASN A 1 259 ? 149.763 124.919 123.380 1.00 32.24 ? 259 ASN A N     1 
ATOM   2077  C  CA    . ASN A 1 259 ? 149.235 123.572 123.568 1.00 26.12 ? 259 ASN A CA    1 
ATOM   2078  C  C     . ASN A 1 259 ? 147.864 123.602 124.232 1.00 30.68 ? 259 ASN A C     1 
ATOM   2079  O  O     . ASN A 1 259 ? 146.962 122.857 123.835 1.00 35.82 ? 259 ASN A O     1 
ATOM   2080  C  CB    . ASN A 1 259 ? 150.218 122.736 124.382 1.00 30.10 ? 259 ASN A CB    1 
ATOM   2081  C  CG    . ASN A 1 259 ? 151.514 122.482 123.642 1.00 35.09 ? 259 ASN A CG    1 
ATOM   2082  O  OD1   . ASN A 1 259 ? 151.535 121.792 122.624 1.00 34.29 ? 259 ASN A OD1   1 
ATOM   2083  N  ND2   . ASN A 1 259 ? 152.604 123.045 124.148 1.00 35.83 ? 259 ASN A ND2   1 
ATOM   2084  N  N     . ASP A 1 260 ? 147.687 124.455 125.243 1.00 29.98 ? 260 ASP A N     1 
ATOM   2085  C  CA    . ASP A 1 260 ? 146.364 124.629 125.834 1.00 25.49 ? 260 ASP A CA    1 
ATOM   2086  C  C     . ASP A 1 260 ? 145.404 125.296 124.860 1.00 26.89 ? 260 ASP A C     1 
ATOM   2087  O  O     . ASP A 1 260 ? 144.202 125.011 124.882 1.00 35.33 ? 260 ASP A O     1 
ATOM   2088  C  CB    . ASP A 1 260 ? 146.464 125.444 127.122 1.00 27.09 ? 260 ASP A CB    1 
ATOM   2089  C  CG    . ASP A 1 260 ? 147.586 124.974 128.024 1.00 39.65 ? 260 ASP A CG    1 
ATOM   2090  O  OD1   . ASP A 1 260 ? 147.720 123.748 128.221 1.00 37.70 ? 260 ASP A OD1   1 
ATOM   2091  O  OD2   . ASP A 1 260 ? 148.335 125.832 128.537 1.00 39.71 ? 260 ASP A OD2   1 
ATOM   2092  N  N     . PHE A 1 261 ? 145.916 126.193 124.015 1.00 31.69 ? 261 PHE A N     1 
ATOM   2093  C  CA    . PHE A 1 261 ? 145.095 126.814 122.982 1.00 22.59 ? 261 PHE A CA    1 
ATOM   2094  C  C     . PHE A 1 261 ? 144.556 125.770 122.014 1.00 22.08 ? 261 PHE A C     1 
ATOM   2095  O  O     . PHE A 1 261 ? 143.388 125.824 121.614 1.00 24.53 ? 261 PHE A O     1 
ATOM   2096  C  CB    . PHE A 1 261 ? 145.926 127.871 122.251 1.00 15.35 ? 261 PHE A CB    1 
ATOM   2097  C  CG    . PHE A 1 261 ? 145.219 128.543 121.110 1.00 22.65 ? 261 PHE A CG    1 
ATOM   2098  C  CD1   . PHE A 1 261 ? 144.385 129.620 121.337 1.00 21.94 ? 261 PHE A CD1   1 
ATOM   2099  C  CD2   . PHE A 1 261 ? 145.428 128.130 119.806 1.00 25.59 ? 261 PHE A CD2   1 
ATOM   2100  C  CE1   . PHE A 1 261 ? 143.746 130.253 120.291 1.00 15.31 ? 261 PHE A CE1   1 
ATOM   2101  C  CE2   . PHE A 1 261 ? 144.791 128.760 118.758 1.00 20.21 ? 261 PHE A CE2   1 
ATOM   2102  C  CZ    . PHE A 1 261 ? 143.952 129.825 119.002 1.00 13.62 ? 261 PHE A CZ    1 
ATOM   2103  N  N     . LEU A 1 262 ? 145.397 124.807 121.630 1.00 27.57 ? 262 LEU A N     1 
ATOM   2104  C  CA    . LEU A 1 262 ? 144.966 123.737 120.739 1.00 23.14 ? 262 LEU A CA    1 
ATOM   2105  C  C     . LEU A 1 262 ? 144.105 122.701 121.450 1.00 31.22 ? 262 LEU A C     1 
ATOM   2106  O  O     . LEU A 1 262 ? 143.246 122.080 120.816 1.00 35.18 ? 262 LEU A O     1 
ATOM   2107  C  CB    . LEU A 1 262 ? 146.182 123.056 120.112 1.00 26.74 ? 262 LEU A CB    1 
ATOM   2108  C  CG    . LEU A 1 262 ? 147.071 123.933 119.233 1.00 24.31 ? 262 LEU A CG    1 
ATOM   2109  C  CD1   . LEU A 1 262 ? 148.327 123.178 118.843 1.00 25.85 ? 262 LEU A CD1   1 
ATOM   2110  C  CD2   . LEU A 1 262 ? 146.316 124.403 118.005 1.00 22.54 ? 262 LEU A CD2   1 
ATOM   2111  N  N     . ASP A 1 263 ? 144.316 122.498 122.752 1.00 38.75 ? 263 ASP A N     1 
ATOM   2112  C  CA    . ASP A 1 263 ? 143.542 121.510 123.493 1.00 31.30 ? 263 ASP A CA    1 
ATOM   2113  C  C     . ASP A 1 263 ? 142.084 121.908 123.670 1.00 32.19 ? 263 ASP A C     1 
ATOM   2114  O  O     . ASP A 1 263 ? 141.277 121.064 124.071 1.00 42.05 ? 263 ASP A O     1 
ATOM   2115  C  CB    . ASP A 1 263 ? 144.173 121.262 124.864 1.00 33.85 ? 263 ASP A CB    1 
ATOM   2116  C  CG    . ASP A 1 263 ? 145.453 120.461 124.779 1.00 40.62 ? 263 ASP A CG    1 
ATOM   2117  O  OD1   . ASP A 1 263 ? 145.692 119.832 123.728 1.00 36.82 ? 263 ASP A OD1   1 
ATOM   2118  O  OD2   . ASP A 1 263 ? 146.222 120.461 125.763 1.00 42.36 ? 263 ASP A OD2   1 
ATOM   2119  N  N     . THR A 1 264 ? 141.727 123.162 123.390 1.00 37.06 ? 264 THR A N     1 
ATOM   2120  C  CA    . THR A 1 264 ? 140.333 123.578 123.457 1.00 36.92 ? 264 THR A CA    1 
ATOM   2121  C  C     . THR A 1 264 ? 139.492 122.993 122.332 1.00 38.53 ? 264 THR A C     1 
ATOM   2122  O  O     . THR A 1 264 ? 138.260 123.050 122.410 1.00 42.07 ? 264 THR A O     1 
ATOM   2123  C  CB    . THR A 1 264 ? 140.234 125.105 123.429 1.00 38.15 ? 264 THR A CB    1 
ATOM   2124  O  OG1   . THR A 1 264 ? 140.802 125.601 122.211 1.00 41.54 ? 264 THR A OG1   1 
ATOM   2125  C  CG2   . THR A 1 264 ? 140.974 125.710 124.609 1.00 33.22 ? 264 THR A CG2   1 
ATOM   2126  N  N     . LYS A 1 265 ? 140.119 122.436 121.298 1.00 34.83 ? 265 LYS A N     1 
ATOM   2127  C  CA    . LYS A 1 265 ? 139.408 121.851 120.171 1.00 39.18 ? 265 LYS A CA    1 
ATOM   2128  C  C     . LYS A 1 265 ? 139.452 120.331 120.157 1.00 38.95 ? 265 LYS A C     1 
ATOM   2129  O  O     . LYS A 1 265 ? 138.847 119.718 119.271 1.00 42.11 ? 265 LYS A O     1 
ATOM   2130  C  CB    . LYS A 1 265 ? 139.970 122.392 118.852 1.00 37.97 ? 265 LYS A CB    1 
ATOM   2131  C  CG    . LYS A 1 265 ? 139.467 123.773 118.494 1.00 37.93 ? 265 LYS A CG    1 
ATOM   2132  C  CD    . LYS A 1 265 ? 137.978 123.891 118.736 1.00 39.03 ? 265 LYS A CD    1 
ATOM   2133  C  CE    . LYS A 1 265 ? 137.461 125.239 118.292 1.00 37.52 ? 265 LYS A CE    1 
ATOM   2134  N  NZ    . LYS A 1 265 ? 136.078 125.485 118.779 1.00 42.31 ? 265 LYS A NZ    1 
ATOM   2135  N  N     . LYS A 1 266 ? 140.153 119.708 121.099 1.00 41.25 ? 266 LYS A N     1 
ATOM   2136  C  CA    . LYS A 1 266 ? 140.175 118.256 121.167 1.00 45.41 ? 266 LYS A CA    1 
ATOM   2137  C  C     . LYS A 1 266 ? 138.798 117.717 121.536 1.00 50.73 ? 266 LYS A C     1 
ATOM   2138  O  O     . LYS A 1 266 ? 138.047 118.333 122.297 1.00 51.86 ? 266 LYS A O     1 
ATOM   2139  C  CB    . LYS A 1 266 ? 141.216 117.780 122.179 1.00 44.47 ? 266 LYS A CB    1 
ATOM   2140  C  CG    . LYS A 1 266 ? 142.635 117.758 121.640 1.00 46.01 ? 266 LYS A CG    1 
ATOM   2141  C  CD    . LYS A 1 266 ? 143.617 117.255 122.683 1.00 48.43 ? 266 LYS A CD    1 
ATOM   2142  C  CE    . LYS A 1 266 ? 144.971 116.955 122.061 1.00 49.17 ? 266 LYS A CE    1 
ATOM   2143  N  NZ    . LYS A 1 266 ? 146.042 116.823 123.087 1.00 47.96 ? 266 LYS A NZ    1 
ATOM   2144  N  N     . ILE A 1 267 ? 138.466 116.555 120.972 1.00 53.63 ? 267 ILE A N     1 
ATOM   2145  C  CA    . ILE A 1 267 ? 137.171 115.940 121.244 1.00 55.08 ? 267 ILE A CA    1 
ATOM   2146  C  C     . ILE A 1 267 ? 137.064 115.537 122.709 1.00 56.65 ? 267 ILE A C     1 
ATOM   2147  O  O     . ILE A 1 267 ? 135.986 115.616 123.312 1.00 53.96 ? 267 ILE A O     1 
ATOM   2148  C  CB    . ILE A 1 267 ? 136.944 114.744 120.301 1.00 55.27 ? 267 ILE A CB    1 
ATOM   2149  C  CG1   . ILE A 1 267 ? 138.209 113.888 120.213 1.00 56.87 ? 267 ILE A CG1   1 
ATOM   2150  C  CG2   . ILE A 1 267 ? 136.520 115.226 118.924 1.00 54.96 ? 267 ILE A CG2   1 
ATOM   2151  C  CD1   . ILE A 1 267 ? 138.051 112.648 119.364 1.00 55.02 ? 267 ILE A CD1   1 
ATOM   2152  N  N     . SER A 1 268 ? 138.173 115.104 123.308 1.00 58.92 ? 268 SER A N     1 
ATOM   2153  C  CA    . SER A 1 268 ? 138.206 114.698 124.706 1.00 60.30 ? 268 SER A CA    1 
ATOM   2154  C  C     . SER A 1 268 ? 138.402 115.870 125.666 1.00 62.36 ? 268 SER A C     1 
ATOM   2155  O  O     . SER A 1 268 ? 138.782 115.648 126.822 1.00 61.48 ? 268 SER A O     1 
ATOM   2156  C  CB    . SER A 1 268 ? 139.308 113.659 124.922 1.00 62.54 ? 268 SER A CB    1 
ATOM   2157  O  OG    . SER A 1 268 ? 140.560 114.140 124.465 1.00 61.12 ? 268 SER A OG    1 
ATOM   2158  N  N     . ALA A 1 269 ? 138.160 117.100 125.222 1.00 65.83 ? 269 ALA A N     1 
ATOM   2159  C  CA    . ALA A 1 269 ? 138.351 118.256 126.087 1.00 64.63 ? 269 ALA A CA    1 
ATOM   2160  C  C     . ALA A 1 269 ? 137.214 118.370 127.096 1.00 65.99 ? 269 ALA A C     1 
ATOM   2161  O  O     . ALA A 1 269 ? 136.054 118.083 126.787 1.00 63.61 ? 269 ALA A O     1 
ATOM   2162  C  CB    . ALA A 1 269 ? 138.446 119.534 125.256 1.00 62.07 ? 269 ALA A CB    1 
ATOM   2163  N  N     . ASP A 1 270 ? 137.556 118.793 128.309 1.00 73.66 ? 270 ASP A N     1 
ATOM   2164  C  CA    . ASP A 1 270 ? 136.565 118.951 129.360 1.00 73.14 ? 270 ASP A CA    1 
ATOM   2165  C  C     . ASP A 1 270 ? 135.727 120.206 129.124 1.00 72.72 ? 270 ASP A C     1 
ATOM   2166  O  O     . ASP A 1 270 ? 136.104 121.109 128.372 1.00 73.37 ? 270 ASP A O     1 
ATOM   2167  C  CB    . ASP A 1 270 ? 137.242 119.018 130.730 1.00 73.59 ? 270 ASP A CB    1 
ATOM   2168  C  CG    . ASP A 1 270 ? 136.308 118.634 131.862 1.00 75.77 ? 270 ASP A CG    1 
ATOM   2169  O  OD1   . ASP A 1 270 ? 135.286 119.325 132.054 1.00 75.46 ? 270 ASP A OD1   1 
ATOM   2170  O  OD2   . ASP A 1 270 ? 136.597 117.640 132.561 1.00 73.86 ? 270 ASP A OD2   1 
ATOM   2171  N  N     . GLU A 1 271 ? 134.568 120.251 129.786 1.00 74.04 ? 271 GLU A N     1 
ATOM   2172  C  CA    . GLU A 1 271 ? 133.666 121.387 129.640 1.00 74.86 ? 271 GLU A CA    1 
ATOM   2173  C  C     . GLU A 1 271 ? 134.244 122.673 130.216 1.00 74.92 ? 271 GLU A C     1 
ATOM   2174  O  O     . GLU A 1 271 ? 133.801 123.761 129.834 1.00 73.75 ? 271 GLU A O     1 
ATOM   2175  C  CB    . GLU A 1 271 ? 132.323 121.078 130.304 1.00 73.33 ? 271 GLU A CB    1 
ATOM   2176  C  CG    . GLU A 1 271 ? 131.585 119.903 129.685 1.00 74.51 ? 271 GLU A CG    1 
ATOM   2177  C  CD    . GLU A 1 271 ? 131.198 120.154 128.241 1.00 75.21 ? 271 GLU A CD    1 
ATOM   2178  O  OE1   . GLU A 1 271 ? 130.791 121.292 127.923 1.00 75.15 ? 271 GLU A OE1   1 
ATOM   2179  O  OE2   . GLU A 1 271 ? 131.304 119.216 127.423 1.00 74.00 ? 271 GLU A OE2   1 
ATOM   2180  N  N     . ASP A 1 272 ? 135.217 122.577 131.121 1.00 73.58 ? 272 ASP A N     1 
ATOM   2181  C  CA    . ASP A 1 272 ? 135.854 123.757 131.691 1.00 73.80 ? 272 ASP A CA    1 
ATOM   2182  C  C     . ASP A 1 272 ? 136.988 124.293 130.828 1.00 72.64 ? 272 ASP A C     1 
ATOM   2183  O  O     . ASP A 1 272 ? 137.593 125.307 131.191 1.00 70.65 ? 272 ASP A O     1 
ATOM   2184  C  CB    . ASP A 1 272 ? 136.383 123.445 133.094 1.00 73.18 ? 272 ASP A CB    1 
ATOM   2185  C  CG    . ASP A 1 272 ? 135.308 123.546 134.158 1.00 75.04 ? 272 ASP A CG    1 
ATOM   2186  O  OD1   . ASP A 1 272 ? 134.241 124.129 133.876 1.00 74.61 ? 272 ASP A OD1   1 
ATOM   2187  O  OD2   . ASP A 1 272 ? 135.533 123.044 135.280 1.00 73.78 ? 272 ASP A OD2   1 
ATOM   2188  N  N     . VAL A 1 273 ? 137.296 123.637 129.709 1.00 64.22 ? 273 VAL A N     1 
ATOM   2189  C  CA    . VAL A 1 273 ? 138.361 124.053 128.805 1.00 63.54 ? 273 VAL A CA    1 
ATOM   2190  C  C     . VAL A 1 273 ? 137.840 124.256 127.387 1.00 61.00 ? 273 VAL A C     1 
ATOM   2191  O  O     . VAL A 1 273 ? 138.161 125.252 126.731 1.00 62.13 ? 273 VAL A O     1 
ATOM   2192  C  CB    . VAL A 1 273 ? 139.533 123.045 128.818 1.00 64.02 ? 273 VAL A CB    1 
ATOM   2193  C  CG1   . VAL A 1 273 ? 140.467 123.291 127.644 1.00 60.52 ? 273 VAL A CG1   1 
ATOM   2194  C  CG2   . VAL A 1 273 ? 140.290 123.131 130.133 1.00 61.67 ? 273 VAL A CG2   1 
ATOM   2195  N  N     . ARG A 1 274 ? 137.027 123.321 126.900 1.00 58.19 ? 274 ARG A N     1 
ATOM   2196  C  CA    . ARG A 1 274 ? 136.602 123.333 125.507 1.00 56.55 ? 274 ARG A CA    1 
ATOM   2197  C  C     . ARG A 1 274 ? 135.769 124.568 125.186 1.00 56.14 ? 274 ARG A C     1 
ATOM   2198  O  O     . ARG A 1 274 ? 134.903 124.978 125.963 1.00 58.40 ? 274 ARG A O     1 
ATOM   2199  C  CB    . ARG A 1 274 ? 135.804 122.064 125.196 1.00 58.20 ? 274 ARG A CB    1 
ATOM   2200  C  CG    . ARG A 1 274 ? 134.652 122.262 124.225 1.00 57.01 ? 274 ARG A CG    1 
ATOM   2201  C  CD    . ARG A 1 274 ? 134.086 120.929 123.754 1.00 57.24 ? 274 ARG A CD    1 
ATOM   2202  N  NE    . ARG A 1 274 ? 134.989 120.201 122.867 1.00 60.93 ? 274 ARG A NE    1 
ATOM   2203  C  CZ    . ARG A 1 274 ? 135.434 120.642 121.696 1.00 60.41 ? 274 ARG A CZ    1 
ATOM   2204  N  NH1   . ARG A 1 274 ? 135.047 121.805 121.196 1.00 59.39 ? 274 ARG A NH1   1 
ATOM   2205  N  NH2   . ARG A 1 274 ? 136.278 119.886 120.999 1.00 55.65 ? 274 ARG A NH2   1 
ATOM   2206  N  N     . VAL A 1 275 ? 136.047 125.165 124.028 1.00 47.55 ? 275 VAL A N     1 
ATOM   2207  C  CA    . VAL A 1 275 ? 135.254 126.255 123.474 1.00 48.54 ? 275 VAL A CA    1 
ATOM   2208  C  C     . VAL A 1 275 ? 134.559 125.738 122.223 1.00 49.00 ? 275 VAL A C     1 
ATOM   2209  O  O     . VAL A 1 275 ? 135.155 124.998 121.431 1.00 50.99 ? 275 VAL A O     1 
ATOM   2210  C  CB    . VAL A 1 275 ? 136.115 127.494 123.160 1.00 46.54 ? 275 VAL A CB    1 
ATOM   2211  C  CG1   . VAL A 1 275 ? 136.600 128.142 124.447 1.00 43.10 ? 275 VAL A CG1   1 
ATOM   2212  C  CG2   . VAL A 1 275 ? 137.291 127.119 122.278 1.00 47.24 ? 275 VAL A CG2   1 
ATOM   2213  N  N     . LYS A 1 276 ? 133.294 126.108 122.056 1.00 47.48 ? 276 LYS A N     1 
ATOM   2214  C  CA    . LYS A 1 276 ? 132.463 125.567 120.987 1.00 48.90 ? 276 LYS A CA    1 
ATOM   2215  C  C     . LYS A 1 276 ? 132.168 126.561 119.877 1.00 46.01 ? 276 LYS A C     1 
ATOM   2216  O  O     . LYS A 1 276 ? 132.200 126.190 118.702 1.00 51.27 ? 276 LYS A O     1 
ATOM   2217  C  CB    . LYS A 1 276 ? 131.142 125.050 121.569 1.00 49.94 ? 276 LYS A CB    1 
ATOM   2218  C  CG    . LYS A 1 276 ? 131.320 123.889 122.535 1.00 50.83 ? 276 LYS A CG    1 
ATOM   2219  C  CD    . LYS A 1 276 ? 130.010 123.492 123.194 1.00 51.95 ? 276 LYS A CD    1 
ATOM   2220  C  CE    . LYS A 1 276 ? 130.215 122.331 124.155 1.00 52.93 ? 276 LYS A CE    1 
ATOM   2221  N  NZ    . LYS A 1 276 ? 129.045 122.137 125.056 1.00 54.64 ? 276 LYS A NZ    1 
ATOM   2222  N  N     . THR A 1 277 ? 131.882 127.816 120.212 1.00 37.21 ? 277 THR A N     1 
ATOM   2223  C  CA    . THR A 1 277 ? 131.530 128.832 119.230 1.00 39.38 ? 277 THR A CA    1 
ATOM   2224  C  C     . THR A 1 277 ? 132.730 129.641 118.761 1.00 41.26 ? 277 THR A C     1 
ATOM   2225  O  O     . THR A 1 277 ? 132.559 130.599 118.000 1.00 39.59 ? 277 THR A O     1 
ATOM   2226  C  CB    . THR A 1 277 ? 130.466 129.771 119.800 1.00 40.72 ? 277 THR A CB    1 
ATOM   2227  O  OG1   . THR A 1 277 ? 131.101 130.850 120.496 1.00 39.31 ? 277 THR A OG1   1 
ATOM   2228  C  CG2   . THR A 1 277 ? 129.566 129.020 120.758 1.00 39.65 ? 277 THR A CG2   1 
ATOM   2229  N  N     . LEU A 1 278 ? 133.935 129.283 119.192 1.00 37.17 ? 278 LEU A N     1 
ATOM   2230  C  CA    . LEU A 1 278 ? 135.139 130.053 118.901 1.00 31.06 ? 278 LEU A CA    1 
ATOM   2231  C  C     . LEU A 1 278 ? 136.058 129.224 118.016 1.00 24.74 ? 278 LEU A C     1 
ATOM   2232  O  O     . LEU A 1 278 ? 136.632 128.231 118.471 1.00 32.27 ? 278 LEU A O     1 
ATOM   2233  C  CB    . LEU A 1 278 ? 135.846 130.462 120.192 1.00 30.38 ? 278 LEU A CB    1 
ATOM   2234  C  CG    . LEU A 1 278 ? 136.755 131.688 120.124 1.00 28.86 ? 278 LEU A CG    1 
ATOM   2235  C  CD1   . LEU A 1 278 ? 135.938 132.959 120.006 1.00 24.83 ? 278 LEU A CD1   1 
ATOM   2236  C  CD2   . LEU A 1 278 ? 137.648 131.743 121.348 1.00 26.51 ? 278 LEU A CD2   1 
ATOM   2237  N  N     . SER A 1 279 ? 136.196 129.633 116.759 1.00 25.32 ? 279 SER A N     1 
ATOM   2238  C  CA    . SER A 1 279 ? 137.209 129.056 115.892 1.00 16.14 ? 279 SER A CA    1 
ATOM   2239  C  C     . SER A 1 279 ? 138.593 129.475 116.372 1.00 18.46 ? 279 SER A C     1 
ATOM   2240  O  O     . SER A 1 279 ? 138.758 130.477 117.071 1.00 29.19 ? 279 SER A O     1 
ATOM   2241  C  CB    . SER A 1 279 ? 136.997 129.499 114.445 1.00 18.32 ? 279 SER A CB    1 
ATOM   2242  O  OG    . SER A 1 279 ? 135.701 129.159 113.989 1.00 27.39 ? 279 SER A OG    1 
ATOM   2243  N  N     . ILE A 1 280 ? 139.598 128.689 116.005 1.00 17.08 ? 280 ILE A N     1 
ATOM   2244  C  CA    . ILE A 1 280 ? 140.963 128.943 116.445 1.00 17.71 ? 280 ILE A CA    1 
ATOM   2245  C  C     . ILE A 1 280 ? 141.887 128.955 115.237 1.00 15.89 ? 280 ILE A C     1 
ATOM   2246  O  O     . ILE A 1 280 ? 141.715 128.170 114.299 1.00 20.57 ? 280 ILE A O     1 
ATOM   2247  C  CB    . ILE A 1 280 ? 141.437 127.912 117.493 1.00 18.10 ? 280 ILE A CB    1 
ATOM   2248  C  CG1   . ILE A 1 280 ? 141.432 126.494 116.928 1.00 24.15 ? 280 ILE A CG1   1 
ATOM   2249  C  CG2   . ILE A 1 280 ? 140.570 127.980 118.731 1.00 19.36 ? 280 ILE A CG2   1 
ATOM   2250  C  CD1   . ILE A 1 280 ? 142.402 125.572 117.629 1.00 18.85 ? 280 ILE A CD1   1 
ATOM   2251  N  N     . GLY A 1 281 ? 142.844 129.872 115.253 1.00 9.97  ? 281 GLY A N     1 
ATOM   2252  C  CA    . GLY A 1 281 ? 143.882 129.907 114.246 1.00 4.47  ? 281 GLY A CA    1 
ATOM   2253  C  C     . GLY A 1 281 ? 145.243 129.995 114.902 1.00 11.33 ? 281 GLY A C     1 
ATOM   2254  O  O     . GLY A 1 281 ? 145.396 130.540 115.993 1.00 21.99 ? 281 GLY A O     1 
ATOM   2255  N  N     . VAL A 1 282 ? 146.237 129.436 114.220 1.00 18.51 ? 282 VAL A N     1 
ATOM   2256  C  CA    . VAL A 1 282 ? 147.611 129.422 114.704 1.00 15.35 ? 282 VAL A CA    1 
ATOM   2257  C  C     . VAL A 1 282 ? 148.481 130.162 113.701 1.00 13.87 ? 282 VAL A C     1 
ATOM   2258  O  O     . VAL A 1 282 ? 148.462 129.851 112.505 1.00 18.50 ? 282 VAL A O     1 
ATOM   2259  C  CB    . VAL A 1 282 ? 148.126 127.988 114.926 1.00 12.59 ? 282 VAL A CB    1 
ATOM   2260  C  CG1   . VAL A 1 282 ? 149.625 127.993 115.143 1.00 20.01 ? 282 VAL A CG1   1 
ATOM   2261  C  CG2   . VAL A 1 282 ? 147.433 127.368 116.119 1.00 21.25 ? 282 VAL A CG2   1 
ATOM   2262  N  N     . VAL A 1 283 ? 149.237 131.136 114.189 1.00 12.20 ? 283 VAL A N     1 
ATOM   2263  C  CA    . VAL A 1 283 ? 150.150 131.917 113.366 1.00 9.17  ? 283 VAL A CA    1 
ATOM   2264  C  C     . VAL A 1 283 ? 151.530 131.288 113.480 1.00 13.33 ? 283 VAL A C     1 
ATOM   2265  O  O     . VAL A 1 283 ? 152.097 131.209 114.576 1.00 24.95 ? 283 VAL A O     1 
ATOM   2266  C  CB    . VAL A 1 283 ? 150.165 133.390 113.798 1.00 9.22  ? 283 VAL A CB    1 
ATOM   2267  C  CG1   . VAL A 1 283 ? 150.949 134.227 112.808 1.00 12.82 ? 283 VAL A CG1   1 
ATOM   2268  C  CG2   . VAL A 1 283 ? 148.745 133.900 113.934 1.00 9.87  ? 283 VAL A CG2   1 
ATOM   2269  N  N     . ILE A 1 284 ? 152.067 130.834 112.353 1.00 15.28 ? 284 ILE A N     1 
ATOM   2270  C  CA    . ILE A 1 284 ? 153.334 130.109 112.345 1.00 15.28 ? 284 ILE A CA    1 
ATOM   2271  C  C     . ILE A 1 284 ? 154.391 130.916 111.601 1.00 21.95 ? 284 ILE A C     1 
ATOM   2272  O  O     . ILE A 1 284 ? 154.326 131.036 110.370 1.00 20.90 ? 284 ILE A O     1 
ATOM   2273  C  CB    . ILE A 1 284 ? 153.171 128.714 111.721 1.00 15.88 ? 284 ILE A CB    1 
ATOM   2274  C  CG1   . ILE A 1 284 ? 152.000 127.977 112.370 1.00 14.26 ? 284 ILE A CG1   1 
ATOM   2275  C  CG2   . ILE A 1 284 ? 154.454 127.918 111.865 1.00 17.42 ? 284 ILE A CG2   1 
ATOM   2276  C  CD1   . ILE A 1 284 ? 151.811 126.568 111.870 1.00 17.18 ? 284 ILE A CD1   1 
ATOM   2277  N  N     . PRO A 1 285 ? 155.367 131.488 112.297 1.00 25.23 ? 285 PRO A N     1 
ATOM   2278  C  CA    . PRO A 1 285 ? 156.488 132.127 111.605 1.00 24.48 ? 285 PRO A CA    1 
ATOM   2279  C  C     . PRO A 1 285 ? 157.385 131.095 110.937 1.00 25.46 ? 285 PRO A C     1 
ATOM   2280  O  O     . PRO A 1 285 ? 157.364 129.905 111.259 1.00 24.55 ? 285 PRO A O     1 
ATOM   2281  C  CB    . PRO A 1 285 ? 157.230 132.863 112.726 1.00 26.19 ? 285 PRO A CB    1 
ATOM   2282  C  CG    . PRO A 1 285 ? 156.244 132.956 113.850 1.00 23.59 ? 285 PRO A CG    1 
ATOM   2283  C  CD    . PRO A 1 285 ? 155.416 131.720 113.749 1.00 19.59 ? 285 PRO A CD    1 
ATOM   2284  N  N     . ASP A 1 286 ? 158.181 131.577 109.980 1.00 29.60 ? 286 ASP A N     1 
ATOM   2285  C  CA    . ASP A 1 286 ? 159.138 130.712 109.298 1.00 24.68 ? 286 ASP A CA    1 
ATOM   2286  C  C     . ASP A 1 286 ? 160.129 130.080 110.264 1.00 34.06 ? 286 ASP A C     1 
ATOM   2287  O  O     . ASP A 1 286 ? 160.688 129.021 109.957 1.00 34.98 ? 286 ASP A O     1 
ATOM   2288  C  CB    . ASP A 1 286 ? 159.891 131.505 108.229 1.00 27.26 ? 286 ASP A CB    1 
ATOM   2289  C  CG    . ASP A 1 286 ? 159.350 131.266 106.835 1.00 38.62 ? 286 ASP A CG    1 
ATOM   2290  O  OD1   . ASP A 1 286 ? 158.116 131.156 106.684 1.00 41.96 ? 286 ASP A OD1   1 
ATOM   2291  O  OD2   . ASP A 1 286 ? 160.160 131.194 105.887 1.00 42.23 ? 286 ASP A OD2   1 
ATOM   2292  N  N     . LYS A 1 287 ? 160.358 130.708 111.420 1.00 33.12 ? 287 LYS A N     1 
ATOM   2293  C  CA    . LYS A 1 287 ? 161.269 130.144 112.409 1.00 27.18 ? 287 LYS A CA    1 
ATOM   2294  C  C     . LYS A 1 287 ? 160.781 128.791 112.906 1.00 27.06 ? 287 LYS A C     1 
ATOM   2295  O  O     . LYS A 1 287 ? 161.577 127.861 113.069 1.00 35.23 ? 287 LYS A O     1 
ATOM   2296  C  CB    . LYS A 1 287 ? 161.440 131.114 113.578 1.00 28.77 ? 287 LYS A CB    1 
ATOM   2297  C  CG    . LYS A 1 287 ? 162.552 130.730 114.537 1.00 27.99 ? 287 LYS A CG    1 
ATOM   2298  C  CD    . LYS A 1 287 ? 163.856 130.513 113.793 1.00 32.24 ? 287 LYS A CD    1 
ATOM   2299  C  CE    . LYS A 1 287 ? 164.988 130.179 114.742 1.00 32.66 ? 287 LYS A CE    1 
ATOM   2300  N  NZ    . LYS A 1 287 ? 166.298 130.145 114.041 1.00 33.63 ? 287 LYS A NZ    1 
ATOM   2301  N  N     . PHE A 1 288 ? 159.478 128.661 113.162 1.00 27.44 ? 288 PHE A N     1 
ATOM   2302  C  CA    . PHE A 1 288 ? 158.944 127.389 113.637 1.00 22.90 ? 288 PHE A CA    1 
ATOM   2303  C  C     . PHE A 1 288 ? 159.096 126.295 112.588 1.00 25.79 ? 288 PHE A C     1 
ATOM   2304  O  O     . PHE A 1 288 ? 159.453 125.157 112.916 1.00 34.50 ? 288 PHE A O     1 
ATOM   2305  C  CB    . PHE A 1 288 ? 157.478 127.547 114.033 1.00 25.13 ? 288 PHE A CB    1 
ATOM   2306  C  CG    . PHE A 1 288 ? 156.893 126.324 114.676 1.00 27.84 ? 288 PHE A CG    1 
ATOM   2307  C  CD1   . PHE A 1 288 ? 157.050 126.099 116.031 1.00 23.07 ? 288 PHE A CD1   1 
ATOM   2308  C  CD2   . PHE A 1 288 ? 156.193 125.396 113.925 1.00 26.57 ? 288 PHE A CD2   1 
ATOM   2309  C  CE1   . PHE A 1 288 ? 156.518 124.975 116.624 1.00 26.87 ? 288 PHE A CE1   1 
ATOM   2310  C  CE2   . PHE A 1 288 ? 155.660 124.270 114.513 1.00 23.83 ? 288 PHE A CE2   1 
ATOM   2311  C  CZ    . PHE A 1 288 ? 155.821 124.060 115.864 1.00 28.33 ? 288 PHE A CZ    1 
ATOM   2312  N  N     . VAL A 1 289 ? 158.817 126.617 111.324 1.00 31.75 ? 289 VAL A N     1 
ATOM   2313  C  CA    . VAL A 1 289 ? 158.959 125.631 110.257 1.00 29.02 ? 289 VAL A CA    1 
ATOM   2314  C  C     . VAL A 1 289 ? 160.418 125.228 110.101 1.00 30.40 ? 289 VAL A C     1 
ATOM   2315  O  O     . VAL A 1 289 ? 160.731 124.056 109.863 1.00 35.72 ? 289 VAL A O     1 
ATOM   2316  C  CB    . VAL A 1 289 ? 158.374 126.181 108.943 1.00 30.70 ? 289 VAL A CB    1 
ATOM   2317  C  CG1   . VAL A 1 289 ? 158.544 125.172 107.819 1.00 31.06 ? 289 VAL A CG1   1 
ATOM   2318  C  CG2   . VAL A 1 289 ? 156.910 126.542 109.128 1.00 24.14 ? 289 VAL A CG2   1 
ATOM   2319  N  N     . GLU A 1 290 ? 161.333 126.191 110.232 1.00 38.55 ? 290 GLU A N     1 
ATOM   2320  C  CA    . GLU A 1 290 ? 162.756 125.874 110.165 1.00 35.22 ? 290 GLU A CA    1 
ATOM   2321  C  C     . GLU A 1 290 ? 163.178 124.975 111.322 1.00 36.16 ? 290 GLU A C     1 
ATOM   2322  O  O     . GLU A 1 290 ? 163.941 124.022 111.131 1.00 42.76 ? 290 GLU A O     1 
ATOM   2323  C  CB    . GLU A 1 290 ? 163.576 127.164 110.151 1.00 35.42 ? 290 GLU A CB    1 
ATOM   2324  C  CG    . GLU A 1 290 ? 164.921 127.067 110.850 1.00 39.86 ? 290 GLU A CG    1 
ATOM   2325  C  CD    . GLU A 1 290 ? 165.675 128.382 110.845 1.00 46.12 ? 290 GLU A CD    1 
ATOM   2326  O  OE1   . GLU A 1 290 ? 165.019 129.445 110.839 1.00 47.26 ? 290 GLU A OE1   1 
ATOM   2327  O  OE2   . GLU A 1 290 ? 166.923 128.355 110.847 1.00 45.38 ? 290 GLU A OE2   1 
ATOM   2328  N  N     . LEU A 1 291 ? 162.687 125.261 112.531 1.00 28.64 ? 291 LEU A N     1 
ATOM   2329  C  CA    . LEU A 1 291 ? 163.030 124.444 113.690 1.00 27.57 ? 291 LEU A CA    1 
ATOM   2330  C  C     . LEU A 1 291 ? 162.499 123.025 113.544 1.00 35.76 ? 291 LEU A C     1 
ATOM   2331  O  O     . LEU A 1 291 ? 163.189 122.057 113.886 1.00 40.17 ? 291 LEU A O     1 
ATOM   2332  C  CB    . LEU A 1 291 ? 162.488 125.087 114.966 1.00 31.13 ? 291 LEU A CB    1 
ATOM   2333  C  CG    . LEU A 1 291 ? 163.182 126.360 115.450 1.00 33.68 ? 291 LEU A CG    1 
ATOM   2334  C  CD1   . LEU A 1 291 ? 162.323 127.083 116.472 1.00 28.69 ? 291 LEU A CD1   1 
ATOM   2335  C  CD2   . LEU A 1 291 ? 164.549 126.042 116.025 1.00 32.08 ? 291 LEU A CD2   1 
ATOM   2336  N  N     . ALA A 1 292 ? 161.269 122.880 113.050 1.00 36.82 ? 292 ALA A N     1 
ATOM   2337  C  CA    . ALA A 1 292 ? 160.713 121.549 112.830 1.00 30.61 ? 292 ALA A CA    1 
ATOM   2338  C  C     . ALA A 1 292 ? 161.458 120.816 111.721 1.00 32.59 ? 292 ALA A C     1 
ATOM   2339  O  O     . ALA A 1 292 ? 161.645 119.597 111.791 1.00 37.03 ? 292 ALA A O     1 
ATOM   2340  C  CB    . ALA A 1 292 ? 159.224 121.650 112.507 1.00 27.08 ? 292 ALA A CB    1 
ATOM   2341  N  N     . ARG A 1 293 ? 161.887 121.545 110.689 1.00 33.84 ? 293 ARG A N     1 
ATOM   2342  C  CA    . ARG A 1 293 ? 162.614 120.928 109.585 1.00 33.92 ? 293 ARG A CA    1 
ATOM   2343  C  C     . ARG A 1 293 ? 163.941 120.343 110.050 1.00 39.51 ? 293 ARG A C     1 
ATOM   2344  O  O     . ARG A 1 293 ? 164.326 119.246 109.630 1.00 41.57 ? 293 ARG A O     1 
ATOM   2345  C  CB    . ARG A 1 293 ? 162.836 121.955 108.475 1.00 35.74 ? 293 ARG A CB    1 
ATOM   2346  C  CG    . ARG A 1 293 ? 163.710 121.475 107.334 1.00 36.17 ? 293 ARG A CG    1 
ATOM   2347  C  CD    . ARG A 1 293 ? 164.144 122.640 106.468 1.00 37.85 ? 293 ARG A CD    1 
ATOM   2348  N  NE    . ARG A 1 293 ? 163.027 123.524 106.158 1.00 43.32 ? 293 ARG A NE    1 
ATOM   2349  C  CZ    . ARG A 1 293 ? 163.055 124.842 106.294 1.00 41.43 ? 293 ARG A CZ    1 
ATOM   2350  N  NH1   . ARG A 1 293 ? 164.133 125.468 106.736 1.00 42.58 ? 293 ARG A NH1   1 
ATOM   2351  N  NH2   . ARG A 1 293 ? 161.975 125.550 105.979 1.00 35.52 ? 293 ARG A NH2   1 
ATOM   2352  N  N     . GLU A 1 294 ? 164.652 121.058 110.918 1.00 45.11 ? 294 GLU A N     1 
ATOM   2353  C  CA    . GLU A 1 294 ? 165.933 120.595 111.433 1.00 43.64 ? 294 GLU A CA    1 
ATOM   2354  C  C     . GLU A 1 294 ? 165.788 119.643 112.612 1.00 45.09 ? 294 GLU A C     1 
ATOM   2355  O  O     . GLU A 1 294 ? 166.806 119.161 113.121 1.00 48.22 ? 294 GLU A O     1 
ATOM   2356  C  CB    . GLU A 1 294 ? 166.795 121.793 111.839 1.00 41.86 ? 294 GLU A CB    1 
ATOM   2357  C  CG    . GLU A 1 294 ? 166.929 122.852 110.758 1.00 44.75 ? 294 GLU A CG    1 
ATOM   2358  C  CD    . GLU A 1 294 ? 167.250 124.222 111.320 1.00 53.66 ? 294 GLU A CD    1 
ATOM   2359  O  OE1   . GLU A 1 294 ? 166.800 124.525 112.444 1.00 51.50 ? 294 GLU A OE1   1 
ATOM   2360  O  OE2   . GLU A 1 294 ? 167.952 124.997 110.637 1.00 52.58 ? 294 GLU A OE2   1 
ATOM   2361  N  N     . ASP A 1 295 ? 164.558 119.370 113.052 1.00 45.46 ? 295 ASP A N     1 
ATOM   2362  C  CA    . ASP A 1 295 ? 164.286 118.493 114.191 1.00 44.32 ? 295 ASP A CA    1 
ATOM   2363  C  C     . ASP A 1 295 ? 164.960 118.995 115.463 1.00 49.31 ? 295 ASP A C     1 
ATOM   2364  O  O     . ASP A 1 295 ? 165.279 118.213 116.363 1.00 52.53 ? 295 ASP A O     1 
ATOM   2365  C  CB    . ASP A 1 295 ? 164.700 117.048 113.899 1.00 47.38 ? 295 ASP A CB    1 
ATOM   2366  C  CG    . ASP A 1 295 ? 163.739 116.036 114.494 1.00 52.01 ? 295 ASP A CG    1 
ATOM   2367  O  OD1   . ASP A 1 295 ? 162.989 116.401 115.423 1.00 50.43 ? 295 ASP A OD1   1 
ATOM   2368  O  OD2   . ASP A 1 295 ? 163.734 114.876 114.031 1.00 51.03 ? 295 ASP A OD2   1 
ATOM   2369  N  N     . LYS A 1 296 ? 165.181 120.303 115.546 1.00 46.38 ? 296 LYS A N     1 
ATOM   2370  C  CA    . LYS A 1 296 ? 165.793 120.903 116.716 1.00 46.23 ? 296 LYS A CA    1 
ATOM   2371  C  C     . LYS A 1 296 ? 164.752 121.101 117.814 1.00 45.45 ? 296 LYS A C     1 
ATOM   2372  O  O     . LYS A 1 296 ? 163.550 120.922 117.610 1.00 46.96 ? 296 LYS A O     1 
ATOM   2373  C  CB    . LYS A 1 296 ? 166.453 122.231 116.349 1.00 46.36 ? 296 LYS A CB    1 
ATOM   2374  C  CG    . LYS A 1 296 ? 167.660 122.081 115.440 1.00 46.70 ? 296 LYS A CG    1 
ATOM   2375  C  CD    . LYS A 1 296 ? 168.310 123.420 115.148 1.00 46.76 ? 296 LYS A CD    1 
ATOM   2376  C  CE    . LYS A 1 296 ? 169.657 123.238 114.468 1.00 46.40 ? 296 LYS A CE    1 
ATOM   2377  N  NZ    . LYS A 1 296 ? 170.188 124.521 113.931 1.00 47.01 ? 296 LYS A NZ    1 
ATOM   2378  N  N     . ALA A 1 297 ? 165.230 121.467 118.999 1.00 47.17 ? 297 ALA A N     1 
ATOM   2379  C  CA    . ALA A 1 297 ? 164.347 121.713 120.130 1.00 45.55 ? 297 ALA A CA    1 
ATOM   2380  C  C     . ALA A 1 297 ? 163.873 123.160 120.099 1.00 45.07 ? 297 ALA A C     1 
ATOM   2381  O  O     . ALA A 1 297 ? 164.674 124.085 120.269 1.00 47.09 ? 297 ALA A O     1 
ATOM   2382  C  CB    . ALA A 1 297 ? 165.062 121.406 121.442 1.00 44.62 ? 297 ALA A CB    1 
ATOM   2383  N  N     . ALA A 1 298 ? 162.578 123.354 119.879 1.00 37.89 ? 298 ALA A N     1 
ATOM   2384  C  CA    . ALA A 1 298 ? 161.997 124.685 119.864 1.00 36.37 ? 298 ALA A CA    1 
ATOM   2385  C  C     . ALA A 1 298 ? 161.566 125.089 121.270 1.00 36.09 ? 298 ALA A C     1 
ATOM   2386  O  O     . ALA A 1 298 ? 161.472 124.266 122.182 1.00 37.71 ? 298 ALA A O     1 
ATOM   2387  C  CB    . ALA A 1 298 ? 160.811 124.743 118.902 1.00 36.43 ? 298 ALA A CB    1 
ATOM   2388  N  N     . TYR A 1 299 ? 161.304 126.381 121.438 1.00 36.66 ? 299 TYR A N     1 
ATOM   2389  C  CA    . TYR A 1 299 ? 160.891 126.929 122.721 1.00 29.46 ? 299 TYR A CA    1 
ATOM   2390  C  C     . TYR A 1 299 ? 159.676 127.818 122.522 1.00 31.54 ? 299 TYR A C     1 
ATOM   2391  O  O     . TYR A 1 299 ? 159.669 128.672 121.631 1.00 39.73 ? 299 TYR A O     1 
ATOM   2392  C  CB    . TYR A 1 299 ? 162.023 127.731 123.370 1.00 33.90 ? 299 TYR A CB    1 
ATOM   2393  C  CG    . TYR A 1 299 ? 163.041 126.881 124.089 1.00 37.95 ? 299 TYR A CG    1 
ATOM   2394  C  CD1   . TYR A 1 299 ? 162.842 126.490 125.404 1.00 36.05 ? 299 TYR A CD1   1 
ATOM   2395  C  CD2   . TYR A 1 299 ? 164.208 126.478 123.456 1.00 37.42 ? 299 TYR A CD2   1 
ATOM   2396  C  CE1   . TYR A 1 299 ? 163.769 125.718 126.066 1.00 35.44 ? 299 TYR A CE1   1 
ATOM   2397  C  CE2   . TYR A 1 299 ? 165.143 125.704 124.110 1.00 37.01 ? 299 TYR A CE2   1 
ATOM   2398  C  CZ    . TYR A 1 299 ? 164.918 125.327 125.416 1.00 40.24 ? 299 TYR A CZ    1 
ATOM   2399  O  OH    . TYR A 1 299 ? 165.845 124.556 126.076 1.00 45.59 ? 299 TYR A OH    1 
ATOM   2400  N  N     . VAL A 1 300 ? 158.657 127.612 123.337 1.00 31.21 ? 300 VAL A N     1 
ATOM   2401  C  CA    . VAL A 1 300 ? 157.553 128.558 123.444 1.00 24.89 ? 300 VAL A CA    1 
ATOM   2402  C  C     . VAL A 1 300 ? 157.869 129.504 124.590 1.00 29.47 ? 300 VAL A C     1 
ATOM   2403  O  O     . VAL A 1 300 ? 158.543 129.138 125.557 1.00 29.33 ? 300 VAL A O     1 
ATOM   2404  C  CB    . VAL A 1 300 ? 156.202 127.842 123.646 1.00 26.32 ? 300 VAL A CB    1 
ATOM   2405  C  CG1   . VAL A 1 300 ? 155.803 127.104 122.380 1.00 29.96 ? 300 VAL A CG1   1 
ATOM   2406  C  CG2   . VAL A 1 300 ? 156.272 126.890 124.825 1.00 29.61 ? 300 VAL A CG2   1 
ATOM   2407  N  N     . PHE A 1 301 ? 157.387 130.736 124.488 1.00 27.36 ? 301 PHE A N     1 
ATOM   2408  C  CA    . PHE A 1 301 ? 157.812 131.797 125.384 1.00 24.55 ? 301 PHE A CA    1 
ATOM   2409  C  C     . PHE A 1 301 ? 156.634 132.373 126.153 1.00 25.24 ? 301 PHE A C     1 
ATOM   2410  O  O     . PHE A 1 301 ? 155.488 132.335 125.696 1.00 32.14 ? 301 PHE A O     1 
ATOM   2411  C  CB    . PHE A 1 301 ? 158.520 132.911 124.612 1.00 28.04 ? 301 PHE A CB    1 
ATOM   2412  C  CG    . PHE A 1 301 ? 159.679 132.430 123.794 1.00 32.17 ? 301 PHE A CG    1 
ATOM   2413  C  CD1   . PHE A 1 301 ? 160.904 132.186 124.388 1.00 29.29 ? 301 PHE A CD1   1 
ATOM   2414  C  CD2   . PHE A 1 301 ? 159.542 132.209 122.437 1.00 26.60 ? 301 PHE A CD2   1 
ATOM   2415  C  CE1   . PHE A 1 301 ? 161.971 131.735 123.643 1.00 32.13 ? 301 PHE A CE1   1 
ATOM   2416  C  CE2   . PHE A 1 301 ? 160.607 131.759 121.688 1.00 28.37 ? 301 PHE A CE2   1 
ATOM   2417  C  CZ    . PHE A 1 301 ? 161.823 131.523 122.292 1.00 32.27 ? 301 PHE A CZ    1 
ATOM   2418  N  N     . TYR A 1 302 ? 156.938 132.902 127.336 1.00 26.52 ? 302 TYR A N     1 
ATOM   2419  C  CA    . TYR A 1 302 ? 155.960 133.618 128.139 1.00 27.75 ? 302 TYR A CA    1 
ATOM   2420  C  C     . TYR A 1 302 ? 155.936 135.064 127.666 1.00 31.00 ? 302 TYR A C     1 
ATOM   2421  O  O     . TYR A 1 302 ? 156.950 135.764 127.806 1.00 29.76 ? 302 TYR A O     1 
ATOM   2422  C  CB    . TYR A 1 302 ? 156.318 133.542 129.615 1.00 28.86 ? 302 TYR A CB    1 
ATOM   2423  C  CG    . TYR A 1 302 ? 156.115 132.175 130.232 1.00 26.73 ? 302 TYR A CG    1 
ATOM   2424  C  CD1   . TYR A 1 302 ? 156.954 131.117 129.916 1.00 28.03 ? 302 TYR A CD1   1 
ATOM   2425  C  CD2   . TYR A 1 302 ? 155.088 131.947 131.136 1.00 26.87 ? 302 TYR A CD2   1 
ATOM   2426  C  CE1   . TYR A 1 302 ? 156.774 129.871 130.477 1.00 30.93 ? 302 TYR A CE1   1 
ATOM   2427  C  CE2   . TYR A 1 302 ? 154.901 130.705 131.705 1.00 30.08 ? 302 TYR A CE2   1 
ATOM   2428  C  CZ    . TYR A 1 302 ? 155.748 129.671 131.372 1.00 34.14 ? 302 TYR A CZ    1 
ATOM   2429  O  OH    . TYR A 1 302 ? 155.566 128.429 131.934 1.00 38.07 ? 302 TYR A OH    1 
ATOM   2430  N  N     . PRO A 1 303 ? 154.831 135.547 127.096 1.00 29.87 ? 303 PRO A N     1 
ATOM   2431  C  CA    . PRO A 1 303 ? 154.840 136.891 126.494 1.00 25.42 ? 303 PRO A CA    1 
ATOM   2432  C  C     . PRO A 1 303 ? 155.146 138.008 127.473 1.00 28.31 ? 303 PRO A C     1 
ATOM   2433  O  O     . PRO A 1 303 ? 155.778 138.999 127.085 1.00 30.23 ? 303 PRO A O     1 
ATOM   2434  C  CB    . PRO A 1 303 ? 153.422 137.025 125.922 1.00 25.05 ? 303 PRO A CB    1 
ATOM   2435  C  CG    . PRO A 1 303 ? 152.918 135.637 125.808 1.00 24.18 ? 303 PRO A CG    1 
ATOM   2436  C  CD    . PRO A 1 303 ? 153.536 134.873 126.926 1.00 25.80 ? 303 PRO A CD    1 
ATOM   2437  N  N     . HIS A 1 304 ? 154.709 137.890 128.729 1.00 32.71 ? 304 HIS A N     1 
ATOM   2438  C  CA    . HIS A 1 304 ? 154.931 138.975 129.677 1.00 27.35 ? 304 HIS A CA    1 
ATOM   2439  C  C     . HIS A 1 304 ? 156.405 139.140 130.010 1.00 32.20 ? 304 HIS A C     1 
ATOM   2440  O  O     . HIS A 1 304 ? 156.869 140.266 130.202 1.00 40.44 ? 304 HIS A O     1 
ATOM   2441  C  CB    . HIS A 1 304 ? 154.128 138.750 130.954 1.00 29.45 ? 304 HIS A CB    1 
ATOM   2442  C  CG    . HIS A 1 304 ? 154.015 139.971 131.809 1.00 32.42 ? 304 HIS A CG    1 
ATOM   2443  N  ND1   . HIS A 1 304 ? 153.767 141.222 131.287 1.00 31.54 ? 304 HIS A ND1   1 
ATOM   2444  C  CD2   . HIS A 1 304 ? 154.125 140.138 133.148 1.00 35.82 ? 304 HIS A CD2   1 
ATOM   2445  C  CE1   . HIS A 1 304 ? 153.726 142.106 132.267 1.00 33.37 ? 304 HIS A CE1   1 
ATOM   2446  N  NE2   . HIS A 1 304 ? 153.939 141.474 133.406 1.00 34.47 ? 304 HIS A NE2   1 
ATOM   2447  N  N     . THR A 1 305 ? 157.155 138.039 130.084 1.00 26.13 ? 305 THR A N     1 
ATOM   2448  C  CA    . THR A 1 305 ? 158.590 138.144 130.315 1.00 29.64 ? 305 THR A CA    1 
ATOM   2449  C  C     . THR A 1 305 ? 159.281 138.872 129.169 1.00 28.52 ? 305 THR A C     1 
ATOM   2450  O  O     . THR A 1 305 ? 160.150 139.721 129.397 1.00 37.11 ? 305 THR A O     1 
ATOM   2451  C  CB    . THR A 1 305 ? 159.192 136.755 130.511 1.00 33.34 ? 305 THR A CB    1 
ATOM   2452  O  OG1   . THR A 1 305 ? 159.054 135.998 129.302 1.00 32.24 ? 305 THR A OG1   1 
ATOM   2453  C  CG2   . THR A 1 305 ? 158.481 136.030 131.639 1.00 30.09 ? 305 THR A CG2   1 
ATOM   2454  N  N     . ILE A 1 306 ? 158.899 138.560 127.930 1.00 32.70 ? 306 ILE A N     1 
ATOM   2455  C  CA    . ILE A 1 306 ? 159.476 139.244 126.778 1.00 28.81 ? 306 ILE A CA    1 
ATOM   2456  C  C     . ILE A 1 306 ? 159.112 140.722 126.797 1.00 30.16 ? 306 ILE A C     1 
ATOM   2457  O  O     . ILE A 1 306 ? 159.952 141.584 126.514 1.00 36.15 ? 306 ILE A O     1 
ATOM   2458  C  CB    . ILE A 1 306 ? 159.023 138.564 125.472 1.00 30.81 ? 306 ILE A CB    1 
ATOM   2459  C  CG1   . ILE A 1 306 ? 159.673 137.189 125.336 1.00 27.59 ? 306 ILE A CG1   1 
ATOM   2460  C  CG2   . ILE A 1 306 ? 159.359 139.428 124.268 1.00 30.75 ? 306 ILE A CG2   1 
ATOM   2461  C  CD1   . ILE A 1 306 ? 159.177 136.404 124.156 1.00 31.13 ? 306 ILE A CD1   1 
ATOM   2462  N  N     . TYR A 1 307 ? 157.859 141.041 127.125 1.00 33.78 ? 307 TYR A N     1 
ATOM   2463  C  CA    . TYR A 1 307 ? 157.446 142.439 127.173 1.00 30.95 ? 307 TYR A CA    1 
ATOM   2464  C  C     . TYR A 1 307 ? 158.192 143.201 128.262 1.00 34.86 ? 307 TYR A C     1 
ATOM   2465  O  O     . TYR A 1 307 ? 158.590 144.353 128.059 1.00 36.59 ? 307 TYR A O     1 
ATOM   2466  C  CB    . TYR A 1 307 ? 155.936 142.534 127.387 1.00 29.41 ? 307 TYR A CB    1 
ATOM   2467  C  CG    . TYR A 1 307 ? 155.409 143.949 127.353 1.00 33.99 ? 307 TYR A CG    1 
ATOM   2468  C  CD1   . TYR A 1 307 ? 155.131 144.576 126.147 1.00 29.48 ? 307 TYR A CD1   1 
ATOM   2469  C  CD2   . TYR A 1 307 ? 155.194 144.660 128.526 1.00 34.80 ? 307 TYR A CD2   1 
ATOM   2470  C  CE1   . TYR A 1 307 ? 154.652 145.868 126.109 1.00 33.11 ? 307 TYR A CE1   1 
ATOM   2471  C  CE2   . TYR A 1 307 ? 154.716 145.953 128.498 1.00 34.76 ? 307 TYR A CE2   1 
ATOM   2472  C  CZ    . TYR A 1 307 ? 154.447 146.553 127.287 1.00 35.56 ? 307 TYR A CZ    1 
ATOM   2473  O  OH    . TYR A 1 307 ? 153.970 147.842 127.252 1.00 38.54 ? 307 TYR A OH    1 
ATOM   2474  N  N     . LYS A 1 308 ? 158.379 142.580 129.428 1.00 36.60 ? 308 LYS A N     1 
ATOM   2475  C  CA    . LYS A 1 308 ? 159.117 143.229 130.505 1.00 34.27 ? 308 LYS A CA    1 
ATOM   2476  C  C     . LYS A 1 308 ? 160.579 143.431 130.132 1.00 33.30 ? 308 LYS A C     1 
ATOM   2477  O  O     . LYS A 1 308 ? 161.163 144.480 130.426 1.00 38.71 ? 308 LYS A O     1 
ATOM   2478  C  CB    . LYS A 1 308 ? 159.001 142.406 131.788 1.00 35.50 ? 308 LYS A CB    1 
ATOM   2479  C  CG    . LYS A 1 308 ? 157.635 142.472 132.448 1.00 34.28 ? 308 LYS A CG    1 
ATOM   2480  C  CD    . LYS A 1 308 ? 157.634 141.765 133.792 1.00 35.62 ? 308 LYS A CD    1 
ATOM   2481  C  CE    . LYS A 1 308 ? 158.156 140.343 133.673 1.00 39.54 ? 308 LYS A CE    1 
ATOM   2482  N  NZ    . LYS A 1 308 ? 157.133 139.336 134.069 1.00 36.80 ? 308 LYS A NZ    1 
ATOM   2483  N  N     . GLU A 1 309 ? 161.188 142.438 129.482 1.00 29.87 ? 309 GLU A N     1 
ATOM   2484  C  CA    . GLU A 1 309 ? 162.610 142.513 129.176 1.00 35.21 ? 309 GLU A CA    1 
ATOM   2485  C  C     . GLU A 1 309 ? 162.904 143.477 128.032 1.00 36.53 ? 309 GLU A C     1 
ATOM   2486  O  O     . GLU A 1 309 ? 163.891 144.219 128.084 1.00 40.04 ? 309 GLU A O     1 
ATOM   2487  C  CB    . GLU A 1 309 ? 163.141 141.118 128.848 1.00 32.53 ? 309 GLU A CB    1 
ATOM   2488  C  CG    . GLU A 1 309 ? 164.553 141.102 128.300 1.00 37.23 ? 309 GLU A CG    1 
ATOM   2489  C  CD    . GLU A 1 309 ? 165.595 141.413 129.352 1.00 43.24 ? 309 GLU A CD    1 
ATOM   2490  O  OE1   . GLU A 1 309 ? 165.252 141.405 130.552 1.00 43.38 ? 309 GLU A OE1   1 
ATOM   2491  O  OE2   . GLU A 1 309 ? 166.759 141.666 128.977 1.00 42.78 ? 309 GLU A OE2   1 
ATOM   2492  N  N     . TYR A 1 310 ? 162.063 143.491 126.999 1.00 35.10 ? 310 TYR A N     1 
ATOM   2493  C  CA    . TYR A 1 310 ? 162.352 144.232 125.782 1.00 36.50 ? 310 TYR A CA    1 
ATOM   2494  C  C     . TYR A 1 310 ? 161.460 145.445 125.570 1.00 34.70 ? 310 TYR A C     1 
ATOM   2495  O  O     . TYR A 1 310 ? 161.773 146.276 124.711 1.00 35.82 ? 310 TYR A O     1 
ATOM   2496  C  CB    . TYR A 1 310 ? 162.234 143.304 124.564 1.00 33.75 ? 310 TYR A CB    1 
ATOM   2497  C  CG    . TYR A 1 310 ? 163.258 142.195 124.554 1.00 34.10 ? 310 TYR A CG    1 
ATOM   2498  C  CD1   . TYR A 1 310 ? 164.520 142.394 124.016 1.00 34.21 ? 310 TYR A CD1   1 
ATOM   2499  C  CD2   . TYR A 1 310 ? 162.964 140.949 125.091 1.00 32.73 ? 310 TYR A CD2   1 
ATOM   2500  C  CE1   . TYR A 1 310 ? 165.459 141.385 124.008 1.00 37.21 ? 310 TYR A CE1   1 
ATOM   2501  C  CE2   . TYR A 1 310 ? 163.896 139.934 125.088 1.00 33.66 ? 310 TYR A CE2   1 
ATOM   2502  C  CZ    . TYR A 1 310 ? 165.142 140.157 124.546 1.00 37.08 ? 310 TYR A CZ    1 
ATOM   2503  O  OH    . TYR A 1 310 ? 166.076 139.149 124.539 1.00 35.96 ? 310 TYR A OH    1 
ATOM   2504  N  N     . GLY A 1 311 ? 160.367 145.573 126.315 1.00 31.50 ? 311 GLY A N     1 
ATOM   2505  C  CA    . GLY A 1 311 ? 159.460 146.684 126.135 1.00 33.10 ? 311 GLY A CA    1 
ATOM   2506  C  C     . GLY A 1 311 ? 158.498 146.542 124.978 1.00 35.98 ? 311 GLY A C     1 
ATOM   2507  O  O     . GLY A 1 311 ? 157.701 147.458 124.742 1.00 39.84 ? 311 GLY A O     1 
ATOM   2508  N  N     . GLN A 1 312 ? 158.545 145.430 124.250 1.00 36.68 ? 312 GLN A N     1 
ATOM   2509  C  CA    . GLN A 1 312 ? 157.651 145.177 123.133 1.00 32.89 ? 312 GLN A CA    1 
ATOM   2510  C  C     . GLN A 1 312 ? 157.003 143.813 123.307 1.00 33.52 ? 312 GLN A C     1 
ATOM   2511  O  O     . GLN A 1 312 ? 157.566 142.918 123.941 1.00 38.23 ? 312 GLN A O     1 
ATOM   2512  C  CB    . GLN A 1 312 ? 158.392 145.225 121.790 1.00 32.70 ? 312 GLN A CB    1 
ATOM   2513  C  CG    . GLN A 1 312 ? 159.088 146.540 121.501 1.00 35.47 ? 312 GLN A CG    1 
ATOM   2514  C  CD    . GLN A 1 312 ? 160.383 146.354 120.735 1.00 40.66 ? 312 GLN A CD    1 
ATOM   2515  O  OE1   . GLN A 1 312 ? 160.406 146.424 119.506 1.00 39.93 ? 312 GLN A OE1   1 
ATOM   2516  N  NE2   . GLN A 1 312 ? 161.470 146.113 121.458 1.00 38.76 ? 312 GLN A NE2   1 
ATOM   2517  N  N     . HIS A 1 313 ? 155.810 143.665 122.738 1.00 31.11 ? 313 HIS A N     1 
ATOM   2518  C  CA    . HIS A 1 313 ? 155.144 142.374 122.742 1.00 29.13 ? 313 HIS A CA    1 
ATOM   2519  C  C     . HIS A 1 313 ? 155.896 141.390 121.851 1.00 32.67 ? 313 HIS A C     1 
ATOM   2520  O  O     . HIS A 1 313 ? 156.608 141.771 120.920 1.00 32.53 ? 313 HIS A O     1 
ATOM   2521  C  CB    . HIS A 1 313 ? 153.697 142.514 122.272 1.00 26.12 ? 313 HIS A CB    1 
ATOM   2522  C  CG    . HIS A 1 313 ? 152.850 143.363 123.168 1.00 31.24 ? 313 HIS A CG    1 
ATOM   2523  N  ND1   . HIS A 1 313 ? 152.363 142.914 124.377 1.00 30.50 ? 313 HIS A ND1   1 
ATOM   2524  C  CD2   . HIS A 1 313 ? 152.403 144.633 123.032 1.00 30.78 ? 313 HIS A CD2   1 
ATOM   2525  C  CE1   . HIS A 1 313 ? 151.652 143.870 124.945 1.00 30.47 ? 313 HIS A CE1   1 
ATOM   2526  N  NE2   . HIS A 1 313 ? 151.660 144.924 124.150 1.00 31.70 ? 313 HIS A NE2   1 
ATOM   2527  N  N     . MET A 1 314 ? 155.739 140.101 122.160 1.00 35.86 ? 314 MET A N     1 
ATOM   2528  C  CA    . MET A 1 314 ? 156.439 139.073 121.398 1.00 29.29 ? 314 MET A CA    1 
ATOM   2529  C  C     . MET A 1 314 ? 155.987 139.055 119.943 1.00 35.86 ? 314 MET A C     1 
ATOM   2530  O  O     . MET A 1 314 ? 156.814 138.937 119.032 1.00 38.08 ? 314 MET A O     1 
ATOM   2531  C  CB    . MET A 1 314 ? 156.224 137.703 122.040 1.00 27.29 ? 314 MET A CB    1 
ATOM   2532  C  CG    . MET A 1 314 ? 156.812 136.556 121.236 1.00 32.96 ? 314 MET A CG    1 
ATOM   2533  S  SD    . MET A 1 314 ? 156.608 134.941 122.007 1.00 43.05 ? 314 MET A SD    1 
ATOM   2534  C  CE    . MET A 1 314 ? 155.232 135.259 123.100 1.00 30.70 ? 314 MET A CE    1 
ATOM   2535  N  N     . ASP A 1 315 ? 154.681 139.170 119.703 1.00 34.64 ? 315 ASP A N     1 
ATOM   2536  C  CA    . ASP A 1 315 ? 154.173 139.135 118.338 1.00 38.29 ? 315 ASP A CA    1 
ATOM   2537  C  C     . ASP A 1 315 ? 154.446 140.422 117.572 1.00 31.49 ? 315 ASP A C     1 
ATOM   2538  O  O     . ASP A 1 315 ? 154.277 140.441 116.349 1.00 38.98 ? 315 ASP A O     1 
ATOM   2539  C  CB    . ASP A 1 315 ? 152.670 138.844 118.333 1.00 31.25 ? 315 ASP A CB    1 
ATOM   2540  C  CG    . ASP A 1 315 ? 151.895 139.769 119.239 1.00 35.15 ? 315 ASP A CG    1 
ATOM   2541  O  OD1   . ASP A 1 315 ? 152.484 140.265 120.221 1.00 38.96 ? 315 ASP A OD1   1 
ATOM   2542  O  OD2   . ASP A 1 315 ? 150.698 140.001 118.969 1.00 32.24 ? 315 ASP A OD2   1 
ATOM   2543  N  N     . GLU A 1 316 ? 154.860 141.487 118.253 1.00 25.80 ? 316 GLU A N     1 
ATOM   2544  C  CA    . GLU A 1 316 ? 155.287 142.709 117.587 1.00 30.07 ? 316 GLU A CA    1 
ATOM   2545  C  C     . GLU A 1 316 ? 156.753 142.673 117.182 1.00 34.85 ? 316 GLU A C     1 
ATOM   2546  O  O     . GLU A 1 316 ? 157.237 143.636 116.579 1.00 33.47 ? 316 GLU A O     1 
ATOM   2547  C  CB    . GLU A 1 316 ? 155.033 143.917 118.490 1.00 32.74 ? 316 GLU A CB    1 
ATOM   2548  C  CG    . GLU A 1 316 ? 153.566 144.174 118.783 1.00 31.54 ? 316 GLU A CG    1 
ATOM   2549  C  CD    . GLU A 1 316 ? 152.900 145.014 117.715 1.00 39.08 ? 316 GLU A CD    1 
ATOM   2550  O  OE1   . GLU A 1 316 ? 151.735 145.418 117.913 1.00 42.23 ? 316 GLU A OE1   1 
ATOM   2551  O  OE2   . GLU A 1 316 ? 153.542 145.275 116.676 1.00 41.39 ? 316 GLU A OE2   1 
ATOM   2552  N  N     . MET A 1 317 ? 157.463 141.596 117.500 1.00 39.89 ? 317 MET A N     1 
ATOM   2553  C  CA    . MET A 1 317 ? 158.876 141.452 117.194 1.00 36.56 ? 317 MET A CA    1 
ATOM   2554  C  C     . MET A 1 317 ? 159.076 140.371 116.140 1.00 34.80 ? 317 MET A C     1 
ATOM   2555  O  O     . MET A 1 317 ? 158.230 139.495 115.944 1.00 37.33 ? 317 MET A O     1 
ATOM   2556  C  CB    . MET A 1 317 ? 159.675 141.107 118.455 1.00 34.63 ? 317 MET A CB    1 
ATOM   2557  C  CG    . MET A 1 317 ? 159.583 142.150 119.554 1.00 34.44 ? 317 MET A CG    1 
ATOM   2558  S  SD    . MET A 1 317 ? 160.413 141.642 121.069 1.00 43.65 ? 317 MET A SD    1 
ATOM   2559  C  CE    . MET A 1 317 ? 161.911 142.616 120.972 1.00 39.15 ? 317 MET A CE    1 
ATOM   2560  N  N     . ASP A 1 318 ? 160.216 140.446 115.459 1.00 42.30 ? 318 ASP A N     1 
ATOM   2561  C  CA    . ASP A 1 318 ? 160.563 139.471 114.431 1.00 39.52 ? 318 ASP A CA    1 
ATOM   2562  C  C     . ASP A 1 318 ? 161.120 138.227 115.108 1.00 38.30 ? 318 ASP A C     1 
ATOM   2563  O  O     . ASP A 1 318 ? 162.201 138.266 115.703 1.00 41.80 ? 318 ASP A O     1 
ATOM   2564  C  CB    . ASP A 1 318 ? 161.572 140.063 113.452 1.00 37.80 ? 318 ASP A CB    1 
ATOM   2565  C  CG    . ASP A 1 318 ? 161.709 139.239 112.189 1.00 47.34 ? 318 ASP A CG    1 
ATOM   2566  O  OD1   . ASP A 1 318 ? 160.742 138.537 111.827 1.00 44.10 ? 318 ASP A OD1   1 
ATOM   2567  O  OD2   . ASP A 1 318 ? 162.785 139.294 111.557 1.00 49.83 ? 318 ASP A OD2   1 
ATOM   2568  N  N     . MET A 1 319 ? 160.384 137.118 115.022 1.00 35.62 ? 319 MET A N     1 
ATOM   2569  C  CA    . MET A 1 319 ? 160.840 135.893 115.666 1.00 36.22 ? 319 MET A CA    1 
ATOM   2570  C  C     . MET A 1 319 ? 162.055 135.304 114.965 1.00 34.57 ? 319 MET A C     1 
ATOM   2571  O  O     . MET A 1 319 ? 162.926 134.730 115.625 1.00 37.81 ? 319 MET A O     1 
ATOM   2572  C  CB    . MET A 1 319 ? 159.709 134.869 115.722 1.00 33.97 ? 319 MET A CB    1 
ATOM   2573  C  CG    . MET A 1 319 ? 160.015 133.684 116.617 1.00 35.15 ? 319 MET A CG    1 
ATOM   2574  S  SD    . MET A 1 319 ? 160.352 134.157 118.324 1.00 43.86 ? 319 MET A SD    1 
ATOM   2575  C  CE    . MET A 1 319 ? 158.694 134.434 118.933 1.00 36.33 ? 319 MET A CE    1 
ATOM   2576  N  N     . ASN A 1 320 ? 162.146 135.450 113.643 1.00 40.15 ? 320 ASN A N     1 
ATOM   2577  C  CA    . ASN A 1 320 ? 163.288 134.912 112.914 1.00 41.19 ? 320 ASN A CA    1 
ATOM   2578  C  C     . ASN A 1 320 ? 164.592 135.607 113.281 1.00 42.82 ? 320 ASN A C     1 
ATOM   2579  O  O     . ASN A 1 320 ? 165.666 135.072 112.989 1.00 42.45 ? 320 ASN A O     1 
ATOM   2580  C  CB    . ASN A 1 320 ? 163.043 135.015 111.409 1.00 42.87 ? 320 ASN A CB    1 
ATOM   2581  C  CG    . ASN A 1 320 ? 162.117 133.930 110.898 1.00 44.74 ? 320 ASN A CG    1 
ATOM   2582  O  OD1   . ASN A 1 320 ? 160.900 134.108 110.851 1.00 39.88 ? 320 ASN A OD1   1 
ATOM   2583  N  ND2   . ASN A 1 320 ? 162.691 132.797 110.510 1.00 41.15 ? 320 ASN A ND2   1 
ATOM   2584  N  N     . GLU A 1 321 ? 164.525 136.781 113.912 1.00 43.90 ? 321 GLU A N     1 
ATOM   2585  C  CA    . GLU A 1 321 ? 165.716 137.491 114.350 1.00 42.44 ? 321 GLU A CA    1 
ATOM   2586  C  C     . GLU A 1 321 ? 165.843 137.603 115.862 1.00 44.43 ? 321 GLU A C     1 
ATOM   2587  O  O     . GLU A 1 321 ? 166.934 137.917 116.349 1.00 47.07 ? 321 GLU A O     1 
ATOM   2588  C  CB    . GLU A 1 321 ? 165.750 138.900 113.737 1.00 42.82 ? 321 GLU A CB    1 
ATOM   2589  C  CG    . GLU A 1 321 ? 165.222 139.996 114.646 1.00 45.12 ? 321 GLU A CG    1 
ATOM   2590  C  CD    . GLU A 1 321 ? 164.895 141.275 113.901 1.00 48.55 ? 321 GLU A CD    1 
ATOM   2591  O  OE1   . GLU A 1 321 ? 164.774 141.227 112.658 1.00 48.75 ? 321 GLU A OE1   1 
ATOM   2592  O  OE2   . GLU A 1 321 ? 164.758 142.328 114.558 1.00 44.77 ? 321 GLU A OE2   1 
ATOM   2593  N  N     . MET A 1 322 ? 164.773 137.345 116.614 1.00 40.56 ? 322 MET A N     1 
ATOM   2594  C  CA    . MET A 1 322 ? 164.792 137.480 118.064 1.00 38.06 ? 322 MET A CA    1 
ATOM   2595  C  C     . MET A 1 322 ? 164.586 136.166 118.804 1.00 35.48 ? 322 MET A C     1 
ATOM   2596  O  O     . MET A 1 322 ? 164.604 136.167 120.037 1.00 40.88 ? 322 MET A O     1 
ATOM   2597  C  CB    . MET A 1 322 ? 163.730 138.487 118.523 1.00 37.17 ? 322 MET A CB    1 
ATOM   2598  C  CG    . MET A 1 322 ? 163.885 139.878 117.937 1.00 39.84 ? 322 MET A CG    1 
ATOM   2599  S  SD    . MET A 1 322 ? 165.054 140.923 118.828 1.00 47.56 ? 322 MET A SD    1 
ATOM   2600  C  CE    . MET A 1 322 ? 164.833 140.346 120.505 1.00 39.12 ? 322 MET A CE    1 
ATOM   2601  N  N     . TYR A 1 323 ? 164.377 135.052 118.098 1.00 33.79 ? 323 TYR A N     1 
ATOM   2602  C  CA    . TYR A 1 323 ? 164.160 133.779 118.781 1.00 33.01 ? 323 TYR A CA    1 
ATOM   2603  C  C     . TYR A 1 323 ? 165.393 133.366 119.574 1.00 37.18 ? 323 TYR A C     1 
ATOM   2604  O  O     . TYR A 1 323 ? 165.291 132.939 120.731 1.00 40.26 ? 323 TYR A O     1 
ATOM   2605  C  CB    . TYR A 1 323 ? 163.783 132.697 117.768 1.00 33.42 ? 323 TYR A CB    1 
ATOM   2606  C  CG    . TYR A 1 323 ? 163.740 131.302 118.352 1.00 34.74 ? 323 TYR A CG    1 
ATOM   2607  C  CD1   . TYR A 1 323 ? 162.609 130.838 119.006 1.00 33.55 ? 323 TYR A CD1   1 
ATOM   2608  C  CD2   . TYR A 1 323 ? 164.832 130.450 118.248 1.00 32.64 ? 323 TYR A CD2   1 
ATOM   2609  C  CE1   . TYR A 1 323 ? 162.568 129.567 119.543 1.00 32.62 ? 323 TYR A CE1   1 
ATOM   2610  C  CE2   . TYR A 1 323 ? 164.799 129.180 118.782 1.00 32.52 ? 323 TYR A CE2   1 
ATOM   2611  C  CZ    . TYR A 1 323 ? 163.665 128.743 119.427 1.00 32.32 ? 323 TYR A CZ    1 
ATOM   2612  O  OH    . TYR A 1 323 ? 163.631 127.477 119.958 1.00 31.30 ? 323 TYR A OH    1 
ATOM   2613  N  N     . ASP A 1 324 ? 166.573 133.489 118.964 1.00 37.95 ? 324 ASP A N     1 
ATOM   2614  C  CA    . ASP A 1 324 ? 167.805 133.129 119.654 1.00 35.36 ? 324 ASP A CA    1 
ATOM   2615  C  C     . ASP A 1 324 ? 168.070 134.062 120.827 1.00 40.11 ? 324 ASP A C     1 
ATOM   2616  O  O     . ASP A 1 324 ? 168.571 133.628 121.870 1.00 46.46 ? 324 ASP A O     1 
ATOM   2617  C  CB    . ASP A 1 324 ? 168.975 133.143 118.675 1.00 41.73 ? 324 ASP A CB    1 
ATOM   2618  C  CG    . ASP A 1 324 ? 168.848 132.081 117.603 1.00 44.43 ? 324 ASP A CG    1 
ATOM   2619  O  OD1   . ASP A 1 324 ? 168.625 130.904 117.954 1.00 41.17 ? 324 ASP A OD1   1 
ATOM   2620  O  OD2   . ASP A 1 324 ? 168.968 132.424 116.408 1.00 44.36 ? 324 ASP A OD2   1 
ATOM   2621  N  N     . LYS A 1 325 ? 167.751 135.348 120.673 1.00 38.73 ? 325 LYS A N     1 
ATOM   2622  C  CA    . LYS A 1 325 ? 167.903 136.284 121.780 1.00 35.05 ? 325 LYS A CA    1 
ATOM   2623  C  C     . LYS A 1 325 ? 166.964 135.939 122.930 1.00 39.49 ? 325 LYS A C     1 
ATOM   2624  O  O     . LYS A 1 325 ? 167.352 136.023 124.100 1.00 43.95 ? 325 LYS A O     1 
ATOM   2625  C  CB    . LYS A 1 325 ? 167.663 137.712 121.293 1.00 37.50 ? 325 LYS A CB    1 
ATOM   2626  C  CG    . LYS A 1 325 ? 168.678 138.186 120.268 1.00 37.79 ? 325 LYS A CG    1 
ATOM   2627  C  CD    . LYS A 1 325 ? 168.359 139.585 119.778 1.00 41.01 ? 325 LYS A CD    1 
ATOM   2628  C  CE    . LYS A 1 325 ? 169.322 140.019 118.687 1.00 41.70 ? 325 LYS A CE    1 
ATOM   2629  N  NZ    . LYS A 1 325 ? 168.834 141.222 117.961 1.00 43.68 ? 325 LYS A NZ    1 
ATOM   2630  N  N     . PHE A 1 326 ? 165.725 135.554 122.616 1.00 39.06 ? 326 PHE A N     1 
ATOM   2631  C  CA    . PHE A 1 326 ? 164.793 135.126 123.655 1.00 33.11 ? 326 PHE A CA    1 
ATOM   2632  C  C     . PHE A 1 326 ? 165.299 133.879 124.365 1.00 35.45 ? 326 PHE A C     1 
ATOM   2633  O  O     . PHE A 1 326 ? 165.206 133.773 125.593 1.00 40.25 ? 326 PHE A O     1 
ATOM   2634  C  CB    . PHE A 1 326 ? 163.413 134.857 123.054 1.00 33.05 ? 326 PHE A CB    1 
ATOM   2635  C  CG    . PHE A 1 326 ? 162.738 136.072 122.489 1.00 35.54 ? 326 PHE A CG    1 
ATOM   2636  C  CD1   . PHE A 1 326 ? 163.140 137.345 122.851 1.00 35.04 ? 326 PHE A CD1   1 
ATOM   2637  C  CD2   . PHE A 1 326 ? 161.694 135.935 121.591 1.00 34.01 ? 326 PHE A CD2   1 
ATOM   2638  C  CE1   . PHE A 1 326 ? 162.514 138.456 122.327 1.00 32.92 ? 326 PHE A CE1   1 
ATOM   2639  C  CE2   . PHE A 1 326 ? 161.064 137.042 121.066 1.00 37.22 ? 326 PHE A CE2   1 
ATOM   2640  C  CZ    . PHE A 1 326 ? 161.475 138.305 121.434 1.00 38.87 ? 326 PHE A CZ    1 
ATOM   2641  N  N     . VAL A 1 327 ? 165.822 132.917 123.604 1.00 38.91 ? 327 VAL A N     1 
ATOM   2642  C  CA    . VAL A 1 327 ? 166.317 131.679 124.199 1.00 38.46 ? 327 VAL A CA    1 
ATOM   2643  C  C     . VAL A 1 327 ? 167.521 131.955 125.092 1.00 40.54 ? 327 VAL A C     1 
ATOM   2644  O  O     . VAL A 1 327 ? 167.624 131.422 126.203 1.00 45.87 ? 327 VAL A O     1 
ATOM   2645  C  CB    . VAL A 1 327 ? 166.645 130.655 123.098 1.00 36.72 ? 327 VAL A CB    1 
ATOM   2646  C  CG1   . VAL A 1 327 ? 167.426 129.485 123.671 1.00 41.15 ? 327 VAL A CG1   1 
ATOM   2647  C  CG2   . VAL A 1 327 ? 165.369 130.170 122.436 1.00 33.60 ? 327 VAL A CG2   1 
ATOM   2648  N  N     . ASP A 1 328 ? 168.445 132.797 124.628 1.00 38.73 ? 328 ASP A N     1 
ATOM   2649  C  CA    . ASP A 1 328 ? 169.645 133.107 125.393 1.00 36.80 ? 328 ASP A CA    1 
ATOM   2650  C  C     . ASP A 1 328 ? 169.380 134.045 126.561 1.00 40.59 ? 328 ASP A C     1 
ATOM   2651  O  O     . ASP A 1 328 ? 170.205 134.117 127.477 1.00 45.67 ? 328 ASP A O     1 
ATOM   2652  C  CB    . ASP A 1 328 ? 170.706 133.721 124.478 1.00 38.80 ? 328 ASP A CB    1 
ATOM   2653  C  CG    . ASP A 1 328 ? 171.171 132.764 123.402 1.00 44.64 ? 328 ASP A CG    1 
ATOM   2654  O  OD1   . ASP A 1 328 ? 170.987 131.541 123.575 1.00 48.16 ? 328 ASP A OD1   1 
ATOM   2655  O  OD2   . ASP A 1 328 ? 171.721 133.233 122.384 1.00 44.65 ? 328 ASP A OD2   1 
ATOM   2656  N  N     . ASN A 1 329 ? 168.263 134.762 126.550 1.00 41.28 ? 329 ASN A N     1 
ATOM   2657  C  CA    . ASN A 1 329 ? 167.968 135.715 127.613 1.00 38.15 ? 329 ASN A CA    1 
ATOM   2658  C  C     . ASN A 1 329 ? 167.528 134.971 128.868 1.00 41.38 ? 329 ASN A C     1 
ATOM   2659  O  O     . ASN A 1 329 ? 166.536 134.237 128.823 1.00 41.64 ? 329 ASN A O     1 
ATOM   2660  C  CB    . ASN A 1 329 ? 166.881 136.685 127.169 1.00 33.86 ? 329 ASN A CB    1 
ATOM   2661  C  CG    . ASN A 1 329 ? 166.866 137.958 127.987 1.00 40.28 ? 329 ASN A CG    1 
ATOM   2662  O  OD1   . ASN A 1 329 ? 166.793 137.922 129.214 1.00 44.81 ? 329 ASN A OD1   1 
ATOM   2663  N  ND2   . ASN A 1 329 ? 166.941 139.096 127.308 1.00 41.33 ? 329 ASN A ND2   1 
ATOM   2664  N  N     . PRO A 1 330 ? 168.228 135.125 129.995 1.00 43.77 ? 330 PRO A N     1 
ATOM   2665  C  CA    . PRO A 1 330 ? 167.779 134.451 131.222 1.00 40.69 ? 330 PRO A CA    1 
ATOM   2666  C  C     . PRO A 1 330 ? 166.516 135.053 131.809 1.00 39.19 ? 330 PRO A C     1 
ATOM   2667  O  O     . PRO A 1 330 ? 165.748 134.335 132.460 1.00 40.91 ? 330 PRO A O     1 
ATOM   2668  C  CB    . PRO A 1 330 ? 168.975 134.614 132.168 1.00 38.16 ? 330 PRO A CB    1 
ATOM   2669  C  CG    . PRO A 1 330 ? 169.669 135.835 131.680 1.00 36.51 ? 330 PRO A CG    1 
ATOM   2670  C  CD    . PRO A 1 330 ? 169.499 135.843 130.189 1.00 37.97 ? 330 PRO A CD    1 
ATOM   2671  N  N     . ARG A 1 331 ? 166.274 136.348 131.599 1.00 37.74 ? 331 ARG A N     1 
ATOM   2672  C  CA    . ARG A 1 331 ? 165.096 137.002 132.151 1.00 40.08 ? 331 ARG A CA    1 
ATOM   2673  C  C     . ARG A 1 331 ? 163.829 136.698 131.365 1.00 40.55 ? 331 ARG A C     1 
ATOM   2674  O  O     . ARG A 1 331 ? 162.733 137.009 131.844 1.00 39.68 ? 331 ARG A O     1 
ATOM   2675  C  CB    . ARG A 1 331 ? 165.319 138.514 132.216 1.00 38.96 ? 331 ARG A CB    1 
ATOM   2676  C  CG    . ARG A 1 331 ? 166.279 138.941 133.313 1.00 39.36 ? 331 ARG A CG    1 
ATOM   2677  C  CD    . ARG A 1 331 ? 166.914 140.286 133.006 1.00 41.53 ? 331 ARG A CD    1 
ATOM   2678  N  NE    . ARG A 1 331 ? 167.539 140.308 131.689 1.00 41.41 ? 331 ARG A NE    1 
ATOM   2679  C  CZ    . ARG A 1 331 ? 168.706 139.748 131.402 1.00 42.72 ? 331 ARG A CZ    1 
ATOM   2680  N  NH1   . ARG A 1 331 ? 169.417 139.119 132.323 1.00 42.04 ? 331 ARG A NH1   1 
ATOM   2681  N  NH2   . ARG A 1 331 ? 169.174 139.824 130.159 1.00 42.32 ? 331 ARG A NH2   1 
ATOM   2682  N  N     . VAL A 1 332 ? 163.950 136.109 130.183 1.00 36.78 ? 332 VAL A N     1 
ATOM   2683  C  CA    . VAL A 1 332 ? 162.801 135.634 129.423 1.00 32.62 ? 332 VAL A CA    1 
ATOM   2684  C  C     . VAL A 1 332 ? 162.504 134.207 129.859 1.00 37.39 ? 332 VAL A C     1 
ATOM   2685  O  O     . VAL A 1 332 ? 163.412 133.374 129.943 1.00 39.27 ? 332 VAL A O     1 
ATOM   2686  C  CB    . VAL A 1 332 ? 163.072 135.710 127.911 1.00 32.49 ? 332 VAL A CB    1 
ATOM   2687  C  CG1   . VAL A 1 332 ? 161.990 134.979 127.135 1.00 33.45 ? 332 VAL A CG1   1 
ATOM   2688  C  CG2   . VAL A 1 332 ? 163.168 137.158 127.460 1.00 34.39 ? 332 VAL A CG2   1 
ATOM   2689  N  N     . LYS A 1 333 ? 161.240 133.929 130.163 1.00 35.68 ? 333 LYS A N     1 
ATOM   2690  C  CA    . LYS A 1 333 ? 160.824 132.590 130.554 1.00 29.52 ? 333 LYS A CA    1 
ATOM   2691  C  C     . LYS A 1 333 ? 160.366 131.824 129.321 1.00 32.91 ? 333 LYS A C     1 
ATOM   2692  O  O     . LYS A 1 333 ? 159.546 132.320 128.542 1.00 36.13 ? 333 LYS A O     1 
ATOM   2693  C  CB    . LYS A 1 333 ? 159.706 132.647 131.594 1.00 28.90 ? 333 LYS A CB    1 
ATOM   2694  C  CG    . LYS A 1 333 ? 159.569 131.385 132.428 1.00 35.12 ? 333 LYS A CG    1 
ATOM   2695  C  CD    . LYS A 1 333 ? 158.369 131.464 133.356 1.00 35.27 ? 333 LYS A CD    1 
ATOM   2696  C  CE    . LYS A 1 333 ? 158.095 130.123 134.017 1.00 36.82 ? 333 LYS A CE    1 
ATOM   2697  N  NZ    . LYS A 1 333 ? 156.915 130.175 134.925 1.00 36.87 ? 333 LYS A NZ    1 
ATOM   2698  N  N     . LYS A 1 334 ? 160.901 130.619 129.144 1.00 38.47 ? 334 LYS A N     1 
ATOM   2699  C  CA    . LYS A 1 334 ? 160.607 129.808 127.975 1.00 34.26 ? 334 LYS A CA    1 
ATOM   2700  C  C     . LYS A 1 334 ? 160.352 128.371 128.401 1.00 35.88 ? 334 LYS A C     1 
ATOM   2701  O  O     . LYS A 1 334 ? 160.847 127.916 129.434 1.00 39.04 ? 334 LYS A O     1 
ATOM   2702  C  CB    . LYS A 1 334 ? 161.751 129.859 126.954 1.00 32.86 ? 334 LYS A CB    1 
ATOM   2703  C  CG    . LYS A 1 334 ? 163.030 129.200 127.428 1.00 35.39 ? 334 LYS A CG    1 
ATOM   2704  C  CD    . LYS A 1 334 ? 164.249 130.021 127.063 1.00 35.72 ? 334 LYS A CD    1 
ATOM   2705  C  CE    . LYS A 1 334 ? 164.220 131.371 127.744 1.00 38.57 ? 334 LYS A CE    1 
ATOM   2706  N  NZ    . LYS A 1 334 ? 165.513 132.094 127.617 1.00 38.93 ? 334 LYS A NZ    1 
ATOM   2707  N  N     . GLU A 1 335 ? 159.565 127.665 127.595 1.00 37.63 ? 335 GLU A N     1 
ATOM   2708  C  CA    . GLU A 1 335 ? 159.260 126.260 127.816 1.00 37.15 ? 335 GLU A CA    1 
ATOM   2709  C  C     . GLU A 1 335 ? 159.687 125.452 126.601 1.00 36.91 ? 335 GLU A C     1 
ATOM   2710  O  O     . GLU A 1 335 ? 159.440 125.850 125.460 1.00 40.70 ? 335 GLU A O     1 
ATOM   2711  C  CB    . GLU A 1 335 ? 157.769 126.047 128.089 1.00 36.49 ? 335 GLU A CB    1 
ATOM   2712  C  CG    . GLU A 1 335 ? 157.486 125.081 129.225 1.00 39.76 ? 335 GLU A CG    1 
ATOM   2713  C  CD    . GLU A 1 335 ? 156.212 125.414 129.974 1.00 44.81 ? 335 GLU A CD    1 
ATOM   2714  O  OE1   . GLU A 1 335 ? 155.300 126.008 129.364 1.00 42.65 ? 335 GLU A OE1   1 
ATOM   2715  O  OE2   . GLU A 1 335 ? 156.124 125.084 131.175 1.00 44.40 ? 335 GLU A OE2   1 
ATOM   2716  N  N     . LYS A 1 336 ? 160.331 124.317 126.853 1.00 38.70 ? 336 LYS A N     1 
ATOM   2717  C  CA    . LYS A 1 336 ? 160.831 123.467 125.782 1.00 34.06 ? 336 LYS A CA    1 
ATOM   2718  C  C     . LYS A 1 336 ? 159.689 122.676 125.156 1.00 38.81 ? 336 LYS A C     1 
ATOM   2719  O  O     . LYS A 1 336 ? 158.881 122.068 125.865 1.00 40.89 ? 336 LYS A O     1 
ATOM   2720  C  CB    . LYS A 1 336 ? 161.901 122.519 126.319 1.00 39.19 ? 336 LYS A CB    1 
ATOM   2721  C  CG    . LYS A 1 336 ? 162.801 121.914 125.259 1.00 44.05 ? 336 LYS A CG    1 
ATOM   2722  C  CD    . LYS A 1 336 ? 163.740 120.891 125.878 1.00 42.21 ? 336 LYS A CD    1 
ATOM   2723  C  CE    . LYS A 1 336 ? 164.935 120.614 124.985 1.00 42.88 ? 336 LYS A CE    1 
ATOM   2724  N  NZ    . LYS A 1 336 ? 164.740 119.391 124.159 1.00 42.77 ? 336 LYS A NZ    1 
ATOM   2725  N  N     . ILE A 1 337 ? 159.623 122.690 123.825 1.00 35.65 ? 337 ILE A N     1 
ATOM   2726  C  CA    . ILE A 1 337 ? 158.633 121.931 123.075 1.00 32.01 ? 337 ILE A CA    1 
ATOM   2727  C  C     . ILE A 1 337 ? 159.328 121.250 121.906 1.00 34.85 ? 337 ILE A C     1 
ATOM   2728  O  O     . ILE A 1 337 ? 160.440 121.610 121.516 1.00 41.32 ? 337 ILE A O     1 
ATOM   2729  C  CB    . ILE A 1 337 ? 157.471 122.811 122.562 1.00 32.97 ? 337 ILE A CB    1 
ATOM   2730  C  CG1   . ILE A 1 337 ? 158.009 123.962 121.712 1.00 35.22 ? 337 ILE A CG1   1 
ATOM   2731  C  CG2   . ILE A 1 337 ? 156.637 123.334 123.721 1.00 36.55 ? 337 ILE A CG2   1 
ATOM   2732  C  CD1   . ILE A 1 337 ? 157.210 124.218 120.461 1.00 32.79 ? 337 ILE A CD1   1 
ATOM   2733  N  N     . ASN A 1 338 ? 158.652 120.248 121.346 1.00 36.33 ? 338 ASN A N     1 
ATOM   2734  C  CA    . ASN A 1 338 ? 159.128 119.595 120.138 1.00 31.88 ? 338 ASN A CA    1 
ATOM   2735  C  C     . ASN A 1 338 ? 158.355 120.150 118.954 1.00 33.99 ? 338 ASN A C     1 
ATOM   2736  O  O     . ASN A 1 338 ? 157.146 119.896 118.846 1.00 36.16 ? 338 ASN A O     1 
ATOM   2737  C  CB    . ASN A 1 338 ? 158.952 118.082 120.230 1.00 34.00 ? 338 ASN A CB    1 
ATOM   2738  C  CG    . ASN A 1 338 ? 159.665 117.344 119.115 1.00 37.04 ? 338 ASN A CG    1 
ATOM   2739  O  OD1   . ASN A 1 338 ? 159.035 116.845 118.184 1.00 38.90 ? 338 ASN A OD1   1 
ATOM   2740  N  ND2   . ASN A 1 338 ? 160.987 117.274 119.203 1.00 35.67 ? 338 ASN A ND2   1 
ATOM   2741  N  N     . PRO A 1 339 ? 158.986 120.917 118.061 1.00 35.90 ? 339 PRO A N     1 
ATOM   2742  C  CA    . PRO A 1 339 ? 158.233 121.518 116.948 1.00 30.06 ? 339 PRO A CA    1 
ATOM   2743  C  C     . PRO A 1 339 ? 157.585 120.502 116.026 1.00 32.65 ? 339 PRO A C     1 
ATOM   2744  O  O     . PRO A 1 339 ? 156.485 120.756 115.521 1.00 37.53 ? 339 PRO A O     1 
ATOM   2745  C  CB    . PRO A 1 339 ? 159.296 122.350 116.218 1.00 34.35 ? 339 PRO A CB    1 
ATOM   2746  C  CG    . PRO A 1 339 ? 160.596 121.735 116.604 1.00 36.27 ? 339 PRO A CG    1 
ATOM   2747  C  CD    . PRO A 1 339 ? 160.419 121.240 118.003 1.00 36.91 ? 339 PRO A CD    1 
ATOM   2748  N  N     . ARG A 1 340 ? 158.227 119.356 115.790 1.00 36.02 ? 340 ARG A N     1 
ATOM   2749  C  CA    . ARG A 1 340 ? 157.610 118.330 114.955 1.00 28.66 ? 340 ARG A CA    1 
ATOM   2750  C  C     . ARG A 1 340 ? 156.414 117.698 115.653 1.00 30.30 ? 340 ARG A C     1 
ATOM   2751  O  O     . ARG A 1 340 ? 155.409 117.379 115.008 1.00 38.15 ? 340 ARG A O     1 
ATOM   2752  C  CB    . ARG A 1 340 ? 158.638 117.269 114.574 1.00 28.58 ? 340 ARG A CB    1 
ATOM   2753  C  CG    . ARG A 1 340 ? 159.604 117.723 113.502 1.00 29.53 ? 340 ARG A CG    1 
ATOM   2754  C  CD    . ARG A 1 340 ? 160.239 116.548 112.790 1.00 34.46 ? 340 ARG A CD    1 
ATOM   2755  N  NE    . ARG A 1 340 ? 161.291 116.984 111.880 1.00 35.78 ? 340 ARG A NE    1 
ATOM   2756  C  CZ    . ARG A 1 340 ? 162.021 116.168 111.134 1.00 33.23 ? 340 ARG A CZ    1 
ATOM   2757  N  NH1   . ARG A 1 340 ? 161.841 114.859 111.162 1.00 31.67 ? 340 ARG A NH1   1 
ATOM   2758  N  NH2   . ARG A 1 340 ? 162.955 116.680 110.338 1.00 35.04 ? 340 ARG A NH2   1 
ATOM   2759  N  N     . LYS A 1 341 ? 156.501 117.509 116.970 1.00 32.46 ? 341 LYS A N     1 
ATOM   2760  C  CA    . LYS A 1 341 ? 155.347 117.027 117.719 1.00 31.08 ? 341 LYS A CA    1 
ATOM   2761  C  C     . LYS A 1 341 ? 154.204 118.030 117.662 1.00 33.65 ? 341 LYS A C     1 
ATOM   2762  O  O     . LYS A 1 341 ? 153.035 117.646 117.547 1.00 37.03 ? 341 LYS A O     1 
ATOM   2763  C  CB    . LYS A 1 341 ? 155.739 116.741 119.167 1.00 36.04 ? 341 LYS A CB    1 
ATOM   2764  C  CG    . LYS A 1 341 ? 155.636 115.279 119.558 1.00 36.36 ? 341 LYS A CG    1 
ATOM   2765  C  CD    . LYS A 1 341 ? 156.394 114.396 118.581 1.00 39.24 ? 341 LYS A CD    1 
ATOM   2766  C  CE    . LYS A 1 341 ? 156.464 112.961 119.075 1.00 41.43 ? 341 LYS A CE    1 
ATOM   2767  N  NZ    . LYS A 1 341 ? 157.580 112.765 120.041 1.00 37.36 ? 341 LYS A NZ    1 
ATOM   2768  N  N     . LEU A 1 342 ? 154.522 119.324 117.737 1.00 31.12 ? 342 LEU A N     1 
ATOM   2769  C  CA    . LEU A 1 342 ? 153.491 120.349 117.614 1.00 26.88 ? 342 LEU A CA    1 
ATOM   2770  C  C     . LEU A 1 342 ? 152.864 120.336 116.225 1.00 29.90 ? 342 LEU A C     1 
ATOM   2771  O  O     . LEU A 1 342 ? 151.649 120.511 116.086 1.00 34.63 ? 342 LEU A O     1 
ATOM   2772  C  CB    . LEU A 1 342 ? 154.078 121.723 117.931 1.00 31.61 ? 342 LEU A CB    1 
ATOM   2773  C  CG    . LEU A 1 342 ? 153.086 122.852 118.215 1.00 30.56 ? 342 LEU A CG    1 
ATOM   2774  C  CD1   . LEU A 1 342 ? 151.922 122.346 119.047 1.00 28.12 ? 342 LEU A CD1   1 
ATOM   2775  C  CD2   . LEU A 1 342 ? 153.780 124.007 118.915 1.00 26.76 ? 342 LEU A CD2   1 
ATOM   2776  N  N     . LEU A 1 343 ? 153.676 120.133 115.185 1.00 31.30 ? 343 LEU A N     1 
ATOM   2777  C  CA    . LEU A 1 343 ? 153.139 120.039 113.830 1.00 26.03 ? 343 LEU A CA    1 
ATOM   2778  C  C     . LEU A 1 343 ? 152.225 118.829 113.679 1.00 27.79 ? 343 LEU A C     1 
ATOM   2779  O  O     . LEU A 1 343 ? 151.162 118.915 113.052 1.00 38.19 ? 343 LEU A O     1 
ATOM   2780  C  CB    . LEU A 1 343 ? 154.283 119.974 112.820 1.00 30.18 ? 343 LEU A CB    1 
ATOM   2781  C  CG    . LEU A 1 343 ? 154.623 121.260 112.069 1.00 30.20 ? 343 LEU A CG    1 
ATOM   2782  C  CD1   . LEU A 1 343 ? 155.648 120.980 110.985 1.00 26.76 ? 343 LEU A CD1   1 
ATOM   2783  C  CD2   . LEU A 1 343 ? 153.371 121.884 111.479 1.00 33.54 ? 343 LEU A CD2   1 
ATOM   2784  N  N     . GLU A 1 344 ? 152.632 117.687 114.236 1.00 33.61 ? 344 GLU A N     1 
ATOM   2785  C  CA    . GLU A 1 344 ? 151.790 116.497 114.189 1.00 33.52 ? 344 GLU A CA    1 
ATOM   2786  C  C     . GLU A 1 344 ? 150.490 116.715 114.951 1.00 32.01 ? 344 GLU A C     1 
ATOM   2787  O  O     . GLU A 1 344 ? 149.427 116.250 114.525 1.00 34.18 ? 344 GLU A O     1 
ATOM   2788  C  CB    . GLU A 1 344 ? 152.550 115.294 114.746 1.00 31.86 ? 344 GLU A CB    1 
ATOM   2789  C  CG    . GLU A 1 344 ? 153.736 114.865 113.895 1.00 34.62 ? 344 GLU A CG    1 
ATOM   2790  C  CD    . GLU A 1 344 ? 154.803 114.144 114.695 1.00 42.60 ? 344 GLU A CD    1 
ATOM   2791  O  OE1   . GLU A 1 344 ? 154.523 113.753 115.847 1.00 44.95 ? 344 GLU A OE1   1 
ATOM   2792  O  OE2   . GLU A 1 344 ? 155.923 113.968 114.171 1.00 39.28 ? 344 GLU A OE2   1 
ATOM   2793  N  N     . LYS A 1 345 ? 150.556 117.411 116.087 1.00 29.52 ? 345 LYS A N     1 
ATOM   2794  C  CA    . LYS A 1 345 ? 149.342 117.733 116.831 1.00 29.38 ? 345 LYS A CA    1 
ATOM   2795  C  C     . LYS A 1 345 ? 148.430 118.647 116.025 1.00 31.57 ? 345 LYS A C     1 
ATOM   2796  O  O     . LYS A 1 345 ? 147.207 118.479 116.035 1.00 35.98 ? 345 LYS A O     1 
ATOM   2797  C  CB    . LYS A 1 345 ? 149.701 118.373 118.171 1.00 29.77 ? 345 LYS A CB    1 
ATOM   2798  C  CG    . LYS A 1 345 ? 148.502 118.857 118.964 1.00 29.70 ? 345 LYS A CG    1 
ATOM   2799  C  CD    . LYS A 1 345 ? 148.897 119.267 120.369 1.00 32.39 ? 345 LYS A CD    1 
ATOM   2800  C  CE    . LYS A 1 345 ? 147.687 119.714 121.168 1.00 37.29 ? 345 LYS A CE    1 
ATOM   2801  N  NZ    . LYS A 1 345 ? 148.037 120.011 122.583 1.00 34.35 ? 345 LYS A NZ    1 
ATOM   2802  N  N     . LEU A 1 346 ? 149.009 119.625 115.324 1.00 31.06 ? 346 LEU A N     1 
ATOM   2803  C  CA    . LEU A 1 346 ? 148.218 120.484 114.449 1.00 26.09 ? 346 LEU A CA    1 
ATOM   2804  C  C     . LEU A 1 346 ? 147.519 119.665 113.373 1.00 28.55 ? 346 LEU A C     1 
ATOM   2805  O  O     . LEU A 1 346 ? 146.327 119.853 113.108 1.00 29.73 ? 346 LEU A O     1 
ATOM   2806  C  CB    . LEU A 1 346 ? 149.110 121.547 113.807 1.00 28.19 ? 346 LEU A CB    1 
ATOM   2807  C  CG    . LEU A 1 346 ? 149.704 122.648 114.684 1.00 29.65 ? 346 LEU A CG    1 
ATOM   2808  C  CD1   . LEU A 1 346 ? 150.694 123.473 113.885 1.00 30.06 ? 346 LEU A CD1   1 
ATOM   2809  C  CD2   . LEU A 1 346 ? 148.613 123.528 115.245 1.00 30.00 ? 346 LEU A CD2   1 
ATOM   2810  N  N     . ALA A 1 347 ? 148.253 118.746 112.742 1.00 30.63 ? 347 ALA A N     1 
ATOM   2811  C  CA    . ALA A 1 347 ? 147.663 117.915 111.696 1.00 27.11 ? 347 ALA A CA    1 
ATOM   2812  C  C     . ALA A 1 347 ? 146.547 117.037 112.248 1.00 32.82 ? 347 ALA A C     1 
ATOM   2813  O  O     . ALA A 1 347 ? 145.490 116.898 111.623 1.00 34.41 ? 347 ALA A O     1 
ATOM   2814  C  CB    . ALA A 1 347 ? 148.740 117.058 111.034 1.00 28.69 ? 347 ALA A CB    1 
ATOM   2815  N  N     . MET A 1 348 ? 146.765 116.438 113.421 1.00 36.75 ? 348 MET A N     1 
ATOM   2816  C  CA    . MET A 1 348 ? 145.740 115.598 114.032 1.00 35.32 ? 348 MET A CA    1 
ATOM   2817  C  C     . MET A 1 348 ? 144.498 116.407 114.382 1.00 35.09 ? 348 MET A C     1 
ATOM   2818  O  O     . MET A 1 348 ? 143.367 115.953 114.167 1.00 39.92 ? 348 MET A O     1 
ATOM   2819  C  CB    . MET A 1 348 ? 146.307 114.911 115.274 1.00 36.23 ? 348 MET A CB    1 
ATOM   2820  C  CG    . MET A 1 348 ? 145.275 114.195 116.126 1.00 42.72 ? 348 MET A CG    1 
ATOM   2821  S  SD    . MET A 1 348 ? 145.066 114.957 117.746 1.00 54.41 ? 348 MET A SD    1 
ATOM   2822  C  CE    . MET A 1 348 ? 146.741 114.874 118.376 1.00 38.29 ? 348 MET A CE    1 
ATOM   2823  N  N     . LEU A 1 349 ? 144.689 117.612 114.922 1.00 31.37 ? 349 LEU A N     1 
ATOM   2824  C  CA    . LEU A 1 349 ? 143.557 118.459 115.278 1.00 29.31 ? 349 LEU A CA    1 
ATOM   2825  C  C     . LEU A 1 349 ? 142.784 118.901 114.043 1.00 25.33 ? 349 LEU A C     1 
ATOM   2826  O  O     . LEU A 1 349 ? 141.553 118.979 114.073 1.00 30.10 ? 349 LEU A O     1 
ATOM   2827  C  CB    . LEU A 1 349 ? 144.041 119.668 116.074 1.00 32.36 ? 349 LEU A CB    1 
ATOM   2828  C  CG    . LEU A 1 349 ? 143.041 120.272 117.059 1.00 33.23 ? 349 LEU A CG    1 
ATOM   2829  C  CD1   . LEU A 1 349 ? 142.775 119.313 118.206 1.00 35.35 ? 349 LEU A CD1   1 
ATOM   2830  C  CD2   . LEU A 1 349 ? 143.545 121.608 117.579 1.00 29.50 ? 349 LEU A CD2   1 
ATOM   2831  N  N     . ARG A 1 350 ? 143.487 119.207 112.949 1.00 27.20 ? 350 ARG A N     1 
ATOM   2832  C  CA    . ARG A 1 350 ? 142.791 119.568 111.719 1.00 26.64 ? 350 ARG A CA    1 
ATOM   2833  C  C     . ARG A 1 350 ? 142.061 118.375 111.119 1.00 32.04 ? 350 ARG A C     1 
ATOM   2834  O  O     . ARG A 1 350 ? 140.984 118.538 110.537 1.00 35.02 ? 350 ARG A O     1 
ATOM   2835  C  CB    . ARG A 1 350 ? 143.768 120.157 110.703 1.00 24.07 ? 350 ARG A CB    1 
ATOM   2836  C  CG    . ARG A 1 350 ? 144.499 121.395 111.185 1.00 28.51 ? 350 ARG A CG    1 
ATOM   2837  C  CD    . ARG A 1 350 ? 145.214 122.093 110.047 1.00 29.25 ? 350 ARG A CD    1 
ATOM   2838  N  NE    . ARG A 1 350 ? 144.380 123.138 109.466 1.00 35.68 ? 350 ARG A NE    1 
ATOM   2839  C  CZ    . ARG A 1 350 ? 144.253 123.364 108.167 1.00 34.36 ? 350 ARG A CZ    1 
ATOM   2840  N  NH1   . ARG A 1 350 ? 144.900 122.637 107.272 1.00 30.10 ? 350 ARG A NH1   1 
ATOM   2841  N  NH2   . ARG A 1 350 ? 143.453 124.343 107.756 1.00 29.81 ? 350 ARG A NH2   1 
ATOM   2842  N  N     . SER A 1 351 ? 142.633 117.176 111.238 1.00 35.69 ? 351 SER A N     1 
ATOM   2843  C  CA    . SER A 1 351 ? 141.950 115.981 110.758 1.00 32.01 ? 351 SER A CA    1 
ATOM   2844  C  C     . SER A 1 351 ? 140.683 115.708 111.557 1.00 37.79 ? 351 SER A C     1 
ATOM   2845  O  O     . SER A 1 351 ? 139.645 115.351 110.986 1.00 43.89 ? 351 SER A O     1 
ATOM   2846  C  CB    . SER A 1 351 ? 142.891 114.780 110.824 1.00 34.68 ? 351 SER A CB    1 
ATOM   2847  O  OG    . SER A 1 351 ? 143.953 114.912 109.897 1.00 44.89 ? 351 SER A OG    1 
ATOM   2848  N  N     . GLU A 1 352 ? 140.744 115.869 112.878 1.00 35.44 ? 352 GLU A N     1 
ATOM   2849  C  CA    . GLU A 1 352 ? 139.619 115.509 113.730 1.00 32.66 ? 352 GLU A CA    1 
ATOM   2850  C  C     . GLU A 1 352 ? 138.568 116.606 113.853 1.00 38.69 ? 352 GLU A C     1 
ATOM   2851  O  O     . GLU A 1 352 ? 137.409 116.297 114.151 1.00 46.61 ? 352 GLU A O     1 
ATOM   2852  C  CB    . GLU A 1 352 ? 140.121 115.117 115.125 1.00 38.77 ? 352 GLU A CB    1 
ATOM   2853  C  CG    . GLU A 1 352 ? 140.208 116.262 116.119 1.00 41.91 ? 352 GLU A CG    1 
ATOM   2854  C  CD    . GLU A 1 352 ? 140.746 115.825 117.466 1.00 45.98 ? 352 GLU A CD    1 
ATOM   2855  O  OE1   . GLU A 1 352 ? 141.774 115.117 117.496 1.00 43.41 ? 352 GLU A OE1   1 
ATOM   2856  O  OE2   . GLU A 1 352 ? 140.141 116.187 118.496 1.00 46.65 ? 352 GLU A OE2   1 
ATOM   2857  N  N     . SER A 1 353 ? 138.932 117.871 113.637 1.00 35.83 ? 353 SER A N     1 
ATOM   2858  C  CA    . SER A 1 353 ? 137.979 118.963 113.798 1.00 37.21 ? 353 SER A CA    1 
ATOM   2859  C  C     . SER A 1 353 ? 138.041 120.029 112.716 1.00 33.46 ? 353 SER A C     1 
ATOM   2860  O  O     . SER A 1 353 ? 137.117 120.844 112.642 1.00 32.12 ? 353 SER A O     1 
ATOM   2861  C  CB    . SER A 1 353 ? 138.176 119.640 115.162 1.00 36.68 ? 353 SER A CB    1 
ATOM   2862  O  OG    . SER A 1 353 ? 139.460 120.230 115.256 1.00 34.35 ? 353 SER A OG    1 
ATOM   2863  N  N     . GLY A 1 354 ? 139.079 120.064 111.881 1.00 25.90 ? 354 GLY A N     1 
ATOM   2864  C  CA    . GLY A 1 354 ? 139.251 121.124 110.913 1.00 28.01 ? 354 GLY A CA    1 
ATOM   2865  C  C     . GLY A 1 354 ? 139.993 122.337 111.428 1.00 23.46 ? 354 GLY A C     1 
ATOM   2866  O  O     . GLY A 1 354 ? 140.306 123.234 110.636 1.00 28.81 ? 354 GLY A O     1 
ATOM   2867  N  N     . TYR A 1 355 ? 140.291 122.389 112.722 1.00 22.35 ? 355 TYR A N     1 
ATOM   2868  C  CA    . TYR A 1 355 ? 140.981 123.474 113.392 1.00 16.74 ? 355 TYR A CA    1 
ATOM   2869  C  C     . TYR A 1 355 ? 142.388 123.040 113.791 1.00 22.30 ? 355 TYR A C     1 
ATOM   2870  O  O     . TYR A 1 355 ? 142.638 121.849 113.986 1.00 28.34 ? 355 TYR A O     1 
ATOM   2871  C  CB    . TYR A 1 355 ? 140.212 123.920 114.642 1.00 24.60 ? 355 TYR A CB    1 
ATOM   2872  C  CG    . TYR A 1 355 ? 138.880 124.559 114.338 1.00 28.51 ? 355 TYR A CG    1 
ATOM   2873  C  CD1   . TYR A 1 355 ? 138.791 125.651 113.488 1.00 22.12 ? 355 TYR A CD1   1 
ATOM   2874  C  CD2   . TYR A 1 355 ? 137.710 124.070 114.902 1.00 30.35 ? 355 TYR A CD2   1 
ATOM   2875  C  CE1   . TYR A 1 355 ? 137.576 126.236 113.206 1.00 29.01 ? 355 TYR A CE1   1 
ATOM   2876  C  CE2   . TYR A 1 355 ? 136.490 124.650 114.627 1.00 26.79 ? 355 TYR A CE2   1 
ATOM   2877  C  CZ    . TYR A 1 355 ? 136.428 125.733 113.779 1.00 29.87 ? 355 TYR A CZ    1 
ATOM   2878  O  OH    . TYR A 1 355 ? 135.213 126.314 113.503 1.00 32.86 ? 355 TYR A OH    1 
ATOM   2879  N  N     . PRO A 1 356 ? 143.333 123.975 113.930 1.00 31.04 ? 356 PRO A N     1 
ATOM   2880  C  CA    . PRO A 1 356 ? 143.220 125.429 113.777 1.00 16.31 ? 356 PRO A CA    1 
ATOM   2881  C  C     . PRO A 1 356 ? 143.380 125.915 112.345 1.00 15.47 ? 356 PRO A C     1 
ATOM   2882  O  O     . PRO A 1 356 ? 143.831 125.183 111.472 1.00 24.92 ? 356 PRO A O     1 
ATOM   2883  C  CB    . PRO A 1 356 ? 144.361 125.937 114.658 1.00 18.84 ? 356 PRO A CB    1 
ATOM   2884  C  CG    . PRO A 1 356 ? 145.426 124.906 114.457 1.00 22.38 ? 356 PRO A CG    1 
ATOM   2885  C  CD    . PRO A 1 356 ? 144.697 123.587 114.330 1.00 19.71 ? 356 PRO A CD    1 
ATOM   2886  N  N     . TYR A 1 357 ? 142.995 127.159 112.082 1.00 24.62 ? 357 TYR A N     1 
ATOM   2887  C  CA    . TYR A 1 357 ? 143.441 127.832 110.874 1.00 11.90 ? 357 TYR A CA    1 
ATOM   2888  C  C     . TYR A 1 357 ? 144.949 128.027 110.950 1.00 13.76 ? 357 TYR A C     1 
ATOM   2889  O  O     . TYR A 1 357 ? 145.497 128.309 112.018 1.00 26.78 ? 357 TYR A O     1 
ATOM   2890  C  CB    . TYR A 1 357 ? 142.749 129.186 110.717 1.00 13.34 ? 357 TYR A CB    1 
ATOM   2891  C  CG    . TYR A 1 357 ? 141.243 129.156 110.846 1.00 16.54 ? 357 TYR A CG    1 
ATOM   2892  C  CD1   . TYR A 1 357 ? 140.514 128.040 110.473 1.00 17.88 ? 357 TYR A CD1   1 
ATOM   2893  C  CD2   . TYR A 1 357 ? 140.551 130.253 111.336 1.00 18.07 ? 357 TYR A CD2   1 
ATOM   2894  C  CE1   . TYR A 1 357 ? 139.140 128.012 110.584 1.00 20.00 ? 357 TYR A CE1   1 
ATOM   2895  C  CE2   . TYR A 1 357 ? 139.178 130.235 111.453 1.00 16.50 ? 357 TYR A CE2   1 
ATOM   2896  C  CZ    . TYR A 1 357 ? 138.477 129.112 111.074 1.00 20.39 ? 357 TYR A CZ    1 
ATOM   2897  O  OH    . TYR A 1 357 ? 137.107 129.087 111.187 1.00 27.88 ? 357 TYR A OH    1 
ATOM   2898  N  N     . ILE A 1 358 ? 145.625 127.867 109.820 1.00 16.49 ? 358 ILE A N     1 
ATOM   2899  C  CA    . ILE A 1 358 ? 147.076 127.989 109.761 1.00 22.67 ? 358 ILE A CA    1 
ATOM   2900  C  C     . ILE A 1 358 ? 147.412 129.255 108.991 1.00 19.01 ? 358 ILE A C     1 
ATOM   2901  O  O     . ILE A 1 358 ? 147.024 129.403 107.826 1.00 20.45 ? 358 ILE A O     1 
ATOM   2902  C  CB    . ILE A 1 358 ? 147.729 126.760 109.110 1.00 22.54 ? 358 ILE A CB    1 
ATOM   2903  C  CG1   . ILE A 1 358 ? 147.333 125.481 109.850 1.00 19.12 ? 358 ILE A CG1   1 
ATOM   2904  C  CG2   . ILE A 1 358 ? 149.240 126.916 109.083 1.00 16.30 ? 358 ILE A CG2   1 
ATOM   2905  C  CD1   . ILE A 1 358 ? 147.557 125.541 111.341 1.00 19.03 ? 358 ILE A CD1   1 
ATOM   2906  N  N     . MET A 1 359 ? 148.127 130.168 109.639 1.00 17.05 ? 359 MET A N     1 
ATOM   2907  C  CA    . MET A 1 359 ? 148.644 131.368 108.997 1.00 9.79  ? 359 MET A CA    1 
ATOM   2908  C  C     . MET A 1 359 ? 150.162 131.289 108.976 1.00 10.97 ? 359 MET A C     1 
ATOM   2909  O  O     . MET A 1 359 ? 150.795 131.193 110.032 1.00 21.05 ? 359 MET A O     1 
ATOM   2910  C  CB    . MET A 1 359 ? 148.187 132.632 109.721 1.00 11.80 ? 359 MET A CB    1 
ATOM   2911  C  CG    . MET A 1 359 ? 148.551 133.908 108.984 1.00 12.14 ? 359 MET A CG    1 
ATOM   2912  S  SD    . MET A 1 359 ? 148.223 135.405 109.921 1.00 31.83 ? 359 MET A SD    1 
ATOM   2913  C  CE    . MET A 1 359 ? 149.815 136.213 109.837 1.00 9.41  ? 359 MET A CE    1 
ATOM   2914  N  N     . PHE A 1 360 ? 150.740 131.332 107.782 1.00 11.40 ? 360 PHE A N     1 
ATOM   2915  C  CA    . PHE A 1 360 ? 152.190 131.347 107.620 1.00 10.70 ? 360 PHE A CA    1 
ATOM   2916  C  C     . PHE A 1 360 ? 152.630 132.803 107.643 1.00 14.79 ? 360 PHE A C     1 
ATOM   2917  O  O     . PHE A 1 360 ? 152.550 133.505 106.634 1.00 19.23 ? 360 PHE A O     1 
ATOM   2918  C  CB    . PHE A 1 360 ? 152.591 130.634 106.336 1.00 14.38 ? 360 PHE A CB    1 
ATOM   2919  C  CG    . PHE A 1 360 ? 152.235 129.178 106.328 1.00 20.16 ? 360 PHE A CG    1 
ATOM   2920  C  CD1   . PHE A 1 360 ? 152.738 128.325 107.295 1.00 19.07 ? 360 PHE A CD1   1 
ATOM   2921  C  CD2   . PHE A 1 360 ? 151.378 128.665 105.371 1.00 15.11 ? 360 PHE A CD2   1 
ATOM   2922  C  CE1   . PHE A 1 360 ? 152.407 126.987 107.297 1.00 19.85 ? 360 PHE A CE1   1 
ATOM   2923  C  CE2   . PHE A 1 360 ? 151.043 127.329 105.370 1.00 15.24 ? 360 PHE A CE2   1 
ATOM   2924  C  CZ    . PHE A 1 360 ? 151.557 126.489 106.334 1.00 17.41 ? 360 PHE A CZ    1 
ATOM   2925  N  N     . GLN A 1 361 ? 153.102 133.252 108.809 1.00 18.75 ? 361 GLN A N     1 
ATOM   2926  C  CA    . GLN A 1 361 ? 153.284 134.679 109.055 1.00 10.48 ? 361 GLN A CA    1 
ATOM   2927  C  C     . GLN A 1 361 ? 154.315 135.289 108.113 1.00 17.96 ? 361 GLN A C     1 
ATOM   2928  O  O     . GLN A 1 361 ? 154.120 136.400 107.606 1.00 23.78 ? 361 GLN A O     1 
ATOM   2929  C  CB    . GLN A 1 361 ? 153.683 134.900 110.513 1.00 18.59 ? 361 GLN A CB    1 
ATOM   2930  C  CG    . GLN A 1 361 ? 154.307 136.248 110.807 1.00 22.72 ? 361 GLN A CG    1 
ATOM   2931  C  CD    . GLN A 1 361 ? 153.687 136.914 112.015 1.00 22.82 ? 361 GLN A CD    1 
ATOM   2932  O  OE1   . GLN A 1 361 ? 153.573 136.308 113.079 1.00 24.76 ? 361 GLN A OE1   1 
ATOM   2933  N  NE2   . GLN A 1 361 ? 153.275 138.165 111.857 1.00 23.04 ? 361 GLN A NE2   1 
ATOM   2934  N  N     . ASP A 1 362 ? 155.420 134.585 107.867 1.00 24.65 ? 362 ASP A N     1 
ATOM   2935  C  CA    . ASP A 1 362 ? 156.435 135.115 106.966 1.00 18.46 ? 362 ASP A CA    1 
ATOM   2936  C  C     . ASP A 1 362 ? 156.006 135.052 105.508 1.00 17.64 ? 362 ASP A C     1 
ATOM   2937  O  O     . ASP A 1 362 ? 156.524 135.820 104.692 1.00 27.15 ? 362 ASP A O     1 
ATOM   2938  C  CB    . ASP A 1 362 ? 157.755 134.373 107.161 1.00 25.33 ? 362 ASP A CB    1 
ATOM   2939  C  CG    . ASP A 1 362 ? 158.351 134.604 108.533 1.00 31.87 ? 362 ASP A CG    1 
ATOM   2940  O  OD1   . ASP A 1 362 ? 157.698 134.250 109.535 1.00 30.50 ? 362 ASP A OD1   1 
ATOM   2941  O  OD2   . ASP A 1 362 ? 159.471 135.150 108.609 1.00 34.05 ? 362 ASP A OD2   1 
ATOM   2942  N  N     . ASN A 1 363 ? 155.083 134.155 105.161 1.00 24.90 ? 363 ASN A N     1 
ATOM   2943  C  CA    . ASN A 1 363 ? 154.512 134.171 103.819 1.00 14.33 ? 363 ASN A CA    1 
ATOM   2944  C  C     . ASN A 1 363 ? 153.630 135.396 103.621 1.00 18.39 ? 363 ASN A C     1 
ATOM   2945  O  O     . ASN A 1 363 ? 153.582 135.966 102.526 1.00 28.95 ? 363 ASN A O     1 
ATOM   2946  C  CB    . ASN A 1 363 ? 153.715 132.893 103.571 1.00 12.40 ? 363 ASN A CB    1 
ATOM   2947  C  CG    . ASN A 1 363 ? 154.585 131.744 103.115 1.00 18.68 ? 363 ASN A CG    1 
ATOM   2948  O  OD1   . ASN A 1 363 ? 155.731 131.938 102.717 1.00 21.66 ? 363 ASN A OD1   1 
ATOM   2949  N  ND2   . ASN A 1 363 ? 154.043 130.535 103.172 1.00 20.31 ? 363 ASN A ND2   1 
ATOM   2950  N  N     . VAL A 1 364 ? 152.920 135.807 104.671 1.00 15.42 ? 364 VAL A N     1 
ATOM   2951  C  CA    . VAL A 1 364 ? 152.083 136.997 104.590 1.00 10.09 ? 364 VAL A CA    1 
ATOM   2952  C  C     . VAL A 1 364 ? 152.937 138.255 104.527 1.00 17.13 ? 364 VAL A C     1 
ATOM   2953  O  O     . VAL A 1 364 ? 152.658 139.174 103.749 1.00 19.66 ? 364 VAL A O     1 
ATOM   2954  C  CB    . VAL A 1 364 ? 151.108 137.039 105.779 1.00 2.18  ? 364 VAL A CB    1 
ATOM   2955  C  CG1   . VAL A 1 364 ? 150.157 138.207 105.636 1.00 9.53  ? 364 VAL A CG1   1 
ATOM   2956  C  CG2   . VAL A 1 364 ? 150.351 135.733 105.889 1.00 7.93  ? 364 VAL A CG2   1 
ATOM   2957  N  N     . ASN A 1 365 ? 153.992 138.317 105.339 1.00 22.49 ? 365 ASN A N     1 
ATOM   2958  C  CA    . ASN A 1 365 ? 154.705 139.566 105.563 1.00 11.51 ? 365 ASN A CA    1 
ATOM   2959  C  C     . ASN A 1 365 ? 155.864 139.795 104.605 1.00 13.82 ? 365 ASN A C     1 
ATOM   2960  O  O     . ASN A 1 365 ? 156.350 140.927 104.513 1.00 22.54 ? 365 ASN A O     1 
ATOM   2961  C  CB    . ASN A 1 365 ? 155.220 139.622 107.002 1.00 17.71 ? 365 ASN A CB    1 
ATOM   2962  C  CG    . ASN A 1 365 ? 154.133 139.981 107.988 1.00 16.43 ? 365 ASN A CG    1 
ATOM   2963  O  OD1   . ASN A 1 365 ? 153.450 140.990 107.833 1.00 21.30 ? 365 ASN A OD1   1 
ATOM   2964  N  ND2   . ASN A 1 365 ? 153.962 139.152 109.008 1.00 15.56 ? 365 ASN A ND2   1 
ATOM   2965  N  N     . LYS A 1 366 ? 156.323 138.765 103.893 1.00 19.78 ? 366 LYS A N     1 
ATOM   2966  C  CA    . LYS A 1 366 ? 157.365 138.986 102.899 1.00 21.89 ? 366 LYS A CA    1 
ATOM   2967  C  C     . LYS A 1 366 ? 156.832 139.713 101.674 1.00 26.05 ? 366 LYS A C     1 
ATOM   2968  O  O     . LYS A 1 366 ? 157.614 140.326 100.940 1.00 30.74 ? 366 LYS A O     1 
ATOM   2969  C  CB    . LYS A 1 366 ? 158.006 137.658 102.492 1.00 18.03 ? 366 LYS A CB    1 
ATOM   2970  C  CG    . LYS A 1 366 ? 157.117 136.757 101.658 1.00 27.17 ? 366 LYS A CG    1 
ATOM   2971  C  CD    . LYS A 1 366 ? 157.945 135.774 100.846 1.00 29.54 ? 366 LYS A CD    1 
ATOM   2972  C  CE    . LYS A 1 366 ? 158.419 134.612 101.703 1.00 23.52 ? 366 LYS A CE    1 
ATOM   2973  N  NZ    . LYS A 1 366 ? 159.605 133.937 101.109 1.00 30.84 ? 366 LYS A NZ    1 
ATOM   2974  N  N     . VAL A 1 367 ? 155.522 139.661 101.444 1.00 25.57 ? 367 VAL A N     1 
ATOM   2975  C  CA    . VAL A 1 367 ? 154.870 140.388 100.364 1.00 13.33 ? 367 VAL A CA    1 
ATOM   2976  C  C     . VAL A 1 367 ? 153.908 141.445 100.878 1.00 21.28 ? 367 VAL A C     1 
ATOM   2977  O  O     . VAL A 1 367 ? 153.246 142.106 100.073 1.00 27.09 ? 367 VAL A O     1 
ATOM   2978  C  CB    . VAL A 1 367 ? 154.142 139.427 99.404  1.00 16.88 ? 367 VAL A CB    1 
ATOM   2979  C  CG1   . VAL A 1 367 ? 155.137 138.752 98.481  1.00 23.05 ? 367 VAL A CG1   1 
ATOM   2980  C  CG2   . VAL A 1 367 ? 153.367 138.391 100.191 1.00 13.74 ? 367 VAL A CG2   1 
ATOM   2981  N  N     . HIS A 1 368 ? 153.809 141.620 102.193 1.00 20.20 ? 368 HIS A N     1 
ATOM   2982  C  CA    . HIS A 1 368 ? 152.910 142.611 102.767 1.00 10.27 ? 368 HIS A CA    1 
ATOM   2983  C  C     . HIS A 1 368 ? 153.363 144.016 102.390 1.00 14.67 ? 368 HIS A C     1 
ATOM   2984  O  O     . HIS A 1 368 ? 154.541 144.358 102.519 1.00 24.31 ? 368 HIS A O     1 
ATOM   2985  C  CB    . HIS A 1 368 ? 152.864 142.452 104.284 1.00 9.20  ? 368 HIS A CB    1 
ATOM   2986  C  CG    . HIS A 1 368 ? 151.923 143.393 104.965 1.00 10.66 ? 368 HIS A CG    1 
ATOM   2987  N  ND1   . HIS A 1 368 ? 152.134 143.852 106.247 1.00 18.64 ? 368 HIS A ND1   1 
ATOM   2988  C  CD2   . HIS A 1 368 ? 150.767 143.958 104.549 1.00 5.53  ? 368 HIS A CD2   1 
ATOM   2989  C  CE1   . HIS A 1 368 ? 151.148 144.659 106.590 1.00 14.62 ? 368 HIS A CE1   1 
ATOM   2990  N  NE2   . HIS A 1 368 ? 150.305 144.741 105.577 1.00 10.90 ? 368 HIS A NE2   1 
ATOM   2991  N  N     . ALA A 1 369 ? 152.417 144.830 101.923 1.00 18.67 ? 369 ALA A N     1 
ATOM   2992  C  CA    . ALA A 1 369 ? 152.742 146.151 101.404 1.00 8.47  ? 369 ALA A CA    1 
ATOM   2993  C  C     . ALA A 1 369 ? 152.815 147.223 102.482 1.00 19.05 ? 369 ALA A C     1 
ATOM   2994  O  O     . ALA A 1 369 ? 153.331 148.313 102.213 1.00 24.60 ? 369 ALA A O     1 
ATOM   2995  C  CB    . ALA A 1 369 ? 151.714 146.563 100.351 1.00 14.33 ? 369 ALA A CB    1 
ATOM   2996  N  N     . ASN A 1 370 ? 152.325 146.947 103.686 1.00 18.75 ? 370 ASN A N     1 
ATOM   2997  C  CA    . ASN A 1 370 ? 152.223 147.949 104.741 1.00 9.79  ? 370 ASN A CA    1 
ATOM   2998  C  C     . ASN A 1 370 ? 152.890 147.459 106.015 1.00 7.91  ? 370 ASN A C     1 
ATOM   2999  O  O     . ASN A 1 370 ? 152.349 147.576 107.115 1.00 17.07 ? 370 ASN A O     1 
ATOM   3000  C  CB    . ASN A 1 370 ? 150.766 148.312 105.004 1.00 10.49 ? 370 ASN A CB    1 
ATOM   3001  C  CG    . ASN A 1 370 ? 150.073 148.858 103.777 1.00 11.77 ? 370 ASN A CG    1 
ATOM   3002  O  OD1   . ASN A 1 370 ? 150.512 149.846 103.194 1.00 27.25 ? 370 ASN A OD1   1 
ATOM   3003  N  ND2   . ASN A 1 370 ? 148.984 148.217 103.378 1.00 13.50 ? 370 ASN A ND2   1 
ATOM   3004  N  N     . ASN A 1 371 ? 154.092 146.896 105.881 1.00 17.69 ? 371 ASN A N     1 
ATOM   3005  C  CA    . ASN A 1 371 ? 154.840 146.472 107.057 1.00 11.20 ? 371 ASN A CA    1 
ATOM   3006  C  C     . ASN A 1 371 ? 155.315 147.653 107.892 1.00 19.27 ? 371 ASN A C     1 
ATOM   3007  O  O     . ASN A 1 371 ? 155.601 147.479 109.081 1.00 21.95 ? 371 ASN A O     1 
ATOM   3008  C  CB    . ASN A 1 371 ? 156.036 145.615 106.645 1.00 6.67  ? 371 ASN A CB    1 
ATOM   3009  C  CG    . ASN A 1 371 ? 155.666 144.166 106.433 1.00 15.83 ? 371 ASN A CG    1 
ATOM   3010  O  OD1   . ASN A 1 371 ? 154.676 143.680 106.974 1.00 23.20 ? 371 ASN A OD1   1 
ATOM   3011  N  ND2   . ASN A 1 371 ? 156.466 143.463 105.643 1.00 18.30 ? 371 ASN A ND2   1 
ATOM   3012  N  N     . HIS A 1 372 ? 155.414 148.842 107.294 1.00 19.76 ? 372 HIS A N     1 
ATOM   3013  C  CA    . HIS A 1 372 ? 155.775 150.031 108.057 1.00 16.32 ? 372 HIS A CA    1 
ATOM   3014  C  C     . HIS A 1 372 ? 154.717 150.356 109.103 1.00 20.32 ? 372 HIS A C     1 
ATOM   3015  O  O     . HIS A 1 372 ? 155.047 150.738 110.231 1.00 30.29 ? 372 HIS A O     1 
ATOM   3016  C  CB    . HIS A 1 372 ? 155.984 151.214 107.113 1.00 18.30 ? 372 HIS A CB    1 
ATOM   3017  C  CG    . HIS A 1 372 ? 154.728 151.679 106.446 1.00 19.42 ? 372 HIS A CG    1 
ATOM   3018  N  ND1   . HIS A 1 372 ? 153.993 150.874 105.603 1.00 18.87 ? 372 HIS A ND1   1 
ATOM   3019  C  CD2   . HIS A 1 372 ? 154.070 152.859 106.508 1.00 23.10 ? 372 HIS A CD2   1 
ATOM   3020  C  CE1   . HIS A 1 372 ? 152.940 151.540 105.170 1.00 18.02 ? 372 HIS A CE1   1 
ATOM   3021  N  NE2   . HIS A 1 372 ? 152.963 152.748 105.703 1.00 23.56 ? 372 HIS A NE2   1 
ATOM   3022  N  N     . ILE A 1 373 ? 153.440 150.226 108.743 1.00 14.06 ? 373 ILE A N     1 
ATOM   3023  C  CA    . ILE A 1 373 ? 152.372 150.412 109.719 1.00 14.90 ? 373 ILE A CA    1 
ATOM   3024  C  C     . ILE A 1 373 ? 152.445 149.332 110.789 1.00 18.56 ? 373 ILE A C     1 
ATOM   3025  O  O     . ILE A 1 373 ? 152.467 149.623 111.990 1.00 29.65 ? 373 ILE A O     1 
ATOM   3026  C  CB    . ILE A 1 373 ? 151.001 150.416 109.019 1.00 17.52 ? 373 ILE A CB    1 
ATOM   3027  C  CG1   . ILE A 1 373 ? 150.916 151.561 108.010 1.00 17.06 ? 373 ILE A CG1   1 
ATOM   3028  C  CG2   . ILE A 1 373 ? 149.877 150.509 110.038 1.00 17.68 ? 373 ILE A CG2   1 
ATOM   3029  C  CD1   . ILE A 1 373 ? 149.740 151.461 107.070 1.00 13.58 ? 373 ILE A CD1   1 
ATOM   3030  N  N     . SER A 1 374 ? 152.513 148.074 110.364 1.00 19.44 ? 374 SER A N     1 
ATOM   3031  C  CA    . SER A 1 374 ? 152.576 146.919 111.246 1.00 12.75 ? 374 SER A CA    1 
ATOM   3032  C  C     . SER A 1 374 ? 152.712 145.676 110.382 1.00 15.79 ? 374 SER A C     1 
ATOM   3033  O  O     . SER A 1 374 ? 152.394 145.691 109.191 1.00 14.98 ? 374 SER A O     1 
ATOM   3034  C  CB    . SER A 1 374 ? 151.336 146.805 112.135 1.00 17.58 ? 374 SER A CB    1 
ATOM   3035  O  OG    . SER A 1 374 ? 151.483 145.766 113.080 1.00 24.95 ? 374 SER A OG    1 
ATOM   3036  N  N     . LYS A 1 375 ? 153.189 144.601 110.996 1.00 23.05 ? 375 LYS A N     1 
ATOM   3037  C  CA    . LYS A 1 375 ? 153.160 143.300 110.352 1.00 15.89 ? 375 LYS A CA    1 
ATOM   3038  C  C     . LYS A 1 375 ? 151.810 142.639 110.583 1.00 14.24 ? 375 LYS A C     1 
ATOM   3039  O  O     . LYS A 1 375 ? 151.129 142.900 111.578 1.00 25.84 ? 375 LYS A O     1 
ATOM   3040  C  CB    . LYS A 1 375 ? 154.276 142.405 110.886 1.00 11.81 ? 375 LYS A CB    1 
ATOM   3041  C  CG    . LYS A 1 375 ? 155.655 143.021 110.809 1.00 19.53 ? 375 LYS A CG    1 
ATOM   3042  C  CD    . LYS A 1 375 ? 156.529 142.262 109.833 1.00 19.36 ? 375 LYS A CD    1 
ATOM   3043  C  CE    . LYS A 1 375 ? 157.839 142.981 109.581 1.00 20.41 ? 375 LYS A CE    1 
ATOM   3044  N  NZ    . LYS A 1 375 ? 158.558 142.403 108.413 1.00 24.71 ? 375 LYS A NZ    1 
ATOM   3045  N  N     . VAL A 1 376 ? 151.417 141.782 109.645 1.00 11.08 ? 376 VAL A N     1 
ATOM   3046  C  CA    . VAL A 1 376 ? 150.189 141.018 109.819 1.00 17.42 ? 376 VAL A CA    1 
ATOM   3047  C  C     . VAL A 1 376 ? 150.440 139.941 110.865 1.00 13.76 ? 376 VAL A C     1 
ATOM   3048  O  O     . VAL A 1 376 ? 151.333 139.100 110.711 1.00 20.40 ? 376 VAL A O     1 
ATOM   3049  C  CB    . VAL A 1 376 ? 149.723 140.413 108.490 1.00 12.71 ? 376 VAL A CB    1 
ATOM   3050  C  CG1   . VAL A 1 376 ? 148.406 139.684 108.677 1.00 14.56 ? 376 VAL A CG1   1 
ATOM   3051  C  CG2   . VAL A 1 376 ? 149.594 141.494 107.434 1.00 3.78  ? 376 VAL A CG2   1 
ATOM   3052  N  N     . LYS A 1 377 ? 149.656 139.968 111.943 1.00 16.95 ? 377 LYS A N     1 
ATOM   3053  C  CA    . LYS A 1 377 ? 149.846 139.041 113.046 1.00 11.63 ? 377 LYS A CA    1 
ATOM   3054  C  C     . LYS A 1 377 ? 148.761 137.985 113.155 1.00 12.60 ? 377 LYS A C     1 
ATOM   3055  O  O     . LYS A 1 377 ? 148.959 137.003 113.872 1.00 27.55 ? 377 LYS A O     1 
ATOM   3056  C  CB    . LYS A 1 377 ? 149.921 139.798 114.380 1.00 13.67 ? 377 LYS A CB    1 
ATOM   3057  C  CG    . LYS A 1 377 ? 150.827 141.007 114.367 1.00 11.73 ? 377 LYS A CG    1 
ATOM   3058  C  CD    . LYS A 1 377 ? 150.381 142.004 115.414 1.00 22.22 ? 377 LYS A CD    1 
ATOM   3059  C  CE    . LYS A 1 377 ? 150.637 143.424 114.970 1.00 19.20 ? 377 LYS A CE    1 
ATOM   3060  N  NZ    . LYS A 1 377 ? 149.946 144.403 115.850 1.00 20.03 ? 377 LYS A NZ    1 
ATOM   3061  N  N     . PHE A 1 378 ? 147.628 138.166 112.484 1.00 13.25 ? 378 PHE A N     1 
ATOM   3062  C  CA    . PHE A 1 378 ? 146.552 137.188 112.537 1.00 7.61  ? 378 PHE A CA    1 
ATOM   3063  C  C     . PHE A 1 378 ? 145.592 137.451 111.389 1.00 11.07 ? 378 PHE A C     1 
ATOM   3064  O  O     . PHE A 1 378 ? 145.624 138.510 110.756 1.00 19.69 ? 378 PHE A O     1 
ATOM   3065  C  CB    . PHE A 1 378 ? 145.824 137.212 113.890 1.00 7.08  ? 378 PHE A CB    1 
ATOM   3066  C  CG    . PHE A 1 378 ? 144.999 138.448 114.139 1.00 6.32  ? 378 PHE A CG    1 
ATOM   3067  C  CD1   . PHE A 1 378 ? 145.539 139.714 113.997 1.00 11.09 ? 378 PHE A CD1   1 
ATOM   3068  C  CD2   . PHE A 1 378 ? 143.684 138.335 114.555 1.00 4.55  ? 378 PHE A CD2   1 
ATOM   3069  C  CE1   . PHE A 1 378 ? 144.780 140.838 114.240 1.00 8.68  ? 378 PHE A CE1   1 
ATOM   3070  C  CE2   . PHE A 1 378 ? 142.923 139.455 114.802 1.00 10.88 ? 378 PHE A CE2   1 
ATOM   3071  C  CZ    . PHE A 1 378 ? 143.473 140.708 114.646 1.00 9.50  ? 378 PHE A CZ    1 
ATOM   3072  N  N     . SER A 1 379 ? 144.748 136.464 111.119 1.00 5.66  ? 379 SER A N     1 
ATOM   3073  C  CA    . SER A 1 379 ? 143.754 136.531 110.064 1.00 7.09  ? 379 SER A CA    1 
ATOM   3074  C  C     . SER A 1 379 ? 142.366 136.662 110.681 1.00 8.53  ? 379 SER A C     1 
ATOM   3075  O  O     . SER A 1 379 ? 142.214 136.817 111.897 1.00 16.81 ? 379 SER A O     1 
ATOM   3076  C  CB    . SER A 1 379 ? 143.865 135.307 109.154 1.00 13.43 ? 379 SER A CB    1 
ATOM   3077  O  OG    . SER A 1 379 ? 143.461 135.624 107.835 1.00 15.33 ? 379 SER A OG    1 
ATOM   3078  N  N     . ASN A 1 380 ? 141.346 136.614 109.833 1.00 9.40  ? 380 ASN A N     1 
ATOM   3079  C  CA    . ASN A 1 380 ? 139.970 136.778 110.261 1.00 8.41  ? 380 ASN A CA    1 
ATOM   3080  C  C     . ASN A 1 380 ? 139.332 135.414 110.518 1.00 16.15 ? 380 ASN A C     1 
ATOM   3081  O  O     . ASN A 1 380 ? 140.001 134.377 110.527 1.00 20.07 ? 380 ASN A O     1 
ATOM   3082  C  CB    . ASN A 1 380 ? 139.191 137.586 109.223 1.00 10.08 ? 380 ASN A CB    1 
ATOM   3083  C  CG    . ASN A 1 380 ? 139.084 136.880 107.893 1.00 7.24  ? 380 ASN A CG    1 
ATOM   3084  O  OD1   . ASN A 1 380 ? 140.043 136.278 107.417 1.00 18.14 ? 380 ASN A OD1   1 
ATOM   3085  N  ND2   . ASN A 1 380 ? 137.912 136.954 107.281 1.00 14.68 ? 380 ASN A ND2   1 
ATOM   3086  N  N     . LEU A 1 381 ? 138.018 135.417 110.747 1.00 17.20 ? 381 LEU A N     1 
ATOM   3087  C  CA    . LEU A 1 381 ? 137.298 134.171 110.974 1.00 10.58 ? 381 LEU A CA    1 
ATOM   3088  C  C     . LEU A 1 381 ? 137.286 133.295 109.728 1.00 10.12 ? 381 LEU A C     1 
ATOM   3089  O  O     . LEU A 1 381 ? 137.273 132.065 109.836 1.00 20.39 ? 381 LEU A O     1 
ATOM   3090  C  CB    . LEU A 1 381 ? 135.873 134.477 111.437 1.00 13.00 ? 381 LEU A CB    1 
ATOM   3091  C  CG    . LEU A 1 381 ? 134.868 133.331 111.553 1.00 16.03 ? 381 LEU A CG    1 
ATOM   3092  C  CD1   . LEU A 1 381 ? 135.196 132.435 112.733 1.00 16.92 ? 381 LEU A CD1   1 
ATOM   3093  C  CD2   . LEU A 1 381 ? 133.464 133.887 111.670 1.00 17.58 ? 381 LEU A CD2   1 
ATOM   3094  N  N     . CYS A 1 382 ? 137.293 133.902 108.545 1.00 18.79 ? 382 CYS A N     1 
ATOM   3095  C  CA    . CYS A 1 382 ? 137.353 133.160 107.294 1.00 13.10 ? 382 CYS A CA    1 
ATOM   3096  C  C     . CYS A 1 382 ? 138.780 132.943 106.809 1.00 8.72  ? 382 CYS A C     1 
ATOM   3097  O  O     . CYS A 1 382 ? 138.974 132.315 105.764 1.00 17.68 ? 382 CYS A O     1 
ATOM   3098  C  CB    . CYS A 1 382 ? 136.537 133.880 106.217 1.00 19.27 ? 382 CYS A CB    1 
ATOM   3099  S  SG    . CYS A 1 382 ? 134.826 134.218 106.686 1.00 28.62 ? 382 CYS A SG    1 
ATOM   3100  N  N     . SER A 1 383 ? 139.772 133.452 107.541 1.00 15.91 ? 383 SER A N     1 
ATOM   3101  C  CA    . SER A 1 383 ? 141.186 133.155 107.300 1.00 10.72 ? 383 SER A CA    1 
ATOM   3102  C  C     . SER A 1 383 ? 141.653 133.653 105.933 1.00 12.76 ? 383 SER A C     1 
ATOM   3103  O  O     . SER A 1 383 ? 142.451 133.002 105.257 1.00 24.86 ? 383 SER A O     1 
ATOM   3104  C  CB    . SER A 1 383 ? 141.463 131.658 107.457 1.00 16.08 ? 383 SER A CB    1 
ATOM   3105  O  OG    . SER A 1 383 ? 142.841 131.370 107.309 1.00 24.59 ? 383 SER A OG    1 
ATOM   3106  N  N     . GLU A 1 384 ? 141.160 134.820 105.518 1.00 13.93 ? 384 GLU A N     1 
ATOM   3107  C  CA    . GLU A 1 384 ? 141.641 135.421 104.279 1.00 6.97  ? 384 GLU A CA    1 
ATOM   3108  C  C     . GLU A 1 384 ? 141.959 136.905 104.389 1.00 15.05 ? 384 GLU A C     1 
ATOM   3109  O  O     . GLU A 1 384 ? 142.636 137.429 103.501 1.00 21.82 ? 384 GLU A O     1 
ATOM   3110  C  CB    . GLU A 1 384 ? 140.630 135.196 103.141 1.00 9.97  ? 384 GLU A CB    1 
ATOM   3111  C  CG    . GLU A 1 384 ? 139.808 136.405 102.720 1.00 11.74 ? 384 GLU A CG    1 
ATOM   3112  C  CD    . GLU A 1 384 ? 138.669 136.706 103.667 1.00 21.78 ? 384 GLU A CD    1 
ATOM   3113  O  OE1   . GLU A 1 384 ? 138.283 135.807 104.439 1.00 15.73 ? 384 GLU A OE1   1 
ATOM   3114  O  OE2   . GLU A 1 384 ? 138.145 137.837 103.624 1.00 27.75 ? 384 GLU A OE2   1 
ATOM   3115  N  N     . VAL A 1 385 ? 141.525 137.595 105.436 1.00 17.78 ? 385 VAL A N     1 
ATOM   3116  C  CA    . VAL A 1 385 ? 141.860 139.000 105.631 1.00 5.61  ? 385 VAL A CA    1 
ATOM   3117  C  C     . VAL A 1 385 ? 143.230 139.074 106.289 1.00 14.92 ? 385 VAL A C     1 
ATOM   3118  O  O     . VAL A 1 385 ? 143.434 138.529 107.378 1.00 21.69 ? 385 VAL A O     1 
ATOM   3119  C  CB    . VAL A 1 385 ? 140.801 139.715 106.481 1.00 6.86  ? 385 VAL A CB    1 
ATOM   3120  C  CG1   . VAL A 1 385 ? 141.251 141.123 106.781 1.00 7.76  ? 385 VAL A CG1   1 
ATOM   3121  C  CG2   . VAL A 1 385 ? 139.471 139.730 105.765 1.00 7.26  ? 385 VAL A CG2   1 
ATOM   3122  N  N     . LEU A 1 386 ? 144.170 139.748 105.628 1.00 16.25 ? 386 LEU A N     1 
ATOM   3123  C  CA    . LEU A 1 386 ? 145.559 139.839 106.079 1.00 2.88  ? 386 LEU A CA    1 
ATOM   3124  C  C     . LEU A 1 386 ? 146.002 141.293 105.962 1.00 4.72  ? 386 LEU A C     1 
ATOM   3125  O  O     . LEU A 1 386 ? 146.517 141.714 104.924 1.00 11.79 ? 386 LEU A O     1 
ATOM   3126  C  CB    . LEU A 1 386 ? 146.450 138.906 105.272 1.00 2.63  ? 386 LEU A CB    1 
ATOM   3127  C  CG    . LEU A 1 386 ? 146.182 137.421 105.503 1.00 7.24  ? 386 LEU A CG    1 
ATOM   3128  C  CD1   . LEU A 1 386 ? 147.038 136.586 104.591 1.00 10.45 ? 386 LEU A CD1   1 
ATOM   3129  C  CD2   . LEU A 1 386 ? 146.438 137.056 106.953 1.00 12.92 ? 386 LEU A CD2   1 
ATOM   3130  N  N     . GLN A 1 387 ? 145.807 142.054 107.035 1.00 13.68 ? 387 GLN A N     1 
ATOM   3131  C  CA    . GLN A 1 387 ? 146.093 143.479 107.052 1.00 10.04 ? 387 GLN A CA    1 
ATOM   3132  C  C     . GLN A 1 387 ? 146.873 143.837 108.308 1.00 13.14 ? 387 GLN A C     1 
ATOM   3133  O  O     . GLN A 1 387 ? 146.858 143.111 109.304 1.00 26.08 ? 387 GLN A O     1 
ATOM   3134  C  CB    . GLN A 1 387 ? 144.803 144.308 106.981 1.00 5.14  ? 387 GLN A CB    1 
ATOM   3135  C  CG    . GLN A 1 387 ? 143.910 143.957 105.810 1.00 7.83  ? 387 GLN A CG    1 
ATOM   3136  C  CD    . GLN A 1 387 ? 142.685 144.830 105.737 1.00 8.88  ? 387 GLN A CD    1 
ATOM   3137  O  OE1   . GLN A 1 387 ? 142.610 145.867 106.392 1.00 26.41 ? 387 GLN A OE1   1 
ATOM   3138  N  NE2   . GLN A 1 387 ? 141.710 144.416 104.941 1.00 13.87 ? 387 GLN A NE2   1 
ATOM   3139  N  N     . ALA A 1 388 ? 147.567 144.968 108.243 1.00 12.57 ? 388 ALA A N     1 
ATOM   3140  C  CA    . ALA A 1 388 ? 148.309 145.461 109.393 1.00 10.63 ? 388 ALA A CA    1 
ATOM   3141  C  C     . ALA A 1 388 ? 147.356 145.961 110.470 1.00 12.93 ? 388 ALA A C     1 
ATOM   3142  O  O     . ALA A 1 388 ? 146.352 146.617 110.180 1.00 24.80 ? 388 ALA A O     1 
ATOM   3143  C  CB    . ALA A 1 388 ? 149.258 146.581 108.971 1.00 12.38 ? 388 ALA A CB    1 
ATOM   3144  N  N     . SER A 1 389 ? 147.672 145.646 111.722 1.00 19.15 ? 389 SER A N     1 
ATOM   3145  C  CA    . SER A 1 389 ? 146.876 146.079 112.859 1.00 13.70 ? 389 SER A CA    1 
ATOM   3146  C  C     . SER A 1 389 ? 147.785 146.634 113.943 1.00 15.84 ? 389 SER A C     1 
ATOM   3147  O  O     . SER A 1 389 ? 148.915 146.175 114.126 1.00 23.31 ? 389 SER A O     1 
ATOM   3148  C  CB    . SER A 1 389 ? 146.033 144.935 113.435 1.00 14.91 ? 389 SER A CB    1 
ATOM   3149  O  OG    . SER A 1 389 ? 146.829 143.796 113.706 1.00 26.65 ? 389 SER A OG    1 
ATOM   3150  N  N     . GLN A 1 390 ? 147.277 147.629 114.662 1.00 18.13 ? 390 GLN A N     1 
ATOM   3151  C  CA    . GLN A 1 390 ? 147.950 148.195 115.821 1.00 15.26 ? 390 GLN A CA    1 
ATOM   3152  C  C     . GLN A 1 390 ? 147.044 148.030 117.030 1.00 14.81 ? 390 GLN A C     1 
ATOM   3153  O  O     . GLN A 1 390 ? 145.867 148.401 116.982 1.00 27.13 ? 390 GLN A O     1 
ATOM   3154  C  CB    . GLN A 1 390 ? 148.291 149.669 115.599 1.00 18.29 ? 390 GLN A CB    1 
ATOM   3155  C  CG    . GLN A 1 390 ? 149.328 149.901 114.517 1.00 17.66 ? 390 GLN A CG    1 
ATOM   3156  C  CD    . GLN A 1 390 ? 149.502 151.365 114.179 1.00 23.72 ? 390 GLN A CD    1 
ATOM   3157  O  OE1   . GLN A 1 390 ? 148.734 152.214 114.630 1.00 31.54 ? 390 GLN A OE1   1 
ATOM   3158  N  NE2   . GLN A 1 390 ? 150.517 151.670 113.381 1.00 22.11 ? 390 GLN A NE2   1 
ATOM   3159  N  N     . VAL A 1 391 ? 147.589 147.467 118.108 1.00 24.22 ? 391 VAL A N     1 
ATOM   3160  C  CA    . VAL A 1 391 ? 146.780 147.182 119.284 1.00 25.39 ? 391 VAL A CA    1 
ATOM   3161  C  C     . VAL A 1 391 ? 146.387 148.482 119.976 1.00 26.53 ? 391 VAL A C     1 
ATOM   3162  O  O     . VAL A 1 391 ? 147.127 149.476 119.969 1.00 27.08 ? 391 VAL A O     1 
ATOM   3163  C  CB    . VAL A 1 391 ? 147.527 146.234 120.243 1.00 17.48 ? 391 VAL A CB    1 
ATOM   3164  C  CG1   . VAL A 1 391 ? 148.593 146.980 121.029 1.00 22.37 ? 391 VAL A CG1   1 
ATOM   3165  C  CG2   . VAL A 1 391 ? 146.550 145.545 121.180 1.00 16.53 ? 391 VAL A CG2   1 
ATOM   3166  N  N     . SER A 1 392 ? 145.192 148.486 120.555 1.00 29.10 ? 392 SER A N     1 
ATOM   3167  C  CA    . SER A 1 392 ? 144.709 149.620 121.322 1.00 19.82 ? 392 SER A CA    1 
ATOM   3168  C  C     . SER A 1 392 ? 145.111 149.477 122.784 1.00 29.19 ? 392 SER A C     1 
ATOM   3169  O  O     . SER A 1 392 ? 145.421 148.387 123.267 1.00 37.02 ? 392 SER A O     1 
ATOM   3170  C  CB    . SER A 1 392 ? 143.190 149.747 121.206 1.00 25.32 ? 392 SER A CB    1 
ATOM   3171  O  OG    . SER A 1 392 ? 142.800 150.045 119.878 1.00 33.86 ? 392 SER A OG    1 
ATOM   3172  N  N     . SER A 1 393 ? 145.104 150.603 123.489 1.00 33.63 ? 393 SER A N     1 
ATOM   3173  C  CA    . SER A 1 393 ? 145.418 150.647 124.914 1.00 31.68 ? 393 SER A CA    1 
ATOM   3174  C  C     . SER A 1 393 ? 144.200 151.218 125.631 1.00 32.43 ? 393 SER A C     1 
ATOM   3175  O  O     . SER A 1 393 ? 144.116 152.424 125.875 1.00 35.28 ? 393 SER A O     1 
ATOM   3176  C  CB    . SER A 1 393 ? 146.672 151.473 125.179 1.00 32.75 ? 393 SER A CB    1 
ATOM   3177  O  OG    . SER A 1 393 ? 146.946 151.550 126.566 1.00 39.68 ? 393 SER A OG    1 
ATOM   3178  N  N     . TYR A 1 394 ? 143.255 150.346 125.966 1.00 34.04 ? 394 TYR A N     1 
ATOM   3179  C  CA    . TYR A 1 394 ? 142.064 150.757 126.694 1.00 32.15 ? 394 TYR A CA    1 
ATOM   3180  C  C     . TYR A 1 394 ? 142.406 150.883 128.172 1.00 35.45 ? 394 TYR A C     1 
ATOM   3181  O  O     . TYR A 1 394 ? 142.777 149.897 128.818 1.00 37.24 ? 394 TYR A O     1 
ATOM   3182  C  CB    . TYR A 1 394 ? 140.929 149.760 126.473 1.00 29.27 ? 394 TYR A CB    1 
ATOM   3183  C  CG    . TYR A 1 394 ? 140.475 149.677 125.034 1.00 29.94 ? 394 TYR A CG    1 
ATOM   3184  C  CD1   . TYR A 1 394 ? 139.762 150.715 124.450 1.00 31.30 ? 394 TYR A CD1   1 
ATOM   3185  C  CD2   . TYR A 1 394 ? 140.763 148.563 124.258 1.00 31.20 ? 394 TYR A CD2   1 
ATOM   3186  C  CE1   . TYR A 1 394 ? 139.347 150.644 123.137 1.00 33.45 ? 394 TYR A CE1   1 
ATOM   3187  C  CE2   . TYR A 1 394 ? 140.352 148.483 122.945 1.00 31.01 ? 394 TYR A CE2   1 
ATOM   3188  C  CZ    . TYR A 1 394 ? 139.645 149.526 122.388 1.00 37.67 ? 394 TYR A CZ    1 
ATOM   3189  O  OH    . TYR A 1 394 ? 139.234 149.450 121.077 1.00 39.96 ? 394 TYR A OH    1 
ATOM   3190  N  N     . THR A 1 395 ? 142.286 152.092 128.700 1.00 34.84 ? 395 THR A N     1 
ATOM   3191  C  CA    . THR A 1 395 ? 142.709 152.420 130.048 1.00 37.61 ? 395 THR A CA    1 
ATOM   3192  C  C     . THR A 1 395 ? 141.503 152.429 130.985 1.00 38.41 ? 395 THR A C     1 
ATOM   3193  O  O     . THR A 1 395 ? 140.403 152.000 130.625 1.00 36.08 ? 395 THR A O     1 
ATOM   3194  C  CB    . THR A 1 395 ? 143.443 153.761 130.042 1.00 37.09 ? 395 THR A CB    1 
ATOM   3195  O  OG1   . THR A 1 395 ? 142.580 154.775 129.517 1.00 38.45 ? 395 THR A OG1   1 
ATOM   3196  C  CG2   . THR A 1 395 ? 144.686 153.673 129.174 1.00 35.49 ? 395 THR A CG2   1 
ATOM   3197  N  N     . ASP A 1 396 ? 141.712 152.909 132.209 1.00 39.69 ? 396 ASP A N     1 
ATOM   3198  C  CA    . ASP A 1 396 ? 140.635 152.999 133.181 1.00 35.13 ? 396 ASP A CA    1 
ATOM   3199  C  C     . ASP A 1 396 ? 139.535 153.933 132.677 1.00 37.09 ? 396 ASP A C     1 
ATOM   3200  O  O     . ASP A 1 396 ? 139.681 154.636 131.675 1.00 43.47 ? 396 ASP A O     1 
ATOM   3201  C  CB    . ASP A 1 396 ? 141.167 153.485 134.528 1.00 37.77 ? 396 ASP A CB    1 
ATOM   3202  C  CG    . ASP A 1 396 ? 142.166 152.524 135.142 1.00 42.21 ? 396 ASP A CG    1 
ATOM   3203  O  OD1   . ASP A 1 396 ? 141.848 151.321 135.243 1.00 39.53 ? 396 ASP A OD1   1 
ATOM   3204  O  OD2   . ASP A 1 396 ? 143.266 152.971 135.527 1.00 44.04 ? 396 ASP A OD2   1 
ATOM   3205  N  N     . TYR A 1 397 ? 138.413 153.929 133.399 1.00 34.23 ? 397 TYR A N     1 
ATOM   3206  C  CA    . TYR A 1 397 ? 137.250 154.698 132.968 1.00 35.81 ? 397 TYR A CA    1 
ATOM   3207  C  C     . TYR A 1 397 ? 137.559 156.188 132.900 1.00 37.74 ? 397 TYR A C     1 
ATOM   3208  O  O     . TYR A 1 397 ? 137.154 156.871 131.953 1.00 40.95 ? 397 TYR A O     1 
ATOM   3209  C  CB    . TYR A 1 397 ? 136.073 154.438 133.910 1.00 30.56 ? 397 TYR A CB    1 
ATOM   3210  C  CG    . TYR A 1 397 ? 134.803 155.149 133.507 1.00 32.57 ? 397 TYR A CG    1 
ATOM   3211  C  CD1   . TYR A 1 397 ? 133.924 154.576 132.599 1.00 32.60 ? 397 TYR A CD1   1 
ATOM   3212  C  CD2   . TYR A 1 397 ? 134.486 156.396 134.029 1.00 34.27 ? 397 TYR A CD2   1 
ATOM   3213  C  CE1   . TYR A 1 397 ? 132.764 155.223 132.225 1.00 29.55 ? 397 TYR A CE1   1 
ATOM   3214  C  CE2   . TYR A 1 397 ? 133.331 157.050 133.660 1.00 33.82 ? 397 TYR A CE2   1 
ATOM   3215  C  CZ    . TYR A 1 397 ? 132.473 156.459 132.760 1.00 35.16 ? 397 TYR A CZ    1 
ATOM   3216  O  OH    . TYR A 1 397 ? 131.320 157.109 132.392 1.00 39.35 ? 397 TYR A OH    1 
ATOM   3217  N  N     . ASP A 1 398 ? 138.278 156.710 133.892 1.00 40.35 ? 398 ASP A N     1 
ATOM   3218  C  CA    . ASP A 1 398 ? 138.574 158.134 133.952 1.00 39.93 ? 398 ASP A CA    1 
ATOM   3219  C  C     . ASP A 1 398 ? 139.648 158.569 132.964 1.00 45.77 ? 398 ASP A C     1 
ATOM   3220  O  O     . ASP A 1 398 ? 139.757 159.768 132.685 1.00 46.54 ? 398 ASP A O     1 
ATOM   3221  C  CB    . ASP A 1 398 ? 139.003 158.515 135.371 1.00 44.00 ? 398 ASP A CB    1 
ATOM   3222  C  CG    . ASP A 1 398 ? 139.872 157.454 136.020 1.00 47.66 ? 398 ASP A CG    1 
ATOM   3223  O  OD1   . ASP A 1 398 ? 139.359 156.348 136.288 1.00 44.75 ? 398 ASP A OD1   1 
ATOM   3224  O  OD2   . ASP A 1 398 ? 141.067 157.725 136.262 1.00 46.71 ? 398 ASP A OD2   1 
ATOM   3225  N  N     . GLU A 1 399 ? 140.432 157.640 132.427 1.00 46.89 ? 399 GLU A N     1 
ATOM   3226  C  CA    . GLU A 1 399 ? 141.552 157.968 131.560 1.00 42.99 ? 399 GLU A CA    1 
ATOM   3227  C  C     . GLU A 1 399 ? 141.172 157.816 130.092 1.00 44.96 ? 399 GLU A C     1 
ATOM   3228  O  O     . GLU A 1 399 ? 140.249 157.082 129.733 1.00 44.67 ? 399 GLU A O     1 
ATOM   3229  C  CB    . GLU A 1 399 ? 142.758 157.080 131.879 1.00 42.34 ? 399 GLU A CB    1 
ATOM   3230  C  CG    . GLU A 1 399 ? 142.812 156.603 133.317 1.00 44.81 ? 399 GLU A CG    1 
ATOM   3231  C  CD    . GLU A 1 399 ? 144.156 156.004 133.680 1.00 50.07 ? 399 GLU A CD    1 
ATOM   3232  O  OE1   . GLU A 1 399 ? 144.448 154.878 133.224 1.00 45.73 ? 399 GLU A OE1   1 
ATOM   3233  O  OE2   . GLU A 1 399 ? 144.919 156.657 134.423 1.00 49.39 ? 399 GLU A OE2   1 
ATOM   3234  N  N     . GLU A 1 400 ? 141.905 158.531 129.243 1.00 42.43 ? 400 GLU A N     1 
ATOM   3235  C  CA    . GLU A 1 400 ? 141.700 158.438 127.805 1.00 40.58 ? 400 GLU A CA    1 
ATOM   3236  C  C     . GLU A 1 400 ? 142.316 157.156 127.260 1.00 41.83 ? 400 GLU A C     1 
ATOM   3237  O  O     . GLU A 1 400 ? 143.346 156.684 127.748 1.00 41.48 ? 400 GLU A O     1 
ATOM   3238  C  CB    . GLU A 1 400 ? 142.307 159.651 127.102 1.00 40.88 ? 400 GLU A CB    1 
ATOM   3239  C  CG    . GLU A 1 400 ? 141.479 160.918 127.222 1.00 44.46 ? 400 GLU A CG    1 
ATOM   3240  C  CD    . GLU A 1 400 ? 140.501 161.085 126.076 1.00 49.34 ? 400 GLU A CD    1 
ATOM   3241  O  OE1   . GLU A 1 400 ? 140.813 160.632 124.955 1.00 50.03 ? 400 GLU A OE1   1 
ATOM   3242  O  OE2   . GLU A 1 400 ? 139.421 161.672 126.296 1.00 45.30 ? 400 GLU A OE2   1 
ATOM   3243  N  N     . ASP A 1 401 ? 141.677 156.591 126.240 1.00 39.29 ? 401 ASP A N     1 
ATOM   3244  C  CA    . ASP A 1 401 ? 142.147 155.360 125.623 1.00 37.10 ? 401 ASP A CA    1 
ATOM   3245  C  C     . ASP A 1 401 ? 142.994 155.668 124.397 1.00 37.95 ? 401 ASP A C     1 
ATOM   3246  O  O     . ASP A 1 401 ? 142.696 156.593 123.637 1.00 40.75 ? 401 ASP A O     1 
ATOM   3247  C  CB    . ASP A 1 401 ? 140.970 154.470 125.225 1.00 35.32 ? 401 ASP A CB    1 
ATOM   3248  C  CG    . ASP A 1 401 ? 140.070 154.135 126.394 1.00 38.91 ? 401 ASP A CG    1 
ATOM   3249  O  OD1   . ASP A 1 401 ? 140.567 154.088 127.537 1.00 42.04 ? 401 ASP A OD1   1 
ATOM   3250  O  OD2   . ASP A 1 401 ? 138.862 153.915 126.169 1.00 41.19 ? 401 ASP A OD2   1 
ATOM   3251  N  N     . GLU A 1 402 ? 144.055 154.887 124.213 1.00 34.95 ? 402 GLU A N     1 
ATOM   3252  C  CA    . GLU A 1 402 ? 144.878 154.958 123.012 1.00 34.12 ? 402 GLU A CA    1 
ATOM   3253  C  C     . GLU A 1 402 ? 144.290 153.999 121.984 1.00 31.91 ? 402 GLU A C     1 
ATOM   3254  O  O     . GLU A 1 402 ? 144.438 152.779 122.107 1.00 40.11 ? 402 GLU A O     1 
ATOM   3255  C  CB    . GLU A 1 402 ? 146.330 154.611 123.325 1.00 37.54 ? 402 GLU A CB    1 
ATOM   3256  C  CG    . GLU A 1 402 ? 147.015 155.591 124.261 1.00 36.25 ? 402 GLU A CG    1 
ATOM   3257  C  CD    . GLU A 1 402 ? 147.837 154.898 125.330 1.00 43.31 ? 402 GLU A CD    1 
ATOM   3258  O  OE1   . GLU A 1 402 ? 149.017 154.584 125.064 1.00 43.95 ? 402 GLU A OE1   1 
ATOM   3259  O  OE2   . GLU A 1 402 ? 147.305 154.668 126.436 1.00 44.04 ? 402 GLU A OE2   1 
ATOM   3260  N  N     . ILE A 1 403 ? 143.623 154.546 120.977 1.00 29.49 ? 403 ILE A N     1 
ATOM   3261  C  CA    . ILE A 1 403 ? 142.918 153.747 119.983 1.00 30.54 ? 403 ILE A CA    1 
ATOM   3262  C  C     . ILE A 1 403 ? 143.898 153.318 118.900 1.00 30.63 ? 403 ILE A C     1 
ATOM   3263  O  O     . ILE A 1 403 ? 144.595 154.154 118.312 1.00 32.76 ? 403 ILE A O     1 
ATOM   3264  C  CB    . ILE A 1 403 ? 141.740 154.532 119.385 1.00 27.66 ? 403 ILE A CB    1 
ATOM   3265  C  CG1   . ILE A 1 403 ? 140.707 154.848 120.470 1.00 30.67 ? 403 ILE A CG1   1 
ATOM   3266  C  CG2   . ILE A 1 403 ? 141.107 153.758 118.245 1.00 23.77 ? 403 ILE A CG2   1 
ATOM   3267  C  CD1   . ILE A 1 403 ? 140.329 153.657 121.323 1.00 31.42 ? 403 ILE A CD1   1 
ATOM   3268  N  N     . GLY A 1 404 ? 143.951 152.015 118.636 1.00 25.45 ? 404 GLY A N     1 
ATOM   3269  C  CA    . GLY A 1 404 ? 144.809 151.481 117.598 1.00 16.92 ? 404 GLY A CA    1 
ATOM   3270  C  C     . GLY A 1 404 ? 144.092 151.293 116.277 1.00 23.35 ? 404 GLY A C     1 
ATOM   3271  O  O     . GLY A 1 404 ? 143.210 152.082 115.927 1.00 34.32 ? 404 GLY A O     1 
ATOM   3272  N  N     . LEU A 1 405 ? 144.462 150.253 115.532 1.00 22.60 ? 405 LEU A N     1 
ATOM   3273  C  CA    . LEU A 1 405 ? 143.866 149.958 114.232 1.00 9.77  ? 405 LEU A CA    1 
ATOM   3274  C  C     . LEU A 1 405 ? 143.372 148.519 114.237 1.00 16.42 ? 405 LEU A C     1 
ATOM   3275  O  O     . LEU A 1 405 ? 144.178 147.584 114.270 1.00 16.96 ? 405 LEU A O     1 
ATOM   3276  C  CB    . LEU A 1 405 ? 144.869 150.180 113.100 1.00 18.15 ? 405 LEU A CB    1 
ATOM   3277  C  CG    . LEU A 1 405 ? 145.415 151.594 112.897 1.00 17.62 ? 405 LEU A CG    1 
ATOM   3278  C  CD1   . LEU A 1 405 ? 146.542 151.580 111.883 1.00 19.62 ? 405 LEU A CD1   1 
ATOM   3279  C  CD2   . LEU A 1 405 ? 144.315 152.546 112.465 1.00 15.63 ? 405 LEU A CD2   1 
ATOM   3280  N  N     . ASP A 1 406 ? 142.055 148.340 114.200 1.00 25.40 ? 406 ASP A N     1 
ATOM   3281  C  CA    . ASP A 1 406 ? 141.444 147.022 114.117 1.00 13.32 ? 406 ASP A CA    1 
ATOM   3282  C  C     . ASP A 1 406 ? 140.909 146.793 112.711 1.00 18.51 ? 406 ASP A C     1 
ATOM   3283  O  O     . ASP A 1 406 ? 140.217 147.646 112.150 1.00 32.31 ? 406 ASP A O     1 
ATOM   3284  C  CB    . ASP A 1 406 ? 140.319 146.870 115.141 1.00 16.61 ? 406 ASP A CB    1 
ATOM   3285  C  CG    . ASP A 1 406 ? 140.830 146.474 116.514 1.00 30.67 ? 406 ASP A CG    1 
ATOM   3286  O  OD1   . ASP A 1 406 ? 142.033 146.166 116.642 1.00 31.59 ? 406 ASP A OD1   1 
ATOM   3287  O  OD2   . ASP A 1 406 ? 140.030 146.478 117.472 1.00 30.48 ? 406 ASP A OD2   1 
ATOM   3288  N  N     . ILE A 1 407 ? 141.212 145.631 112.158 1.00 23.70 ? 407 ILE A N     1 
ATOM   3289  C  CA    . ILE A 1 407 ? 141.002 145.378 110.739 1.00 17.78 ? 407 ILE A CA    1 
ATOM   3290  C  C     . ILE A 1 407 ? 139.528 145.122 110.455 1.00 17.96 ? 407 ILE A C     1 
ATOM   3291  O  O     . ILE A 1 407 ? 138.826 144.468 111.235 1.00 21.99 ? 407 ILE A O     1 
ATOM   3292  C  CB    . ILE A 1 407 ? 141.869 144.194 110.279 1.00 14.15 ? 407 ILE A CB    1 
ATOM   3293  C  CG1   . ILE A 1 407 ? 143.345 144.465 110.562 1.00 3.15  ? 407 ILE A CG1   1 
ATOM   3294  C  CG2   . ILE A 1 407 ? 141.661 143.922 108.817 1.00 17.32 ? 407 ILE A CG2   1 
ATOM   3295  C  CD1   . ILE A 1 407 ? 144.095 143.245 111.006 1.00 18.82 ? 407 ILE A CD1   1 
ATOM   3296  N  N     . SER A 1 408 ? 139.061 145.648 109.325 1.00 27.79 ? 408 SER A N     1 
ATOM   3297  C  CA    . SER A 1 408 ? 137.759 145.322 108.762 1.00 20.46 ? 408 SER A CA    1 
ATOM   3298  C  C     . SER A 1 408 ? 137.765 145.755 107.305 1.00 24.79 ? 408 SER A C     1 
ATOM   3299  O  O     . SER A 1 408 ? 138.201 146.864 106.988 1.00 36.48 ? 408 SER A O     1 
ATOM   3300  C  CB    . SER A 1 408 ? 136.619 146.009 109.522 1.00 21.82 ? 408 SER A CB    1 
ATOM   3301  O  OG    . SER A 1 408 ? 136.318 147.272 108.958 1.00 29.52 ? 408 SER A OG    1 
ATOM   3302  N  N     . CYS A 1 409 ? 137.292 144.880 106.423 1.00 20.94 ? 409 CYS A N     1 
ATOM   3303  C  CA    . CYS A 1 409 ? 137.219 145.196 105.005 1.00 26.57 ? 409 CYS A CA    1 
ATOM   3304  C  C     . CYS A 1 409 ? 135.880 144.744 104.443 1.00 26.37 ? 409 CYS A C     1 
ATOM   3305  O  O     . CYS A 1 409 ? 135.256 143.803 104.937 1.00 23.99 ? 409 CYS A O     1 
ATOM   3306  C  CB    . CYS A 1 409 ? 138.374 144.556 104.216 1.00 22.36 ? 409 CYS A CB    1 
ATOM   3307  S  SG    . CYS A 1 409 ? 138.256 142.773 103.971 1.00 38.26 ? 409 CYS A SG    1 
ATOM   3308  N  N     . ASN A 1 410 ? 135.442 145.442 103.400 1.00 23.01 ? 410 ASN A N     1 
ATOM   3309  C  CA    . ASN A 1 410 ? 134.203 145.115 102.712 1.00 18.52 ? 410 ASN A CA    1 
ATOM   3310  C  C     . ASN A 1 410 ? 134.496 144.094 101.626 1.00 21.25 ? 410 ASN A C     1 
ATOM   3311  O  O     . ASN A 1 410 ? 135.461 144.242 100.870 1.00 23.71 ? 410 ASN A O     1 
ATOM   3312  C  CB    . ASN A 1 410 ? 133.571 146.362 102.101 1.00 22.58 ? 410 ASN A CB    1 
ATOM   3313  C  CG    . ASN A 1 410 ? 134.250 147.630 102.545 1.00 29.80 ? 410 ASN A CG    1 
ATOM   3314  O  OD1   . ASN A 1 410 ? 134.708 147.741 103.682 1.00 30.21 ? 410 ASN A OD1   1 
ATOM   3315  N  ND2   . ASN A 1 410 ? 134.334 148.595 101.643 1.00 29.07 ? 410 ASN A ND2   1 
ATOM   3316  N  N     . LEU A 1 411 ? 133.661 143.070 101.547 1.00 17.44 ? 411 LEU A N     1 
ATOM   3317  C  CA    . LEU A 1 411 ? 133.877 141.959 100.638 1.00 11.42 ? 411 LEU A CA    1 
ATOM   3318  C  C     . LEU A 1 411 ? 133.059 142.143 99.367  1.00 13.80 ? 411 LEU A C     1 
ATOM   3319  O  O     . LEU A 1 411 ? 131.978 142.735 99.378  1.00 19.87 ? 411 LEU A O     1 
ATOM   3320  C  CB    . LEU A 1 411 ? 133.508 140.638 101.312 1.00 21.45 ? 411 LEU A CB    1 
ATOM   3321  C  CG    . LEU A 1 411 ? 134.230 140.300 102.616 1.00 15.76 ? 411 LEU A CG    1 
ATOM   3322  C  CD1   . LEU A 1 411 ? 134.148 138.817 102.878 1.00 21.23 ? 411 LEU A CD1   1 
ATOM   3323  C  CD2   . LEU A 1 411 ? 135.680 140.741 102.562 1.00 20.25 ? 411 LEU A CD2   1 
ATOM   3324  N  N     . GLY A 1 412 ? 133.596 141.629 98.267  1.00 23.15 ? 412 GLY A N     1 
ATOM   3325  C  CA    . GLY A 1 412 ? 132.912 141.635 96.992  1.00 10.61 ? 412 GLY A CA    1 
ATOM   3326  C  C     . GLY A 1 412 ? 133.605 140.698 96.031  1.00 12.11 ? 412 GLY A C     1 
ATOM   3327  O  O     . GLY A 1 412 ? 134.836 140.661 95.984  1.00 26.38 ? 412 GLY A O     1 
ATOM   3328  N  N     . SER A 1 413 ? 132.840 139.934 95.259  1.00 14.46 ? 413 SER A N     1 
ATOM   3329  C  CA    . SER A 1 413 ? 133.397 138.894 94.407  1.00 9.62  ? 413 SER A CA    1 
ATOM   3330  C  C     . SER A 1 413 ? 133.092 139.182 92.947  1.00 16.40 ? 413 SER A C     1 
ATOM   3331  O  O     . SER A 1 413 ? 131.948 139.483 92.593  1.00 25.16 ? 413 SER A O     1 
ATOM   3332  C  CB    . SER A 1 413 ? 132.849 137.521 94.791  1.00 12.10 ? 413 SER A CB    1 
ATOM   3333  O  OG    . SER A 1 413 ? 133.376 137.101 96.033  1.00 30.65 ? 413 SER A OG    1 
ATOM   3334  N  N     . LEU A 1 414 ? 134.117 139.092 92.107  1.00 21.13 ? 414 LEU A N     1 
ATOM   3335  C  CA    . LEU A 1 414 ? 133.915 139.027 90.670  1.00 13.66 ? 414 LEU A CA    1 
ATOM   3336  C  C     . LEU A 1 414 ? 133.509 137.615 90.278  1.00 20.62 ? 414 LEU A C     1 
ATOM   3337  O  O     . LEU A 1 414 ? 134.028 136.633 90.814  1.00 22.53 ? 414 LEU A O     1 
ATOM   3338  C  CB    . LEU A 1 414 ? 135.189 139.419 89.923  1.00 16.65 ? 414 LEU A CB    1 
ATOM   3339  C  CG    . LEU A 1 414 ? 135.945 140.663 90.379  1.00 20.57 ? 414 LEU A CG    1 
ATOM   3340  C  CD1   . LEU A 1 414 ? 137.266 140.750 89.644  1.00 24.65 ? 414 LEU A CD1   1 
ATOM   3341  C  CD2   . LEU A 1 414 ? 135.115 141.907 90.135  1.00 25.17 ? 414 LEU A CD2   1 
ATOM   3342  N  N     . ASN A 1 415 ? 132.575 137.513 89.341  1.00 28.39 ? 415 ASN A N     1 
ATOM   3343  C  CA    . ASN A 1 415 ? 132.225 136.230 88.746  1.00 25.89 ? 415 ASN A CA    1 
ATOM   3344  C  C     . ASN A 1 415 ? 133.134 136.020 87.543  1.00 27.77 ? 415 ASN A C     1 
ATOM   3345  O  O     . ASN A 1 415 ? 132.963 136.671 86.508  1.00 29.69 ? 415 ASN A O     1 
ATOM   3346  C  CB    . ASN A 1 415 ? 130.753 136.196 88.352  1.00 21.20 ? 415 ASN A CB    1 
ATOM   3347  C  CG    . ASN A 1 415 ? 130.229 134.790 88.164  1.00 24.71 ? 415 ASN A CG    1 
ATOM   3348  O  OD1   . ASN A 1 415 ? 130.829 133.979 87.462  1.00 33.35 ? 415 ASN A OD1   1 
ATOM   3349  N  ND2   . ASN A 1 415 ? 129.100 134.492 88.791  1.00 30.36 ? 415 ASN A ND2   1 
ATOM   3350  N  N     . ILE A 1 416 ? 134.103 135.112 87.683  1.00 19.83 ? 416 ILE A N     1 
ATOM   3351  C  CA    . ILE A 1 416 ? 135.124 134.940 86.654  1.00 21.56 ? 416 ILE A CA    1 
ATOM   3352  C  C     . ILE A 1 416 ? 134.493 134.521 85.333  1.00 29.55 ? 416 ILE A C     1 
ATOM   3353  O  O     . ILE A 1 416 ? 134.890 134.994 84.262  1.00 27.92 ? 416 ILE A O     1 
ATOM   3354  C  CB    . ILE A 1 416 ? 136.190 133.934 87.126  1.00 23.73 ? 416 ILE A CB    1 
ATOM   3355  C  CG1   . ILE A 1 416 ? 136.962 134.504 88.315  1.00 22.50 ? 416 ILE A CG1   1 
ATOM   3356  C  CG2   . ILE A 1 416 ? 137.142 133.590 85.998  1.00 15.87 ? 416 ILE A CG2   1 
ATOM   3357  C  CD1   . ILE A 1 416 ? 137.866 133.509 88.997  1.00 19.58 ? 416 ILE A CD1   1 
ATOM   3358  N  N     . LEU A 1 417 ? 133.491 133.641 85.386  1.00 24.53 ? 417 LEU A N     1 
ATOM   3359  C  CA    . LEU A 1 417 ? 132.846 133.180 84.161  1.00 27.89 ? 417 LEU A CA    1 
ATOM   3360  C  C     . LEU A 1 417 ? 132.159 134.326 83.428  1.00 29.11 ? 417 LEU A C     1 
ATOM   3361  O  O     . LEU A 1 417 ? 132.358 134.516 82.223  1.00 35.97 ? 417 LEU A O     1 
ATOM   3362  C  CB    . LEU A 1 417 ? 131.844 132.073 84.486  1.00 28.62 ? 417 LEU A CB    1 
ATOM   3363  C  CG    . LEU A 1 417 ? 131.302 131.271 83.304  1.00 26.04 ? 417 LEU A CG    1 
ATOM   3364  C  CD1   . LEU A 1 417 ? 131.270 129.802 83.654  1.00 27.26 ? 417 LEU A CD1   1 
ATOM   3365  C  CD2   . LEU A 1 417 ? 129.919 131.757 82.913  1.00 33.06 ? 417 LEU A CD2   1 
ATOM   3366  N  N     . ASN A 1 418 ? 131.348 135.106 84.143  1.00 30.72 ? 418 ASN A N     1 
ATOM   3367  C  CA    . ASN A 1 418 ? 130.601 136.182 83.503  1.00 30.97 ? 418 ASN A CA    1 
ATOM   3368  C  C     . ASN A 1 418 ? 131.493 137.360 83.141  1.00 29.97 ? 418 ASN A C     1 
ATOM   3369  O  O     . ASN A 1 418 ? 131.245 138.031 82.134  1.00 32.51 ? 418 ASN A O     1 
ATOM   3370  C  CB    . ASN A 1 418 ? 129.462 136.641 84.413  1.00 26.78 ? 418 ASN A CB    1 
ATOM   3371  C  CG    . ASN A 1 418 ? 128.385 135.591 84.566  1.00 32.01 ? 418 ASN A CG    1 
ATOM   3372  O  OD1   . ASN A 1 418 ? 128.063 134.876 83.619  1.00 37.08 ? 418 ASN A OD1   1 
ATOM   3373  N  ND2   . ASN A 1 418 ? 127.825 135.486 85.763  1.00 33.11 ? 418 ASN A ND2   1 
ATOM   3374  N  N     . VAL A 1 419 ? 132.522 137.629 83.945  1.00 29.36 ? 419 VAL A N     1 
ATOM   3375  C  CA    . VAL A 1 419 ? 133.472 138.683 83.609  1.00 28.93 ? 419 VAL A CA    1 
ATOM   3376  C  C     . VAL A 1 419 ? 134.250 138.317 82.352  1.00 32.05 ? 419 VAL A C     1 
ATOM   3377  O  O     . VAL A 1 419 ? 134.454 139.155 81.465  1.00 35.53 ? 419 VAL A O     1 
ATOM   3378  C  CB    . VAL A 1 419 ? 134.406 138.953 84.803  1.00 27.84 ? 419 VAL A CB    1 
ATOM   3379  C  CG1   . VAL A 1 419 ? 135.657 139.666 84.353  1.00 32.11 ? 419 VAL A CG1   1 
ATOM   3380  C  CG2   . VAL A 1 419 ? 133.687 139.765 85.860  1.00 27.38 ? 419 VAL A CG2   1 
ATOM   3381  N  N     . MET A 1 420 ? 134.690 137.061 82.249  1.00 38.30 ? 420 MET A N     1 
ATOM   3382  C  CA    . MET A 1 420 ? 135.430 136.621 81.073  1.00 30.99 ? 420 MET A CA    1 
ATOM   3383  C  C     . MET A 1 420 ? 134.540 136.541 79.841  1.00 30.23 ? 420 MET A C     1 
ATOM   3384  O  O     . MET A 1 420 ? 135.002 136.813 78.727  1.00 35.98 ? 420 MET A O     1 
ATOM   3385  C  CB    . MET A 1 420 ? 136.084 135.269 81.346  1.00 32.03 ? 420 MET A CB    1 
ATOM   3386  C  CG    . MET A 1 420 ? 137.357 135.355 82.165  1.00 31.19 ? 420 MET A CG    1 
ATOM   3387  S  SD    . MET A 1 420 ? 138.585 136.419 81.395  1.00 39.88 ? 420 MET A SD    1 
ATOM   3388  C  CE    . MET A 1 420 ? 139.300 135.291 80.204  1.00 30.64 ? 420 MET A CE    1 
ATOM   3389  N  N     . GLU A 1 421 ? 133.272 136.163 80.016  1.00 38.66 ? 421 GLU A N     1 
ATOM   3390  C  CA    . GLU A 1 421 ? 132.345 136.129 78.889  1.00 36.27 ? 421 GLU A CA    1 
ATOM   3391  C  C     . GLU A 1 421 ? 132.115 137.524 78.324  1.00 41.31 ? 421 GLU A C     1 
ATOM   3392  O  O     . GLU A 1 421 ? 132.059 137.707 77.102  1.00 43.55 ? 421 GLU A O     1 
ATOM   3393  C  CB    . GLU A 1 421 ? 131.021 135.503 79.323  1.00 35.38 ? 421 GLU A CB    1 
ATOM   3394  C  CG    . GLU A 1 421 ? 130.971 133.991 79.194  1.00 41.70 ? 421 GLU A CG    1 
ATOM   3395  C  CD    . GLU A 1 421 ? 129.635 133.418 79.623  1.00 46.59 ? 421 GLU A CD    1 
ATOM   3396  O  OE1   . GLU A 1 421 ? 128.851 134.154 80.258  1.00 44.64 ? 421 GLU A OE1   1 
ATOM   3397  O  OE2   . GLU A 1 421 ? 129.368 132.235 79.325  1.00 45.22 ? 421 GLU A OE2   1 
ATOM   3398  N  N     . HIS A 1 422 ? 131.980 138.520 79.197  1.00 37.73 ? 422 HIS A N     1 
ATOM   3399  C  CA    . HIS A 1 422 ? 131.742 139.894 78.776  1.00 34.52 ? 422 HIS A CA    1 
ATOM   3400  C  C     . HIS A 1 422 ? 133.019 140.630 78.399  1.00 38.92 ? 422 HIS A C     1 
ATOM   3401  O  O     . HIS A 1 422 ? 132.934 141.771 77.930  1.00 39.05 ? 422 HIS A O     1 
ATOM   3402  C  CB    . HIS A 1 422 ? 131.018 140.663 79.883  1.00 33.77 ? 422 HIS A CB    1 
ATOM   3403  C  CG    . HIS A 1 422 ? 129.639 140.157 80.168  1.00 36.34 ? 422 HIS A CG    1 
ATOM   3404  N  ND1   . HIS A 1 422 ? 129.386 139.163 81.088  1.00 36.26 ? 422 HIS A ND1   1 
ATOM   3405  C  CD2   . HIS A 1 422 ? 128.436 140.507 79.654  1.00 38.65 ? 422 HIS A CD2   1 
ATOM   3406  C  CE1   . HIS A 1 422 ? 128.089 138.922 81.129  1.00 39.69 ? 422 HIS A CE1   1 
ATOM   3407  N  NE2   . HIS A 1 422 ? 127.489 139.725 80.268  1.00 40.81 ? 422 HIS A NE2   1 
ATOM   3408  N  N     . LYS A 1 423 ? 134.185 140.010 78.586  1.00 43.08 ? 423 LYS A N     1 
ATOM   3409  C  CA    . LYS A 1 423 ? 135.477 140.641 78.316  1.00 43.45 ? 423 LYS A CA    1 
ATOM   3410  C  C     . LYS A 1 423 ? 135.579 141.988 79.026  1.00 43.14 ? 423 LYS A C     1 
ATOM   3411  O  O     . LYS A 1 423 ? 135.970 143.002 78.444  1.00 46.59 ? 423 LYS A O     1 
ATOM   3412  C  CB    . LYS A 1 423 ? 135.711 140.793 76.813  1.00 40.78 ? 423 LYS A CB    1 
ATOM   3413  C  CG    . LYS A 1 423 ? 135.466 139.526 76.015  1.00 42.27 ? 423 LYS A CG    1 
ATOM   3414  C  CD    . LYS A 1 423 ? 136.742 138.716 75.870  1.00 46.66 ? 423 LYS A CD    1 
ATOM   3415  C  CE    . LYS A 1 423 ? 136.444 137.267 75.521  1.00 46.42 ? 423 LYS A CE    1 
ATOM   3416  N  NZ    . LYS A 1 423 ? 136.260 136.428 76.736  1.00 44.51 ? 423 LYS A NZ    1 
ATOM   3417  N  N     . SER A 1 424 ? 135.221 141.989 80.306  1.00 31.80 ? 424 SER A N     1 
ATOM   3418  C  CA    . SER A 1 424 ? 135.067 143.213 81.082  1.00 32.25 ? 424 SER A CA    1 
ATOM   3419  C  C     . SER A 1 424 ? 135.784 143.102 82.417  1.00 36.30 ? 424 SER A C     1 
ATOM   3420  O  O     . SER A 1 424 ? 135.224 143.399 83.471  1.00 39.39 ? 424 SER A O     1 
ATOM   3421  C  CB    . SER A 1 424 ? 133.593 143.531 81.302  1.00 35.73 ? 424 SER A CB    1 
ATOM   3422  O  OG    . SER A 1 424 ? 133.021 142.637 82.240  1.00 32.01 ? 424 SER A OG    1 
ATOM   3423  N  N     . ILE A 1 425 ? 137.041 142.657 82.396  1.00 34.14 ? 425 ILE A N     1 
ATOM   3424  C  CA    . ILE A 1 425 ? 137.820 142.619 83.631  1.00 28.16 ? 425 ILE A CA    1 
ATOM   3425  C  C     . ILE A 1 425 ? 138.031 144.030 84.166  1.00 30.59 ? 425 ILE A C     1 
ATOM   3426  O  O     . ILE A 1 425 ? 137.812 144.303 85.351  1.00 36.49 ? 425 ILE A O     1 
ATOM   3427  C  CB    . ILE A 1 425 ? 139.158 141.891 83.407  1.00 32.52 ? 425 ILE A CB    1 
ATOM   3428  C  CG1   . ILE A 1 425 ? 138.940 140.379 83.368  1.00 32.95 ? 425 ILE A CG1   1 
ATOM   3429  C  CG2   . ILE A 1 425 ? 140.154 142.252 84.497  1.00 28.56 ? 425 ILE A CG2   1 
ATOM   3430  C  CD1   . ILE A 1 425 ? 140.182 139.585 83.073  1.00 32.71 ? 425 ILE A CD1   1 
ATOM   3431  N  N     . GLU A 1 426 ? 138.432 144.954 83.291  1.00 29.02 ? 426 GLU A N     1 
ATOM   3432  C  CA    . GLU A 1 426 ? 138.758 146.307 83.730  1.00 27.70 ? 426 GLU A CA    1 
ATOM   3433  C  C     . GLU A 1 426 ? 137.541 147.017 84.311  1.00 30.22 ? 426 GLU A C     1 
ATOM   3434  O  O     . GLU A 1 426 ? 137.589 147.541 85.431  1.00 37.50 ? 426 GLU A O     1 
ATOM   3435  C  CB    . GLU A 1 426 ? 139.333 147.104 82.561  1.00 29.76 ? 426 GLU A CB    1 
ATOM   3436  C  CG    . GLU A 1 426 ? 139.335 148.606 82.773  1.00 33.77 ? 426 GLU A CG    1 
ATOM   3437  C  CD    . GLU A 1 426 ? 140.055 149.347 81.666  1.00 39.35 ? 426 GLU A CD    1 
ATOM   3438  O  OE1   . GLU A 1 426 ? 140.338 148.727 80.620  1.00 37.97 ? 426 GLU A OE1   1 
ATOM   3439  O  OE2   . GLU A 1 426 ? 140.340 150.550 81.843  1.00 38.44 ? 426 GLU A OE2   1 
ATOM   3440  N  N     . LYS A 1 427 ? 136.440 147.045 83.558  1.00 32.80 ? 427 LYS A N     1 
ATOM   3441  C  CA    . LYS A 1 427 ? 135.256 147.772 84.002  1.00 29.64 ? 427 LYS A CA    1 
ATOM   3442  C  C     . LYS A 1 427 ? 134.665 147.148 85.258  1.00 30.31 ? 427 LYS A C     1 
ATOM   3443  O  O     . LYS A 1 427 ? 134.275 147.866 86.186  1.00 37.08 ? 427 LYS A O     1 
ATOM   3444  C  CB    . LYS A 1 427 ? 134.190 147.852 82.895  1.00 35.05 ? 427 LYS A CB    1 
ATOM   3445  C  CG    . LYS A 1 427 ? 134.547 148.511 81.527  1.00 37.86 ? 427 LYS A CG    1 
ATOM   3446  C  CD    . LYS A 1 427 ? 135.856 148.121 80.827  1.00 39.06 ? 427 LYS A CD    1 
ATOM   3447  C  CE    . LYS A 1 427 ? 135.974 146.619 80.599  1.00 35.13 ? 427 LYS A CE    1 
ATOM   3448  N  NZ    . LYS A 1 427 ? 137.278 146.245 79.984  1.00 35.38 ? 427 LYS A NZ    1 
ATOM   3449  N  N     . THR A 1 428 ? 134.592 145.817 85.308  1.00 29.40 ? 428 THR A N     1 
ATOM   3450  C  CA    . THR A 1 428 ? 134.061 145.158 86.495  1.00 22.88 ? 428 THR A CA    1 
ATOM   3451  C  C     . THR A 1 428 ? 134.930 145.431 87.713  1.00 28.65 ? 428 THR A C     1 
ATOM   3452  O  O     . THR A 1 428 ? 134.412 145.728 88.794  1.00 31.10 ? 428 THR A O     1 
ATOM   3453  C  CB    . THR A 1 428 ? 133.935 143.654 86.266  1.00 25.04 ? 428 THR A CB    1 
ATOM   3454  O  OG1   . THR A 1 428 ? 133.330 143.413 84.991  1.00 29.45 ? 428 THR A OG1   1 
ATOM   3455  C  CG2   . THR A 1 428 ? 133.080 143.029 87.351  1.00 26.25 ? 428 THR A CG2   1 
ATOM   3456  N  N     . VAL A 1 429 ? 136.253 145.345 87.559  1.00 28.88 ? 429 VAL A N     1 
ATOM   3457  C  CA    . VAL A 1 429 ? 137.144 145.571 88.693  1.00 22.74 ? 429 VAL A CA    1 
ATOM   3458  C  C     . VAL A 1 429 ? 137.023 147.005 89.188  1.00 24.19 ? 429 VAL A C     1 
ATOM   3459  O  O     . VAL A 1 429 ? 136.944 147.252 90.396  1.00 29.81 ? 429 VAL A O     1 
ATOM   3460  C  CB    . VAL A 1 429 ? 138.596 145.217 88.322  1.00 24.53 ? 429 VAL A CB    1 
ATOM   3461  C  CG1   . VAL A 1 429 ? 139.557 145.809 89.330  1.00 19.89 ? 429 VAL A CG1   1 
ATOM   3462  C  CG2   . VAL A 1 429 ? 138.775 143.712 88.266  1.00 23.69 ? 429 VAL A CG2   1 
ATOM   3463  N  N     . LYS A 1 430 ? 136.983 147.972 88.268  1.00 24.16 ? 430 LYS A N     1 
ATOM   3464  C  CA    . LYS A 1 430 ? 136.901 149.369 88.683  1.00 23.54 ? 430 LYS A CA    1 
ATOM   3465  C  C     . LYS A 1 430 ? 135.560 149.686 89.339  1.00 23.46 ? 430 LYS A C     1 
ATOM   3466  O  O     . LYS A 1 430 ? 135.515 150.377 90.365  1.00 31.44 ? 430 LYS A O     1 
ATOM   3467  C  CB    . LYS A 1 430 ? 137.159 150.284 87.487  1.00 25.30 ? 430 LYS A CB    1 
ATOM   3468  C  CG    . LYS A 1 430 ? 138.571 150.167 86.941  1.00 27.66 ? 430 LYS A CG    1 
ATOM   3469  C  CD    . LYS A 1 430 ? 138.953 151.363 86.095  1.00 30.66 ? 430 LYS A CD    1 
ATOM   3470  C  CE    . LYS A 1 430 ? 140.398 151.264 85.644  1.00 30.26 ? 430 LYS A CE    1 
ATOM   3471  N  NZ    . LYS A 1 430 ? 140.798 152.419 84.797  1.00 33.94 ? 430 LYS A NZ    1 
ATOM   3472  N  N     . LEU A 1 431 ? 134.458 149.188 88.774  1.00 25.70 ? 431 LEU A N     1 
ATOM   3473  C  CA    . LEU A 1 431 ? 133.150 149.439 89.369  1.00 20.20 ? 431 LEU A CA    1 
ATOM   3474  C  C     . LEU A 1 431 ? 133.014 148.757 90.725  1.00 23.52 ? 431 LEU A C     1 
ATOM   3475  O  O     . LEU A 1 431 ? 132.433 149.325 91.657  1.00 29.44 ? 431 LEU A O     1 
ATOM   3476  C  CB    . LEU A 1 431 ? 132.048 148.974 88.421  1.00 27.87 ? 431 LEU A CB    1 
ATOM   3477  C  CG    . LEU A 1 431 ? 131.371 150.039 87.559  1.00 30.93 ? 431 LEU A CG    1 
ATOM   3478  C  CD1   . LEU A 1 431 ? 130.260 149.417 86.735  1.00 30.04 ? 431 LEU A CD1   1 
ATOM   3479  C  CD2   . LEU A 1 431 ? 130.836 151.172 88.419  1.00 31.48 ? 431 LEU A CD2   1 
ATOM   3480  N  N     . ALA A 1 432 ? 133.537 147.535 90.855  1.00 25.52 ? 432 ALA A N     1 
ATOM   3481  C  CA    . ALA A 1 432 ? 133.520 146.849 92.140  1.00 16.24 ? 432 ALA A CA    1 
ATOM   3482  C  C     . ALA A 1 432 ? 134.370 147.583 93.164  1.00 26.66 ? 432 ALA A C     1 
ATOM   3483  O  O     . ALA A 1 432 ? 134.005 147.661 94.342  1.00 29.48 ? 432 ALA A O     1 
ATOM   3484  C  CB    . ALA A 1 432 ? 134.007 145.412 91.971  1.00 21.93 ? 432 ALA A CB    1 
ATOM   3485  N  N     . THR A 1 433 ? 135.514 148.121 92.736  1.00 28.11 ? 433 THR A N     1 
ATOM   3486  C  CA    . THR A 1 433 ? 136.342 148.917 93.632  1.00 21.71 ? 433 THR A CA    1 
ATOM   3487  C  C     . THR A 1 433 ? 135.599 150.158 94.102  1.00 23.79 ? 433 THR A C     1 
ATOM   3488  O  O     . THR A 1 433 ? 135.657 150.515 95.283  1.00 34.73 ? 433 THR A O     1 
ATOM   3489  C  CB    . THR A 1 433 ? 137.646 149.304 92.934  1.00 27.41 ? 433 THR A CB    1 
ATOM   3490  O  OG1   . THR A 1 433 ? 138.350 148.119 92.545  1.00 28.79 ? 433 THR A OG1   1 
ATOM   3491  C  CG2   . THR A 1 433 ? 138.525 150.129 93.858  1.00 24.80 ? 433 THR A CG2   1 
ATOM   3492  N  N     . ASP A 1 434 ? 134.888 150.826 93.191  1.00 22.79 ? 434 ASP A N     1 
ATOM   3493  C  CA    . ASP A 1 434 ? 134.100 151.993 93.577  1.00 23.51 ? 434 ASP A CA    1 
ATOM   3494  C  C     . ASP A 1 434 ? 133.004 151.622 94.570  1.00 21.24 ? 434 ASP A C     1 
ATOM   3495  O  O     . ASP A 1 434 ? 132.780 152.333 95.557  1.00 25.32 ? 434 ASP A O     1 
ATOM   3496  C  CB    . ASP A 1 434 ? 133.496 152.652 92.338  1.00 24.29 ? 434 ASP A CB    1 
ATOM   3497  C  CG    . ASP A 1 434 ? 134.546 153.212 91.406  1.00 31.68 ? 434 ASP A CG    1 
ATOM   3498  O  OD1   . ASP A 1 434 ? 135.664 153.504 91.877  1.00 35.87 ? 434 ASP A OD1   1 
ATOM   3499  O  OD2   . ASP A 1 434 ? 134.253 153.365 90.202  1.00 32.69 ? 434 ASP A OD2   1 
ATOM   3500  N  N     . SER A 1 435 ? 132.305 150.512 94.321  1.00 22.75 ? 435 SER A N     1 
ATOM   3501  C  CA    . SER A 1 435 ? 131.241 150.087 95.226  1.00 21.20 ? 435 SER A CA    1 
ATOM   3502  C  C     . SER A 1 435 ? 131.789 149.729 96.603  1.00 23.57 ? 435 SER A C     1 
ATOM   3503  O  O     . SER A 1 435 ? 131.194 150.086 97.627  1.00 29.74 ? 435 SER A O     1 
ATOM   3504  C  CB    . SER A 1 435 ? 130.485 148.904 94.623  1.00 23.10 ? 435 SER A CB    1 
ATOM   3505  O  OG    . SER A 1 435 ? 131.239 147.711 94.723  1.00 20.72 ? 435 SER A OG    1 
ATOM   3506  N  N     . LEU A 1 436 ? 132.924 149.030 96.648  1.00 19.50 ? 436 LEU A N     1 
ATOM   3507  C  CA    . LEU A 1 436 ? 133.530 148.679 97.927  1.00 12.42 ? 436 LEU A CA    1 
ATOM   3508  C  C     . LEU A 1 436 ? 134.036 149.917 98.655  1.00 18.26 ? 436 LEU A C     1 
ATOM   3509  O  O     . LEU A 1 436 ? 133.952 149.998 99.885  1.00 21.98 ? 436 LEU A O     1 
ATOM   3510  C  CB    . LEU A 1 436 ? 134.658 147.673 97.709  1.00 23.30 ? 436 LEU A CB    1 
ATOM   3511  C  CG    . LEU A 1 436 ? 134.225 146.273 97.270  1.00 19.70 ? 436 LEU A CG    1 
ATOM   3512  C  CD1   . LEU A 1 436 ? 135.414 145.464 96.782  1.00 12.35 ? 436 LEU A CD1   1 
ATOM   3513  C  CD2   . LEU A 1 436 ? 133.511 145.554 98.398  1.00 20.67 ? 436 LEU A CD2   1 
ATOM   3514  N  N     . THR A 1 437 ? 134.562 150.894 97.912  1.00 23.73 ? 437 THR A N     1 
ATOM   3515  C  CA    . THR A 1 437 ? 134.961 152.158 98.519  1.00 20.82 ? 437 THR A CA    1 
ATOM   3516  C  C     . THR A 1 437 ? 133.765 152.874 99.128  1.00 23.47 ? 437 THR A C     1 
ATOM   3517  O  O     . THR A 1 437 ? 133.858 153.432 100.227 1.00 34.84 ? 437 THR A O     1 
ATOM   3518  C  CB    . THR A 1 437 ? 135.638 153.046 97.477  1.00 19.97 ? 437 THR A CB    1 
ATOM   3519  O  OG1   . THR A 1 437 ? 136.626 152.286 96.771  1.00 21.86 ? 437 THR A OG1   1 
ATOM   3520  C  CG2   . THR A 1 437 ? 136.298 154.239 98.138  1.00 22.30 ? 437 THR A CG2   1 
ATOM   3521  N  N     . HIS A 1 438 ? 132.633 152.874 98.424  1.00 22.06 ? 438 HIS A N     1 
ATOM   3522  C  CA    . HIS A 1 438 ? 131.429 153.492 98.968  1.00 24.16 ? 438 HIS A CA    1 
ATOM   3523  C  C     . HIS A 1 438 ? 130.957 152.770 100.224 1.00 24.30 ? 438 HIS A C     1 
ATOM   3524  O  O     . HIS A 1 438 ? 130.539 153.409 101.197 1.00 31.77 ? 438 HIS A O     1 
ATOM   3525  C  CB    . HIS A 1 438 ? 130.323 153.513 97.914  1.00 26.27 ? 438 HIS A CB    1 
ATOM   3526  C  CG    . HIS A 1 438 ? 129.021 154.047 98.421  1.00 27.00 ? 438 HIS A CG    1 
ATOM   3527  N  ND1   . HIS A 1 438 ? 128.757 155.395 98.516  1.00 27.89 ? 438 HIS A ND1   1 
ATOM   3528  C  CD2   . HIS A 1 438 ? 127.912 153.413 98.870  1.00 28.35 ? 438 HIS A CD2   1 
ATOM   3529  C  CE1   . HIS A 1 438 ? 127.540 155.570 98.997  1.00 32.39 ? 438 HIS A CE1   1 
ATOM   3530  N  NE2   . HIS A 1 438 ? 127.006 154.383 99.222  1.00 31.76 ? 438 HIS A NE2   1 
ATOM   3531  N  N     . VAL A 1 439 ? 131.013 151.436 100.221 1.00 25.70 ? 439 VAL A N     1 
ATOM   3532  C  CA    . VAL A 1 439 ? 130.613 150.678 101.405 1.00 20.72 ? 439 VAL A CA    1 
ATOM   3533  C  C     . VAL A 1 439 ? 131.533 150.995 102.577 1.00 26.21 ? 439 VAL A C     1 
ATOM   3534  O  O     . VAL A 1 439 ? 131.084 151.125 103.722 1.00 35.96 ? 439 VAL A O     1 
ATOM   3535  C  CB    . VAL A 1 439 ? 130.585 149.170 101.095 1.00 23.35 ? 439 VAL A CB    1 
ATOM   3536  C  CG1   . VAL A 1 439 ? 130.304 148.375 102.355 1.00 24.23 ? 439 VAL A CG1   1 
ATOM   3537  C  CG2   . VAL A 1 439 ? 129.536 148.867 100.046 1.00 24.66 ? 439 VAL A CG2   1 
ATOM   3538  N  N     . SER A 1 440 ? 132.834 151.126 102.312 1.00 25.23 ? 440 SER A N     1 
ATOM   3539  C  CA    . SER A 1 440 ? 133.773 151.505 103.363 1.00 20.42 ? 440 SER A CA    1 
ATOM   3540  C  C     . SER A 1 440 ? 133.469 152.898 103.898 1.00 25.97 ? 440 SER A C     1 
ATOM   3541  O  O     . SER A 1 440 ? 133.530 153.135 105.110 1.00 33.32 ? 440 SER A O     1 
ATOM   3542  C  CB    . SER A 1 440 ? 135.206 151.438 102.835 1.00 25.81 ? 440 SER A CB    1 
ATOM   3543  O  OG    . SER A 1 440 ? 136.146 151.461 103.893 1.00 30.90 ? 440 SER A OG    1 
ATOM   3544  N  N     . GLU A 1 441 ? 133.143 153.834 103.006 1.00 29.40 ? 441 GLU A N     1 
ATOM   3545  C  CA    . GLU A 1 441 ? 132.888 155.207 103.427 1.00 21.80 ? 441 GLU A CA    1 
ATOM   3546  C  C     . GLU A 1 441 ? 131.592 155.332 104.218 1.00 30.49 ? 441 GLU A C     1 
ATOM   3547  O  O     . GLU A 1 441 ? 131.507 156.160 105.131 1.00 39.53 ? 441 GLU A O     1 
ATOM   3548  C  CB    . GLU A 1 441 ? 132.856 156.128 102.210 1.00 22.63 ? 441 GLU A CB    1 
ATOM   3549  C  CG    . GLU A 1 441 ? 134.224 156.418 101.623 1.00 27.83 ? 441 GLU A CG    1 
ATOM   3550  C  CD    . GLU A 1 441 ? 134.146 157.219 100.342 1.00 38.44 ? 441 GLU A CD    1 
ATOM   3551  O  OE1   . GLU A 1 441 ? 133.735 156.653 99.307  1.00 39.62 ? 441 GLU A OE1   1 
ATOM   3552  O  OE2   . GLU A 1 441 ? 134.497 158.417 100.368 1.00 37.50 ? 441 GLU A OE2   1 
ATOM   3553  N  N     . THR A 1 442 ? 130.578 154.536 103.889 1.00 32.56 ? 442 THR A N     1 
ATOM   3554  C  CA    . THR A 1 442 ? 129.297 154.611 104.579 1.00 31.20 ? 442 THR A CA    1 
ATOM   3555  C  C     . THR A 1 442 ? 129.235 153.737 105.824 1.00 32.00 ? 442 THR A C     1 
ATOM   3556  O  O     . THR A 1 442 ? 128.227 153.772 106.537 1.00 38.85 ? 442 THR A O     1 
ATOM   3557  C  CB    . THR A 1 442 ? 128.154 154.228 103.633 1.00 31.17 ? 442 THR A CB    1 
ATOM   3558  O  OG1   . THR A 1 442 ? 128.316 152.872 103.202 1.00 30.62 ? 442 THR A OG1   1 
ATOM   3559  C  CG2   . THR A 1 442 ? 128.135 155.148 102.425 1.00 30.70 ? 442 THR A CG2   1 
ATOM   3560  N  N     . THR A 1 443 ? 130.275 152.959 106.105 1.00 31.28 ? 443 THR A N     1 
ATOM   3561  C  CA    . THR A 1 443 ? 130.322 152.143 107.309 1.00 35.01 ? 443 THR A CA    1 
ATOM   3562  C  C     . THR A 1 443 ? 130.860 152.977 108.464 1.00 36.21 ? 443 THR A C     1 
ATOM   3563  O  O     . THR A 1 443 ? 131.909 153.617 108.341 1.00 38.49 ? 443 THR A O     1 
ATOM   3564  C  CB    . THR A 1 443 ? 131.196 150.907 107.096 1.00 34.37 ? 443 THR A CB    1 
ATOM   3565  O  OG1   . THR A 1 443 ? 130.596 150.063 106.105 1.00 38.40 ? 443 THR A OG1   1 
ATOM   3566  C  CG2   . THR A 1 443 ? 131.342 150.129 108.392 1.00 29.49 ? 443 THR A CG2   1 
ATOM   3567  N  N     . ASP A 1 444 ? 130.136 152.974 109.582 1.00 42.54 ? 444 ASP A N     1 
ATOM   3568  C  CA    . ASP A 1 444 ? 130.518 153.753 110.760 1.00 42.79 ? 444 ASP A CA    1 
ATOM   3569  C  C     . ASP A 1 444 ? 130.147 152.946 112.000 1.00 42.20 ? 444 ASP A C     1 
ATOM   3570  O  O     . ASP A 1 444 ? 128.986 152.938 112.418 1.00 43.12 ? 444 ASP A O     1 
ATOM   3571  C  CB    . ASP A 1 444 ? 129.841 155.118 110.760 1.00 44.20 ? 444 ASP A CB    1 
ATOM   3572  C  CG    . ASP A 1 444 ? 130.727 156.205 111.330 1.00 47.28 ? 444 ASP A CG    1 
ATOM   3573  O  OD1   . ASP A 1 444 ? 131.114 156.099 112.511 1.00 44.23 ? 444 ASP A OD1   1 
ATOM   3574  O  OD2   . ASP A 1 444 ? 131.036 157.167 110.597 1.00 48.34 ? 444 ASP A OD2   1 
ATOM   3575  N  N     . ILE A 1 445 ? 131.134 152.273 112.582 1.00 38.37 ? 445 ILE A N     1 
ATOM   3576  C  CA    . ILE A 1 445 ? 130.933 151.464 113.778 1.00 41.41 ? 445 ILE A CA    1 
ATOM   3577  C  C     . ILE A 1 445 ? 131.194 152.356 114.987 1.00 45.40 ? 445 ILE A C     1 
ATOM   3578  O  O     . ILE A 1 445 ? 132.331 152.765 115.233 1.00 45.80 ? 445 ILE A O     1 
ATOM   3579  C  CB    . ILE A 1 445 ? 131.847 150.235 113.785 1.00 40.68 ? 445 ILE A CB    1 
ATOM   3580  C  CG1   . ILE A 1 445 ? 131.761 149.500 112.444 1.00 38.69 ? 445 ILE A CG1   1 
ATOM   3581  C  CG2   . ILE A 1 445 ? 131.488 149.312 114.937 1.00 40.29 ? 445 ILE A CG2   1 
ATOM   3582  C  CD1   . ILE A 1 445 ? 130.686 148.440 112.383 1.00 37.72 ? 445 ILE A CD1   1 
ATOM   3583  N  N     . ARG A 1 446 ? 130.142 152.651 115.750 1.00 47.50 ? 446 ARG A N     1 
ATOM   3584  C  CA    . ARG A 1 446 ? 130.222 153.598 116.853 1.00 50.80 ? 446 ARG A CA    1 
ATOM   3585  C  C     . ARG A 1 446 ? 130.399 152.916 118.205 1.00 49.77 ? 446 ARG A C     1 
ATOM   3586  O  O     . ARG A 1 446 ? 130.262 153.569 119.244 1.00 46.16 ? 446 ARG A O     1 
ATOM   3587  C  CB    . ARG A 1 446 ? 128.985 154.497 116.863 1.00 47.38 ? 446 ARG A CB    1 
ATOM   3588  C  CG    . ARG A 1 446 ? 127.667 153.750 116.763 1.00 46.74 ? 446 ARG A CG    1 
ATOM   3589  C  CD    . ARG A 1 446 ? 126.528 154.676 116.355 1.00 50.56 ? 446 ARG A CD    1 
ATOM   3590  N  NE    . ARG A 1 446 ? 126.763 155.305 115.060 1.00 52.16 ? 446 ARG A NE    1 
ATOM   3591  C  CZ    . ARG A 1 446 ? 127.197 156.548 114.892 1.00 52.74 ? 446 ARG A CZ    1 
ATOM   3592  N  NH1   . ARG A 1 446 ? 127.440 157.340 115.923 1.00 49.08 ? 446 ARG A NH1   1 
ATOM   3593  N  NH2   . ARG A 1 446 ? 127.393 157.006 113.659 1.00 51.39 ? 446 ARG A NH2   1 
ATOM   3594  N  N     . ASN A 1 447 ? 130.701 151.617 118.213 1.00 40.67 ? 447 ASN A N     1 
ATOM   3595  C  CA    . ASN A 1 447 ? 131.010 150.910 119.446 1.00 35.64 ? 447 ASN A CA    1 
ATOM   3596  C  C     . ASN A 1 447 ? 132.318 150.137 119.375 1.00 36.48 ? 447 ASN A C     1 
ATOM   3597  O  O     . ASN A 1 447 ? 132.682 149.477 120.353 1.00 37.97 ? 447 ASN A O     1 
ATOM   3598  C  CB    . ASN A 1 447 ? 129.867 149.956 119.820 1.00 35.01 ? 447 ASN A CB    1 
ATOM   3599  C  CG    . ASN A 1 447 ? 129.120 150.406 121.056 1.00 33.30 ? 447 ASN A CG    1 
ATOM   3600  O  OD1   . ASN A 1 447 ? 129.721 150.674 122.095 1.00 37.48 ? 447 ASN A OD1   1 
ATOM   3601  N  ND2   . ASN A 1 447 ? 127.802 150.503 120.947 1.00 35.62 ? 447 ASN A ND2   1 
ATOM   3602  N  N     . ALA A 1 448 ? 133.029 150.196 118.249 1.00 39.77 ? 448 ALA A N     1 
ATOM   3603  C  CA    . ALA A 1 448 ? 134.359 149.610 118.095 1.00 34.40 ? 448 ALA A CA    1 
ATOM   3604  C  C     . ALA A 1 448 ? 135.284 150.728 117.638 1.00 33.53 ? 448 ALA A C     1 
ATOM   3605  O  O     . ALA A 1 448 ? 135.417 150.980 116.430 1.00 33.45 ? 448 ALA A O     1 
ATOM   3606  C  CB    . ALA A 1 448 ? 134.345 148.450 117.104 1.00 29.07 ? 448 ALA A CB    1 
ATOM   3607  N  N     . PRO A 1 449 ? 135.923 151.443 118.569 1.00 31.41 ? 449 PRO A N     1 
ATOM   3608  C  CA    . PRO A 1 449 ? 136.705 152.628 118.174 1.00 28.17 ? 449 PRO A CA    1 
ATOM   3609  C  C     . PRO A 1 449 ? 137.844 152.322 117.221 1.00 30.57 ? 449 PRO A C     1 
ATOM   3610  O  O     . PRO A 1 449 ? 138.100 153.101 116.295 1.00 29.91 ? 449 PRO A O     1 
ATOM   3611  C  CB    . PRO A 1 449 ? 137.224 153.168 119.516 1.00 28.42 ? 449 PRO A CB    1 
ATOM   3612  C  CG    . PRO A 1 449 ? 136.440 152.457 120.569 1.00 32.10 ? 449 PRO A CG    1 
ATOM   3613  C  CD    . PRO A 1 449 ? 136.043 151.148 120.004 1.00 29.92 ? 449 PRO A CD    1 
ATOM   3614  N  N     . ALA A 1 450 ? 138.536 151.198 117.416 1.00 32.32 ? 450 ALA A N     1 
ATOM   3615  C  CA    . ALA A 1 450 ? 139.666 150.875 116.555 1.00 23.55 ? 450 ALA A CA    1 
ATOM   3616  C  C     . ALA A 1 450 ? 139.208 150.430 115.175 1.00 25.93 ? 450 ALA A C     1 
ATOM   3617  O  O     . ALA A 1 450 ? 139.861 150.749 114.177 1.00 27.89 ? 450 ALA A O     1 
ATOM   3618  C  CB    . ALA A 1 450 ? 140.535 149.804 117.209 1.00 24.99 ? 450 ALA A CB    1 
ATOM   3619  N  N     . VAL A 1 451 ? 138.088 149.708 115.096 1.00 31.42 ? 451 VAL A N     1 
ATOM   3620  C  CA    . VAL A 1 451 ? 137.512 149.361 113.800 1.00 23.60 ? 451 VAL A CA    1 
ATOM   3621  C  C     . VAL A 1 451 ? 137.129 150.625 113.042 1.00 24.18 ? 451 VAL A C     1 
ATOM   3622  O  O     . VAL A 1 451 ? 137.411 150.763 111.847 1.00 30.42 ? 451 VAL A O     1 
ATOM   3623  C  CB    . VAL A 1 451 ? 136.305 148.422 113.985 1.00 25.32 ? 451 VAL A CB    1 
ATOM   3624  C  CG1   . VAL A 1 451 ? 135.457 148.381 112.725 1.00 26.85 ? 451 VAL A CG1   1 
ATOM   3625  C  CG2   . VAL A 1 451 ? 136.771 147.028 114.362 1.00 25.45 ? 451 VAL A CG2   1 
ATOM   3626  N  N     . ARG A 1 452 ? 136.491 151.569 113.734 1.00 25.32 ? 452 ARG A N     1 
ATOM   3627  C  CA    . ARG A 1 452 ? 136.138 152.849 113.127 1.00 25.30 ? 452 ARG A CA    1 
ATOM   3628  C  C     . ARG A 1 452 ? 137.374 153.580 112.616 1.00 26.72 ? 452 ARG A C     1 
ATOM   3629  O  O     . ARG A 1 452 ? 137.409 154.044 111.468 1.00 32.24 ? 452 ARG A O     1 
ATOM   3630  C  CB    . ARG A 1 452 ? 135.402 153.710 114.153 1.00 27.80 ? 452 ARG A CB    1 
ATOM   3631  C  CG    . ARG A 1 452 ? 134.344 154.637 113.597 1.00 27.41 ? 452 ARG A CG    1 
ATOM   3632  C  CD    . ARG A 1 452 ? 134.239 155.871 114.475 1.00 29.77 ? 452 ARG A CD    1 
ATOM   3633  N  NE    . ARG A 1 452 ? 133.026 156.640 114.231 1.00 38.95 ? 452 ARG A NE    1 
ATOM   3634  C  CZ    . ARG A 1 452 ? 132.170 157.000 115.177 1.00 39.25 ? 452 ARG A CZ    1 
ATOM   3635  N  NH1   . ARG A 1 452 ? 132.366 156.679 116.445 1.00 36.87 ? 452 ARG A NH1   1 
ATOM   3636  N  NH2   . ARG A 1 452 ? 131.091 157.702 114.843 1.00 39.20 ? 452 ARG A NH2   1 
ATOM   3637  N  N     . ARG A 1 453 ? 138.399 153.693 113.463 1.00 27.52 ? 453 ARG A N     1 
ATOM   3638  C  CA    . ARG A 1 453 ? 139.590 154.446 113.088 1.00 25.67 ? 453 ARG A CA    1 
ATOM   3639  C  C     . ARG A 1 453 ? 140.309 153.796 111.914 1.00 31.32 ? 453 ARG A C     1 
ATOM   3640  O  O     . ARG A 1 453 ? 140.752 154.487 110.990 1.00 35.57 ? 453 ARG A O     1 
ATOM   3641  C  CB    . ARG A 1 453 ? 140.526 154.577 114.289 1.00 26.90 ? 453 ARG A CB    1 
ATOM   3642  C  CG    . ARG A 1 453 ? 141.659 155.564 114.083 1.00 29.92 ? 453 ARG A CG    1 
ATOM   3643  C  CD    . ARG A 1 453 ? 142.788 155.323 115.065 1.00 27.04 ? 453 ARG A CD    1 
ATOM   3644  N  NE    . ARG A 1 453 ? 144.062 155.814 114.556 1.00 29.81 ? 453 ARG A NE    1 
ATOM   3645  C  CZ    . ARG A 1 453 ? 145.239 155.273 114.836 1.00 32.02 ? 453 ARG A CZ    1 
ATOM   3646  N  NH1   . ARG A 1 453 ? 145.346 154.223 115.632 1.00 30.75 ? 453 ARG A NH1   1 
ATOM   3647  N  NH2   . ARG A 1 453 ? 146.338 155.798 114.301 1.00 30.23 ? 453 ARG A NH2   1 
ATOM   3648  N  N     . ALA A 1 454 ? 140.426 152.466 111.925 1.00 26.84 ? 454 ALA A N     1 
ATOM   3649  C  CA    . ALA A 1 454 ? 141.105 151.779 110.836 1.00 20.54 ? 454 ALA A CA    1 
ATOM   3650  C  C     . ALA A 1 454 ? 140.292 151.816 109.551 1.00 19.93 ? 454 ALA A C     1 
ATOM   3651  O  O     . ALA A 1 454 ? 140.869 151.857 108.463 1.00 25.65 ? 454 ALA A O     1 
ATOM   3652  C  CB    . ALA A 1 454 ? 141.411 150.337 111.231 1.00 23.86 ? 454 ALA A CB    1 
ATOM   3653  N  N     . ASN A 1 455 ? 138.962 151.804 109.646 1.00 24.57 ? 455 ASN A N     1 
ATOM   3654  C  CA    . ASN A 1 455 ? 138.148 151.954 108.447 1.00 23.18 ? 455 ASN A CA    1 
ATOM   3655  C  C     . ASN A 1 455 ? 138.312 153.342 107.846 1.00 26.37 ? 455 ASN A C     1 
ATOM   3656  O  O     . ASN A 1 455 ? 138.356 153.493 106.619 1.00 32.93 ? 455 ASN A O     1 
ATOM   3657  C  CB    . ASN A 1 455 ? 136.682 151.673 108.768 1.00 20.82 ? 455 ASN A CB    1 
ATOM   3658  C  CG    . ASN A 1 455 ? 135.801 151.715 107.538 1.00 28.26 ? 455 ASN A CG    1 
ATOM   3659  O  OD1   . ASN A 1 455 ? 135.960 150.912 106.621 1.00 35.92 ? 455 ASN A OD1   1 
ATOM   3660  N  ND2   . ASN A 1 455 ? 134.865 152.655 107.511 1.00 27.11 ? 455 ASN A ND2   1 
ATOM   3661  N  N     . LYS A 1 456 ? 138.396 154.370 108.692 1.00 29.49 ? 456 LYS A N     1 
ATOM   3662  C  CA    . LYS A 1 456 ? 138.582 155.723 108.175 1.00 26.36 ? 456 LYS A CA    1 
ATOM   3663  C  C     . LYS A 1 456 ? 139.984 155.920 107.607 1.00 27.09 ? 456 LYS A C     1 
ATOM   3664  O  O     . LYS A 1 456 ? 140.158 156.623 106.606 1.00 31.02 ? 456 LYS A O     1 
ATOM   3665  C  CB    . LYS A 1 456 ? 138.296 156.750 109.269 1.00 26.75 ? 456 LYS A CB    1 
ATOM   3666  C  CG    . LYS A 1 456 ? 136.893 156.666 109.841 1.00 29.78 ? 456 LYS A CG    1 
ATOM   3667  C  CD    . LYS A 1 456 ? 136.562 157.884 110.683 1.00 34.02 ? 456 LYS A CD    1 
ATOM   3668  C  CE    . LYS A 1 456 ? 135.075 157.955 110.988 1.00 33.30 ? 456 LYS A CE    1 
ATOM   3669  N  NZ    . LYS A 1 456 ? 134.244 157.627 109.798 1.00 32.80 ? 456 LYS A NZ    1 
ATOM   3670  N  N     . ALA A 1 457 ? 140.995 155.311 108.226 1.00 26.96 ? 457 ALA A N     1 
ATOM   3671  C  CA    . ALA A 1 457 ? 142.383 155.567 107.857 1.00 22.43 ? 457 ALA A CA    1 
ATOM   3672  C  C     . ALA A 1 457 ? 142.877 154.664 106.731 1.00 27.37 ? 457 ALA A C     1 
ATOM   3673  O  O     . ALA A 1 457 ? 143.400 155.152 105.726 1.00 32.85 ? 457 ALA A O     1 
ATOM   3674  C  CB    . ALA A 1 457 ? 143.281 155.410 109.087 1.00 22.58 ? 457 ALA A CB    1 
ATOM   3675  N  N     . MET A 1 458 ? 142.729 153.348 106.888 1.00 30.23 ? 458 MET A N     1 
ATOM   3676  C  CA    . MET A 1 458 ? 143.252 152.402 105.910 1.00 20.52 ? 458 MET A CA    1 
ATOM   3677  C  C     . MET A 1 458 ? 142.411 152.367 104.642 1.00 22.41 ? 458 MET A C     1 
ATOM   3678  O  O     . MET A 1 458 ? 142.954 152.207 103.544 1.00 30.57 ? 458 MET A O     1 
ATOM   3679  C  CB    . MET A 1 458 ? 143.331 151.007 106.529 1.00 21.89 ? 458 MET A CB    1 
ATOM   3680  C  CG    . MET A 1 458 ? 144.000 150.966 107.888 1.00 22.10 ? 458 MET A CG    1 
ATOM   3681  S  SD    . MET A 1 458 ? 145.743 151.404 107.800 1.00 32.95 ? 458 MET A SD    1 
ATOM   3682  C  CE    . MET A 1 458 ? 146.486 149.777 107.723 1.00 25.44 ? 458 MET A CE    1 
ATOM   3683  N  N     . LYS A 1 459 ? 141.090 152.504 104.775 1.00 16.31 ? 459 LYS A N     1 
ATOM   3684  C  CA    . LYS A 1 459 ? 140.167 152.416 103.642 1.00 21.55 ? 459 LYS A CA    1 
ATOM   3685  C  C     . LYS A 1 459 ? 140.345 151.101 102.887 1.00 17.81 ? 459 LYS A C     1 
ATOM   3686  O  O     . LYS A 1 459 ? 140.346 151.064 101.656 1.00 25.33 ? 459 LYS A O     1 
ATOM   3687  C  CB    . LYS A 1 459 ? 140.328 153.610 102.699 1.00 22.29 ? 459 LYS A CB    1 
ATOM   3688  C  CG    . LYS A 1 459 ? 140.316 154.955 103.398 1.00 25.20 ? 459 LYS A CG    1 
ATOM   3689  C  CD    . LYS A 1 459 ? 141.253 155.932 102.717 1.00 24.57 ? 459 LYS A CD    1 
ATOM   3690  C  CE    . LYS A 1 459 ? 141.255 157.273 103.421 1.00 28.81 ? 459 LYS A CE    1 
ATOM   3691  N  NZ    . LYS A 1 459 ? 142.292 158.182 102.863 1.00 31.33 ? 459 LYS A NZ    1 
ATOM   3692  N  N     . SER A 1 460 ? 140.497 150.011 103.634 1.00 19.84 ? 460 SER A N     1 
ATOM   3693  C  CA    . SER A 1 460 ? 140.751 148.707 103.040 1.00 13.49 ? 460 SER A CA    1 
ATOM   3694  C  C     . SER A 1 460 ? 139.469 148.097 102.495 1.00 20.51 ? 460 SER A C     1 
ATOM   3695  O  O     . SER A 1 460 ? 138.403 148.198 103.107 1.00 30.20 ? 460 SER A O     1 
ATOM   3696  C  CB    . SER A 1 460 ? 141.372 147.764 104.068 1.00 9.40  ? 460 SER A CB    1 
ATOM   3697  O  OG    . SER A 1 460 ? 142.461 148.378 104.732 1.00 29.56 ? 460 SER A OG    1 
ATOM   3698  N  N     . ILE A 1 461 ? 139.583 147.456 101.333 1.00 13.07 ? 461 ILE A N     1 
ATOM   3699  C  CA    . ILE A 1 461 ? 138.481 146.735 100.717 1.00 14.03 ? 461 ILE A CA    1 
ATOM   3700  C  C     . ILE A 1 461 ? 138.975 145.346 100.346 1.00 14.45 ? 461 ILE A C     1 
ATOM   3701  O  O     . ILE A 1 461 ? 140.176 145.101 100.220 1.00 22.99 ? 461 ILE A O     1 
ATOM   3702  C  CB    . ILE A 1 461 ? 137.923 147.458 99.472  1.00 13.73 ? 461 ILE A CB    1 
ATOM   3703  C  CG1   . ILE A 1 461 ? 139.010 147.595 98.406  1.00 7.22  ? 461 ILE A CG1   1 
ATOM   3704  C  CG2   . ILE A 1 461 ? 137.363 148.820 99.850  1.00 14.63 ? 461 ILE A CG2   1 
ATOM   3705  C  CD1   . ILE A 1 461 ? 138.551 148.284 97.151  1.00 6.44  ? 461 ILE A CD1   1 
ATOM   3706  N  N     . GLY A 1 462 ? 138.032 144.423 100.196 1.00 15.79 ? 462 GLY A N     1 
ATOM   3707  C  CA    . GLY A 1 462 ? 138.376 143.106 99.704  1.00 7.58  ? 462 GLY A CA    1 
ATOM   3708  C  C     . GLY A 1 462 ? 137.599 142.730 98.463  1.00 5.83  ? 462 GLY A C     1 
ATOM   3709  O  O     . GLY A 1 462 ? 136.392 142.490 98.532  1.00 23.58 ? 462 GLY A O     1 
ATOM   3710  N  N     . LEU A 1 463 ? 138.280 142.659 97.325  1.00 14.19 ? 463 LEU A N     1 
ATOM   3711  C  CA    . LEU A 1 463 ? 137.657 142.285 96.062  1.00 11.66 ? 463 LEU A CA    1 
ATOM   3712  C  C     . LEU A 1 463 ? 138.109 140.875 95.710  1.00 16.29 ? 463 LEU A C     1 
ATOM   3713  O  O     . LEU A 1 463 ? 139.257 140.664 95.306  1.00 28.24 ? 463 LEU A O     1 
ATOM   3714  C  CB    . LEU A 1 463 ? 138.015 143.276 94.957  1.00 17.99 ? 463 LEU A CB    1 
ATOM   3715  C  CG    . LEU A 1 463 ? 137.438 142.977 93.572  1.00 17.43 ? 463 LEU A CG    1 
ATOM   3716  C  CD1   . LEU A 1 463 ? 135.939 142.745 93.650  1.00 7.87  ? 463 LEU A CD1   1 
ATOM   3717  C  CD2   . LEU A 1 463 ? 137.759 144.102 92.603  1.00 15.04 ? 463 LEU A CD2   1 
ATOM   3718  N  N     . GLY A 1 464 ? 137.206 139.909 95.872  1.00 18.35 ? 464 GLY A N     1 
ATOM   3719  C  CA    . GLY A 1 464 ? 137.490 138.526 95.572  1.00 12.24 ? 464 GLY A CA    1 
ATOM   3720  C  C     . GLY A 1 464 ? 136.943 138.102 94.222  1.00 12.55 ? 464 GLY A C     1 
ATOM   3721  O  O     . GLY A 1 464 ? 136.468 138.907 93.419  1.00 18.70 ? 464 GLY A O     1 
ATOM   3722  N  N     . ALA A 1 465 ? 137.026 136.800 93.974  1.00 15.45 ? 465 ALA A N     1 
ATOM   3723  C  CA    . ALA A 1 465 ? 136.489 136.207 92.764  1.00 11.81 ? 465 ALA A CA    1 
ATOM   3724  C  C     . ALA A 1 465 ? 135.904 134.845 93.100  1.00 17.71 ? 465 ALA A C     1 
ATOM   3725  O  O     . ALA A 1 465 ? 136.266 134.221 94.099  1.00 29.82 ? 465 ALA A O     1 
ATOM   3726  C  CB    . ALA A 1 465 ? 137.558 136.080 91.673  1.00 16.04 ? 465 ALA A CB    1 
ATOM   3727  N  N     . MET A 1 466 ? 134.978 134.396 92.257  1.00 21.76 ? 466 MET A N     1 
ATOM   3728  C  CA    . MET A 1 466 ? 134.415 133.060 92.359  1.00 21.37 ? 466 MET A CA    1 
ATOM   3729  C  C     . MET A 1 466 ? 134.231 132.506 90.954  1.00 20.50 ? 466 MET A C     1 
ATOM   3730  O  O     . MET A 1 466 ? 134.543 133.167 89.960  1.00 24.86 ? 466 MET A O     1 
ATOM   3731  C  CB    . MET A 1 466 ? 133.086 133.052 93.120  1.00 26.38 ? 466 MET A CB    1 
ATOM   3732  C  CG    . MET A 1 466 ? 132.093 134.099 92.664  1.00 28.30 ? 466 MET A CG    1 
ATOM   3733  S  SD    . MET A 1 466 ? 130.551 133.971 93.582  1.00 39.25 ? 466 MET A SD    1 
ATOM   3734  C  CE    . MET A 1 466 ? 130.017 135.671 93.569  1.00 26.70 ? 466 MET A CE    1 
ATOM   3735  N  N     . ASN A 1 467 ? 133.718 131.277 90.884  1.00 20.70 ? 467 ASN A N     1 
ATOM   3736  C  CA    . ASN A 1 467 ? 133.451 130.588 89.622  1.00 20.59 ? 467 ASN A CA    1 
ATOM   3737  C  C     . ASN A 1 467 ? 134.728 130.330 88.829  1.00 21.04 ? 467 ASN A C     1 
ATOM   3738  O  O     . ASN A 1 467 ? 134.697 130.244 87.601  1.00 26.84 ? 467 ASN A O     1 
ATOM   3739  C  CB    . ASN A 1 467 ? 132.441 131.358 88.765  1.00 21.13 ? 467 ASN A CB    1 
ATOM   3740  C  CG    . ASN A 1 467 ? 131.394 130.458 88.151  1.00 26.17 ? 467 ASN A CG    1 
ATOM   3741  O  OD1   . ASN A 1 467 ? 131.326 129.269 88.453  1.00 30.49 ? 467 ASN A OD1   1 
ATOM   3742  N  ND2   . ASN A 1 467 ? 130.560 131.025 87.293  1.00 28.22 ? 467 ASN A ND2   1 
ATOM   3743  N  N     . LEU A 1 468 ? 135.864 130.212 89.517  1.00 17.83 ? 468 LEU A N     1 
ATOM   3744  C  CA    . LEU A 1 468 ? 137.096 129.838 88.831  1.00 19.39 ? 468 LEU A CA    1 
ATOM   3745  C  C     . LEU A 1 468 ? 137.010 128.412 88.306  1.00 22.99 ? 468 LEU A C     1 
ATOM   3746  O  O     . LEU A 1 468 ? 137.267 128.155 87.124  1.00 24.24 ? 468 LEU A O     1 
ATOM   3747  C  CB    . LEU A 1 468 ? 138.293 129.993 89.768  1.00 23.56 ? 468 LEU A CB    1 
ATOM   3748  C  CG    . LEU A 1 468 ? 139.604 129.391 89.254  1.00 20.18 ? 468 LEU A CG    1 
ATOM   3749  C  CD1   . LEU A 1 468 ? 140.185 130.239 88.137  1.00 17.87 ? 468 LEU A CD1   1 
ATOM   3750  C  CD2   . LEU A 1 468 ? 140.607 129.218 90.377  1.00 14.95 ? 468 LEU A CD2   1 
ATOM   3751  N  N     . HIS A 1 469 ? 136.628 127.470 89.172  1.00 25.28 ? 469 HIS A N     1 
ATOM   3752  C  CA    . HIS A 1 469 ? 136.479 126.089 88.733  1.00 15.64 ? 469 HIS A CA    1 
ATOM   3753  C  C     . HIS A 1 469 ? 135.325 125.948 87.752  1.00 25.35 ? 469 HIS A C     1 
ATOM   3754  O  O     . HIS A 1 469 ? 135.410 125.166 86.802  1.00 36.75 ? 469 HIS A O     1 
ATOM   3755  C  CB    . HIS A 1 469 ? 136.278 125.163 89.930  1.00 20.17 ? 469 HIS A CB    1 
ATOM   3756  C  CG    . HIS A 1 469 ? 136.399 123.710 89.591  1.00 23.85 ? 469 HIS A CG    1 
ATOM   3757  N  ND1   . HIS A 1 469 ? 136.103 122.708 90.488  1.00 29.66 ? 469 HIS A ND1   1 
ATOM   3758  C  CD2   . HIS A 1 469 ? 136.790 123.090 88.452  1.00 25.75 ? 469 HIS A CD2   1 
ATOM   3759  C  CE1   . HIS A 1 469 ? 136.300 121.534 89.916  1.00 26.66 ? 469 HIS A CE1   1 
ATOM   3760  N  NE2   . HIS A 1 469 ? 136.718 121.738 88.681  1.00 23.65 ? 469 HIS A NE2   1 
ATOM   3761  N  N     . GLY A 1 470 ? 134.237 126.687 87.967  1.00 23.10 ? 470 GLY A N     1 
ATOM   3762  C  CA    . GLY A 1 470 ? 133.139 126.648 87.015  1.00 18.48 ? 470 GLY A CA    1 
ATOM   3763  C  C     . GLY A 1 470 ? 133.552 127.132 85.640  1.00 14.18 ? 470 GLY A C     1 
ATOM   3764  O  O     . GLY A 1 470 ? 133.229 126.511 84.623  1.00 32.12 ? 470 GLY A O     1 
ATOM   3765  N  N     . TYR A 1 471 ? 134.289 128.244 85.593  1.00 17.64 ? 471 TYR A N     1 
ATOM   3766  C  CA    . TYR A 1 471 ? 134.763 128.767 84.317  1.00 21.52 ? 471 TYR A CA    1 
ATOM   3767  C  C     . TYR A 1 471 ? 135.725 127.797 83.644  1.00 27.21 ? 471 TYR A C     1 
ATOM   3768  O  O     . TYR A 1 471 ? 135.653 127.586 82.429  1.00 29.85 ? 471 TYR A O     1 
ATOM   3769  C  CB    . TYR A 1 471 ? 135.433 130.126 84.521  1.00 22.55 ? 471 TYR A CB    1 
ATOM   3770  C  CG    . TYR A 1 471 ? 136.059 130.688 83.267  1.00 26.27 ? 471 TYR A CG    1 
ATOM   3771  C  CD1   . TYR A 1 471 ? 135.274 131.264 82.279  1.00 26.32 ? 471 TYR A CD1   1 
ATOM   3772  C  CD2   . TYR A 1 471 ? 137.430 130.630 83.064  1.00 20.63 ? 471 TYR A CD2   1 
ATOM   3773  C  CE1   . TYR A 1 471 ? 135.837 131.775 81.129  1.00 26.51 ? 471 TYR A CE1   1 
ATOM   3774  C  CE2   . TYR A 1 471 ? 138.002 131.135 81.915  1.00 20.89 ? 471 TYR A CE2   1 
ATOM   3775  C  CZ    . TYR A 1 471 ? 137.201 131.708 80.952  1.00 28.31 ? 471 TYR A CZ    1 
ATOM   3776  O  OH    . TYR A 1 471 ? 137.767 132.215 79.807  1.00 31.74 ? 471 TYR A OH    1 
ATOM   3777  N  N     . LEU A 1 472 ? 136.638 127.202 84.416  1.00 22.68 ? 472 LEU A N     1 
ATOM   3778  C  CA    . LEU A 1 472 ? 137.606 126.280 83.829  1.00 21.92 ? 472 LEU A CA    1 
ATOM   3779  C  C     . LEU A 1 472 ? 136.933 125.008 83.325  1.00 27.56 ? 472 LEU A C     1 
ATOM   3780  O  O     . LEU A 1 472 ? 137.246 124.527 82.230  1.00 31.78 ? 472 LEU A O     1 
ATOM   3781  C  CB    . LEU A 1 472 ? 138.696 125.945 84.846  1.00 27.12 ? 472 LEU A CB    1 
ATOM   3782  C  CG    . LEU A 1 472 ? 139.603 127.099 85.276  1.00 29.31 ? 472 LEU A CG    1 
ATOM   3783  C  CD1   . LEU A 1 472 ? 140.360 126.732 86.540  1.00 23.36 ? 472 LEU A CD1   1 
ATOM   3784  C  CD2   . LEU A 1 472 ? 140.560 127.488 84.164  1.00 22.41 ? 472 LEU A CD2   1 
ATOM   3785  N  N     . ALA A 1 473 ? 136.011 124.446 84.109  1.00 29.02 ? 473 ALA A N     1 
ATOM   3786  C  CA    . ALA A 1 473 ? 135.331 123.221 83.710  1.00 25.20 ? 473 ALA A CA    1 
ATOM   3787  C  C     . ALA A 1 473 ? 134.413 123.458 82.519  1.00 32.27 ? 473 ALA A C     1 
ATOM   3788  O  O     . ALA A 1 473 ? 134.269 122.583 81.657  1.00 40.05 ? 473 ALA A O     1 
ATOM   3789  C  CB    . ALA A 1 473 ? 134.547 122.654 84.891  1.00 26.41 ? 473 ALA A CB    1 
ATOM   3790  N  N     . GLN A 1 474 ? 133.783 124.631 82.450  1.00 28.29 ? 474 GLN A N     1 
ATOM   3791  C  CA    . GLN A 1 474 ? 132.945 124.957 81.307  1.00 25.45 ? 474 GLN A CA    1 
ATOM   3792  C  C     . GLN A 1 474 ? 133.752 125.380 80.089  1.00 24.28 ? 474 GLN A C     1 
ATOM   3793  O  O     . GLN A 1 474 ? 133.167 125.597 79.023  1.00 34.45 ? 474 GLN A O     1 
ATOM   3794  C  CB    . GLN A 1 474 ? 131.949 126.056 81.681  1.00 28.23 ? 474 GLN A CB    1 
ATOM   3795  C  CG    . GLN A 1 474 ? 130.783 125.552 82.510  1.00 30.74 ? 474 GLN A CG    1 
ATOM   3796  C  CD    . GLN A 1 474 ? 129.974 126.672 83.122  1.00 30.55 ? 474 GLN A CD    1 
ATOM   3797  O  OE1   . GLN A 1 474 ? 129.304 127.425 82.417  1.00 33.03 ? 474 GLN A OE1   1 
ATOM   3798  N  NE2   . GLN A 1 474 ? 130.032 126.789 84.442  1.00 31.70 ? 474 GLN A NE2   1 
ATOM   3799  N  N     . ASN A 1 475 ? 135.072 125.506 80.221  1.00 32.02 ? 475 ASN A N     1 
ATOM   3800  C  CA    . ASN A 1 475 ? 135.955 125.803 79.102  1.00 33.54 ? 475 ASN A CA    1 
ATOM   3801  C  C     . ASN A 1 475 ? 136.890 124.645 78.782  1.00 33.94 ? 475 ASN A C     1 
ATOM   3802  O  O     . ASN A 1 475 ? 137.858 124.829 78.038  1.00 37.52 ? 475 ASN A O     1 
ATOM   3803  C  CB    . ASN A 1 475 ? 136.764 127.069 79.388  1.00 34.78 ? 475 ASN A CB    1 
ATOM   3804  C  CG    . ASN A 1 475 ? 135.939 128.329 79.246  1.00 30.57 ? 475 ASN A CG    1 
ATOM   3805  O  OD1   . ASN A 1 475 ? 135.910 128.950 78.185  1.00 34.76 ? 475 ASN A OD1   1 
ATOM   3806  N  ND2   . ASN A 1 475 ? 135.253 128.708 80.315  1.00 26.43 ? 475 ASN A ND2   1 
ATOM   3807  N  N     . GLY A 1 476 ? 136.625 123.462 79.326  1.00 29.81 ? 476 GLY A N     1 
ATOM   3808  C  CA    . GLY A 1 476 ? 137.455 122.299 79.066  1.00 29.94 ? 476 GLY A CA    1 
ATOM   3809  C  C     . GLY A 1 476 ? 138.861 122.387 79.617  1.00 34.05 ? 476 GLY A C     1 
ATOM   3810  O  O     . GLY A 1 476 ? 139.813 121.973 78.943  1.00 36.00 ? 476 GLY A O     1 
ATOM   3811  N  N     . ILE A 1 477 ? 139.019 122.917 80.827  1.00 31.51 ? 477 ILE A N     1 
ATOM   3812  C  CA    . ILE A 1 477 ? 140.319 123.031 81.477  1.00 28.73 ? 477 ILE A CA    1 
ATOM   3813  C  C     . ILE A 1 477 ? 140.236 122.357 82.838  1.00 31.61 ? 477 ILE A C     1 
ATOM   3814  O  O     . ILE A 1 477 ? 139.348 122.672 83.637  1.00 35.05 ? 477 ILE A O     1 
ATOM   3815  C  CB    . ILE A 1 477 ? 140.760 124.500 81.628  1.00 27.74 ? 477 ILE A CB    1 
ATOM   3816  C  CG1   . ILE A 1 477 ? 140.776 125.198 80.267  1.00 31.95 ? 477 ILE A CG1   1 
ATOM   3817  C  CG2   . ILE A 1 477 ? 142.126 124.577 82.278  1.00 31.27 ? 477 ILE A CG2   1 
ATOM   3818  C  CD1   . ILE A 1 477 ? 140.733 126.703 80.356  1.00 33.36 ? 477 ILE A CD1   1 
ATOM   3819  N  N     . ALA A 1 478 ? 141.154 121.431 83.096  1.00 31.23 ? 478 ALA A N     1 
ATOM   3820  C  CA    . ALA A 1 478 ? 141.213 120.781 84.397  1.00 26.49 ? 478 ALA A CA    1 
ATOM   3821  C  C     . ALA A 1 478 ? 141.759 121.744 85.443  1.00 33.56 ? 478 ALA A C     1 
ATOM   3822  O  O     . ALA A 1 478 ? 142.645 122.552 85.160  1.00 35.64 ? 478 ALA A O     1 
ATOM   3823  C  CB    . ALA A 1 478 ? 142.083 119.528 84.329  1.00 28.98 ? 478 ALA A CB    1 
ATOM   3824  N  N     . TYR A 1 479 ? 141.222 121.652 86.661  1.00 31.25 ? 479 TYR A N     1 
ATOM   3825  C  CA    . TYR A 1 479 ? 141.647 122.550 87.730  1.00 22.57 ? 479 TYR A CA    1 
ATOM   3826  C  C     . TYR A 1 479 ? 143.125 122.366 88.052  1.00 30.18 ? 479 TYR A C     1 
ATOM   3827  O  O     . TYR A 1 479 ? 143.839 123.343 88.307  1.00 39.53 ? 479 TYR A O     1 
ATOM   3828  C  CB    . TYR A 1 479 ? 140.791 122.321 88.975  1.00 21.85 ? 479 TYR A CB    1 
ATOM   3829  C  CG    . TYR A 1 479 ? 140.975 123.360 90.057  1.00 27.67 ? 479 TYR A CG    1 
ATOM   3830  C  CD1   . TYR A 1 479 ? 140.201 124.512 90.077  1.00 24.07 ? 479 TYR A CD1   1 
ATOM   3831  C  CD2   . TYR A 1 479 ? 141.916 123.187 91.065  1.00 29.03 ? 479 TYR A CD2   1 
ATOM   3832  C  CE1   . TYR A 1 479 ? 140.360 125.462 91.063  1.00 24.73 ? 479 TYR A CE1   1 
ATOM   3833  C  CE2   . TYR A 1 479 ? 142.083 124.133 92.054  1.00 26.84 ? 479 TYR A CE2   1 
ATOM   3834  C  CZ    . TYR A 1 479 ? 141.303 125.269 92.048  1.00 30.36 ? 479 TYR A CZ    1 
ATOM   3835  O  OH    . TYR A 1 479 ? 141.462 126.216 93.033  1.00 31.12 ? 479 TYR A OH    1 
ATOM   3836  N  N     . GLU A 1 480 ? 143.601 121.122 88.047  1.00 34.66 ? 480 GLU A N     1 
ATOM   3837  C  CA    . GLU A 1 480 ? 144.999 120.835 88.338  1.00 30.27 ? 480 GLU A CA    1 
ATOM   3838  C  C     . GLU A 1 480 ? 145.921 121.084 87.154  1.00 32.20 ? 480 GLU A C     1 
ATOM   3839  O  O     . GLU A 1 480 ? 147.143 121.039 87.326  1.00 38.56 ? 480 GLU A O     1 
ATOM   3840  C  CB    . GLU A 1 480 ? 145.161 119.383 88.782  1.00 35.99 ? 480 GLU A CB    1 
ATOM   3841  C  CG    . GLU A 1 480 ? 144.345 118.989 89.989  1.00 33.00 ? 480 GLU A CG    1 
ATOM   3842  C  CD    . GLU A 1 480 ? 144.029 117.510 89.993  1.00 41.30 ? 480 GLU A CD    1 
ATOM   3843  O  OE1   . GLU A 1 480 ? 143.013 117.118 89.383  1.00 41.62 ? 480 GLU A OE1   1 
ATOM   3844  O  OE2   . GLU A 1 480 ? 144.798 116.738 90.602  1.00 42.97 ? 480 GLU A OE2   1 
ATOM   3845  N  N     . SER A 1 481 ? 145.376 121.335 85.969  1.00 33.92 ? 481 SER A N     1 
ATOM   3846  C  CA    . SER A 1 481 ? 146.201 121.464 84.783  1.00 33.29 ? 481 SER A CA    1 
ATOM   3847  C  C     . SER A 1 481 ? 147.041 122.740 84.839  1.00 34.57 ? 481 SER A C     1 
ATOM   3848  O  O     . SER A 1 481 ? 146.643 123.730 85.459  1.00 38.16 ? 481 SER A O     1 
ATOM   3849  C  CB    . SER A 1 481 ? 145.331 121.469 83.530  1.00 32.77 ? 481 SER A CB    1 
ATOM   3850  O  OG    . SER A 1 481 ? 144.800 122.757 83.283  1.00 35.69 ? 481 SER A OG    1 
ATOM   3851  N  N     . PRO A 1 482 ? 148.221 122.733 84.213  1.00 38.29 ? 482 PRO A N     1 
ATOM   3852  C  CA    . PRO A 1 482 ? 149.012 123.971 84.131  1.00 36.10 ? 482 PRO A CA    1 
ATOM   3853  C  C     . PRO A 1 482 ? 148.304 125.091 83.392  1.00 36.16 ? 482 PRO A C     1 
ATOM   3854  O  O     . PRO A 1 482 ? 148.569 126.267 83.667  1.00 39.68 ? 482 PRO A O     1 
ATOM   3855  C  CB    . PRO A 1 482 ? 150.284 123.524 83.397  1.00 35.48 ? 482 PRO A CB    1 
ATOM   3856  C  CG    . PRO A 1 482 ? 150.354 122.052 83.609  1.00 37.24 ? 482 PRO A CG    1 
ATOM   3857  C  CD    . PRO A 1 482 ? 148.936 121.580 83.642  1.00 39.90 ? 482 PRO A CD    1 
ATOM   3858  N  N     . GLU A 1 483 ? 147.418 124.761 82.449  1.00 37.40 ? 483 GLU A N     1 
ATOM   3859  C  CA    . GLU A 1 483 ? 146.665 125.791 81.741  1.00 36.03 ? 483 GLU A CA    1 
ATOM   3860  C  C     . GLU A 1 483 ? 145.739 126.544 82.686  1.00 33.45 ? 483 GLU A C     1 
ATOM   3861  O  O     . GLU A 1 483 ? 145.546 127.757 82.541  1.00 36.43 ? 483 GLU A O     1 
ATOM   3862  C  CB    . GLU A 1 483 ? 145.871 125.165 80.596  1.00 38.34 ? 483 GLU A CB    1 
ATOM   3863  C  CG    . GLU A 1 483 ? 146.734 124.655 79.457  1.00 40.83 ? 483 GLU A CG    1 
ATOM   3864  C  CD    . GLU A 1 483 ? 147.140 123.207 79.641  1.00 43.59 ? 483 GLU A CD    1 
ATOM   3865  O  OE1   . GLU A 1 483 ? 146.854 122.641 80.717  1.00 40.91 ? 483 GLU A OE1   1 
ATOM   3866  O  OE2   . GLU A 1 483 ? 147.750 122.635 78.715  1.00 43.32 ? 483 GLU A OE2   1 
ATOM   3867  N  N     . ALA A 1 484 ? 145.150 125.841 83.655  1.00 28.20 ? 484 ALA A N     1 
ATOM   3868  C  CA    . ALA A 1 484 ? 144.309 126.504 84.645  1.00 28.95 ? 484 ALA A CA    1 
ATOM   3869  C  C     . ALA A 1 484 ? 145.112 127.498 85.472  1.00 29.18 ? 484 ALA A C     1 
ATOM   3870  O  O     . ALA A 1 484 ? 144.654 128.618 85.728  1.00 31.45 ? 484 ALA A O     1 
ATOM   3871  C  CB    . ALA A 1 484 ? 143.648 125.469 85.549  1.00 28.44 ? 484 ALA A CB    1 
ATOM   3872  N  N     . ARG A 1 485 ? 146.312 127.105 85.902  1.00 30.84 ? 485 ARG A N     1 
ATOM   3873  C  CA    . ARG A 1 485 ? 147.159 128.020 86.658  1.00 24.75 ? 485 ARG A CA    1 
ATOM   3874  C  C     . ARG A 1 485 ? 147.628 129.184 85.799  1.00 26.37 ? 485 ARG A C     1 
ATOM   3875  O  O     . ARG A 1 485 ? 147.764 130.302 86.301  1.00 36.40 ? 485 ARG A O     1 
ATOM   3876  C  CB    . ARG A 1 485 ? 148.352 127.269 87.245  1.00 27.67 ? 485 ARG A CB    1 
ATOM   3877  C  CG    . ARG A 1 485 ? 147.988 126.367 88.407  1.00 26.23 ? 485 ARG A CG    1 
ATOM   3878  C  CD    . ARG A 1 485 ? 149.226 125.822 89.088  1.00 29.56 ? 485 ARG A CD    1 
ATOM   3879  N  NE    . ARG A 1 485 ? 150.038 125.016 88.186  1.00 31.92 ? 485 ARG A NE    1 
ATOM   3880  C  CZ    . ARG A 1 485 ? 149.814 123.737 87.920  1.00 32.71 ? 485 ARG A CZ    1 
ATOM   3881  N  NH1   . ARG A 1 485 ? 148.807 123.081 88.472  1.00 30.76 ? 485 ARG A NH1   1 
ATOM   3882  N  NH2   . ARG A 1 485 ? 150.624 123.098 87.081  1.00 29.71 ? 485 ARG A NH2   1 
ATOM   3883  N  N     . ASP A 1 486 ? 147.873 128.946 84.510  1.00 31.75 ? 486 ASP A N     1 
ATOM   3884  C  CA    . ASP A 1 486 ? 148.224 130.032 83.600  1.00 30.66 ? 486 ASP A CA    1 
ATOM   3885  C  C     . ASP A 1 486 ? 147.083 131.036 83.480  1.00 30.12 ? 486 ASP A C     1 
ATOM   3886  O  O     . ASP A 1 486 ? 147.297 132.258 83.527  1.00 37.03 ? 486 ASP A O     1 
ATOM   3887  C  CB    . ASP A 1 486 ? 148.587 129.452 82.235  1.00 33.76 ? 486 ASP A CB    1 
ATOM   3888  C  CG    . ASP A 1 486 ? 149.101 130.495 81.274  1.00 40.95 ? 486 ASP A CG    1 
ATOM   3889  O  OD1   . ASP A 1 486 ? 150.049 131.224 81.631  1.00 42.50 ? 486 ASP A OD1   1 
ATOM   3890  O  OD2   . ASP A 1 486 ? 148.555 130.581 80.156  1.00 39.85 ? 486 ASP A OD2   1 
ATOM   3891  N  N     . PHE A 1 487 ? 145.854 130.534 83.330  1.00 30.44 ? 487 PHE A N     1 
ATOM   3892  C  CA    . PHE A 1 487 ? 144.706 131.429 83.273  1.00 25.80 ? 487 PHE A CA    1 
ATOM   3893  C  C     . PHE A 1 487 ? 144.547 132.200 84.571  1.00 25.21 ? 487 PHE A C     1 
ATOM   3894  O  O     . PHE A 1 487 ? 144.261 133.399 84.551  1.00 30.97 ? 487 PHE A O     1 
ATOM   3895  C  CB    . PHE A 1 487 ? 143.418 130.665 82.978  1.00 26.81 ? 487 PHE A CB    1 
ATOM   3896  C  CG    . PHE A 1 487 ? 142.183 131.441 83.342  1.00 29.87 ? 487 PHE A CG    1 
ATOM   3897  C  CD1   . PHE A 1 487 ? 141.747 132.480 82.540  1.00 26.76 ? 487 PHE A CD1   1 
ATOM   3898  C  CD2   . PHE A 1 487 ? 141.484 131.162 84.505  1.00 25.98 ? 487 PHE A CD2   1 
ATOM   3899  C  CE1   . PHE A 1 487 ? 140.630 133.212 82.877  1.00 27.75 ? 487 PHE A CE1   1 
ATOM   3900  C  CE2   . PHE A 1 487 ? 140.366 131.894 84.847  1.00 24.55 ? 487 PHE A CE2   1 
ATOM   3901  C  CZ    . PHE A 1 487 ? 139.940 132.919 84.030  1.00 28.63 ? 487 PHE A CZ    1 
ATOM   3902  N  N     . ALA A 1 488 ? 144.689 131.520 85.710  1.00 25.96 ? 488 ALA A N     1 
ATOM   3903  C  CA    . ALA A 1 488 ? 144.559 132.202 86.991  1.00 21.07 ? 488 ALA A CA    1 
ATOM   3904  C  C     . ALA A 1 488 ? 145.621 133.281 87.140  1.00 28.95 ? 488 ALA A C     1 
ATOM   3905  O  O     . ALA A 1 488 ? 145.329 134.391 87.599  1.00 35.80 ? 488 ALA A O     1 
ATOM   3906  C  CB    . ALA A 1 488 ? 144.647 131.194 88.134  1.00 18.94 ? 488 ALA A CB    1 
ATOM   3907  N  N     . ASN A 1 489 ? 146.854 132.979 86.732  1.00 28.82 ? 489 ASN A N     1 
ATOM   3908  C  CA    . ASN A 1 489 ? 147.926 133.965 86.775  1.00 21.55 ? 489 ASN A CA    1 
ATOM   3909  C  C     . ASN A 1 489 ? 147.561 135.204 85.972  1.00 20.46 ? 489 ASN A C     1 
ATOM   3910  O  O     . ASN A 1 489 ? 147.597 136.325 86.491  1.00 30.10 ? 489 ASN A O     1 
ATOM   3911  C  CB    . ASN A 1 489 ? 149.217 133.339 86.247  1.00 22.65 ? 489 ASN A CB    1 
ATOM   3912  C  CG    . ASN A 1 489 ? 150.453 134.082 86.696  1.00 30.09 ? 489 ASN A CG    1 
ATOM   3913  O  OD1   . ASN A 1 489 ? 150.584 134.445 87.863  1.00 36.96 ? 489 ASN A OD1   1 
ATOM   3914  N  ND2   . ASN A 1 489 ? 151.377 134.301 85.770  1.00 29.04 ? 489 ASN A ND2   1 
ATOM   3915  N  N     . THR A 1 490 ? 147.175 135.018 84.707  1.00 26.54 ? 490 THR A N     1 
ATOM   3916  C  CA    . THR A 1 490 ? 146.858 136.172 83.868  1.00 24.86 ? 490 THR A CA    1 
ATOM   3917  C  C     . THR A 1 490 ? 145.644 136.930 84.394  1.00 25.99 ? 490 THR A C     1 
ATOM   3918  O  O     . THR A 1 490 ? 145.661 138.165 84.483  1.00 27.76 ? 490 THR A O     1 
ATOM   3919  C  CB    . THR A 1 490 ? 146.623 135.727 82.426  1.00 27.03 ? 490 THR A CB    1 
ATOM   3920  O  OG1   . THR A 1 490 ? 147.745 134.959 81.977  1.00 31.63 ? 490 THR A OG1   1 
ATOM   3921  C  CG2   . THR A 1 490 ? 146.448 136.936 81.519  1.00 26.39 ? 490 THR A CG2   1 
ATOM   3922  N  N     . PHE A 1 491 ? 144.588 136.204 84.765  1.00 21.53 ? 491 PHE A N     1 
ATOM   3923  C  CA    . PHE A 1 491 ? 143.349 136.835 85.201  1.00 18.55 ? 491 PHE A CA    1 
ATOM   3924  C  C     . PHE A 1 491 ? 143.564 137.657 86.461  1.00 25.90 ? 491 PHE A C     1 
ATOM   3925  O  O     . PHE A 1 491 ? 143.130 138.810 86.545  1.00 27.54 ? 491 PHE A O     1 
ATOM   3926  C  CB    . PHE A 1 491 ? 142.280 135.766 85.434  1.00 24.64 ? 491 PHE A CB    1 
ATOM   3927  C  CG    . PHE A 1 491 ? 140.985 136.307 85.967  1.00 22.07 ? 491 PHE A CG    1 
ATOM   3928  C  CD1   . PHE A 1 491 ? 140.022 136.797 85.105  1.00 18.09 ? 491 PHE A CD1   1 
ATOM   3929  C  CD2   . PHE A 1 491 ? 140.731 136.330 87.327  1.00 18.26 ? 491 PHE A CD2   1 
ATOM   3930  C  CE1   . PHE A 1 491 ? 138.834 137.299 85.586  1.00 15.30 ? 491 PHE A CE1   1 
ATOM   3931  C  CE2   . PHE A 1 491 ? 139.547 136.834 87.814  1.00 18.25 ? 491 PHE A CE2   1 
ATOM   3932  C  CZ    . PHE A 1 491 ? 138.595 137.317 86.942  1.00 19.72 ? 491 PHE A CZ    1 
ATOM   3933  N  N     . PHE A 1 492 ? 144.240 137.084 87.456  1.00 20.22 ? 492 PHE A N     1 
ATOM   3934  C  CA    . PHE A 1 492 ? 144.415 137.798 88.707  1.00 12.89 ? 492 PHE A CA    1 
ATOM   3935  C  C     . PHE A 1 492 ? 145.504 138.856 88.629  1.00 12.20 ? 492 PHE A C     1 
ATOM   3936  O  O     . PHE A 1 492 ? 145.429 139.843 89.364  1.00 22.35 ? 492 PHE A O     1 
ATOM   3937  C  CB    . PHE A 1 492 ? 144.680 136.805 89.836  1.00 19.73 ? 492 PHE A CB    1 
ATOM   3938  C  CG    . PHE A 1 492 ? 143.452 136.054 90.259  1.00 16.48 ? 492 PHE A CG    1 
ATOM   3939  C  CD1   . PHE A 1 492 ? 142.506 136.654 91.069  1.00 16.24 ? 492 PHE A CD1   1 
ATOM   3940  C  CD2   . PHE A 1 492 ? 143.224 134.765 89.814  1.00 21.85 ? 492 PHE A CD2   1 
ATOM   3941  C  CE1   . PHE A 1 492 ? 141.367 135.972 91.447  1.00 15.21 ? 492 PHE A CE1   1 
ATOM   3942  C  CE2   . PHE A 1 492 ? 142.088 134.079 90.188  1.00 16.36 ? 492 PHE A CE2   1 
ATOM   3943  C  CZ    . PHE A 1 492 ? 141.160 134.682 91.005  1.00 15.92 ? 492 PHE A CZ    1 
ATOM   3944  N  N     . MET A 1 493 ? 146.480 138.715 87.726  1.00 12.75 ? 493 MET A N     1 
ATOM   3945  C  CA    . MET A 1 493 ? 147.374 139.835 87.462  1.00 22.11 ? 493 MET A CA    1 
ATOM   3946  C  C     . MET A 1 493 ? 146.599 141.002 86.873  1.00 18.70 ? 493 MET A C     1 
ATOM   3947  O  O     . MET A 1 493 ? 146.826 142.157 87.246  1.00 28.63 ? 493 MET A O     1 
ATOM   3948  C  CB    . MET A 1 493 ? 148.509 139.402 86.528  1.00 24.56 ? 493 MET A CB    1 
ATOM   3949  C  CG    . MET A 1 493 ? 149.304 140.540 85.874  1.00 19.44 ? 493 MET A CG    1 
ATOM   3950  S  SD    . MET A 1 493 ? 148.566 141.313 84.418  1.00 34.48 ? 493 MET A SD    1 
ATOM   3951  C  CE    . MET A 1 493 ? 148.619 139.960 83.252  1.00 28.68 ? 493 MET A CE    1 
ATOM   3952  N  N     . MET A 1 494 ? 145.675 140.721 85.950  1.00 21.20 ? 494 MET A N     1 
ATOM   3953  C  CA    . MET A 1 494 ? 144.874 141.791 85.363  1.00 17.37 ? 494 MET A CA    1 
ATOM   3954  C  C     . MET A 1 494 ? 143.964 142.426 86.406  1.00 19.78 ? 494 MET A C     1 
ATOM   3955  O  O     . MET A 1 494 ? 143.788 143.652 86.429  1.00 31.53 ? 494 MET A O     1 
ATOM   3956  C  CB    . MET A 1 494 ? 144.056 141.248 84.192  1.00 23.73 ? 494 MET A CB    1 
ATOM   3957  C  CG    . MET A 1 494 ? 144.803 141.280 82.875  1.00 23.24 ? 494 MET A CG    1 
ATOM   3958  S  SD    . MET A 1 494 ? 144.025 140.367 81.534  1.00 41.12 ? 494 MET A SD    1 
ATOM   3959  C  CE    . MET A 1 494 ? 142.586 141.384 81.241  1.00 27.98 ? 494 MET A CE    1 
ATOM   3960  N  N     . VAL A 1 495 ? 143.376 141.602 87.274  1.00 22.94 ? 495 VAL A N     1 
ATOM   3961  C  CA    . VAL A 1 495 ? 142.534 142.118 88.349  1.00 13.48 ? 495 VAL A CA    1 
ATOM   3962  C  C     . VAL A 1 495 ? 143.345 143.013 89.275  1.00 19.65 ? 495 VAL A C     1 
ATOM   3963  O  O     . VAL A 1 495 ? 142.892 144.093 89.669  1.00 28.27 ? 495 VAL A O     1 
ATOM   3964  C  CB    . VAL A 1 495 ? 141.874 140.957 89.115  1.00 15.28 ? 495 VAL A CB    1 
ATOM   3965  C  CG1   . VAL A 1 495 ? 141.271 141.450 90.420  1.00 11.60 ? 495 VAL A CG1   1 
ATOM   3966  C  CG2   . VAL A 1 495 ? 140.817 140.293 88.256  1.00 17.77 ? 495 VAL A CG2   1 
ATOM   3967  N  N     . ASN A 1 496 ? 144.557 142.582 89.636  1.00 22.70 ? 496 ASN A N     1 
ATOM   3968  C  CA    . ASN A 1 496 ? 145.421 143.408 90.473  1.00 16.03 ? 496 ASN A CA    1 
ATOM   3969  C  C     . ASN A 1 496 ? 145.783 144.711 89.775  1.00 17.94 ? 496 ASN A C     1 
ATOM   3970  O  O     . ASN A 1 496 ? 145.772 145.779 90.396  1.00 22.82 ? 496 ASN A O     1 
ATOM   3971  C  CB    . ASN A 1 496 ? 146.684 142.630 90.843  1.00 19.77 ? 496 ASN A CB    1 
ATOM   3972  C  CG    . ASN A 1 496 ? 147.404 143.222 92.032  1.00 18.63 ? 496 ASN A CG    1 
ATOM   3973  O  OD1   . ASN A 1 496 ? 146.778 143.731 92.959  1.00 26.03 ? 496 ASN A OD1   1 
ATOM   3974  N  ND2   . ASN A 1 496 ? 148.727 143.157 92.014  1.00 18.43 ? 496 ASN A ND2   1 
ATOM   3975  N  N     . PHE A 1 497 ? 146.101 144.641 88.481  1.00 21.19 ? 497 PHE A N     1 
ATOM   3976  C  CA    . PHE A 1 497 ? 146.447 145.839 87.724  1.00 16.31 ? 497 PHE A CA    1 
ATOM   3977  C  C     . PHE A 1 497 ? 145.311 146.847 87.753  1.00 24.63 ? 497 PHE A C     1 
ATOM   3978  O  O     . PHE A 1 497 ? 145.517 148.029 88.052  1.00 29.39 ? 497 PHE A O     1 
ATOM   3979  C  CB    . PHE A 1 497 ? 146.785 145.460 86.281  1.00 18.39 ? 497 PHE A CB    1 
ATOM   3980  C  CG    . PHE A 1 497 ? 147.158 146.629 85.415  1.00 20.13 ? 497 PHE A CG    1 
ATOM   3981  C  CD1   . PHE A 1 497 ? 148.470 147.059 85.338  1.00 23.83 ? 497 PHE A CD1   1 
ATOM   3982  C  CD2   . PHE A 1 497 ? 146.198 147.295 84.672  1.00 21.42 ? 497 PHE A CD2   1 
ATOM   3983  C  CE1   . PHE A 1 497 ? 148.815 148.131 84.541  1.00 25.09 ? 497 PHE A CE1   1 
ATOM   3984  C  CE2   . PHE A 1 497 ? 146.538 148.367 83.876  1.00 22.93 ? 497 PHE A CE2   1 
ATOM   3985  C  CZ    . PHE A 1 497 ? 147.849 148.785 83.810  1.00 25.35 ? 497 PHE A CZ    1 
ATOM   3986  N  N     . TYR A 1 498 ? 144.094 146.393 87.462  1.00 26.86 ? 498 TYR A N     1 
ATOM   3987  C  CA    . TYR A 1 498 ? 142.978 147.325 87.385  1.00 18.64 ? 498 TYR A CA    1 
ATOM   3988  C  C     . TYR A 1 498 ? 142.511 147.783 88.760  1.00 22.48 ? 498 TYR A C     1 
ATOM   3989  O  O     . TYR A 1 498 ? 142.038 148.913 88.895  1.00 26.42 ? 498 TYR A O     1 
ATOM   3990  C  CB    . TYR A 1 498 ? 141.838 146.702 86.583  1.00 20.25 ? 498 TYR A CB    1 
ATOM   3991  C  CG    . TYR A 1 498 ? 142.171 146.625 85.113  1.00 25.25 ? 498 TYR A CG    1 
ATOM   3992  C  CD1   . TYR A 1 498 ? 142.458 147.774 84.391  1.00 25.55 ? 498 TYR A CD1   1 
ATOM   3993  C  CD2   . TYR A 1 498 ? 142.220 145.407 84.451  1.00 26.39 ? 498 TYR A CD2   1 
ATOM   3994  C  CE1   . TYR A 1 498 ? 142.775 147.715 83.052  1.00 26.21 ? 498 TYR A CE1   1 
ATOM   3995  C  CE2   . TYR A 1 498 ? 142.534 145.338 83.110  1.00 25.22 ? 498 TYR A CE2   1 
ATOM   3996  C  CZ    . TYR A 1 498 ? 142.810 146.496 82.415  1.00 30.10 ? 498 TYR A CZ    1 
ATOM   3997  O  OH    . TYR A 1 498 ? 143.124 146.438 81.078  1.00 32.47 ? 498 TYR A OH    1 
ATOM   3998  N  N     . SER A 1 499 ? 142.670 146.956 89.796  1.00 23.69 ? 499 SER A N     1 
ATOM   3999  C  CA    . SER A 1 499 ? 142.362 147.412 91.146  1.00 16.03 ? 499 SER A CA    1 
ATOM   4000  C  C     . SER A 1 499 ? 143.350 148.476 91.606  1.00 19.50 ? 499 SER A C     1 
ATOM   4001  O  O     . SER A 1 499 ? 142.954 149.471 92.223  1.00 30.12 ? 499 SER A O     1 
ATOM   4002  C  CB    . SER A 1 499 ? 142.349 146.230 92.115  1.00 15.15 ? 499 SER A CB    1 
ATOM   4003  O  OG    . SER A 1 499 ? 143.656 145.743 92.352  1.00 24.19 ? 499 SER A OG    1 
ATOM   4004  N  N     . ILE A 1 500 ? 144.639 148.292 91.309  1.00 17.74 ? 500 ILE A N     1 
ATOM   4005  C  CA    . ILE A 1 500 ? 145.631 149.310 91.638  1.00 19.58 ? 500 ILE A CA    1 
ATOM   4006  C  C     . ILE A 1 500 ? 145.361 150.585 90.852  1.00 17.76 ? 500 ILE A C     1 
ATOM   4007  O  O     . ILE A 1 500 ? 145.468 151.696 91.386  1.00 26.77 ? 500 ILE A O     1 
ATOM   4008  C  CB    . ILE A 1 500 ? 147.054 148.776 91.385  1.00 23.45 ? 500 ILE A CB    1 
ATOM   4009  C  CG1   . ILE A 1 500 ? 147.400 147.674 92.382  1.00 18.99 ? 500 ILE A CG1   1 
ATOM   4010  C  CG2   . ILE A 1 500 ? 148.072 149.891 91.488  1.00 20.54 ? 500 ILE A CG2   1 
ATOM   4011  C  CD1   . ILE A 1 500 ? 148.570 146.833 91.959  1.00 19.64 ? 500 ILE A CD1   1 
ATOM   4012  N  N     . GLN A 1 501 ? 145.001 150.447 89.574  1.00 24.29 ? 501 GLN A N     1 
ATOM   4013  C  CA    . GLN A 1 501 ? 144.684 151.617 88.762  1.00 22.63 ? 501 GLN A CA    1 
ATOM   4014  C  C     . GLN A 1 501 ? 143.481 152.368 89.315  1.00 28.25 ? 501 GLN A C     1 
ATOM   4015  O  O     . GLN A 1 501 ? 143.496 153.600 89.399  1.00 34.14 ? 501 GLN A O     1 
ATOM   4016  C  CB    . GLN A 1 501 ? 144.432 151.194 87.316  1.00 25.08 ? 501 GLN A CB    1 
ATOM   4017  C  CG    . GLN A 1 501 ? 144.932 152.185 86.287  1.00 24.81 ? 501 GLN A CG    1 
ATOM   4018  C  CD    . GLN A 1 501 ? 144.652 151.738 84.870  1.00 29.15 ? 501 GLN A CD    1 
ATOM   4019  O  OE1   . GLN A 1 501 ? 143.500 151.549 84.483  1.00 28.82 ? 501 GLN A OE1   1 
ATOM   4020  N  NE2   . GLN A 1 501 ? 145.708 151.563 84.087  1.00 33.49 ? 501 GLN A NE2   1 
ATOM   4021  N  N     . ARG A 1 502 ? 142.428 151.644 89.700  1.00 29.28 ? 502 ARG A N     1 
ATOM   4022  C  CA    . ARG A 1 502 ? 141.252 152.295 90.263  1.00 20.98 ? 502 ARG A CA    1 
ATOM   4023  C  C     . ARG A 1 502 ? 141.566 152.948 91.602  1.00 18.94 ? 502 ARG A C     1 
ATOM   4024  O  O     . ARG A 1 502 ? 141.071 154.041 91.891  1.00 29.88 ? 502 ARG A O     1 
ATOM   4025  C  CB    . ARG A 1 502 ? 140.111 151.290 90.409  1.00 23.83 ? 502 ARG A CB    1 
ATOM   4026  C  CG    . ARG A 1 502 ? 138.760 151.934 90.656  1.00 27.10 ? 502 ARG A CG    1 
ATOM   4027  C  CD    . ARG A 1 502 ? 138.478 153.033 89.649  1.00 27.76 ? 502 ARG A CD    1 
ATOM   4028  N  NE    . ARG A 1 502 ? 137.379 153.888 90.080  1.00 25.60 ? 502 ARG A NE    1 
ATOM   4029  C  CZ    . ARG A 1 502 ? 137.334 155.200 89.894  1.00 28.28 ? 502 ARG A CZ    1 
ATOM   4030  N  NH1   . ARG A 1 502 ? 138.310 155.843 89.276  1.00 32.45 ? 502 ARG A NH1   1 
ATOM   4031  N  NH2   . ARG A 1 502 ? 136.284 155.882 90.340  1.00 30.40 ? 502 ARG A NH2   1 
ATOM   4032  N  N     . SER A 1 503 ? 142.379 152.295 92.435  1.00 19.48 ? 503 SER A N     1 
ATOM   4033  C  CA    . SER A 1 503 ? 142.761 152.892 93.710  1.00 24.44 ? 503 SER A CA    1 
ATOM   4034  C  C     . SER A 1 503 ? 143.552 154.177 93.499  1.00 25.54 ? 503 SER A C     1 
ATOM   4035  O  O     . SER A 1 503 ? 143.318 155.181 94.183  1.00 27.70 ? 503 SER A O     1 
ATOM   4036  C  CB    . SER A 1 503 ? 143.567 151.887 94.532  1.00 19.63 ? 503 SER A CB    1 
ATOM   4037  O  OG    . SER A 1 503 ? 143.509 152.190 95.912  1.00 24.01 ? 503 SER A OG    1 
ATOM   4038  N  N     . ALA A 1 504 ? 144.482 154.168 92.542  1.00 28.12 ? 504 ALA A N     1 
ATOM   4039  C  CA    . ALA A 1 504 ? 145.254 155.367 92.241  1.00 26.18 ? 504 ALA A CA    1 
ATOM   4040  C  C     . ALA A 1 504 ? 144.370 156.470 91.674  1.00 30.34 ? 504 ALA A C     1 
ATOM   4041  O  O     . ALA A 1 504 ? 144.550 157.647 92.005  1.00 37.61 ? 504 ALA A O     1 
ATOM   4042  C  CB    . ALA A 1 504 ? 146.385 155.028 91.273  1.00 27.98 ? 504 ALA A CB    1 
ATOM   4043  N  N     . GLU A 1 505 ? 143.410 156.113 90.819  1.00 29.58 ? 505 GLU A N     1 
ATOM   4044  C  CA    . GLU A 1 505 ? 142.495 157.109 90.272  1.00 30.12 ? 505 GLU A CA    1 
ATOM   4045  C  C     . GLU A 1 505 ? 141.609 157.705 91.358  1.00 31.29 ? 505 GLU A C     1 
ATOM   4046  O  O     . GLU A 1 505 ? 141.340 158.910 91.353  1.00 36.03 ? 505 GLU A O     1 
ATOM   4047  C  CB    . GLU A 1 505 ? 141.645 156.487 89.166  1.00 29.80 ? 505 GLU A CB    1 
ATOM   4048  C  CG    . GLU A 1 505 ? 142.408 156.203 87.886  1.00 33.25 ? 505 GLU A CG    1 
ATOM   4049  C  CD    . GLU A 1 505 ? 141.775 155.100 87.062  1.00 36.60 ? 505 GLU A CD    1 
ATOM   4050  O  OE1   . GLU A 1 505 ? 140.706 154.594 87.461  1.00 37.45 ? 505 GLU A OE1   1 
ATOM   4051  O  OE2   . GLU A 1 505 ? 142.348 154.737 86.013  1.00 39.82 ? 505 GLU A OE2   1 
ATOM   4052  N  N     . ILE A 1 506 ? 141.143 156.878 92.295  1.00 28.96 ? 506 ILE A N     1 
ATOM   4053  C  CA    . ILE A 1 506 ? 140.345 157.383 93.407  1.00 26.46 ? 506 ILE A CA    1 
ATOM   4054  C  C     . ILE A 1 506 ? 141.178 158.308 94.283  1.00 28.58 ? 506 ILE A C     1 
ATOM   4055  O  O     . ILE A 1 506 ? 140.701 159.358 94.729  1.00 37.57 ? 506 ILE A O     1 
ATOM   4056  C  CB    . ILE A 1 506 ? 139.752 156.213 94.214  1.00 26.55 ? 506 ILE A CB    1 
ATOM   4057  C  CG1   . ILE A 1 506 ? 138.692 155.479 93.394  1.00 29.05 ? 506 ILE A CG1   1 
ATOM   4058  C  CG2   . ILE A 1 506 ? 139.148 156.708 95.515  1.00 27.10 ? 506 ILE A CG2   1 
ATOM   4059  C  CD1   . ILE A 1 506 ? 138.310 154.133 93.962  1.00 23.34 ? 506 ILE A CD1   1 
ATOM   4060  N  N     . ALA A 1 507 ? 142.434 157.938 94.545  1.00 31.80 ? 507 ALA A N     1 
ATOM   4061  C  CA    . ALA A 1 507 ? 143.311 158.807 95.323  1.00 29.69 ? 507 ALA A CA    1 
ATOM   4062  C  C     . ALA A 1 507 ? 143.545 160.134 94.612  1.00 30.79 ? 507 ALA A C     1 
ATOM   4063  O  O     . ALA A 1 507 ? 143.567 161.193 95.250  1.00 34.61 ? 507 ALA A O     1 
ATOM   4064  C  CB    . ALA A 1 507 ? 144.637 158.101 95.598  1.00 25.56 ? 507 ALA A CB    1 
ATOM   4065  N  N     . LYS A 1 508 ? 143.729 160.097 93.291  1.00 36.48 ? 508 LYS A N     1 
ATOM   4066  C  CA    . LYS A 1 508 ? 143.923 161.326 92.528  1.00 34.22 ? 508 LYS A CA    1 
ATOM   4067  C  C     . LYS A 1 508 ? 142.674 162.200 92.549  1.00 38.41 ? 508 LYS A C     1 
ATOM   4068  O  O     . LYS A 1 508 ? 142.770 163.425 92.690  1.00 43.89 ? 508 LYS A O     1 
ATOM   4069  C  CB    . LYS A 1 508 ? 144.316 160.988 91.091  1.00 36.81 ? 508 LYS A CB    1 
ATOM   4070  C  CG    . LYS A 1 508 ? 144.327 162.178 90.150  1.00 40.29 ? 508 LYS A CG    1 
ATOM   4071  C  CD    . LYS A 1 508 ? 144.358 161.733 88.698  1.00 39.60 ? 508 LYS A CD    1 
ATOM   4072  C  CE    . LYS A 1 508 ? 144.623 162.904 87.769  1.00 39.20 ? 508 LYS A CE    1 
ATOM   4073  N  NZ    . LYS A 1 508 ? 145.467 162.511 86.609  1.00 42.36 ? 508 LYS A NZ    1 
ATOM   4074  N  N     . GLU A 1 509 ? 141.496 161.591 92.407  1.00 35.84 ? 509 GLU A N     1 
ATOM   4075  C  CA    . GLU A 1 509 ? 140.256 162.360 92.381  1.00 36.69 ? 509 GLU A CA    1 
ATOM   4076  C  C     . GLU A 1 509 ? 139.960 162.974 93.743  1.00 39.75 ? 509 GLU A C     1 
ATOM   4077  O  O     . GLU A 1 509 ? 139.652 164.167 93.844  1.00 43.99 ? 509 GLU A O     1 
ATOM   4078  C  CB    . GLU A 1 509 ? 139.099 161.469 91.929  1.00 36.97 ? 509 GLU A CB    1 
ATOM   4079  C  CG    . GLU A 1 509 ? 139.100 161.151 90.444  1.00 43.07 ? 509 GLU A CG    1 
ATOM   4080  C  CD    . GLU A 1 509 ? 138.317 159.893 90.117  1.00 45.10 ? 509 GLU A CD    1 
ATOM   4081  O  OE1   . GLU A 1 509 ? 137.656 159.349 91.027  1.00 43.20 ? 509 GLU A OE1   1 
ATOM   4082  O  OE2   . GLU A 1 509 ? 138.361 159.449 88.951  1.00 42.26 ? 509 GLU A OE2   1 
ATOM   4083  N  N     . LYS A 1 510 ? 140.048 162.173 94.804  1.00 36.90 ? 510 LYS A N     1 
ATOM   4084  C  CA    . LYS A 1 510 ? 139.774 162.656 96.149  1.00 32.46 ? 510 LYS A CA    1 
ATOM   4085  C  C     . LYS A 1 510 ? 140.955 163.388 96.767  1.00 34.29 ? 510 LYS A C     1 
ATOM   4086  O  O     . LYS A 1 510 ? 140.801 163.980 97.841  1.00 40.57 ? 510 LYS A O     1 
ATOM   4087  C  CB    . LYS A 1 510 ? 139.362 161.489 97.048  1.00 30.96 ? 510 LYS A CB    1 
ATOM   4088  C  CG    . LYS A 1 510 ? 138.256 160.633 96.461  1.00 33.71 ? 510 LYS A CG    1 
ATOM   4089  C  CD    . LYS A 1 510 ? 137.621 159.737 97.508  1.00 33.63 ? 510 LYS A CD    1 
ATOM   4090  C  CE    . LYS A 1 510 ? 136.501 158.911 96.901  1.00 36.37 ? 510 LYS A CE    1 
ATOM   4091  N  NZ    . LYS A 1 510 ? 135.434 158.599 97.887  1.00 34.72 ? 510 LYS A NZ    1 
ATOM   4092  N  N     . GLY A 1 511 ? 142.120 163.363 96.125  1.00 37.37 ? 511 GLY A N     1 
ATOM   4093  C  CA    . GLY A 1 511 ? 143.278 164.067 96.632  1.00 37.28 ? 511 GLY A CA    1 
ATOM   4094  C  C     . GLY A 1 511 ? 143.852 163.520 97.916  1.00 41.19 ? 511 GLY A C     1 
ATOM   4095  O  O     . GLY A 1 511 ? 144.702 164.177 98.524  1.00 43.03 ? 511 GLY A O     1 
ATOM   4096  N  N     . GLU A 1 512 ? 143.419 162.340 98.352  1.00 34.04 ? 512 GLU A N     1 
ATOM   4097  C  CA    . GLU A 1 512 ? 143.901 161.745 99.586  1.00 29.80 ? 512 GLU A CA    1 
ATOM   4098  C  C     . GLU A 1 512 ? 144.227 160.276 99.364  1.00 29.69 ? 512 GLU A C     1 
ATOM   4099  O  O     . GLU A 1 512 ? 143.584 159.591 98.564  1.00 33.43 ? 512 GLU A O     1 
ATOM   4100  C  CB    . GLU A 1 512 ? 142.875 161.887 100.718 1.00 32.09 ? 512 GLU A CB    1 
ATOM   4101  C  CG    . GLU A 1 512 ? 141.530 161.248 100.430 1.00 32.12 ? 512 GLU A CG    1 
ATOM   4102  C  CD    . GLU A 1 512 ? 140.823 160.796 101.690 1.00 36.11 ? 512 GLU A CD    1 
ATOM   4103  O  OE1   . GLU A 1 512 ? 141.518 160.456 102.669 1.00 36.05 ? 512 GLU A OE1   1 
ATOM   4104  O  OE2   . GLU A 1 512 ? 139.574 160.780 101.702 1.00 35.52 ? 512 GLU A OE2   1 
ATOM   4105  N  N     . THR A 1 513 ? 145.238 159.804 100.081 1.00 29.58 ? 513 THR A N     1 
ATOM   4106  C  CA    . THR A 1 513 ? 145.641 158.408 100.099 1.00 26.01 ? 513 THR A CA    1 
ATOM   4107  C  C     . THR A 1 513 ? 145.288 157.804 101.454 1.00 27.48 ? 513 THR A C     1 
ATOM   4108  O  O     . THR A 1 513 ? 144.799 158.489 102.357 1.00 37.51 ? 513 THR A O     1 
ATOM   4109  C  CB    . THR A 1 513 ? 147.138 158.278 99.810  1.00 25.01 ? 513 THR A CB    1 
ATOM   4110  O  OG1   . THR A 1 513 ? 147.879 159.002 100.798 1.00 29.23 ? 513 THR A OG1   1 
ATOM   4111  C  CG2   . THR A 1 513 ? 147.464 158.833 98.438  1.00 24.07 ? 513 THR A CG2   1 
ATOM   4112  N  N     . PHE A 1 514 ? 145.531 156.505 101.598 1.00 22.35 ? 514 PHE A N     1 
ATOM   4113  C  CA    . PHE A 1 514 ? 145.318 155.888 102.896 1.00 25.42 ? 514 PHE A CA    1 
ATOM   4114  C  C     . PHE A 1 514 ? 146.428 156.300 103.859 1.00 26.18 ? 514 PHE A C     1 
ATOM   4115  O  O     . PHE A 1 514 ? 147.530 156.680 103.454 1.00 28.31 ? 514 PHE A O     1 
ATOM   4116  C  CB    . PHE A 1 514 ? 145.226 154.364 102.773 1.00 17.87 ? 514 PHE A CB    1 
ATOM   4117  C  CG    . PHE A 1 514 ? 146.511 153.693 102.378 1.00 19.57 ? 514 PHE A CG    1 
ATOM   4118  C  CD1   . PHE A 1 514 ? 146.828 153.508 101.045 1.00 18.07 ? 514 PHE A CD1   1 
ATOM   4119  C  CD2   . PHE A 1 514 ? 147.385 153.213 103.339 1.00 22.33 ? 514 PHE A CD2   1 
ATOM   4120  C  CE1   . PHE A 1 514 ? 147.999 152.878 100.680 1.00 18.75 ? 514 PHE A CE1   1 
ATOM   4121  C  CE2   . PHE A 1 514 ? 148.557 152.583 102.977 1.00 17.58 ? 514 PHE A CE2   1 
ATOM   4122  C  CZ    . PHE A 1 514 ? 148.863 152.417 101.646 1.00 17.88 ? 514 PHE A CZ    1 
ATOM   4123  N  N     . ASP A 1 515 ? 146.114 156.244 105.150 1.00 29.43 ? 515 ASP A N     1 
ATOM   4124  C  CA    . ASP A 1 515 ? 147.040 156.724 106.166 1.00 27.53 ? 515 ASP A CA    1 
ATOM   4125  C  C     . ASP A 1 515 ? 148.346 155.943 106.124 1.00 29.91 ? 515 ASP A C     1 
ATOM   4126  O  O     . ASP A 1 515 ? 148.353 154.716 105.996 1.00 36.02 ? 515 ASP A O     1 
ATOM   4127  C  CB    . ASP A 1 515 ? 146.407 156.618 107.553 1.00 30.32 ? 515 ASP A CB    1 
ATOM   4128  C  CG    . ASP A 1 515 ? 145.505 157.792 107.870 1.00 38.50 ? 515 ASP A CG    1 
ATOM   4129  O  OD1   . ASP A 1 515 ? 145.024 158.448 106.922 1.00 37.71 ? 515 ASP A OD1   1 
ATOM   4130  O  OD2   . ASP A 1 515 ? 145.276 158.060 109.068 1.00 39.46 ? 515 ASP A OD2   1 
ATOM   4131  N  N     . GLN A 1 516 ? 149.456 156.674 106.238 1.00 27.97 ? 516 GLN A N     1 
ATOM   4132  C  CA    . GLN A 1 516 ? 150.800 156.103 106.163 1.00 28.56 ? 516 GLN A CA    1 
ATOM   4133  C  C     . GLN A 1 516 ? 151.030 155.390 104.833 1.00 25.41 ? 516 GLN A C     1 
ATOM   4134  O  O     . GLN A 1 516 ? 151.654 154.330 104.775 1.00 32.91 ? 516 GLN A O     1 
ATOM   4135  C  CB    . GLN A 1 516 ? 151.071 155.160 107.338 1.00 25.95 ? 516 GLN A CB    1 
ATOM   4136  C  CG    . GLN A 1 516 ? 150.902 155.798 108.703 1.00 27.76 ? 516 GLN A CG    1 
ATOM   4137  C  CD    . GLN A 1 516 ? 151.152 154.821 109.831 1.00 29.61 ? 516 GLN A CD    1 
ATOM   4138  O  OE1   . GLN A 1 516 ? 152.292 154.443 110.097 1.00 28.81 ? 516 GLN A OE1   1 
ATOM   4139  N  NE2   . GLN A 1 516 ? 150.085 154.406 110.502 1.00 29.64 ? 516 GLN A NE2   1 
ATOM   4140  N  N     . TYR A 1 517 ? 150.514 155.974 103.750 1.00 24.22 ? 517 TYR A N     1 
ATOM   4141  C  CA    . TYR A 1 517 ? 150.776 155.412 102.430 1.00 24.09 ? 517 TYR A CA    1 
ATOM   4142  C  C     . TYR A 1 517 ? 152.230 155.595 102.019 1.00 27.52 ? 517 TYR A C     1 
ATOM   4143  O  O     . TYR A 1 517 ? 152.796 154.723 101.350 1.00 35.31 ? 517 TYR A O     1 
ATOM   4144  C  CB    . TYR A 1 517 ? 149.859 156.044 101.381 1.00 25.19 ? 517 TYR A CB    1 
ATOM   4145  C  CG    . TYR A 1 517 ? 150.451 156.016 99.990  1.00 27.97 ? 517 TYR A CG    1 
ATOM   4146  C  CD1   . TYR A 1 517 ? 150.416 154.859 99.224  1.00 22.15 ? 517 TYR A CD1   1 
ATOM   4147  C  CD2   . TYR A 1 517 ? 151.062 157.141 99.450  1.00 26.57 ? 517 TYR A CD2   1 
ATOM   4148  C  CE1   . TYR A 1 517 ? 150.964 154.823 97.960  1.00 27.86 ? 517 TYR A CE1   1 
ATOM   4149  C  CE2   . TYR A 1 517 ? 151.615 157.112 98.189  1.00 25.62 ? 517 TYR A CE2   1 
ATOM   4150  C  CZ    . TYR A 1 517 ? 151.565 155.951 97.449  1.00 26.78 ? 517 TYR A CZ    1 
ATOM   4151  O  OH    . TYR A 1 517 ? 152.110 155.922 96.188  1.00 35.07 ? 517 TYR A OH    1 
ATOM   4152  N  N     . GLU A 1 518 ? 152.849 156.714 102.405 1.00 30.63 ? 518 GLU A N     1 
ATOM   4153  C  CA    . GLU A 1 518 ? 154.188 157.036 101.925 1.00 33.35 ? 518 GLU A CA    1 
ATOM   4154  C  C     . GLU A 1 518 ? 155.230 156.016 102.365 1.00 35.27 ? 518 GLU A C     1 
ATOM   4155  O  O     . GLU A 1 518 ? 156.268 155.886 101.708 1.00 38.44 ? 518 GLU A O     1 
ATOM   4156  C  CB    . GLU A 1 518 ? 154.591 158.432 102.399 1.00 34.40 ? 518 GLU A CB    1 
ATOM   4157  C  CG    . GLU A 1 518 ? 153.823 159.563 101.730 1.00 36.71 ? 518 GLU A CG    1 
ATOM   4158  C  CD    . GLU A 1 518 ? 154.090 159.661 100.237 1.00 43.38 ? 518 GLU A CD    1 
ATOM   4159  O  OE1   . GLU A 1 518 ? 155.157 159.196 99.783  1.00 39.00 ? 518 GLU A OE1   1 
ATOM   4160  O  OE2   . GLU A 1 518 ? 153.230 160.210 99.517  1.00 40.24 ? 518 GLU A OE2   1 
ATOM   4161  N  N     . GLY A 1 519 ? 154.984 155.295 103.456 1.00 24.09 ? 519 GLY A N     1 
ATOM   4162  C  CA    . GLY A 1 519 ? 155.873 154.232 103.872 1.00 20.46 ? 519 GLY A CA    1 
ATOM   4163  C  C     . GLY A 1 519 ? 155.606 152.884 103.249 1.00 22.44 ? 519 GLY A C     1 
ATOM   4164  O  O     . GLY A 1 519 ? 156.387 151.951 103.457 1.00 32.14 ? 519 GLY A O     1 
ATOM   4165  N  N     . SER A 1 520 ? 154.524 152.755 102.488 1.00 21.53 ? 520 SER A N     1 
ATOM   4166  C  CA    . SER A 1 520 ? 154.146 151.488 101.884 1.00 23.08 ? 520 SER A CA    1 
ATOM   4167  C  C     . SER A 1 520 ? 155.038 151.169 100.688 1.00 22.78 ? 520 SER A C     1 
ATOM   4168  O  O     . SER A 1 520 ? 155.769 152.018 100.173 1.00 28.72 ? 520 SER A O     1 
ATOM   4169  C  CB    . SER A 1 520 ? 152.680 151.519 101.458 1.00 20.19 ? 520 SER A CB    1 
ATOM   4170  O  OG    . SER A 1 520 ? 152.454 152.546 100.510 1.00 20.54 ? 520 SER A OG    1 
ATOM   4171  N  N     . THR A 1 521 ? 154.969 149.913 100.242 1.00 20.70 ? 521 THR A N     1 
ATOM   4172  C  CA    . THR A 1 521 ? 155.747 149.495 99.082  1.00 19.23 ? 521 THR A CA    1 
ATOM   4173  C  C     . THR A 1 521 ? 155.198 150.072 97.785  1.00 25.44 ? 521 THR A C     1 
ATOM   4174  O  O     . THR A 1 521 ? 155.932 150.137 96.794  1.00 28.37 ? 521 THR A O     1 
ATOM   4175  C  CB    . THR A 1 521 ? 155.790 147.971 98.990  1.00 28.34 ? 521 THR A CB    1 
ATOM   4176  O  OG1   . THR A 1 521 ? 154.457 147.453 99.022  1.00 28.13 ? 521 THR A OG1   1 
ATOM   4177  C  CG2   . THR A 1 521 ? 156.572 147.395 100.154 1.00 20.43 ? 521 THR A CG2   1 
ATOM   4178  N  N     . TYR A 1 522 ? 153.926 150.475 97.764  1.00 28.28 ? 522 TYR A N     1 
ATOM   4179  C  CA    . TYR A 1 522 ? 153.400 151.185 96.603  1.00 21.73 ? 522 TYR A CA    1 
ATOM   4180  C  C     . TYR A 1 522 ? 154.110 152.518 96.413  1.00 26.31 ? 522 TYR A C     1 
ATOM   4181  O  O     . TYR A 1 522 ? 154.458 152.891 95.287  1.00 29.40 ? 522 TYR A O     1 
ATOM   4182  C  CB    . TYR A 1 522 ? 151.895 151.408 96.749  1.00 18.74 ? 522 TYR A CB    1 
ATOM   4183  C  CG    . TYR A 1 522 ? 151.087 150.163 97.027  1.00 21.69 ? 522 TYR A CG    1 
ATOM   4184  C  CD1   . TYR A 1 522 ? 150.863 149.220 96.034  1.00 21.01 ? 522 TYR A CD1   1 
ATOM   4185  C  CD2   . TYR A 1 522 ? 150.523 149.944 98.275  1.00 24.15 ? 522 TYR A CD2   1 
ATOM   4186  C  CE1   . TYR A 1 522 ? 150.115 148.087 96.282  1.00 20.07 ? 522 TYR A CE1   1 
ATOM   4187  C  CE2   . TYR A 1 522 ? 149.772 148.817 98.531  1.00 22.72 ? 522 TYR A CE2   1 
ATOM   4188  C  CZ    . TYR A 1 522 ? 149.573 147.890 97.532  1.00 22.98 ? 522 TYR A CZ    1 
ATOM   4189  O  OH    . TYR A 1 522 ? 148.827 146.764 97.784  1.00 27.68 ? 522 TYR A OH    1 
ATOM   4190  N  N     . ALA A 1 523 ? 154.328 153.252 97.507  1.00 28.78 ? 523 ALA A N     1 
ATOM   4191  C  CA    . ALA A 1 523 ? 154.996 154.545 97.414  1.00 26.99 ? 523 ALA A CA    1 
ATOM   4192  C  C     . ALA A 1 523 ? 156.461 154.386 97.032  1.00 28.90 ? 523 ALA A C     1 
ATOM   4193  O  O     . ALA A 1 523 ? 156.983 155.154 96.216  1.00 32.42 ? 523 ALA A O     1 
ATOM   4194  C  CB    . ALA A 1 523 ? 154.863 155.299 98.735  1.00 24.34 ? 523 ALA A CB    1 
ATOM   4195  N  N     . THR A 1 524 ? 157.141 153.394 97.611  1.00 28.61 ? 524 THR A N     1 
ATOM   4196  C  CA    . THR A 1 524 ? 158.543 153.164 97.289  1.00 28.04 ? 524 THR A CA    1 
ATOM   4197  C  C     . THR A 1 524 ? 158.725 152.511 95.926  1.00 31.24 ? 524 THR A C     1 
ATOM   4198  O  O     . THR A 1 524 ? 159.833 152.548 95.380  1.00 36.15 ? 524 THR A O     1 
ATOM   4199  C  CB    . THR A 1 524 ? 159.197 152.299 98.366  1.00 30.43 ? 524 THR A CB    1 
ATOM   4200  O  OG1   . THR A 1 524 ? 158.712 150.955 98.263  1.00 33.09 ? 524 THR A OG1   1 
ATOM   4201  C  CG2   . THR A 1 524 ? 158.881 152.841 99.750  1.00 28.37 ? 524 THR A CG2   1 
ATOM   4202  N  N     . GLY A 1 525 ? 157.671 151.921 95.365  1.00 27.07 ? 525 GLY A N     1 
ATOM   4203  C  CA    . GLY A 1 525 ? 157.754 151.254 94.085  1.00 28.42 ? 525 GLY A CA    1 
ATOM   4204  C  C     . GLY A 1 525 ? 158.258 149.829 94.133  1.00 32.47 ? 525 GLY A C     1 
ATOM   4205  O  O     . GLY A 1 525 ? 158.336 149.184 93.080  1.00 32.82 ? 525 GLY A O     1 
ATOM   4206  N  N     . GLU A 1 526 ? 158.604 149.317 95.315  1.00 32.46 ? 526 GLU A N     1 
ATOM   4207  C  CA    . GLU A 1 526 ? 159.074 147.943 95.434  1.00 33.26 ? 526 GLU A CA    1 
ATOM   4208  C  C     . GLU A 1 526 ? 157.965 146.934 95.161  1.00 36.95 ? 526 GLU A C     1 
ATOM   4209  O  O     . GLU A 1 526 ? 158.253 145.819 94.711  1.00 41.27 ? 526 GLU A O     1 
ATOM   4210  C  CB    . GLU A 1 526 ? 159.681 147.731 96.826  1.00 33.31 ? 526 GLU A CB    1 
ATOM   4211  C  CG    . GLU A 1 526 ? 159.682 146.300 97.332  1.00 33.71 ? 526 GLU A CG    1 
ATOM   4212  C  CD    . GLU A 1 526 ? 159.729 146.219 98.845  1.00 40.85 ? 526 GLU A CD    1 
ATOM   4213  O  OE1   . GLU A 1 526 ? 159.781 147.283 99.495  1.00 44.59 ? 526 GLU A OE1   1 
ATOM   4214  O  OE2   . GLU A 1 526 ? 159.714 145.092 99.383  1.00 38.86 ? 526 GLU A OE2   1 
ATOM   4215  N  N     . TYR A 1 527 ? 156.706 147.314 95.394  1.00 34.07 ? 527 TYR A N     1 
ATOM   4216  C  CA    . TYR A 1 527 ? 155.589 146.413 95.137  1.00 25.60 ? 527 TYR A CA    1 
ATOM   4217  C  C     . TYR A 1 527 ? 155.521 145.993 93.675  1.00 26.75 ? 527 TYR A C     1 
ATOM   4218  O  O     . TYR A 1 527 ? 155.112 144.868 93.371  1.00 29.32 ? 527 TYR A O     1 
ATOM   4219  C  CB    . TYR A 1 527 ? 154.278 147.080 95.558  1.00 22.77 ? 527 TYR A CB    1 
ATOM   4220  C  CG    . TYR A 1 527 ? 153.043 146.244 95.304  1.00 26.86 ? 527 TYR A CG    1 
ATOM   4221  C  CD1   . TYR A 1 527 ? 152.574 145.357 96.262  1.00 23.99 ? 527 TYR A CD1   1 
ATOM   4222  C  CD2   . TYR A 1 527 ? 152.344 146.345 94.108  1.00 27.28 ? 527 TYR A CD2   1 
ATOM   4223  C  CE1   . TYR A 1 527 ? 151.448 144.592 96.034  1.00 25.77 ? 527 TYR A CE1   1 
ATOM   4224  C  CE2   . TYR A 1 527 ? 151.221 145.582 93.872  1.00 25.28 ? 527 TYR A CE2   1 
ATOM   4225  C  CZ    . TYR A 1 527 ? 150.776 144.709 94.838  1.00 19.15 ? 527 TYR A CZ    1 
ATOM   4226  O  OH    . TYR A 1 527 ? 149.654 143.950 94.608  1.00 29.90 ? 527 TYR A OH    1 
ATOM   4227  N  N     . PHE A 1 528 ? 155.917 146.875 92.761  1.00 29.00 ? 528 PHE A N     1 
ATOM   4228  C  CA    . PHE A 1 528 ? 155.760 146.652 91.331  1.00 27.87 ? 528 PHE A CA    1 
ATOM   4229  C  C     . PHE A 1 528 ? 156.962 145.970 90.690  1.00 34.29 ? 528 PHE A C     1 
ATOM   4230  O  O     . PHE A 1 528 ? 157.038 145.919 89.460  1.00 41.89 ? 528 PHE A O     1 
ATOM   4231  C  CB    . PHE A 1 528 ? 155.495 147.981 90.619  1.00 29.30 ? 528 PHE A CB    1 
ATOM   4232  C  CG    . PHE A 1 528 ? 154.293 148.719 91.131  1.00 31.01 ? 528 PHE A CG    1 
ATOM   4233  C  CD1   . PHE A 1 528 ? 154.409 149.623 92.174  1.00 30.22 ? 528 PHE A CD1   1 
ATOM   4234  C  CD2   . PHE A 1 528 ? 153.047 148.519 90.563  1.00 28.75 ? 528 PHE A CD2   1 
ATOM   4235  C  CE1   . PHE A 1 528 ? 153.305 150.306 92.643  1.00 32.43 ? 528 PHE A CE1   1 
ATOM   4236  C  CE2   . PHE A 1 528 ? 151.940 149.200 91.028  1.00 29.85 ? 528 PHE A CE2   1 
ATOM   4237  C  CZ    . PHE A 1 528 ? 152.070 150.093 92.069  1.00 28.53 ? 528 PHE A CZ    1 
ATOM   4238  N  N     . ASP A 1 529 ? 157.900 145.452 91.488  1.00 35.20 ? 529 ASP A N     1 
ATOM   4239  C  CA    . ASP A 1 529 ? 159.132 144.901 90.928  1.00 32.51 ? 529 ASP A CA    1 
ATOM   4240  C  C     . ASP A 1 529 ? 158.849 143.719 90.009  1.00 34.15 ? 529 ASP A C     1 
ATOM   4241  O  O     . ASP A 1 529 ? 159.289 143.695 88.852  1.00 41.52 ? 529 ASP A O     1 
ATOM   4242  C  CB    . ASP A 1 529 ? 160.074 144.486 92.058  1.00 36.13 ? 529 ASP A CB    1 
ATOM   4243  C  CG    . ASP A 1 529 ? 160.795 145.664 92.680  1.00 42.04 ? 529 ASP A CG    1 
ATOM   4244  O  OD1   . ASP A 1 529 ? 160.723 146.774 92.113  1.00 41.16 ? 529 ASP A OD1   1 
ATOM   4245  O  OD2   . ASP A 1 529 ? 161.435 145.479 93.736  1.00 40.79 ? 529 ASP A OD2   1 
ATOM   4246  N  N     . LYS A 1 530 ? 158.104 142.728 90.504  1.00 37.82 ? 530 LYS A N     1 
ATOM   4247  C  CA    . LYS A 1 530 ? 157.797 141.555 89.696  1.00 38.28 ? 530 LYS A CA    1 
ATOM   4248  C  C     . LYS A 1 530 ? 156.857 141.881 88.546  1.00 36.90 ? 530 LYS A C     1 
ATOM   4249  O  O     . LYS A 1 530 ? 156.782 141.112 87.584  1.00 41.12 ? 530 LYS A O     1 
ATOM   4250  C  CB    . LYS A 1 530 ? 157.191 140.455 90.567  1.00 37.73 ? 530 LYS A CB    1 
ATOM   4251  C  CG    . LYS A 1 530 ? 155.675 140.475 90.635  1.00 31.64 ? 530 LYS A CG    1 
ATOM   4252  C  CD    . LYS A 1 530 ? 155.161 139.510 91.685  1.00 34.18 ? 530 LYS A CD    1 
ATOM   4253  C  CE    . LYS A 1 530 ? 153.648 139.447 91.677  1.00 35.75 ? 530 LYS A CE    1 
ATOM   4254  N  NZ    . LYS A 1 530 ? 153.098 139.583 93.051  1.00 39.41 ? 530 LYS A NZ    1 
ATOM   4255  N  N     . TYR A 1 531 ? 156.145 142.999 88.622  1.00 32.42 ? 531 TYR A N     1 
ATOM   4256  C  CA    . TYR A 1 531 ? 155.236 143.391 87.557  1.00 28.27 ? 531 TYR A CA    1 
ATOM   4257  C  C     . TYR A 1 531 ? 155.932 144.169 86.453  1.00 30.25 ? 531 TYR A C     1 
ATOM   4258  O  O     . TYR A 1 531 ? 155.545 144.053 85.285  1.00 36.05 ? 531 TYR A O     1 
ATOM   4259  C  CB    . TYR A 1 531 ? 154.087 144.213 88.137  1.00 25.81 ? 531 TYR A CB    1 
ATOM   4260  C  CG    . TYR A 1 531 ? 153.091 143.382 88.903  1.00 30.64 ? 531 TYR A CG    1 
ATOM   4261  C  CD1   . TYR A 1 531 ? 152.500 142.269 88.322  1.00 29.96 ? 531 TYR A CD1   1 
ATOM   4262  C  CD2   . TYR A 1 531 ? 152.744 143.702 90.207  1.00 27.71 ? 531 TYR A CD2   1 
ATOM   4263  C  CE1   . TYR A 1 531 ? 151.588 141.503 89.015  1.00 32.17 ? 531 TYR A CE1   1 
ATOM   4264  C  CE2   . TYR A 1 531 ? 151.834 142.941 90.908  1.00 26.11 ? 531 TYR A CE2   1 
ATOM   4265  C  CZ    . TYR A 1 531 ? 151.259 141.843 90.307  1.00 29.56 ? 531 TYR A CZ    1 
ATOM   4266  O  OH    . TYR A 1 531 ? 150.350 141.080 90.999  1.00 31.69 ? 531 TYR A OH    1 
ATOM   4267  N  N     . VAL A 1 532 ? 156.953 144.958 86.796  1.00 35.78 ? 532 VAL A N     1 
ATOM   4268  C  CA    . VAL A 1 532 ? 157.752 145.640 85.783  1.00 35.84 ? 532 VAL A CA    1 
ATOM   4269  C  C     . VAL A 1 532 ? 158.872 144.765 85.244  1.00 38.64 ? 532 VAL A C     1 
ATOM   4270  O  O     . VAL A 1 532 ? 159.453 145.095 84.199  1.00 43.70 ? 532 VAL A O     1 
ATOM   4271  C  CB    . VAL A 1 532 ? 158.348 146.953 86.331  1.00 36.79 ? 532 VAL A CB    1 
ATOM   4272  C  CG1   . VAL A 1 532 ? 157.245 147.858 86.854  1.00 33.15 ? 532 VAL A CG1   1 
ATOM   4273  C  CG2   . VAL A 1 532 ? 159.376 146.665 87.414  1.00 36.63 ? 532 VAL A CG2   1 
ATOM   4274  N  N     . SER A 1 533 ? 159.195 143.659 85.915  1.00 37.73 ? 533 SER A N     1 
ATOM   4275  C  CA    . SER A 1 533 ? 160.246 142.759 85.457  1.00 35.99 ? 533 SER A CA    1 
ATOM   4276  C  C     . SER A 1 533 ? 159.714 141.522 84.748  1.00 41.21 ? 533 SER A C     1 
ATOM   4277  O  O     . SER A 1 533 ? 160.296 141.092 83.748  1.00 43.95 ? 533 SER A O     1 
ATOM   4278  C  CB    . SER A 1 533 ? 161.120 142.327 86.638  1.00 40.64 ? 533 SER A CB    1 
ATOM   4279  O  OG    . SER A 1 533 ? 160.547 141.226 87.321  1.00 42.21 ? 533 SER A OG    1 
ATOM   4280  N  N     . THR A 1 534 ? 158.624 140.939 85.237  1.00 43.17 ? 534 THR A N     1 
ATOM   4281  C  CA    . THR A 1 534 ? 158.093 139.689 84.715  1.00 39.07 ? 534 THR A CA    1 
ATOM   4282  C  C     . THR A 1 534 ? 156.801 139.943 83.950  1.00 38.66 ? 534 THR A C     1 
ATOM   4283  O  O     . THR A 1 534 ? 155.927 140.681 84.416  1.00 43.23 ? 534 THR A O     1 
ATOM   4284  C  CB    . THR A 1 534 ? 157.840 138.687 85.849  1.00 37.20 ? 534 THR A CB    1 
ATOM   4285  O  OG1   . THR A 1 534 ? 159.088 138.309 86.442  1.00 43.09 ? 534 THR A OG1   1 
ATOM   4286  C  CG2   . THR A 1 534 ? 157.139 137.442 85.329  1.00 41.08 ? 534 THR A CG2   1 
ATOM   4287  N  N     . ASP A 1 535 ? 156.690 139.335 82.772  1.00 42.39 ? 535 ASP A N     1 
ATOM   4288  C  CA    . ASP A 1 535 ? 155.471 139.395 81.979  1.00 42.10 ? 535 ASP A CA    1 
ATOM   4289  C  C     . ASP A 1 535 ? 154.540 138.267 82.400  1.00 44.86 ? 535 ASP A C     1 
ATOM   4290  O  O     . ASP A 1 535 ? 154.976 137.125 82.573  1.00 45.56 ? 535 ASP A O     1 
ATOM   4291  C  CB    . ASP A 1 535 ? 155.791 139.293 80.488  1.00 42.52 ? 535 ASP A CB    1 
ATOM   4292  C  CG    . ASP A 1 535 ? 154.586 138.897 79.659  1.00 48.09 ? 535 ASP A CG    1 
ATOM   4293  O  OD1   . ASP A 1 535 ? 153.749 139.777 79.365  1.00 48.92 ? 535 ASP A OD1   1 
ATOM   4294  O  OD2   . ASP A 1 535 ? 154.475 137.705 79.303  1.00 47.38 ? 535 ASP A OD2   1 
ATOM   4295  N  N     . PHE A 1 536 ? 153.258 138.590 82.569  1.00 34.31 ? 536 PHE A N     1 
ATOM   4296  C  CA    . PHE A 1 536 ? 152.264 137.625 83.020  1.00 32.55 ? 536 PHE A CA    1 
ATOM   4297  C  C     . PHE A 1 536 ? 151.251 137.288 81.932  1.00 38.52 ? 536 PHE A C     1 
ATOM   4298  O  O     . PHE A 1 536 ? 150.135 136.857 82.239  1.00 41.07 ? 536 PHE A O     1 
ATOM   4299  C  CB    . PHE A 1 536 ? 151.556 138.142 84.273  1.00 33.19 ? 536 PHE A CB    1 
ATOM   4300  C  CG    . PHE A 1 536 ? 152.453 138.248 85.472  1.00 33.52 ? 536 PHE A CG    1 
ATOM   4301  C  CD1   . PHE A 1 536 ? 153.201 139.391 85.695  1.00 32.73 ? 536 PHE A CD1   1 
ATOM   4302  C  CD2   . PHE A 1 536 ? 152.553 137.203 86.373  1.00 28.96 ? 536 PHE A CD2   1 
ATOM   4303  C  CE1   . PHE A 1 536 ? 154.028 139.488 86.795  1.00 34.68 ? 536 PHE A CE1   1 
ATOM   4304  C  CE2   . PHE A 1 536 ? 153.381 137.295 87.474  1.00 28.53 ? 536 PHE A CE2   1 
ATOM   4305  C  CZ    . PHE A 1 536 ? 154.117 138.440 87.686  1.00 32.57 ? 536 PHE A CZ    1 
ATOM   4306  N  N     . SER A 1 537 ? 151.617 137.484 80.669  1.00 40.44 ? 537 SER A N     1 
ATOM   4307  C  CA    . SER A 1 537 ? 150.775 137.058 79.566  1.00 38.48 ? 537 SER A CA    1 
ATOM   4308  C  C     . SER A 1 537 ? 150.664 135.534 79.559  1.00 39.81 ? 537 SER A C     1 
ATOM   4309  O  O     . SER A 1 537 ? 151.592 134.838 79.979  1.00 43.43 ? 537 SER A O     1 
ATOM   4310  C  CB    . SER A 1 537 ? 151.355 137.553 78.243  1.00 38.87 ? 537 SER A CB    1 
ATOM   4311  O  OG    . SER A 1 537 ? 150.485 137.297 77.155  1.00 46.76 ? 537 SER A OG    1 
ATOM   4312  N  N     . PRO A 1 538 ? 149.531 134.990 79.110  1.00 40.05 ? 538 PRO A N     1 
ATOM   4313  C  CA    . PRO A 1 538 ? 149.367 133.531 79.116  1.00 38.55 ? 538 PRO A CA    1 
ATOM   4314  C  C     . PRO A 1 538 ? 150.434 132.838 78.280  1.00 41.70 ? 538 PRO A C     1 
ATOM   4315  O  O     . PRO A 1 538 ? 150.796 133.295 77.194  1.00 40.49 ? 538 PRO A O     1 
ATOM   4316  C  CB    . PRO A 1 538 ? 147.969 133.329 78.521  1.00 37.53 ? 538 PRO A CB    1 
ATOM   4317  C  CG    . PRO A 1 538 ? 147.268 134.619 78.747  1.00 39.80 ? 538 PRO A CG    1 
ATOM   4318  C  CD    . PRO A 1 538 ? 148.317 135.678 78.639  1.00 36.93 ? 538 PRO A CD    1 
ATOM   4319  N  N     . LYS A 1 539 ? 150.935 131.720 78.803  1.00 43.45 ? 539 LYS A N     1 
ATOM   4320  C  CA    . LYS A 1 539 ? 151.960 130.938 78.128  1.00 42.74 ? 539 LYS A CA    1 
ATOM   4321  C  C     . LYS A 1 539 ? 151.389 129.875 77.201  1.00 44.66 ? 539 LYS A C     1 
ATOM   4322  O  O     . LYS A 1 539 ? 152.149 129.266 76.441  1.00 49.52 ? 539 LYS A O     1 
ATOM   4323  C  CB    . LYS A 1 539 ? 152.877 130.268 79.157  1.00 44.50 ? 539 LYS A CB    1 
ATOM   4324  C  CG    . LYS A 1 539 ? 153.157 131.115 80.385  1.00 46.46 ? 539 LYS A CG    1 
ATOM   4325  C  CD    . LYS A 1 539 ? 154.486 131.842 80.265  1.00 46.59 ? 539 LYS A CD    1 
ATOM   4326  C  CE    . LYS A 1 539 ? 154.580 132.983 81.266  1.00 47.32 ? 539 LYS A CE    1 
ATOM   4327  N  NZ    . LYS A 1 539 ? 153.793 134.172 80.834  1.00 45.14 ? 539 LYS A NZ    1 
ATOM   4328  N  N     . TYR A 1 540 ? 150.082 129.638 77.241  1.00 44.08 ? 540 TYR A N     1 
ATOM   4329  C  CA    . TYR A 1 540 ? 149.435 128.632 76.414  1.00 44.14 ? 540 TYR A CA    1 
ATOM   4330  C  C     . TYR A 1 540 ? 148.492 129.297 75.423  1.00 46.90 ? 540 TYR A C     1 
ATOM   4331  O  O     . TYR A 1 540 ? 147.799 130.262 75.761  1.00 45.86 ? 540 TYR A O     1 
ATOM   4332  C  CB    . TYR A 1 540 ? 148.670 127.618 77.271  1.00 42.75 ? 540 TYR A CB    1 
ATOM   4333  C  CG    . TYR A 1 540 ? 149.531 126.928 78.303  1.00 46.28 ? 540 TYR A CG    1 
ATOM   4334  C  CD1   . TYR A 1 540 ? 150.080 125.679 78.049  1.00 46.08 ? 540 TYR A CD1   1 
ATOM   4335  C  CD2   . TYR A 1 540 ? 149.797 127.522 79.529  1.00 45.86 ? 540 TYR A CD2   1 
ATOM   4336  C  CE1   . TYR A 1 540 ? 150.871 125.043 78.983  1.00 42.66 ? 540 TYR A CE1   1 
ATOM   4337  C  CE2   . TYR A 1 540 ? 150.587 126.893 80.470  1.00 46.68 ? 540 TYR A CE2   1 
ATOM   4338  C  CZ    . TYR A 1 540 ? 151.120 125.654 80.192  1.00 46.46 ? 540 TYR A CZ    1 
ATOM   4339  O  OH    . TYR A 1 540 ? 151.908 125.023 81.125  1.00 45.65 ? 540 TYR A OH    1 
ATOM   4340  N  N     . GLU A 1 541 ? 148.480 128.779 74.192  1.00 49.77 ? 541 GLU A N     1 
ATOM   4341  C  CA    . GLU A 1 541 ? 147.622 129.349 73.160  1.00 47.81 ? 541 GLU A CA    1 
ATOM   4342  C  C     . GLU A 1 541 ? 146.148 129.172 73.494  1.00 49.24 ? 541 GLU A C     1 
ATOM   4343  O  O     . GLU A 1 541 ? 145.324 130.014 73.121  1.00 47.98 ? 541 GLU A O     1 
ATOM   4344  C  CB    . GLU A 1 541 ? 147.952 128.729 71.798  1.00 49.69 ? 541 GLU A CB    1 
ATOM   4345  C  CG    . GLU A 1 541 ? 147.389 127.330 71.565  1.00 52.61 ? 541 GLU A CG    1 
ATOM   4346  C  CD    . GLU A 1 541 ? 148.085 126.265 72.393  1.00 57.95 ? 541 GLU A CD    1 
ATOM   4347  O  OE1   . GLU A 1 541 ? 149.213 126.516 72.868  1.00 55.32 ? 541 GLU A OE1   1 
ATOM   4348  O  OE2   . GLU A 1 541 ? 147.503 125.173 72.569  1.00 52.51 ? 541 GLU A OE2   1 
ATOM   4349  N  N     . LYS A 1 542 ? 145.794 128.090 74.193  1.00 47.57 ? 542 LYS A N     1 
ATOM   4350  C  CA    . LYS A 1 542 ? 144.408 127.902 74.609  1.00 44.97 ? 542 LYS A CA    1 
ATOM   4351  C  C     . LYS A 1 542 ? 143.974 128.993 75.577  1.00 43.81 ? 542 LYS A C     1 
ATOM   4352  O  O     . LYS A 1 542 ? 142.864 129.526 75.469  1.00 44.91 ? 542 LYS A O     1 
ATOM   4353  C  CB    . LYS A 1 542 ? 144.236 126.523 75.243  1.00 43.14 ? 542 LYS A CB    1 
ATOM   4354  C  CG    . LYS A 1 542 ? 142.789 126.108 75.442  1.00 44.10 ? 542 LYS A CG    1 
ATOM   4355  C  CD    . LYS A 1 542 ? 142.665 125.059 76.533  1.00 44.96 ? 542 LYS A CD    1 
ATOM   4356  C  CE    . LYS A 1 542 ? 141.323 124.351 76.467  1.00 46.75 ? 542 LYS A CE    1 
ATOM   4357  N  NZ    . LYS A 1 542 ? 140.201 125.309 76.269  1.00 46.50 ? 542 LYS A NZ    1 
ATOM   4358  N  N     . ILE A 1 543 ? 144.836 129.333 76.536  1.00 41.73 ? 543 ILE A N     1 
ATOM   4359  C  CA    . ILE A 1 543 ? 144.512 130.381 77.497  1.00 38.85 ? 543 ILE A CA    1 
ATOM   4360  C  C     . ILE A 1 543 ? 144.543 131.750 76.830  1.00 39.24 ? 543 ILE A C     1 
ATOM   4361  O  O     . ILE A 1 543 ? 143.730 132.627 77.145  1.00 41.48 ? 543 ILE A O     1 
ATOM   4362  C  CB    . ILE A 1 543 ? 145.471 130.311 78.699  1.00 38.85 ? 543 ILE A CB    1 
ATOM   4363  C  CG1   . ILE A 1 543 ? 145.426 128.921 79.335  1.00 39.27 ? 543 ILE A CG1   1 
ATOM   4364  C  CG2   . ILE A 1 543 ? 145.119 131.372 79.721  1.00 39.96 ? 543 ILE A CG2   1 
ATOM   4365  C  CD1   . ILE A 1 543 ? 144.026 128.418 79.614  1.00 38.23 ? 543 ILE A CD1   1 
ATOM   4366  N  N     . ALA A 1 544 ? 145.484 131.959 75.905  1.00 41.31 ? 544 ALA A N     1 
ATOM   4367  C  CA    . ALA A 1 544 ? 145.603 133.256 75.247  1.00 44.44 ? 544 ALA A CA    1 
ATOM   4368  C  C     . ALA A 1 544 ? 144.363 133.594 74.429  1.00 43.26 ? 544 ALA A C     1 
ATOM   4369  O  O     . ALA A 1 544 ? 144.030 134.773 74.269  1.00 43.50 ? 544 ALA A O     1 
ATOM   4370  C  CB    . ALA A 1 544 ? 146.846 133.282 74.360  1.00 44.28 ? 544 ALA A CB    1 
ATOM   4371  N  N     . ASN A 1 545 ? 143.672 132.582 73.899  1.00 45.46 ? 545 ASN A N     1 
ATOM   4372  C  CA    . ASN A 1 545 ? 142.433 132.844 73.174  1.00 46.98 ? 545 ASN A CA    1 
ATOM   4373  C  C     . ASN A 1 545 ? 141.294 133.198 74.120  1.00 47.21 ? 545 ASN A C     1 
ATOM   4374  O  O     . ASN A 1 545 ? 140.344 133.877 73.715  1.00 46.69 ? 545 ASN A O     1 
ATOM   4375  C  CB    . ASN A 1 545 ? 142.055 131.640 72.313  1.00 46.81 ? 545 ASN A CB    1 
ATOM   4376  C  CG    . ASN A 1 545 ? 143.180 131.201 71.400  1.00 50.60 ? 545 ASN A CG    1 
ATOM   4377  O  OD1   . ASN A 1 545 ? 144.116 131.957 71.142  1.00 50.63 ? 545 ASN A OD1   1 
ATOM   4378  N  ND2   . ASN A 1 545 ? 143.096 129.972 70.904  1.00 49.01 ? 545 ASN A ND2   1 
ATOM   4379  N  N     . LEU A 1 546 ? 141.364 132.744 75.374  1.00 44.61 ? 546 LEU A N     1 
ATOM   4380  C  CA    . LEU A 1 546 ? 140.339 133.106 76.348  1.00 42.49 ? 546 LEU A CA    1 
ATOM   4381  C  C     . LEU A 1 546 ? 140.345 134.601 76.633  1.00 42.05 ? 546 LEU A C     1 
ATOM   4382  O  O     . LEU A 1 546 ? 139.298 135.177 76.948  1.00 45.35 ? 546 LEU A O     1 
ATOM   4383  C  CB    . LEU A 1 546 ? 140.543 132.320 77.642  1.00 41.58 ? 546 LEU A CB    1 
ATOM   4384  C  CG    . LEU A 1 546 ? 140.337 130.807 77.580  1.00 39.41 ? 546 LEU A CG    1 
ATOM   4385  C  CD1   . LEU A 1 546 ? 140.659 130.176 78.922  1.00 39.40 ? 546 LEU A CD1   1 
ATOM   4386  C  CD2   . LEU A 1 546 ? 138.918 130.472 77.156  1.00 39.40 ? 546 LEU A CD2   1 
ATOM   4387  N  N     . PHE A 1 547 ? 141.505 135.243 76.524  1.00 40.45 ? 547 PHE A N     1 
ATOM   4388  C  CA    . PHE A 1 547 ? 141.640 136.672 76.759  1.00 40.64 ? 547 PHE A CA    1 
ATOM   4389  C  C     . PHE A 1 547 ? 141.599 137.483 75.471  1.00 40.93 ? 547 PHE A C     1 
ATOM   4390  O  O     . PHE A 1 547 ? 141.875 138.686 75.499  1.00 41.35 ? 547 PHE A O     1 
ATOM   4391  C  CB    . PHE A 1 547 ? 142.938 136.960 77.517  1.00 36.36 ? 547 PHE A CB    1 
ATOM   4392  C  CG    . PHE A 1 547 ? 142.917 136.507 78.947  1.00 37.93 ? 547 PHE A CG    1 
ATOM   4393  C  CD1   . PHE A 1 547 ? 142.398 137.321 79.938  1.00 37.86 ? 547 PHE A CD1   1 
ATOM   4394  C  CD2   . PHE A 1 547 ? 143.416 135.266 79.301  1.00 37.32 ? 547 PHE A CD2   1 
ATOM   4395  C  CE1   . PHE A 1 547 ? 142.380 136.906 81.255  1.00 33.49 ? 547 PHE A CE1   1 
ATOM   4396  C  CE2   . PHE A 1 547 ? 143.400 134.847 80.616  1.00 35.40 ? 547 PHE A CE2   1 
ATOM   4397  C  CZ    . PHE A 1 547 ? 142.881 135.667 81.593  1.00 34.60 ? 547 PHE A CZ    1 
ATOM   4398  N  N     . GLU A 1 548 ? 141.271 136.853 74.345  1.00 50.79 ? 548 GLU A N     1 
ATOM   4399  C  CA    . GLU A 1 548 ? 141.195 137.565 73.078  1.00 52.60 ? 548 GLU A CA    1 
ATOM   4400  C  C     . GLU A 1 548 ? 140.087 138.608 73.124  1.00 51.77 ? 548 GLU A C     1 
ATOM   4401  O  O     . GLU A 1 548 ? 138.985 138.347 73.614  1.00 52.16 ? 548 GLU A O     1 
ATOM   4402  C  CB    . GLU A 1 548 ? 140.966 136.576 71.931  1.00 49.23 ? 548 GLU A CB    1 
ATOM   4403  C  CG    . GLU A 1 548 ? 140.345 137.163 70.666  1.00 51.80 ? 548 GLU A CG    1 
ATOM   4404  C  CD    . GLU A 1 548 ? 138.826 137.136 70.682  1.00 52.46 ? 548 GLU A CD    1 
ATOM   4405  O  OE1   . GLU A 1 548 ? 138.209 138.101 70.185  1.00 52.18 ? 548 GLU A OE1   1 
ATOM   4406  O  OE2   . GLU A 1 548 ? 138.253 136.149 71.189  1.00 53.95 ? 548 GLU A OE2   1 
ATOM   4407  N  N     . GLY A 1 549 ? 140.383 139.797 72.604  1.00 45.80 ? 549 GLY A N     1 
ATOM   4408  C  CA    . GLY A 1 549 ? 139.473 140.917 72.695  1.00 45.85 ? 549 GLY A CA    1 
ATOM   4409  C  C     . GLY A 1 549 ? 139.570 141.707 73.980  1.00 46.62 ? 549 GLY A C     1 
ATOM   4410  O  O     . GLY A 1 549 ? 138.793 142.652 74.167  1.00 47.28 ? 549 GLY A O     1 
ATOM   4411  N  N     . MET A 1 550 ? 140.494 141.352 74.868  1.00 46.69 ? 550 MET A N     1 
ATOM   4412  C  CA    . MET A 1 550 ? 140.693 142.044 76.133  1.00 43.67 ? 550 MET A CA    1 
ATOM   4413  C  C     . MET A 1 550 ? 142.179 142.314 76.303  1.00 43.97 ? 550 MET A C     1 
ATOM   4414  O  O     . MET A 1 550 ? 142.993 141.389 76.218  1.00 47.86 ? 550 MET A O     1 
ATOM   4415  C  CB    . MET A 1 550 ? 140.157 141.211 77.300  1.00 43.43 ? 550 MET A CB    1 
ATOM   4416  C  CG    . MET A 1 550 ? 139.648 142.027 78.470  1.00 47.81 ? 550 MET A CG    1 
ATOM   4417  S  SD    . MET A 1 550 ? 139.192 141.011 79.888  1.00 53.52 ? 550 MET A SD    1 
ATOM   4418  C  CE    . MET A 1 550 ? 139.195 139.371 79.171  1.00 44.33 ? 550 MET A CE    1 
ATOM   4419  N  N     . HIS A 1 551 ? 142.531 143.575 76.541  1.00 41.19 ? 551 HIS A N     1 
ATOM   4420  C  CA    . HIS A 1 551 ? 143.936 143.952 76.619  1.00 40.72 ? 551 HIS A CA    1 
ATOM   4421  C  C     . HIS A 1 551 ? 144.566 143.421 77.900  1.00 41.77 ? 551 HIS A C     1 
ATOM   4422  O  O     . HIS A 1 551 ? 144.034 143.614 78.997  1.00 42.60 ? 551 HIS A O     1 
ATOM   4423  C  CB    . HIS A 1 551 ? 144.086 145.470 76.550  1.00 39.80 ? 551 HIS A CB    1 
ATOM   4424  C  CG    . HIS A 1 551 ? 145.464 145.953 76.877  1.00 44.81 ? 551 HIS A CG    1 
ATOM   4425  N  ND1   . HIS A 1 551 ? 146.501 145.914 75.971  1.00 47.40 ? 551 HIS A ND1   1 
ATOM   4426  C  CD2   . HIS A 1 551 ? 145.977 146.482 78.013  1.00 44.00 ? 551 HIS A CD2   1 
ATOM   4427  C  CE1   . HIS A 1 551 ? 147.593 146.400 76.534  1.00 44.89 ? 551 HIS A CE1   1 
ATOM   4428  N  NE2   . HIS A 1 551 ? 147.302 146.751 77.773  1.00 43.06 ? 551 HIS A NE2   1 
ATOM   4429  N  N     . ILE A 1 552 ? 145.704 142.755 77.756  1.00 37.54 ? 552 ILE A N     1 
ATOM   4430  C  CA    . ILE A 1 552 ? 146.470 142.228 78.882  1.00 36.75 ? 552 ILE A CA    1 
ATOM   4431  C  C     . ILE A 1 552 ? 147.615 143.194 79.161  1.00 38.99 ? 552 ILE A C     1 
ATOM   4432  O  O     . ILE A 1 552 ? 148.462 143.400 78.278  1.00 41.59 ? 552 ILE A O     1 
ATOM   4433  C  CB    . ILE A 1 552 ? 146.999 140.816 78.592  1.00 36.55 ? 552 ILE A CB    1 
ATOM   4434  C  CG1   . ILE A 1 552 ? 145.840 139.864 78.302  1.00 35.33 ? 552 ILE A CG1   1 
ATOM   4435  C  CG2   . ILE A 1 552 ? 147.828 140.310 79.755  1.00 35.95 ? 552 ILE A CG2   1 
ATOM   4436  C  CD1   . ILE A 1 552 ? 146.271 138.549 77.703  1.00 38.96 ? 552 ILE A CD1   1 
ATOM   4437  N  N     . PRO A 1 553 ? 147.675 143.811 80.341  1.00 41.59 ? 553 PRO A N     1 
ATOM   4438  C  CA    . PRO A 1 553 ? 148.774 144.739 80.632  1.00 37.88 ? 553 PRO A CA    1 
ATOM   4439  C  C     . PRO A 1 553 ? 150.127 144.051 80.554  1.00 37.52 ? 553 PRO A C     1 
ATOM   4440  O  O     . PRO A 1 553 ? 150.316 142.941 81.058  1.00 35.06 ? 553 PRO A O     1 
ATOM   4441  C  CB    . PRO A 1 553 ? 148.467 145.216 82.056  1.00 34.59 ? 553 PRO A CB    1 
ATOM   4442  C  CG    . PRO A 1 553 ? 147.011 144.970 82.234  1.00 32.77 ? 553 PRO A CG    1 
ATOM   4443  C  CD    . PRO A 1 553 ? 146.696 143.752 81.436  1.00 34.25 ? 553 PRO A CD    1 
ATOM   4444  N  N     . THR A 1 554 ? 151.073 144.730 79.920  1.00 42.29 ? 554 THR A N     1 
ATOM   4445  C  CA    . THR A 1 554 ? 152.423 144.234 79.735  1.00 39.99 ? 554 THR A CA    1 
ATOM   4446  C  C     . THR A 1 554 ? 153.334 144.825 80.808  1.00 35.76 ? 554 THR A C     1 
ATOM   4447  O  O     . THR A 1 554 ? 152.875 145.435 81.777  1.00 38.46 ? 554 THR A O     1 
ATOM   4448  C  CB    . THR A 1 554 ? 152.910 144.568 78.325  1.00 38.61 ? 554 THR A CB    1 
ATOM   4449  O  OG1   . THR A 1 554 ? 152.922 145.989 78.147  1.00 43.72 ? 554 THR A OG1   1 
ATOM   4450  C  CG2   . THR A 1 554 ? 151.992 143.944 77.288  1.00 41.01 ? 554 THR A CG2   1 
ATOM   4451  N  N     . THR A 1 555 ? 154.643 144.634 80.643  1.00 38.47 ? 555 THR A N     1 
ATOM   4452  C  CA    . THR A 1 555 ? 155.592 145.262 81.555  1.00 36.19 ? 555 THR A CA    1 
ATOM   4453  C  C     . THR A 1 555 ? 155.571 146.779 81.408  1.00 39.01 ? 555 THR A C     1 
ATOM   4454  O  O     . THR A 1 555 ? 155.725 147.503 82.395  1.00 42.44 ? 555 THR A O     1 
ATOM   4455  C  CB    . THR A 1 555 ? 156.999 144.720 81.314  1.00 39.56 ? 555 THR A CB    1 
ATOM   4456  O  OG1   . THR A 1 555 ? 157.189 144.489 79.913  1.00 48.32 ? 555 THR A OG1   1 
ATOM   4457  C  CG2   . THR A 1 555 ? 157.202 143.415 82.070  1.00 38.31 ? 555 THR A CG2   1 
ATOM   4458  N  N     . GLU A 1 556 ? 155.387 147.276 80.182  1.00 40.31 ? 556 GLU A N     1 
ATOM   4459  C  CA    . GLU A 1 556 ? 155.300 148.718 79.970  1.00 42.32 ? 556 GLU A CA    1 
ATOM   4460  C  C     . GLU A 1 556 ? 154.066 149.304 80.646  1.00 42.67 ? 556 GLU A C     1 
ATOM   4461  O  O     . GLU A 1 556 ? 154.129 150.382 81.252  1.00 44.98 ? 556 GLU A O     1 
ATOM   4462  C  CB    . GLU A 1 556 ? 155.289 149.027 78.472  1.00 42.96 ? 556 GLU A CB    1 
ATOM   4463  C  CG    . GLU A 1 556 ? 156.507 148.531 77.684  1.00 45.88 ? 556 GLU A CG    1 
ATOM   4464  C  CD    . GLU A 1 556 ? 157.820 148.584 78.457  1.00 49.68 ? 556 GLU A CD    1 
ATOM   4465  O  OE1   . GLU A 1 556 ? 158.641 147.658 78.289  1.00 50.16 ? 556 GLU A OE1   1 
ATOM   4466  O  OE2   . GLU A 1 556 ? 158.066 149.572 79.183  1.00 43.92 ? 556 GLU A OE2   1 
ATOM   4467  N  N     . ASP A 1 557 ? 152.931 148.608 80.549  1.00 43.07 ? 557 ASP A N     1 
ATOM   4468  C  CA    . ASP A 1 557 ? 151.723 149.066 81.224  1.00 40.33 ? 557 ASP A CA    1 
ATOM   4469  C  C     . ASP A 1 557 ? 151.917 149.087 82.733  1.00 37.75 ? 557 ASP A C     1 
ATOM   4470  O  O     . ASP A 1 557 ? 151.456 150.009 83.414  1.00 38.62 ? 557 ASP A O     1 
ATOM   4471  C  CB    . ASP A 1 557 ? 150.542 148.173 80.847  1.00 38.35 ? 557 ASP A CB    1 
ATOM   4472  C  CG    . ASP A 1 557 ? 149.801 148.674 79.629  1.00 44.42 ? 557 ASP A CG    1 
ATOM   4473  O  OD1   . ASP A 1 557 ? 149.507 149.886 79.568  1.00 46.00 ? 557 ASP A OD1   1 
ATOM   4474  O  OD2   . ASP A 1 557 ? 149.511 147.856 78.731  1.00 44.79 ? 557 ASP A OD2   1 
ATOM   4475  N  N     . TRP A 1 558 ? 152.602 148.080 83.273  1.00 30.80 ? 558 TRP A N     1 
ATOM   4476  C  CA    . TRP A 1 558 ? 152.864 148.056 84.705  1.00 27.59 ? 558 TRP A CA    1 
ATOM   4477  C  C     . TRP A 1 558 ? 153.836 149.152 85.122  1.00 35.28 ? 558 TRP A C     1 
ATOM   4478  O  O     . TRP A 1 558 ? 153.704 149.701 86.217  1.00 36.79 ? 558 TRP A O     1 
ATOM   4479  C  CB    . TRP A 1 558 ? 153.388 146.685 85.121  1.00 29.60 ? 558 TRP A CB    1 
ATOM   4480  C  CG    . TRP A 1 558 ? 152.306 145.724 85.501  1.00 29.60 ? 558 TRP A CG    1 
ATOM   4481  C  CD1   . TRP A 1 558 ? 151.860 144.661 84.773  1.00 28.40 ? 558 TRP A CD1   1 
ATOM   4482  C  CD2   . TRP A 1 558 ? 151.528 145.741 86.703  1.00 29.70 ? 558 TRP A CD2   1 
ATOM   4483  N  NE1   . TRP A 1 558 ? 150.857 144.012 85.450  1.00 30.99 ? 558 TRP A NE1   1 
ATOM   4484  C  CE2   . TRP A 1 558 ? 150.636 144.654 86.639  1.00 30.70 ? 558 TRP A CE2   1 
ATOM   4485  C  CE3   . TRP A 1 558 ? 151.506 146.565 87.832  1.00 33.45 ? 558 TRP A CE3   1 
ATOM   4486  C  CZ2   . TRP A 1 558 ? 149.730 144.373 87.657  1.00 24.50 ? 558 TRP A CZ2   1 
ATOM   4487  C  CZ3   . TRP A 1 558 ? 150.605 146.284 88.840  1.00 27.95 ? 558 TRP A CZ3   1 
ATOM   4488  C  CH2   . TRP A 1 558 ? 149.730 145.198 88.746  1.00 19.63 ? 558 TRP A CH2   1 
ATOM   4489  N  N     . LYS A 1 559 ? 154.812 149.486 84.274  1.00 40.63 ? 559 LYS A N     1 
ATOM   4490  C  CA    . LYS A 1 559 ? 155.691 150.616 84.569  1.00 35.90 ? 559 LYS A CA    1 
ATOM   4491  C  C     . LYS A 1 559 ? 154.912 151.925 84.587  1.00 36.87 ? 559 LYS A C     1 
ATOM   4492  O  O     . LYS A 1 559 ? 155.125 152.776 85.462  1.00 40.94 ? 559 LYS A O     1 
ATOM   4493  C  CB    . LYS A 1 559 ? 156.825 150.686 83.547  1.00 39.29 ? 559 LYS A CB    1 
ATOM   4494  C  CG    . LYS A 1 559 ? 157.827 149.551 83.637  1.00 38.55 ? 559 LYS A CG    1 
ATOM   4495  C  CD    . LYS A 1 559 ? 158.687 149.482 82.388  1.00 41.53 ? 559 LYS A CD    1 
ATOM   4496  C  CE    . LYS A 1 559 ? 159.750 148.403 82.504  1.00 40.98 ? 559 LYS A CE    1 
ATOM   4497  N  NZ    . LYS A 1 559 ? 160.485 148.479 83.796  1.00 44.20 ? 559 LYS A NZ    1 
ATOM   4498  N  N     . LYS A 1 560 ? 154.007 152.105 83.623  1.00 37.14 ? 560 LYS A N     1 
ATOM   4499  C  CA    . LYS A 1 560 ? 153.170 153.300 83.611  1.00 33.99 ? 560 LYS A CA    1 
ATOM   4500  C  C     . LYS A 1 560 ? 152.288 153.365 84.851  1.00 36.62 ? 560 LYS A C     1 
ATOM   4501  O  O     . LYS A 1 560 ? 152.122 154.434 85.448  1.00 42.51 ? 560 LYS A O     1 
ATOM   4502  C  CB    . LYS A 1 560 ? 152.318 153.333 82.343  1.00 34.13 ? 560 LYS A CB    1 
ATOM   4503  C  CG    . LYS A 1 560 ? 153.110 153.567 81.069  1.00 38.73 ? 560 LYS A CG    1 
ATOM   4504  C  CD    . LYS A 1 560 ? 152.199 153.609 79.855  1.00 39.97 ? 560 LYS A CD    1 
ATOM   4505  C  CE    . LYS A 1 560 ? 152.892 153.048 78.625  1.00 40.24 ? 560 LYS A CE    1 
ATOM   4506  N  NZ    . LYS A 1 560 ? 152.546 151.618 78.393  1.00 41.34 ? 560 LYS A NZ    1 
ATOM   4507  N  N     . LEU A 1 561 ? 151.716 152.229 85.256  1.00 33.91 ? 561 LEU A N     1 
ATOM   4508  C  CA    . LEU A 1 561 ? 150.901 152.197 86.466  1.00 30.30 ? 561 LEU A CA    1 
ATOM   4509  C  C     . LEU A 1 561 ? 151.736 152.484 87.707  1.00 32.34 ? 561 LEU A C     1 
ATOM   4510  O  O     . LEU A 1 561 ? 151.265 153.144 88.637  1.00 35.96 ? 561 LEU A O     1 
ATOM   4511  C  CB    . LEU A 1 561 ? 150.200 150.846 86.597  1.00 31.57 ? 561 LEU A CB    1 
ATOM   4512  C  CG    . LEU A 1 561 ? 149.369 150.683 87.871  1.00 31.80 ? 561 LEU A CG    1 
ATOM   4513  C  CD1   . LEU A 1 561 ? 148.271 151.729 87.922  1.00 27.87 ? 561 LEU A CD1   1 
ATOM   4514  C  CD2   . LEU A 1 561 ? 148.787 149.289 87.976  1.00 29.12 ? 561 LEU A CD2   1 
ATOM   4515  N  N     . LYS A 1 562 ? 152.971 151.981 87.747  1.00 34.18 ? 562 LYS A N     1 
ATOM   4516  C  CA    . LYS A 1 562 ? 153.855 152.264 88.872  1.00 33.79 ? 562 LYS A CA    1 
ATOM   4517  C  C     . LYS A 1 562 ? 154.162 153.751 88.965  1.00 34.76 ? 562 LYS A C     1 
ATOM   4518  O  O     . LYS A 1 562 ? 154.148 154.328 90.058  1.00 39.30 ? 562 LYS A O     1 
ATOM   4519  C  CB    . LYS A 1 562 ? 155.143 151.452 88.733  1.00 35.38 ? 562 LYS A CB    1 
ATOM   4520  C  CG    . LYS A 1 562 ? 156.245 151.849 89.695  1.00 31.74 ? 562 LYS A CG    1 
ATOM   4521  C  CD    . LYS A 1 562 ? 157.531 151.106 89.384  1.00 29.19 ? 562 LYS A CD    1 
ATOM   4522  C  CE    . LYS A 1 562 ? 158.656 151.535 90.307  1.00 35.46 ? 562 LYS A CE    1 
ATOM   4523  N  NZ    . LYS A 1 562 ? 159.720 150.499 90.393  1.00 41.73 ? 562 LYS A NZ    1 
ATOM   4524  N  N     . ALA A 1 563 ? 154.434 154.391 87.826  1.00 33.23 ? 563 ALA A N     1 
ATOM   4525  C  CA    . ALA A 1 563 ? 154.647 155.836 87.824  1.00 33.68 ? 563 ALA A CA    1 
ATOM   4526  C  C     . ALA A 1 563 ? 153.390 156.579 88.264  1.00 36.70 ? 563 ALA A C     1 
ATOM   4527  O  O     . ALA A 1 563 ? 153.464 157.547 89.032  1.00 43.35 ? 563 ALA A O     1 
ATOM   4528  C  CB    . ALA A 1 563 ? 155.090 156.299 86.438  1.00 36.16 ? 563 ALA A CB    1 
ATOM   4529  N  N     . PHE A 1 564 ? 152.224 156.133 87.790  1.00 34.74 ? 564 PHE A N     1 
ATOM   4530  C  CA    . PHE A 1 564 ? 150.963 156.759 88.174  1.00 32.14 ? 564 PHE A CA    1 
ATOM   4531  C  C     . PHE A 1 564 ? 150.728 156.655 89.676  1.00 35.78 ? 564 PHE A C     1 
ATOM   4532  O  O     . PHE A 1 564 ? 150.289 157.618 90.313  1.00 38.79 ? 564 PHE A O     1 
ATOM   4533  C  CB    . PHE A 1 564 ? 149.816 156.107 87.400  1.00 33.73 ? 564 PHE A CB    1 
ATOM   4534  C  CG    . PHE A 1 564 ? 148.533 156.882 87.433  1.00 34.30 ? 564 PHE A CG    1 
ATOM   4535  C  CD1   . PHE A 1 564 ? 148.264 157.842 86.474  1.00 36.18 ? 564 PHE A CD1   1 
ATOM   4536  C  CD2   . PHE A 1 564 ? 147.586 156.638 88.411  1.00 35.29 ? 564 PHE A CD2   1 
ATOM   4537  C  CE1   . PHE A 1 564 ? 147.080 158.553 86.497  1.00 39.38 ? 564 PHE A CE1   1 
ATOM   4538  C  CE2   . PHE A 1 564 ? 146.401 157.345 88.440  1.00 35.43 ? 564 PHE A CE2   1 
ATOM   4539  C  CZ    . PHE A 1 564 ? 146.147 158.302 87.481  1.00 38.87 ? 564 PHE A CZ    1 
ATOM   4540  N  N     . VAL A 1 565 ? 151.015 155.490 90.256  1.00 35.42 ? 565 VAL A N     1 
ATOM   4541  C  CA    . VAL A 1 565 ? 150.843 155.297 91.692  1.00 30.12 ? 565 VAL A CA    1 
ATOM   4542  C  C     . VAL A 1 565 ? 151.842 156.142 92.469  1.00 34.33 ? 565 VAL A C     1 
ATOM   4543  O  O     . VAL A 1 565 ? 151.502 156.744 93.494  1.00 36.70 ? 565 VAL A O     1 
ATOM   4544  C  CB    . VAL A 1 565 ? 150.965 153.803 92.041  1.00 29.51 ? 565 VAL A CB    1 
ATOM   4545  C  CG1   . VAL A 1 565 ? 151.162 153.610 93.534  1.00 29.22 ? 565 VAL A CG1   1 
ATOM   4546  C  CG2   . VAL A 1 565 ? 149.737 153.057 91.564  1.00 34.16 ? 565 VAL A CG2   1 
ATOM   4547  N  N     . ALA A 1 566 ? 153.088 156.206 91.996  1.00 37.13 ? 566 ALA A N     1 
ATOM   4548  C  CA    . ALA A 1 566 ? 154.094 157.010 92.678  1.00 36.67 ? 566 ALA A CA    1 
ATOM   4549  C  C     . ALA A 1 566 ? 153.753 158.492 92.633  1.00 38.97 ? 566 ALA A C     1 
ATOM   4550  O  O     . ALA A 1 566 ? 154.108 159.237 93.553  1.00 43.04 ? 566 ALA A O     1 
ATOM   4551  C  CB    . ALA A 1 566 ? 155.470 156.763 92.062  1.00 36.69 ? 566 ALA A CB    1 
ATOM   4552  N  N     . GLU A 1 567 ? 153.070 158.940 91.581  1.00 40.85 ? 567 GLU A N     1 
ATOM   4553  C  CA    . GLU A 1 567 ? 152.752 160.352 91.438  1.00 39.75 ? 567 GLU A CA    1 
ATOM   4554  C  C     . GLU A 1 567 ? 151.401 160.738 92.032  1.00 40.56 ? 567 GLU A C     1 
ATOM   4555  O  O     . GLU A 1 567 ? 151.194 161.918 92.336  1.00 43.95 ? 567 GLU A O     1 
ATOM   4556  C  CB    . GLU A 1 567 ? 152.811 160.746 89.957  1.00 41.85 ? 567 GLU A CB    1 
ATOM   4557  C  CG    . GLU A 1 567 ? 152.856 162.239 89.698  1.00 43.74 ? 567 GLU A CG    1 
ATOM   4558  C  CD    . GLU A 1 567 ? 151.581 162.751 89.073  1.00 47.95 ? 567 GLU A CD    1 
ATOM   4559  O  OE1   . GLU A 1 567 ? 150.910 161.958 88.381  1.00 46.80 ? 567 GLU A OE1   1 
ATOM   4560  O  OE2   . GLU A 1 567 ? 151.249 163.939 89.271  1.00 46.38 ? 567 GLU A OE2   1 
ATOM   4561  N  N     . HIS A 1 568 ? 150.485 159.784 92.221  1.00 40.27 ? 568 HIS A N     1 
ATOM   4562  C  CA    . HIS A 1 568 ? 149.177 160.068 92.796  1.00 39.21 ? 568 HIS A CA    1 
ATOM   4563  C  C     . HIS A 1 568 ? 148.857 159.307 94.074  1.00 35.94 ? 568 HIS A C     1 
ATOM   4564  O  O     . HIS A 1 568 ? 147.958 159.732 94.806  1.00 39.86 ? 568 HIS A O     1 
ATOM   4565  C  CB    . HIS A 1 568 ? 148.064 159.783 91.777  1.00 36.96 ? 568 HIS A CB    1 
ATOM   4566  C  CG    . HIS A 1 568 ? 148.039 160.737 90.625  1.00 38.52 ? 568 HIS A CG    1 
ATOM   4567  N  ND1   . HIS A 1 568 ? 147.498 160.410 89.401  1.00 43.01 ? 568 HIS A ND1   1 
ATOM   4568  C  CD2   . HIS A 1 568 ? 148.492 162.007 90.510  1.00 39.13 ? 568 HIS A CD2   1 
ATOM   4569  C  CE1   . HIS A 1 568 ? 147.625 161.436 88.579  1.00 41.82 ? 568 HIS A CE1   1 
ATOM   4570  N  NE2   . HIS A 1 568 ? 148.219 162.420 89.229  1.00 42.98 ? 568 HIS A NE2   1 
ATOM   4571  N  N     . GLY A 1 569 ? 149.549 158.211 94.365  1.00 29.43 ? 569 GLY A N     1 
ATOM   4572  C  CA    . GLY A 1 569 ? 149.269 157.453 95.566  1.00 30.32 ? 569 GLY A CA    1 
ATOM   4573  C  C     . GLY A 1 569 ? 148.156 156.441 95.383  1.00 29.07 ? 569 GLY A C     1 
ATOM   4574  O  O     . GLY A 1 569 ? 147.563 156.293 94.314  1.00 34.59 ? 569 GLY A O     1 
ATOM   4575  N  N     . MET A 1 570 ? 147.871 155.725 96.467  1.00 25.11 ? 570 MET A N     1 
ATOM   4576  C  CA    . MET A 1 570 ? 146.840 154.698 96.495  1.00 22.56 ? 570 MET A CA    1 
ATOM   4577  C  C     . MET A 1 570 ? 145.816 155.029 97.569  1.00 24.18 ? 570 MET A C     1 
ATOM   4578  O  O     . MET A 1 570 ? 146.175 155.453 98.671  1.00 32.01 ? 570 MET A O     1 
ATOM   4579  C  CB    . MET A 1 570 ? 147.441 153.315 96.761  1.00 28.31 ? 570 MET A CB    1 
ATOM   4580  C  CG    . MET A 1 570 ? 148.343 152.806 95.655  1.00 25.46 ? 570 MET A CG    1 
ATOM   4581  S  SD    . MET A 1 570 ? 147.489 151.677 94.550  1.00 37.35 ? 570 MET A SD    1 
ATOM   4582  C  CE    . MET A 1 570 ? 147.327 150.248 95.609  1.00 24.98 ? 570 MET A CE    1 
ATOM   4583  N  N     . TYR A 1 571 ? 144.539 154.829 97.246  1.00 17.09 ? 571 TYR A N     1 
ATOM   4584  C  CA    . TYR A 1 571 ? 143.479 155.145 98.194  1.00 10.23 ? 571 TYR A CA    1 
ATOM   4585  C  C     . TYR A 1 571 ? 143.247 154.025 99.198  1.00 18.52 ? 571 TYR A C     1 
ATOM   4586  O  O     . TYR A 1 571 ? 142.905 154.297 100.353 1.00 21.74 ? 571 TYR A O     1 
ATOM   4587  C  CB    . TYR A 1 571 ? 142.182 155.452 97.447  1.00 21.02 ? 571 TYR A CB    1 
ATOM   4588  C  CG    . TYR A 1 571 ? 141.120 156.083 98.312  1.00 25.37 ? 571 TYR A CG    1 
ATOM   4589  C  CD1   . TYR A 1 571 ? 141.195 157.421 98.668  1.00 23.98 ? 571 TYR A CD1   1 
ATOM   4590  C  CD2   . TYR A 1 571 ? 140.042 155.342 98.774  1.00 19.74 ? 571 TYR A CD2   1 
ATOM   4591  C  CE1   . TYR A 1 571 ? 140.230 158.002 99.458  1.00 26.01 ? 571 TYR A CE1   1 
ATOM   4592  C  CE2   . TYR A 1 571 ? 139.072 155.915 99.566  1.00 21.24 ? 571 TYR A CE2   1 
ATOM   4593  C  CZ    . TYR A 1 571 ? 139.169 157.246 99.903  1.00 28.94 ? 571 TYR A CZ    1 
ATOM   4594  O  OH    . TYR A 1 571 ? 138.204 157.824 100.692 1.00 27.29 ? 571 TYR A OH    1 
ATOM   4595  N  N     . HIS A 1 572 ? 143.423 152.774 98.787  1.00 23.03 ? 572 HIS A N     1 
ATOM   4596  C  CA    . HIS A 1 572 ? 143.175 151.620 99.640  1.00 15.47 ? 572 HIS A CA    1 
ATOM   4597  C  C     . HIS A 1 572 ? 144.497 150.974 100.024 1.00 12.80 ? 572 HIS A C     1 
ATOM   4598  O  O     . HIS A 1 572 ? 145.333 150.700 99.157  1.00 26.21 ? 572 HIS A O     1 
ATOM   4599  C  CB    . HIS A 1 572 ? 142.279 150.598 98.938  1.00 14.86 ? 572 HIS A CB    1 
ATOM   4600  C  CG    . HIS A 1 572 ? 141.117 151.205 98.220  1.00 9.45  ? 572 HIS A CG    1 
ATOM   4601  N  ND1   . HIS A 1 572 ? 141.162 151.542 96.885  1.00 20.06 ? 572 HIS A ND1   1 
ATOM   4602  C  CD2   . HIS A 1 572 ? 139.876 151.533 98.649  1.00 16.33 ? 572 HIS A CD2   1 
ATOM   4603  C  CE1   . HIS A 1 572 ? 139.999 152.053 96.523  1.00 20.21 ? 572 HIS A CE1   1 
ATOM   4604  N  NE2   . HIS A 1 572 ? 139.201 152.058 97.575  1.00 25.22 ? 572 HIS A NE2   1 
ATOM   4605  N  N     . SER A 1 573 ? 144.683 150.738 101.324 1.00 7.36  ? 573 SER A N     1 
ATOM   4606  C  CA    . SER A 1 573 ? 145.855 149.997 101.775 1.00 8.79  ? 573 SER A CA    1 
ATOM   4607  C  C     . SER A 1 573 ? 145.819 148.564 101.267 1.00 15.66 ? 573 SER A C     1 
ATOM   4608  O  O     . SER A 1 573 ? 146.849 148.010 100.868 1.00 24.42 ? 573 SER A O     1 
ATOM   4609  C  CB    . SER A 1 573 ? 145.942 150.027 103.300 1.00 13.38 ? 573 SER A CB    1 
ATOM   4610  O  OG    . SER A 1 573 ? 144.690 149.720 103.884 1.00 21.84 ? 573 SER A OG    1 
ATOM   4611  N  N     . TYR A 1 574 ? 144.638 147.951 101.271 1.00 16.56 ? 574 TYR A N     1 
ATOM   4612  C  CA    . TYR A 1 574 ? 144.436 146.604 100.767 1.00 4.86  ? 574 TYR A CA    1 
ATOM   4613  C  C     . TYR A 1 574 ? 143.226 146.610 99.848  1.00 9.42  ? 574 TYR A C     1 
ATOM   4614  O  O     . TYR A 1 574 ? 142.255 147.330 100.096 1.00 13.71 ? 574 TYR A O     1 
ATOM   4615  C  CB    . TYR A 1 574 ? 144.239 145.610 101.914 1.00 13.23 ? 574 TYR A CB    1 
ATOM   4616  C  CG    . TYR A 1 574 ? 145.340 145.673 102.944 1.00 7.99  ? 574 TYR A CG    1 
ATOM   4617  C  CD1   . TYR A 1 574 ? 145.288 146.589 103.985 1.00 6.61  ? 574 TYR A CD1   1 
ATOM   4618  C  CD2   . TYR A 1 574 ? 146.438 144.831 102.869 1.00 8.95  ? 574 TYR A CD2   1 
ATOM   4619  C  CE1   . TYR A 1 574 ? 146.291 146.663 104.921 1.00 9.26  ? 574 TYR A CE1   1 
ATOM   4620  C  CE2   . TYR A 1 574 ? 147.447 144.896 103.806 1.00 17.33 ? 574 TYR A CE2   1 
ATOM   4621  C  CZ    . TYR A 1 574 ? 147.367 145.815 104.829 1.00 8.22  ? 574 TYR A CZ    1 
ATOM   4622  O  OH    . TYR A 1 574 ? 148.365 145.888 105.769 1.00 14.30 ? 574 TYR A OH    1 
ATOM   4623  N  N     . ARG A 1 575 ? 143.290 145.825 98.788  1.00 16.16 ? 575 ARG A N     1 
ATOM   4624  C  CA    . ARG A 1 575 ? 142.222 145.861 97.795  1.00 7.00  ? 575 ARG A CA    1 
ATOM   4625  C  C     . ARG A 1 575 ? 141.603 144.501 97.519  1.00 11.88 ? 575 ARG A C     1 
ATOM   4626  O  O     . ARG A 1 575 ? 140.387 144.414 97.343  1.00 20.36 ? 575 ARG A O     1 
ATOM   4627  C  CB    . ARG A 1 575 ? 142.748 146.455 96.482  1.00 15.25 ? 575 ARG A CB    1 
ATOM   4628  C  CG    . ARG A 1 575 ? 143.302 147.859 96.605  1.00 6.43  ? 575 ARG A CG    1 
ATOM   4629  C  CD    . ARG A 1 575 ? 144.349 148.112 95.541  1.00 12.88 ? 575 ARG A CD    1 
ATOM   4630  N  NE    . ARG A 1 575 ? 145.588 147.399 95.824  1.00 21.48 ? 575 ARG A NE    1 
ATOM   4631  C  CZ    . ARG A 1 575 ? 145.991 146.310 95.186  1.00 14.06 ? 575 ARG A CZ    1 
ATOM   4632  N  NH1   . ARG A 1 575 ? 145.278 145.778 94.208  1.00 16.98 ? 575 ARG A NH1   1 
ATOM   4633  N  NH2   . ARG A 1 575 ? 147.139 145.739 95.538  1.00 9.95  ? 575 ARG A NH2   1 
ATOM   4634  N  N     . LEU A 1 576 ? 142.403 143.441 97.476  1.00 19.83 ? 576 LEU A N     1 
ATOM   4635  C  CA    . LEU A 1 576 ? 141.953 142.137 97.011  1.00 9.72  ? 576 LEU A CA    1 
ATOM   4636  C  C     . LEU A 1 576 ? 142.066 141.115 98.130  1.00 6.79  ? 576 LEU A C     1 
ATOM   4637  O  O     . LEU A 1 576 ? 143.133 140.959 98.729  1.00 15.59 ? 576 LEU A O     1 
ATOM   4638  C  CB    . LEU A 1 576 ? 142.772 141.679 95.802  1.00 5.77  ? 576 LEU A CB    1 
ATOM   4639  C  CG    . LEU A 1 576 ? 142.867 142.657 94.631  1.00 10.04 ? 576 LEU A CG    1 
ATOM   4640  C  CD1   . LEU A 1 576 ? 143.821 142.132 93.575  1.00 12.63 ? 576 LEU A CD1   1 
ATOM   4641  C  CD2   . LEU A 1 576 ? 141.498 142.913 94.033  1.00 10.31 ? 576 LEU A CD2   1 
ATOM   4642  N  N     . CYS A 1 577 ? 140.962 140.426 98.407  1.00 4.60  ? 577 CYS A N     1 
ATOM   4643  C  CA    . CYS A 1 577 ? 140.962 139.265 99.285  1.00 3.63  ? 577 CYS A CA    1 
ATOM   4644  C  C     . CYS A 1 577 ? 139.886 138.314 98.787  1.00 17.05 ? 577 CYS A C     1 
ATOM   4645  O  O     . CYS A 1 577 ? 138.779 138.748 98.461  1.00 21.81 ? 577 CYS A O     1 
ATOM   4646  C  CB    . CYS A 1 577 ? 140.726 139.659 100.750 1.00 4.91  ? 577 CYS A CB    1 
ATOM   4647  S  SG    . CYS A 1 577 ? 139.011 139.913 101.258 1.00 33.12 ? 577 CYS A SG    1 
ATOM   4648  N  N     . ILE A 1 578 ? 140.217 137.030 98.709  1.00 15.01 ? 578 ILE A N     1 
ATOM   4649  C  CA    . ILE A 1 578 ? 139.322 136.024 98.153  1.00 10.21 ? 578 ILE A CA    1 
ATOM   4650  C  C     . ILE A 1 578 ? 138.659 135.302 99.321  1.00 4.66  ? 578 ILE A C     1 
ATOM   4651  O  O     . ILE A 1 578 ? 139.257 134.429 99.955  1.00 16.19 ? 578 ILE A O     1 
ATOM   4652  C  CB    . ILE A 1 578 ? 140.059 135.062 97.219  1.00 10.36 ? 578 ILE A CB    1 
ATOM   4653  C  CG1   . ILE A 1 578 ? 140.710 135.846 96.079  1.00 0.67  ? 578 ILE A CG1   1 
ATOM   4654  C  CG2   . ILE A 1 578 ? 139.103 134.035 96.653  1.00 13.68 ? 578 ILE A CG2   1 
ATOM   4655  C  CD1   . ILE A 1 578 ? 141.344 134.981 95.033  1.00 7.71  ? 578 ILE A CD1   1 
ATOM   4656  N  N     . ALA A 1 579 ? 137.416 135.675 99.598  1.00 17.26 ? 579 ALA A N     1 
ATOM   4657  C  CA    . ALA A 1 579 ? 136.626 135.109 100.679 1.00 13.13 ? 579 ALA A CA    1 
ATOM   4658  C  C     . ALA A 1 579 ? 135.977 133.802 100.237 1.00 21.68 ? 579 ALA A C     1 
ATOM   4659  O  O     . ALA A 1 579 ? 135.958 133.472 99.051  1.00 28.40 ? 579 ALA A O     1 
ATOM   4660  C  CB    . ALA A 1 579 ? 135.577 136.124 101.122 1.00 11.41 ? 579 ALA A CB    1 
ATOM   4661  N  N     . PRO A 1 580 ? 135.456 133.013 101.183 1.00 26.68 ? 580 PRO A N     1 
ATOM   4662  C  CA    . PRO A 1 580 ? 134.767 131.769 100.795 1.00 23.53 ? 580 PRO A CA    1 
ATOM   4663  C  C     . PRO A 1 580 ? 133.553 131.975 99.899  1.00 25.61 ? 580 PRO A C     1 
ATOM   4664  O  O     . PRO A 1 580 ? 133.285 131.117 99.048  1.00 33.40 ? 580 PRO A O     1 
ATOM   4665  C  CB    . PRO A 1 580 ? 134.371 131.148 102.144 1.00 24.92 ? 580 PRO A CB    1 
ATOM   4666  C  CG    . PRO A 1 580 ? 134.621 132.203 103.175 1.00 25.14 ? 580 PRO A CG    1 
ATOM   4667  C  CD    . PRO A 1 580 ? 135.695 133.070 102.634 1.00 21.78 ? 580 PRO A CD    1 
ATOM   4668  N  N     . THR A 1 581 ? 132.819 133.077 100.055 1.00 23.15 ? 581 THR A N     1 
ATOM   4669  C  CA    . THR A 1 581 ? 131.614 133.369 99.268  1.00 33.97 ? 581 THR A CA    1 
ATOM   4670  C  C     . THR A 1 581 ? 130.628 132.198 99.317  1.00 31.93 ? 581 THR A C     1 
ATOM   4671  O  O     . THR A 1 581 ? 130.321 131.554 98.314  1.00 32.55 ? 581 THR A O     1 
ATOM   4672  C  CB    . THR A 1 581 ? 131.956 133.722 97.815  1.00 32.50 ? 581 THR A CB    1 
ATOM   4673  O  OG1   . THR A 1 581 ? 132.008 132.527 97.027  1.00 27.75 ? 581 THR A OG1   1 
ATOM   4674  C  CG2   . THR A 1 581 ? 133.282 134.457 97.723  1.00 31.57 ? 581 THR A CG2   1 
ATOM   4675  N  N     . GLY A 1 582 ? 130.137 131.943 100.527 1.00 35.20 ? 582 GLY A N     1 
ATOM   4676  C  CA    . GLY A 1 582 ? 129.328 130.769 100.786 1.00 33.36 ? 582 GLY A CA    1 
ATOM   4677  C  C     . GLY A 1 582 ? 127.994 130.695 100.069 1.00 35.60 ? 582 GLY A C     1 
ATOM   4678  O  O     . GLY A 1 582 ? 127.804 129.837 99.203  1.00 37.25 ? 582 GLY A O     1 
ATOM   4679  N  N     . SER A 1 583 ? 127.063 131.585 100.410 1.00 37.33 ? 583 SER A N     1 
ATOM   4680  C  CA    . SER A 1 583 ? 125.695 131.467 99.919  1.00 39.19 ? 583 SER A CA    1 
ATOM   4681  C  C     . SER A 1 583 ? 125.419 132.291 98.669  1.00 36.87 ? 583 SER A C     1 
ATOM   4682  O  O     . SER A 1 583 ? 124.480 131.970 97.933  1.00 38.72 ? 583 SER A O     1 
ATOM   4683  C  CB    . SER A 1 583 ? 124.704 131.871 101.015 1.00 42.49 ? 583 SER A CB    1 
ATOM   4684  O  OG    . SER A 1 583 ? 123.422 131.320 100.768 1.00 40.25 ? 583 SER A OG    1 
ATOM   4685  N  N     . ILE A 1 584 ? 126.202 133.340 98.410  1.00 33.01 ? 584 ILE A N     1 
ATOM   4686  C  CA    . ILE A 1 584 ? 125.995 134.126 97.199  1.00 31.17 ? 584 ILE A CA    1 
ATOM   4687  C  C     . ILE A 1 584 ? 126.418 133.361 95.954  1.00 33.72 ? 584 ILE A C     1 
ATOM   4688  O  O     . ILE A 1 584 ? 126.078 133.767 94.837  1.00 40.88 ? 584 ILE A O     1 
ATOM   4689  C  CB    . ILE A 1 584 ? 126.742 135.470 97.285  1.00 35.71 ? 584 ILE A CB    1 
ATOM   4690  C  CG1   . ILE A 1 584 ? 128.211 135.245 97.645  1.00 35.62 ? 584 ILE A CG1   1 
ATOM   4691  C  CG2   . ILE A 1 584 ? 126.066 136.392 98.285  1.00 33.65 ? 584 ILE A CG2   1 
ATOM   4692  C  CD1   . ILE A 1 584 ? 129.043 136.507 97.637  1.00 33.79 ? 584 ILE A CD1   1 
ATOM   4693  N  N     . SER A 1 585 ? 127.160 132.263 96.115  1.00 32.49 ? 585 SER A N     1 
ATOM   4694  C  CA    . SER A 1 585 ? 127.559 131.462 94.964  1.00 29.51 ? 585 SER A CA    1 
ATOM   4695  C  C     . SER A 1 585 ? 126.363 130.778 94.315  1.00 31.16 ? 585 SER A C     1 
ATOM   4696  O  O     . SER A 1 585 ? 126.344 130.598 93.092  1.00 33.18 ? 585 SER A O     1 
ATOM   4697  C  CB    . SER A 1 585 ? 128.601 130.428 95.383  1.00 29.71 ? 585 SER A CB    1 
ATOM   4698  O  OG    . SER A 1 585 ? 128.144 129.666 96.486  1.00 35.69 ? 585 SER A OG    1 
ATOM   4699  N  N     . TYR A 1 586 ? 125.369 130.378 95.110  1.00 32.14 ? 586 TYR A N     1 
ATOM   4700  C  CA    . TYR A 1 586 ? 124.148 129.818 94.542  1.00 33.76 ? 586 TYR A CA    1 
ATOM   4701  C  C     . TYR A 1 586 ? 123.402 130.860 93.721  1.00 32.66 ? 586 TYR A C     1 
ATOM   4702  O  O     . TYR A 1 586 ? 123.000 130.595 92.583  1.00 39.04 ? 586 TYR A O     1 
ATOM   4703  C  CB    . TYR A 1 586 ? 123.248 129.279 95.651  1.00 33.61 ? 586 TYR A CB    1 
ATOM   4704  C  CG    . TYR A 1 586 ? 123.843 128.147 96.449  1.00 34.78 ? 586 TYR A CG    1 
ATOM   4705  C  CD1   . TYR A 1 586 ? 123.770 126.839 95.994  1.00 35.37 ? 586 TYR A CD1   1 
ATOM   4706  C  CD2   . TYR A 1 586 ? 124.468 128.385 97.664  1.00 32.51 ? 586 TYR A CD2   1 
ATOM   4707  C  CE1   . TYR A 1 586 ? 124.308 125.801 96.724  1.00 36.51 ? 586 TYR A CE1   1 
ATOM   4708  C  CE2   . TYR A 1 586 ? 125.010 127.353 98.400  1.00 34.47 ? 586 TYR A CE2   1 
ATOM   4709  C  CZ    . TYR A 1 586 ? 124.928 126.063 97.925  1.00 37.63 ? 586 TYR A CZ    1 
ATOM   4710  O  OH    . TYR A 1 586 ? 125.466 125.032 98.658  1.00 40.91 ? 586 TYR A OH    1 
ATOM   4711  N  N     . VAL A 1 587 ? 123.221 132.056 94.284  1.00 29.57 ? 587 VAL A N     1 
ATOM   4712  C  CA    . VAL A 1 587 ? 122.474 133.113 93.607  1.00 27.76 ? 587 VAL A CA    1 
ATOM   4713  C  C     . VAL A 1 587 ? 123.135 133.472 92.285  1.00 31.27 ? 587 VAL A C     1 
ATOM   4714  O  O     . VAL A 1 587 ? 122.460 133.662 91.265  1.00 33.32 ? 587 VAL A O     1 
ATOM   4715  C  CB    . VAL A 1 587 ? 122.344 134.340 94.528  1.00 30.35 ? 587 VAL A CB    1 
ATOM   4716  C  CG1   . VAL A 1 587 ? 121.748 135.515 93.776  1.00 30.99 ? 587 VAL A CG1   1 
ATOM   4717  C  CG2   . VAL A 1 587 ? 121.509 133.997 95.749  1.00 31.88 ? 587 VAL A CG2   1 
ATOM   4718  N  N     . GLN A 1 588 ? 124.461 133.562 92.276  1.00 33.13 ? 588 GLN A N     1 
ATOM   4719  C  CA    . GLN A 1 588 ? 125.205 133.882 91.067  1.00 29.62 ? 588 GLN A CA    1 
ATOM   4720  C  C     . GLN A 1 588 ? 125.405 132.679 90.160  1.00 29.03 ? 588 GLN A C     1 
ATOM   4721  O  O     . GLN A 1 588 ? 125.977 132.836 89.076  1.00 32.12 ? 588 GLN A O     1 
ATOM   4722  C  CB    . GLN A 1 588 ? 126.566 134.478 91.431  1.00 25.58 ? 588 GLN A CB    1 
ATOM   4723  C  CG    . GLN A 1 588 ? 126.501 135.892 91.967  1.00 24.81 ? 588 GLN A CG    1 
ATOM   4724  C  CD    . GLN A 1 588 ? 126.740 136.927 90.891  1.00 27.86 ? 588 GLN A CD    1 
ATOM   4725  O  OE1   . GLN A 1 588 ? 127.593 136.749 90.024  1.00 28.96 ? 588 GLN A OE1   1 
ATOM   4726  N  NE2   . GLN A 1 588 ? 125.990 138.019 90.942  1.00 30.16 ? 588 GLN A NE2   1 
ATOM   4727  N  N     . SER A 1 589 ? 124.945 131.499 90.572  1.00 32.63 ? 589 SER A N     1 
ATOM   4728  C  CA    . SER A 1 589 ? 125.145 130.255 89.834  1.00 29.87 ? 589 SER A CA    1 
ATOM   4729  C  C     . SER A 1 589 ? 126.628 130.059 89.527  1.00 32.47 ? 589 SER A C     1 
ATOM   4730  O  O     . SER A 1 589 ? 127.058 129.967 88.377  1.00 30.69 ? 589 SER A O     1 
ATOM   4731  C  CB    . SER A 1 589 ? 124.300 130.229 88.559  1.00 30.91 ? 589 SER A CB    1 
ATOM   4732  O  OG    . SER A 1 589 ? 123.958 128.901 88.207  1.00 40.83 ? 589 SER A OG    1 
ATOM   4733  N  N     . SER A 1 590 ? 127.413 130.008 90.600  1.00 32.95 ? 590 SER A N     1 
ATOM   4734  C  CA    . SER A 1 590 ? 128.861 129.979 90.504  1.00 26.30 ? 590 SER A CA    1 
ATOM   4735  C  C     . SER A 1 590 ? 129.419 129.015 91.537  1.00 27.35 ? 590 SER A C     1 
ATOM   4736  O  O     . SER A 1 590 ? 128.795 128.757 92.568  1.00 31.41 ? 590 SER A O     1 
ATOM   4737  C  CB    . SER A 1 590 ? 129.457 131.377 90.715  1.00 23.85 ? 590 SER A CB    1 
ATOM   4738  O  OG    . SER A 1 590 ? 129.862 131.558 92.058  1.00 32.77 ? 590 SER A OG    1 
ATOM   4739  N  N     . THR A 1 591 ? 130.598 128.475 91.245  1.00 27.95 ? 591 THR A N     1 
ATOM   4740  C  CA    . THR A 1 591 ? 131.306 127.672 92.228  1.00 22.82 ? 591 THR A CA    1 
ATOM   4741  C  C     . THR A 1 591 ? 131.876 128.569 93.320  1.00 27.65 ? 591 THR A C     1 
ATOM   4742  O  O     . THR A 1 591 ? 132.213 129.733 93.087  1.00 25.19 ? 591 THR A O     1 
ATOM   4743  C  CB    . THR A 1 591 ? 132.422 126.865 91.568  1.00 24.84 ? 591 THR A CB    1 
ATOM   4744  O  OG1   . THR A 1 591 ? 133.459 127.747 91.126  1.00 32.13 ? 591 THR A OG1   1 
ATOM   4745  C  CG2   . THR A 1 591 ? 131.883 126.095 90.378  1.00 25.61 ? 591 THR A CG2   1 
ATOM   4746  N  N     . ALA A 1 592 ? 131.978 128.017 94.524  1.00 27.31 ? 592 ALA A N     1 
ATOM   4747  C  CA    . ALA A 1 592 ? 132.348 128.812 95.687  1.00 24.20 ? 592 ALA A CA    1 
ATOM   4748  C  C     . ALA A 1 592 ? 133.816 129.211 95.613  1.00 29.01 ? 592 ALA A C     1 
ATOM   4749  O  O     . ALA A 1 592 ? 134.701 128.349 95.598  1.00 31.77 ? 592 ALA A O     1 
ATOM   4750  C  CB    . ALA A 1 592 ? 132.070 128.031 96.969  1.00 27.91 ? 592 ALA A CB    1 
ATOM   4751  N  N     . SER A 1 593 ? 134.065 130.516 95.564  1.00 28.14 ? 593 SER A N     1 
ATOM   4752  C  CA    . SER A 1 593 ? 135.410 131.100 95.642  1.00 12.73 ? 593 SER A CA    1 
ATOM   4753  C  C     . SER A 1 593 ? 136.253 130.564 94.481  1.00 13.75 ? 593 SER A C     1 
ATOM   4754  O  O     . SER A 1 593 ? 135.719 130.175 93.434  1.00 27.00 ? 593 SER A O     1 
ATOM   4755  C  CB    . SER A 1 593 ? 135.989 130.838 97.020  1.00 27.68 ? 593 SER A CB    1 
ATOM   4756  O  OG    . SER A 1 593 ? 137.211 131.524 97.207  1.00 29.12 ? 593 SER A OG    1 
ATOM   4757  N  N     . VAL A 1 594 ? 137.576 130.550 94.652  1.00 23.48 ? 594 VAL A N     1 
ATOM   4758  C  CA    . VAL A 1 594 ? 138.481 129.974 93.668  1.00 20.26 ? 594 VAL A CA    1 
ATOM   4759  C  C     . VAL A 1 594 ? 138.838 128.533 93.991  1.00 15.68 ? 594 VAL A C     1 
ATOM   4760  O  O     . VAL A 1 594 ? 139.668 127.935 93.295  1.00 17.58 ? 594 VAL A O     1 
ATOM   4761  C  CB    . VAL A 1 594 ? 139.757 130.828 93.532  1.00 18.50 ? 594 VAL A CB    1 
ATOM   4762  C  CG1   . VAL A 1 594 ? 139.428 132.172 92.901  1.00 12.96 ? 594 VAL A CG1   1 
ATOM   4763  C  CG2   . VAL A 1 594 ? 140.414 131.022 94.885  1.00 17.14 ? 594 VAL A CG2   1 
ATOM   4764  N  N     . MET A 1 595 ? 138.237 127.960 95.029  1.00 22.80 ? 595 MET A N     1 
ATOM   4765  C  CA    . MET A 1 595 ? 138.481 126.574 95.382  1.00 21.56 ? 595 MET A CA    1 
ATOM   4766  C  C     . MET A 1 595 ? 137.731 125.637 94.435  1.00 24.24 ? 595 MET A C     1 
ATOM   4767  O  O     . MET A 1 595 ? 136.711 126.015 93.852  1.00 24.71 ? 595 MET A O     1 
ATOM   4768  C  CB    . MET A 1 595 ? 138.052 126.313 96.825  1.00 23.85 ? 595 MET A CB    1 
ATOM   4769  C  CG    . MET A 1 595 ? 139.196 126.066 97.814  1.00 21.94 ? 595 MET A CG    1 
ATOM   4770  S  SD    . MET A 1 595 ? 140.670 127.091 97.629  1.00 31.09 ? 595 MET A SD    1 
ATOM   4771  C  CE    . MET A 1 595 ? 139.990 128.745 97.672  1.00 31.74 ? 595 MET A CE    1 
ATOM   4772  N  N     . PRO A 1 596 ? 138.223 124.414 94.258  1.00 31.46 ? 596 PRO A N     1 
ATOM   4773  C  CA    . PRO A 1 596 ? 137.505 123.442 93.429  1.00 20.82 ? 596 PRO A CA    1 
ATOM   4774  C  C     . PRO A 1 596 ? 136.227 122.964 94.103  1.00 26.49 ? 596 PRO A C     1 
ATOM   4775  O  O     . PRO A 1 596 ? 136.052 123.058 95.319  1.00 31.11 ? 596 PRO A O     1 
ATOM   4776  C  CB    . PRO A 1 596 ? 138.511 122.298 93.271  1.00 23.11 ? 596 PRO A CB    1 
ATOM   4777  C  CG    . PRO A 1 596 ? 139.405 122.421 94.453  1.00 29.13 ? 596 PRO A CG    1 
ATOM   4778  C  CD    . PRO A 1 596 ? 139.505 123.883 94.751  1.00 28.81 ? 596 PRO A CD    1 
ATOM   4779  N  N     . ILE A 1 597 ? 135.321 122.443 93.275  1.00 27.65 ? 597 ILE A N     1 
ATOM   4780  C  CA    . ILE A 1 597 ? 134.027 121.988 93.763  1.00 30.83 ? 597 ILE A CA    1 
ATOM   4781  C  C     . ILE A 1 597 ? 134.197 120.742 94.622  1.00 30.58 ? 597 ILE A C     1 
ATOM   4782  O  O     . ILE A 1 597 ? 135.108 119.930 94.416  1.00 31.78 ? 597 ILE A O     1 
ATOM   4783  C  CB    . ILE A 1 597 ? 133.067 121.720 92.589  1.00 32.41 ? 597 ILE A CB    1 
ATOM   4784  C  CG1   . ILE A 1 597 ? 133.531 120.502 91.787  1.00 28.01 ? 597 ILE A CG1   1 
ATOM   4785  C  CG2   . ILE A 1 597 ? 132.974 122.938 91.698  1.00 29.64 ? 597 ILE A CG2   1 
ATOM   4786  C  CD1   . ILE A 1 597 ? 132.411 119.714 91.167  1.00 29.02 ? 597 ILE A CD1   1 
ATOM   4787  N  N     . MET A 1 598 ? 133.308 120.589 95.601  1.00 40.97 ? 598 MET A N     1 
ATOM   4788  C  CA    . MET A 1 598 ? 133.316 119.417 96.467  1.00 42.52 ? 598 MET A CA    1 
ATOM   4789  C  C     . MET A 1 598 ? 132.480 118.278 95.900  1.00 41.85 ? 598 MET A C     1 
ATOM   4790  O  O     . MET A 1 598 ? 132.914 117.121 95.924  1.00 45.77 ? 598 MET A O     1 
ATOM   4791  C  CB    . MET A 1 598 ? 132.810 119.793 97.861  1.00 42.49 ? 598 MET A CB    1 
ATOM   4792  C  CG    . MET A 1 598 ? 133.346 121.116 98.377  1.00 40.25 ? 598 MET A CG    1 
ATOM   4793  S  SD    . MET A 1 598 ? 133.205 121.290 100.165 1.00 57.57 ? 598 MET A SD    1 
ATOM   4794  C  CE    . MET A 1 598 ? 131.868 120.152 100.519 1.00 45.17 ? 598 MET A CE    1 
ATOM   4795  N  N     . GLU A 1 599 ? 131.287 118.581 95.394  1.00 40.92 ? 599 GLU A N     1 
ATOM   4796  C  CA    . GLU A 1 599 ? 130.406 117.595 94.786  1.00 39.56 ? 599 GLU A CA    1 
ATOM   4797  C  C     . GLU A 1 599 ? 129.964 118.095 93.420  1.00 38.42 ? 599 GLU A C     1 
ATOM   4798  O  O     . GLU A 1 599 ? 129.702 119.287 93.245  1.00 42.40 ? 599 GLU A O     1 
ATOM   4799  C  CB    . GLU A 1 599 ? 129.173 117.324 95.660  1.00 43.03 ? 599 GLU A CB    1 
ATOM   4800  C  CG    . GLU A 1 599 ? 129.436 117.382 97.155  1.00 44.21 ? 599 GLU A CG    1 
ATOM   4801  C  CD    . GLU A 1 599 ? 128.160 117.380 97.973  1.00 48.36 ? 599 GLU A CD    1 
ATOM   4802  O  OE1   . GLU A 1 599 ? 127.507 116.319 98.059  1.00 47.93 ? 599 GLU A OE1   1 
ATOM   4803  O  OE2   . GLU A 1 599 ? 127.809 118.440 98.533  1.00 46.29 ? 599 GLU A OE2   1 
ATOM   4804  N  N     . ARG A 1 600 ? 129.888 117.180 92.451  1.00 41.85 ? 600 ARG A N     1 
ATOM   4805  C  CA    . ARG A 1 600 ? 129.374 117.547 91.135  1.00 37.69 ? 600 ARG A CA    1 
ATOM   4806  C  C     . ARG A 1 600 ? 127.897 117.906 91.211  1.00 38.40 ? 600 ARG A C     1 
ATOM   4807  O  O     . ARG A 1 600 ? 127.468 118.940 90.685  1.00 41.86 ? 600 ARG A O     1 
ATOM   4808  C  CB    . ARG A 1 600 ? 129.599 116.406 90.146  1.00 36.87 ? 600 ARG A CB    1 
ATOM   4809  C  CG    . ARG A 1 600 ? 131.002 116.342 89.586  1.00 36.92 ? 600 ARG A CG    1 
ATOM   4810  C  CD    . ARG A 1 600 ? 131.074 115.376 88.426  1.00 37.11 ? 600 ARG A CD    1 
ATOM   4811  N  NE    . ARG A 1 600 ? 132.445 115.107 88.011  1.00 35.73 ? 600 ARG A NE    1 
ATOM   4812  C  CZ    . ARG A 1 600 ? 133.242 114.222 88.593  1.00 38.81 ? 600 ARG A CZ    1 
ATOM   4813  N  NH1   . ARG A 1 600 ? 132.843 113.516 89.637  1.00 37.60 ? 600 ARG A NH1   1 
ATOM   4814  N  NH2   . ARG A 1 600 ? 134.470 114.043 88.116  1.00 40.09 ? 600 ARG A NH2   1 
ATOM   4815  N  N     . ILE A 1 601 ? 127.103 117.060 91.859  1.00 45.21 ? 601 ILE A N     1 
ATOM   4816  C  CA    . ILE A 1 601 ? 125.704 117.341 92.151  1.00 43.51 ? 601 ILE A CA    1 
ATOM   4817  C  C     . ILE A 1 601 ? 125.567 117.388 93.663  1.00 42.73 ? 601 ILE A C     1 
ATOM   4818  O  O     . ILE A 1 601 ? 125.860 116.401 94.349  1.00 46.32 ? 601 ILE A O     1 
ATOM   4819  C  CB    . ILE A 1 601 ? 124.763 116.292 91.539  1.00 43.06 ? 601 ILE A CB    1 
ATOM   4820  C  CG1   . ILE A 1 601 ? 125.107 116.064 90.067  1.00 43.64 ? 601 ILE A CG1   1 
ATOM   4821  C  CG2   . ILE A 1 601 ? 123.317 116.735 91.682  1.00 42.79 ? 601 ILE A CG2   1 
ATOM   4822  C  CD1   . ILE A 1 601 ? 124.253 115.018 89.395  1.00 43.76 ? 601 ILE A CD1   1 
ATOM   4823  N  N     . GLU A 1 602 ? 125.126 118.527 94.180  1.00 50.42 ? 602 GLU A N     1 
ATOM   4824  C  CA    . GLU A 1 602 ? 125.091 118.775 95.613  1.00 50.37 ? 602 GLU A CA    1 
ATOM   4825  C  C     . GLU A 1 602 ? 123.689 118.492 96.136  1.00 52.22 ? 602 GLU A C     1 
ATOM   4826  O  O     . GLU A 1 602 ? 122.719 119.117 95.696  1.00 54.41 ? 602 GLU A O     1 
ATOM   4827  C  CB    . GLU A 1 602 ? 125.512 120.212 95.917  1.00 50.22 ? 602 GLU A CB    1 
ATOM   4828  C  CG    . GLU A 1 602 ? 125.054 120.736 97.260  1.00 50.61 ? 602 GLU A CG    1 
ATOM   4829  C  CD    . GLU A 1 602 ? 125.332 122.215 97.424  1.00 55.20 ? 602 GLU A CD    1 
ATOM   4830  O  OE1   . GLU A 1 602 ? 126.334 122.698 96.856  1.00 53.01 ? 602 GLU A OE1   1 
ATOM   4831  O  OE2   . GLU A 1 602 ? 124.550 122.895 98.121  1.00 56.53 ? 602 GLU A OE2   1 
ATOM   4832  N  N     . GLU A 1 603 ? 123.588 117.547 97.065  1.00 57.66 ? 603 GLU A N     1 
ATOM   4833  C  CA    . GLU A 1 603 ? 122.317 117.144 97.648  1.00 57.80 ? 603 GLU A CA    1 
ATOM   4834  C  C     . GLU A 1 603 ? 122.142 117.821 99.000  1.00 59.19 ? 603 GLU A C     1 
ATOM   4835  O  O     . GLU A 1 603 ? 123.015 117.720 99.868  1.00 58.89 ? 603 GLU A O     1 
ATOM   4836  C  CB    . GLU A 1 603 ? 122.250 115.624 97.805  1.00 59.44 ? 603 GLU A CB    1 
ATOM   4837  C  CG    . GLU A 1 603 ? 120.945 115.113 98.391  1.00 61.07 ? 603 GLU A CG    1 
ATOM   4838  C  CD    . GLU A 1 603 ? 121.025 113.656 98.806  1.00 62.24 ? 603 GLU A CD    1 
ATOM   4839  O  OE1   . GLU A 1 603 ? 121.034 112.780 97.916  1.00 60.34 ? 603 GLU A OE1   1 
ATOM   4840  O  OE2   . GLU A 1 603 ? 121.081 113.386 100.024 1.00 60.42 ? 603 GLU A OE2   1 
ATOM   4841  N  N     . ARG A 1 604 ? 121.018 118.510 99.173  1.00 62.00 ? 604 ARG A N     1 
ATOM   4842  C  CA    . ARG A 1 604 ? 120.717 119.220 100.406 1.00 62.24 ? 604 ARG A CA    1 
ATOM   4843  C  C     . ARG A 1 604 ? 119.291 118.918 100.837 1.00 63.01 ? 604 ARG A C     1 
ATOM   4844  O  O     . ARG A 1 604 ? 118.436 118.572 100.018 1.00 64.89 ? 604 ARG A O     1 
ATOM   4845  C  CB    . ARG A 1 604 ? 120.893 120.737 100.245 1.00 60.51 ? 604 ARG A CB    1 
ATOM   4846  C  CG    . ARG A 1 604 ? 122.301 121.179 99.892  1.00 61.38 ? 604 ARG A CG    1 
ATOM   4847  C  CD    . ARG A 1 604 ? 123.249 120.996 101.063 1.00 63.38 ? 604 ARG A CD    1 
ATOM   4848  N  NE    . ARG A 1 604 ? 124.220 119.937 100.820 1.00 64.08 ? 604 ARG A NE    1 
ATOM   4849  C  CZ    . ARG A 1 604 ? 125.515 120.140 100.625 1.00 62.78 ? 604 ARG A CZ    1 
ATOM   4850  N  NH1   . ARG A 1 604 ? 126.034 121.357 100.644 1.00 61.31 ? 604 ARG A NH1   1 
ATOM   4851  N  NH2   . ARG A 1 604 ? 126.311 119.097 100.406 1.00 60.54 ? 604 ARG A NH2   1 
ATOM   4852  N  N     . THR A 1 605 ? 119.044 119.050 102.138 1.00 68.90 ? 605 THR A N     1 
ATOM   4853  C  CA    . THR A 1 605 ? 117.714 118.891 102.711 1.00 70.31 ? 605 THR A CA    1 
ATOM   4854  C  C     . THR A 1 605 ? 117.324 120.195 103.389 1.00 69.41 ? 605 THR A C     1 
ATOM   4855  O  O     . THR A 1 605 ? 117.993 120.633 104.331 1.00 69.34 ? 605 THR A O     1 
ATOM   4856  C  CB    . THR A 1 605 ? 117.674 117.732 103.710 1.00 70.47 ? 605 THR A CB    1 
ATOM   4857  O  OG1   . THR A 1 605 ? 118.560 116.694 103.278 1.00 70.94 ? 605 THR A OG1   1 
ATOM   4858  C  CG2   . THR A 1 605 ? 116.265 117.173 103.817 1.00 69.52 ? 605 THR A CG2   1 
ATOM   4859  N  N     . TYR A 1 606 ? 116.247 120.812 102.912 1.00 69.64 ? 606 TYR A N     1 
ATOM   4860  C  CA    . TYR A 1 606 ? 115.730 122.055 103.473 1.00 71.86 ? 606 TYR A CA    1 
ATOM   4861  C  C     . TYR A 1 606 ? 114.382 121.750 104.113 1.00 73.74 ? 606 TYR A C     1 
ATOM   4862  O  O     . TYR A 1 606 ? 113.412 121.441 103.412 1.00 71.50 ? 606 TYR A O     1 
ATOM   4863  C  CB    . TYR A 1 606 ? 115.609 123.133 102.398 1.00 70.11 ? 606 TYR A CB    1 
ATOM   4864  C  CG    . TYR A 1 606 ? 116.941 123.579 101.841 1.00 70.69 ? 606 TYR A CG    1 
ATOM   4865  C  CD1   . TYR A 1 606 ? 117.733 124.492 102.525 1.00 68.80 ? 606 TYR A CD1   1 
ATOM   4866  C  CD2   . TYR A 1 606 ? 117.412 123.080 100.635 1.00 70.30 ? 606 TYR A CD2   1 
ATOM   4867  C  CE1   . TYR A 1 606 ? 118.954 124.897 102.019 1.00 69.66 ? 606 TYR A CE1   1 
ATOM   4868  C  CE2   . TYR A 1 606 ? 118.628 123.479 100.122 1.00 67.96 ? 606 TYR A CE2   1 
ATOM   4869  C  CZ    . TYR A 1 606 ? 119.396 124.387 100.818 1.00 70.52 ? 606 TYR A CZ    1 
ATOM   4870  O  OH    . TYR A 1 606 ? 120.610 124.785 100.308 1.00 71.41 ? 606 TYR A OH    1 
ATOM   4871  N  N     . GLY A 1 607 ? 114.324 121.843 105.435 1.00 81.34 ? 607 GLY A N     1 
ATOM   4872  C  CA    . GLY A 1 607 ? 113.127 121.422 106.144 1.00 79.98 ? 607 GLY A CA    1 
ATOM   4873  C  C     . GLY A 1 607 ? 112.911 119.934 105.950 1.00 80.00 ? 607 GLY A C     1 
ATOM   4874  O  O     . GLY A 1 607 ? 113.803 119.114 106.198 1.00 79.97 ? 607 GLY A O     1 
ATOM   4875  N  N     . ASN A 1 608 ? 111.712 119.566 105.497 1.00 81.78 ? 608 ASN A N     1 
ATOM   4876  C  CA    . ASN A 1 608 ? 111.379 118.182 105.187 1.00 82.61 ? 608 ASN A CA    1 
ATOM   4877  C  C     . ASN A 1 608 ? 111.409 117.908 103.687 1.00 82.35 ? 608 ASN A C     1 
ATOM   4878  O  O     . ASN A 1 608 ? 110.753 116.976 103.210 1.00 82.38 ? 608 ASN A O     1 
ATOM   4879  C  CB    . ASN A 1 608 ? 110.011 117.822 105.768 1.00 81.98 ? 608 ASN A CB    1 
ATOM   4880  C  CG    . ASN A 1 608 ? 109.963 117.963 107.278 1.00 82.65 ? 608 ASN A CG    1 
ATOM   4881  O  OD1   . ASN A 1 608 ? 110.998 118.049 107.939 1.00 81.93 ? 608 ASN A OD1   1 
ATOM   4882  N  ND2   . ASN A 1 608 ? 108.756 117.984 107.831 1.00 82.08 ? 608 ASN A ND2   1 
ATOM   4883  N  N     . SER A 1 609 ? 112.164 118.704 102.935 1.00 78.75 ? 609 SER A N     1 
ATOM   4884  C  CA    . SER A 1 609 ? 112.258 118.578 101.489 1.00 78.80 ? 609 SER A CA    1 
ATOM   4885  C  C     . SER A 1 609 ? 113.708 118.349 101.087 1.00 78.58 ? 609 SER A C     1 
ATOM   4886  O  O     . SER A 1 609 ? 114.616 119.010 101.600 1.00 78.27 ? 609 SER A O     1 
ATOM   4887  C  CB    . SER A 1 609 ? 111.716 119.829 100.792 1.00 77.51 ? 609 SER A CB    1 
ATOM   4888  O  OG    . SER A 1 609 ? 112.476 120.975 101.136 1.00 78.81 ? 609 SER A OG    1 
ATOM   4889  N  N     . LYS A 1 610 ? 113.918 117.413 100.166 1.00 68.33 ? 610 LYS A N     1 
ATOM   4890  C  CA    . LYS A 1 610 ? 115.243 117.082 99.660  1.00 67.43 ? 610 LYS A CA    1 
ATOM   4891  C  C     . LYS A 1 610 ? 115.373 117.580 98.228  1.00 67.49 ? 610 LYS A C     1 
ATOM   4892  O  O     . LYS A 1 610 ? 114.517 117.292 97.386  1.00 68.72 ? 610 LYS A O     1 
ATOM   4893  C  CB    . LYS A 1 610 ? 115.493 115.574 99.727  1.00 67.96 ? 610 LYS A CB    1 
ATOM   4894  C  CG    . LYS A 1 610 ? 116.503 115.065 98.712  1.00 67.24 ? 610 LYS A CG    1 
ATOM   4895  C  CD    . LYS A 1 610 ? 117.130 113.756 99.165  1.00 67.75 ? 610 LYS A CD    1 
ATOM   4896  C  CE    . LYS A 1 610 ? 117.621 113.844 100.600 1.00 67.14 ? 610 LYS A CE    1 
ATOM   4897  N  NZ    . LYS A 1 610 ? 118.617 114.936 100.776 1.00 67.49 ? 610 LYS A NZ    1 
ATOM   4898  N  N     . THR A 1 611 ? 116.443 118.324 97.958  1.00 65.20 ? 611 THR A N     1 
ATOM   4899  C  CA    . THR A 1 611 ? 116.667 118.913 96.647  1.00 64.16 ? 611 THR A CA    1 
ATOM   4900  C  C     . THR A 1 611 ? 118.135 118.773 96.275  1.00 62.40 ? 611 THR A C     1 
ATOM   4901  O  O     . THR A 1 611 ? 119.006 118.683 97.143  1.00 61.97 ? 611 THR A O     1 
ATOM   4902  C  CB    . THR A 1 611 ? 116.255 120.388 96.616  1.00 65.09 ? 611 THR A CB    1 
ATOM   4903  O  OG1   . THR A 1 611 ? 116.628 120.964 95.359  1.00 68.47 ? 611 THR A OG1   1 
ATOM   4904  C  CG2   . THR A 1 611 ? 116.930 121.147 97.744  1.00 61.83 ? 611 THR A CG2   1 
ATOM   4905  N  N     . TYR A 1 612 ? 118.401 118.755 94.971  1.00 55.66 ? 612 TYR A N     1 
ATOM   4906  C  CA    . TYR A 1 612 ? 119.738 118.517 94.449  1.00 54.43 ? 612 TYR A CA    1 
ATOM   4907  C  C     . TYR A 1 612 ? 120.186 119.700 93.604  1.00 56.53 ? 612 TYR A C     1 
ATOM   4908  O  O     . TYR A 1 612 ? 119.400 120.259 92.833  1.00 55.45 ? 612 TYR A O     1 
ATOM   4909  C  CB    . TYR A 1 612 ? 119.802 117.231 93.612  1.00 57.22 ? 612 TYR A CB    1 
ATOM   4910  C  CG    . TYR A 1 612 ? 119.306 115.986 94.319  1.00 59.00 ? 612 TYR A CG    1 
ATOM   4911  C  CD1   . TYR A 1 612 ? 120.184 114.964 94.653  1.00 58.43 ? 612 TYR A CD1   1 
ATOM   4912  C  CD2   . TYR A 1 612 ? 117.958 115.809 94.606  1.00 58.08 ? 612 TYR A CD2   1 
ATOM   4913  C  CE1   . TYR A 1 612 ? 119.739 113.821 95.285  1.00 59.41 ? 612 TYR A CE1   1 
ATOM   4914  C  CE2   . TYR A 1 612 ? 117.505 114.669 95.238  1.00 58.80 ? 612 TYR A CE2   1 
ATOM   4915  C  CZ    . TYR A 1 612 ? 118.400 113.677 95.574  1.00 60.88 ? 612 TYR A CZ    1 
ATOM   4916  O  OH    . TYR A 1 612 ? 117.953 112.537 96.201  1.00 61.69 ? 612 TYR A OH    1 
ATOM   4917  N  N     . TYR A 1 613 ? 121.453 120.072 93.753  1.00 51.94 ? 613 TYR A N     1 
ATOM   4918  C  CA    . TYR A 1 613 ? 122.039 121.199 93.028  1.00 42.79 ? 613 TYR A CA    1 
ATOM   4919  C  C     . TYR A 1 613 ? 123.220 120.739 92.189  1.00 41.78 ? 613 TYR A C     1 
ATOM   4920  O  O     . TYR A 1 613 ? 124.327 120.546 92.723  1.00 45.13 ? 613 TYR A O     1 
ATOM   4921  C  CB    . TYR A 1 613 ? 122.475 122.296 93.997  1.00 41.93 ? 613 TYR A CB    1 
ATOM   4922  C  CG    . TYR A 1 613 ? 123.121 123.481 93.317  1.00 42.84 ? 613 TYR A CG    1 
ATOM   4923  C  CD1   . TYR A 1 613 ? 122.525 124.085 92.220  1.00 42.88 ? 613 TYR A CD1   1 
ATOM   4924  C  CD2   . TYR A 1 613 ? 124.326 123.996 93.775  1.00 42.49 ? 613 TYR A CD2   1 
ATOM   4925  C  CE1   . TYR A 1 613 ? 123.108 125.168 91.598  1.00 43.14 ? 613 TYR A CE1   1 
ATOM   4926  C  CE2   . TYR A 1 613 ? 124.917 125.079 93.159  1.00 43.89 ? 613 TYR A CE2   1 
ATOM   4927  C  CZ    . TYR A 1 613 ? 124.303 125.661 92.071  1.00 47.02 ? 613 TYR A CZ    1 
ATOM   4928  O  OH    . TYR A 1 613 ? 124.887 126.741 91.453  1.00 47.35 ? 613 TYR A OH    1 
ATOM   4929  N  N     . PRO A 1 614 ? 123.045 120.543 90.886  1.00 41.37 ? 614 PRO A N     1 
ATOM   4930  C  CA    . PRO A 1 614 ? 124.204 120.307 90.022  1.00 40.74 ? 614 PRO A CA    1 
ATOM   4931  C  C     . PRO A 1 614 ? 125.083 121.544 89.960  1.00 40.58 ? 614 PRO A C     1 
ATOM   4932  O  O     . PRO A 1 614 ? 124.616 122.675 90.117  1.00 44.30 ? 614 PRO A O     1 
ATOM   4933  C  CB    . PRO A 1 614 ? 123.582 119.996 88.655  1.00 37.62 ? 614 PRO A CB    1 
ATOM   4934  C  CG    . PRO A 1 614 ? 122.123 119.776 88.913  1.00 43.39 ? 614 PRO A CG    1 
ATOM   4935  C  CD    . PRO A 1 614 ? 121.786 120.569 90.127  1.00 42.54 ? 614 PRO A CD    1 
ATOM   4936  N  N     . MET A 1 615 ? 126.373 121.319 89.740  1.00 38.05 ? 615 MET A N     1 
ATOM   4937  C  CA    . MET A 1 615 ? 127.298 122.432 89.623  1.00 37.40 ? 615 MET A CA    1 
ATOM   4938  C  C     . MET A 1 615 ? 126.938 123.275 88.401  1.00 41.48 ? 615 MET A C     1 
ATOM   4939  O  O     . MET A 1 615 ? 126.421 122.753 87.409  1.00 37.88 ? 615 MET A O     1 
ATOM   4940  C  CB    . MET A 1 615 ? 128.735 121.928 89.520  1.00 33.40 ? 615 MET A CB    1 
ATOM   4941  C  CG    . MET A 1 615 ? 129.391 121.700 90.869  1.00 36.12 ? 615 MET A CG    1 
ATOM   4942  S  SD    . MET A 1 615 ? 128.971 122.979 92.067  1.00 52.26 ? 615 MET A SD    1 
ATOM   4943  C  CE    . MET A 1 615 ? 128.021 122.038 93.257  1.00 36.13 ? 615 MET A CE    1 
ATOM   4944  N  N     . PRO A 1 616 ? 127.172 124.584 88.458  1.00 40.40 ? 616 PRO A N     1 
ATOM   4945  C  CA    . PRO A 1 616 ? 126.770 125.456 87.347  1.00 36.00 ? 616 PRO A CA    1 
ATOM   4946  C  C     . PRO A 1 616 ? 127.427 125.040 86.040  1.00 37.10 ? 616 PRO A C     1 
ATOM   4947  O  O     . PRO A 1 616 ? 128.650 124.927 85.947  1.00 39.01 ? 616 PRO A O     1 
ATOM   4948  C  CB    . PRO A 1 616 ? 127.242 126.840 87.801  1.00 36.82 ? 616 PRO A CB    1 
ATOM   4949  C  CG    . PRO A 1 616 ? 127.291 126.745 89.287  1.00 39.11 ? 616 PRO A CG    1 
ATOM   4950  C  CD    . PRO A 1 616 ? 127.712 125.348 89.594  1.00 35.76 ? 616 PRO A CD    1 
ATOM   4951  N  N     . GLY A 1 617 ? 126.599 124.818 85.024  1.00 35.76 ? 617 GLY A N     1 
ATOM   4952  C  CA    . GLY A 1 617 ? 127.086 124.392 83.731  1.00 30.51 ? 617 GLY A CA    1 
ATOM   4953  C  C     . GLY A 1 617 ? 127.435 122.927 83.627  1.00 38.01 ? 617 GLY A C     1 
ATOM   4954  O  O     . GLY A 1 617 ? 127.993 122.514 82.604  1.00 40.78 ? 617 GLY A O     1 
ATOM   4955  N  N     . LEU A 1 618 ? 127.134 122.129 84.649  1.00 39.48 ? 618 LEU A N     1 
ATOM   4956  C  CA    . LEU A 1 618 ? 127.460 120.711 84.612  1.00 34.81 ? 618 LEU A CA    1 
ATOM   4957  C  C     . LEU A 1 618 ? 126.639 120.001 83.544  1.00 39.73 ? 618 LEU A C     1 
ATOM   4958  O  O     . LEU A 1 618 ? 125.438 120.240 83.395  1.00 40.06 ? 618 LEU A O     1 
ATOM   4959  C  CB    . LEU A 1 618 ? 127.216 120.068 85.977  1.00 34.76 ? 618 LEU A CB    1 
ATOM   4960  C  CG    . LEU A 1 618 ? 127.519 118.574 86.108  1.00 37.22 ? 618 LEU A CG    1 
ATOM   4961  C  CD1   . LEU A 1 618 ? 128.985 118.284 85.826  1.00 34.89 ? 618 LEU A CD1   1 
ATOM   4962  C  CD2   . LEU A 1 618 ? 127.126 118.064 87.484  1.00 35.54 ? 618 LEU A CD2   1 
ATOM   4963  N  N     . ALA A 1 619 ? 127.300 119.123 82.799  1.00 43.51 ? 619 ALA A N     1 
ATOM   4964  C  CA    . ALA A 1 619 ? 126.668 118.351 81.739  1.00 43.47 ? 619 ALA A CA    1 
ATOM   4965  C  C     . ALA A 1 619 ? 127.506 117.098 81.517  1.00 45.93 ? 619 ALA A C     1 
ATOM   4966  O  O     . ALA A 1 619 ? 128.386 116.771 82.320  1.00 49.74 ? 619 ALA A O     1 
ATOM   4967  C  CB    . ALA A 1 619 ? 126.524 119.185 80.462  1.00 42.19 ? 619 ALA A CB    1 
ATOM   4968  N  N     . SER A 1 620 ? 127.229 116.387 80.425  1.00 50.33 ? 620 SER A N     1 
ATOM   4969  C  CA    . SER A 1 620 ? 128.031 115.219 80.087  1.00 50.26 ? 620 SER A CA    1 
ATOM   4970  C  C     . SER A 1 620 ? 129.288 115.598 79.316  1.00 50.52 ? 620 SER A C     1 
ATOM   4971  O  O     . SER A 1 620 ? 130.274 114.854 79.343  1.00 53.39 ? 620 SER A O     1 
ATOM   4972  C  CB    . SER A 1 620 ? 127.198 114.223 79.280  1.00 53.22 ? 620 SER A CB    1 
ATOM   4973  O  OG    . SER A 1 620 ? 126.024 113.856 79.984  1.00 55.05 ? 620 SER A OG    1 
ATOM   4974  N  N     . ASN A 1 621 ? 129.273 116.742 78.629  1.00 48.50 ? 621 ASN A N     1 
ATOM   4975  C  CA    . ASN A 1 621 ? 130.442 117.156 77.861  1.00 49.10 ? 621 ASN A CA    1 
ATOM   4976  C  C     . ASN A 1 621 ? 131.549 117.692 78.760  1.00 51.83 ? 621 ASN A C     1 
ATOM   4977  O  O     . ASN A 1 621 ? 132.712 117.740 78.342  1.00 51.97 ? 621 ASN A O     1 
ATOM   4978  C  CB    . ASN A 1 621 ? 130.042 118.206 76.824  1.00 49.17 ? 621 ASN A CB    1 
ATOM   4979  C  CG    . ASN A 1 621 ? 130.019 119.610 77.393  1.00 51.20 ? 621 ASN A CG    1 
ATOM   4980  O  OD1   . ASN A 1 621 ? 129.133 119.964 78.170  1.00 50.41 ? 621 ASN A OD1   1 
ATOM   4981  N  ND2   . ASN A 1 621 ? 130.998 120.420 77.008  1.00 48.30 ? 621 ASN A ND2   1 
ATOM   4982  N  N     . ASN A 1 622 ? 131.216 118.101 79.984  1.00 44.18 ? 622 ASN A N     1 
ATOM   4983  C  CA    . ASN A 1 622 ? 132.196 118.610 80.935  1.00 39.96 ? 622 ASN A CA    1 
ATOM   4984  C  C     . ASN A 1 622 ? 132.043 117.955 82.304  1.00 42.40 ? 622 ASN A C     1 
ATOM   4985  O  O     . ASN A 1 622 ? 132.341 118.568 83.331  1.00 47.75 ? 622 ASN A O     1 
ATOM   4986  C  CB    . ASN A 1 622 ? 132.107 120.133 81.047  1.00 42.49 ? 622 ASN A CB    1 
ATOM   4987  C  CG    . ASN A 1 622 ? 130.717 120.622 81.424  1.00 42.61 ? 622 ASN A CG    1 
ATOM   4988  O  OD1   . ASN A 1 622 ? 129.977 119.954 82.143  1.00 43.80 ? 622 ASN A OD1   1 
ATOM   4989  N  ND2   . ASN A 1 622 ? 130.360 121.803 80.936  1.00 41.75 ? 622 ASN A ND2   1 
ATOM   4990  N  N     . TRP A 1 623 ? 131.566 116.709 82.331  1.00 38.36 ? 623 TRP A N     1 
ATOM   4991  C  CA    . TRP A 1 623 ? 131.383 116.013 83.600  1.00 38.52 ? 623 TRP A CA    1 
ATOM   4992  C  C     . TRP A 1 623 ? 132.714 115.773 84.301  1.00 38.74 ? 623 TRP A C     1 
ATOM   4993  O  O     . TRP A 1 623 ? 132.830 115.974 85.516  1.00 37.17 ? 623 TRP A O     1 
ATOM   4994  C  CB    . TRP A 1 623 ? 130.655 114.690 83.369  1.00 41.85 ? 623 TRP A CB    1 
ATOM   4995  C  CG    . TRP A 1 623 ? 130.520 113.848 84.600  1.00 38.29 ? 623 TRP A CG    1 
ATOM   4996  C  CD1   . TRP A 1 623 ? 131.388 112.892 85.038  1.00 37.81 ? 623 TRP A CD1   1 
ATOM   4997  C  CD2   . TRP A 1 623 ? 129.449 113.882 85.550  1.00 36.32 ? 623 TRP A CD2   1 
ATOM   4998  N  NE1   . TRP A 1 623 ? 130.927 112.331 86.203  1.00 38.41 ? 623 TRP A NE1   1 
ATOM   4999  C  CE2   . TRP A 1 623 ? 129.736 112.920 86.537  1.00 38.86 ? 623 TRP A CE2   1 
ATOM   5000  C  CE3   . TRP A 1 623 ? 128.275 114.632 85.661  1.00 38.23 ? 623 TRP A CE3   1 
ATOM   5001  C  CZ2   . TRP A 1 623 ? 128.895 112.690 87.623  1.00 37.43 ? 623 TRP A CZ2   1 
ATOM   5002  C  CZ3   . TRP A 1 623 ? 127.441 114.401 86.739  1.00 39.19 ? 623 TRP A CZ3   1 
ATOM   5003  C  CH2   . TRP A 1 623 ? 127.755 113.440 87.705  1.00 38.40 ? 623 TRP A CH2   1 
ATOM   5004  N  N     . PHE A 1 624 ? 133.730 115.341 83.556  1.00 43.25 ? 624 PHE A N     1 
ATOM   5005  C  CA    . PHE A 1 624 ? 135.014 115.006 84.155  1.00 42.42 ? 624 PHE A CA    1 
ATOM   5006  C  C     . PHE A 1 624 ? 135.918 116.212 84.351  1.00 42.92 ? 624 PHE A C     1 
ATOM   5007  O  O     . PHE A 1 624 ? 136.902 116.116 85.092  1.00 49.79 ? 624 PHE A O     1 
ATOM   5008  C  CB    . PHE A 1 624 ? 135.725 113.948 83.308  1.00 41.73 ? 624 PHE A CB    1 
ATOM   5009  C  CG    . PHE A 1 624 ? 135.038 112.612 83.322  1.00 45.94 ? 624 PHE A CG    1 
ATOM   5010  C  CD1   . PHE A 1 624 ? 135.015 111.846 84.475  1.00 42.67 ? 624 PHE A CD1   1 
ATOM   5011  C  CD2   . PHE A 1 624 ? 134.396 112.134 82.192  1.00 45.33 ? 624 PHE A CD2   1 
ATOM   5012  C  CE1   . PHE A 1 624 ? 134.377 110.622 84.497  1.00 41.80 ? 624 PHE A CE1   1 
ATOM   5013  C  CE2   . PHE A 1 624 ? 133.756 110.911 82.209  1.00 43.20 ? 624 PHE A CE2   1 
ATOM   5014  C  CZ    . PHE A 1 624 ? 133.747 110.154 83.363  1.00 45.67 ? 624 PHE A CZ    1 
ATOM   5015  N  N     . PHE A 1 625 ? 135.612 117.343 83.712  1.00 35.22 ? 625 PHE A N     1 
ATOM   5016  C  CA    . PHE A 1 625 ? 136.306 118.580 84.040  1.00 32.31 ? 625 PHE A CA    1 
ATOM   5017  C  C     . PHE A 1 625 ? 135.833 119.159 85.364  1.00 32.15 ? 625 PHE A C     1 
ATOM   5018  O  O     . PHE A 1 625 ? 136.551 119.963 85.968  1.00 36.91 ? 625 PHE A O     1 
ATOM   5019  C  CB    . PHE A 1 625 ? 136.127 119.606 82.923  1.00 30.82 ? 625 PHE A CB    1 
ATOM   5020  C  CG    . PHE A 1 625 ? 136.890 119.280 81.675  1.00 30.66 ? 625 PHE A CG    1 
ATOM   5021  C  CD1   . PHE A 1 625 ? 138.273 119.264 81.681  1.00 33.16 ? 625 PHE A CD1   1 
ATOM   5022  C  CD2   . PHE A 1 625 ? 136.228 118.994 80.495  1.00 34.03 ? 625 PHE A CD2   1 
ATOM   5023  C  CE1   . PHE A 1 625 ? 138.981 118.968 80.534  1.00 36.53 ? 625 PHE A CE1   1 
ATOM   5024  C  CE2   . PHE A 1 625 ? 136.930 118.698 79.345  1.00 32.06 ? 625 PHE A CE2   1 
ATOM   5025  C  CZ    . PHE A 1 625 ? 138.308 118.685 79.365  1.00 35.76 ? 625 PHE A CZ    1 
ATOM   5026  N  N     . TYR A 1 626 ? 134.648 118.771 85.825  1.00 29.04 ? 626 TYR A N     1 
ATOM   5027  C  CA    . TYR A 1 626 ? 134.158 119.151 87.148  1.00 30.28 ? 626 TYR A CA    1 
ATOM   5028  C  C     . TYR A 1 626 ? 134.624 118.162 88.208  1.00 27.04 ? 626 TYR A C     1 
ATOM   5029  O  O     . TYR A 1 626 ? 133.836 117.631 88.986  1.00 30.43 ? 626 TYR A O     1 
ATOM   5030  C  CB    . TYR A 1 626 ? 132.639 119.256 87.129  1.00 32.36 ? 626 TYR A CB    1 
ATOM   5031  C  CG    . TYR A 1 626 ? 132.131 120.642 86.830  1.00 29.43 ? 626 TYR A CG    1 
ATOM   5032  C  CD1   . TYR A 1 626 ? 132.286 121.670 87.747  1.00 32.99 ? 626 TYR A CD1   1 
ATOM   5033  C  CD2   . TYR A 1 626 ? 131.498 120.925 85.628  1.00 30.28 ? 626 TYR A CD2   1 
ATOM   5034  C  CE1   . TYR A 1 626 ? 131.825 122.940 87.478  1.00 29.62 ? 626 TYR A CE1   1 
ATOM   5035  C  CE2   . TYR A 1 626 ? 131.034 122.191 85.350  1.00 28.81 ? 626 TYR A CE2   1 
ATOM   5036  C  CZ    . TYR A 1 626 ? 131.199 123.194 86.279  1.00 28.21 ? 626 TYR A CZ    1 
ATOM   5037  O  OH    . TYR A 1 626 ? 130.741 124.459 86.009  1.00 33.91 ? 626 TYR A OH    1 
ATOM   5038  N  N     . LYS A 1 627 ? 135.930 117.915 88.237  1.00 32.07 ? 627 LYS A N     1 
ATOM   5039  C  CA    . LYS A 1 627 ? 136.499 116.971 89.187  1.00 32.47 ? 627 LYS A CA    1 
ATOM   5040  C  C     . LYS A 1 627 ? 136.291 117.463 90.612  1.00 32.37 ? 627 LYS A C     1 
ATOM   5041  O  O     . LYS A 1 627 ? 136.515 118.638 90.916  1.00 36.96 ? 627 LYS A O     1 
ATOM   5042  C  CB    . LYS A 1 627 ? 137.987 116.782 88.896  1.00 35.47 ? 627 LYS A CB    1 
ATOM   5043  C  CG    . LYS A 1 627 ? 138.661 115.709 89.724  1.00 35.18 ? 627 LYS A CG    1 
ATOM   5044  C  CD    . LYS A 1 627 ? 140.061 115.436 89.208  1.00 33.16 ? 627 LYS A CD    1 
ATOM   5045  C  CE    . LYS A 1 627 ? 140.760 114.380 90.039  1.00 39.12 ? 627 LYS A CE    1 
ATOM   5046  N  NZ    . LYS A 1 627 ? 142.187 114.233 89.644  1.00 39.51 ? 627 LYS A NZ    1 
ATOM   5047  N  N     . GLU A 1 628 ? 135.851 116.563 91.484  1.00 36.69 ? 628 GLU A N     1 
ATOM   5048  C  CA    . GLU A 1 628 ? 135.610 116.930 92.870  1.00 36.47 ? 628 GLU A CA    1 
ATOM   5049  C  C     . GLU A 1 628 ? 136.924 117.238 93.580  1.00 39.35 ? 628 GLU A C     1 
ATOM   5050  O  O     . GLU A 1 628 ? 137.977 116.681 93.260  1.00 42.90 ? 628 GLU A O     1 
ATOM   5051  C  CB    . GLU A 1 628 ? 134.863 115.814 93.597  1.00 37.64 ? 628 GLU A CB    1 
ATOM   5052  C  CG    . GLU A 1 628 ? 133.472 115.550 93.046  1.00 39.46 ? 628 GLU A CG    1 
ATOM   5053  C  CD    . GLU A 1 628 ? 132.686 114.569 93.893  1.00 47.51 ? 628 GLU A CD    1 
ATOM   5054  O  OE1   . GLU A 1 628 ? 133.129 114.266 95.021  1.00 43.90 ? 628 GLU A OE1   1 
ATOM   5055  O  OE2   . GLU A 1 628 ? 131.623 114.103 93.432  1.00 43.99 ? 628 GLU A OE2   1 
ATOM   5056  N  N     . ALA A 1 629 ? 136.848 118.148 94.553  1.00 38.52 ? 629 ALA A N     1 
ATOM   5057  C  CA    . ALA A 1 629 ? 138.048 118.599 95.250  1.00 34.49 ? 629 ALA A CA    1 
ATOM   5058  C  C     . ALA A 1 629 ? 138.718 117.473 96.024  1.00 37.26 ? 629 ALA A C     1 
ATOM   5059  O  O     . ALA A 1 629 ? 139.934 117.506 96.237  1.00 45.05 ? 629 ALA A O     1 
ATOM   5060  C  CB    . ALA A 1 629 ? 137.701 119.751 96.190  1.00 34.93 ? 629 ALA A CB    1 
ATOM   5061  N  N     . TYR A 1 630 ? 137.948 116.478 96.463  1.00 42.58 ? 630 TYR A N     1 
ATOM   5062  C  CA    . TYR A 1 630 ? 138.532 115.390 97.238  1.00 42.36 ? 630 TYR A CA    1 
ATOM   5063  C  C     . TYR A 1 630 ? 139.327 114.431 96.363  1.00 44.50 ? 630 TYR A C     1 
ATOM   5064  O  O     . TYR A 1 630 ? 140.263 113.786 96.847  1.00 45.85 ? 630 TYR A O     1 
ATOM   5065  C  CB    . TYR A 1 630 ? 137.436 114.639 97.989  1.00 40.03 ? 630 TYR A CB    1 
ATOM   5066  C  CG    . TYR A 1 630 ? 136.668 115.502 98.961  1.00 41.51 ? 630 TYR A CG    1 
ATOM   5067  C  CD1   . TYR A 1 630 ? 137.214 115.851 100.187 1.00 39.33 ? 630 TYR A CD1   1 
ATOM   5068  C  CD2   . TYR A 1 630 ? 135.398 115.967 98.652  1.00 40.90 ? 630 TYR A CD2   1 
ATOM   5069  C  CE1   . TYR A 1 630 ? 136.517 116.638 101.079 1.00 40.09 ? 630 TYR A CE1   1 
ATOM   5070  C  CE2   . TYR A 1 630 ? 134.693 116.755 99.538  1.00 41.29 ? 630 TYR A CE2   1 
ATOM   5071  C  CZ    . TYR A 1 630 ? 135.258 117.087 100.750 1.00 44.58 ? 630 TYR A CZ    1 
ATOM   5072  O  OH    . TYR A 1 630 ? 134.562 117.872 101.639 1.00 48.41 ? 630 TYR A OH    1 
ATOM   5073  N  N     . ASP A 1 631 ? 138.980 114.325 95.081  1.00 41.52 ? 631 ASP A N     1 
ATOM   5074  C  CA    . ASP A 1 631 ? 139.643 113.383 94.190  1.00 40.98 ? 631 ASP A CA    1 
ATOM   5075  C  C     . ASP A 1 631 ? 140.924 113.930 93.575  1.00 44.93 ? 631 ASP A C     1 
ATOM   5076  O  O     . ASP A 1 631 ? 141.647 113.168 92.925  1.00 48.10 ? 631 ASP A O     1 
ATOM   5077  C  CB    . ASP A 1 631 ? 138.689 112.957 93.071  1.00 43.00 ? 631 ASP A CB    1 
ATOM   5078  C  CG    . ASP A 1 631 ? 137.328 112.542 93.590  1.00 49.51 ? 631 ASP A CG    1 
ATOM   5079  O  OD1   . ASP A 1 631 ? 137.270 111.873 94.642  1.00 48.78 ? 631 ASP A OD1   1 
ATOM   5080  O  OD2   . ASP A 1 631 ? 136.316 112.883 92.942  1.00 51.84 ? 631 ASP A OD2   1 
ATOM   5081  N  N     . MET A 1 632 ? 141.228 115.209 93.760  1.00 39.93 ? 632 MET A N     1 
ATOM   5082  C  CA    . MET A 1 632 ? 142.391 115.815 93.131  1.00 38.03 ? 632 MET A CA    1 
ATOM   5083  C  C     . MET A 1 632 ? 143.549 115.939 94.113  1.00 37.27 ? 632 MET A C     1 
ATOM   5084  O  O     . MET A 1 632 ? 143.377 115.884 95.333  1.00 39.83 ? 632 MET A O     1 
ATOM   5085  C  CB    . MET A 1 632 ? 142.051 117.192 92.555  1.00 38.22 ? 632 MET A CB    1 
ATOM   5086  C  CG    . MET A 1 632 ? 141.110 118.027 93.385  1.00 41.02 ? 632 MET A CG    1 
ATOM   5087  S  SD    . MET A 1 632 ? 140.873 119.660 92.665  1.00 49.08 ? 632 MET A SD    1 
ATOM   5088  C  CE    . MET A 1 632 ? 139.747 119.283 91.328  1.00 34.79 ? 632 MET A CE    1 
ATOM   5089  N  N     . ASP A 1 633 ? 144.743 116.109 93.552  1.00 33.89 ? 633 ASP A N     1 
ATOM   5090  C  CA    . ASP A 1 633 ? 145.952 116.263 94.350  1.00 30.53 ? 633 ASP A CA    1 
ATOM   5091  C  C     . ASP A 1 633 ? 145.947 117.620 95.042  1.00 28.76 ? 633 ASP A C     1 
ATOM   5092  O  O     . ASP A 1 633 ? 145.806 118.658 94.386  1.00 29.95 ? 633 ASP A O     1 
ATOM   5093  C  CB    . ASP A 1 633 ? 147.184 116.119 93.460  1.00 26.20 ? 633 ASP A CB    1 
ATOM   5094  C  CG    . ASP A 1 633 ? 148.464 115.947 94.252  1.00 38.07 ? 633 ASP A CG    1 
ATOM   5095  O  OD1   . ASP A 1 633 ? 148.393 115.839 95.494  1.00 39.48 ? 633 ASP A OD1   1 
ATOM   5096  O  OD2   . ASP A 1 633 ? 149.546 115.926 93.630  1.00 36.17 ? 633 ASP A OD2   1 
ATOM   5097  N  N     . MET A 1 634 ? 146.099 117.615 96.367  1.00 28.02 ? 634 MET A N     1 
ATOM   5098  C  CA    . MET A 1 634 ? 146.159 118.870 97.107  1.00 23.71 ? 634 MET A CA    1 
ATOM   5099  C  C     . MET A 1 634 ? 147.417 119.665 96.795  1.00 25.90 ? 634 MET A C     1 
ATOM   5100  O  O     . MET A 1 634 ? 147.435 120.878 97.019  1.00 27.05 ? 634 MET A O     1 
ATOM   5101  C  CB    . MET A 1 634 ? 146.068 118.606 98.610  1.00 24.09 ? 634 MET A CB    1 
ATOM   5102  C  CG    . MET A 1 634 ? 144.646 118.552 99.140  1.00 29.24 ? 634 MET A CG    1 
ATOM   5103  S  SD    . MET A 1 634 ? 143.664 119.978 98.638  1.00 39.84 ? 634 MET A SD    1 
ATOM   5104  C  CE    . MET A 1 634 ? 142.407 119.187 97.639  1.00 28.32 ? 634 MET A CE    1 
ATOM   5105  N  N     . PHE A 1 635 ? 148.466 119.017 96.284  1.00 25.63 ? 635 PHE A N     1 
ATOM   5106  C  CA    . PHE A 1 635 ? 149.652 119.756 95.865  1.00 21.97 ? 635 PHE A CA    1 
ATOM   5107  C  C     . PHE A 1 635 ? 149.348 120.650 94.670  1.00 21.22 ? 635 PHE A C     1 
ATOM   5108  O  O     . PHE A 1 635 ? 149.808 121.795 94.610  1.00 26.95 ? 635 PHE A O     1 
ATOM   5109  C  CB    . PHE A 1 635 ? 150.789 118.787 95.544  1.00 20.92 ? 635 PHE A CB    1 
ATOM   5110  C  CG    . PHE A 1 635 ? 151.634 118.430 96.734  1.00 27.51 ? 635 PHE A CG    1 
ATOM   5111  C  CD1   . PHE A 1 635 ? 151.058 118.234 97.977  1.00 23.54 ? 635 PHE A CD1   1 
ATOM   5112  C  CD2   . PHE A 1 635 ? 153.005 118.295 96.611  1.00 25.00 ? 635 PHE A CD2   1 
ATOM   5113  C  CE1   . PHE A 1 635 ? 151.831 117.909 99.072  1.00 24.22 ? 635 PHE A CE1   1 
ATOM   5114  C  CE2   . PHE A 1 635 ? 153.783 117.971 97.704  1.00 27.15 ? 635 PHE A CE2   1 
ATOM   5115  C  CZ    . PHE A 1 635 ? 153.195 117.777 98.936  1.00 24.36 ? 635 PHE A CZ    1 
ATOM   5116  N  N     . LYS A 1 636 ? 148.559 120.154 93.716  1.00 26.30 ? 636 LYS A N     1 
ATOM   5117  C  CA    . LYS A 1 636 ? 148.197 120.972 92.565  1.00 25.85 ? 636 LYS A CA    1 
ATOM   5118  C  C     . LYS A 1 636 ? 147.225 122.083 92.948  1.00 23.41 ? 636 LYS A C     1 
ATOM   5119  O  O     . LYS A 1 636 ? 147.291 123.184 92.389  1.00 30.95 ? 636 LYS A O     1 
ATOM   5120  C  CB    . LYS A 1 636 ? 147.612 120.090 91.464  1.00 27.89 ? 636 LYS A CB    1 
ATOM   5121  C  CG    . LYS A 1 636 ? 148.581 119.030 90.966  1.00 26.64 ? 636 LYS A CG    1 
ATOM   5122  C  CD    . LYS A 1 636 ? 148.645 118.994 89.452  1.00 30.84 ? 636 LYS A CD    1 
ATOM   5123  C  CE    . LYS A 1 636 ? 148.464 117.582 88.923  1.00 32.46 ? 636 LYS A CE    1 
ATOM   5124  N  NZ    . LYS A 1 636 ? 148.631 117.524 87.446  1.00 32.99 ? 636 LYS A NZ    1 
ATOM   5125  N  N     . VAL A 1 637 ? 146.329 121.823 93.902  1.00 19.64 ? 637 VAL A N     1 
ATOM   5126  C  CA    . VAL A 1 637 ? 145.463 122.882 94.409  1.00 17.52 ? 637 VAL A CA    1 
ATOM   5127  C  C     . VAL A 1 637 ? 146.288 123.943 95.129  1.00 23.09 ? 637 VAL A C     1 
ATOM   5128  O  O     . VAL A 1 637 ? 146.014 125.144 95.017  1.00 26.82 ? 637 VAL A O     1 
ATOM   5129  C  CB    . VAL A 1 637 ? 144.372 122.291 95.319  1.00 21.13 ? 637 VAL A CB    1 
ATOM   5130  C  CG1   . VAL A 1 637 ? 143.407 123.374 95.769  1.00 21.91 ? 637 VAL A CG1   1 
ATOM   5131  C  CG2   . VAL A 1 637 ? 143.629 121.181 94.597  1.00 24.57 ? 637 VAL A CG2   1 
ATOM   5132  N  N     . VAL A 1 638 ? 147.308 123.519 95.878  1.00 25.70 ? 638 VAL A N     1 
ATOM   5133  C  CA    . VAL A 1 638 ? 148.219 124.468 96.513  1.00 21.58 ? 638 VAL A CA    1 
ATOM   5134  C  C     . VAL A 1 638 ? 148.938 125.292 95.457  1.00 18.15 ? 638 VAL A C     1 
ATOM   5135  O  O     . VAL A 1 638 ? 149.112 126.506 95.608  1.00 32.21 ? 638 VAL A O     1 
ATOM   5136  C  CB    . VAL A 1 638 ? 149.217 123.729 97.425  1.00 21.82 ? 638 VAL A CB    1 
ATOM   5137  C  CG1   . VAL A 1 638 ? 150.445 124.587 97.675  1.00 16.01 ? 638 VAL A CG1   1 
ATOM   5138  C  CG2   . VAL A 1 638 ? 148.562 123.343 98.735  1.00 21.84 ? 638 VAL A CG2   1 
ATOM   5139  N  N     . ASP A 1 639 ? 149.372 124.645 94.375  1.00 13.60 ? 639 ASP A N     1 
ATOM   5140  C  CA    . ASP A 1 639 ? 150.018 125.367 93.284  1.00 17.83 ? 639 ASP A CA    1 
ATOM   5141  C  C     . ASP A 1 639 ? 149.086 126.413 92.689  1.00 23.54 ? 639 ASP A C     1 
ATOM   5142  O  O     . ASP A 1 639 ? 149.500 127.546 92.421  1.00 29.08 ? 639 ASP A O     1 
ATOM   5143  C  CB    . ASP A 1 639 ? 150.473 124.383 92.207  1.00 16.47 ? 639 ASP A CB    1 
ATOM   5144  C  CG    . ASP A 1 639 ? 151.714 123.615 92.606  1.00 30.49 ? 639 ASP A CG    1 
ATOM   5145  O  OD1   . ASP A 1 639 ? 152.603 124.212 93.247  1.00 34.50 ? 639 ASP A OD1   1 
ATOM   5146  O  OD2   . ASP A 1 639 ? 151.800 122.413 92.282  1.00 35.01 ? 639 ASP A OD2   1 
ATOM   5147  N  N     . MET A 1 640 ? 147.818 126.052 92.485  1.00 22.78 ? 640 MET A N     1 
ATOM   5148  C  CA    . MET A 1 640 ? 146.852 126.998 91.934  1.00 21.35 ? 640 MET A CA    1 
ATOM   5149  C  C     . MET A 1 640 ? 146.628 128.178 92.876  1.00 22.57 ? 640 MET A C     1 
ATOM   5150  O  O     . MET A 1 640 ? 146.627 129.340 92.449  1.00 25.21 ? 640 MET A O     1 
ATOM   5151  C  CB    . MET A 1 640 ? 145.535 126.280 91.645  1.00 23.71 ? 640 MET A CB    1 
ATOM   5152  C  CG    . MET A 1 640 ? 144.354 127.207 91.429  1.00 23.96 ? 640 MET A CG    1 
ATOM   5153  S  SD    . MET A 1 640 ? 144.431 128.074 89.855  1.00 24.60 ? 640 MET A SD    1 
ATOM   5154  C  CE    . MET A 1 640 ? 143.412 127.012 88.842  1.00 25.54 ? 640 MET A CE    1 
ATOM   5155  N  N     . ILE A 1 641 ? 146.448 127.897 94.168  1.00 22.52 ? 641 ILE A N     1 
ATOM   5156  C  CA    . ILE A 1 641 ? 146.180 128.965 95.126  1.00 16.89 ? 641 ILE A CA    1 
ATOM   5157  C  C     . ILE A 1 641 ? 147.397 129.868 95.277  1.00 18.04 ? 641 ILE A C     1 
ATOM   5158  O  O     . ILE A 1 641 ? 147.265 131.087 95.436  1.00 26.34 ? 641 ILE A O     1 
ATOM   5159  C  CB    . ILE A 1 641 ? 145.730 128.374 96.475  1.00 24.38 ? 641 ILE A CB    1 
ATOM   5160  C  CG1   . ILE A 1 641 ? 144.462 127.540 96.296  1.00 22.92 ? 641 ILE A CG1   1 
ATOM   5161  C  CG2   . ILE A 1 641 ? 145.471 129.475 97.490  1.00 15.87 ? 641 ILE A CG2   1 
ATOM   5162  C  CD1   . ILE A 1 641 ? 143.375 128.236 95.511  1.00 19.44 ? 641 ILE A CD1   1 
ATOM   5163  N  N     . ALA A 1 642 ? 148.600 129.293 95.220  1.00 13.27 ? 642 ALA A N     1 
ATOM   5164  C  CA    . ALA A 1 642 ? 149.814 130.096 95.290  1.00 15.32 ? 642 ALA A CA    1 
ATOM   5165  C  C     . ALA A 1 642 ? 150.005 130.930 94.033  1.00 15.19 ? 642 ALA A C     1 
ATOM   5166  O  O     . ALA A 1 642 ? 150.536 132.043 94.105  1.00 24.79 ? 642 ALA A O     1 
ATOM   5167  C  CB    . ALA A 1 642 ? 151.024 129.194 95.521  1.00 16.31 ? 642 ALA A CB    1 
ATOM   5168  N  N     . THR A 1 643 ? 149.595 130.408 92.875  1.00 18.17 ? 643 THR A N     1 
ATOM   5169  C  CA    . THR A 1 643 ? 149.607 131.213 91.661  1.00 20.31 ? 643 THR A CA    1 
ATOM   5170  C  C     . THR A 1 643 ? 148.654 132.394 91.783  1.00 18.50 ? 643 THR A C     1 
ATOM   5171  O  O     . THR A 1 643 ? 148.990 133.518 91.393  1.00 22.00 ? 643 THR A O     1 
ATOM   5172  C  CB    . THR A 1 643 ? 149.244 130.347 90.454  1.00 22.24 ? 643 THR A CB    1 
ATOM   5173  O  OG1   . THR A 1 643 ? 150.253 129.349 90.263  1.00 29.18 ? 643 THR A OG1   1 
ATOM   5174  C  CG2   . THR A 1 643 ? 149.137 131.193 89.202  1.00 18.12 ? 643 THR A CG2   1 
ATOM   5175  N  N     . ILE A 1 644 ? 147.461 132.161 92.332  1.00 15.70 ? 644 ILE A N     1 
ATOM   5176  C  CA    . ILE A 1 644 ? 146.524 133.259 92.540  1.00 14.76 ? 644 ILE A CA    1 
ATOM   5177  C  C     . ILE A 1 644 ? 147.025 134.193 93.637  1.00 18.29 ? 644 ILE A C     1 
ATOM   5178  O  O     . ILE A 1 644 ? 146.887 135.418 93.538  1.00 23.00 ? 644 ILE A O     1 
ATOM   5179  C  CB    . ILE A 1 644 ? 145.120 132.715 92.857  1.00 16.20 ? 644 ILE A CB    1 
ATOM   5180  C  CG1   . ILE A 1 644 ? 144.608 131.848 91.708  1.00 14.07 ? 644 ILE A CG1   1 
ATOM   5181  C  CG2   . ILE A 1 644 ? 144.157 133.854 93.117  1.00 8.59  ? 644 ILE A CG2   1 
ATOM   5182  C  CD1   . ILE A 1 644 ? 143.422 130.994 92.080  1.00 21.17 ? 644 ILE A CD1   1 
ATOM   5183  N  N     . GLN A 1 645 ? 147.620 133.632 94.694  1.00 11.95 ? 645 GLN A N     1 
ATOM   5184  C  CA    . GLN A 1 645 ? 147.998 134.430 95.857  1.00 11.59 ? 645 GLN A CA    1 
ATOM   5185  C  C     . GLN A 1 645 ? 149.043 135.486 95.519  1.00 19.34 ? 645 GLN A C     1 
ATOM   5186  O  O     . GLN A 1 645 ? 149.091 136.537 96.167  1.00 23.88 ? 645 GLN A O     1 
ATOM   5187  C  CB    . GLN A 1 645 ? 148.509 133.519 96.973  1.00 9.04  ? 645 GLN A CB    1 
ATOM   5188  C  CG    . GLN A 1 645 ? 148.854 134.235 98.268  1.00 10.60 ? 645 GLN A CG    1 
ATOM   5189  C  CD    . GLN A 1 645 ? 147.648 134.875 98.920  1.00 12.88 ? 645 GLN A CD    1 
ATOM   5190  O  OE1   . GLN A 1 645 ? 146.916 134.226 99.664  1.00 18.52 ? 645 GLN A OE1   1 
ATOM   5191  N  NE2   . GLN A 1 645 ? 147.440 136.157 98.650  1.00 4.86  ? 645 GLN A NE2   1 
ATOM   5192  N  N     . GLN A 1 646 ? 149.879 135.237 94.512  1.00 21.25 ? 646 GLN A N     1 
ATOM   5193  C  CA    . GLN A 1 646 ? 150.922 136.196 94.172  1.00 14.92 ? 646 GLN A CA    1 
ATOM   5194  C  C     . GLN A 1 646 ? 150.370 137.500 93.611  1.00 15.83 ? 646 GLN A C     1 
ATOM   5195  O  O     . GLN A 1 646 ? 151.106 138.490 93.562  1.00 21.15 ? 646 GLN A O     1 
ATOM   5196  C  CB    . GLN A 1 646 ? 151.906 135.570 93.184  1.00 20.38 ? 646 GLN A CB    1 
ATOM   5197  C  CG    . GLN A 1 646 ? 151.455 135.591 91.742  1.00 22.68 ? 646 GLN A CG    1 
ATOM   5198  C  CD    . GLN A 1 646 ? 152.391 134.820 90.835  1.00 30.21 ? 646 GLN A CD    1 
ATOM   5199  O  OE1   . GLN A 1 646 ? 151.998 133.836 90.210  1.00 24.34 ? 646 GLN A OE1   1 
ATOM   5200  N  NE2   . GLN A 1 646 ? 153.639 135.265 90.759  1.00 27.44 ? 646 GLN A NE2   1 
ATOM   5201  N  N     . HIS A 1 647 ? 149.104 137.531 93.203  1.00 21.73 ? 647 HIS A N     1 
ATOM   5202  C  CA    . HIS A 1 647 ? 148.461 138.748 92.730  1.00 14.60 ? 647 HIS A CA    1 
ATOM   5203  C  C     . HIS A 1 647 ? 147.445 139.301 93.717  1.00 15.15 ? 647 HIS A C     1 
ATOM   5204  O  O     . HIS A 1 647 ? 146.799 140.311 93.421  1.00 24.96 ? 647 HIS A O     1 
ATOM   5205  C  CB    . HIS A 1 647 ? 147.783 138.496 91.380  1.00 11.86 ? 647 HIS A CB    1 
ATOM   5206  C  CG    . HIS A 1 647 ? 148.688 137.886 90.358  1.00 16.28 ? 647 HIS A CG    1 
ATOM   5207  N  ND1   . HIS A 1 647 ? 149.831 138.510 89.910  1.00 19.27 ? 647 HIS A ND1   1 
ATOM   5208  C  CD2   . HIS A 1 647 ? 148.620 136.707 89.698  1.00 16.71 ? 647 HIS A CD2   1 
ATOM   5209  C  CE1   . HIS A 1 647 ? 150.429 137.742 89.018  1.00 20.77 ? 647 HIS A CE1   1 
ATOM   5210  N  NE2   . HIS A 1 647 ? 149.713 136.642 88.870  1.00 20.25 ? 647 HIS A NE2   1 
ATOM   5211  N  N     . ILE A 1 648 ? 147.285 138.669 94.875  1.00 12.89 ? 648 ILE A N     1 
ATOM   5212  C  CA    . ILE A 1 648 ? 146.321 139.081 95.889  1.00 12.29 ? 648 ILE A CA    1 
ATOM   5213  C  C     . ILE A 1 648 ? 147.104 139.650 97.064  1.00 13.58 ? 648 ILE A C     1 
ATOM   5214  O  O     . ILE A 1 648 ? 147.985 138.978 97.613  1.00 25.13 ? 648 ILE A O     1 
ATOM   5215  C  CB    . ILE A 1 648 ? 145.431 137.907 96.326  1.00 10.06 ? 648 ILE A CB    1 
ATOM   5216  C  CG1   . ILE A 1 648 ? 144.715 137.297 95.118  1.00 11.93 ? 648 ILE A CG1   1 
ATOM   5217  C  CG2   . ILE A 1 648 ? 144.419 138.350 97.367  1.00 5.15  ? 648 ILE A CG2   1 
ATOM   5218  C  CD1   . ILE A 1 648 ? 143.634 138.176 94.538  1.00 5.64  ? 648 ILE A CD1   1 
ATOM   5219  N  N     . ASP A 1 649 ? 146.792 140.891 97.447  1.00 9.32  ? 649 ASP A N     1 
ATOM   5220  C  CA    . ASP A 1 649 ? 147.542 141.528 98.526  1.00 7.33  ? 649 ASP A CA    1 
ATOM   5221  C  C     . ASP A 1 649 ? 147.185 140.939 99.882  1.00 8.77  ? 649 ASP A C     1 
ATOM   5222  O  O     . ASP A 1 649 ? 148.053 140.819 100.753 1.00 26.91 ? 649 ASP A O     1 
ATOM   5223  C  CB    . ASP A 1 649 ? 147.304 143.038 98.522  1.00 17.78 ? 649 ASP A CB    1 
ATOM   5224  C  CG    . ASP A 1 649 ? 145.851 143.400 98.317  1.00 19.43 ? 649 ASP A CG    1 
ATOM   5225  O  OD1   . ASP A 1 649 ? 145.390 143.377 97.159  1.00 24.80 ? 649 ASP A OD1   1 
ATOM   5226  O  OD2   . ASP A 1 649 ? 145.169 143.712 99.312  1.00 20.28 ? 649 ASP A OD2   1 
ATOM   5227  N  N     . GLN A 1 650 ? 145.924 140.585 100.084 1.00 13.08 ? 650 GLN A N     1 
ATOM   5228  C  CA    . GLN A 1 650 ? 145.487 139.882 101.280 1.00 4.25  ? 650 GLN A CA    1 
ATOM   5229  C  C     . GLN A 1 650 ? 145.530 138.378 101.003 1.00 10.45 ? 650 GLN A C     1 
ATOM   5230  O  O     . GLN A 1 650 ? 146.141 137.932 100.029 1.00 20.61 ? 650 GLN A O     1 
ATOM   5231  C  CB    . GLN A 1 650 ? 144.110 140.389 101.706 1.00 5.28  ? 650 GLN A CB    1 
ATOM   5232  C  CG    . GLN A 1 650 ? 144.066 141.884 101.964 1.00 8.65  ? 650 GLN A CG    1 
ATOM   5233  C  CD    . GLN A 1 650 ? 142.733 142.342 102.510 1.00 14.15 ? 650 GLN A CD    1 
ATOM   5234  O  OE1   . GLN A 1 650 ? 142.387 142.051 103.653 1.00 15.95 ? 650 GLN A OE1   1 
ATOM   5235  N  NE2   . GLN A 1 650 ? 141.977 143.066 101.696 1.00 4.34  ? 650 GLN A NE2   1 
ATOM   5236  N  N     . GLY A 1 651 ? 144.913 137.574 101.866 1.00 10.73 ? 651 GLY A N     1 
ATOM   5237  C  CA    . GLY A 1 651 ? 144.950 136.136 101.735 1.00 5.85  ? 651 GLY A CA    1 
ATOM   5238  C  C     . GLY A 1 651 ? 143.773 135.567 100.958 1.00 5.21  ? 651 GLY A C     1 
ATOM   5239  O  O     . GLY A 1 651 ? 142.889 136.271 100.478 1.00 10.79 ? 651 GLY A O     1 
ATOM   5240  N  N     . ILE A 1 652 ? 143.790 134.243 100.841 1.00 12.91 ? 652 ILE A N     1 
ATOM   5241  C  CA    . ILE A 1 652 ? 142.754 133.473 100.168 1.00 3.24  ? 652 ILE A CA    1 
ATOM   5242  C  C     . ILE A 1 652 ? 142.285 132.394 101.130 1.00 11.86 ? 652 ILE A C     1 
ATOM   5243  O  O     . ILE A 1 652 ? 143.107 131.672 101.701 1.00 26.33 ? 652 ILE A O     1 
ATOM   5244  C  CB    . ILE A 1 652 ? 143.272 132.843 98.861  1.00 7.06  ? 652 ILE A CB    1 
ATOM   5245  C  CG1   . ILE A 1 652 ? 143.881 133.911 97.951  1.00 3.93  ? 652 ILE A CG1   1 
ATOM   5246  C  CG2   . ILE A 1 652 ? 142.164 132.090 98.152  1.00 11.98 ? 652 ILE A CG2   1 
ATOM   5247  C  CD1   . ILE A 1 652 ? 144.480 133.357 96.689  1.00 5.34  ? 652 ILE A CD1   1 
ATOM   5248  N  N     . SER A 1 653 ? 140.973 132.288 101.314 1.00 11.68 ? 653 SER A N     1 
ATOM   5249  C  CA    . SER A 1 653 ? 140.409 131.265 102.192 1.00 13.23 ? 653 SER A CA    1 
ATOM   5250  C  C     . SER A 1 653 ? 140.627 129.905 101.547 1.00 18.13 ? 653 SER A C     1 
ATOM   5251  O  O     . SER A 1 653 ? 139.867 129.489 100.673 1.00 21.51 ? 653 SER A O     1 
ATOM   5252  C  CB    . SER A 1 653 ? 138.930 131.527 102.439 1.00 14.30 ? 653 SER A CB    1 
ATOM   5253  O  OG    . SER A 1 653 ? 138.733 132.229 103.650 1.00 21.56 ? 653 SER A OG    1 
ATOM   5254  N  N     . PHE A 1 654 ? 141.663 129.201 101.990 1.00 22.21 ? 654 PHE A N     1 
ATOM   5255  C  CA    . PHE A 1 654 ? 142.133 127.980 101.346 1.00 10.61 ? 654 PHE A CA    1 
ATOM   5256  C  C     . PHE A 1 654 ? 141.698 126.780 102.178 1.00 13.13 ? 654 PHE A C     1 
ATOM   5257  O  O     . PHE A 1 654 ? 142.280 126.502 103.231 1.00 22.28 ? 654 PHE A O     1 
ATOM   5258  C  CB    . PHE A 1 654 ? 143.651 128.021 101.183 1.00 16.55 ? 654 PHE A CB    1 
ATOM   5259  C  CG    . PHE A 1 654 ? 144.214 126.878 100.393 1.00 17.38 ? 654 PHE A CG    1 
ATOM   5260  C  CD1   . PHE A 1 654 ? 143.403 126.100 99.588  1.00 18.60 ? 654 PHE A CD1   1 
ATOM   5261  C  CD2   . PHE A 1 654 ? 145.563 126.588 100.453 1.00 21.62 ? 654 PHE A CD2   1 
ATOM   5262  C  CE1   . PHE A 1 654 ? 143.926 125.053 98.865  1.00 18.51 ? 654 PHE A CE1   1 
ATOM   5263  C  CE2   . PHE A 1 654 ? 146.090 125.545 99.729  1.00 21.58 ? 654 PHE A CE2   1 
ATOM   5264  C  CZ    . PHE A 1 654 ? 145.271 124.776 98.934  1.00 20.71 ? 654 PHE A CZ    1 
ATOM   5265  N  N     . THR A 1 655 ? 140.690 126.063 101.692 1.00 21.54 ? 655 THR A N     1 
ATOM   5266  C  CA    . THR A 1 655 ? 140.213 124.851 102.341 1.00 23.12 ? 655 THR A CA    1 
ATOM   5267  C  C     . THR A 1 655 ? 140.965 123.644 101.795 1.00 26.49 ? 655 THR A C     1 
ATOM   5268  O  O     . THR A 1 655 ? 141.142 123.512 100.580 1.00 26.77 ? 655 THR A O     1 
ATOM   5269  C  CB    . THR A 1 655 ? 138.709 124.681 102.121 1.00 23.71 ? 655 THR A CB    1 
ATOM   5270  O  OG1   . THR A 1 655 ? 138.011 125.773 102.731 1.00 32.15 ? 655 THR A OG1   1 
ATOM   5271  C  CG2   . THR A 1 655 ? 138.221 123.376 102.726 1.00 26.58 ? 655 THR A CG2   1 
ATOM   5272  N  N     . LEU A 1 656 ? 141.415 122.774 102.694 1.00 30.32 ? 656 LEU A N     1 
ATOM   5273  C  CA    . LEU A 1 656 ? 142.066 121.531 102.309 1.00 29.72 ? 656 LEU A CA    1 
ATOM   5274  C  C     . LEU A 1 656 ? 141.040 120.408 102.284 1.00 28.65 ? 656 LEU A C     1 
ATOM   5275  O  O     . LEU A 1 656 ? 140.344 120.170 103.275 1.00 28.61 ? 656 LEU A O     1 
ATOM   5276  C  CB    . LEU A 1 656 ? 143.201 121.185 103.273 1.00 29.83 ? 656 LEU A CB    1 
ATOM   5277  C  CG    . LEU A 1 656 ? 144.409 122.117 103.254 1.00 32.42 ? 656 LEU A CG    1 
ATOM   5278  C  CD1   . LEU A 1 656 ? 145.538 121.535 104.084 1.00 30.10 ? 656 LEU A CD1   1 
ATOM   5279  C  CD2   . LEU A 1 656 ? 144.866 122.388 101.829 1.00 28.23 ? 656 LEU A CD2   1 
ATOM   5280  N  N     . PHE A 1 657 ? 140.954 119.721 101.152 1.00 27.83 ? 657 PHE A N     1 
ATOM   5281  C  CA    . PHE A 1 657 ? 139.983 118.655 100.948 1.00 27.55 ? 657 PHE A CA    1 
ATOM   5282  C  C     . PHE A 1 657 ? 140.714 117.321 101.042 1.00 34.69 ? 657 PHE A C     1 
ATOM   5283  O  O     . PHE A 1 657 ? 141.488 116.963 100.149 1.00 38.33 ? 657 PHE A O     1 
ATOM   5284  C  CB    . PHE A 1 657 ? 139.283 118.825 99.604  1.00 29.33 ? 657 PHE A CB    1 
ATOM   5285  C  CG    . PHE A 1 657 ? 138.668 120.181 99.420  1.00 34.16 ? 657 PHE A CG    1 
ATOM   5286  C  CD1   . PHE A 1 657 ? 137.384 120.438 99.864  1.00 30.88 ? 657 PHE A CD1   1 
ATOM   5287  C  CD2   . PHE A 1 657 ? 139.380 121.205 98.816  1.00 35.54 ? 657 PHE A CD2   1 
ATOM   5288  C  CE1   . PHE A 1 657 ? 136.817 121.685 99.700  1.00 33.55 ? 657 PHE A CE1   1 
ATOM   5289  C  CE2   . PHE A 1 657 ? 138.817 122.453 98.649  1.00 32.12 ? 657 PHE A CE2   1 
ATOM   5290  C  CZ    . PHE A 1 657 ? 137.534 122.693 99.093  1.00 33.18 ? 657 PHE A CZ    1 
ATOM   5291  N  N     . LEU A 1 658 ? 140.461 116.590 102.122 1.00 42.19 ? 658 LEU A N     1 
ATOM   5292  C  CA    . LEU A 1 658 ? 141.223 115.402 102.470 1.00 41.18 ? 658 LEU A CA    1 
ATOM   5293  C  C     . LEU A 1 658 ? 140.354 114.157 102.364 1.00 45.13 ? 658 LEU A C     1 
ATOM   5294  O  O     . LEU A 1 658 ? 139.167 114.184 102.702 1.00 48.31 ? 658 LEU A O     1 
ATOM   5295  C  CB    . LEU A 1 658 ? 141.780 115.518 103.890 1.00 39.46 ? 658 LEU A CB    1 
ATOM   5296  C  CG    . LEU A 1 658 ? 142.241 116.906 104.330 1.00 38.71 ? 658 LEU A CG    1 
ATOM   5297  C  CD1   . LEU A 1 658 ? 142.382 116.954 105.838 1.00 37.95 ? 658 LEU A CD1   1 
ATOM   5298  C  CD2   . LEU A 1 658 ? 143.549 117.275 103.655 1.00 40.81 ? 658 LEU A CD2   1 
ATOM   5299  N  N     . LYS A 1 659 ? 140.949 113.071 101.885 1.00 48.90 ? 659 LYS A N     1 
ATOM   5300  C  CA    . LYS A 1 659 ? 140.287 111.780 101.925 1.00 49.60 ? 659 LYS A CA    1 
ATOM   5301  C  C     . LYS A 1 659 ? 140.496 111.123 103.286 1.00 50.34 ? 659 LYS A C     1 
ATOM   5302  O  O     . LYS A 1 659 ? 141.371 111.509 104.064 1.00 53.66 ? 659 LYS A O     1 
ATOM   5303  C  CB    . LYS A 1 659 ? 140.807 110.868 100.815 1.00 51.08 ? 659 LYS A CB    1 
ATOM   5304  C  CG    . LYS A 1 659 ? 140.346 111.258 99.423  1.00 50.91 ? 659 LYS A CG    1 
ATOM   5305  C  CD    . LYS A 1 659 ? 140.712 110.192 98.405  1.00 50.95 ? 659 LYS A CD    1 
ATOM   5306  C  CE    . LYS A 1 659 ? 140.168 110.533 97.029  1.00 50.58 ? 659 LYS A CE    1 
ATOM   5307  N  NZ    . LYS A 1 659 ? 140.147 109.347 96.131  1.00 50.14 ? 659 LYS A NZ    1 
ATOM   5308  N  N     . ASP A 1 660 ? 139.665 110.121 103.573 1.00 56.69 ? 660 ASP A N     1 
ATOM   5309  C  CA    . ASP A 1 660 ? 139.820 109.365 104.809 1.00 56.18 ? 660 ASP A CA    1 
ATOM   5310  C  C     . ASP A 1 660 ? 141.097 108.535 104.821 1.00 57.16 ? 660 ASP A C     1 
ATOM   5311  O  O     . ASP A 1 660 ? 141.625 108.249 105.901 1.00 56.69 ? 660 ASP A O     1 
ATOM   5312  C  CB    . ASP A 1 660 ? 138.609 108.457 105.026 1.00 57.83 ? 660 ASP A CB    1 
ATOM   5313  C  CG    . ASP A 1 660 ? 137.629 109.023 106.032 1.00 58.05 ? 660 ASP A CG    1 
ATOM   5314  O  OD1   . ASP A 1 660 ? 136.561 108.410 106.234 1.00 57.38 ? 660 ASP A OD1   1 
ATOM   5315  O  OD2   . ASP A 1 660 ? 137.930 110.078 106.626 1.00 56.10 ? 660 ASP A OD2   1 
ATOM   5316  N  N     . THR A 1 661 ? 141.604 108.151 103.648 1.00 55.18 ? 661 THR A N     1 
ATOM   5317  C  CA    . THR A 1 661 ? 142.762 107.267 103.588 1.00 54.76 ? 661 THR A CA    1 
ATOM   5318  C  C     . THR A 1 661 ? 144.044 107.962 104.030 1.00 55.24 ? 661 THR A C     1 
ATOM   5319  O  O     . THR A 1 661 ? 144.908 107.326 104.643 1.00 58.08 ? 661 THR A O     1 
ATOM   5320  C  CB    . THR A 1 661 ? 142.930 106.718 102.172 1.00 56.00 ? 661 THR A CB    1 
ATOM   5321  O  OG1   . THR A 1 661 ? 142.572 107.729 101.221 1.00 55.86 ? 661 THR A OG1   1 
ATOM   5322  C  CG2   . THR A 1 661 ? 142.042 105.501 101.966 1.00 55.72 ? 661 THR A CG2   1 
ATOM   5323  N  N     . MET A 1 662 ? 144.192 109.250 103.732 1.00 53.82 ? 662 MET A N     1 
ATOM   5324  C  CA    . MET A 1 662 ? 145.438 109.945 104.020 1.00 54.01 ? 662 MET A CA    1 
ATOM   5325  C  C     . MET A 1 662 ? 145.597 110.173 105.518 1.00 52.76 ? 662 MET A C     1 
ATOM   5326  O  O     . MET A 1 662 ? 144.624 110.431 106.233 1.00 52.95 ? 662 MET A O     1 
ATOM   5327  C  CB    . MET A 1 662 ? 145.505 111.276 103.269 1.00 52.25 ? 662 MET A CB    1 
ATOM   5328  C  CG    . MET A 1 662 ? 144.421 112.273 103.620 1.00 53.21 ? 662 MET A CG    1 
ATOM   5329  S  SD    . MET A 1 662 ? 144.581 113.805 102.681 1.00 61.43 ? 662 MET A SD    1 
ATOM   5330  C  CE    . MET A 1 662 ? 145.434 113.231 101.214 1.00 50.18 ? 662 MET A CE    1 
ATOM   5331  N  N     . THR A 1 663 ? 146.837 110.070 105.988 1.00 44.74 ? 663 THR A N     1 
ATOM   5332  C  CA    . THR A 1 663 ? 147.151 110.134 107.406 1.00 45.03 ? 663 THR A CA    1 
ATOM   5333  C  C     . THR A 1 663 ? 147.405 111.583 107.818 1.00 46.29 ? 663 THR A C     1 
ATOM   5334  O  O     . THR A 1 663 ? 147.204 112.519 107.040 1.00 49.37 ? 663 THR A O     1 
ATOM   5335  C  CB    . THR A 1 663 ? 148.353 109.245 107.712 1.00 44.03 ? 663 THR A CB    1 
ATOM   5336  O  OG1   . THR A 1 663 ? 149.537 109.842 107.171 1.00 41.55 ? 663 THR A OG1   1 
ATOM   5337  C  CG2   . THR A 1 663 ? 148.164 107.874 107.084 1.00 45.94 ? 663 THR A CG2   1 
ATOM   5338  N  N     . THR A 1 664 ? 147.845 111.785 109.063 1.00 39.78 ? 664 THR A N     1 
ATOM   5339  C  CA    . THR A 1 664 ? 148.225 113.125 109.493 1.00 41.62 ? 664 THR A CA    1 
ATOM   5340  C  C     . THR A 1 664 ? 149.519 113.573 108.829 1.00 40.41 ? 664 THR A C     1 
ATOM   5341  O  O     . THR A 1 664 ? 149.754 114.778 108.681 1.00 42.84 ? 664 THR A O     1 
ATOM   5342  C  CB    . THR A 1 664 ? 148.368 113.182 111.014 1.00 41.64 ? 664 THR A CB    1 
ATOM   5343  O  OG1   . THR A 1 664 ? 149.405 112.289 111.435 1.00 41.35 ? 664 THR A OG1   1 
ATOM   5344  C  CG2   . THR A 1 664 ? 147.062 112.795 111.688 1.00 40.22 ? 664 THR A CG2   1 
ATOM   5345  N  N     . ARG A 1 665 ? 150.368 112.624 108.428 1.00 40.84 ? 665 ARG A N     1 
ATOM   5346  C  CA    . ARG A 1 665 ? 151.587 112.980 107.712 1.00 39.24 ? 665 ARG A CA    1 
ATOM   5347  C  C     . ARG A 1 665 ? 151.270 113.615 106.367 1.00 41.65 ? 665 ARG A C     1 
ATOM   5348  O  O     . ARG A 1 665 ? 151.961 114.541 105.935 1.00 43.16 ? 665 ARG A O     1 
ATOM   5349  C  CB    . ARG A 1 665 ? 152.471 111.749 107.521 1.00 39.58 ? 665 ARG A CB    1 
ATOM   5350  C  CG    . ARG A 1 665 ? 153.765 112.043 106.785 1.00 38.22 ? 665 ARG A CG    1 
ATOM   5351  C  CD    . ARG A 1 665 ? 154.682 110.839 106.768 1.00 39.56 ? 665 ARG A CD    1 
ATOM   5352  N  NE    . ARG A 1 665 ? 155.752 110.981 105.789 1.00 42.11 ? 665 ARG A NE    1 
ATOM   5353  C  CZ    . ARG A 1 665 ? 155.595 110.845 104.479 1.00 45.39 ? 665 ARG A CZ    1 
ATOM   5354  N  NH1   . ARG A 1 665 ? 154.418 110.554 103.950 1.00 44.30 ? 665 ARG A NH1   1 
ATOM   5355  N  NH2   . ARG A 1 665 ? 156.646 111.003 103.680 1.00 42.48 ? 665 ARG A NH2   1 
ATOM   5356  N  N     . ASP A 1 666 ? 150.234 113.126 105.683 1.00 39.11 ? 666 ASP A N     1 
ATOM   5357  C  CA    . ASP A 1 666 ? 149.846 113.727 104.412 1.00 35.33 ? 666 ASP A CA    1 
ATOM   5358  C  C     . ASP A 1 666 ? 149.337 115.151 104.604 1.00 37.69 ? 666 ASP A C     1 
ATOM   5359  O  O     . ASP A 1 666 ? 149.655 116.043 103.810 1.00 40.14 ? 666 ASP A O     1 
ATOM   5360  C  CB    . ASP A 1 666 ? 148.791 112.862 103.724 1.00 40.89 ? 666 ASP A CB    1 
ATOM   5361  C  CG    . ASP A 1 666 ? 149.320 111.493 103.347 1.00 45.44 ? 666 ASP A CG    1 
ATOM   5362  O  OD1   . ASP A 1 666 ? 150.422 111.421 102.765 1.00 45.27 ? 666 ASP A OD1   1 
ATOM   5363  O  OD2   . ASP A 1 666 ? 148.636 110.489 103.632 1.00 45.03 ? 666 ASP A OD2   1 
ATOM   5364  N  N     . LEU A 1 667 ? 148.547 115.383 105.654 1.00 36.75 ? 667 LEU A N     1 
ATOM   5365  C  CA    . LEU A 1 667 ? 148.085 116.734 105.949 1.00 31.14 ? 667 LEU A CA    1 
ATOM   5366  C  C     . LEU A 1 667 ? 149.260 117.648 106.281 1.00 30.06 ? 667 LEU A C     1 
ATOM   5367  O  O     . LEU A 1 667 ? 149.312 118.799 105.831 1.00 35.60 ? 667 LEU A O     1 
ATOM   5368  C  CB    . LEU A 1 667 ? 147.078 116.691 107.102 1.00 35.01 ? 667 LEU A CB    1 
ATOM   5369  C  CG    . LEU A 1 667 ? 146.446 117.961 107.682 1.00 36.35 ? 667 LEU A CG    1 
ATOM   5370  C  CD1   . LEU A 1 667 ? 146.258 119.045 106.631 1.00 35.30 ? 667 LEU A CD1   1 
ATOM   5371  C  CD2   . LEU A 1 667 ? 145.121 117.630 108.345 1.00 33.24 ? 667 LEU A CD2   1 
ATOM   5372  N  N     . ASN A 1 668 ? 150.223 117.143 107.055 1.00 32.51 ? 668 ASN A N     1 
ATOM   5373  C  CA    . ASN A 1 668 ? 151.410 117.931 107.372 1.00 26.57 ? 668 ASN A CA    1 
ATOM   5374  C  C     . ASN A 1 668 ? 152.225 118.232 106.122 1.00 26.89 ? 668 ASN A C     1 
ATOM   5375  O  O     . ASN A 1 668 ? 152.767 119.332 105.977 1.00 33.54 ? 668 ASN A O     1 
ATOM   5376  C  CB    . ASN A 1 668 ? 152.262 117.197 108.406 1.00 27.63 ? 668 ASN A CB    1 
ATOM   5377  C  CG    . ASN A 1 668 ? 151.966 117.639 109.821 1.00 30.63 ? 668 ASN A CG    1 
ATOM   5378  O  OD1   . ASN A 1 668 ? 151.457 118.735 110.047 1.00 32.62 ? 668 ASN A OD1   1 
ATOM   5379  N  ND2   . ASN A 1 668 ? 152.276 116.782 110.785 1.00 36.88 ? 668 ASN A ND2   1 
ATOM   5380  N  N     . ARG A 1 669 ? 152.333 117.263 105.212 1.00 30.66 ? 669 ARG A N     1 
ATOM   5381  C  CA    . ARG A 1 669 ? 153.042 117.490 103.958 1.00 31.69 ? 669 ARG A CA    1 
ATOM   5382  C  C     . ARG A 1 669 ? 152.347 118.549 103.117 1.00 27.17 ? 669 ARG A C     1 
ATOM   5383  O  O     . ARG A 1 669 ? 153.007 119.391 102.499 1.00 31.75 ? 669 ARG A O     1 
ATOM   5384  C  CB    . ARG A 1 669 ? 153.161 116.183 103.176 1.00 28.48 ? 669 ARG A CB    1 
ATOM   5385  C  CG    . ARG A 1 669 ? 154.258 115.259 103.661 1.00 30.06 ? 669 ARG A CG    1 
ATOM   5386  C  CD    . ARG A 1 669 ? 154.720 114.341 102.546 1.00 34.76 ? 669 ARG A CD    1 
ATOM   5387  N  NE    . ARG A 1 669 ? 155.637 115.008 101.631 1.00 33.79 ? 669 ARG A NE    1 
ATOM   5388  C  CZ    . ARG A 1 669 ? 155.551 114.946 100.309 1.00 33.33 ? 669 ARG A CZ    1 
ATOM   5389  N  NH1   . ARG A 1 669 ? 154.593 114.259 99.710  1.00 33.75 ? 669 ARG A NH1   1 
ATOM   5390  N  NH2   . ARG A 1 669 ? 156.448 115.593 99.570  1.00 33.32 ? 669 ARG A NH2   1 
ATOM   5391  N  N     . ILE A 1 670 ? 151.014 118.518 103.073 1.00 23.36 ? 670 ILE A N     1 
ATOM   5392  C  CA    . ILE A 1 670 ? 150.277 119.548 102.345 1.00 28.26 ? 670 ILE A CA    1 
ATOM   5393  C  C     . ILE A 1 670 ? 150.519 120.916 102.969 1.00 30.67 ? 670 ILE A C     1 
ATOM   5394  O  O     . ILE A 1 670 ? 150.727 121.908 102.261 1.00 28.63 ? 670 ILE A O     1 
ATOM   5395  C  CB    . ILE A 1 670 ? 148.776 119.205 102.292 1.00 28.38 ? 670 ILE A CB    1 
ATOM   5396  C  CG1   . ILE A 1 670 ? 148.548 117.920 101.497 1.00 30.04 ? 670 ILE A CG1   1 
ATOM   5397  C  CG2   . ILE A 1 670 ? 147.992 120.344 101.668 1.00 28.11 ? 670 ILE A CG2   1 
ATOM   5398  C  CD1   . ILE A 1 670 ? 147.246 117.229 101.821 1.00 29.41 ? 670 ILE A CD1   1 
ATOM   5399  N  N     . ASP A 1 671 ? 150.502 120.991 104.302 1.00 28.80 ? 671 ASP A N     1 
ATOM   5400  C  CA    . ASP A 1 671 ? 150.753 122.263 104.978 1.00 23.05 ? 671 ASP A CA    1 
ATOM   5401  C  C     . ASP A 1 671 ? 152.162 122.776 104.698 1.00 23.56 ? 671 ASP A C     1 
ATOM   5402  O  O     . ASP A 1 671 ? 152.360 123.973 104.456 1.00 25.94 ? 671 ASP A O     1 
ATOM   5403  C  CB    . ASP A 1 671 ? 150.531 122.110 106.482 1.00 26.09 ? 671 ASP A CB    1 
ATOM   5404  C  CG    . ASP A 1 671 ? 149.111 121.709 106.826 1.00 37.46 ? 671 ASP A CG    1 
ATOM   5405  O  OD1   . ASP A 1 671 ? 148.190 122.057 106.059 1.00 35.94 ? 671 ASP A OD1   1 
ATOM   5406  O  OD2   . ASP A 1 671 ? 148.915 121.043 107.866 1.00 37.19 ? 671 ASP A OD2   1 
ATOM   5407  N  N     . LEU A 1 672 ? 153.153 121.885 104.721 1.00 25.26 ? 672 LEU A N     1 
ATOM   5408  C  CA    . LEU A 1 672 ? 154.531 122.295 104.474 1.00 19.05 ? 672 LEU A CA    1 
ATOM   5409  C  C     . LEU A 1 672 ? 154.752 122.689 103.020 1.00 19.20 ? 672 LEU A C     1 
ATOM   5410  O  O     . LEU A 1 672 ? 155.546 123.592 102.740 1.00 25.09 ? 672 LEU A O     1 
ATOM   5411  C  CB    . LEU A 1 672 ? 155.490 121.176 104.875 1.00 22.43 ? 672 LEU A CB    1 
ATOM   5412  C  CG    . LEU A 1 672 ? 155.578 120.899 106.376 1.00 24.04 ? 672 LEU A CG    1 
ATOM   5413  C  CD1   . LEU A 1 672 ? 156.216 119.545 106.636 1.00 19.73 ? 672 LEU A CD1   1 
ATOM   5414  C  CD2   . LEU A 1 672 ? 156.344 122.008 107.079 1.00 21.37 ? 672 LEU A CD2   1 
ATOM   5415  N  N     . TYR A 1 673 ? 154.068 122.029 102.085 1.00 21.63 ? 673 TYR A N     1 
ATOM   5416  C  CA    . TYR A 1 673 ? 154.164 122.420 100.685 1.00 19.42 ? 673 TYR A CA    1 
ATOM   5417  C  C     . TYR A 1 673 ? 153.473 123.755 100.443 1.00 21.35 ? 673 TYR A C     1 
ATOM   5418  O  O     . TYR A 1 673 ? 153.935 124.562 99.628  1.00 23.80 ? 673 TYR A O     1 
ATOM   5419  C  CB    . TYR A 1 673 ? 153.567 121.331 99.796  1.00 14.97 ? 673 TYR A CB    1 
ATOM   5420  C  CG    . TYR A 1 673 ? 153.684 121.616 98.320  1.00 18.82 ? 673 TYR A CG    1 
ATOM   5421  C  CD1   . TYR A 1 673 ? 154.925 121.711 97.709  1.00 18.87 ? 673 TYR A CD1   1 
ATOM   5422  C  CD2   . TYR A 1 673 ? 152.553 121.787 97.535  1.00 17.85 ? 673 TYR A CD2   1 
ATOM   5423  C  CE1   . TYR A 1 673 ? 155.037 121.970 96.362  1.00 23.63 ? 673 TYR A CE1   1 
ATOM   5424  C  CE2   . TYR A 1 673 ? 152.656 122.046 96.186  1.00 21.17 ? 673 TYR A CE2   1 
ATOM   5425  C  CZ    . TYR A 1 673 ? 153.900 122.135 95.604  1.00 25.30 ? 673 TYR A CZ    1 
ATOM   5426  O  OH    . TYR A 1 673 ? 154.011 122.393 94.259  1.00 24.07 ? 673 TYR A OH    1 
ATOM   5427  N  N     . ALA A 1 674 ? 152.360 124.000 101.135 1.00 22.95 ? 674 ALA A N     1 
ATOM   5428  C  CA    . ALA A 1 674 ? 151.711 125.303 101.061 1.00 16.66 ? 674 ALA A CA    1 
ATOM   5429  C  C     . ALA A 1 674 ? 152.619 126.396 101.604 1.00 17.10 ? 674 ALA A C     1 
ATOM   5430  O  O     . ALA A 1 674 ? 152.730 127.474 101.010 1.00 25.30 ? 674 ALA A O     1 
ATOM   5431  C  CB    . ALA A 1 674 ? 150.388 125.268 101.824 1.00 13.19 ? 674 ALA A CB    1 
ATOM   5432  N  N     . HIS A 1 675 ? 153.289 126.132 102.727 1.00 15.42 ? 675 HIS A N     1 
ATOM   5433  C  CA    . HIS A 1 675 ? 154.242 127.098 103.261 1.00 19.50 ? 675 HIS A CA    1 
ATOM   5434  C  C     . HIS A 1 675 ? 155.400 127.322 102.295 1.00 19.79 ? 675 HIS A C     1 
ATOM   5435  O  O     . HIS A 1 675 ? 155.866 128.453 102.122 1.00 23.66 ? 675 HIS A O     1 
ATOM   5436  C  CB    . HIS A 1 675 ? 154.760 126.630 104.619 1.00 17.92 ? 675 HIS A CB    1 
ATOM   5437  C  CG    . HIS A 1 675 ? 155.894 127.451 105.146 1.00 21.55 ? 675 HIS A CG    1 
ATOM   5438  N  ND1   . HIS A 1 675 ? 157.210 127.059 105.039 1.00 28.39 ? 675 HIS A ND1   1 
ATOM   5439  C  CD2   . HIS A 1 675 ? 155.908 128.647 105.779 1.00 19.98 ? 675 HIS A CD2   1 
ATOM   5440  C  CE1   . HIS A 1 675 ? 157.986 127.977 105.585 1.00 24.09 ? 675 HIS A CE1   1 
ATOM   5441  N  NE2   . HIS A 1 675 ? 157.221 128.951 106.042 1.00 24.56 ? 675 HIS A NE2   1 
ATOM   5442  N  N     . HIS A 1 676 ? 155.882 126.250 101.663 1.00 22.88 ? 676 HIS A N     1 
ATOM   5443  C  CA    . HIS A 1 676 ? 156.979 126.371 100.709 1.00 19.32 ? 676 HIS A CA    1 
ATOM   5444  C  C     . HIS A 1 676 ? 156.567 127.171 99.480  1.00 25.51 ? 676 HIS A C     1 
ATOM   5445  O  O     . HIS A 1 676 ? 157.366 127.941 98.935  1.00 25.89 ? 676 HIS A O     1 
ATOM   5446  C  CB    . HIS A 1 676 ? 157.467 124.981 100.303 1.00 23.81 ? 676 HIS A CB    1 
ATOM   5447  C  CG    . HIS A 1 676 ? 158.406 124.985 99.138  1.00 24.79 ? 676 HIS A CG    1 
ATOM   5448  N  ND1   . HIS A 1 676 ? 159.722 125.381 99.243  1.00 22.15 ? 676 HIS A ND1   1 
ATOM   5449  C  CD2   . HIS A 1 676 ? 158.219 124.641 97.842  1.00 25.69 ? 676 HIS A CD2   1 
ATOM   5450  C  CE1   . HIS A 1 676 ? 160.305 125.280 98.062  1.00 28.61 ? 676 HIS A CE1   1 
ATOM   5451  N  NE2   . HIS A 1 676 ? 159.415 124.834 97.194  1.00 28.04 ? 676 HIS A NE2   1 
ATOM   5452  N  N     . ARG A 1 677 ? 155.327 127.006 99.031  1.00 23.86 ? 677 ARG A N     1 
ATOM   5453  C  CA    . ARG A 1 677 ? 154.856 127.625 97.801  1.00 20.06 ? 677 ARG A CA    1 
ATOM   5454  C  C     . ARG A 1 677 ? 154.348 129.046 98.001  1.00 19.83 ? 677 ARG A C     1 
ATOM   5455  O  O     . ARG A 1 677 ? 153.885 129.662 97.036  1.00 27.16 ? 677 ARG A O     1 
ATOM   5456  C  CB    . ARG A 1 677 ? 153.755 126.770 97.169  1.00 22.95 ? 677 ARG A CB    1 
ATOM   5457  C  CG    . ARG A 1 677 ? 154.276 125.616 96.330  1.00 22.13 ? 677 ARG A CG    1 
ATOM   5458  C  CD    . ARG A 1 677 ? 154.882 126.110 95.029  1.00 17.95 ? 677 ARG A CD    1 
ATOM   5459  N  NE    . ARG A 1 677 ? 153.876 126.285 93.988  1.00 27.26 ? 677 ARG A NE    1 
ATOM   5460  C  CZ    . ARG A 1 677 ? 153.596 127.441 93.402  1.00 32.14 ? 677 ARG A CZ    1 
ATOM   5461  N  NH1   . ARG A 1 677 ? 154.233 128.554 93.729  1.00 29.66 ? 677 ARG A NH1   1 
ATOM   5462  N  NH2   . ARG A 1 677 ? 152.653 127.483 92.466  1.00 25.04 ? 677 ARG A NH2   1 
ATOM   5463  N  N     . GLY A 1 678 ? 154.421 129.581 99.215  1.00 17.64 ? 678 GLY A N     1 
ATOM   5464  C  CA    . GLY A 1 678 ? 153.995 130.941 99.464  1.00 10.09 ? 678 GLY A CA    1 
ATOM   5465  C  C     . GLY A 1 678 ? 152.549 131.106 99.864  1.00 16.22 ? 678 GLY A C     1 
ATOM   5466  O  O     . GLY A 1 678 ? 152.024 132.220 99.777  1.00 21.01 ? 678 GLY A O     1 
ATOM   5467  N  N     . ILE A 1 679 ? 151.884 130.034 100.293 1.00 17.85 ? 679 ILE A N     1 
ATOM   5468  C  CA    . ILE A 1 679 ? 150.510 130.145 100.764 1.00 11.19 ? 679 ILE A CA    1 
ATOM   5469  C  C     . ILE A 1 679 ? 150.493 130.937 102.062 1.00 13.37 ? 679 ILE A C     1 
ATOM   5470  O  O     . ILE A 1 679 ? 151.274 130.668 102.983 1.00 28.73 ? 679 ILE A O     1 
ATOM   5471  C  CB    . ILE A 1 679 ? 149.886 128.754 100.946 1.00 15.99 ? 679 ILE A CB    1 
ATOM   5472  C  CG1   . ILE A 1 679 ? 149.706 128.072 99.590  1.00 12.53 ? 679 ILE A CG1   1 
ATOM   5473  C  CG2   . ILE A 1 679 ? 148.564 128.844 101.689 1.00 14.19 ? 679 ILE A CG2   1 
ATOM   5474  C  CD1   . ILE A 1 679 ? 148.836 128.835 98.642  1.00 12.97 ? 679 ILE A CD1   1 
ATOM   5475  N  N     . LYS A 1 680 ? 149.605 131.927 102.136 1.00 10.05 ? 680 LYS A N     1 
ATOM   5476  C  CA    . LYS A 1 680 ? 149.565 132.799 103.303 1.00 7.58  ? 680 LYS A CA    1 
ATOM   5477  C  C     . LYS A 1 680 ? 148.763 132.179 104.440 1.00 5.25  ? 680 LYS A C     1 
ATOM   5478  O  O     . LYS A 1 680 ? 149.201 132.191 105.595 1.00 17.15 ? 680 LYS A O     1 
ATOM   5479  C  CB    . LYS A 1 680 ? 148.985 134.158 102.914 1.00 9.33  ? 680 LYS A CB    1 
ATOM   5480  C  CG    . LYS A 1 680 ? 149.857 134.961 101.971 1.00 0.00  ? 680 LYS A CG    1 
ATOM   5481  C  CD    . LYS A 1 680 ? 149.289 136.349 101.764 1.00 6.74  ? 680 LYS A CD    1 
ATOM   5482  C  CE    . LYS A 1 680 ? 150.033 137.098 100.684 1.00 10.02 ? 680 LYS A CE    1 
ATOM   5483  N  NZ    . LYS A 1 680 ? 149.501 138.472 100.513 1.00 15.43 ? 680 LYS A NZ    1 
ATOM   5484  N  N     . THR A 1 681 ? 147.588 131.633 104.136 1.00 11.38 ? 681 THR A N     1 
ATOM   5485  C  CA    . THR A 1 681 ? 146.718 131.051 105.146 1.00 8.74  ? 681 THR A CA    1 
ATOM   5486  C  C     . THR A 1 681 ? 146.109 129.761 104.617 1.00 14.03 ? 681 THR A C     1 
ATOM   5487  O  O     . THR A 1 681 ? 145.926 129.592 103.410 1.00 23.83 ? 681 THR A O     1 
ATOM   5488  C  CB    . THR A 1 681 ? 145.591 132.013 105.561 1.00 14.45 ? 681 THR A CB    1 
ATOM   5489  O  OG1   . THR A 1 681 ? 144.968 132.559 104.392 1.00 20.98 ? 681 THR A OG1   1 
ATOM   5490  C  CG2   . THR A 1 681 ? 146.129 133.146 106.418 1.00 12.19 ? 681 THR A CG2   1 
ATOM   5491  N  N     . ILE A 1 682 ? 145.794 128.854 105.537 1.00 11.40 ? 682 ILE A N     1 
ATOM   5492  C  CA    . ILE A 1 682 ? 145.047 127.638 105.239 1.00 12.13 ? 682 ILE A CA    1 
ATOM   5493  C  C     . ILE A 1 682 ? 143.778 127.656 106.076 1.00 14.62 ? 682 ILE A C     1 
ATOM   5494  O  O     . ILE A 1 682 ? 143.843 127.765 107.305 1.00 15.36 ? 682 ILE A O     1 
ATOM   5495  C  CB    . ILE A 1 682 ? 145.872 126.370 105.520 1.00 16.24 ? 682 ILE A CB    1 
ATOM   5496  C  CG1   . ILE A 1 682 ? 147.252 126.471 104.871 1.00 18.24 ? 682 ILE A CG1   1 
ATOM   5497  C  CG2   . ILE A 1 682 ? 145.142 125.150 105.011 1.00 19.31 ? 682 ILE A CG2   1 
ATOM   5498  C  CD1   . ILE A 1 682 ? 148.103 125.240 105.056 1.00 19.47 ? 682 ILE A CD1   1 
ATOM   5499  N  N     . TYR A 1 683 ? 142.626 127.557 105.412 1.00 16.62 ? 683 TYR A N     1 
ATOM   5500  C  CA    . TYR A 1 683 ? 141.354 127.772 106.102 1.00 11.50 ? 683 TYR A CA    1 
ATOM   5501  C  C     . TYR A 1 683 ? 140.875 126.517 106.825 1.00 24.28 ? 683 TYR A C     1 
ATOM   5502  O  O     . TYR A 1 683 ? 140.812 126.480 108.056 1.00 34.30 ? 683 TYR A O     1 
ATOM   5503  C  CB    . TYR A 1 683 ? 140.301 128.253 105.099 1.00 19.13 ? 683 TYR A CB    1 
ATOM   5504  C  CG    . TYR A 1 683 ? 138.991 128.666 105.725 1.00 16.38 ? 683 TYR A CG    1 
ATOM   5505  C  CD1   . TYR A 1 683 ? 138.935 129.106 107.040 1.00 16.33 ? 683 TYR A CD1   1 
ATOM   5506  C  CD2   . TYR A 1 683 ? 137.811 128.629 104.997 1.00 13.13 ? 683 TYR A CD2   1 
ATOM   5507  C  CE1   . TYR A 1 683 ? 137.745 129.486 107.614 1.00 19.78 ? 683 TYR A CE1   1 
ATOM   5508  C  CE2   . TYR A 1 683 ? 136.613 129.011 105.564 1.00 18.47 ? 683 TYR A CE2   1 
ATOM   5509  C  CZ    . TYR A 1 683 ? 136.587 129.438 106.872 1.00 21.12 ? 683 TYR A CZ    1 
ATOM   5510  O  OH    . TYR A 1 683 ? 135.397 129.821 107.446 1.00 27.75 ? 683 TYR A OH    1 
ATOM   5511  N  N     . TYR A 1 684 ? 140.557 125.469 106.080 1.00 31.92 ? 684 TYR A N     1 
ATOM   5512  C  CA    . TYR A 1 684 ? 139.884 124.317 106.652 1.00 24.87 ? 684 TYR A CA    1 
ATOM   5513  C  C     . TYR A 1 684 ? 140.511 123.036 106.138 1.00 34.98 ? 684 TYR A C     1 
ATOM   5514  O  O     . TYR A 1 684 ? 141.032 122.981 105.022 1.00 36.07 ? 684 TYR A O     1 
ATOM   5515  C  CB    . TYR A 1 684 ? 138.387 124.322 106.324 1.00 27.85 ? 684 TYR A CB    1 
ATOM   5516  C  CG    . TYR A 1 684 ? 137.526 124.937 107.400 1.00 26.13 ? 684 TYR A CG    1 
ATOM   5517  C  CD1   . TYR A 1 684 ? 137.758 124.666 108.740 1.00 28.97 ? 684 TYR A CD1   1 
ATOM   5518  C  CD2   . TYR A 1 684 ? 136.482 125.790 107.075 1.00 28.13 ? 684 TYR A CD2   1 
ATOM   5519  C  CE1   . TYR A 1 684 ? 136.974 125.227 109.727 1.00 32.79 ? 684 TYR A CE1   1 
ATOM   5520  C  CE2   . TYR A 1 684 ? 135.694 126.357 108.053 1.00 27.42 ? 684 TYR A CE2   1 
ATOM   5521  C  CZ    . TYR A 1 684 ? 135.944 126.073 109.378 1.00 33.39 ? 684 TYR A CZ    1 
ATOM   5522  O  OH    . TYR A 1 684 ? 135.160 126.635 110.358 1.00 36.86 ? 684 TYR A OH    1 
ATOM   5523  N  N     . ALA A 1 685 ? 140.461 122.008 106.975 1.00 33.23 ? 685 ALA A N     1 
ATOM   5524  C  CA    . ALA A 1 685 ? 140.850 120.655 106.604 1.00 30.99 ? 685 ALA A CA    1 
ATOM   5525  C  C     . ALA A 1 685 ? 139.561 119.841 106.538 1.00 34.93 ? 685 ALA A C     1 
ATOM   5526  O  O     . ALA A 1 685 ? 139.165 119.195 107.509 1.00 42.10 ? 685 ALA A O     1 
ATOM   5527  C  CB    . ALA A 1 685 ? 141.845 120.075 107.599 1.00 31.82 ? 685 ALA A CB    1 
ATOM   5528  N  N     . ARG A 1 686 ? 138.904 119.886 105.383 1.00 36.04 ? 686 ARG A N     1 
ATOM   5529  C  CA    . ARG A 1 686 ? 137.650 119.176 105.177 1.00 36.45 ? 686 ARG A CA    1 
ATOM   5530  C  C     . ARG A 1 686 ? 137.939 117.751 104.729 1.00 40.70 ? 686 ARG A C     1 
ATOM   5531  O  O     . ARG A 1 686 ? 138.678 117.533 103.765 1.00 42.20 ? 686 ARG A O     1 
ATOM   5532  C  CB    . ARG A 1 686 ? 136.787 119.892 104.138 1.00 39.20 ? 686 ARG A CB    1 
ATOM   5533  C  CG    . ARG A 1 686 ? 136.034 121.089 104.678 1.00 42.82 ? 686 ARG A CG    1 
ATOM   5534  C  CD    . ARG A 1 686 ? 134.776 121.343 103.870 1.00 42.82 ? 686 ARG A CD    1 
ATOM   5535  N  NE    . ARG A 1 686 ? 133.992 120.127 103.697 1.00 44.23 ? 686 ARG A NE    1 
ATOM   5536  C  CZ    . ARG A 1 686 ? 132.689 120.039 103.926 1.00 45.44 ? 686 ARG A CZ    1 
ATOM   5537  N  NH1   . ARG A 1 686 ? 131.986 121.084 104.331 1.00 43.48 ? 686 ARG A NH1   1 
ATOM   5538  N  NH2   . ARG A 1 686 ? 132.076 118.873 103.742 1.00 44.55 ? 686 ARG A NH2   1 
ATOM   5539  N  N     . THR A 1 687 ? 137.352 116.786 105.428 1.00 45.95 ? 687 THR A N     1 
ATOM   5540  C  CA    . THR A 1 687 ? 137.574 115.375 105.154 1.00 48.17 ? 687 THR A CA    1 
ATOM   5541  C  C     . THR A 1 687 ? 136.278 114.731 104.679 1.00 46.49 ? 687 THR A C     1 
ATOM   5542  O  O     . THR A 1 687 ? 135.204 114.999 105.225 1.00 49.96 ? 687 THR A O     1 
ATOM   5543  C  CB    . THR A 1 687 ? 138.098 114.654 106.399 1.00 47.83 ? 687 THR A CB    1 
ATOM   5544  O  OG1   . THR A 1 687 ? 139.337 115.246 106.808 1.00 46.65 ? 687 THR A OG1   1 
ATOM   5545  C  CG2   . THR A 1 687 ? 138.334 113.187 106.105 1.00 47.75 ? 687 THR A CG2   1 
ATOM   5546  N  N     . LYS A 1 688 ? 136.385 113.888 103.656 1.00 46.14 ? 688 LYS A N     1 
ATOM   5547  C  CA    . LYS A 1 688 ? 135.228 113.178 103.126 1.00 51.72 ? 688 LYS A CA    1 
ATOM   5548  C  C     . LYS A 1 688 ? 135.217 111.728 103.599 1.00 55.09 ? 688 LYS A C     1 
ATOM   5549  O  O     . LYS A 1 688 ? 136.249 111.187 103.997 1.00 57.18 ? 688 LYS A O     1 
ATOM   5550  C  CB    . LYS A 1 688 ? 135.215 113.232 101.597 1.00 50.44 ? 688 LYS A CB    1 
ATOM   5551  C  CG    . LYS A 1 688 ? 136.092 112.185 100.932 1.00 49.94 ? 688 LYS A CG    1 
ATOM   5552  C  CD    . LYS A 1 688 ? 135.634 111.890 99.512  1.00 52.76 ? 688 LYS A CD    1 
ATOM   5553  C  CE    . LYS A 1 688 ? 134.118 111.849 99.406  1.00 52.11 ? 688 LYS A CE    1 
ATOM   5554  N  NZ    . LYS A 1 688 ? 133.673 111.494 98.030  1.00 50.72 ? 688 LYS A NZ    1 
ATOM   5555  N  N     . VAL B 1 6   ? 153.496 115.603 164.470 1.00 57.97 ? 6   VAL B N     1 
ATOM   5556  C  CA    . VAL B 1 6   ? 152.413 116.387 165.049 1.00 60.05 ? 6   VAL B CA    1 
ATOM   5557  C  C     . VAL B 1 6   ? 152.974 117.472 165.962 1.00 60.17 ? 6   VAL B C     1 
ATOM   5558  O  O     . VAL B 1 6   ? 153.723 117.179 166.894 1.00 56.37 ? 6   VAL B O     1 
ATOM   5559  C  CB    . VAL B 1 6   ? 151.423 115.491 165.811 1.00 58.69 ? 6   VAL B CB    1 
ATOM   5560  C  CG1   . VAL B 1 6   ? 150.242 116.308 166.305 1.00 56.32 ? 6   VAL B CG1   1 
ATOM   5561  C  CG2   . VAL B 1 6   ? 150.951 114.350 164.923 1.00 58.72 ? 6   VAL B CG2   1 
ATOM   5562  N  N     . PRO B 1 7   ? 152.619 118.725 165.683 1.00 58.87 ? 7   PRO B N     1 
ATOM   5563  C  CA    . PRO B 1 7   ? 153.120 119.835 166.503 1.00 54.24 ? 7   PRO B CA    1 
ATOM   5564  C  C     . PRO B 1 7   ? 152.652 119.726 167.946 1.00 55.72 ? 7   PRO B C     1 
ATOM   5565  O  O     . PRO B 1 7   ? 151.595 119.166 168.242 1.00 59.41 ? 7   PRO B O     1 
ATOM   5566  C  CB    . PRO B 1 7   ? 152.536 121.077 165.824 1.00 53.75 ? 7   PRO B CB    1 
ATOM   5567  C  CG    . PRO B 1 7   ? 152.164 120.660 164.455 1.00 56.26 ? 7   PRO B CG    1 
ATOM   5568  C  CD    . PRO B 1 7   ? 151.967 119.178 164.443 1.00 56.60 ? 7   PRO B CD    1 
ATOM   5569  N  N     . LYS B 1 8   ? 153.470 120.269 168.852 1.00 55.34 ? 8   LYS B N     1 
ATOM   5570  C  CA    . LYS B 1 8   ? 153.142 120.219 170.274 1.00 55.20 ? 8   LYS B CA    1 
ATOM   5571  C  C     . LYS B 1 8   ? 151.853 120.973 170.573 1.00 57.23 ? 8   LYS B C     1 
ATOM   5572  O  O     . LYS B 1 8   ? 151.013 120.500 171.349 1.00 59.54 ? 8   LYS B O     1 
ATOM   5573  C  CB    . LYS B 1 8   ? 154.297 120.787 171.097 1.00 55.38 ? 8   LYS B CB    1 
ATOM   5574  C  CG    . LYS B 1 8   ? 154.270 120.382 172.560 1.00 56.00 ? 8   LYS B CG    1 
ATOM   5575  C  CD    . LYS B 1 8   ? 154.807 121.490 173.449 1.00 56.97 ? 8   LYS B CD    1 
ATOM   5576  C  CE    . LYS B 1 8   ? 154.135 121.478 174.812 1.00 57.58 ? 8   LYS B CE    1 
ATOM   5577  N  NZ    . LYS B 1 8   ? 154.983 122.114 175.855 1.00 56.38 ? 8   LYS B NZ    1 
ATOM   5578  N  N     . TRP B 1 9   ? 151.678 122.151 169.970 1.00 56.70 ? 9   TRP B N     1 
ATOM   5579  C  CA    . TRP B 1 9   ? 150.447 122.904 170.180 1.00 51.70 ? 9   TRP B CA    1 
ATOM   5580  C  C     . TRP B 1 9   ? 149.243 122.186 169.587 1.00 52.20 ? 9   TRP B C     1 
ATOM   5581  O  O     . TRP B 1 9   ? 148.141 122.277 170.135 1.00 56.97 ? 9   TRP B O     1 
ATOM   5582  C  CB    . TRP B 1 9   ? 150.570 124.307 169.591 1.00 51.19 ? 9   TRP B CB    1 
ATOM   5583  C  CG    . TRP B 1 9   ? 150.951 124.342 168.144 1.00 49.96 ? 9   TRP B CG    1 
ATOM   5584  C  CD1   . TRP B 1 9   ? 150.105 124.346 167.075 1.00 49.51 ? 9   TRP B CD1   1 
ATOM   5585  C  CD2   . TRP B 1 9   ? 152.276 124.404 167.606 1.00 49.59 ? 9   TRP B CD2   1 
ATOM   5586  N  NE1   . TRP B 1 9   ? 150.820 124.395 165.905 1.00 49.18 ? 9   TRP B NE1   1 
ATOM   5587  C  CE2   . TRP B 1 9   ? 152.156 124.434 166.203 1.00 50.90 ? 9   TRP B CE2   1 
ATOM   5588  C  CE3   . TRP B 1 9   ? 153.553 124.432 168.174 1.00 47.46 ? 9   TRP B CE3   1 
ATOM   5589  C  CZ2   . TRP B 1 9   ? 153.263 124.488 165.361 1.00 50.48 ? 9   TRP B CZ2   1 
ATOM   5590  C  CZ3   . TRP B 1 9   ? 154.649 124.487 167.337 1.00 51.47 ? 9   TRP B CZ3   1 
ATOM   5591  C  CH2   . TRP B 1 9   ? 154.498 124.514 165.946 1.00 52.10 ? 9   TRP B CH2   1 
ATOM   5592  N  N     . ILE B 1 10  ? 149.429 121.476 168.474 1.00 53.44 ? 10  ILE B N     1 
ATOM   5593  C  CA    . ILE B 1 10  ? 148.330 120.710 167.899 1.00 54.32 ? 10  ILE B CA    1 
ATOM   5594  C  C     . ILE B 1 10  ? 147.941 119.564 168.825 1.00 54.59 ? 10  ILE B C     1 
ATOM   5595  O  O     . ILE B 1 10  ? 146.753 119.272 169.009 1.00 56.11 ? 10  ILE B O     1 
ATOM   5596  C  CB    . ILE B 1 10  ? 148.706 120.209 166.493 1.00 55.48 ? 10  ILE B CB    1 
ATOM   5597  C  CG1   . ILE B 1 10  ? 148.624 121.353 165.479 1.00 54.75 ? 10  ILE B CG1   1 
ATOM   5598  C  CG2   . ILE B 1 10  ? 147.797 119.072 166.064 1.00 55.38 ? 10  ILE B CG2   1 
ATOM   5599  C  CD1   . ILE B 1 10  ? 147.488 122.321 165.728 1.00 54.33 ? 10  ILE B CD1   1 
ATOM   5600  N  N     . GLN B 1 11  ? 148.931 118.902 169.429 1.00 58.16 ? 11  GLN B N     1 
ATOM   5601  C  CA    . GLN B 1 11  ? 148.631 117.860 170.405 1.00 57.58 ? 11  GLN B CA    1 
ATOM   5602  C  C     . GLN B 1 11  ? 147.895 118.429 171.609 1.00 59.07 ? 11  GLN B C     1 
ATOM   5603  O  O     . GLN B 1 11  ? 146.903 117.852 172.067 1.00 60.06 ? 11  GLN B O     1 
ATOM   5604  C  CB    . GLN B 1 11  ? 149.917 117.166 170.852 1.00 57.49 ? 11  GLN B CB    1 
ATOM   5605  C  CG    . GLN B 1 11  ? 150.360 116.022 169.959 1.00 60.45 ? 11  GLN B CG    1 
ATOM   5606  C  CD    . GLN B 1 11  ? 151.865 115.844 169.952 1.00 61.85 ? 11  GLN B CD    1 
ATOM   5607  O  OE1   . GLN B 1 11  ? 152.467 115.589 168.910 1.00 61.31 ? 11  GLN B OE1   1 
ATOM   5608  N  NE2   . GLN B 1 11  ? 152.481 115.980 171.120 1.00 59.83 ? 11  GLN B NE2   1 
ATOM   5609  N  N     . LEU B 1 12  ? 148.362 119.567 172.131 1.00 58.83 ? 12  LEU B N     1 
ATOM   5610  C  CA    . LEU B 1 12  ? 147.716 120.171 173.294 1.00 55.54 ? 12  LEU B CA    1 
ATOM   5611  C  C     . LEU B 1 12  ? 146.286 120.591 172.978 1.00 58.52 ? 12  LEU B C     1 
ATOM   5612  O  O     . LEU B 1 12  ? 145.384 120.422 173.806 1.00 60.23 ? 12  LEU B O     1 
ATOM   5613  C  CB    . LEU B 1 12  ? 148.529 121.368 173.784 1.00 56.26 ? 12  LEU B CB    1 
ATOM   5614  C  CG    . LEU B 1 12  ? 149.617 121.068 174.814 1.00 58.27 ? 12  LEU B CG    1 
ATOM   5615  C  CD1   . LEU B 1 12  ? 150.522 122.273 174.996 1.00 58.53 ? 12  LEU B CD1   1 
ATOM   5616  C  CD2   . LEU B 1 12  ? 148.999 120.654 176.137 1.00 57.01 ? 12  LEU B CD2   1 
ATOM   5617  N  N     . ASN B 1 13  ? 146.064 121.148 171.787 1.00 54.63 ? 13  ASN B N     1 
ATOM   5618  C  CA    . ASN B 1 13  ? 144.715 121.530 171.385 1.00 53.66 ? 13  ASN B CA    1 
ATOM   5619  C  C     . ASN B 1 13  ? 143.827 120.305 171.212 1.00 56.12 ? 13  ASN B C     1 
ATOM   5620  O  O     . ASN B 1 13  ? 142.610 120.378 171.414 1.00 60.69 ? 13  ASN B O     1 
ATOM   5621  C  CB    . ASN B 1 13  ? 144.774 122.350 170.095 1.00 54.56 ? 13  ASN B CB    1 
ATOM   5622  C  CG    . ASN B 1 13  ? 143.410 122.579 169.484 1.00 54.49 ? 13  ASN B CG    1 
ATOM   5623  O  OD1   . ASN B 1 13  ? 142.976 121.831 168.609 1.00 55.16 ? 13  ASN B OD1   1 
ATOM   5624  N  ND2   . ASN B 1 13  ? 142.724 123.619 169.940 1.00 55.20 ? 13  ASN B ND2   1 
ATOM   5625  N  N     . ASN B 1 14  ? 144.418 119.168 170.840 1.00 58.52 ? 14  ASN B N     1 
ATOM   5626  C  CA    . ASN B 1 14  ? 143.645 117.945 170.669 1.00 56.76 ? 14  ASN B CA    1 
ATOM   5627  C  C     . ASN B 1 14  ? 143.264 117.304 171.997 1.00 58.74 ? 14  ASN B C     1 
ATOM   5628  O  O     . ASN B 1 14  ? 142.368 116.454 172.021 1.00 62.07 ? 14  ASN B O     1 
ATOM   5629  C  CB    . ASN B 1 14  ? 144.425 116.947 169.813 1.00 59.56 ? 14  ASN B CB    1 
ATOM   5630  C  CG    . ASN B 1 14  ? 144.346 117.263 168.334 1.00 58.80 ? 14  ASN B CG    1 
ATOM   5631  O  OD1   . ASN B 1 14  ? 144.099 118.403 167.943 1.00 58.75 ? 14  ASN B OD1   1 
ATOM   5632  N  ND2   . ASN B 1 14  ? 144.558 116.251 167.502 1.00 58.21 ? 14  ASN B ND2   1 
ATOM   5633  N  N     . GLU B 1 15  ? 143.915 117.686 173.097 1.00 60.34 ? 15  GLU B N     1 
ATOM   5634  C  CA    . GLU B 1 15  ? 143.578 117.135 174.404 1.00 60.67 ? 15  GLU B CA    1 
ATOM   5635  C  C     . GLU B 1 15  ? 142.301 117.722 174.986 1.00 62.22 ? 15  GLU B C     1 
ATOM   5636  O  O     . GLU B 1 15  ? 141.863 117.271 176.049 1.00 64.76 ? 15  GLU B O     1 
ATOM   5637  C  CB    . GLU B 1 15  ? 144.727 117.348 175.394 1.00 61.20 ? 15  GLU B CB    1 
ATOM   5638  C  CG    . GLU B 1 15  ? 146.087 116.916 174.883 1.00 62.78 ? 15  GLU B CG    1 
ATOM   5639  C  CD    . GLU B 1 15  ? 147.146 116.927 175.966 1.00 65.94 ? 15  GLU B CD    1 
ATOM   5640  O  OE1   . GLU B 1 15  ? 146.776 116.922 177.158 1.00 64.48 ? 15  GLU B OE1   1 
ATOM   5641  O  OE2   . GLU B 1 15  ? 148.347 116.941 175.625 1.00 65.78 ? 15  GLU B OE2   1 
ATOM   5642  N  N     . ILE B 1 16  ? 141.706 118.721 174.331 1.00 61.42 ? 16  ILE B N     1 
ATOM   5643  C  CA    . ILE B 1 16  ? 140.424 119.248 174.790 1.00 60.63 ? 16  ILE B CA    1 
ATOM   5644  C  C     . ILE B 1 16  ? 139.351 118.172 174.710 1.00 60.78 ? 16  ILE B C     1 
ATOM   5645  O  O     . ILE B 1 16  ? 138.546 118.006 175.635 1.00 61.35 ? 16  ILE B O     1 
ATOM   5646  C  CB    . ILE B 1 16  ? 140.038 120.497 173.976 1.00 62.02 ? 16  ILE B CB    1 
ATOM   5647  C  CG1   . ILE B 1 16  ? 141.174 121.521 174.004 1.00 61.06 ? 16  ILE B CG1   1 
ATOM   5648  C  CG2   . ILE B 1 16  ? 138.749 121.102 174.508 1.00 61.03 ? 16  ILE B CG2   1 
ATOM   5649  C  CD1   . ILE B 1 16  ? 140.752 122.915 173.610 1.00 58.49 ? 16  ILE B CD1   1 
ATOM   5650  N  N     . MET B 1 17  ? 139.326 117.419 173.608 1.00 62.38 ? 17  MET B N     1 
ATOM   5651  C  CA    . MET B 1 17  ? 138.330 116.368 173.443 1.00 63.17 ? 17  MET B CA    1 
ATOM   5652  C  C     . MET B 1 17  ? 138.567 115.187 174.372 1.00 63.95 ? 17  MET B C     1 
ATOM   5653  O  O     . MET B 1 17  ? 137.622 114.444 174.658 1.00 64.92 ? 17  MET B O     1 
ATOM   5654  C  CB    . MET B 1 17  ? 138.305 115.885 171.993 1.00 63.34 ? 17  MET B CB    1 
ATOM   5655  C  CG    . MET B 1 17  ? 138.093 116.949 170.902 1.00 63.35 ? 17  MET B CG    1 
ATOM   5656  S  SD    . MET B 1 17  ? 136.557 117.914 170.819 1.00 69.97 ? 17  MET B SD    1 
ATOM   5657  C  CE    . MET B 1 17  ? 136.624 118.972 172.261 1.00 62.74 ? 17  MET B CE    1 
ATOM   5658  N  N     . ILE B 1 18  ? 139.797 114.989 174.841 1.00 63.63 ? 18  ILE B N     1 
ATOM   5659  C  CA    . ILE B 1 18  ? 140.064 113.936 175.816 1.00 63.53 ? 18  ILE B CA    1 
ATOM   5660  C  C     . ILE B 1 18  ? 139.366 114.332 177.114 1.00 63.99 ? 18  ILE B C     1 
ATOM   5661  O  O     . ILE B 1 18  ? 139.762 115.295 177.777 1.00 64.69 ? 18  ILE B O     1 
ATOM   5662  C  CB    . ILE B 1 18  ? 141.567 113.716 176.026 1.00 63.34 ? 18  ILE B CB    1 
ATOM   5663  C  CG1   . ILE B 1 18  ? 142.161 112.873 174.892 1.00 63.01 ? 18  ILE B CG1   1 
ATOM   5664  C  CG2   . ILE B 1 18  ? 141.828 113.014 177.351 1.00 63.60 ? 18  ILE B CG2   1 
ATOM   5665  C  CD1   . ILE B 1 18  ? 142.367 113.612 173.588 1.00 62.48 ? 18  ILE B CD1   1 
ATOM   5666  N  N     . GLN B 1 19  ? 138.309 113.606 177.463 1.00 68.29 ? 19  GLN B N     1 
ATOM   5667  C  CA    . GLN B 1 19  ? 137.476 113.968 178.601 1.00 69.07 ? 19  GLN B CA    1 
ATOM   5668  C  C     . GLN B 1 19  ? 138.120 113.472 179.888 1.00 69.75 ? 19  GLN B C     1 
ATOM   5669  O  O     . GLN B 1 19  ? 138.295 112.264 180.078 1.00 70.53 ? 19  GLN B O     1 
ATOM   5670  C  CB    . GLN B 1 19  ? 136.074 113.387 178.435 1.00 69.89 ? 19  GLN B CB    1 
ATOM   5671  C  CG    . GLN B 1 19  ? 135.153 114.240 177.579 1.00 68.96 ? 19  GLN B CG    1 
ATOM   5672  C  CD    . GLN B 1 19  ? 133.740 114.300 178.121 1.00 70.79 ? 19  GLN B CD    1 
ATOM   5673  O  OE1   . GLN B 1 19  ? 133.479 113.901 179.255 1.00 71.49 ? 19  GLN B OE1   1 
ATOM   5674  N  NE2   . GLN B 1 19  ? 132.817 114.803 177.309 1.00 69.03 ? 19  GLN B NE2   1 
ATOM   5675  N  N     . LYS B 1 20  ? 138.474 114.404 180.767 1.00 74.61 ? 20  LYS B N     1 
ATOM   5676  C  CA    . LYS B 1 20  ? 139.050 114.092 182.067 1.00 74.52 ? 20  LYS B CA    1 
ATOM   5677  C  C     . LYS B 1 20  ? 138.025 114.426 183.141 1.00 76.56 ? 20  LYS B C     1 
ATOM   5678  O  O     . LYS B 1 20  ? 137.522 115.554 183.192 1.00 74.53 ? 20  LYS B O     1 
ATOM   5679  C  CB    . LYS B 1 20  ? 140.347 114.869 182.292 1.00 72.45 ? 20  LYS B CB    1 
ATOM   5680  C  CG    . LYS B 1 20  ? 141.018 114.586 183.625 1.00 75.29 ? 20  LYS B CG    1 
ATOM   5681  C  CD    . LYS B 1 20  ? 141.853 115.769 184.090 1.00 75.59 ? 20  LYS B CD    1 
ATOM   5682  C  CE    . LYS B 1 20  ? 141.004 117.018 184.256 1.00 76.33 ? 20  LYS B CE    1 
ATOM   5683  N  NZ    . LYS B 1 20  ? 139.728 116.734 184.969 1.00 77.87 ? 20  LYS B NZ    1 
ATOM   5684  N  N     . ASP B 1 21  ? 137.717 113.443 183.990 1.00 82.29 ? 21  ASP B N     1 
ATOM   5685  C  CA    . ASP B 1 21  ? 136.732 113.595 185.062 1.00 82.21 ? 21  ASP B CA    1 
ATOM   5686  C  C     . ASP B 1 21  ? 135.364 113.991 184.507 1.00 82.26 ? 21  ASP B C     1 
ATOM   5687  O  O     . ASP B 1 21  ? 134.628 114.774 185.112 1.00 81.97 ? 21  ASP B O     1 
ATOM   5688  C  CB    . ASP B 1 21  ? 137.210 114.599 186.114 1.00 82.26 ? 21  ASP B CB    1 
ATOM   5689  C  CG    . ASP B 1 21  ? 136.469 114.463 187.431 1.00 83.67 ? 21  ASP B CG    1 
ATOM   5690  O  OD1   . ASP B 1 21  ? 136.197 113.317 187.847 1.00 82.48 ? 21  ASP B OD1   1 
ATOM   5691  O  OD2   . ASP B 1 21  ? 136.160 115.503 188.051 1.00 83.71 ? 21  ASP B OD2   1 
ATOM   5692  N  N     . GLY B 1 22  ? 135.020 113.447 183.342 1.00 75.01 ? 22  GLY B N     1 
ATOM   5693  C  CA    . GLY B 1 22  ? 133.724 113.692 182.745 1.00 74.45 ? 22  GLY B CA    1 
ATOM   5694  C  C     . GLY B 1 22  ? 133.541 115.057 182.124 1.00 75.68 ? 22  GLY B C     1 
ATOM   5695  O  O     . GLY B 1 22  ? 132.409 115.414 181.780 1.00 75.69 ? 22  GLY B O     1 
ATOM   5696  N  N     . LYS B 1 23  ? 134.610 115.833 181.969 1.00 72.00 ? 23  LYS B N     1 
ATOM   5697  C  CA    . LYS B 1 23  ? 134.531 117.171 181.404 1.00 69.27 ? 23  LYS B CA    1 
ATOM   5698  C  C     . LYS B 1 23  ? 135.643 117.371 180.387 1.00 69.93 ? 23  LYS B C     1 
ATOM   5699  O  O     . LYS B 1 23  ? 136.724 116.786 180.500 1.00 69.34 ? 23  LYS B O     1 
ATOM   5700  C  CB    . LYS B 1 23  ? 134.633 118.249 182.491 1.00 68.66 ? 23  LYS B CB    1 
ATOM   5701  C  CG    . LYS B 1 23  ? 133.487 118.253 183.485 1.00 68.69 ? 23  LYS B CG    1 
ATOM   5702  C  CD    . LYS B 1 23  ? 133.644 119.386 184.482 1.00 68.70 ? 23  LYS B CD    1 
ATOM   5703  C  CE    . LYS B 1 23  ? 132.587 119.325 185.568 1.00 69.50 ? 23  LYS B CE    1 
ATOM   5704  N  NZ    . LYS B 1 23  ? 132.827 120.348 186.622 1.00 68.44 ? 23  LYS B NZ    1 
ATOM   5705  N  N     . PHE B 1 24  ? 135.366 118.206 179.388 1.00 65.17 ? 24  PHE B N     1 
ATOM   5706  C  CA    . PHE B 1 24  ? 136.394 118.579 178.428 1.00 62.48 ? 24  PHE B CA    1 
ATOM   5707  C  C     . PHE B 1 24  ? 137.489 119.381 179.120 1.00 61.32 ? 24  PHE B C     1 
ATOM   5708  O  O     . PHE B 1 24  ? 137.236 120.139 180.060 1.00 61.43 ? 24  PHE B O     1 
ATOM   5709  C  CB    . PHE B 1 24  ? 135.797 119.401 177.286 1.00 61.08 ? 24  PHE B CB    1 
ATOM   5710  C  CG    . PHE B 1 24  ? 134.808 118.650 176.445 1.00 60.82 ? 24  PHE B CG    1 
ATOM   5711  C  CD1   . PHE B 1 24  ? 133.463 118.644 176.773 1.00 61.36 ? 24  PHE B CD1   1 
ATOM   5712  C  CD2   . PHE B 1 24  ? 135.222 117.950 175.327 1.00 63.41 ? 24  PHE B CD2   1 
ATOM   5713  C  CE1   . PHE B 1 24  ? 132.550 117.955 175.998 1.00 62.43 ? 24  PHE B CE1   1 
ATOM   5714  C  CE2   . PHE B 1 24  ? 134.313 117.258 174.550 1.00 63.90 ? 24  PHE B CE2   1 
ATOM   5715  C  CZ    . PHE B 1 24  ? 132.976 117.261 174.886 1.00 61.59 ? 24  PHE B CZ    1 
ATOM   5716  N  N     . GLN B 1 25  ? 138.723 119.205 178.649 1.00 62.57 ? 25  GLN B N     1 
ATOM   5717  C  CA    . GLN B 1 25  ? 139.863 119.942 179.190 1.00 63.18 ? 25  GLN B CA    1 
ATOM   5718  C  C     . GLN B 1 25  ? 139.974 121.265 178.439 1.00 63.77 ? 25  GLN B C     1 
ATOM   5719  O  O     . GLN B 1 25  ? 140.798 121.450 177.541 1.00 63.68 ? 25  GLN B O     1 
ATOM   5720  C  CB    . GLN B 1 25  ? 141.138 119.116 179.087 1.00 64.11 ? 25  GLN B CB    1 
ATOM   5721  C  CG    . GLN B 1 25  ? 141.158 117.899 179.998 1.00 62.16 ? 25  GLN B CG    1 
ATOM   5722  C  CD    . GLN B 1 25  ? 142.326 116.980 179.713 1.00 63.56 ? 25  GLN B CD    1 
ATOM   5723  O  OE1   . GLN B 1 25  ? 143.411 117.145 180.269 1.00 63.17 ? 25  GLN B OE1   1 
ATOM   5724  N  NE2   . GLN B 1 25  ? 142.109 116.004 178.841 1.00 63.72 ? 25  GLN B NE2   1 
ATOM   5725  N  N     . PHE B 1 26  ? 139.107 122.205 178.823 1.00 58.85 ? 26  PHE B N     1 
ATOM   5726  C  CA    . PHE B 1 26  ? 139.081 123.507 178.166 1.00 56.73 ? 26  PHE B CA    1 
ATOM   5727  C  C     . PHE B 1 26  ? 140.346 124.306 178.448 1.00 58.82 ? 26  PHE B C     1 
ATOM   5728  O  O     . PHE B 1 26  ? 140.739 125.147 177.631 1.00 59.02 ? 26  PHE B O     1 
ATOM   5729  C  CB    . PHE B 1 26  ? 137.847 124.292 178.609 1.00 53.25 ? 26  PHE B CB    1 
ATOM   5730  C  CG    . PHE B 1 26  ? 136.562 123.769 178.039 1.00 55.00 ? 26  PHE B CG    1 
ATOM   5731  C  CD1   . PHE B 1 26  ? 136.426 123.565 176.677 1.00 55.00 ? 26  PHE B CD1   1 
ATOM   5732  C  CD2   . PHE B 1 26  ? 135.491 123.478 178.865 1.00 55.01 ? 26  PHE B CD2   1 
ATOM   5733  C  CE1   . PHE B 1 26  ? 135.246 123.082 176.150 1.00 55.87 ? 26  PHE B CE1   1 
ATOM   5734  C  CE2   . PHE B 1 26  ? 134.307 122.995 178.342 1.00 53.40 ? 26  PHE B CE2   1 
ATOM   5735  C  CZ    . PHE B 1 26  ? 134.185 122.797 176.983 1.00 53.55 ? 26  PHE B CZ    1 
ATOM   5736  N  N     . ASP B 1 27  ? 140.992 124.063 179.590 1.00 62.64 ? 27  ASP B N     1 
ATOM   5737  C  CA    . ASP B 1 27  ? 142.214 124.776 179.939 1.00 59.20 ? 27  ASP B CA    1 
ATOM   5738  C  C     . ASP B 1 27  ? 143.398 124.386 179.066 1.00 60.62 ? 27  ASP B C     1 
ATOM   5739  O  O     . ASP B 1 27  ? 144.422 125.076 179.101 1.00 61.67 ? 27  ASP B O     1 
ATOM   5740  C  CB    . ASP B 1 27  ? 142.557 124.533 181.409 1.00 60.65 ? 27  ASP B CB    1 
ATOM   5741  C  CG    . ASP B 1 27  ? 141.350 124.663 182.317 1.00 64.03 ? 27  ASP B CG    1 
ATOM   5742  O  OD1   . ASP B 1 27  ? 140.292 124.088 181.985 1.00 63.65 ? 27  ASP B OD1   1 
ATOM   5743  O  OD2   . ASP B 1 27  ? 141.458 125.340 183.360 1.00 64.07 ? 27  ASP B OD2   1 
ATOM   5744  N  N     . LYS B 1 28  ? 143.289 123.305 178.291 1.00 60.59 ? 28  LYS B N     1 
ATOM   5745  C  CA    . LYS B 1 28  ? 144.378 122.906 177.410 1.00 61.37 ? 28  LYS B CA    1 
ATOM   5746  C  C     . LYS B 1 28  ? 144.580 123.880 176.259 1.00 60.98 ? 28  LYS B C     1 
ATOM   5747  O  O     . LYS B 1 28  ? 145.668 123.911 175.675 1.00 61.77 ? 28  LYS B O     1 
ATOM   5748  C  CB    . LYS B 1 28  ? 144.125 121.503 176.859 1.00 61.09 ? 28  LYS B CB    1 
ATOM   5749  C  CG    . LYS B 1 28  ? 144.357 120.392 177.866 1.00 61.09 ? 28  LYS B CG    1 
ATOM   5750  C  CD    . LYS B 1 28  ? 145.838 120.150 178.083 1.00 61.29 ? 28  LYS B CD    1 
ATOM   5751  C  CE    . LYS B 1 28  ? 146.082 119.307 179.321 1.00 61.29 ? 28  LYS B CE    1 
ATOM   5752  N  NZ    . LYS B 1 28  ? 147.513 118.922 179.447 1.00 59.71 ? 28  LYS B NZ    1 
ATOM   5753  N  N     . ASP B 1 29  ? 143.562 124.675 175.919 1.00 57.69 ? 29  ASP B N     1 
ATOM   5754  C  CA    . ASP B 1 29  ? 143.703 125.612 174.811 1.00 55.54 ? 29  ASP B CA    1 
ATOM   5755  C  C     . ASP B 1 29  ? 144.617 126.776 175.173 1.00 55.37 ? 29  ASP B C     1 
ATOM   5756  O  O     . ASP B 1 29  ? 145.309 127.310 174.300 1.00 57.07 ? 29  ASP B O     1 
ATOM   5757  C  CB    . ASP B 1 29  ? 142.330 126.117 174.374 1.00 55.50 ? 29  ASP B CB    1 
ATOM   5758  C  CG    . ASP B 1 29  ? 142.156 126.096 172.869 1.00 57.66 ? 29  ASP B CG    1 
ATOM   5759  O  OD1   . ASP B 1 29  ? 142.816 125.270 172.204 1.00 57.48 ? 29  ASP B OD1   1 
ATOM   5760  O  OD2   . ASP B 1 29  ? 141.347 126.891 172.350 1.00 55.26 ? 29  ASP B OD2   1 
ATOM   5761  N  N     . LYS B 1 30  ? 144.629 127.188 176.443 1.00 56.47 ? 30  LYS B N     1 
ATOM   5762  C  CA    . LYS B 1 30  ? 145.620 128.164 176.887 1.00 57.05 ? 30  LYS B CA    1 
ATOM   5763  C  C     . LYS B 1 30  ? 147.027 127.592 176.784 1.00 56.75 ? 30  LYS B C     1 
ATOM   5764  O  O     . LYS B 1 30  ? 147.952 128.273 176.324 1.00 56.83 ? 30  LYS B O     1 
ATOM   5765  C  CB    . LYS B 1 30  ? 145.324 128.605 178.319 1.00 55.42 ? 30  LYS B CB    1 
ATOM   5766  C  CG    . LYS B 1 30  ? 144.028 129.379 178.477 1.00 56.87 ? 30  LYS B CG    1 
ATOM   5767  C  CD    . LYS B 1 30  ? 144.290 130.825 178.872 1.00 57.78 ? 30  LYS B CD    1 
ATOM   5768  C  CE    . LYS B 1 30  ? 145.360 130.923 179.949 1.00 58.61 ? 30  LYS B CE    1 
ATOM   5769  N  NZ    . LYS B 1 30  ? 145.410 132.277 180.565 1.00 57.72 ? 30  LYS B NZ    1 
ATOM   5770  N  N     . GLU B 1 31  ? 147.205 126.338 177.201 1.00 58.08 ? 31  GLU B N     1 
ATOM   5771  C  CA    . GLU B 1 31  ? 148.482 125.669 176.992 1.00 55.46 ? 31  GLU B CA    1 
ATOM   5772  C  C     . GLU B 1 31  ? 148.777 125.518 175.507 1.00 56.04 ? 31  GLU B C     1 
ATOM   5773  O  O     . GLU B 1 31  ? 149.924 125.671 175.076 1.00 58.40 ? 31  GLU B O     1 
ATOM   5774  C  CB    . GLU B 1 31  ? 148.482 124.305 177.682 1.00 55.62 ? 31  GLU B CB    1 
ATOM   5775  C  CG    . GLU B 1 31  ? 148.460 124.377 179.199 1.00 57.01 ? 31  GLU B CG    1 
ATOM   5776  C  CD    . GLU B 1 31  ? 148.516 123.009 179.846 1.00 62.46 ? 31  GLU B CD    1 
ATOM   5777  O  OE1   . GLU B 1 31  ? 148.483 122.000 179.111 1.00 64.13 ? 31  GLU B OE1   1 
ATOM   5778  O  OE2   . GLU B 1 31  ? 148.593 122.940 181.091 1.00 60.16 ? 31  GLU B OE2   1 
ATOM   5779  N  N     . ALA B 1 32  ? 147.749 125.225 174.708 1.00 51.79 ? 32  ALA B N     1 
ATOM   5780  C  CA    . ALA B 1 32  ? 147.949 125.073 173.271 1.00 50.18 ? 32  ALA B CA    1 
ATOM   5781  C  C     . ALA B 1 32  ? 148.428 126.371 172.635 1.00 51.72 ? 32  ALA B C     1 
ATOM   5782  O  O     . ALA B 1 32  ? 149.371 126.363 171.838 1.00 52.56 ? 32  ALA B O     1 
ATOM   5783  C  CB    . ALA B 1 32  ? 146.659 124.595 172.607 1.00 50.20 ? 32  ALA B CB    1 
ATOM   5784  N  N     . VAL B 1 33  ? 147.801 127.499 172.978 1.00 53.59 ? 33  VAL B N     1 
ATOM   5785  C  CA    . VAL B 1 33  ? 148.207 128.770 172.382 1.00 50.69 ? 33  VAL B CA    1 
ATOM   5786  C  C     . VAL B 1 33  ? 149.573 129.199 172.907 1.00 52.97 ? 33  VAL B C     1 
ATOM   5787  O  O     . VAL B 1 33  ? 150.389 129.757 172.161 1.00 53.80 ? 33  VAL B O     1 
ATOM   5788  C  CB    . VAL B 1 33  ? 147.132 129.852 172.607 1.00 47.27 ? 33  VAL B CB    1 
ATOM   5789  C  CG1   . VAL B 1 33  ? 146.977 130.192 174.077 1.00 48.33 ? 33  VAL B CG1   1 
ATOM   5790  C  CG2   . VAL B 1 33  ? 147.458 131.099 171.798 1.00 49.02 ? 33  VAL B CG2   1 
ATOM   5791  N  N     . HIS B 1 34  ? 149.851 128.948 174.190 1.00 51.32 ? 34  HIS B N     1 
ATOM   5792  C  CA    . HIS B 1 34  ? 151.167 129.275 174.731 1.00 47.98 ? 34  HIS B CA    1 
ATOM   5793  C  C     . HIS B 1 34  ? 152.260 128.487 174.021 1.00 49.08 ? 34  HIS B C     1 
ATOM   5794  O  O     . HIS B 1 34  ? 153.302 129.041 173.650 1.00 51.96 ? 34  HIS B O     1 
ATOM   5795  C  CB    . HIS B 1 34  ? 151.201 129.004 176.234 1.00 51.91 ? 34  HIS B CB    1 
ATOM   5796  C  CG    . HIS B 1 34  ? 152.513 129.329 176.875 1.00 52.54 ? 34  HIS B CG    1 
ATOM   5797  N  ND1   . HIS B 1 34  ? 153.524 128.403 177.012 1.00 52.00 ? 34  HIS B ND1   1 
ATOM   5798  C  CD2   . HIS B 1 34  ? 152.981 130.479 177.415 1.00 52.16 ? 34  HIS B CD2   1 
ATOM   5799  C  CE1   . HIS B 1 34  ? 154.558 128.967 177.610 1.00 51.07 ? 34  HIS B CE1   1 
ATOM   5800  N  NE2   . HIS B 1 34  ? 154.254 130.227 177.866 1.00 52.82 ? 34  HIS B NE2   1 
ATOM   5801  N  N     . SER B 1 35  ? 152.035 127.186 173.821 1.00 53.78 ? 35  SER B N     1 
ATOM   5802  C  CA    . SER B 1 35  ? 153.003 126.367 173.102 1.00 52.45 ? 35  SER B CA    1 
ATOM   5803  C  C     . SER B 1 35  ? 153.135 126.819 171.656 1.00 52.75 ? 35  SER B C     1 
ATOM   5804  O  O     . SER B 1 35  ? 154.248 126.906 171.128 1.00 54.73 ? 35  SER B O     1 
ATOM   5805  C  CB    . SER B 1 35  ? 152.598 124.896 173.171 1.00 52.15 ? 35  SER B CB    1 
ATOM   5806  O  OG    . SER B 1 35  ? 153.501 124.087 172.439 1.00 54.74 ? 35  SER B OG    1 
ATOM   5807  N  N     . TYR B 1 36  ? 152.008 127.118 171.003 1.00 50.13 ? 36  TYR B N     1 
ATOM   5808  C  CA    . TYR B 1 36  ? 152.044 127.607 169.629 1.00 49.68 ? 36  TYR B CA    1 
ATOM   5809  C  C     . TYR B 1 36  ? 152.931 128.833 169.516 1.00 47.88 ? 36  TYR B C     1 
ATOM   5810  O  O     . TYR B 1 36  ? 153.855 128.871 168.697 1.00 48.67 ? 36  TYR B O     1 
ATOM   5811  C  CB    . TYR B 1 36  ? 150.627 127.928 169.154 1.00 46.02 ? 36  TYR B CB    1 
ATOM   5812  C  CG    . TYR B 1 36  ? 150.560 128.500 167.757 1.00 44.62 ? 36  TYR B CG    1 
ATOM   5813  C  CD1   . TYR B 1 36  ? 151.220 127.888 166.703 1.00 45.40 ? 36  TYR B CD1   1 
ATOM   5814  C  CD2   . TYR B 1 36  ? 149.836 129.655 167.494 1.00 45.85 ? 36  TYR B CD2   1 
ATOM   5815  C  CE1   . TYR B 1 36  ? 151.159 128.404 165.426 1.00 46.78 ? 36  TYR B CE1   1 
ATOM   5816  C  CE2   . TYR B 1 36  ? 149.770 130.180 166.220 1.00 45.52 ? 36  TYR B CE2   1 
ATOM   5817  C  CZ    . TYR B 1 36  ? 150.434 129.551 165.190 1.00 46.91 ? 36  TYR B CZ    1 
ATOM   5818  O  OH    . TYR B 1 36  ? 150.373 130.071 163.918 1.00 47.34 ? 36  TYR B OH    1 
ATOM   5819  N  N     . PHE B 1 37  ? 152.686 129.834 170.361 1.00 51.83 ? 37  PHE B N     1 
ATOM   5820  C  CA    . PHE B 1 37  ? 153.520 131.028 170.348 1.00 51.25 ? 37  PHE B CA    1 
ATOM   5821  C  C     . PHE B 1 37  ? 154.978 130.672 170.596 1.00 52.40 ? 37  PHE B C     1 
ATOM   5822  O  O     . PHE B 1 37  ? 155.814 130.810 169.697 1.00 55.17 ? 37  PHE B O     1 
ATOM   5823  C  CB    . PHE B 1 37  ? 153.017 132.037 171.378 1.00 52.82 ? 37  PHE B CB    1 
ATOM   5824  C  CG    . PHE B 1 37  ? 152.163 133.114 170.785 1.00 53.20 ? 37  PHE B CG    1 
ATOM   5825  C  CD1   . PHE B 1 37  ? 152.740 134.250 170.248 1.00 52.18 ? 37  PHE B CD1   1 
ATOM   5826  C  CD2   . PHE B 1 37  ? 150.789 132.981 170.740 1.00 52.67 ? 37  PHE B CD2   1 
ATOM   5827  C  CE1   . PHE B 1 37  ? 151.960 135.239 169.693 1.00 53.65 ? 37  PHE B CE1   1 
ATOM   5828  C  CE2   . PHE B 1 37  ? 150.006 133.967 170.186 1.00 51.56 ? 37  PHE B CE2   1 
ATOM   5829  C  CZ    . PHE B 1 37  ? 150.592 135.096 169.660 1.00 52.00 ? 37  PHE B CZ    1 
ATOM   5830  N  N     . VAL B 1 38  ? 155.273 130.118 171.776 1.00 55.36 ? 38  VAL B N     1 
ATOM   5831  C  CA    . VAL B 1 38  ? 156.650 129.938 172.229 1.00 56.26 ? 38  VAL B CA    1 
ATOM   5832  C  C     . VAL B 1 38  ? 157.453 129.061 171.274 1.00 55.50 ? 38  VAL B C     1 
ATOM   5833  O  O     . VAL B 1 38  ? 158.671 129.236 171.140 1.00 57.45 ? 38  VAL B O     1 
ATOM   5834  C  CB    . VAL B 1 38  ? 156.638 129.378 173.669 1.00 54.71 ? 38  VAL B CB    1 
ATOM   5835  C  CG1   . VAL B 1 38  ? 157.877 128.548 173.962 1.00 56.15 ? 38  VAL B CG1   1 
ATOM   5836  C  CG2   . VAL B 1 38  ? 156.504 130.513 174.673 1.00 53.28 ? 38  VAL B CG2   1 
ATOM   5837  N  N     . ASP B 1 39  ? 156.801 128.136 170.568 1.00 54.17 ? 39  ASP B N     1 
ATOM   5838  C  CA    . ASP B 1 39  ? 157.519 127.201 169.712 1.00 53.96 ? 39  ASP B CA    1 
ATOM   5839  C  C     . ASP B 1 39  ? 157.542 127.595 168.242 1.00 57.65 ? 39  ASP B C     1 
ATOM   5840  O  O     . ASP B 1 39  ? 158.476 127.207 167.534 1.00 60.73 ? 39  ASP B O     1 
ATOM   5841  C  CB    . ASP B 1 39  ? 156.912 125.800 169.838 1.00 55.79 ? 39  ASP B CB    1 
ATOM   5842  C  CG    . ASP B 1 39  ? 157.028 125.238 171.239 1.00 59.41 ? 39  ASP B CG    1 
ATOM   5843  O  OD1   . ASP B 1 39  ? 157.628 125.911 172.102 1.00 59.13 ? 39  ASP B OD1   1 
ATOM   5844  O  OD2   . ASP B 1 39  ? 156.518 124.125 171.480 1.00 61.25 ? 39  ASP B OD2   1 
ATOM   5845  N  N     . TYR B 1 40  ? 156.556 128.344 167.751 1.00 57.62 ? 40  TYR B N     1 
ATOM   5846  C  CA    . TYR B 1 40  ? 156.494 128.671 166.333 1.00 55.83 ? 40  TYR B CA    1 
ATOM   5847  C  C     . TYR B 1 40  ? 156.534 130.167 166.068 1.00 58.69 ? 40  TYR B C     1 
ATOM   5848  O  O     . TYR B 1 40  ? 157.298 130.617 165.206 1.00 61.70 ? 40  TYR B O     1 
ATOM   5849  C  CB    . TYR B 1 40  ? 155.223 128.063 165.720 1.00 52.93 ? 40  TYR B CB    1 
ATOM   5850  C  CG    . TYR B 1 40  ? 155.155 128.156 164.215 1.00 56.23 ? 40  TYR B CG    1 
ATOM   5851  C  CD1   . TYR B 1 40  ? 155.879 127.286 163.413 1.00 56.78 ? 40  TYR B CD1   1 
ATOM   5852  C  CD2   . TYR B 1 40  ? 154.361 129.111 163.594 1.00 57.78 ? 40  TYR B CD2   1 
ATOM   5853  C  CE1   . TYR B 1 40  ? 155.819 127.366 162.036 1.00 58.14 ? 40  TYR B CE1   1 
ATOM   5854  C  CE2   . TYR B 1 40  ? 154.293 129.199 162.219 1.00 57.12 ? 40  TYR B CE2   1 
ATOM   5855  C  CZ    . TYR B 1 40  ? 155.024 128.324 161.445 1.00 59.51 ? 40  TYR B CZ    1 
ATOM   5856  O  OH    . TYR B 1 40  ? 154.960 128.408 160.073 1.00 60.35 ? 40  TYR B OH    1 
ATOM   5857  N  N     . ILE B 1 41  ? 155.733 130.955 166.787 1.00 54.49 ? 41  ILE B N     1 
ATOM   5858  C  CA    . ILE B 1 41  ? 155.572 132.360 166.431 1.00 53.76 ? 41  ILE B CA    1 
ATOM   5859  C  C     . ILE B 1 41  ? 156.820 133.148 166.804 1.00 53.36 ? 41  ILE B C     1 
ATOM   5860  O  O     . ILE B 1 41  ? 157.356 133.910 165.993 1.00 55.71 ? 41  ILE B O     1 
ATOM   5861  C  CB    . ILE B 1 41  ? 154.313 132.944 167.096 1.00 52.69 ? 41  ILE B CB    1 
ATOM   5862  C  CG1   . ILE B 1 41  ? 153.063 132.204 166.618 1.00 51.77 ? 41  ILE B CG1   1 
ATOM   5863  C  CG2   . ILE B 1 41  ? 154.195 134.430 166.800 1.00 52.10 ? 41  ILE B CG2   1 
ATOM   5864  C  CD1   . ILE B 1 41  ? 152.931 132.139 165.114 1.00 50.71 ? 41  ILE B CD1   1 
ATOM   5865  N  N     . ASN B 1 42  ? 157.307 132.967 168.034 1.00 53.59 ? 42  ASN B N     1 
ATOM   5866  C  CA    . ASN B 1 42  ? 158.510 133.673 168.457 1.00 55.13 ? 42  ASN B CA    1 
ATOM   5867  C  C     . ASN B 1 42  ? 159.727 133.239 167.652 1.00 57.18 ? 42  ASN B C     1 
ATOM   5868  O  O     . ASN B 1 42  ? 160.672 134.019 167.491 1.00 58.34 ? 42  ASN B O     1 
ATOM   5869  C  CB    . ASN B 1 42  ? 158.749 133.454 169.951 1.00 55.66 ? 42  ASN B CB    1 
ATOM   5870  C  CG    . ASN B 1 42  ? 157.620 133.993 170.806 1.00 56.99 ? 42  ASN B CG    1 
ATOM   5871  O  OD1   . ASN B 1 42  ? 156.624 134.499 170.291 1.00 58.64 ? 42  ASN B OD1   1 
ATOM   5872  N  ND2   . ASN B 1 42  ? 157.773 133.892 172.120 1.00 58.50 ? 42  ASN B ND2   1 
ATOM   5873  N  N     . GLN B 1 43  ? 159.725 132.007 167.142 1.00 59.81 ? 43  GLN B N     1 
ATOM   5874  C  CA    . GLN B 1 43  ? 160.815 131.552 166.288 1.00 57.99 ? 43  GLN B CA    1 
ATOM   5875  C  C     . GLN B 1 43  ? 160.726 132.158 164.893 1.00 58.56 ? 43  GLN B C     1 
ATOM   5876  O  O     . GLN B 1 43  ? 161.752 132.510 164.300 1.00 60.93 ? 43  GLN B O     1 
ATOM   5877  C  CB    . GLN B 1 43  ? 160.814 130.025 166.202 1.00 57.74 ? 43  GLN B CB    1 
ATOM   5878  C  CG    . GLN B 1 43  ? 161.674 129.336 167.251 1.00 59.92 ? 43  GLN B CG    1 
ATOM   5879  C  CD    . GLN B 1 43  ? 161.159 129.552 168.659 1.00 61.29 ? 43  GLN B CD    1 
ATOM   5880  O  OE1   . GLN B 1 43  ? 159.993 129.889 168.859 1.00 60.95 ? 43  GLN B OE1   1 
ATOM   5881  N  NE2   . GLN B 1 43  ? 162.027 129.359 169.644 1.00 60.11 ? 43  GLN B NE2   1 
ATOM   5882  N  N     . ASN B 1 44  ? 159.515 132.286 164.354 1.00 55.35 ? 44  ASN B N     1 
ATOM   5883  C  CA    . ASN B 1 44  ? 159.310 132.741 162.987 1.00 57.07 ? 44  ASN B CA    1 
ATOM   5884  C  C     . ASN B 1 44  ? 158.983 134.226 162.895 1.00 57.21 ? 44  ASN B C     1 
ATOM   5885  O  O     . ASN B 1 44  ? 158.654 134.709 161.808 1.00 56.66 ? 44  ASN B O     1 
ATOM   5886  C  CB    . ASN B 1 44  ? 158.204 131.920 162.318 1.00 54.93 ? 44  ASN B CB    1 
ATOM   5887  C  CG    . ASN B 1 44  ? 158.585 130.462 162.138 1.00 58.18 ? 44  ASN B CG    1 
ATOM   5888  O  OD1   . ASN B 1 44  ? 158.696 129.975 161.014 1.00 60.74 ? 44  ASN B OD1   1 
ATOM   5889  N  ND2   . ASN B 1 44  ? 158.774 129.755 163.247 1.00 57.76 ? 44  ASN B ND2   1 
ATOM   5890  N  N     . THR B 1 45  ? 159.061 134.957 164.002 1.00 57.23 ? 45  THR B N     1 
ATOM   5891  C  CA    . THR B 1 45  ? 158.826 136.395 163.997 1.00 57.83 ? 45  THR B CA    1 
ATOM   5892  C  C     . THR B 1 45  ? 160.150 137.117 163.782 1.00 56.93 ? 45  THR B C     1 
ATOM   5893  O  O     . THR B 1 45  ? 161.074 136.980 164.590 1.00 58.12 ? 45  THR B O     1 
ATOM   5894  C  CB    . THR B 1 45  ? 158.181 136.853 165.304 1.00 56.34 ? 45  THR B CB    1 
ATOM   5895  O  OG1   . THR B 1 45  ? 156.875 136.278 165.423 1.00 59.75 ? 45  THR B OG1   1 
ATOM   5896  C  CG2   . THR B 1 45  ? 158.070 138.369 165.340 1.00 54.73 ? 45  THR B CG2   1 
ATOM   5897  N  N     . VAL B 1 46  ? 160.241 137.881 162.693 1.00 56.07 ? 46  VAL B N     1 
ATOM   5898  C  CA    . VAL B 1 46  ? 161.426 138.693 162.453 1.00 55.95 ? 46  VAL B CA    1 
ATOM   5899  C  C     . VAL B 1 46  ? 161.506 139.777 163.516 1.00 56.60 ? 46  VAL B C     1 
ATOM   5900  O  O     . VAL B 1 46  ? 160.548 140.530 163.732 1.00 57.97 ? 46  VAL B O     1 
ATOM   5901  C  CB    . VAL B 1 46  ? 161.393 139.301 161.044 1.00 54.56 ? 46  VAL B CB    1 
ATOM   5902  C  CG1   . VAL B 1 46  ? 162.652 140.112 160.789 1.00 54.64 ? 46  VAL B CG1   1 
ATOM   5903  C  CG2   . VAL B 1 46  ? 161.239 138.215 160.003 1.00 54.51 ? 46  VAL B CG2   1 
ATOM   5904  N  N     . PHE B 1 47  ? 162.648 139.861 164.187 1.00 60.81 ? 47  PHE B N     1 
ATOM   5905  C  CA    . PHE B 1 47  ? 162.864 140.846 165.233 1.00 62.30 ? 47  PHE B CA    1 
ATOM   5906  C  C     . PHE B 1 47  ? 163.913 141.852 164.786 1.00 62.65 ? 47  PHE B C     1 
ATOM   5907  O  O     . PHE B 1 47  ? 164.885 141.496 164.112 1.00 62.19 ? 47  PHE B O     1 
ATOM   5908  C  CB    . PHE B 1 47  ? 163.298 140.183 166.541 1.00 62.07 ? 47  PHE B CB    1 
ATOM   5909  C  CG    . PHE B 1 47  ? 163.243 141.101 167.728 1.00 63.28 ? 47  PHE B CG    1 
ATOM   5910  C  CD1   . PHE B 1 47  ? 162.030 141.439 168.303 1.00 62.18 ? 47  PHE B CD1   1 
ATOM   5911  C  CD2   . PHE B 1 47  ? 164.404 141.629 168.267 1.00 62.70 ? 47  PHE B CD2   1 
ATOM   5912  C  CE1   . PHE B 1 47  ? 161.975 142.285 169.394 1.00 63.51 ? 47  PHE B CE1   1 
ATOM   5913  C  CE2   . PHE B 1 47  ? 164.356 142.475 169.359 1.00 62.19 ? 47  PHE B CE2   1 
ATOM   5914  C  CZ    . PHE B 1 47  ? 163.139 142.803 169.922 1.00 62.97 ? 47  PHE B CZ    1 
ATOM   5915  N  N     . PHE B 1 48  ? 163.705 143.108 165.162 1.00 60.68 ? 48  PHE B N     1 
ATOM   5916  C  CA    . PHE B 1 48  ? 164.606 144.198 164.832 1.00 58.19 ? 48  PHE B CA    1 
ATOM   5917  C  C     . PHE B 1 48  ? 165.091 144.847 166.120 1.00 60.46 ? 48  PHE B C     1 
ATOM   5918  O  O     . PHE B 1 48  ? 164.418 144.787 167.153 1.00 61.16 ? 48  PHE B O     1 
ATOM   5919  C  CB    . PHE B 1 48  ? 163.922 145.243 163.940 1.00 59.03 ? 48  PHE B CB    1 
ATOM   5920  C  CG    . PHE B 1 48  ? 163.384 144.689 162.648 1.00 57.51 ? 48  PHE B CG    1 
ATOM   5921  C  CD1   . PHE B 1 48  ? 162.211 143.952 162.623 1.00 57.38 ? 48  PHE B CD1   1 
ATOM   5922  C  CD2   . PHE B 1 48  ? 164.048 144.915 161.456 1.00 60.09 ? 48  PHE B CD2   1 
ATOM   5923  C  CE1   . PHE B 1 48  ? 161.715 143.450 161.437 1.00 58.76 ? 48  PHE B CE1   1 
ATOM   5924  C  CE2   . PHE B 1 48  ? 163.556 144.414 160.266 1.00 60.19 ? 48  PHE B CE2   1 
ATOM   5925  C  CZ    . PHE B 1 48  ? 162.389 143.681 160.258 1.00 58.50 ? 48  PHE B CZ    1 
ATOM   5926  N  N     . HIS B 1 49  ? 166.274 145.460 166.051 1.00 65.66 ? 49  HIS B N     1 
ATOM   5927  C  CA    . HIS B 1 49  ? 166.861 146.062 167.244 1.00 65.90 ? 49  HIS B CA    1 
ATOM   5928  C  C     . HIS B 1 49  ? 165.979 147.177 167.792 1.00 67.31 ? 49  HIS B C     1 
ATOM   5929  O  O     . HIS B 1 49  ? 165.827 147.317 169.011 1.00 67.84 ? 49  HIS B O     1 
ATOM   5930  C  CB    . HIS B 1 49  ? 168.262 146.588 166.931 1.00 66.72 ? 49  HIS B CB    1 
ATOM   5931  C  CG    . HIS B 1 49  ? 169.133 146.739 168.139 1.00 69.75 ? 49  HIS B CG    1 
ATOM   5932  N  ND1   . HIS B 1 49  ? 168.890 147.678 169.120 1.00 69.16 ? 49  HIS B ND1   1 
ATOM   5933  C  CD2   . HIS B 1 49  ? 170.245 146.070 168.527 1.00 68.63 ? 49  HIS B CD2   1 
ATOM   5934  C  CE1   . HIS B 1 49  ? 169.815 147.581 170.058 1.00 68.14 ? 49  HIS B CE1   1 
ATOM   5935  N  NE2   . HIS B 1 49  ? 170.649 146.613 169.722 1.00 68.81 ? 49  HIS B NE2   1 
ATOM   5936  N  N     . ASN B 1 50  ? 165.391 147.978 166.909 1.00 65.36 ? 50  ASN B N     1 
ATOM   5937  C  CA    . ASN B 1 50  ? 164.504 149.057 167.311 1.00 63.07 ? 50  ASN B CA    1 
ATOM   5938  C  C     . ASN B 1 50  ? 163.317 149.105 166.361 1.00 61.85 ? 50  ASN B C     1 
ATOM   5939  O  O     . ASN B 1 50  ? 163.336 148.513 165.280 1.00 61.12 ? 50  ASN B O     1 
ATOM   5940  C  CB    . ASN B 1 50  ? 165.230 150.409 167.328 1.00 62.00 ? 50  ASN B CB    1 
ATOM   5941  C  CG    . ASN B 1 50  ? 166.055 150.641 166.079 1.00 63.75 ? 50  ASN B CG    1 
ATOM   5942  O  OD1   . ASN B 1 50  ? 165.516 150.905 165.006 1.00 64.56 ? 50  ASN B OD1   1 
ATOM   5943  N  ND2   . ASN B 1 50  ? 167.372 150.541 166.213 1.00 64.21 ? 50  ASN B ND2   1 
ATOM   5944  N  N     . LEU B 1 51  ? 162.270 149.815 166.789 1.00 59.03 ? 51  LEU B N     1 
ATOM   5945  C  CA    . LEU B 1 51  ? 161.094 149.979 165.942 1.00 59.28 ? 51  LEU B CA    1 
ATOM   5946  C  C     . LEU B 1 51  ? 161.417 150.774 164.684 1.00 60.17 ? 51  LEU B C     1 
ATOM   5947  O  O     . LEU B 1 51  ? 160.797 150.553 163.637 1.00 61.13 ? 51  LEU B O     1 
ATOM   5948  C  CB    . LEU B 1 51  ? 159.972 150.657 166.730 1.00 58.62 ? 51  LEU B CB    1 
ATOM   5949  C  CG    . LEU B 1 51  ? 158.689 151.004 165.973 1.00 57.45 ? 51  LEU B CG    1 
ATOM   5950  C  CD1   . LEU B 1 51  ? 158.063 149.761 165.359 1.00 55.15 ? 51  LEU B CD1   1 
ATOM   5951  C  CD2   . LEU B 1 51  ? 157.707 151.707 166.889 1.00 57.45 ? 51  LEU B CD2   1 
ATOM   5952  N  N     . LYS B 1 52  ? 162.377 151.699 164.765 1.00 59.09 ? 52  LYS B N     1 
ATOM   5953  C  CA    . LYS B 1 52  ? 162.761 152.476 163.590 1.00 57.68 ? 52  LYS B CA    1 
ATOM   5954  C  C     . LYS B 1 52  ? 163.308 151.579 162.489 1.00 60.03 ? 52  LYS B C     1 
ATOM   5955  O  O     . LYS B 1 52  ? 162.966 151.749 161.312 1.00 60.40 ? 52  LYS B O     1 
ATOM   5956  C  CB    . LYS B 1 52  ? 163.792 153.534 163.979 1.00 57.25 ? 52  LYS B CB    1 
ATOM   5957  C  CG    . LYS B 1 52  ? 163.765 154.781 163.115 1.00 60.81 ? 52  LYS B CG    1 
ATOM   5958  C  CD    . LYS B 1 52  ? 164.927 155.702 163.450 1.00 62.62 ? 52  LYS B CD    1 
ATOM   5959  C  CE    . LYS B 1 52  ? 164.636 156.528 164.691 1.00 60.23 ? 52  LYS B CE    1 
ATOM   5960  N  NZ    . LYS B 1 52  ? 165.786 156.541 165.636 1.00 60.91 ? 52  LYS B NZ    1 
ATOM   5961  N  N     . GLU B 1 53  ? 164.161 150.618 162.851 1.00 62.37 ? 53  GLU B N     1 
ATOM   5962  C  CA    . GLU B 1 53  ? 164.709 149.702 161.856 1.00 61.10 ? 53  GLU B CA    1 
ATOM   5963  C  C     . GLU B 1 53  ? 163.612 148.856 161.225 1.00 60.74 ? 53  GLU B C     1 
ATOM   5964  O  O     . GLU B 1 53  ? 163.610 148.637 160.008 1.00 61.39 ? 53  GLU B O     1 
ATOM   5965  C  CB    . GLU B 1 53  ? 165.774 148.811 162.495 1.00 60.99 ? 53  GLU B CB    1 
ATOM   5966  C  CG    . GLU B 1 53  ? 166.718 148.162 161.497 1.00 62.19 ? 53  GLU B CG    1 
ATOM   5967  C  CD    . GLU B 1 53  ? 166.980 146.702 161.807 1.00 64.43 ? 53  GLU B CD    1 
ATOM   5968  O  OE1   . GLU B 1 53  ? 167.127 146.363 163.000 1.00 64.92 ? 53  GLU B OE1   1 
ATOM   5969  O  OE2   . GLU B 1 53  ? 167.043 145.893 160.857 1.00 63.58 ? 53  GLU B OE2   1 
ATOM   5970  N  N     . LYS B 1 54  ? 162.667 148.375 162.036 1.00 57.70 ? 54  LYS B N     1 
ATOM   5971  C  CA    . LYS B 1 54  ? 161.564 147.580 161.507 1.00 57.75 ? 54  LYS B CA    1 
ATOM   5972  C  C     . LYS B 1 54  ? 160.715 148.396 160.543 1.00 55.25 ? 54  LYS B C     1 
ATOM   5973  O  O     . LYS B 1 54  ? 160.359 147.925 159.456 1.00 56.32 ? 54  LYS B O     1 
ATOM   5974  C  CB    . LYS B 1 54  ? 160.706 147.048 162.655 1.00 56.87 ? 54  LYS B CB    1 
ATOM   5975  C  CG    . LYS B 1 54  ? 159.386 146.447 162.208 1.00 56.38 ? 54  LYS B CG    1 
ATOM   5976  C  CD    . LYS B 1 54  ? 158.697 145.718 163.344 1.00 57.08 ? 54  LYS B CD    1 
ATOM   5977  C  CE    . LYS B 1 54  ? 157.379 145.115 162.889 1.00 58.21 ? 54  LYS B CE    1 
ATOM   5978  N  NZ    . LYS B 1 54  ? 156.940 144.009 163.782 1.00 58.54 ? 54  LYS B NZ    1 
ATOM   5979  N  N     . LEU B 1 55  ? 160.388 149.632 160.923 1.00 56.67 ? 55  LEU B N     1 
ATOM   5980  C  CA    . LEU B 1 55  ? 159.574 150.479 160.060 1.00 56.83 ? 55  LEU B CA    1 
ATOM   5981  C  C     . LEU B 1 55  ? 160.297 150.796 158.759 1.00 59.10 ? 55  LEU B C     1 
ATOM   5982  O  O     . LEU B 1 55  ? 159.686 150.776 157.684 1.00 61.69 ? 55  LEU B O     1 
ATOM   5983  C  CB    . LEU B 1 55  ? 159.198 151.765 160.793 1.00 57.48 ? 55  LEU B CB    1 
ATOM   5984  C  CG    . LEU B 1 55  ? 158.140 151.621 161.887 1.00 57.67 ? 55  LEU B CG    1 
ATOM   5985  C  CD1   . LEU B 1 55  ? 157.979 152.927 162.640 1.00 58.14 ? 55  LEU B CD1   1 
ATOM   5986  C  CD2   . LEU B 1 55  ? 156.814 151.169 161.296 1.00 57.16 ? 55  LEU B CD2   1 
ATOM   5987  N  N     . ASP B 1 56  ? 161.598 151.092 158.837 1.00 61.03 ? 56  ASP B N     1 
ATOM   5988  C  CA    . ASP B 1 56  ? 162.372 151.375 157.633 1.00 60.62 ? 56  ASP B CA    1 
ATOM   5989  C  C     . ASP B 1 56  ? 162.433 150.159 156.718 1.00 60.04 ? 56  ASP B C     1 
ATOM   5990  O  O     . ASP B 1 56  ? 162.278 150.283 155.497 1.00 62.63 ? 56  ASP B O     1 
ATOM   5991  C  CB    . ASP B 1 56  ? 163.779 151.834 158.012 1.00 62.11 ? 56  ASP B CB    1 
ATOM   5992  C  CG    . ASP B 1 56  ? 163.869 153.334 158.208 1.00 63.88 ? 56  ASP B CG    1 
ATOM   5993  O  OD1   . ASP B 1 56  ? 163.031 154.060 157.634 1.00 62.91 ? 56  ASP B OD1   1 
ATOM   5994  O  OD2   . ASP B 1 56  ? 164.777 153.786 158.936 1.00 63.62 ? 56  ASP B OD2   1 
ATOM   5995  N  N     . TYR B 1 57  ? 162.650 148.973 157.294 1.00 56.00 ? 57  TYR B N     1 
ATOM   5996  C  CA    . TYR B 1 57  ? 162.656 147.752 156.497 1.00 57.10 ? 57  TYR B CA    1 
ATOM   5997  C  C     . TYR B 1 57  ? 161.310 147.530 155.826 1.00 57.47 ? 57  TYR B C     1 
ATOM   5998  O  O     . TYR B 1 57  ? 161.248 147.122 154.661 1.00 58.69 ? 57  TYR B O     1 
ATOM   5999  C  CB    . TYR B 1 57  ? 163.021 146.555 157.376 1.00 58.38 ? 57  TYR B CB    1 
ATOM   6000  C  CG    . TYR B 1 57  ? 162.875 145.213 156.691 1.00 57.44 ? 57  TYR B CG    1 
ATOM   6001  C  CD1   . TYR B 1 57  ? 163.897 144.696 155.907 1.00 57.74 ? 57  TYR B CD1   1 
ATOM   6002  C  CD2   . TYR B 1 57  ? 161.717 144.459 156.836 1.00 58.73 ? 57  TYR B CD2   1 
ATOM   6003  C  CE1   . TYR B 1 57  ? 163.768 143.471 155.282 1.00 57.34 ? 57  TYR B CE1   1 
ATOM   6004  C  CE2   . TYR B 1 57  ? 161.579 143.235 156.214 1.00 59.85 ? 57  TYR B CE2   1 
ATOM   6005  C  CZ    . TYR B 1 57  ? 162.607 142.745 155.439 1.00 60.09 ? 57  TYR B CZ    1 
ATOM   6006  O  OH    . TYR B 1 57  ? 162.472 141.524 154.820 1.00 60.28 ? 57  TYR B OH    1 
ATOM   6007  N  N     . LEU B 1 58  ? 160.218 147.791 156.545 1.00 55.34 ? 58  LEU B N     1 
ATOM   6008  C  CA    . LEU B 1 58  ? 158.897 147.532 155.985 1.00 55.03 ? 58  LEU B CA    1 
ATOM   6009  C  C     . LEU B 1 58  ? 158.550 148.522 154.878 1.00 53.66 ? 58  LEU B C     1 
ATOM   6010  O  O     . LEU B 1 58  ? 157.969 148.134 153.859 1.00 55.01 ? 58  LEU B O     1 
ATOM   6011  C  CB    . LEU B 1 58  ? 157.848 147.549 157.095 1.00 54.11 ? 58  LEU B CB    1 
ATOM   6012  C  CG    . LEU B 1 58  ? 157.951 146.340 158.029 1.00 53.51 ? 58  LEU B CG    1 
ATOM   6013  C  CD1   . LEU B 1 58  ? 157.132 146.533 159.291 1.00 53.73 ? 58  LEU B CD1   1 
ATOM   6014  C  CD2   . LEU B 1 58  ? 157.537 145.068 157.308 1.00 52.41 ? 58  LEU B CD2   1 
ATOM   6015  N  N     . VAL B 1 59  ? 158.890 149.803 155.048 1.00 56.93 ? 59  VAL B N     1 
ATOM   6016  C  CA    . VAL B 1 59  ? 158.559 150.767 154.000 1.00 59.26 ? 59  VAL B CA    1 
ATOM   6017  C  C     . VAL B 1 59  ? 159.456 150.567 152.783 1.00 60.71 ? 59  VAL B C     1 
ATOM   6018  O  O     . VAL B 1 59  ? 158.989 150.614 151.639 1.00 58.37 ? 59  VAL B O     1 
ATOM   6019  C  CB    . VAL B 1 59  ? 158.631 152.218 154.516 1.00 58.34 ? 59  VAL B CB    1 
ATOM   6020  C  CG1   . VAL B 1 59  ? 157.410 152.550 155.368 1.00 57.40 ? 59  VAL B CG1   1 
ATOM   6021  C  CG2   . VAL B 1 59  ? 159.936 152.501 155.238 1.00 58.57 ? 59  VAL B CG2   1 
ATOM   6022  N  N     . GLU B 1 60  ? 160.756 150.340 153.003 1.00 61.66 ? 60  GLU B N     1 
ATOM   6023  C  CA    . GLU B 1 60  ? 161.689 150.270 151.885 1.00 60.98 ? 60  GLU B CA    1 
ATOM   6024  C  C     . GLU B 1 60  ? 161.581 148.960 151.114 1.00 61.72 ? 60  GLU B C     1 
ATOM   6025  O  O     . GLU B 1 60  ? 161.947 148.913 149.934 1.00 63.20 ? 60  GLU B O     1 
ATOM   6026  C  CB    . GLU B 1 60  ? 163.122 150.485 152.381 1.00 61.09 ? 60  GLU B CB    1 
ATOM   6027  C  CG    . GLU B 1 60  ? 163.833 149.229 152.847 1.00 61.76 ? 60  GLU B CG    1 
ATOM   6028  C  CD    . GLU B 1 60  ? 165.059 149.533 153.688 1.00 64.05 ? 60  GLU B CD    1 
ATOM   6029  O  OE1   . GLU B 1 60  ? 165.362 150.727 153.890 1.00 62.90 ? 60  GLU B OE1   1 
ATOM   6030  O  OE2   . GLU B 1 60  ? 165.717 148.577 154.149 1.00 61.76 ? 60  GLU B OE2   1 
ATOM   6031  N  N     . ASN B 1 61  ? 161.087 147.894 151.744 1.00 58.11 ? 61  ASN B N     1 
ATOM   6032  C  CA    . ASN B 1 61  ? 160.908 146.613 151.075 1.00 58.28 ? 61  ASN B CA    1 
ATOM   6033  C  C     . ASN B 1 61  ? 159.505 146.436 150.509 1.00 58.34 ? 61  ASN B C     1 
ATOM   6034  O  O     . ASN B 1 61  ? 159.076 145.297 150.290 1.00 59.50 ? 61  ASN B O     1 
ATOM   6035  C  CB    . ASN B 1 61  ? 161.238 145.462 152.027 1.00 59.00 ? 61  ASN B CB    1 
ATOM   6036  C  CG    . ASN B 1 61  ? 162.727 145.220 152.152 1.00 60.62 ? 61  ASN B CG    1 
ATOM   6037  O  OD1   . ASN B 1 61  ? 163.286 144.355 151.478 1.00 60.06 ? 61  ASN B OD1   1 
ATOM   6038  N  ND2   . ASN B 1 61  ? 163.380 145.984 153.018 1.00 60.25 ? 61  ASN B ND2   1 
ATOM   6039  N  N     . GLN B 1 62  ? 158.786 147.536 150.277 1.00 57.06 ? 62  GLN B N     1 
ATOM   6040  C  CA    . GLN B 1 62  ? 157.467 147.512 149.643 1.00 58.43 ? 62  GLN B CA    1 
ATOM   6041  C  C     . GLN B 1 62  ? 156.464 146.685 150.445 1.00 57.90 ? 62  GLN B C     1 
ATOM   6042  O  O     . GLN B 1 62  ? 155.674 145.922 149.887 1.00 58.97 ? 62  GLN B O     1 
ATOM   6043  C  CB    . GLN B 1 62  ? 157.558 147.005 148.201 1.00 58.14 ? 62  GLN B CB    1 
ATOM   6044  C  CG    . GLN B 1 62  ? 158.530 147.784 147.329 1.00 58.07 ? 62  GLN B CG    1 
ATOM   6045  C  CD    . GLN B 1 62  ? 158.219 149.266 147.289 1.00 60.64 ? 62  GLN B CD    1 
ATOM   6046  O  OE1   . GLN B 1 62  ? 158.813 150.058 148.021 1.00 60.11 ? 62  GLN B OE1   1 
ATOM   6047  N  NE2   . GLN B 1 62  ? 157.282 149.650 146.431 1.00 58.99 ? 62  GLN B NE2   1 
ATOM   6048  N  N     . TYR B 1 63  ? 156.492 146.839 151.767 1.00 56.64 ? 63  TYR B N     1 
ATOM   6049  C  CA    . TYR B 1 63  ? 155.506 146.213 152.640 1.00 56.08 ? 63  TYR B CA    1 
ATOM   6050  C  C     . TYR B 1 63  ? 154.469 147.199 153.155 1.00 55.04 ? 63  TYR B C     1 
ATOM   6051  O  O     . TYR B 1 63  ? 153.286 146.859 153.239 1.00 55.44 ? 63  TYR B O     1 
ATOM   6052  C  CB    . TYR B 1 63  ? 156.194 145.540 153.832 1.00 53.69 ? 63  TYR B CB    1 
ATOM   6053  C  CG    . TYR B 1 63  ? 156.906 144.254 153.488 1.00 55.91 ? 63  TYR B CG    1 
ATOM   6054  C  CD1   . TYR B 1 63  ? 156.226 143.199 152.896 1.00 54.20 ? 63  TYR B CD1   1 
ATOM   6055  C  CD2   . TYR B 1 63  ? 158.257 144.093 153.760 1.00 56.34 ? 63  TYR B CD2   1 
ATOM   6056  C  CE1   . TYR B 1 63  ? 156.873 142.022 152.582 1.00 55.04 ? 63  TYR B CE1   1 
ATOM   6057  C  CE2   . TYR B 1 63  ? 158.911 142.921 153.451 1.00 55.95 ? 63  TYR B CE2   1 
ATOM   6058  C  CZ    . TYR B 1 63  ? 158.215 141.888 152.862 1.00 57.96 ? 63  TYR B CZ    1 
ATOM   6059  O  OH    . TYR B 1 63  ? 158.867 140.717 152.552 1.00 60.40 ? 63  TYR B OH    1 
ATOM   6060  N  N     . TYR B 1 64  ? 154.886 148.412 153.499 1.00 51.27 ? 64  TYR B N     1 
ATOM   6061  C  CA    . TYR B 1 64  ? 154.000 149.451 153.997 1.00 49.76 ? 64  TYR B CA    1 
ATOM   6062  C  C     . TYR B 1 64  ? 153.899 150.586 152.987 1.00 52.16 ? 64  TYR B C     1 
ATOM   6063  O  O     . TYR B 1 64  ? 154.581 150.606 151.960 1.00 55.68 ? 64  TYR B O     1 
ATOM   6064  C  CB    . TYR B 1 64  ? 154.496 149.996 155.340 1.00 51.19 ? 64  TYR B CB    1 
ATOM   6065  C  CG    . TYR B 1 64  ? 154.208 149.103 156.520 1.00 50.02 ? 64  TYR B CG    1 
ATOM   6066  C  CD1   . TYR B 1 64  ? 153.454 147.947 156.375 1.00 49.03 ? 64  TYR B CD1   1 
ATOM   6067  C  CD2   . TYR B 1 64  ? 154.687 149.419 157.781 1.00 50.36 ? 64  TYR B CD2   1 
ATOM   6068  C  CE1   . TYR B 1 64  ? 153.191 147.130 157.454 1.00 46.58 ? 64  TYR B CE1   1 
ATOM   6069  C  CE2   . TYR B 1 64  ? 154.429 148.611 158.862 1.00 50.68 ? 64  TYR B CE2   1 
ATOM   6070  C  CZ    . TYR B 1 64  ? 153.681 147.468 158.695 1.00 49.78 ? 64  TYR B CZ    1 
ATOM   6071  O  OH    . TYR B 1 64  ? 153.426 146.663 159.778 1.00 54.17 ? 64  TYR B OH    1 
ATOM   6072  N  N     . GLU B 1 65  ? 153.033 151.542 153.302 1.00 55.85 ? 65  GLU B N     1 
ATOM   6073  C  CA    . GLU B 1 65  ? 152.902 152.770 152.532 1.00 56.17 ? 65  GLU B CA    1 
ATOM   6074  C  C     . GLU B 1 65  ? 153.573 153.904 153.292 1.00 57.52 ? 65  GLU B C     1 
ATOM   6075  O  O     . GLU B 1 65  ? 153.274 154.132 154.468 1.00 57.81 ? 65  GLU B O     1 
ATOM   6076  C  CB    . GLU B 1 65  ? 151.432 153.103 152.273 1.00 53.92 ? 65  GLU B CB    1 
ATOM   6077  C  CG    . GLU B 1 65  ? 150.712 152.107 151.381 1.00 52.71 ? 65  GLU B CG    1 
ATOM   6078  C  CD    . GLU B 1 65  ? 149.216 152.347 151.332 1.00 57.89 ? 65  GLU B CD    1 
ATOM   6079  O  OE1   . GLU B 1 65  ? 148.604 152.521 152.406 1.00 58.05 ? 65  GLU B OE1   1 
ATOM   6080  O  OE2   . GLU B 1 65  ? 148.651 152.363 150.218 1.00 56.20 ? 65  GLU B OE2   1 
ATOM   6081  N  N     . GLU B 1 66  ? 154.488 154.606 152.622 1.00 57.87 ? 66  GLU B N     1 
ATOM   6082  C  CA    . GLU B 1 66  ? 155.176 155.719 153.263 1.00 59.54 ? 66  GLU B CA    1 
ATOM   6083  C  C     . GLU B 1 66  ? 154.267 156.926 153.456 1.00 59.79 ? 66  GLU B C     1 
ATOM   6084  O  O     . GLU B 1 66  ? 154.567 157.784 154.292 1.00 58.46 ? 66  GLU B O     1 
ATOM   6085  C  CB    . GLU B 1 66  ? 156.407 156.113 152.443 1.00 60.63 ? 66  GLU B CB    1 
ATOM   6086  C  CG    . GLU B 1 66  ? 157.421 157.007 153.163 1.00 60.64 ? 66  GLU B CG    1 
ATOM   6087  C  CD    . GLU B 1 66  ? 157.736 156.549 154.579 1.00 63.10 ? 66  GLU B CD    1 
ATOM   6088  O  OE1   . GLU B 1 66  ? 156.973 156.887 155.509 1.00 61.57 ? 66  GLU B OE1   1 
ATOM   6089  O  OE2   . GLU B 1 66  ? 158.755 155.850 154.761 1.00 61.58 ? 66  GLU B OE2   1 
ATOM   6090  N  N     . GLU B 1 67  ? 153.162 157.006 152.710 1.00 58.00 ? 67  GLU B N     1 
ATOM   6091  C  CA    . GLU B 1 67  ? 152.311 158.191 152.761 1.00 56.14 ? 67  GLU B CA    1 
ATOM   6092  C  C     . GLU B 1 67  ? 151.664 158.358 154.131 1.00 58.82 ? 67  GLU B C     1 
ATOM   6093  O  O     . GLU B 1 67  ? 151.712 159.444 154.720 1.00 59.72 ? 67  GLU B O     1 
ATOM   6094  C  CB    . GLU B 1 67  ? 151.244 158.114 151.670 1.00 57.93 ? 67  GLU B CB    1 
ATOM   6095  C  CG    . GLU B 1 67  ? 151.804 158.010 150.262 1.00 58.15 ? 67  GLU B CG    1 
ATOM   6096  C  CD    . GLU B 1 67  ? 151.854 156.581 149.761 1.00 60.57 ? 67  GLU B CD    1 
ATOM   6097  O  OE1   . GLU B 1 67  ? 150.778 156.007 149.491 1.00 61.25 ? 67  GLU B OE1   1 
ATOM   6098  O  OE2   . GLU B 1 67  ? 152.969 156.032 149.637 1.00 61.51 ? 67  GLU B OE2   1 
ATOM   6099  N  N     . PHE B 1 68  ? 151.052 157.295 154.655 1.00 52.91 ? 68  PHE B N     1 
ATOM   6100  C  CA    . PHE B 1 68  ? 150.349 157.414 155.928 1.00 49.36 ? 68  PHE B CA    1 
ATOM   6101  C  C     . PHE B 1 68  ? 151.307 157.445 157.112 1.00 49.86 ? 68  PHE B C     1 
ATOM   6102  O  O     . PHE B 1 68  ? 151.001 158.074 158.131 1.00 52.53 ? 68  PHE B O     1 
ATOM   6103  C  CB    . PHE B 1 68  ? 149.330 156.278 156.080 1.00 48.95 ? 68  PHE B CB    1 
ATOM   6104  C  CG    . PHE B 1 68  ? 149.885 155.025 156.698 1.00 46.25 ? 68  PHE B CG    1 
ATOM   6105  C  CD1   . PHE B 1 68  ? 150.528 154.081 155.919 1.00 48.91 ? 68  PHE B CD1   1 
ATOM   6106  C  CD2   . PHE B 1 68  ? 149.736 154.776 158.053 1.00 45.50 ? 68  PHE B CD2   1 
ATOM   6107  C  CE1   . PHE B 1 68  ? 151.034 152.925 156.482 1.00 48.62 ? 68  PHE B CE1   1 
ATOM   6108  C  CE2   . PHE B 1 68  ? 150.240 153.622 158.620 1.00 47.40 ? 68  PHE B CE2   1 
ATOM   6109  C  CZ    . PHE B 1 68  ? 150.886 152.694 157.832 1.00 48.80 ? 68  PHE B CZ    1 
ATOM   6110  N  N     . LEU B 1 69  ? 152.460 156.783 157.005 1.00 49.41 ? 69  LEU B N     1 
ATOM   6111  C  CA    . LEU B 1 69  ? 153.426 156.810 158.096 1.00 50.85 ? 69  LEU B CA    1 
ATOM   6112  C  C     . LEU B 1 69  ? 154.157 158.144 158.181 1.00 53.02 ? 69  LEU B C     1 
ATOM   6113  O  O     . LEU B 1 69  ? 154.593 158.537 159.268 1.00 50.98 ? 69  LEU B O     1 
ATOM   6114  C  CB    . LEU B 1 69  ? 154.432 155.670 157.941 1.00 50.43 ? 69  LEU B CB    1 
ATOM   6115  C  CG    . LEU B 1 69  ? 153.962 154.309 158.455 1.00 50.07 ? 69  LEU B CG    1 
ATOM   6116  C  CD1   . LEU B 1 69  ? 154.950 153.218 158.081 1.00 49.97 ? 69  LEU B CD1   1 
ATOM   6117  C  CD2   . LEU B 1 69  ? 153.745 154.350 159.959 1.00 50.22 ? 69  LEU B CD2   1 
ATOM   6118  N  N     . SER B 1 70  ? 154.297 158.850 157.056 1.00 56.58 ? 70  SER B N     1 
ATOM   6119  C  CA    . SER B 1 70  ? 154.953 160.152 157.068 1.00 54.09 ? 70  SER B CA    1 
ATOM   6120  C  C     . SER B 1 70  ? 154.124 161.210 157.781 1.00 52.26 ? 70  SER B C     1 
ATOM   6121  O  O     . SER B 1 70  ? 154.654 162.278 158.108 1.00 53.82 ? 70  SER B O     1 
ATOM   6122  C  CB    . SER B 1 70  ? 155.250 160.608 155.640 1.00 53.54 ? 70  SER B CB    1 
ATOM   6123  O  OG    . SER B 1 70  ? 154.084 160.556 154.839 1.00 54.19 ? 70  SER B OG    1 
ATOM   6124  N  N     . LEU B 1 71  ? 152.841 160.943 158.026 1.00 47.53 ? 71  LEU B N     1 
ATOM   6125  C  CA    . LEU B 1 71  ? 151.980 161.900 158.708 1.00 46.72 ? 71  LEU B CA    1 
ATOM   6126  C  C     . LEU B 1 71  ? 152.317 162.050 160.184 1.00 47.32 ? 71  LEU B C     1 
ATOM   6127  O  O     . LEU B 1 71  ? 151.818 162.982 160.823 1.00 49.68 ? 71  LEU B O     1 
ATOM   6128  C  CB    . LEU B 1 71  ? 150.516 161.484 158.552 1.00 46.58 ? 71  LEU B CB    1 
ATOM   6129  C  CG    . LEU B 1 71  ? 149.900 161.703 157.170 1.00 49.77 ? 71  LEU B CG    1 
ATOM   6130  C  CD1   . LEU B 1 71  ? 148.386 161.705 157.254 1.00 48.58 ? 71  LEU B CD1   1 
ATOM   6131  C  CD2   . LEU B 1 71  ? 150.405 162.999 156.555 1.00 48.90 ? 71  LEU B CD2   1 
ATOM   6132  N  N     . TYR B 1 72  ? 153.141 161.165 160.736 1.00 45.13 ? 72  TYR B N     1 
ATOM   6133  C  CA    . TYR B 1 72  ? 153.535 161.211 162.135 1.00 44.50 ? 72  TYR B CA    1 
ATOM   6134  C  C     . TYR B 1 72  ? 155.047 161.323 162.240 1.00 47.77 ? 72  TYR B C     1 
ATOM   6135  O  O     . TYR B 1 72  ? 155.779 160.761 161.420 1.00 49.07 ? 72  TYR B O     1 
ATOM   6136  C  CB    . TYR B 1 72  ? 153.079 159.959 162.895 1.00 46.11 ? 72  TYR B CB    1 
ATOM   6137  C  CG    . TYR B 1 72  ? 151.643 159.554 162.667 1.00 44.01 ? 72  TYR B CG    1 
ATOM   6138  C  CD1   . TYR B 1 72  ? 151.292 158.747 161.593 1.00 41.37 ? 72  TYR B CD1   1 
ATOM   6139  C  CD2   . TYR B 1 72  ? 150.643 159.955 163.540 1.00 45.06 ? 72  TYR B CD2   1 
ATOM   6140  C  CE1   . TYR B 1 72  ? 149.985 158.370 161.384 1.00 41.12 ? 72  TYR B CE1   1 
ATOM   6141  C  CE2   . TYR B 1 72  ? 149.332 159.579 163.340 1.00 42.88 ? 72  TYR B CE2   1 
ATOM   6142  C  CZ    . TYR B 1 72  ? 149.009 158.787 162.261 1.00 42.92 ? 72  TYR B CZ    1 
ATOM   6143  O  OH    . TYR B 1 72  ? 147.705 158.409 162.055 1.00 45.61 ? 72  TYR B OH    1 
ATOM   6144  N  N     . SER B 1 73  ? 155.511 162.051 163.250 1.00 54.54 ? 73  SER B N     1 
ATOM   6145  C  CA    . SER B 1 73  ? 156.899 161.926 163.659 1.00 54.82 ? 73  SER B CA    1 
ATOM   6146  C  C     . SER B 1 73  ? 157.125 160.534 164.235 1.00 54.83 ? 73  SER B C     1 
ATOM   6147  O  O     . SER B 1 73  ? 156.200 159.895 164.744 1.00 57.41 ? 73  SER B O     1 
ATOM   6148  C  CB    . SER B 1 73  ? 157.256 162.994 164.691 1.00 53.30 ? 73  SER B CB    1 
ATOM   6149  O  OG    . SER B 1 73  ? 156.624 162.735 165.931 1.00 52.49 ? 73  SER B OG    1 
ATOM   6150  N  N     . PHE B 1 74  ? 158.367 160.053 164.141 1.00 56.24 ? 74  PHE B N     1 
ATOM   6151  C  CA    . PHE B 1 74  ? 158.644 158.699 164.609 1.00 56.40 ? 74  PHE B CA    1 
ATOM   6152  C  C     . PHE B 1 74  ? 158.364 158.546 166.097 1.00 55.82 ? 74  PHE B C     1 
ATOM   6153  O  O     . PHE B 1 74  ? 158.059 157.441 166.557 1.00 59.39 ? 74  PHE B O     1 
ATOM   6154  C  CB    . PHE B 1 74  ? 160.087 158.299 164.311 1.00 56.63 ? 74  PHE B CB    1 
ATOM   6155  C  CG    . PHE B 1 74  ? 160.469 156.980 164.913 1.00 57.27 ? 74  PHE B CG    1 
ATOM   6156  C  CD1   . PHE B 1 74  ? 159.927 155.803 164.426 1.00 56.49 ? 74  PHE B CD1   1 
ATOM   6157  C  CD2   . PHE B 1 74  ? 161.340 156.916 165.987 1.00 57.68 ? 74  PHE B CD2   1 
ATOM   6158  C  CE1   . PHE B 1 74  ? 160.260 154.588 164.984 1.00 58.33 ? 74  PHE B CE1   1 
ATOM   6159  C  CE2   . PHE B 1 74  ? 161.679 155.702 166.549 1.00 57.92 ? 74  PHE B CE2   1 
ATOM   6160  C  CZ    . PHE B 1 74  ? 161.137 154.537 166.048 1.00 59.59 ? 74  PHE B CZ    1 
ATOM   6161  N  N     . GLU B 1 75  ? 158.464 159.632 166.866 1.00 55.93 ? 75  GLU B N     1 
ATOM   6162  C  CA    . GLU B 1 75  ? 158.131 159.557 168.284 1.00 58.25 ? 75  GLU B CA    1 
ATOM   6163  C  C     . GLU B 1 75  ? 156.665 159.197 168.485 1.00 60.00 ? 75  GLU B C     1 
ATOM   6164  O  O     . GLU B 1 75  ? 156.328 158.394 169.363 1.00 59.53 ? 75  GLU B O     1 
ATOM   6165  C  CB    . GLU B 1 75  ? 158.462 160.881 168.972 1.00 56.73 ? 75  GLU B CB    1 
ATOM   6166  C  CG    . GLU B 1 75  ? 159.949 161.185 169.039 1.00 57.36 ? 75  GLU B CG    1 
ATOM   6167  C  CD    . GLU B 1 75  ? 160.754 160.025 169.591 1.00 62.30 ? 75  GLU B CD    1 
ATOM   6168  O  OE1   . GLU B 1 75  ? 160.504 159.622 170.747 1.00 62.38 ? 75  GLU B OE1   1 
ATOM   6169  O  OE2   . GLU B 1 75  ? 161.637 159.515 168.870 1.00 61.15 ? 75  GLU B OE2   1 
ATOM   6170  N  N     . ASP B 1 76  ? 155.777 159.779 167.676 1.00 56.62 ? 76  ASP B N     1 
ATOM   6171  C  CA    . ASP B 1 76  ? 154.356 159.467 167.785 1.00 54.99 ? 76  ASP B CA    1 
ATOM   6172  C  C     . ASP B 1 76  ? 154.078 158.010 167.437 1.00 55.65 ? 76  ASP B C     1 
ATOM   6173  O  O     . ASP B 1 76  ? 153.286 157.343 168.112 1.00 58.43 ? 76  ASP B O     1 
ATOM   6174  C  CB    . ASP B 1 76  ? 153.549 160.400 166.884 1.00 55.46 ? 76  ASP B CB    1 
ATOM   6175  C  CG    . ASP B 1 76  ? 153.664 161.852 167.299 1.00 58.04 ? 76  ASP B CG    1 
ATOM   6176  O  OD1   . ASP B 1 76  ? 153.677 162.122 168.518 1.00 57.83 ? 76  ASP B OD1   1 
ATOM   6177  O  OD2   . ASP B 1 76  ? 153.735 162.723 166.408 1.00 57.45 ? 76  ASP B OD2   1 
ATOM   6178  N  N     . ILE B 1 77  ? 154.719 157.500 166.383 1.00 49.10 ? 77  ILE B N     1 
ATOM   6179  C  CA    . ILE B 1 77  ? 154.541 156.099 166.010 1.00 49.26 ? 77  ILE B CA    1 
ATOM   6180  C  C     . ILE B 1 77  ? 155.074 155.187 167.106 1.00 50.68 ? 77  ILE B C     1 
ATOM   6181  O  O     . ILE B 1 77  ? 154.480 154.146 167.417 1.00 53.48 ? 77  ILE B O     1 
ATOM   6182  C  CB    . ILE B 1 77  ? 155.219 155.818 164.657 1.00 49.68 ? 77  ILE B CB    1 
ATOM   6183  C  CG1   . ILE B 1 77  ? 154.605 156.691 163.564 1.00 49.01 ? 77  ILE B CG1   1 
ATOM   6184  C  CG2   . ILE B 1 77  ? 155.094 154.350 164.292 1.00 49.56 ? 77  ILE B CG2   1 
ATOM   6185  C  CD1   . ILE B 1 77  ? 155.415 156.730 162.293 1.00 50.14 ? 77  ILE B CD1   1 
ATOM   6186  N  N     . LYS B 1 78  ? 156.208 155.559 167.703 1.00 52.55 ? 78  LYS B N     1 
ATOM   6187  C  CA    . LYS B 1 78  ? 156.765 154.773 168.797 1.00 51.99 ? 78  LYS B CA    1 
ATOM   6188  C  C     . LYS B 1 78  ? 155.820 154.747 169.989 1.00 52.96 ? 78  LYS B C     1 
ATOM   6189  O  O     . LYS B 1 78  ? 155.643 153.704 170.625 1.00 55.56 ? 78  LYS B O     1 
ATOM   6190  C  CB    . LYS B 1 78  ? 158.129 155.331 169.199 1.00 54.92 ? 78  LYS B CB    1 
ATOM   6191  C  CG    . LYS B 1 78  ? 158.838 154.524 170.270 1.00 54.91 ? 78  LYS B CG    1 
ATOM   6192  C  CD    . LYS B 1 78  ? 160.266 154.211 169.858 1.00 55.10 ? 78  LYS B CD    1 
ATOM   6193  C  CE    . LYS B 1 78  ? 161.262 154.712 170.889 1.00 56.03 ? 78  LYS B CE    1 
ATOM   6194  N  NZ    . LYS B 1 78  ? 162.667 154.507 170.442 1.00 55.40 ? 78  LYS B NZ    1 
ATOM   6195  N  N     . GLU B 1 79  ? 155.196 155.884 170.305 1.00 52.82 ? 79  GLU B N     1 
ATOM   6196  C  CA    . GLU B 1 79  ? 154.234 155.909 171.404 1.00 52.28 ? 79  GLU B CA    1 
ATOM   6197  C  C     . GLU B 1 79  ? 152.982 155.104 171.078 1.00 50.68 ? 79  GLU B C     1 
ATOM   6198  O  O     . GLU B 1 79  ? 152.401 154.478 171.970 1.00 52.14 ? 79  GLU B O     1 
ATOM   6199  C  CB    . GLU B 1 79  ? 153.868 157.351 171.758 1.00 52.25 ? 79  GLU B CB    1 
ATOM   6200  C  CG    . GLU B 1 79  ? 155.033 158.218 172.242 1.00 54.54 ? 79  GLU B CG    1 
ATOM   6201  C  CD    . GLU B 1 79  ? 156.109 157.447 173.001 1.00 56.45 ? 79  GLU B CD    1 
ATOM   6202  O  OE1   . GLU B 1 79  ? 157.305 157.697 172.741 1.00 55.10 ? 79  GLU B OE1   1 
ATOM   6203  O  OE2   . GLU B 1 79  ? 155.772 156.635 173.890 1.00 54.99 ? 79  GLU B OE2   1 
ATOM   6204  N  N     . VAL B 1 80  ? 152.552 155.105 169.815 1.00 47.81 ? 80  VAL B N     1 
ATOM   6205  C  CA    . VAL B 1 80  ? 151.414 154.280 169.417 1.00 45.27 ? 80  VAL B CA    1 
ATOM   6206  C  C     . VAL B 1 80  ? 151.739 152.800 169.596 1.00 48.33 ? 80  VAL B C     1 
ATOM   6207  O  O     . VAL B 1 80  ? 150.933 152.026 170.133 1.00 49.90 ? 80  VAL B O     1 
ATOM   6208  C  CB    . VAL B 1 80  ? 151.008 154.608 167.968 1.00 45.21 ? 80  VAL B CB    1 
ATOM   6209  C  CG1   . VAL B 1 80  ? 150.097 153.538 167.405 1.00 45.94 ? 80  VAL B CG1   1 
ATOM   6210  C  CG2   . VAL B 1 80  ? 150.333 155.968 167.907 1.00 45.74 ? 80  VAL B CG2   1 
ATOM   6211  N  N     . PHE B 1 81  ? 152.932 152.386 169.163 1.00 47.37 ? 81  PHE B N     1 
ATOM   6212  C  CA    . PHE B 1 81  ? 153.350 151.000 169.356 1.00 43.77 ? 81  PHE B CA    1 
ATOM   6213  C  C     . PHE B 1 81  ? 153.498 150.670 170.837 1.00 45.19 ? 81  PHE B C     1 
ATOM   6214  O  O     . PHE B 1 81  ? 153.205 149.547 171.262 1.00 49.91 ? 81  PHE B O     1 
ATOM   6215  C  CB    . PHE B 1 81  ? 154.657 150.737 168.610 1.00 44.10 ? 81  PHE B CB    1 
ATOM   6216  C  CG    . PHE B 1 81  ? 154.465 150.305 167.185 1.00 43.67 ? 81  PHE B CG    1 
ATOM   6217  C  CD1   . PHE B 1 81  ? 154.169 151.231 166.200 1.00 44.34 ? 81  PHE B CD1   1 
ATOM   6218  C  CD2   . PHE B 1 81  ? 154.584 148.973 166.830 1.00 43.97 ? 81  PHE B CD2   1 
ATOM   6219  C  CE1   . PHE B 1 81  ? 153.991 150.835 164.888 1.00 44.91 ? 81  PHE B CE1   1 
ATOM   6220  C  CE2   . PHE B 1 81  ? 154.409 148.573 165.520 1.00 44.88 ? 81  PHE B CE2   1 
ATOM   6221  C  CZ    . PHE B 1 81  ? 154.112 149.506 164.549 1.00 43.99 ? 81  PHE B CZ    1 
ATOM   6222  N  N     . LYS B 1 82  ? 153.958 151.635 171.636 1.00 47.68 ? 82  LYS B N     1 
ATOM   6223  C  CA    . LYS B 1 82  ? 154.017 151.449 173.082 1.00 50.55 ? 82  LYS B CA    1 
ATOM   6224  C  C     . LYS B 1 82  ? 152.629 151.199 173.652 1.00 50.84 ? 82  LYS B C     1 
ATOM   6225  O  O     . LYS B 1 82  ? 152.439 150.324 174.503 1.00 50.96 ? 82  LYS B O     1 
ATOM   6226  C  CB    . LYS B 1 82  ? 154.644 152.678 173.740 1.00 52.02 ? 82  LYS B CB    1 
ATOM   6227  C  CG    . LYS B 1 82  ? 155.969 152.438 174.436 1.00 52.03 ? 82  LYS B CG    1 
ATOM   6228  C  CD    . LYS B 1 82  ? 157.116 152.324 173.452 1.00 53.19 ? 82  LYS B CD    1 
ATOM   6229  C  CE    . LYS B 1 82  ? 158.449 152.443 174.171 1.00 53.69 ? 82  LYS B CE    1 
ATOM   6230  N  NZ    . LYS B 1 82  ? 159.469 151.506 173.633 1.00 54.43 ? 82  LYS B NZ    1 
ATOM   6231  N  N     . THR B 1 83  ? 151.644 151.972 173.192 1.00 46.47 ? 83  THR B N     1 
ATOM   6232  C  CA    . THR B 1 83  ? 150.272 151.791 173.651 1.00 45.12 ? 83  THR B CA    1 
ATOM   6233  C  C     . THR B 1 83  ? 149.744 150.415 173.269 1.00 46.44 ? 83  THR B C     1 
ATOM   6234  O  O     . THR B 1 83  ? 149.036 149.774 174.054 1.00 49.90 ? 83  THR B O     1 
ATOM   6235  C  CB    . THR B 1 83  ? 149.378 152.889 173.079 1.00 44.84 ? 83  THR B CB    1 
ATOM   6236  O  OG1   . THR B 1 83  ? 149.964 154.168 173.346 1.00 50.07 ? 83  THR B OG1   1 
ATOM   6237  C  CG2   . THR B 1 83  ? 147.998 152.836 173.711 1.00 46.71 ? 83  THR B CG2   1 
ATOM   6238  N  N     . ALA B 1 84  ? 150.071 149.948 172.062 1.00 41.64 ? 84  ALA B N     1 
ATOM   6239  C  CA    . ALA B 1 84  ? 149.636 148.614 171.657 1.00 38.48 ? 84  ALA B CA    1 
ATOM   6240  C  C     . ALA B 1 84  ? 150.264 147.531 172.526 1.00 41.92 ? 84  ALA B C     1 
ATOM   6241  O  O     . ALA B 1 84  ? 149.583 146.583 172.934 1.00 48.02 ? 84  ALA B O     1 
ATOM   6242  C  CB    . ALA B 1 84  ? 149.966 148.374 170.188 1.00 40.73 ? 84  ALA B CB    1 
ATOM   6243  N  N     . TYR B 1 85  ? 151.561 147.649 172.818 1.00 47.00 ? 85  TYR B N     1 
ATOM   6244  C  CA    . TYR B 1 85  ? 152.241 146.642 173.622 1.00 43.22 ? 85  TYR B CA    1 
ATOM   6245  C  C     . TYR B 1 85  ? 152.046 146.846 175.117 1.00 44.67 ? 85  TYR B C     1 
ATOM   6246  O  O     . TYR B 1 85  ? 152.366 145.942 175.896 1.00 46.69 ? 85  TYR B O     1 
ATOM   6247  C  CB    . TYR B 1 85  ? 153.735 146.625 173.294 1.00 44.32 ? 85  TYR B CB    1 
ATOM   6248  C  CG    . TYR B 1 85  ? 154.068 145.946 171.985 1.00 44.32 ? 85  TYR B CG    1 
ATOM   6249  C  CD1   . TYR B 1 85  ? 154.059 146.651 170.791 1.00 45.04 ? 85  TYR B CD1   1 
ATOM   6250  C  CD2   . TYR B 1 85  ? 154.393 144.597 171.945 1.00 44.05 ? 85  TYR B CD2   1 
ATOM   6251  C  CE1   . TYR B 1 85  ? 154.363 146.035 169.595 1.00 44.52 ? 85  TYR B CE1   1 
ATOM   6252  C  CE2   . TYR B 1 85  ? 154.697 143.973 170.754 1.00 44.74 ? 85  TYR B CE2   1 
ATOM   6253  C  CZ    . TYR B 1 85  ? 154.680 144.696 169.583 1.00 46.03 ? 85  TYR B CZ    1 
ATOM   6254  O  OH    . TYR B 1 85  ? 154.984 144.077 168.394 1.00 47.57 ? 85  TYR B OH    1 
ATOM   6255  N  N     . ALA B 1 86  ? 151.534 148.005 175.538 1.00 47.09 ? 86  ALA B N     1 
ATOM   6256  C  CA    . ALA B 1 86  ? 151.273 148.227 176.955 1.00 47.12 ? 86  ALA B CA    1 
ATOM   6257  C  C     . ALA B 1 86  ? 150.155 147.341 177.482 1.00 49.10 ? 86  ALA B C     1 
ATOM   6258  O  O     . ALA B 1 86  ? 150.124 147.050 178.682 1.00 48.13 ? 86  ALA B O     1 
ATOM   6259  C  CB    . ALA B 1 86  ? 150.929 149.694 177.210 1.00 43.94 ? 86  ALA B CB    1 
ATOM   6260  N  N     . LYS B 1 87  ? 149.238 146.908 176.616 1.00 42.66 ? 87  LYS B N     1 
ATOM   6261  C  CA    . LYS B 1 87  ? 148.135 146.060 177.045 1.00 43.21 ? 87  LYS B CA    1 
ATOM   6262  C  C     . LYS B 1 87  ? 148.567 144.630 177.336 1.00 45.36 ? 87  LYS B C     1 
ATOM   6263  O  O     . LYS B 1 87  ? 147.865 143.928 178.071 1.00 44.58 ? 87  LYS B O     1 
ATOM   6264  C  CB    . LYS B 1 87  ? 147.034 146.053 175.983 1.00 45.39 ? 87  LYS B CB    1 
ATOM   6265  C  CG    . LYS B 1 87  ? 145.636 145.858 176.542 1.00 45.07 ? 87  LYS B CG    1 
ATOM   6266  C  CD    . LYS B 1 87  ? 144.938 144.686 175.876 1.00 42.58 ? 87  LYS B CD    1 
ATOM   6267  C  CE    . LYS B 1 87  ? 143.669 144.307 176.618 1.00 42.10 ? 87  LYS B CE    1 
ATOM   6268  N  NZ    . LYS B 1 87  ? 142.939 143.199 175.942 1.00 40.49 ? 87  LYS B NZ    1 
ATOM   6269  N  N     . LYS B 1 88  ? 149.702 144.194 176.787 1.00 49.00 ? 88  LYS B N     1 
ATOM   6270  C  CA    . LYS B 1 88  ? 150.178 142.818 176.930 1.00 46.10 ? 88  LYS B CA    1 
ATOM   6271  C  C     . LYS B 1 88  ? 149.091 141.827 176.521 1.00 45.35 ? 88  LYS B C     1 
ATOM   6272  O  O     . LYS B 1 88  ? 148.759 140.890 177.250 1.00 48.23 ? 88  LYS B O     1 
ATOM   6273  C  CB    . LYS B 1 88  ? 150.665 142.546 178.354 1.00 47.63 ? 88  LYS B CB    1 
ATOM   6274  C  CG    . LYS B 1 88  ? 151.533 143.650 178.936 1.00 46.09 ? 88  LYS B CG    1 
ATOM   6275  C  CD    . LYS B 1 88  ? 152.852 143.102 179.454 1.00 48.03 ? 88  LYS B CD    1 
ATOM   6276  C  CE    . LYS B 1 88  ? 152.654 142.302 180.730 1.00 50.07 ? 88  LYS B CE    1 
ATOM   6277  N  NZ    . LYS B 1 88  ? 153.822 141.427 181.024 1.00 50.12 ? 88  LYS B NZ    1 
ATOM   6278  N  N     . PHE B 1 89  ? 148.524 142.056 175.339 1.00 43.43 ? 89  PHE B N     1 
ATOM   6279  C  CA    . PHE B 1 89  ? 147.407 141.247 174.874 1.00 39.68 ? 89  PHE B CA    1 
ATOM   6280  C  C     . PHE B 1 89  ? 147.838 139.803 174.664 1.00 41.73 ? 89  PHE B C     1 
ATOM   6281  O  O     . PHE B 1 89  ? 148.884 139.531 174.067 1.00 42.64 ? 89  PHE B O     1 
ATOM   6282  C  CB    . PHE B 1 89  ? 146.841 141.818 173.574 1.00 39.67 ? 89  PHE B CB    1 
ATOM   6283  C  CG    . PHE B 1 89  ? 145.799 140.945 172.937 1.00 39.04 ? 89  PHE B CG    1 
ATOM   6284  C  CD1   . PHE B 1 89  ? 144.494 140.959 173.395 1.00 37.34 ? 89  PHE B CD1   1 
ATOM   6285  C  CD2   . PHE B 1 89  ? 146.125 140.101 171.890 1.00 39.26 ? 89  PHE B CD2   1 
ATOM   6286  C  CE1   . PHE B 1 89  ? 143.536 140.156 172.819 1.00 38.36 ? 89  PHE B CE1   1 
ATOM   6287  C  CE2   . PHE B 1 89  ? 145.170 139.295 171.310 1.00 35.76 ? 89  PHE B CE2   1 
ATOM   6288  C  CZ    . PHE B 1 89  ? 143.874 139.323 171.774 1.00 37.26 ? 89  PHE B CZ    1 
ATOM   6289  N  N     . ARG B 1 90  ? 147.021 138.876 175.152 1.00 44.10 ? 90  ARG B N     1 
ATOM   6290  C  CA    . ARG B 1 90  ? 147.259 137.450 174.996 1.00 43.69 ? 90  ARG B CA    1 
ATOM   6291  C  C     . ARG B 1 90  ? 146.070 136.825 174.285 1.00 44.03 ? 90  ARG B C     1 
ATOM   6292  O  O     . ARG B 1 90  ? 144.919 137.064 174.666 1.00 46.44 ? 90  ARG B O     1 
ATOM   6293  C  CB    . ARG B 1 90  ? 147.481 136.774 176.351 1.00 46.30 ? 90  ARG B CB    1 
ATOM   6294  C  CG    . ARG B 1 90  ? 148.663 137.320 177.127 1.00 45.66 ? 90  ARG B CG    1 
ATOM   6295  C  CD    . ARG B 1 90  ? 149.945 136.606 176.746 1.00 47.41 ? 90  ARG B CD    1 
ATOM   6296  N  NE    . ARG B 1 90  ? 150.772 137.417 175.860 1.00 49.93 ? 90  ARG B NE    1 
ATOM   6297  C  CZ    . ARG B 1 90  ? 151.534 138.425 176.260 1.00 48.74 ? 90  ARG B CZ    1 
ATOM   6298  N  NH1   . ARG B 1 90  ? 151.618 138.765 177.535 1.00 47.12 ? 90  ARG B NH1   1 
ATOM   6299  N  NH2   . ARG B 1 90  ? 152.230 139.109 175.357 1.00 49.47 ? 90  ARG B NH2   1 
ATOM   6300  N  N     . PHE B 1 91  ? 146.347 136.039 173.257 1.00 37.76 ? 91  PHE B N     1 
ATOM   6301  C  CA    . PHE B 1 91  ? 145.290 135.287 172.599 1.00 39.24 ? 91  PHE B CA    1 
ATOM   6302  C  C     . PHE B 1 91  ? 144.773 134.215 173.551 1.00 43.11 ? 91  PHE B C     1 
ATOM   6303  O  O     . PHE B 1 91  ? 145.563 133.409 174.055 1.00 44.30 ? 91  PHE B O     1 
ATOM   6304  C  CB    . PHE B 1 91  ? 145.807 134.655 171.312 1.00 39.50 ? 91  PHE B CB    1 
ATOM   6305  C  CG    . PHE B 1 91  ? 145.964 135.627 170.178 1.00 40.30 ? 91  PHE B CG    1 
ATOM   6306  C  CD1   . PHE B 1 91  ? 144.856 136.111 169.503 1.00 42.64 ? 91  PHE B CD1   1 
ATOM   6307  C  CD2   . PHE B 1 91  ? 147.219 136.058 169.787 1.00 41.39 ? 91  PHE B CD2   1 
ATOM   6308  C  CE1   . PHE B 1 91  ? 144.998 137.003 168.459 1.00 39.55 ? 91  PHE B CE1   1 
ATOM   6309  C  CE2   . PHE B 1 91  ? 147.365 136.950 168.744 1.00 39.90 ? 91  PHE B CE2   1 
ATOM   6310  C  CZ    . PHE B 1 91  ? 146.254 137.421 168.079 1.00 37.18 ? 91  PHE B CZ    1 
ATOM   6311  N  N     . PRO B 1 92  ? 143.468 134.172 173.828 1.00 43.10 ? 92  PRO B N     1 
ATOM   6312  C  CA    . PRO B 1 92  ? 142.971 133.198 174.811 1.00 40.90 ? 92  PRO B CA    1 
ATOM   6313  C  C     . PRO B 1 92  ? 142.981 131.771 174.302 1.00 40.26 ? 92  PRO B C     1 
ATOM   6314  O  O     . PRO B 1 92  ? 143.122 130.840 175.103 1.00 43.13 ? 92  PRO B O     1 
ATOM   6315  C  CB    . PRO B 1 92  ? 141.547 133.689 175.093 1.00 40.49 ? 92  PRO B CB    1 
ATOM   6316  C  CG    . PRO B 1 92  ? 141.139 134.355 173.827 1.00 40.38 ? 92  PRO B CG    1 
ATOM   6317  C  CD    . PRO B 1 92  ? 142.382 134.981 173.250 1.00 41.63 ? 92  PRO B CD    1 
ATOM   6318  N  N     . SER B 1 93  ? 142.841 131.569 172.996 1.00 38.94 ? 93  SER B N     1 
ATOM   6319  C  CA    . SER B 1 93  ? 142.747 130.244 172.412 1.00 40.56 ? 93  SER B CA    1 
ATOM   6320  C  C     . SER B 1 93  ? 143.779 130.104 171.304 1.00 42.41 ? 93  SER B C     1 
ATOM   6321  O  O     . SER B 1 93  ? 144.266 131.093 170.752 1.00 46.40 ? 93  SER B O     1 
ATOM   6322  C  CB    . SER B 1 93  ? 141.341 129.978 171.860 1.00 44.26 ? 93  SER B CB    1 
ATOM   6323  O  OG    . SER B 1 93  ? 141.292 130.197 170.463 1.00 48.45 ? 93  SER B OG    1 
ATOM   6324  N  N     . PHE B 1 94  ? 144.119 128.853 170.991 1.00 42.28 ? 94  PHE B N     1 
ATOM   6325  C  CA    . PHE B 1 94  ? 145.070 128.602 169.914 1.00 41.03 ? 94  PHE B CA    1 
ATOM   6326  C  C     . PHE B 1 94  ? 144.511 129.041 168.568 1.00 42.95 ? 94  PHE B C     1 
ATOM   6327  O  O     . PHE B 1 94  ? 145.256 129.533 167.713 1.00 46.30 ? 94  PHE B O     1 
ATOM   6328  C  CB    . PHE B 1 94  ? 145.453 127.125 169.871 1.00 41.51 ? 94  PHE B CB    1 
ATOM   6329  C  CG    . PHE B 1 94  ? 146.043 126.700 168.560 1.00 42.66 ? 94  PHE B CG    1 
ATOM   6330  C  CD1   . PHE B 1 94  ? 147.300 127.131 168.181 1.00 43.10 ? 94  PHE B CD1   1 
ATOM   6331  C  CD2   . PHE B 1 94  ? 145.334 125.887 167.695 1.00 43.68 ? 94  PHE B CD2   1 
ATOM   6332  C  CE1   . PHE B 1 94  ? 147.839 126.754 166.970 1.00 43.51 ? 94  PHE B CE1   1 
ATOM   6333  C  CE2   . PHE B 1 94  ? 145.872 125.507 166.484 1.00 41.93 ? 94  PHE B CE2   1 
ATOM   6334  C  CZ    . PHE B 1 94  ? 147.126 125.941 166.122 1.00 41.56 ? 94  PHE B CZ    1 
ATOM   6335  N  N     . MET B 1 95  ? 143.206 128.858 168.355 1.00 39.51 ? 95  MET B N     1 
ATOM   6336  C  CA    . MET B 1 95  ? 142.621 129.169 167.056 1.00 36.89 ? 95  MET B CA    1 
ATOM   6337  C  C     . MET B 1 95  ? 142.658 130.660 166.756 1.00 40.77 ? 95  MET B C     1 
ATOM   6338  O  O     . MET B 1 95  ? 142.821 131.044 165.596 1.00 42.60 ? 95  MET B O     1 
ATOM   6339  C  CB    . MET B 1 95  ? 141.186 128.646 166.983 1.00 41.23 ? 95  MET B CB    1 
ATOM   6340  C  CG    . MET B 1 95  ? 140.498 128.799 165.623 1.00 44.82 ? 95  MET B CG    1 
ATOM   6341  S  SD    . MET B 1 95  ? 141.266 128.130 164.121 1.00 53.38 ? 95  MET B SD    1 
ATOM   6342  C  CE    . MET B 1 95  ? 142.262 126.766 164.718 1.00 43.09 ? 95  MET B CE    1 
ATOM   6343  N  N     . SER B 1 96  ? 142.522 131.512 167.774 1.00 36.22 ? 96  SER B N     1 
ATOM   6344  C  CA    . SER B 1 96  ? 142.616 132.952 167.550 1.00 34.36 ? 96  SER B CA    1 
ATOM   6345  C  C     . SER B 1 96  ? 143.976 133.332 166.977 1.00 36.56 ? 96  SER B C     1 
ATOM   6346  O  O     . SER B 1 96  ? 144.068 133.987 165.929 1.00 32.98 ? 96  SER B O     1 
ATOM   6347  C  CB    . SER B 1 96  ? 142.367 133.696 168.861 1.00 35.97 ? 96  SER B CB    1 
ATOM   6348  O  OG    . SER B 1 96  ? 141.347 133.071 169.617 1.00 40.73 ? 96  SER B OG    1 
ATOM   6349  N  N     . ALA B 1 97  ? 145.048 132.912 167.653 1.00 36.61 ? 97  ALA B N     1 
ATOM   6350  C  CA    . ALA B 1 97  ? 146.395 133.224 167.195 1.00 34.24 ? 97  ALA B CA    1 
ATOM   6351  C  C     . ALA B 1 97  ? 146.690 132.567 165.856 1.00 36.03 ? 97  ALA B C     1 
ATOM   6352  O  O     . ALA B 1 97  ? 147.327 133.175 164.989 1.00 39.59 ? 97  ALA B O     1 
ATOM   6353  C  CB    . ALA B 1 97  ? 147.415 132.784 168.241 1.00 38.05 ? 97  ALA B CB    1 
ATOM   6354  N  N     . PHE B 1 98  ? 146.249 131.322 165.674 1.00 38.13 ? 98  PHE B N     1 
ATOM   6355  C  CA    . PHE B 1 98  ? 146.480 130.631 164.411 1.00 36.12 ? 98  PHE B CA    1 
ATOM   6356  C  C     . PHE B 1 98  ? 145.809 131.365 163.259 1.00 37.83 ? 98  PHE B C     1 
ATOM   6357  O  O     . PHE B 1 98  ? 146.425 131.594 162.213 1.00 46.76 ? 98  PHE B O     1 
ATOM   6358  C  CB    . PHE B 1 98  ? 145.975 129.192 164.502 1.00 40.19 ? 98  PHE B CB    1 
ATOM   6359  C  CG    . PHE B 1 98  ? 146.068 128.436 163.209 1.00 40.40 ? 98  PHE B CG    1 
ATOM   6360  C  CD1   . PHE B 1 98  ? 147.263 127.867 162.811 1.00 40.06 ? 98  PHE B CD1   1 
ATOM   6361  C  CD2   . PHE B 1 98  ? 144.960 128.297 162.390 1.00 41.48 ? 98  PHE B CD2   1 
ATOM   6362  C  CE1   . PHE B 1 98  ? 147.353 127.173 161.623 1.00 39.90 ? 98  PHE B CE1   1 
ATOM   6363  C  CE2   . PHE B 1 98  ? 145.045 127.606 161.200 1.00 44.21 ? 98  PHE B CE2   1 
ATOM   6364  C  CZ    . PHE B 1 98  ? 146.243 127.043 160.817 1.00 43.27 ? 98  PHE B CZ    1 
ATOM   6365  N  N     . LYS B 1 99  ? 144.547 131.759 163.441 1.00 41.08 ? 99  LYS B N     1 
ATOM   6366  C  CA    . LYS B 1 99  ? 143.831 132.466 162.389 1.00 39.30 ? 99  LYS B CA    1 
ATOM   6367  C  C     . LYS B 1 99  ? 144.479 133.808 162.091 1.00 37.69 ? 99  LYS B C     1 
ATOM   6368  O  O     . LYS B 1 99  ? 144.638 134.178 160.922 1.00 41.75 ? 99  LYS B O     1 
ATOM   6369  C  CB    . LYS B 1 99  ? 142.367 132.650 162.782 1.00 38.89 ? 99  LYS B CB    1 
ATOM   6370  C  CG    . LYS B 1 99  ? 141.506 131.421 162.556 1.00 42.09 ? 99  LYS B CG    1 
ATOM   6371  C  CD    . LYS B 1 99  ? 141.614 130.925 161.127 1.00 42.64 ? 99  LYS B CD    1 
ATOM   6372  C  CE    . LYS B 1 99  ? 140.354 130.194 160.701 1.00 42.04 ? 99  LYS B CE    1 
ATOM   6373  N  NZ    . LYS B 1 99  ? 139.907 130.612 159.345 1.00 46.15 ? 99  LYS B NZ    1 
ATOM   6374  N  N     . PHE B 1 100 ? 144.884 134.546 163.128 1.00 37.04 ? 100 PHE B N     1 
ATOM   6375  C  CA    . PHE B 1 100 ? 145.523 135.832 162.874 1.00 35.88 ? 100 PHE B CA    1 
ATOM   6376  C  C     . PHE B 1 100 ? 146.836 135.657 162.124 1.00 37.90 ? 100 PHE B C     1 
ATOM   6377  O  O     . PHE B 1 100 ? 147.063 136.296 161.091 1.00 40.64 ? 100 PHE B O     1 
ATOM   6378  C  CB    . PHE B 1 100 ? 145.764 136.598 164.171 1.00 35.19 ? 100 PHE B CB    1 
ATOM   6379  C  CG    . PHE B 1 100 ? 146.520 137.876 163.959 1.00 37.77 ? 100 PHE B CG    1 
ATOM   6380  C  CD1   . PHE B 1 100 ? 145.908 138.962 163.359 1.00 37.08 ? 100 PHE B CD1   1 
ATOM   6381  C  CD2   . PHE B 1 100 ? 147.853 137.976 164.311 1.00 34.97 ? 100 PHE B CD2   1 
ATOM   6382  C  CE1   . PHE B 1 100 ? 146.604 140.132 163.140 1.00 37.94 ? 100 PHE B CE1   1 
ATOM   6383  C  CE2   . PHE B 1 100 ? 148.552 139.142 164.092 1.00 35.73 ? 100 PHE B CE2   1 
ATOM   6384  C  CZ    . PHE B 1 100 ? 147.927 140.221 163.507 1.00 37.70 ? 100 PHE B CZ    1 
ATOM   6385  N  N     . TYR B 1 101 ? 147.710 134.784 162.616 1.00 39.84 ? 101 TYR B N     1 
ATOM   6386  C  CA    . TYR B 1 101 ? 149.029 134.633 162.022 1.00 37.49 ? 101 TYR B CA    1 
ATOM   6387  C  C     . TYR B 1 101 ? 149.010 133.827 160.732 1.00 37.01 ? 101 TYR B C     1 
ATOM   6388  O  O     . TYR B 1 101 ? 150.055 133.703 160.086 1.00 43.38 ? 101 TYR B O     1 
ATOM   6389  C  CB    . TYR B 1 101 ? 149.985 134.001 163.034 1.00 37.70 ? 101 TYR B CB    1 
ATOM   6390  C  CG    . TYR B 1 101 ? 150.412 134.976 164.105 1.00 35.75 ? 101 TYR B CG    1 
ATOM   6391  C  CD1   . TYR B 1 101 ? 151.296 136.007 163.821 1.00 36.37 ? 101 TYR B CD1   1 
ATOM   6392  C  CD2   . TYR B 1 101 ? 149.910 134.884 165.394 1.00 38.11 ? 101 TYR B CD2   1 
ATOM   6393  C  CE1   . TYR B 1 101 ? 151.678 136.907 164.793 1.00 37.96 ? 101 TYR B CE1   1 
ATOM   6394  C  CE2   . TYR B 1 101 ? 150.285 135.779 166.371 1.00 39.90 ? 101 TYR B CE2   1 
ATOM   6395  C  CZ    . TYR B 1 101 ? 151.170 136.788 166.066 1.00 39.87 ? 101 TYR B CZ    1 
ATOM   6396  O  OH    . TYR B 1 101 ? 151.544 137.681 167.041 1.00 39.62 ? 101 TYR B OH    1 
ATOM   6397  N  N     . ASN B 1 102 ? 147.861 133.274 160.343 1.00 39.70 ? 102 ASN B N     1 
ATOM   6398  C  CA    . ASN B 1 102 ? 147.739 132.623 159.049 1.00 42.26 ? 102 ASN B CA    1 
ATOM   6399  C  C     . ASN B 1 102 ? 146.968 133.445 158.025 1.00 43.56 ? 102 ASN B C     1 
ATOM   6400  O  O     . ASN B 1 102 ? 147.115 133.194 156.824 1.00 46.97 ? 102 ASN B O     1 
ATOM   6401  C  CB    . ASN B 1 102 ? 147.060 131.258 159.206 1.00 41.18 ? 102 ASN B CB    1 
ATOM   6402  C  CG    . ASN B 1 102 ? 148.047 130.146 159.494 1.00 44.61 ? 102 ASN B CG    1 
ATOM   6403  O  OD1   . ASN B 1 102 ? 148.904 130.271 160.368 1.00 47.05 ? 102 ASN B OD1   1 
ATOM   6404  N  ND2   . ASN B 1 102 ? 147.935 129.049 158.755 1.00 43.03 ? 102 ASN B ND2   1 
ATOM   6405  N  N     . ASP B 1 103 ? 146.157 134.411 158.454 1.00 43.95 ? 103 ASP B N     1 
ATOM   6406  C  CA    . ASP B 1 103 ? 145.336 135.170 157.519 1.00 44.05 ? 103 ASP B CA    1 
ATOM   6407  C  C     . ASP B 1 103 ? 145.668 136.652 157.467 1.00 43.39 ? 103 ASP B C     1 
ATOM   6408  O  O     . ASP B 1 103 ? 145.602 137.249 156.390 1.00 47.48 ? 103 ASP B O     1 
ATOM   6409  C  CB    . ASP B 1 103 ? 143.850 135.003 157.873 1.00 45.26 ? 103 ASP B CB    1 
ATOM   6410  C  CG    . ASP B 1 103 ? 143.363 133.577 157.699 1.00 48.87 ? 103 ASP B CG    1 
ATOM   6411  O  OD1   . ASP B 1 103 ? 144.150 132.728 157.233 1.00 48.67 ? 103 ASP B OD1   1 
ATOM   6412  O  OD2   . ASP B 1 103 ? 142.191 133.305 158.033 1.00 51.92 ? 103 ASP B OD2   1 
ATOM   6413  N  N     . TYR B 1 104 ? 146.023 137.268 158.592 1.00 37.80 ? 104 TYR B N     1 
ATOM   6414  C  CA    . TYR B 1 104 ? 146.152 138.716 158.672 1.00 41.53 ? 104 TYR B CA    1 
ATOM   6415  C  C     . TYR B 1 104 ? 147.555 139.204 158.993 1.00 40.24 ? 104 TYR B C     1 
ATOM   6416  O  O     . TYR B 1 104 ? 147.884 140.339 158.645 1.00 44.46 ? 104 TYR B O     1 
ATOM   6417  C  CB    . TYR B 1 104 ? 145.185 139.275 159.727 1.00 38.67 ? 104 TYR B CB    1 
ATOM   6418  C  CG    . TYR B 1 104 ? 143.751 138.861 159.503 1.00 40.70 ? 104 TYR B CG    1 
ATOM   6419  C  CD1   . TYR B 1 104 ? 142.928 139.580 158.648 1.00 40.19 ? 104 TYR B CD1   1 
ATOM   6420  C  CD2   . TYR B 1 104 ? 143.223 137.746 160.139 1.00 36.96 ? 104 TYR B CD2   1 
ATOM   6421  C  CE1   . TYR B 1 104 ? 141.620 139.204 158.436 1.00 40.49 ? 104 TYR B CE1   1 
ATOM   6422  C  CE2   . TYR B 1 104 ? 141.915 137.362 159.932 1.00 38.03 ? 104 TYR B CE2   1 
ATOM   6423  C  CZ    . TYR B 1 104 ? 141.118 138.095 159.080 1.00 41.67 ? 104 TYR B CZ    1 
ATOM   6424  O  OH    . TYR B 1 104 ? 139.813 137.718 158.869 1.00 41.37 ? 104 TYR B OH    1 
ATOM   6425  N  N     . ALA B 1 105 ? 148.382 138.396 159.649 1.00 42.80 ? 105 ALA B N     1 
ATOM   6426  C  CA    . ALA B 1 105 ? 149.730 138.830 159.984 1.00 42.72 ? 105 ALA B CA    1 
ATOM   6427  C  C     . ALA B 1 105 ? 150.569 138.995 158.724 1.00 44.93 ? 105 ALA B C     1 
ATOM   6428  O  O     . ALA B 1 105 ? 150.517 138.170 157.809 1.00 43.81 ? 105 ALA B O     1 
ATOM   6429  C  CB    . ALA B 1 105 ? 150.395 137.833 160.929 1.00 39.71 ? 105 ALA B CB    1 
ATOM   6430  N  N     . LEU B 1 106 ? 151.345 140.075 158.681 1.00 46.41 ? 106 LEU B N     1 
ATOM   6431  C  CA    . LEU B 1 106 ? 152.196 140.336 157.529 1.00 45.19 ? 106 LEU B CA    1 
ATOM   6432  C  C     . LEU B 1 106 ? 153.355 139.349 157.499 1.00 47.74 ? 106 LEU B C     1 
ATOM   6433  O  O     . LEU B 1 106 ? 154.056 139.164 158.499 1.00 47.85 ? 106 LEU B O     1 
ATOM   6434  C  CB    . LEU B 1 106 ? 152.720 141.770 157.569 1.00 48.04 ? 106 LEU B CB    1 
ATOM   6435  C  CG    . LEU B 1 106 ? 153.517 142.244 156.352 1.00 45.80 ? 106 LEU B CG    1 
ATOM   6436  C  CD1   . LEU B 1 106 ? 152.624 142.329 155.128 1.00 45.22 ? 106 LEU B CD1   1 
ATOM   6437  C  CD2   . LEU B 1 106 ? 154.173 143.584 156.632 1.00 46.06 ? 106 LEU B CD2   1 
ATOM   6438  N  N     . LYS B 1 107 ? 153.555 138.720 156.348 1.00 55.14 ? 107 LYS B N     1 
ATOM   6439  C  CA    . LYS B 1 107 ? 154.620 137.754 156.147 1.00 55.66 ? 107 LYS B CA    1 
ATOM   6440  C  C     . LYS B 1 107 ? 155.580 138.259 155.080 1.00 56.84 ? 107 LYS B C     1 
ATOM   6441  O  O     . LYS B 1 107 ? 155.279 139.196 154.335 1.00 55.61 ? 107 LYS B O     1 
ATOM   6442  C  CB    . LYS B 1 107 ? 154.064 136.384 155.740 1.00 55.06 ? 107 LYS B CB    1 
ATOM   6443  C  CG    . LYS B 1 107 ? 153.597 135.534 156.903 1.00 53.34 ? 107 LYS B CG    1 
ATOM   6444  C  CD    . LYS B 1 107 ? 152.748 134.374 156.425 1.00 55.59 ? 107 LYS B CD    1 
ATOM   6445  C  CE    . LYS B 1 107 ? 151.964 133.769 157.570 1.00 56.58 ? 107 LYS B CE    1 
ATOM   6446  N  NZ    . LYS B 1 107 ? 151.573 134.800 158.571 1.00 55.48 ? 107 LYS B NZ    1 
ATOM   6447  N  N     . THR B 1 108 ? 156.749 137.628 155.021 1.00 60.65 ? 108 THR B N     1 
ATOM   6448  C  CA    . THR B 1 108 ? 157.731 137.963 154.004 1.00 60.69 ? 108 THR B CA    1 
ATOM   6449  C  C     . THR B 1 108 ? 157.180 137.643 152.614 1.00 61.72 ? 108 THR B C     1 
ATOM   6450  O  O     . THR B 1 108 ? 156.171 136.953 152.457 1.00 61.70 ? 108 THR B O     1 
ATOM   6451  C  CB    . THR B 1 108 ? 159.034 137.203 154.246 1.00 60.08 ? 108 THR B CB    1 
ATOM   6452  O  OG1   . THR B 1 108 ? 158.746 135.814 154.450 1.00 61.28 ? 108 THR B OG1   1 
ATOM   6453  C  CG2   . THR B 1 108 ? 159.754 137.746 155.467 1.00 57.84 ? 108 THR B CG2   1 
ATOM   6454  N  N     . ASN B 1 109 ? 157.865 138.163 151.592 1.00 63.49 ? 109 ASN B N     1 
ATOM   6455  C  CA    . ASN B 1 109 ? 157.413 137.955 150.219 1.00 63.78 ? 109 ASN B CA    1 
ATOM   6456  C  C     . ASN B 1 109 ? 157.391 136.478 149.846 1.00 65.62 ? 109 ASN B C     1 
ATOM   6457  O  O     . ASN B 1 109 ? 156.610 136.071 148.979 1.00 65.04 ? 109 ASN B O     1 
ATOM   6458  C  CB    . ASN B 1 109 ? 158.297 138.736 149.248 1.00 62.18 ? 109 ASN B CB    1 
ATOM   6459  C  CG    . ASN B 1 109 ? 158.342 140.216 149.564 1.00 64.02 ? 109 ASN B CG    1 
ATOM   6460  O  OD1   . ASN B 1 109 ? 157.333 140.914 149.464 1.00 65.96 ? 109 ASN B OD1   1 
ATOM   6461  N  ND2   . ASN B 1 109 ? 159.515 140.705 149.947 1.00 63.49 ? 109 ASN B ND2   1 
ATOM   6462  N  N     . ASP B 1 110 ? 158.232 135.663 150.480 1.00 65.94 ? 110 ASP B N     1 
ATOM   6463  C  CA    . ASP B 1 110 ? 158.210 134.222 150.279 1.00 67.50 ? 110 ASP B CA    1 
ATOM   6464  C  C     . ASP B 1 110 ? 157.315 133.506 151.285 1.00 66.75 ? 110 ASP B C     1 
ATOM   6465  O  O     . ASP B 1 110 ? 157.277 132.271 151.290 1.00 67.21 ? 110 ASP B O     1 
ATOM   6466  C  CB    . ASP B 1 110 ? 159.631 133.651 150.338 1.00 67.93 ? 110 ASP B CB    1 
ATOM   6467  C  CG    . ASP B 1 110 ? 160.287 133.849 151.688 1.00 69.37 ? 110 ASP B CG    1 
ATOM   6468  O  OD1   . ASP B 1 110 ? 159.906 134.798 152.401 1.00 69.15 ? 110 ASP B OD1   1 
ATOM   6469  O  OD2   . ASP B 1 110 ? 161.186 133.056 152.035 1.00 69.08 ? 110 ASP B OD2   1 
ATOM   6470  N  N     . LYS B 1 111 ? 156.599 134.256 152.127 1.00 64.94 ? 111 LYS B N     1 
ATOM   6471  C  CA    . LYS B 1 111 ? 155.670 133.695 153.112 1.00 64.07 ? 111 LYS B CA    1 
ATOM   6472  C  C     . LYS B 1 111 ? 156.364 132.693 154.031 1.00 65.88 ? 111 LYS B C     1 
ATOM   6473  O  O     . LYS B 1 111 ? 155.819 131.635 154.351 1.00 66.40 ? 111 LYS B O     1 
ATOM   6474  C  CB    . LYS B 1 111 ? 154.457 133.057 152.430 1.00 64.79 ? 111 LYS B CB    1 
ATOM   6475  C  CG    . LYS B 1 111 ? 153.839 133.898 151.322 1.00 64.70 ? 111 LYS B CG    1 
ATOM   6476  C  CD    . LYS B 1 111 ? 153.488 135.298 151.807 1.00 65.86 ? 111 LYS B CD    1 
ATOM   6477  C  CE    . LYS B 1 111 ? 152.280 135.282 152.729 1.00 66.86 ? 111 LYS B CE    1 
ATOM   6478  N  NZ    . LYS B 1 111 ? 151.067 134.751 152.051 1.00 67.12 ? 111 LYS B NZ    1 
ATOM   6479  N  N     . LYS B 1 112 ? 157.577 133.031 154.461 1.00 64.86 ? 112 LYS B N     1 
ATOM   6480  C  CA    . LYS B 1 112 ? 158.373 132.170 155.327 1.00 64.46 ? 112 LYS B CA    1 
ATOM   6481  C  C     . LYS B 1 112 ? 158.446 132.662 156.763 1.00 63.96 ? 112 LYS B C     1 
ATOM   6482  O  O     . LYS B 1 112 ? 158.314 131.861 157.691 1.00 64.39 ? 112 LYS B O     1 
ATOM   6483  C  CB    . LYS B 1 112 ? 159.794 132.032 154.764 1.00 64.09 ? 112 LYS B CB    1 
ATOM   6484  C  CG    . LYS B 1 112 ? 160.861 131.687 155.792 1.00 65.85 ? 112 LYS B CG    1 
ATOM   6485  C  CD    . LYS B 1 112 ? 160.813 130.216 156.176 1.00 64.33 ? 112 LYS B CD    1 
ATOM   6486  C  CE    . LYS B 1 112 ? 161.363 129.995 157.576 1.00 64.72 ? 112 LYS B CE    1 
ATOM   6487  N  NZ    . LYS B 1 112 ? 160.502 130.622 158.615 1.00 64.57 ? 112 LYS B NZ    1 
ATOM   6488  N  N     . LYS B 1 113 ? 158.640 133.957 156.972 1.00 60.44 ? 113 LYS B N     1 
ATOM   6489  C  CA    . LYS B 1 113 ? 158.768 134.544 158.298 1.00 59.20 ? 113 LYS B CA    1 
ATOM   6490  C  C     . LYS B 1 113 ? 157.597 135.488 158.559 1.00 59.30 ? 113 LYS B C     1 
ATOM   6491  O  O     . LYS B 1 113 ? 156.763 135.738 157.686 1.00 57.83 ? 113 LYS B O     1 
ATOM   6492  C  CB    . LYS B 1 113 ? 160.108 135.270 158.437 1.00 57.43 ? 113 LYS B CB    1 
ATOM   6493  C  CG    . LYS B 1 113 ? 161.295 134.352 158.677 1.00 58.13 ? 113 LYS B CG    1 
ATOM   6494  C  CD    . LYS B 1 113 ? 161.308 133.824 160.100 1.00 59.40 ? 113 LYS B CD    1 
ATOM   6495  C  CE    . LYS B 1 113 ? 162.699 133.374 160.512 1.00 57.57 ? 113 LYS B CE    1 
ATOM   6496  N  NZ    . LYS B 1 113 ? 162.773 131.897 160.682 1.00 58.33 ? 113 LYS B NZ    1 
ATOM   6497  N  N     . ILE B 1 114 ? 157.542 136.016 159.779 1.00 52.73 ? 114 ILE B N     1 
ATOM   6498  C  CA    . ILE B 1 114 ? 156.452 136.876 160.228 1.00 50.49 ? 114 ILE B CA    1 
ATOM   6499  C  C     . ILE B 1 114 ? 157.029 138.245 160.560 1.00 51.83 ? 114 ILE B C     1 
ATOM   6500  O  O     . ILE B 1 114 ? 157.945 138.355 161.385 1.00 54.25 ? 114 ILE B O     1 
ATOM   6501  C  CB    . ILE B 1 114 ? 155.724 136.281 161.444 1.00 51.56 ? 114 ILE B CB    1 
ATOM   6502  C  CG1   . ILE B 1 114 ? 154.864 135.088 161.026 1.00 50.63 ? 114 ILE B CG1   1 
ATOM   6503  C  CG2   . ILE B 1 114 ? 154.873 137.334 162.130 1.00 51.44 ? 114 ILE B CG2   1 
ATOM   6504  C  CD1   . ILE B 1 114 ? 154.422 134.225 162.185 1.00 48.50 ? 114 ILE B CD1   1 
ATOM   6505  N  N     . LEU B 1 115 ? 156.493 139.286 159.922 1.00 48.55 ? 115 LEU B N     1 
ATOM   6506  C  CA    . LEU B 1 115 ? 156.909 140.653 160.216 1.00 47.85 ? 115 LEU B CA    1 
ATOM   6507  C  C     . LEU B 1 115 ? 156.042 141.312 161.279 1.00 49.37 ? 115 LEU B C     1 
ATOM   6508  O  O     . LEU B 1 115 ? 156.552 142.072 162.108 1.00 50.40 ? 115 LEU B O     1 
ATOM   6509  C  CB    . LEU B 1 115 ? 156.880 141.512 158.948 1.00 49.27 ? 115 LEU B CB    1 
ATOM   6510  C  CG    . LEU B 1 115 ? 157.988 141.355 157.908 1.00 48.06 ? 115 LEU B CG    1 
ATOM   6511  C  CD1   . LEU B 1 115 ? 159.343 141.172 158.574 1.00 49.52 ? 115 LEU B CD1   1 
ATOM   6512  C  CD2   . LEU B 1 115 ? 157.682 140.213 156.968 1.00 49.61 ? 115 LEU B CD2   1 
ATOM   6513  N  N     . GLU B 1 116 ? 154.742 141.037 161.273 1.00 46.35 ? 116 GLU B N     1 
ATOM   6514  C  CA    . GLU B 1 116 ? 153.783 141.748 162.106 1.00 45.61 ? 116 GLU B CA    1 
ATOM   6515  C  C     . GLU B 1 116 ? 153.245 140.838 163.199 1.00 44.43 ? 116 GLU B C     1 
ATOM   6516  O  O     . GLU B 1 116 ? 152.795 139.722 162.922 1.00 47.28 ? 116 GLU B O     1 
ATOM   6517  C  CB    . GLU B 1 116 ? 152.621 142.280 161.265 1.00 43.90 ? 116 GLU B CB    1 
ATOM   6518  C  CG    . GLU B 1 116 ? 152.741 143.741 160.892 1.00 43.88 ? 116 GLU B CG    1 
ATOM   6519  C  CD    . GLU B 1 116 ? 151.599 144.206 160.013 1.00 46.92 ? 116 GLU B CD    1 
ATOM   6520  O  OE1   . GLU B 1 116 ? 150.771 143.360 159.617 1.00 47.20 ? 116 GLU B OE1   1 
ATOM   6521  O  OE2   . GLU B 1 116 ? 151.527 145.417 159.720 1.00 50.29 ? 116 GLU B OE2   1 
ATOM   6522  N  N     . ARG B 1 117 ? 153.291 141.322 164.436 1.00 40.32 ? 117 ARG B N     1 
ATOM   6523  C  CA    . ARG B 1 117 ? 152.544 140.714 165.521 1.00 41.72 ? 117 ARG B CA    1 
ATOM   6524  C  C     . ARG B 1 117 ? 151.133 141.296 165.529 1.00 41.31 ? 117 ARG B C     1 
ATOM   6525  O  O     . ARG B 1 117 ? 150.772 142.124 164.690 1.00 40.50 ? 117 ARG B O     1 
ATOM   6526  C  CB    . ARG B 1 117 ? 153.251 140.944 166.855 1.00 41.89 ? 117 ARG B CB    1 
ATOM   6527  C  CG    . ARG B 1 117 ? 154.644 140.346 166.932 1.00 41.84 ? 117 ARG B CG    1 
ATOM   6528  C  CD    . ARG B 1 117 ? 154.639 138.876 166.543 1.00 45.93 ? 117 ARG B CD    1 
ATOM   6529  N  NE    . ARG B 1 117 ? 154.424 137.999 167.688 1.00 43.78 ? 117 ARG B NE    1 
ATOM   6530  C  CZ    . ARG B 1 117 ? 155.308 137.787 168.654 1.00 45.03 ? 117 ARG B CZ    1 
ATOM   6531  N  NH1   . ARG B 1 117 ? 156.499 138.362 168.641 1.00 43.59 ? 117 ARG B NH1   1 
ATOM   6532  N  NH2   . ARG B 1 117 ? 154.990 136.974 169.657 1.00 46.79 ? 117 ARG B NH2   1 
ATOM   6533  N  N     . TYR B 1 118 ? 150.314 140.854 166.484 1.00 39.65 ? 118 TYR B N     1 
ATOM   6534  C  CA    . TYR B 1 118 ? 148.983 141.434 166.621 1.00 35.31 ? 118 TYR B CA    1 
ATOM   6535  C  C     . TYR B 1 118 ? 149.072 142.913 166.969 1.00 37.58 ? 118 TYR B C     1 
ATOM   6536  O  O     . TYR B 1 118 ? 148.337 143.739 166.413 1.00 39.89 ? 118 TYR B O     1 
ATOM   6537  C  CB    . TYR B 1 118 ? 148.184 140.674 167.677 1.00 35.66 ? 118 TYR B CB    1 
ATOM   6538  C  CG    . TYR B 1 118 ? 146.706 140.978 167.657 1.00 36.80 ? 118 TYR B CG    1 
ATOM   6539  C  CD1   . TYR B 1 118 ? 145.963 140.826 166.495 1.00 34.44 ? 118 TYR B CD1   1 
ATOM   6540  C  CD2   . TYR B 1 118 ? 146.054 141.420 168.797 1.00 36.00 ? 118 TYR B CD2   1 
ATOM   6541  C  CE1   . TYR B 1 118 ? 144.614 141.103 166.471 1.00 34.22 ? 118 TYR B CE1   1 
ATOM   6542  C  CE2   . TYR B 1 118 ? 144.703 141.696 168.784 1.00 33.45 ? 118 TYR B CE2   1 
ATOM   6543  C  CZ    . TYR B 1 118 ? 143.988 141.537 167.617 1.00 34.53 ? 118 TYR B CZ    1 
ATOM   6544  O  OH    . TYR B 1 118 ? 142.642 141.815 167.597 1.00 41.80 ? 118 TYR B OH    1 
ATOM   6545  N  N     . GLU B 1 119 ? 149.983 143.265 167.877 1.00 42.63 ? 119 GLU B N     1 
ATOM   6546  C  CA    . GLU B 1 119 ? 150.155 144.661 168.258 1.00 38.88 ? 119 GLU B CA    1 
ATOM   6547  C  C     . GLU B 1 119 ? 150.656 145.500 167.089 1.00 37.91 ? 119 GLU B C     1 
ATOM   6548  O  O     . GLU B 1 119 ? 150.228 146.644 166.920 1.00 45.68 ? 119 GLU B O     1 
ATOM   6549  C  CB    . GLU B 1 119 ? 151.107 144.764 169.447 1.00 38.95 ? 119 GLU B CB    1 
ATOM   6550  C  CG    . GLU B 1 119 ? 150.557 144.166 170.729 1.00 40.04 ? 119 GLU B CG    1 
ATOM   6551  C  CD    . GLU B 1 119 ? 150.983 142.725 170.931 1.00 44.74 ? 119 GLU B CD    1 
ATOM   6552  O  OE1   . GLU B 1 119 ? 151.223 142.025 169.925 1.00 43.86 ? 119 GLU B OE1   1 
ATOM   6553  O  OE2   . GLU B 1 119 ? 151.077 142.290 172.098 1.00 44.72 ? 119 GLU B OE2   1 
ATOM   6554  N  N     . ASP B 1 120 ? 151.564 144.957 166.275 1.00 40.75 ? 120 ASP B N     1 
ATOM   6555  C  CA    . ASP B 1 120 ? 152.063 145.706 165.124 1.00 40.26 ? 120 ASP B CA    1 
ATOM   6556  C  C     . ASP B 1 120 ? 150.953 145.967 164.112 1.00 39.26 ? 120 ASP B C     1 
ATOM   6557  O  O     . ASP B 1 120 ? 150.814 147.084 163.600 1.00 43.56 ? 120 ASP B O     1 
ATOM   6558  C  CB    . ASP B 1 120 ? 153.219 144.955 164.465 1.00 44.13 ? 120 ASP B CB    1 
ATOM   6559  C  CG    . ASP B 1 120 ? 154.245 144.470 165.464 1.00 46.48 ? 120 ASP B CG    1 
ATOM   6560  O  OD1   . ASP B 1 120 ? 154.549 145.216 166.417 1.00 45.85 ? 120 ASP B OD1   1 
ATOM   6561  O  OD2   . ASP B 1 120 ? 154.753 143.343 165.293 1.00 49.45 ? 120 ASP B OD2   1 
ATOM   6562  N  N     . ARG B 1 121 ? 150.156 144.940 163.811 1.00 35.25 ? 121 ARG B N     1 
ATOM   6563  C  CA    . ARG B 1 121 ? 149.042 145.107 162.885 1.00 33.69 ? 121 ARG B CA    1 
ATOM   6564  C  C     . ARG B 1 121 ? 148.038 146.123 163.413 1.00 36.50 ? 121 ARG B C     1 
ATOM   6565  O  O     . ARG B 1 121 ? 147.559 146.983 162.664 1.00 43.14 ? 121 ARG B O     1 
ATOM   6566  C  CB    . ARG B 1 121 ? 148.369 143.757 162.638 1.00 36.39 ? 121 ARG B CB    1 
ATOM   6567  C  CG    . ARG B 1 121 ? 147.120 143.811 161.779 1.00 34.76 ? 121 ARG B CG    1 
ATOM   6568  C  CD    . ARG B 1 121 ? 147.454 143.698 160.306 1.00 33.68 ? 121 ARG B CD    1 
ATOM   6569  N  NE    . ARG B 1 121 ? 147.286 144.973 159.622 1.00 42.56 ? 121 ARG B NE    1 
ATOM   6570  C  CZ    . ARG B 1 121 ? 148.082 145.418 158.661 1.00 39.48 ? 121 ARG B CZ    1 
ATOM   6571  N  NH1   . ARG B 1 121 ? 149.116 144.712 158.238 1.00 41.42 ? 121 ARG B NH1   1 
ATOM   6572  N  NH2   . ARG B 1 121 ? 147.835 146.602 158.111 1.00 33.60 ? 121 ARG B NH2   1 
ATOM   6573  N  N     . ILE B 1 122 ? 147.723 146.050 164.707 1.00 35.30 ? 122 ILE B N     1 
ATOM   6574  C  CA    . ILE B 1 122 ? 146.764 146.983 165.288 1.00 30.76 ? 122 ILE B CA    1 
ATOM   6575  C  C     . ILE B 1 122 ? 147.317 148.403 165.274 1.00 30.77 ? 122 ILE B C     1 
ATOM   6576  O  O     . ILE B 1 122 ? 146.590 149.359 164.984 1.00 36.93 ? 122 ILE B O     1 
ATOM   6577  C  CB    . ILE B 1 122 ? 146.374 146.522 166.704 1.00 34.81 ? 122 ILE B CB    1 
ATOM   6578  C  CG1   . ILE B 1 122 ? 145.310 145.429 166.609 1.00 32.14 ? 122 ILE B CG1   1 
ATOM   6579  C  CG2   . ILE B 1 122 ? 145.873 147.689 167.543 1.00 32.00 ? 122 ILE B CG2   1 
ATOM   6580  C  CD1   . ILE B 1 122 ? 144.680 145.074 167.917 1.00 32.21 ? 122 ILE B CD1   1 
ATOM   6581  N  N     . SER B 1 123 ? 148.608 148.568 165.571 1.00 34.15 ? 123 SER B N     1 
ATOM   6582  C  CA    . SER B 1 123 ? 149.215 149.894 165.537 1.00 33.22 ? 123 SER B CA    1 
ATOM   6583  C  C     . SER B 1 123 ? 149.193 150.477 164.133 1.00 35.55 ? 123 SER B C     1 
ATOM   6584  O  O     . SER B 1 123 ? 148.903 151.663 163.952 1.00 36.07 ? 123 SER B O     1 
ATOM   6585  C  CB    . SER B 1 123 ? 150.649 149.832 166.055 1.00 33.03 ? 123 SER B CB    1 
ATOM   6586  O  OG    . SER B 1 123 ? 150.701 149.274 167.349 1.00 37.27 ? 123 SER B OG    1 
ATOM   6587  N  N     . ILE B 1 124 ? 149.504 149.660 163.126 1.00 36.67 ? 124 ILE B N     1 
ATOM   6588  C  CA    . ILE B 1 124 ? 149.496 150.155 161.754 1.00 35.62 ? 124 ILE B CA    1 
ATOM   6589  C  C     . ILE B 1 124 ? 148.082 150.535 161.330 1.00 38.80 ? 124 ILE B C     1 
ATOM   6590  O  O     . ILE B 1 124 ? 147.868 151.581 160.702 1.00 39.11 ? 124 ILE B O     1 
ATOM   6591  C  CB    . ILE B 1 124 ? 150.121 149.113 160.810 1.00 39.46 ? 124 ILE B CB    1 
ATOM   6592  C  CG1   . ILE B 1 124 ? 151.641 149.124 160.966 1.00 40.38 ? 124 ILE B CG1   1 
ATOM   6593  C  CG2   . ILE B 1 124 ? 149.730 149.387 159.367 1.00 37.07 ? 124 ILE B CG2   1 
ATOM   6594  C  CD1   . ILE B 1 124 ? 152.256 150.503 160.841 1.00 36.94 ? 124 ILE B CD1   1 
ATOM   6595  N  N     . VAL B 1 125 ? 147.094 149.708 161.682 1.00 33.89 ? 125 VAL B N     1 
ATOM   6596  C  CA    . VAL B 1 125 ? 145.710 150.017 161.334 1.00 31.45 ? 125 VAL B CA    1 
ATOM   6597  C  C     . VAL B 1 125 ? 145.260 151.302 162.021 1.00 27.89 ? 125 VAL B C     1 
ATOM   6598  O  O     . VAL B 1 125 ? 144.588 152.144 161.415 1.00 35.52 ? 125 VAL B O     1 
ATOM   6599  C  CB    . VAL B 1 125 ? 144.795 148.828 161.681 1.00 36.50 ? 125 VAL B CB    1 
ATOM   6600  C  CG1   . VAL B 1 125 ? 143.338 149.230 161.596 1.00 33.21 ? 125 VAL B CG1   1 
ATOM   6601  C  CG2   . VAL B 1 125 ? 145.072 147.662 160.747 1.00 29.17 ? 125 VAL B CG2   1 
ATOM   6602  N  N     . ALA B 1 126 ? 145.631 151.479 163.291 1.00 25.71 ? 126 ALA B N     1 
ATOM   6603  C  CA    . ALA B 1 126 ? 145.255 152.687 164.019 1.00 27.34 ? 126 ALA B CA    1 
ATOM   6604  C  C     . ALA B 1 126 ? 145.927 153.926 163.443 1.00 31.15 ? 126 ALA B C     1 
ATOM   6605  O  O     . ALA B 1 126 ? 145.301 154.988 163.342 1.00 35.00 ? 126 ALA B O     1 
ATOM   6606  C  CB    . ALA B 1 126 ? 145.606 152.532 165.495 1.00 30.76 ? 126 ALA B CB    1 
ATOM   6607  N  N     . LEU B 1 127 ? 147.206 153.817 163.078 1.00 35.27 ? 127 LEU B N     1 
ATOM   6608  C  CA    . LEU B 1 127 ? 147.910 154.951 162.491 1.00 28.49 ? 127 LEU B CA    1 
ATOM   6609  C  C     . LEU B 1 127 ? 147.321 155.317 161.137 1.00 28.50 ? 127 LEU B C     1 
ATOM   6610  O  O     . LEU B 1 127 ? 147.274 156.497 160.773 1.00 33.93 ? 127 LEU B O     1 
ATOM   6611  C  CB    . LEU B 1 127 ? 149.400 154.637 162.366 1.00 30.95 ? 127 LEU B CB    1 
ATOM   6612  C  CG    . LEU B 1 127 ? 150.219 154.627 163.658 1.00 33.23 ? 127 LEU B CG    1 
ATOM   6613  C  CD1   . LEU B 1 127 ? 151.521 153.873 163.458 1.00 37.82 ? 127 LEU B CD1   1 
ATOM   6614  C  CD2   . LEU B 1 127 ? 150.489 156.039 164.140 1.00 33.37 ? 127 LEU B CD2   1 
ATOM   6615  N  N     . PHE B 1 128 ? 146.875 154.318 160.374 1.00 32.62 ? 128 PHE B N     1 
ATOM   6616  C  CA    . PHE B 1 128 ? 146.194 154.608 159.118 1.00 33.05 ? 128 PHE B CA    1 
ATOM   6617  C  C     . PHE B 1 128 ? 144.836 155.258 159.368 1.00 30.77 ? 128 PHE B C     1 
ATOM   6618  O  O     . PHE B 1 128 ? 144.432 156.166 158.633 1.00 38.25 ? 128 PHE B O     1 
ATOM   6619  C  CB    . PHE B 1 128 ? 146.059 153.324 158.294 1.00 30.40 ? 128 PHE B CB    1 
ATOM   6620  C  CG    . PHE B 1 128 ? 145.078 153.421 157.158 1.00 36.00 ? 128 PHE B CG    1 
ATOM   6621  C  CD1   . PHE B 1 128 ? 145.514 153.744 155.886 1.00 36.53 ? 128 PHE B CD1   1 
ATOM   6622  C  CD2   . PHE B 1 128 ? 143.735 153.138 157.346 1.00 34.22 ? 128 PHE B CD2   1 
ATOM   6623  C  CE1   . PHE B 1 128 ? 144.626 153.827 154.835 1.00 36.04 ? 128 PHE B CE1   1 
ATOM   6624  C  CE2   . PHE B 1 128 ? 142.843 153.221 156.298 1.00 34.13 ? 128 PHE B CE2   1 
ATOM   6625  C  CZ    . PHE B 1 128 ? 143.290 153.564 155.041 1.00 34.72 ? 128 PHE B CZ    1 
ATOM   6626  N  N     . PHE B 1 129 ? 144.118 154.802 160.398 1.00 28.05 ? 129 PHE B N     1 
ATOM   6627  C  CA    . PHE B 1 129 ? 142.811 155.371 160.712 1.00 23.12 ? 129 PHE B CA    1 
ATOM   6628  C  C     . PHE B 1 129 ? 142.919 156.830 161.138 1.00 30.39 ? 129 PHE B C     1 
ATOM   6629  O  O     . PHE B 1 129 ? 142.114 157.666 160.714 1.00 33.48 ? 129 PHE B O     1 
ATOM   6630  C  CB    . PHE B 1 129 ? 142.136 154.563 161.819 1.00 26.32 ? 129 PHE B CB    1 
ATOM   6631  C  CG    . PHE B 1 129 ? 141.475 153.307 161.343 1.00 28.18 ? 129 PHE B CG    1 
ATOM   6632  C  CD1   . PHE B 1 129 ? 141.242 153.092 159.998 1.00 28.02 ? 129 PHE B CD1   1 
ATOM   6633  C  CD2   . PHE B 1 129 ? 141.078 152.340 162.250 1.00 29.20 ? 129 PHE B CD2   1 
ATOM   6634  C  CE1   . PHE B 1 129 ? 140.632 151.934 159.567 1.00 26.30 ? 129 PHE B CE1   1 
ATOM   6635  C  CE2   . PHE B 1 129 ? 140.464 151.182 161.824 1.00 30.50 ? 129 PHE B CE2   1 
ATOM   6636  C  CZ    . PHE B 1 129 ? 140.242 150.978 160.482 1.00 29.53 ? 129 PHE B CZ    1 
ATOM   6637  N  N     . ALA B 1 130 ? 143.901 157.151 161.982 1.00 35.41 ? 130 ALA B N     1 
ATOM   6638  C  CA    . ALA B 1 130 ? 143.965 158.486 162.568 1.00 35.50 ? 130 ALA B CA    1 
ATOM   6639  C  C     . ALA B 1 130 ? 144.337 159.547 161.541 1.00 41.36 ? 130 ALA B C     1 
ATOM   6640  O  O     . ALA B 1 130 ? 143.910 160.701 161.669 1.00 45.26 ? 130 ALA B O     1 
ATOM   6641  C  CB    . ALA B 1 130 ? 144.955 158.501 163.726 1.00 34.08 ? 130 ALA B CB    1 
ATOM   6642  N  N     . ASN B 1 131 ? 145.131 159.184 160.533 1.00 41.50 ? 131 ASN B N     1 
ATOM   6643  C  CA    . ASN B 1 131 ? 145.499 160.089 159.443 1.00 41.27 ? 131 ASN B CA    1 
ATOM   6644  C  C     . ASN B 1 131 ? 146.219 161.334 159.963 1.00 42.49 ? 131 ASN B C     1 
ATOM   6645  O  O     . ASN B 1 131 ? 145.919 162.464 159.573 1.00 45.58 ? 131 ASN B O     1 
ATOM   6646  C  CB    . ASN B 1 131 ? 144.268 160.472 158.616 1.00 40.00 ? 131 ASN B CB    1 
ATOM   6647  C  CG    . ASN B 1 131 ? 144.619 160.881 157.201 1.00 44.68 ? 131 ASN B CG    1 
ATOM   6648  O  OD1   . ASN B 1 131 ? 145.469 160.268 156.557 1.00 44.24 ? 131 ASN B OD1   1 
ATOM   6649  N  ND2   . ASN B 1 131 ? 143.960 161.922 156.707 1.00 43.13 ? 131 ASN B ND2   1 
ATOM   6650  N  N     . GLY B 1 132 ? 147.184 161.119 160.856 1.00 42.78 ? 132 GLY B N     1 
ATOM   6651  C  CA    . GLY B 1 132 ? 148.038 162.183 161.345 1.00 40.91 ? 132 GLY B CA    1 
ATOM   6652  C  C     . GLY B 1 132 ? 147.810 162.595 162.783 1.00 44.92 ? 132 GLY B C     1 
ATOM   6653  O  O     . GLY B 1 132 ? 148.602 163.387 163.309 1.00 49.36 ? 132 GLY B O     1 
ATOM   6654  N  N     . ASP B 1 133 ? 146.769 162.094 163.440 1.00 46.71 ? 133 ASP B N     1 
ATOM   6655  C  CA    . ASP B 1 133 ? 146.463 162.457 164.818 1.00 47.09 ? 133 ASP B CA    1 
ATOM   6656  C  C     . ASP B 1 133 ? 147.025 161.392 165.753 1.00 48.73 ? 133 ASP B C     1 
ATOM   6657  O  O     . ASP B 1 133 ? 146.653 160.219 165.658 1.00 49.06 ? 133 ASP B O     1 
ATOM   6658  C  CB    . ASP B 1 133 ? 144.955 162.611 165.016 1.00 47.38 ? 133 ASP B CB    1 
ATOM   6659  C  CG    . ASP B 1 133 ? 144.604 163.358 166.289 1.00 51.26 ? 133 ASP B CG    1 
ATOM   6660  O  OD1   . ASP B 1 133 ? 145.498 163.554 167.139 1.00 52.19 ? 133 ASP B OD1   1 
ATOM   6661  O  OD2   . ASP B 1 133 ? 143.427 163.746 166.443 1.00 49.66 ? 133 ASP B OD2   1 
ATOM   6662  N  N     . THR B 1 134 ? 147.917 161.802 166.656 1.00 49.47 ? 134 THR B N     1 
ATOM   6663  C  CA    . THR B 1 134 ? 148.546 160.841 167.556 1.00 46.36 ? 134 THR B CA    1 
ATOM   6664  C  C     . THR B 1 134 ? 147.581 160.378 168.641 1.00 47.43 ? 134 THR B C     1 
ATOM   6665  O  O     . THR B 1 134 ? 147.523 159.184 168.958 1.00 50.12 ? 134 THR B O     1 
ATOM   6666  C  CB    . THR B 1 134 ? 149.798 161.452 168.179 1.00 52.47 ? 134 THR B CB    1 
ATOM   6667  O  OG1   . THR B 1 134 ? 150.674 161.900 167.138 1.00 54.23 ? 134 THR B OG1   1 
ATOM   6668  C  CG2   . THR B 1 134 ? 150.522 160.425 169.033 1.00 49.98 ? 134 THR B CG2   1 
ATOM   6669  N  N     . GLU B 1 135 ? 146.820 161.305 169.226 1.00 46.15 ? 135 GLU B N     1 
ATOM   6670  C  CA    . GLU B 1 135 ? 145.848 160.925 170.245 1.00 46.14 ? 135 GLU B CA    1 
ATOM   6671  C  C     . GLU B 1 135 ? 144.751 160.048 169.658 1.00 49.30 ? 135 GLU B C     1 
ATOM   6672  O  O     . GLU B 1 135 ? 144.315 159.080 170.292 1.00 50.27 ? 135 GLU B O     1 
ATOM   6673  C  CB    . GLU B 1 135 ? 145.253 162.173 170.895 1.00 48.01 ? 135 GLU B CB    1 
ATOM   6674  C  CG    . GLU B 1 135 ? 146.290 163.121 171.470 1.00 48.26 ? 135 GLU B CG    1 
ATOM   6675  C  CD    . GLU B 1 135 ? 147.387 162.396 172.225 1.00 53.26 ? 135 GLU B CD    1 
ATOM   6676  O  OE1   . GLU B 1 135 ? 147.075 161.725 173.232 1.00 52.48 ? 135 GLU B OE1   1 
ATOM   6677  O  OE2   . GLU B 1 135 ? 148.560 162.494 171.809 1.00 54.52 ? 135 GLU B OE2   1 
ATOM   6678  N  N     . LYS B 1 136 ? 144.292 160.370 168.448 1.00 41.35 ? 136 LYS B N     1 
ATOM   6679  C  CA    . LYS B 1 136 ? 143.303 159.530 167.782 1.00 39.84 ? 136 LYS B CA    1 
ATOM   6680  C  C     . LYS B 1 136 ? 143.868 158.145 167.488 1.00 40.61 ? 136 LYS B C     1 
ATOM   6681  O  O     . LYS B 1 136 ? 143.165 157.137 167.629 1.00 45.24 ? 136 LYS B O     1 
ATOM   6682  C  CB    . LYS B 1 136 ? 142.828 160.205 166.496 1.00 45.19 ? 136 LYS B CB    1 
ATOM   6683  C  CG    . LYS B 1 136 ? 141.537 159.650 165.930 1.00 41.81 ? 136 LYS B CG    1 
ATOM   6684  C  CD    . LYS B 1 136 ? 140.329 160.253 166.617 1.00 43.55 ? 136 LYS B CD    1 
ATOM   6685  C  CE    . LYS B 1 136 ? 139.053 159.942 165.856 1.00 45.31 ? 136 LYS B CE    1 
ATOM   6686  N  NZ    . LYS B 1 136 ? 137.905 160.750 166.352 1.00 46.75 ? 136 LYS B NZ    1 
ATOM   6687  N  N     . ALA B 1 137 ? 145.134 158.076 167.070 1.00 35.32 ? 137 ALA B N     1 
ATOM   6688  C  CA    . ALA B 1 137 ? 145.763 156.781 166.827 1.00 32.93 ? 137 ALA B CA    1 
ATOM   6689  C  C     . ALA B 1 137 ? 145.856 155.965 168.108 1.00 35.43 ? 137 ALA B C     1 
ATOM   6690  O  O     . ALA B 1 137 ? 145.623 154.752 168.097 1.00 37.84 ? 137 ALA B O     1 
ATOM   6691  C  CB    . ALA B 1 137 ? 147.149 156.974 166.211 1.00 33.03 ? 137 ALA B CB    1 
ATOM   6692  N  N     . LYS B 1 138 ? 146.198 156.613 169.223 1.00 40.00 ? 138 LYS B N     1 
ATOM   6693  C  CA    . LYS B 1 138 ? 146.240 155.910 170.502 1.00 39.35 ? 138 LYS B CA    1 
ATOM   6694  C  C     . LYS B 1 138 ? 144.852 155.440 170.918 1.00 38.24 ? 138 LYS B C     1 
ATOM   6695  O  O     . LYS B 1 138 ? 144.702 154.354 171.490 1.00 39.85 ? 138 LYS B O     1 
ATOM   6696  C  CB    . LYS B 1 138 ? 146.852 156.809 171.575 1.00 44.98 ? 138 LYS B CB    1 
ATOM   6697  C  CG    . LYS B 1 138 ? 148.318 156.526 171.853 1.00 43.86 ? 138 LYS B CG    1 
ATOM   6698  C  CD    . LYS B 1 138 ? 149.142 157.800 171.866 1.00 42.48 ? 138 LYS B CD    1 
ATOM   6699  C  CE    . LYS B 1 138 ? 148.623 158.785 172.895 1.00 41.38 ? 138 LYS B CE    1 
ATOM   6700  N  NZ    . LYS B 1 138 ? 149.499 159.985 173.000 1.00 44.01 ? 138 LYS B NZ    1 
ATOM   6701  N  N     . GLU B 1 139 ? 143.825 156.248 170.648 1.00 41.59 ? 139 GLU B N     1 
ATOM   6702  C  CA    . GLU B 1 139 ? 142.458 155.831 170.943 1.00 38.77 ? 139 GLU B CA    1 
ATOM   6703  C  C     . GLU B 1 139 ? 142.062 154.612 170.120 1.00 35.68 ? 139 GLU B C     1 
ATOM   6704  O  O     . GLU B 1 139 ? 141.435 153.681 170.638 1.00 42.24 ? 139 GLU B O     1 
ATOM   6705  C  CB    . GLU B 1 139 ? 141.491 156.987 170.690 1.00 36.87 ? 139 GLU B CB    1 
ATOM   6706  C  CG    . GLU B 1 139 ? 141.027 157.686 171.953 1.00 40.67 ? 139 GLU B CG    1 
ATOM   6707  C  CD    . GLU B 1 139 ? 140.853 159.178 171.762 1.00 47.08 ? 139 GLU B CD    1 
ATOM   6708  O  OE1   . GLU B 1 139 ? 140.335 159.588 170.703 1.00 45.20 ? 139 GLU B OE1   1 
ATOM   6709  O  OE2   . GLU B 1 139 ? 141.235 159.942 172.673 1.00 45.07 ? 139 GLU B OE2   1 
ATOM   6710  N  N     . TYR B 1 140 ? 142.419 154.599 168.834 1.00 28.59 ? 140 TYR B N     1 
ATOM   6711  C  CA    . TYR B 1 140 ? 142.141 153.432 168.000 1.00 29.66 ? 140 TYR B CA    1 
ATOM   6712  C  C     . TYR B 1 140 ? 142.909 152.211 168.491 1.00 32.28 ? 140 TYR B C     1 
ATOM   6713  O  O     . TYR B 1 140 ? 142.388 151.088 168.470 1.00 33.93 ? 140 TYR B O     1 
ATOM   6714  C  CB    . TYR B 1 140 ? 142.494 153.723 166.543 1.00 31.78 ? 140 TYR B CB    1 
ATOM   6715  C  CG    . TYR B 1 140 ? 141.518 154.610 165.812 1.00 33.17 ? 140 TYR B CG    1 
ATOM   6716  C  CD1   . TYR B 1 140 ? 140.170 154.289 165.741 1.00 35.70 ? 140 TYR B CD1   1 
ATOM   6717  C  CD2   . TYR B 1 140 ? 141.951 155.761 165.172 1.00 33.02 ? 140 TYR B CD2   1 
ATOM   6718  C  CE1   . TYR B 1 140 ? 139.282 155.098 165.062 1.00 33.91 ? 140 TYR B CE1   1 
ATOM   6719  C  CE2   . TYR B 1 140 ? 141.073 156.572 164.495 1.00 32.09 ? 140 TYR B CE2   1 
ATOM   6720  C  CZ    . TYR B 1 140 ? 139.741 156.240 164.443 1.00 30.48 ? 140 TYR B CZ    1 
ATOM   6721  O  OH    . TYR B 1 140 ? 138.871 157.057 163.763 1.00 35.68 ? 140 TYR B OH    1 
ATOM   6722  N  N     . VAL B 1 141 ? 144.159 152.409 168.919 1.00 35.66 ? 141 VAL B N     1 
ATOM   6723  C  CA    . VAL B 1 141 ? 144.950 151.312 169.467 1.00 34.53 ? 141 VAL B CA    1 
ATOM   6724  C  C     . VAL B 1 141 ? 144.278 150.738 170.704 1.00 32.82 ? 141 VAL B C     1 
ATOM   6725  O  O     . VAL B 1 141 ? 144.182 149.518 170.865 1.00 37.08 ? 141 VAL B O     1 
ATOM   6726  C  CB    . VAL B 1 141 ? 146.383 151.783 169.777 1.00 36.65 ? 141 VAL B CB    1 
ATOM   6727  C  CG1   . VAL B 1 141 ? 147.028 150.868 170.791 1.00 34.91 ? 141 VAL B CG1   1 
ATOM   6728  C  CG2   . VAL B 1 141 ? 147.210 151.802 168.519 1.00 34.92 ? 141 VAL B CG2   1 
ATOM   6729  N  N     . ASN B 1 142 ? 143.812 151.605 171.602 1.00 33.89 ? 142 ASN B N     1 
ATOM   6730  C  CA    . ASN B 1 142 ? 143.127 151.125 172.796 1.00 33.24 ? 142 ASN B CA    1 
ATOM   6731  C  C     . ASN B 1 142 ? 141.831 150.412 172.436 1.00 35.00 ? 142 ASN B C     1 
ATOM   6732  O  O     . ASN B 1 142 ? 141.474 149.407 173.059 1.00 39.10 ? 142 ASN B O     1 
ATOM   6733  C  CB    . ASN B 1 142 ? 142.859 152.286 173.750 1.00 31.86 ? 142 ASN B CB    1 
ATOM   6734  C  CG    . ASN B 1 142 ? 144.096 152.710 174.509 1.00 36.63 ? 142 ASN B CG    1 
ATOM   6735  O  OD1   . ASN B 1 142 ? 144.817 151.878 175.058 1.00 35.32 ? 142 ASN B OD1   1 
ATOM   6736  N  ND2   . ASN B 1 142 ? 144.353 154.012 174.543 1.00 38.38 ? 142 ASN B ND2   1 
ATOM   6737  N  N     . LEU B 1 143 ? 141.113 150.920 171.433 1.00 32.86 ? 143 LEU B N     1 
ATOM   6738  C  CA    . LEU B 1 143 ? 139.856 150.302 171.029 1.00 28.95 ? 143 LEU B CA    1 
ATOM   6739  C  C     . LEU B 1 143 ? 140.072 148.911 170.447 1.00 32.16 ? 143 LEU B C     1 
ATOM   6740  O  O     . LEU B 1 143 ? 139.292 147.992 170.720 1.00 35.06 ? 143 LEU B O     1 
ATOM   6741  C  CB    . LEU B 1 143 ? 139.140 151.198 170.021 1.00 29.33 ? 143 LEU B CB    1 
ATOM   6742  C  CG    . LEU B 1 143 ? 137.627 151.017 169.934 1.00 33.02 ? 143 LEU B CG    1 
ATOM   6743  C  CD1   . LEU B 1 143 ? 136.967 151.592 171.172 1.00 31.64 ? 143 LEU B CD1   1 
ATOM   6744  C  CD2   . LEU B 1 143 ? 137.094 151.676 168.680 1.00 32.38 ? 143 LEU B CD2   1 
ATOM   6745  N  N     . MET B 1 144 ? 141.118 148.735 169.640 1.00 34.08 ? 144 MET B N     1 
ATOM   6746  C  CA    . MET B 1 144 ? 141.334 147.463 168.962 1.00 26.42 ? 144 MET B CA    1 
ATOM   6747  C  C     . MET B 1 144 ? 142.114 146.454 169.795 1.00 26.64 ? 144 MET B C     1 
ATOM   6748  O  O     . MET B 1 144 ? 141.841 145.252 169.704 1.00 33.33 ? 144 MET B O     1 
ATOM   6749  C  CB    . MET B 1 144 ? 142.049 147.694 167.629 1.00 28.47 ? 144 MET B CB    1 
ATOM   6750  C  CG    . MET B 1 144 ? 141.224 148.484 166.628 1.00 28.70 ? 144 MET B CG    1 
ATOM   6751  S  SD    . MET B 1 144 ? 141.933 148.482 164.975 1.00 43.31 ? 144 MET B SD    1 
ATOM   6752  C  CE    . MET B 1 144 ? 143.374 149.506 165.242 1.00 27.53 ? 144 MET B CE    1 
ATOM   6753  N  N     . ILE B 1 145 ? 143.086 146.901 170.593 1.00 28.99 ? 145 ILE B N     1 
ATOM   6754  C  CA    . ILE B 1 145 ? 143.818 145.977 171.453 1.00 29.70 ? 145 ILE B CA    1 
ATOM   6755  C  C     . ILE B 1 145 ? 142.927 145.483 172.585 1.00 34.64 ? 145 ILE B C     1 
ATOM   6756  O  O     . ILE B 1 145 ? 143.081 144.350 173.055 1.00 37.65 ? 145 ILE B O     1 
ATOM   6757  C  CB    . ILE B 1 145 ? 145.117 146.630 171.969 1.00 31.59 ? 145 ILE B CB    1 
ATOM   6758  C  CG1   . ILE B 1 145 ? 146.195 145.568 172.197 1.00 32.44 ? 145 ILE B CG1   1 
ATOM   6759  C  CG2   . ILE B 1 145 ? 144.878 147.426 173.244 1.00 33.03 ? 145 ILE B CG2   1 
ATOM   6760  C  CD1   . ILE B 1 145 ? 146.716 144.940 170.926 1.00 34.42 ? 145 ILE B CD1   1 
ATOM   6761  N  N     . ASN B 1 146 ? 141.981 146.311 173.038 1.00 33.24 ? 146 ASN B N     1 
ATOM   6762  C  CA    . ASN B 1 146 ? 140.934 145.832 173.930 1.00 27.82 ? 146 ASN B CA    1 
ATOM   6763  C  C     . ASN B 1 146 ? 139.916 144.977 173.197 1.00 29.80 ? 146 ASN B C     1 
ATOM   6764  O  O     . ASN B 1 146 ? 139.060 144.368 173.847 1.00 37.20 ? 146 ASN B O     1 
ATOM   6765  C  CB    . ASN B 1 146 ? 140.229 147.006 174.606 1.00 28.55 ? 146 ASN B CB    1 
ATOM   6766  C  CG    . ASN B 1 146 ? 141.107 147.706 175.621 1.00 32.48 ? 146 ASN B CG    1 
ATOM   6767  O  OD1   . ASN B 1 146 ? 142.099 147.151 176.088 1.00 38.58 ? 146 ASN B OD1   1 
ATOM   6768  N  ND2   . ASN B 1 146 ? 140.747 148.936 175.966 1.00 33.68 ? 146 ASN B ND2   1 
ATOM   6769  N  N     . GLN B 1 147 ? 139.994 144.931 171.866 1.00 32.40 ? 147 GLN B N     1 
ATOM   6770  C  CA    . GLN B 1 147 ? 139.121 144.106 171.035 1.00 24.51 ? 147 GLN B CA    1 
ATOM   6771  C  C     . GLN B 1 147 ? 137.657 144.488 171.219 1.00 24.47 ? 147 GLN B C     1 
ATOM   6772  O  O     . GLN B 1 147 ? 136.772 143.635 171.223 1.00 34.49 ? 147 GLN B O     1 
ATOM   6773  C  CB    . GLN B 1 147 ? 139.344 142.619 171.311 1.00 25.20 ? 147 GLN B CB    1 
ATOM   6774  C  CG    . GLN B 1 147 ? 140.700 142.119 170.856 1.00 25.15 ? 147 GLN B CG    1 
ATOM   6775  C  CD    . GLN B 1 147 ? 140.755 140.615 170.739 1.00 29.77 ? 147 GLN B CD    1 
ATOM   6776  O  OE1   . GLN B 1 147 ? 140.274 139.897 171.612 1.00 37.61 ? 147 GLN B OE1   1 
ATOM   6777  N  NE2   . GLN B 1 147 ? 141.349 140.128 169.658 1.00 30.35 ? 147 GLN B NE2   1 
ATOM   6778  N  N     . GLU B 1 148 ? 137.403 145.787 171.384 1.00 26.45 ? 148 GLU B N     1 
ATOM   6779  C  CA    . GLU B 1 148 ? 136.033 146.283 171.396 1.00 24.56 ? 148 GLU B CA    1 
ATOM   6780  C  C     . GLU B 1 148 ? 135.497 146.484 169.988 1.00 28.90 ? 148 GLU B C     1 
ATOM   6781  O  O     . GLU B 1 148 ? 134.301 146.286 169.747 1.00 33.64 ? 148 GLU B O     1 
ATOM   6782  C  CB    . GLU B 1 148 ? 135.951 147.597 172.170 1.00 20.87 ? 148 GLU B CB    1 
ATOM   6783  C  CG    . GLU B 1 148 ? 136.318 147.488 173.631 1.00 23.69 ? 148 GLU B CG    1 
ATOM   6784  C  CD    . GLU B 1 148 ? 136.709 148.825 174.224 1.00 33.43 ? 148 GLU B CD    1 
ATOM   6785  O  OE1   . GLU B 1 148 ? 137.850 149.269 173.987 1.00 33.27 ? 148 GLU B OE1   1 
ATOM   6786  O  OE2   . GLU B 1 148 ? 135.874 149.437 174.921 1.00 39.02 ? 148 GLU B OE2   1 
ATOM   6787  N  N     . TYR B 1 149 ? 136.358 146.878 169.055 1.00 26.11 ? 149 TYR B N     1 
ATOM   6788  C  CA    . TYR B 1 149 ? 135.981 147.097 167.668 1.00 20.16 ? 149 TYR B CA    1 
ATOM   6789  C  C     . TYR B 1 149 ? 136.952 146.355 166.768 1.00 24.15 ? 149 TYR B C     1 
ATOM   6790  O  O     . TYR B 1 149 ? 138.169 146.440 166.958 1.00 30.46 ? 149 TYR B O     1 
ATOM   6791  C  CB    . TYR B 1 149 ? 135.977 148.587 167.320 1.00 22.77 ? 149 TYR B CB    1 
ATOM   6792  C  CG    . TYR B 1 149 ? 135.864 148.862 165.841 1.00 23.91 ? 149 TYR B CG    1 
ATOM   6793  C  CD1   . TYR B 1 149 ? 134.734 148.482 165.131 1.00 20.04 ? 149 TYR B CD1   1 
ATOM   6794  C  CD2   . TYR B 1 149 ? 136.888 149.497 165.152 1.00 18.58 ? 149 TYR B CD2   1 
ATOM   6795  C  CE1   . TYR B 1 149 ? 134.626 148.729 163.780 1.00 19.71 ? 149 TYR B CE1   1 
ATOM   6796  C  CE2   . TYR B 1 149 ? 136.789 149.746 163.800 1.00 24.21 ? 149 TYR B CE2   1 
ATOM   6797  C  CZ    . TYR B 1 149 ? 135.654 149.361 163.119 1.00 19.92 ? 149 TYR B CZ    1 
ATOM   6798  O  OH    . TYR B 1 149 ? 135.548 149.607 161.772 1.00 16.50 ? 149 TYR B OH    1 
ATOM   6799  N  N     . GLN B 1 150 ? 136.415 145.631 165.797 1.00 20.70 ? 150 GLN B N     1 
ATOM   6800  C  CA    . GLN B 1 150 ? 137.224 144.905 164.822 1.00 15.05 ? 150 GLN B CA    1 
ATOM   6801  C  C     . GLN B 1 150 ? 136.930 145.431 163.427 1.00 21.26 ? 150 GLN B C     1 
ATOM   6802  O  O     . GLN B 1 150 ? 135.805 145.249 162.926 1.00 29.29 ? 150 GLN B O     1 
ATOM   6803  C  CB    . GLN B 1 150 ? 136.945 143.405 164.897 1.00 20.52 ? 150 GLN B CB    1 
ATOM   6804  C  CG    . GLN B 1 150 ? 137.600 142.576 163.805 1.00 21.23 ? 150 GLN B CG    1 
ATOM   6805  C  CD    . GLN B 1 150 ? 139.101 142.757 163.747 1.00 21.53 ? 150 GLN B CD    1 
ATOM   6806  O  OE1   . GLN B 1 150 ? 139.821 142.376 164.669 1.00 27.25 ? 150 GLN B OE1   1 
ATOM   6807  N  NE2   . GLN B 1 150 ? 139.583 143.335 162.656 1.00 19.19 ? 150 GLN B NE2   1 
ATOM   6808  N  N     . PRO B 1 151 ? 137.880 146.091 162.769 1.00 26.27 ? 151 PRO B N     1 
ATOM   6809  C  CA    . PRO B 1 151 ? 137.689 146.429 161.356 1.00 15.70 ? 151 PRO B CA    1 
ATOM   6810  C  C     . PRO B 1 151 ? 137.537 145.165 160.527 1.00 21.78 ? 151 PRO B C     1 
ATOM   6811  O  O     . PRO B 1 151 ? 138.052 144.101 160.878 1.00 28.13 ? 151 PRO B O     1 
ATOM   6812  C  CB    . PRO B 1 151 ? 138.967 147.193 160.993 1.00 18.86 ? 151 PRO B CB    1 
ATOM   6813  C  CG    . PRO B 1 151 ? 139.536 147.640 162.297 1.00 21.49 ? 151 PRO B CG    1 
ATOM   6814  C  CD    . PRO B 1 151 ? 139.158 146.596 163.294 1.00 20.38 ? 151 PRO B CD    1 
ATOM   6815  N  N     . SER B 1 152 ? 136.805 145.287 159.425 1.00 24.55 ? 152 SER B N     1 
ATOM   6816  C  CA    . SER B 1 152 ? 136.521 144.134 158.585 1.00 19.78 ? 152 SER B CA    1 
ATOM   6817  C  C     . SER B 1 152 ? 137.811 143.513 158.058 1.00 24.04 ? 152 SER B C     1 
ATOM   6818  O  O     . SER B 1 152 ? 138.890 144.108 158.110 1.00 24.78 ? 152 SER B O     1 
ATOM   6819  C  CB    . SER B 1 152 ? 135.618 144.532 157.420 1.00 22.17 ? 152 SER B CB    1 
ATOM   6820  O  OG    . SER B 1 152 ? 136.278 145.428 156.545 1.00 25.86 ? 152 SER B OG    1 
ATOM   6821  N  N     . THR B 1 153 ? 137.683 142.288 157.554 1.00 30.82 ? 153 THR B N     1 
ATOM   6822  C  CA    . THR B 1 153 ? 138.831 141.583 156.990 1.00 22.06 ? 153 THR B CA    1 
ATOM   6823  C  C     . THR B 1 153 ? 139.578 142.393 155.935 1.00 30.63 ? 153 THR B C     1 
ATOM   6824  O  O     . THR B 1 153 ? 140.817 142.442 156.007 1.00 34.04 ? 153 THR B O     1 
ATOM   6825  C  CB    . THR B 1 153 ? 138.375 140.230 156.422 1.00 27.86 ? 153 THR B CB    1 
ATOM   6826  O  OG1   . THR B 1 153 ? 138.055 139.339 157.496 1.00 32.93 ? 153 THR B OG1   1 
ATOM   6827  C  CG2   . THR B 1 153 ? 139.464 139.606 155.565 1.00 30.47 ? 153 THR B CG2   1 
ATOM   6828  N  N     . PRO B 1 154 ? 138.927 143.051 154.966 1.00 32.57 ? 154 PRO B N     1 
ATOM   6829  C  CA    . PRO B 1 154 ? 139.701 143.896 154.038 1.00 22.63 ? 154 PRO B CA    1 
ATOM   6830  C  C     . PRO B 1 154 ? 140.439 145.025 154.735 1.00 23.68 ? 154 PRO B C     1 
ATOM   6831  O  O     . PRO B 1 154 ? 141.636 145.224 154.493 1.00 31.51 ? 154 PRO B O     1 
ATOM   6832  C  CB    . PRO B 1 154 ? 138.630 144.421 153.073 1.00 25.30 ? 154 PRO B CB    1 
ATOM   6833  C  CG    . PRO B 1 154 ? 137.521 143.460 153.180 1.00 23.91 ? 154 PRO B CG    1 
ATOM   6834  C  CD    . PRO B 1 154 ? 137.502 143.014 154.592 1.00 26.33 ? 154 PRO B CD    1 
ATOM   6835  N  N     . THR B 1 155 ? 139.756 145.770 155.605 1.00 27.05 ? 155 THR B N     1 
ATOM   6836  C  CA    . THR B 1 155 ? 140.396 146.889 156.288 1.00 23.60 ? 155 THR B CA    1 
ATOM   6837  C  C     . THR B 1 155 ? 141.513 146.410 157.206 1.00 26.50 ? 155 THR B C     1 
ATOM   6838  O  O     . THR B 1 155 ? 142.633 146.927 157.162 1.00 27.38 ? 155 THR B O     1 
ATOM   6839  C  CB    . THR B 1 155 ? 139.358 147.684 157.080 1.00 25.02 ? 155 THR B CB    1 
ATOM   6840  O  OG1   . THR B 1 155 ? 138.249 148.003 156.233 1.00 25.61 ? 155 THR B OG1   1 
ATOM   6841  C  CG2   . THR B 1 155 ? 139.968 148.965 157.608 1.00 22.08 ? 155 THR B CG2   1 
ATOM   6842  N  N     . PHE B 1 156 ? 141.227 145.412 158.044 1.00 28.67 ? 156 PHE B N     1 
ATOM   6843  C  CA    . PHE B 1 156 ? 142.228 144.930 158.990 1.00 23.12 ? 156 PHE B CA    1 
ATOM   6844  C  C     . PHE B 1 156 ? 143.432 144.336 158.270 1.00 29.32 ? 156 PHE B C     1 
ATOM   6845  O  O     . PHE B 1 156 ? 144.577 144.541 158.685 1.00 32.11 ? 156 PHE B O     1 
ATOM   6846  C  CB    . PHE B 1 156 ? 141.604 143.900 159.931 1.00 27.11 ? 156 PHE B CB    1 
ATOM   6847  C  CG    . PHE B 1 156 ? 142.385 143.684 161.195 1.00 30.89 ? 156 PHE B CG    1 
ATOM   6848  C  CD1   . PHE B 1 156 ? 142.668 144.744 162.037 1.00 28.24 ? 156 PHE B CD1   1 
ATOM   6849  C  CD2   . PHE B 1 156 ? 142.835 142.422 161.541 1.00 24.72 ? 156 PHE B CD2   1 
ATOM   6850  C  CE1   . PHE B 1 156 ? 143.386 144.551 163.199 1.00 29.64 ? 156 PHE B CE1   1 
ATOM   6851  C  CE2   . PHE B 1 156 ? 143.551 142.224 162.701 1.00 26.47 ? 156 PHE B CE2   1 
ATOM   6852  C  CZ    . PHE B 1 156 ? 143.827 143.289 163.531 1.00 30.20 ? 156 PHE B CZ    1 
ATOM   6853  N  N     . LEU B 1 157 ? 143.191 143.595 157.187 1.00 31.85 ? 157 LEU B N     1 
ATOM   6854  C  CA    . LEU B 1 157 ? 144.278 142.924 156.485 1.00 29.11 ? 157 LEU B CA    1 
ATOM   6855  C  C     . LEU B 1 157 ? 145.111 143.899 155.661 1.00 33.88 ? 157 LEU B C     1 
ATOM   6856  O  O     . LEU B 1 157 ? 146.340 143.779 155.607 1.00 40.31 ? 157 LEU B O     1 
ATOM   6857  C  CB    . LEU B 1 157 ? 143.708 141.821 155.595 1.00 32.66 ? 157 LEU B CB    1 
ATOM   6858  C  CG    . LEU B 1 157 ? 144.658 141.159 154.600 1.00 32.69 ? 157 LEU B CG    1 
ATOM   6859  C  CD1   . LEU B 1 157 ? 145.683 140.313 155.328 1.00 32.97 ? 157 LEU B CD1   1 
ATOM   6860  C  CD2   . LEU B 1 157 ? 143.882 140.323 153.598 1.00 30.67 ? 157 LEU B CD2   1 
ATOM   6861  N  N     . ASN B 1 158 ? 144.469 144.876 155.019 1.00 35.02 ? 158 ASN B N     1 
ATOM   6862  C  CA    . ASN B 1 158 ? 145.130 145.646 153.976 1.00 30.74 ? 158 ASN B CA    1 
ATOM   6863  C  C     . ASN B 1 158 ? 145.546 147.049 154.395 1.00 34.21 ? 158 ASN B C     1 
ATOM   6864  O  O     . ASN B 1 158 ? 146.363 147.658 153.698 1.00 40.46 ? 158 ASN B O     1 
ATOM   6865  C  CB    . ASN B 1 158 ? 144.219 145.748 152.748 1.00 33.17 ? 158 ASN B CB    1 
ATOM   6866  C  CG    . ASN B 1 158 ? 144.017 144.414 152.064 1.00 37.77 ? 158 ASN B CG    1 
ATOM   6867  O  OD1   . ASN B 1 158 ? 144.963 143.648 151.884 1.00 38.65 ? 158 ASN B OD1   1 
ATOM   6868  N  ND2   . ASN B 1 158 ? 142.780 144.126 151.682 1.00 36.78 ? 158 ASN B ND2   1 
ATOM   6869  N  N     . ALA B 1 159 ? 145.021 147.578 155.498 1.00 33.17 ? 159 ALA B N     1 
ATOM   6870  C  CA    . ALA B 1 159 ? 145.318 148.957 155.867 1.00 33.36 ? 159 ALA B CA    1 
ATOM   6871  C  C     . ALA B 1 159 ? 146.810 149.146 156.103 1.00 38.15 ? 159 ALA B C     1 
ATOM   6872  O  O     . ALA B 1 159 ? 147.436 148.389 156.849 1.00 42.56 ? 159 ALA B O     1 
ATOM   6873  C  CB    . ALA B 1 159 ? 144.535 149.357 157.116 1.00 33.86 ? 159 ALA B CB    1 
ATOM   6874  N  N     . GLY B 1 160 ? 147.377 150.165 155.463 1.00 42.65 ? 160 GLY B N     1 
ATOM   6875  C  CA    . GLY B 1 160 ? 148.788 150.450 155.608 1.00 39.89 ? 160 GLY B CA    1 
ATOM   6876  C  C     . GLY B 1 160 ? 149.720 149.511 154.880 1.00 42.44 ? 160 GLY B C     1 
ATOM   6877  O  O     . GLY B 1 160 ? 150.891 149.409 155.257 1.00 49.26 ? 160 GLY B O     1 
ATOM   6878  N  N     . ARG B 1 161 ? 149.246 148.821 153.849 1.00 44.11 ? 161 ARG B N     1 
ATOM   6879  C  CA    . ARG B 1 161 ? 150.063 147.895 153.079 1.00 45.27 ? 161 ARG B CA    1 
ATOM   6880  C  C     . ARG B 1 161 ? 150.219 148.401 151.652 1.00 47.84 ? 161 ARG B C     1 
ATOM   6881  O  O     . ARG B 1 161 ? 149.248 148.840 151.029 1.00 48.45 ? 161 ARG B O     1 
ATOM   6882  C  CB    . ARG B 1 161 ? 149.452 146.493 153.071 1.00 42.02 ? 161 ARG B CB    1 
ATOM   6883  C  CG    . ARG B 1 161 ? 149.520 145.781 154.408 1.00 42.07 ? 161 ARG B CG    1 
ATOM   6884  C  CD    . ARG B 1 161 ? 149.457 144.278 154.231 1.00 42.44 ? 161 ARG B CD    1 
ATOM   6885  N  NE    . ARG B 1 161 ? 149.400 143.581 155.509 1.00 44.01 ? 161 ARG B NE    1 
ATOM   6886  C  CZ    . ARG B 1 161 ? 149.053 142.310 155.655 1.00 45.39 ? 161 ARG B CZ    1 
ATOM   6887  N  NH1   . ARG B 1 161 ? 148.738 141.556 154.615 1.00 47.17 ? 161 ARG B NH1   1 
ATOM   6888  N  NH2   . ARG B 1 161 ? 149.020 141.783 156.875 1.00 45.25 ? 161 ARG B NH2   1 
ATOM   6889  N  N     . LYS B 1 162 ? 151.451 148.341 151.141 1.00 56.88 ? 162 LYS B N     1 
ATOM   6890  C  CA    . LYS B 1 162 ? 151.717 148.810 149.784 1.00 56.94 ? 162 LYS B CA    1 
ATOM   6891  C  C     . LYS B 1 162 ? 151.065 147.903 148.748 1.00 57.80 ? 162 LYS B C     1 
ATOM   6892  O  O     . LYS B 1 162 ? 150.384 148.378 147.832 1.00 59.09 ? 162 LYS B O     1 
ATOM   6893  C  CB    . LYS B 1 162 ? 153.225 148.900 149.551 1.00 57.18 ? 162 LYS B CB    1 
ATOM   6894  C  CG    . LYS B 1 162 ? 153.622 149.106 148.101 1.00 58.45 ? 162 LYS B CG    1 
ATOM   6895  C  CD    . LYS B 1 162 ? 153.573 150.576 147.724 1.00 58.12 ? 162 LYS B CD    1 
ATOM   6896  C  CE    . LYS B 1 162 ? 154.628 151.372 148.473 1.00 57.18 ? 162 LYS B CE    1 
ATOM   6897  N  NZ    . LYS B 1 162 ? 154.317 152.827 148.493 1.00 57.81 ? 162 LYS B NZ    1 
ATOM   6898  N  N     . ARG B 1 163 ? 151.260 146.592 148.877 1.00 58.71 ? 163 ARG B N     1 
ATOM   6899  C  CA    . ARG B 1 163 ? 150.660 145.625 147.958 1.00 60.54 ? 163 ARG B CA    1 
ATOM   6900  C  C     . ARG B 1 163 ? 149.351 145.088 148.539 1.00 62.48 ? 163 ARG B C     1 
ATOM   6901  O  O     . ARG B 1 163 ? 149.213 143.915 148.885 1.00 61.03 ? 163 ARG B O     1 
ATOM   6902  C  CB    . ARG B 1 163 ? 151.640 144.497 147.658 1.00 61.07 ? 163 ARG B CB    1 
ATOM   6903  C  CG    . ARG B 1 163 ? 152.731 144.871 146.668 1.00 62.30 ? 163 ARG B CG    1 
ATOM   6904  C  CD    . ARG B 1 163 ? 153.878 143.881 146.723 1.00 61.57 ? 163 ARG B CD    1 
ATOM   6905  N  NE    . ARG B 1 163 ? 154.757 144.127 147.859 1.00 64.19 ? 163 ARG B NE    1 
ATOM   6906  C  CZ    . ARG B 1 163 ? 155.496 143.197 148.448 1.00 65.44 ? 163 ARG B CZ    1 
ATOM   6907  N  NH1   . ARG B 1 163 ? 155.485 141.940 148.035 1.00 63.07 ? 163 ARG B NH1   1 
ATOM   6908  N  NH2   . ARG B 1 163 ? 156.266 143.537 149.478 1.00 62.35 ? 163 ARG B NH2   1 
ATOM   6909  N  N     . ARG B 1 164 ? 148.379 145.987 148.638 1.00 56.39 ? 164 ARG B N     1 
ATOM   6910  C  CA    . ARG B 1 164 ? 147.104 145.703 149.273 1.00 53.68 ? 164 ARG B CA    1 
ATOM   6911  C  C     . ARG B 1 164 ? 145.980 145.707 148.247 1.00 52.99 ? 164 ARG B C     1 
ATOM   6912  O  O     . ARG B 1 164 ? 146.071 146.353 147.199 1.00 52.61 ? 164 ARG B O     1 
ATOM   6913  C  CB    . ARG B 1 164 ? 146.796 146.730 150.367 1.00 52.38 ? 164 ARG B CB    1 
ATOM   6914  C  CG    . ARG B 1 164 ? 146.327 148.079 149.836 1.00 51.08 ? 164 ARG B CG    1 
ATOM   6915  C  CD    . ARG B 1 164 ? 145.821 148.976 150.954 1.00 52.89 ? 164 ARG B CD    1 
ATOM   6916  N  NE    . ARG B 1 164 ? 145.570 150.340 150.507 1.00 53.91 ? 164 ARG B NE    1 
ATOM   6917  C  CZ    . ARG B 1 164 ? 144.498 150.722 149.826 1.00 55.48 ? 164 ARG B CZ    1 
ATOM   6918  N  NH1   . ARG B 1 164 ? 143.548 149.863 149.493 1.00 51.48 ? 164 ARG B NH1   1 
ATOM   6919  N  NH2   . ARG B 1 164 ? 144.375 151.998 149.472 1.00 54.60 ? 164 ARG B NH2   1 
ATOM   6920  N  N     . GLY B 1 165 ? 144.923 144.962 148.556 1.00 49.19 ? 165 GLY B N     1 
ATOM   6921  C  CA    . GLY B 1 165 ? 143.673 145.101 147.848 1.00 46.07 ? 165 GLY B CA    1 
ATOM   6922  C  C     . GLY B 1 165 ? 142.878 146.273 148.384 1.00 49.42 ? 165 GLY B C     1 
ATOM   6923  O  O     . GLY B 1 165 ? 143.325 147.030 149.246 1.00 50.61 ? 165 GLY B O     1 
ATOM   6924  N  N     . GLU B 1 166 ? 141.671 146.428 147.855 1.00 46.23 ? 166 GLU B N     1 
ATOM   6925  C  CA    . GLU B 1 166 ? 140.800 147.492 148.326 1.00 42.23 ? 166 GLU B CA    1 
ATOM   6926  C  C     . GLU B 1 166 ? 140.336 147.207 149.751 1.00 42.20 ? 166 GLU B C     1 
ATOM   6927  O  O     . GLU B 1 166 ? 140.241 146.054 150.180 1.00 39.07 ? 166 GLU B O     1 
ATOM   6928  C  CB    . GLU B 1 166 ? 139.595 147.649 147.399 1.00 40.97 ? 166 GLU B CB    1 
ATOM   6929  C  CG    . GLU B 1 166 ? 139.211 149.094 147.121 1.00 43.85 ? 166 GLU B CG    1 
ATOM   6930  C  CD    . GLU B 1 166 ? 140.289 149.859 146.373 1.00 47.68 ? 166 GLU B CD    1 
ATOM   6931  O  OE1   . GLU B 1 166 ? 141.090 149.221 145.658 1.00 47.24 ? 166 GLU B OE1   1 
ATOM   6932  O  OE2   . GLU B 1 166 ? 140.337 151.100 146.500 1.00 46.54 ? 166 GLU B OE2   1 
ATOM   6933  N  N     . LEU B 1 167 ? 140.056 148.279 150.490 1.00 36.59 ? 167 LEU B N     1 
ATOM   6934  C  CA    . LEU B 1 167 ? 139.535 148.146 151.843 1.00 32.27 ? 167 LEU B CA    1 
ATOM   6935  C  C     . LEU B 1 167 ? 138.048 147.822 151.868 1.00 34.43 ? 167 LEU B C     1 
ATOM   6936  O  O     . LEU B 1 167 ? 137.511 147.529 152.941 1.00 36.83 ? 167 LEU B O     1 
ATOM   6937  C  CB    . LEU B 1 167 ? 139.799 149.428 152.636 1.00 32.98 ? 167 LEU B CB    1 
ATOM   6938  C  CG    . LEU B 1 167 ? 141.030 149.452 153.546 1.00 33.31 ? 167 LEU B CG    1 
ATOM   6939  C  CD1   . LEU B 1 167 ? 142.238 148.833 152.866 1.00 32.95 ? 167 LEU B CD1   1 
ATOM   6940  C  CD2   . LEU B 1 167 ? 141.331 150.873 153.974 1.00 31.08 ? 167 LEU B CD2   1 
ATOM   6941  N  N     . VAL B 1 168 ? 137.380 147.867 150.719 1.00 35.63 ? 168 VAL B N     1 
ATOM   6942  C  CA    . VAL B 1 168 ? 135.975 147.507 150.587 1.00 29.40 ? 168 VAL B CA    1 
ATOM   6943  C  C     . VAL B 1 168 ? 135.894 146.207 149.802 1.00 32.26 ? 168 VAL B C     1 
ATOM   6944  O  O     . VAL B 1 168 ? 136.606 146.028 148.807 1.00 37.33 ? 168 VAL B O     1 
ATOM   6945  C  CB    . VAL B 1 168 ? 135.172 148.623 149.890 1.00 28.52 ? 168 VAL B CB    1 
ATOM   6946  C  CG1   . VAL B 1 168 ? 133.697 148.262 149.817 1.00 32.86 ? 168 VAL B CG1   1 
ATOM   6947  C  CG2   . VAL B 1 168 ? 135.367 149.944 150.607 1.00 30.94 ? 168 VAL B CG2   1 
ATOM   6948  N  N     . SER B 1 169 ? 135.036 145.293 150.255 1.00 29.41 ? 169 SER B N     1 
ATOM   6949  C  CA    . SER B 1 169 ? 134.866 144.018 149.576 1.00 29.02 ? 169 SER B CA    1 
ATOM   6950  C  C     . SER B 1 169 ? 133.428 143.707 149.190 1.00 30.91 ? 169 SER B C     1 
ATOM   6951  O  O     . SER B 1 169 ? 133.186 142.658 148.584 1.00 38.63 ? 169 SER B O     1 
ATOM   6952  C  CB    . SER B 1 169 ? 135.410 142.868 150.436 1.00 34.49 ? 169 SER B CB    1 
ATOM   6953  O  OG    . SER B 1 169 ? 136.796 142.682 150.212 1.00 40.44 ? 169 SER B OG    1 
ATOM   6954  N  N     . CYS B 1 170 ? 132.471 144.568 149.519 1.00 25.09 ? 170 CYS B N     1 
ATOM   6955  C  CA    . CYS B 1 170 ? 131.084 144.379 149.113 1.00 24.18 ? 170 CYS B CA    1 
ATOM   6956  C  C     . CYS B 1 170 ? 130.700 145.499 148.160 1.00 24.19 ? 170 CYS B C     1 
ATOM   6957  O  O     . CYS B 1 170 ? 130.822 146.680 148.500 1.00 30.45 ? 170 CYS B O     1 
ATOM   6958  C  CB    . CYS B 1 170 ? 130.147 144.338 150.324 1.00 32.80 ? 170 CYS B CB    1 
ATOM   6959  S  SG    . CYS B 1 170 ? 130.252 145.747 151.448 1.00 42.57 ? 170 CYS B SG    1 
ATOM   6960  N  N     . PHE B 1 171 ? 130.248 145.125 146.967 1.00 24.39 ? 171 PHE B N     1 
ATOM   6961  C  CA    . PHE B 1 171 ? 129.806 146.071 145.955 1.00 14.26 ? 171 PHE B CA    1 
ATOM   6962  C  C     . PHE B 1 171 ? 128.473 145.608 145.395 1.00 17.63 ? 171 PHE B C     1 
ATOM   6963  O  O     . PHE B 1 171 ? 128.227 144.406 145.268 1.00 23.62 ? 171 PHE B O     1 
ATOM   6964  C  CB    . PHE B 1 171 ? 130.834 146.208 144.827 1.00 18.55 ? 171 PHE B CB    1 
ATOM   6965  C  CG    . PHE B 1 171 ? 132.219 146.509 145.310 1.00 19.12 ? 171 PHE B CG    1 
ATOM   6966  C  CD1   . PHE B 1 171 ? 132.584 147.800 145.639 1.00 20.35 ? 171 PHE B CD1   1 
ATOM   6967  C  CD2   . PHE B 1 171 ? 133.157 145.501 145.438 1.00 20.39 ? 171 PHE B CD2   1 
ATOM   6968  C  CE1   . PHE B 1 171 ? 133.854 148.079 146.090 1.00 14.42 ? 171 PHE B CE1   1 
ATOM   6969  C  CE2   . PHE B 1 171 ? 134.430 145.777 145.887 1.00 18.94 ? 171 PHE B CE2   1 
ATOM   6970  C  CZ    . PHE B 1 171 ? 134.778 147.068 146.213 1.00 13.79 ? 171 PHE B CZ    1 
ATOM   6971  N  N     . LEU B 1 172 ? 127.612 146.568 145.071 1.00 14.92 ? 172 LEU B N     1 
ATOM   6972  C  CA    . LEU B 1 172 ? 126.286 146.291 144.536 1.00 9.87  ? 172 LEU B CA    1 
ATOM   6973  C  C     . LEU B 1 172 ? 126.108 147.101 143.265 1.00 13.75 ? 172 LEU B C     1 
ATOM   6974  O  O     . LEU B 1 172 ? 126.110 148.334 143.310 1.00 19.02 ? 172 LEU B O     1 
ATOM   6975  C  CB    . LEU B 1 172 ? 125.190 146.637 145.549 1.00 10.83 ? 172 LEU B CB    1 
ATOM   6976  C  CG    . LEU B 1 172 ? 125.072 145.807 146.827 1.00 6.40  ? 172 LEU B CG    1 
ATOM   6977  C  CD1   . LEU B 1 172 ? 126.103 146.233 147.856 1.00 12.59 ? 172 LEU B CD1   1 
ATOM   6978  C  CD2   . LEU B 1 172 ? 123.676 145.951 147.389 1.00 15.78 ? 172 LEU B CD2   1 
ATOM   6979  N  N     . LEU B 1 173 ? 125.946 146.412 142.141 1.00 19.26 ? 173 LEU B N     1 
ATOM   6980  C  CA    . LEU B 1 173 ? 125.843 147.048 140.838 1.00 10.48 ? 173 LEU B CA    1 
ATOM   6981  C  C     . LEU B 1 173 ? 124.437 146.894 140.278 1.00 18.22 ? 173 LEU B C     1 
ATOM   6982  O  O     . LEU B 1 173 ? 123.846 145.813 140.344 1.00 26.18 ? 173 LEU B O     1 
ATOM   6983  C  CB    . LEU B 1 173 ? 126.847 146.449 139.852 1.00 14.24 ? 173 LEU B CB    1 
ATOM   6984  C  CG    . LEU B 1 173 ? 128.301 146.316 140.296 1.00 19.23 ? 173 LEU B CG    1 
ATOM   6985  C  CD1   . LEU B 1 173 ? 129.135 145.807 139.136 1.00 21.14 ? 173 LEU B CD1   1 
ATOM   6986  C  CD2   . LEU B 1 173 ? 128.838 147.641 140.807 1.00 23.54 ? 173 LEU B CD2   1 
ATOM   6987  N  N     . GLU B 1 174 ? 123.908 147.983 139.734 1.00 25.28 ? 174 GLU B N     1 
ATOM   6988  C  CA    . GLU B 1 174 ? 122.694 147.939 138.936 1.00 21.49 ? 174 GLU B CA    1 
ATOM   6989  C  C     . GLU B 1 174 ? 123.064 147.709 137.478 1.00 19.90 ? 174 GLU B C     1 
ATOM   6990  O  O     . GLU B 1 174 ? 123.986 148.340 136.954 1.00 28.78 ? 174 GLU B O     1 
ATOM   6991  C  CB    . GLU B 1 174 ? 121.904 149.240 139.073 1.00 24.52 ? 174 GLU B CB    1 
ATOM   6992  C  CG    . GLU B 1 174 ? 121.319 149.488 140.447 1.00 22.51 ? 174 GLU B CG    1 
ATOM   6993  C  CD    . GLU B 1 174 ? 119.825 149.258 140.488 1.00 25.44 ? 174 GLU B CD    1 
ATOM   6994  O  OE1   . GLU B 1 174 ? 119.265 148.795 139.474 1.00 28.46 ? 174 GLU B OE1   1 
ATOM   6995  O  OE2   . GLU B 1 174 ? 119.207 149.545 141.534 1.00 24.98 ? 174 GLU B OE2   1 
ATOM   6996  N  N     . VAL B 1 175 ? 122.344 146.805 136.824 1.00 17.66 ? 175 VAL B N     1 
ATOM   6997  C  CA    . VAL B 1 175 ? 122.572 146.482 135.421 1.00 17.83 ? 175 VAL B CA    1 
ATOM   6998  C  C     . VAL B 1 175 ? 121.365 146.961 134.627 1.00 22.49 ? 175 VAL B C     1 
ATOM   6999  O  O     . VAL B 1 175 ? 120.232 146.543 134.892 1.00 23.87 ? 175 VAL B O     1 
ATOM   7000  C  CB    . VAL B 1 175 ? 122.810 144.979 135.213 1.00 19.08 ? 175 VAL B CB    1 
ATOM   7001  C  CG1   . VAL B 1 175 ? 123.323 144.713 133.808 1.00 12.25 ? 175 VAL B CG1   1 
ATOM   7002  C  CG2   . VAL B 1 175 ? 123.781 144.446 136.255 1.00 18.56 ? 175 VAL B CG2   1 
ATOM   7003  N  N     . ASN B 1 176 ? 121.607 147.837 133.660 1.00 18.63 ? 176 ASN B N     1 
ATOM   7004  C  CA    . ASN B 1 176 ? 120.549 148.355 132.809 1.00 18.65 ? 176 ASN B CA    1 
ATOM   7005  C  C     . ASN B 1 176 ? 120.294 147.411 131.640 1.00 22.67 ? 176 ASN B C     1 
ATOM   7006  O  O     . ASN B 1 176 ? 121.141 146.598 131.264 1.00 26.31 ? 176 ASN B O     1 
ATOM   7007  C  CB    . ASN B 1 176 ? 120.906 149.748 132.294 1.00 18.85 ? 176 ASN B CB    1 
ATOM   7008  C  CG    . ASN B 1 176 ? 119.715 150.674 132.244 1.00 18.14 ? 176 ASN B CG    1 
ATOM   7009  O  OD1   . ASN B 1 176 ? 118.569 150.231 132.212 1.00 25.09 ? 176 ASN B OD1   1 
ATOM   7010  N  ND2   . ASN B 1 176 ? 119.979 151.974 132.235 1.00 19.60 ? 176 ASN B ND2   1 
ATOM   7011  N  N     . ASP B 1 177 ? 119.102 147.535 131.059 1.00 26.87 ? 177 ASP B N     1 
ATOM   7012  C  CA    . ASP B 1 177 ? 118.648 146.634 130.001 1.00 22.72 ? 177 ASP B CA    1 
ATOM   7013  C  C     . ASP B 1 177 ? 119.213 147.106 128.663 1.00 23.20 ? 177 ASP B C     1 
ATOM   7014  O  O     . ASP B 1 177 ? 118.533 147.724 127.840 1.00 28.37 ? 177 ASP B O     1 
ATOM   7015  C  CB    . ASP B 1 177 ? 117.128 146.567 129.981 1.00 20.53 ? 177 ASP B CB    1 
ATOM   7016  C  CG    . ASP B 1 177 ? 116.609 145.425 129.145 1.00 25.75 ? 177 ASP B CG    1 
ATOM   7017  O  OD1   . ASP B 1 177 ? 117.256 144.359 129.127 1.00 32.78 ? 177 ASP B OD1   1 
ATOM   7018  O  OD2   . ASP B 1 177 ? 115.549 145.592 128.509 1.00 30.27 ? 177 ASP B OD2   1 
ATOM   7019  N  N     . SER B 1 178 ? 120.487 146.794 128.445 1.00 18.86 ? 178 SER B N     1 
ATOM   7020  C  CA    . SER B 1 178 ? 121.175 147.141 127.209 1.00 17.72 ? 178 SER B CA    1 
ATOM   7021  C  C     . SER B 1 178 ? 122.467 146.342 127.138 1.00 20.48 ? 178 SER B C     1 
ATOM   7022  O  O     . SER B 1 178 ? 123.031 145.955 128.164 1.00 28.98 ? 178 SER B O     1 
ATOM   7023  C  CB    . SER B 1 178 ? 121.462 148.643 127.123 1.00 16.19 ? 178 SER B CB    1 
ATOM   7024  O  OG    . SER B 1 178 ? 122.711 148.959 127.704 1.00 25.21 ? 178 SER B OG    1 
ATOM   7025  N  N     . LEU B 1 179 ? 122.926 146.095 125.909 1.00 29.39 ? 179 LEU B N     1 
ATOM   7026  C  CA    . LEU B 1 179 ? 124.180 145.372 125.723 1.00 18.99 ? 179 LEU B CA    1 
ATOM   7027  C  C     . LEU B 1 179 ? 125.366 146.188 126.220 1.00 17.40 ? 179 LEU B C     1 
ATOM   7028  O  O     . LEU B 1 179 ? 126.314 145.632 126.784 1.00 25.18 ? 179 LEU B O     1 
ATOM   7029  C  CB    . LEU B 1 179 ? 124.364 144.999 124.253 1.00 22.26 ? 179 LEU B CB    1 
ATOM   7030  C  CG    . LEU B 1 179 ? 125.560 144.093 123.946 1.00 21.48 ? 179 LEU B CG    1 
ATOM   7031  C  CD1   . LEU B 1 179 ? 125.341 142.703 124.520 1.00 19.09 ? 179 LEU B CD1   1 
ATOM   7032  C  CD2   . LEU B 1 179 ? 125.816 144.024 122.452 1.00 21.60 ? 179 LEU B CD2   1 
ATOM   7033  N  N     . ASN B 1 180 ? 125.333 147.506 126.012 1.00 20.45 ? 180 ASN B N     1 
ATOM   7034  C  CA    . ASN B 1 180 ? 126.387 148.370 126.533 1.00 16.58 ? 180 ASN B CA    1 
ATOM   7035  C  C     . ASN B 1 180 ? 126.474 148.264 128.049 1.00 22.35 ? 180 ASN B C     1 
ATOM   7036  O  O     . ASN B 1 180 ? 127.562 148.101 128.615 1.00 27.95 ? 180 ASN B O     1 
ATOM   7037  C  CB    . ASN B 1 180 ? 126.125 149.817 126.115 1.00 23.89 ? 180 ASN B CB    1 
ATOM   7038  C  CG    . ASN B 1 180 ? 126.595 150.116 124.709 1.00 29.34 ? 180 ASN B CG    1 
ATOM   7039  O  OD1   . ASN B 1 180 ? 127.429 149.402 124.157 1.00 32.64 ? 180 ASN B OD1   1 
ATOM   7040  N  ND2   . ASN B 1 180 ? 126.059 151.177 124.119 1.00 27.64 ? 180 ASN B ND2   1 
ATOM   7041  N  N     . ASP B 1 181 ? 125.325 148.333 128.721 1.00 24.47 ? 181 ASP B N     1 
ATOM   7042  C  CA    . ASP B 1 181 ? 125.305 148.261 130.175 1.00 17.52 ? 181 ASP B CA    1 
ATOM   7043  C  C     . ASP B 1 181 ? 125.676 146.873 130.679 1.00 20.25 ? 181 ASP B C     1 
ATOM   7044  O  O     . ASP B 1 181 ? 126.327 146.754 131.718 1.00 28.82 ? 181 ASP B O     1 
ATOM   7045  C  CB    . ASP B 1 181 ? 123.930 148.675 130.692 1.00 27.28 ? 181 ASP B CB    1 
ATOM   7046  C  CG    . ASP B 1 181 ? 123.649 150.149 130.472 1.00 29.31 ? 181 ASP B CG    1 
ATOM   7047  O  OD1   . ASP B 1 181 ? 124.262 150.982 131.169 1.00 28.66 ? 181 ASP B OD1   1 
ATOM   7048  O  OD2   . ASP B 1 181 ? 122.816 150.475 129.602 1.00 25.59 ? 181 ASP B OD2   1 
ATOM   7049  N  N     . ILE B 1 182 ? 125.286 145.819 129.962 1.00 21.70 ? 182 ILE B N     1 
ATOM   7050  C  CA    . ILE B 1 182 ? 125.658 144.466 130.369 1.00 21.08 ? 182 ILE B CA    1 
ATOM   7051  C  C     . ILE B 1 182 ? 127.164 144.258 130.237 1.00 19.46 ? 182 ILE B C     1 
ATOM   7052  O  O     . ILE B 1 182 ? 127.806 143.677 131.123 1.00 23.23 ? 182 ILE B O     1 
ATOM   7053  C  CB    . ILE B 1 182 ? 124.861 143.432 129.554 1.00 20.99 ? 182 ILE B CB    1 
ATOM   7054  C  CG1   . ILE B 1 182 ? 123.431 143.338 130.085 1.00 21.44 ? 182 ILE B CG1   1 
ATOM   7055  C  CG2   . ILE B 1 182 ? 125.535 142.071 129.594 1.00 21.30 ? 182 ILE B CG2   1 
ATOM   7056  C  CD1   . ILE B 1 182 ? 122.481 142.644 129.151 1.00 21.17 ? 182 ILE B CD1   1 
ATOM   7057  N  N     . SER B 1 183 ? 127.751 144.725 129.134 1.00 23.49 ? 183 SER B N     1 
ATOM   7058  C  CA    . SER B 1 183 ? 129.197 144.625 128.968 1.00 19.39 ? 183 SER B CA    1 
ATOM   7059  C  C     . SER B 1 183 ? 129.930 145.434 130.029 1.00 20.64 ? 183 SER B C     1 
ATOM   7060  O  O     . SER B 1 183 ? 130.942 144.982 130.579 1.00 26.38 ? 183 SER B O     1 
ATOM   7061  C  CB    . SER B 1 183 ? 129.596 145.089 127.570 1.00 18.79 ? 183 SER B CB    1 
ATOM   7062  O  OG    . SER B 1 183 ? 129.090 146.382 127.299 1.00 31.36 ? 183 SER B OG    1 
ATOM   7063  N  N     . ARG B 1 184 ? 129.433 146.636 130.333 1.00 25.58 ? 184 ARG B N     1 
ATOM   7064  C  CA    . ARG B 1 184 ? 130.047 147.437 131.385 1.00 19.55 ? 184 ARG B CA    1 
ATOM   7065  C  C     . ARG B 1 184 ? 129.911 146.761 132.743 1.00 25.31 ? 184 ARG B C     1 
ATOM   7066  O  O     . ARG B 1 184 ? 130.820 146.838 133.572 1.00 29.89 ? 184 ARG B O     1 
ATOM   7067  C  CB    . ARG B 1 184 ? 129.428 148.832 131.415 1.00 19.16 ? 184 ARG B CB    1 
ATOM   7068  C  CG    . ARG B 1 184 ? 130.129 149.787 132.359 1.00 27.04 ? 184 ARG B CG    1 
ATOM   7069  C  CD    . ARG B 1 184 ? 131.629 149.772 132.155 1.00 25.80 ? 184 ARG B CD    1 
ATOM   7070  N  NE    . ARG B 1 184 ? 132.044 150.730 131.139 1.00 33.22 ? 184 ARG B NE    1 
ATOM   7071  C  CZ    . ARG B 1 184 ? 133.216 150.705 130.520 1.00 32.76 ? 184 ARG B CZ    1 
ATOM   7072  N  NH1   . ARG B 1 184 ? 134.119 149.775 130.787 1.00 25.70 ? 184 ARG B NH1   1 
ATOM   7073  N  NH2   . ARG B 1 184 ? 133.490 151.637 129.613 1.00 30.58 ? 184 ARG B NH2   1 
ATOM   7074  N  N     . ALA B 1 185 ? 128.776 146.107 132.994 1.00 28.93 ? 185 ALA B N     1 
ATOM   7075  C  CA    . ALA B 1 185 ? 128.598 145.377 134.243 1.00 12.28 ? 185 ALA B CA    1 
ATOM   7076  C  C     . ALA B 1 185 ? 129.590 144.231 134.354 1.00 15.16 ? 185 ALA B C     1 
ATOM   7077  O  O     . ALA B 1 185 ? 130.163 144.002 135.423 1.00 22.70 ? 185 ALA B O     1 
ATOM   7078  C  CB    . ALA B 1 185 ? 127.165 144.857 134.349 1.00 12.25 ? 185 ALA B CB    1 
ATOM   7079  N  N     . ILE B 1 186 ? 129.808 143.500 133.259 1.00 22.77 ? 186 ILE B N     1 
ATOM   7080  C  CA    . ILE B 1 186 ? 130.799 142.425 133.271 1.00 23.44 ? 186 ILE B CA    1 
ATOM   7081  C  C     . ILE B 1 186 ? 132.190 142.989 133.538 1.00 19.44 ? 186 ILE B C     1 
ATOM   7082  O  O     . ILE B 1 186 ? 132.957 142.445 134.345 1.00 25.70 ? 186 ILE B O     1 
ATOM   7083  C  CB    . ILE B 1 186 ? 130.748 141.638 131.948 1.00 27.22 ? 186 ILE B CB    1 
ATOM   7084  C  CG1   . ILE B 1 186 ? 129.557 140.680 131.943 1.00 22.07 ? 186 ILE B CG1   1 
ATOM   7085  C  CG2   . ILE B 1 186 ? 132.042 140.871 131.720 1.00 24.19 ? 186 ILE B CG2   1 
ATOM   7086  C  CD1   . ILE B 1 186 ? 128.907 140.533 130.592 1.00 27.23 ? 186 ILE B CD1   1 
ATOM   7087  N  N     . ASP B 1 187 ? 132.528 144.097 132.877 1.00 23.26 ? 187 ASP B N     1 
ATOM   7088  C  CA    . ASP B 1 187 ? 133.834 144.719 133.077 1.00 20.53 ? 187 ASP B CA    1 
ATOM   7089  C  C     . ASP B 1 187 ? 134.023 145.158 134.524 1.00 27.89 ? 187 ASP B C     1 
ATOM   7090  O  O     . ASP B 1 187 ? 135.060 144.885 135.137 1.00 32.08 ? 187 ASP B O     1 
ATOM   7091  C  CB    . ASP B 1 187 ? 133.992 145.907 132.130 1.00 19.59 ? 187 ASP B CB    1 
ATOM   7092  C  CG    . ASP B 1 187 ? 135.072 146.871 132.578 1.00 32.40 ? 187 ASP B CG    1 
ATOM   7093  O  OD1   . ASP B 1 187 ? 136.223 146.429 132.777 1.00 31.40 ? 187 ASP B OD1   1 
ATOM   7094  O  OD2   . ASP B 1 187 ? 134.769 148.072 132.733 1.00 38.13 ? 187 ASP B OD2   1 
ATOM   7095  N  N     . ILE B 1 188 ? 133.024 145.839 135.088 1.00 24.03 ? 188 ILE B N     1 
ATOM   7096  C  CA    . ILE B 1 188 ? 133.136 146.345 136.451 1.00 23.04 ? 188 ILE B CA    1 
ATOM   7097  C  C     . ILE B 1 188 ? 133.168 145.196 137.449 1.00 24.95 ? 188 ILE B C     1 
ATOM   7098  O  O     . ILE B 1 188 ? 133.878 145.255 138.458 1.00 27.55 ? 188 ILE B O     1 
ATOM   7099  C  CB    . ILE B 1 188 ? 131.991 147.329 136.750 1.00 26.18 ? 188 ILE B CB    1 
ATOM   7100  C  CG1   . ILE B 1 188 ? 132.111 148.574 135.875 1.00 24.64 ? 188 ILE B CG1   1 
ATOM   7101  C  CG2   . ILE B 1 188 ? 132.006 147.744 138.204 1.00 25.38 ? 188 ILE B CG2   1 
ATOM   7102  C  CD1   . ILE B 1 188 ? 130.943 149.516 136.011 1.00 21.69 ? 188 ILE B CD1   1 
ATOM   7103  N  N     . SER B 1 189 ? 132.402 144.135 137.189 1.00 19.31 ? 189 SER B N     1 
ATOM   7104  C  CA    . SER B 1 189 ? 132.445 142.964 138.055 1.00 15.05 ? 189 SER B CA    1 
ATOM   7105  C  C     . SER B 1 189 ? 133.831 142.339 138.060 1.00 21.57 ? 189 SER B C     1 
ATOM   7106  O  O     . SER B 1 189 ? 134.348 141.976 139.120 1.00 26.12 ? 189 SER B O     1 
ATOM   7107  C  CB    . SER B 1 189 ? 131.398 141.946 137.609 1.00 20.90 ? 189 SER B CB    1 
ATOM   7108  O  OG    . SER B 1 189 ? 130.107 142.525 137.587 1.00 28.23 ? 189 SER B OG    1 
ATOM   7109  N  N     . MET B 1 190 ? 134.453 142.211 136.884 1.00 29.03 ? 190 MET B N     1 
ATOM   7110  C  CA    . MET B 1 190 ? 135.807 141.668 136.835 1.00 22.65 ? 190 MET B CA    1 
ATOM   7111  C  C     . MET B 1 190 ? 136.804 142.593 137.523 1.00 18.61 ? 190 MET B C     1 
ATOM   7112  O  O     . MET B 1 190 ? 137.718 142.125 138.209 1.00 21.90 ? 190 MET B O     1 
ATOM   7113  C  CB    . MET B 1 190 ? 136.224 141.403 135.390 1.00 22.18 ? 190 MET B CB    1 
ATOM   7114  C  CG    . MET B 1 190 ? 135.423 140.306 134.720 1.00 25.57 ? 190 MET B CG    1 
ATOM   7115  S  SD    . MET B 1 190 ? 136.278 139.534 133.335 1.00 33.49 ? 190 MET B SD    1 
ATOM   7116  C  CE    . MET B 1 190 ? 136.285 140.878 132.158 1.00 25.19 ? 190 MET B CE    1 
ATOM   7117  N  N     . GLN B 1 191 ? 136.644 143.908 137.357 1.00 21.94 ? 191 GLN B N     1 
ATOM   7118  C  CA    . GLN B 1 191 ? 137.560 144.848 137.997 1.00 23.40 ? 191 GLN B CA    1 
ATOM   7119  C  C     . GLN B 1 191 ? 137.438 144.805 139.516 1.00 25.02 ? 191 GLN B C     1 
ATOM   7120  O  O     . GLN B 1 191 ? 138.445 144.895 140.227 1.00 29.97 ? 191 GLN B O     1 
ATOM   7121  C  CB    . GLN B 1 191 ? 137.311 146.266 137.483 1.00 23.67 ? 191 GLN B CB    1 
ATOM   7122  C  CG    . GLN B 1 191 ? 137.570 146.448 136.000 1.00 23.47 ? 191 GLN B CG    1 
ATOM   7123  C  CD    . GLN B 1 191 ? 139.043 146.450 135.649 1.00 26.31 ? 191 GLN B CD    1 
ATOM   7124  O  OE1   . GLN B 1 191 ? 139.906 146.448 136.526 1.00 28.50 ? 191 GLN B OE1   1 
ATOM   7125  N  NE2   . GLN B 1 191 ? 139.338 146.449 134.356 1.00 26.75 ? 191 GLN B NE2   1 
ATOM   7126  N  N     . LEU B 1 192 ? 136.215 144.681 140.032 1.00 25.35 ? 192 LEU B N     1 
ATOM   7127  C  CA    . LEU B 1 192 ? 136.019 144.655 141.477 1.00 19.38 ? 192 LEU B CA    1 
ATOM   7128  C  C     . LEU B 1 192 ? 136.411 143.309 142.073 1.00 25.01 ? 192 LEU B C     1 
ATOM   7129  O  O     . LEU B 1 192 ? 136.958 143.257 143.179 1.00 34.27 ? 192 LEU B O     1 
ATOM   7130  C  CB    . LEU B 1 192 ? 134.569 144.994 141.815 1.00 19.28 ? 192 LEU B CB    1 
ATOM   7131  C  CG    . LEU B 1 192 ? 134.122 146.418 141.478 1.00 20.35 ? 192 LEU B CG    1 
ATOM   7132  C  CD1   . LEU B 1 192 ? 132.616 146.544 141.597 1.00 19.44 ? 192 LEU B CD1   1 
ATOM   7133  C  CD2   . LEU B 1 192 ? 134.822 147.430 142.367 1.00 19.37 ? 192 LEU B CD2   1 
ATOM   7134  N  N     . SER B 1 193 ? 136.140 142.213 141.361 1.00 27.15 ? 193 SER B N     1 
ATOM   7135  C  CA    . SER B 1 193 ? 136.611 140.908 141.805 1.00 21.34 ? 193 SER B CA    1 
ATOM   7136  C  C     . SER B 1 193 ? 138.129 140.831 141.772 1.00 28.55 ? 193 SER B C     1 
ATOM   7137  O  O     . SER B 1 193 ? 138.734 140.133 142.591 1.00 35.91 ? 193 SER B O     1 
ATOM   7138  C  CB    . SER B 1 193 ? 135.996 139.810 140.938 1.00 26.38 ? 193 SER B CB    1 
ATOM   7139  O  OG    . SER B 1 193 ? 136.287 138.526 141.457 1.00 39.84 ? 193 SER B OG    1 
ATOM   7140  N  N     . LYS B 1 194 ? 138.758 141.540 140.833 1.00 33.61 ? 194 LYS B N     1 
ATOM   7141  C  CA    . LYS B 1 194 ? 140.213 141.634 140.812 1.00 31.77 ? 194 LYS B CA    1 
ATOM   7142  C  C     . LYS B 1 194 ? 140.736 142.276 142.090 1.00 34.78 ? 194 LYS B C     1 
ATOM   7143  O  O     . LYS B 1 194 ? 141.747 141.834 142.648 1.00 41.56 ? 194 LYS B O     1 
ATOM   7144  C  CB    . LYS B 1 194 ? 140.657 142.425 139.581 1.00 28.15 ? 194 LYS B CB    1 
ATOM   7145  C  CG    . LYS B 1 194 ? 142.068 142.968 139.653 1.00 35.94 ? 194 LYS B CG    1 
ATOM   7146  C  CD    . LYS B 1 194 ? 142.318 143.991 138.561 1.00 36.99 ? 194 LYS B CD    1 
ATOM   7147  C  CE    . LYS B 1 194 ? 143.806 144.217 138.348 1.00 35.83 ? 194 LYS B CE    1 
ATOM   7148  N  NZ    . LYS B 1 194 ? 144.065 145.220 137.280 1.00 36.52 ? 194 LYS B NZ    1 
ATOM   7149  N  N     . LEU B 1 195 ? 140.052 143.313 142.575 1.00 33.22 ? 195 LEU B N     1 
ATOM   7150  C  CA    . LEU B 1 195 ? 140.409 143.944 143.838 1.00 34.67 ? 195 LEU B CA    1 
ATOM   7151  C  C     . LEU B 1 195 ? 140.123 143.056 145.042 1.00 34.36 ? 195 LEU B C     1 
ATOM   7152  O  O     . LEU B 1 195 ? 140.540 143.398 146.153 1.00 40.23 ? 195 LEU B O     1 
ATOM   7153  C  CB    . LEU B 1 195 ? 139.663 145.269 143.991 1.00 36.73 ? 195 LEU B CB    1 
ATOM   7154  C  CG    . LEU B 1 195 ? 139.913 146.310 142.900 1.00 35.87 ? 195 LEU B CG    1 
ATOM   7155  C  CD1   . LEU B 1 195 ? 139.125 147.580 143.178 1.00 32.11 ? 195 LEU B CD1   1 
ATOM   7156  C  CD2   . LEU B 1 195 ? 141.397 146.606 142.775 1.00 33.52 ? 195 LEU B CD2   1 
ATOM   7157  N  N     . GLY B 1 196 ? 139.423 141.943 144.853 1.00 30.82 ? 196 GLY B N     1 
ATOM   7158  C  CA    . GLY B 1 196 ? 139.110 141.035 145.932 1.00 30.59 ? 196 GLY B CA    1 
ATOM   7159  C  C     . GLY B 1 196 ? 137.746 141.213 146.555 1.00 35.45 ? 196 GLY B C     1 
ATOM   7160  O  O     . GLY B 1 196 ? 137.473 140.592 147.588 1.00 36.92 ? 196 GLY B O     1 
ATOM   7161  N  N     . GLY B 1 197 ? 136.882 142.031 145.964 1.00 30.33 ? 197 GLY B N     1 
ATOM   7162  C  CA    . GLY B 1 197 ? 135.580 142.328 146.534 1.00 26.32 ? 197 GLY B CA    1 
ATOM   7163  C  C     . GLY B 1 197 ? 134.475 141.481 145.929 1.00 27.46 ? 197 GLY B C     1 
ATOM   7164  O  O     . GLY B 1 197 ? 134.482 141.191 144.733 1.00 30.77 ? 197 GLY B O     1 
ATOM   7165  N  N     . GLY B 1 198 ? 133.525 141.090 146.774 1.00 25.04 ? 198 GLY B N     1 
ATOM   7166  C  CA    . GLY B 1 198 ? 132.332 140.430 146.281 1.00 17.30 ? 198 GLY B CA    1 
ATOM   7167  C  C     . GLY B 1 198 ? 131.400 141.427 145.616 1.00 16.03 ? 198 GLY B C     1 
ATOM   7168  O  O     . GLY B 1 198 ? 131.197 142.540 146.101 1.00 22.55 ? 198 GLY B O     1 
ATOM   7169  N  N     . VAL B 1 199 ? 130.832 141.020 144.485 1.00 22.41 ? 199 VAL B N     1 
ATOM   7170  C  CA    . VAL B 1 199 ? 130.029 141.899 143.645 1.00 18.49 ? 199 VAL B CA    1 
ATOM   7171  C  C     . VAL B 1 199 ? 128.619 141.337 143.556 1.00 11.05 ? 199 VAL B C     1 
ATOM   7172  O  O     . VAL B 1 199 ? 128.434 140.153 143.256 1.00 18.21 ? 199 VAL B O     1 
ATOM   7173  C  CB    . VAL B 1 199 ? 130.642 142.055 142.242 1.00 14.59 ? 199 VAL B CB    1 
ATOM   7174  C  CG1   . VAL B 1 199 ? 129.900 143.118 141.455 1.00 17.90 ? 199 VAL B CG1   1 
ATOM   7175  C  CG2   . VAL B 1 199 ? 132.118 142.389 142.344 1.00 18.44 ? 199 VAL B CG2   1 
ATOM   7176  N  N     . SER B 1 200 ? 127.632 142.184 143.821 1.00 17.22 ? 200 SER B N     1 
ATOM   7177  C  CA    . SER B 1 200 ? 126.227 141.831 143.686 1.00 8.33  ? 200 SER B CA    1 
ATOM   7178  C  C     . SER B 1 200 ? 125.631 142.618 142.530 1.00 14.44 ? 200 SER B C     1 
ATOM   7179  O  O     . SER B 1 200 ? 125.847 143.829 142.423 1.00 22.15 ? 200 SER B O     1 
ATOM   7180  C  CB    . SER B 1 200 ? 125.460 142.116 144.977 1.00 12.86 ? 200 SER B CB    1 
ATOM   7181  O  OG    . SER B 1 200 ? 124.267 141.357 145.032 1.00 19.88 ? 200 SER B OG    1 
ATOM   7182  N  N     . LEU B 1 201 ? 124.890 141.932 141.667 1.00 19.33 ? 201 LEU B N     1 
ATOM   7183  C  CA    . LEU B 1 201 ? 124.325 142.533 140.470 1.00 9.74  ? 201 LEU B CA    1 
ATOM   7184  C  C     . LEU B 1 201 ? 122.811 142.401 140.496 1.00 12.81 ? 201 LEU B C     1 
ATOM   7185  O  O     . LEU B 1 201 ? 122.282 141.325 140.788 1.00 14.91 ? 201 LEU B O     1 
ATOM   7186  C  CB    . LEU B 1 201 ? 124.899 141.880 139.211 1.00 18.77 ? 201 LEU B CB    1 
ATOM   7187  C  CG    . LEU B 1 201 ? 126.416 142.010 139.072 1.00 19.37 ? 201 LEU B CG    1 
ATOM   7188  C  CD1   . LEU B 1 201 ? 127.098 140.676 139.328 1.00 21.97 ? 201 LEU B CD1   1 
ATOM   7189  C  CD2   . LEU B 1 201 ? 126.786 142.554 137.706 1.00 17.56 ? 201 LEU B CD2   1 
ATOM   7190  N  N     . ASN B 1 202 ? 122.123 143.500 140.204 1.00 16.34 ? 202 ASN B N     1 
ATOM   7191  C  CA    . ASN B 1 202 ? 120.671 143.507 140.083 1.00 8.30  ? 202 ASN B CA    1 
ATOM   7192  C  C     . ASN B 1 202 ? 120.312 143.216 138.631 1.00 19.45 ? 202 ASN B C     1 
ATOM   7193  O  O     . ASN B 1 202 ? 120.616 144.012 137.738 1.00 30.05 ? 202 ASN B O     1 
ATOM   7194  C  CB    . ASN B 1 202 ? 120.099 144.847 140.535 1.00 11.42 ? 202 ASN B CB    1 
ATOM   7195  C  CG    . ASN B 1 202 ? 118.618 144.777 140.834 1.00 14.78 ? 202 ASN B CG    1 
ATOM   7196  O  OD1   . ASN B 1 202 ? 118.079 143.708 141.115 1.00 21.09 ? 202 ASN B OD1   1 
ATOM   7197  N  ND2   . ASN B 1 202 ? 117.951 145.921 140.779 1.00 14.38 ? 202 ASN B ND2   1 
ATOM   7198  N  N     . LEU B 1 203 ? 119.668 142.077 138.395 1.00 13.06 ? 203 LEU B N     1 
ATOM   7199  C  CA    . LEU B 1 203 ? 119.296 141.655 137.054 1.00 10.85 ? 203 LEU B CA    1 
ATOM   7200  C  C     . LEU B 1 203 ? 117.822 141.884 136.752 1.00 13.05 ? 203 LEU B C     1 
ATOM   7201  O  O     . LEU B 1 203 ? 117.327 141.400 135.730 1.00 20.28 ? 203 LEU B O     1 
ATOM   7202  C  CB    . LEU B 1 203 ? 119.648 140.179 136.853 1.00 17.67 ? 203 LEU B CB    1 
ATOM   7203  C  CG    . LEU B 1 203 ? 121.115 139.785 137.042 1.00 18.20 ? 203 LEU B CG    1 
ATOM   7204  C  CD1   . LEU B 1 203 ? 121.381 138.427 136.420 1.00 16.04 ? 203 LEU B CD1   1 
ATOM   7205  C  CD2   . LEU B 1 203 ? 122.047 140.834 136.455 1.00 17.80 ? 203 LEU B CD2   1 
ATOM   7206  N  N     . SER B 1 204 ? 117.112 142.617 137.613 1.00 16.87 ? 204 SER B N     1 
ATOM   7207  C  CA    . SER B 1 204 ? 115.670 142.767 137.446 1.00 18.09 ? 204 SER B CA    1 
ATOM   7208  C  C     . SER B 1 204 ? 115.321 143.681 136.280 1.00 20.64 ? 204 SER B C     1 
ATOM   7209  O  O     . SER B 1 204 ? 114.247 143.538 135.686 1.00 26.49 ? 204 SER B O     1 
ATOM   7210  C  CB    . SER B 1 204 ? 115.047 143.295 138.736 1.00 13.81 ? 204 SER B CB    1 
ATOM   7211  O  OG    . SER B 1 204 ? 115.236 142.380 139.798 1.00 21.36 ? 204 SER B OG    1 
ATOM   7212  N  N     . LYS B 1 205 ? 116.197 144.626 135.944 1.00 17.46 ? 205 LYS B N     1 
ATOM   7213  C  CA    . LYS B 1 205 ? 115.936 145.515 134.821 1.00 17.30 ? 205 LYS B CA    1 
ATOM   7214  C  C     . LYS B 1 205 ? 116.131 144.835 133.475 1.00 21.19 ? 205 LYS B C     1 
ATOM   7215  O  O     . LYS B 1 205 ? 115.533 145.270 132.487 1.00 27.89 ? 205 LYS B O     1 
ATOM   7216  C  CB    . LYS B 1 205 ? 116.829 146.752 134.906 1.00 17.56 ? 205 LYS B CB    1 
ATOM   7217  C  CG    . LYS B 1 205 ? 116.469 147.679 136.043 1.00 15.41 ? 205 LYS B CG    1 
ATOM   7218  C  CD    . LYS B 1 205 ? 117.331 148.920 136.026 1.00 20.56 ? 205 LYS B CD    1 
ATOM   7219  C  CE    . LYS B 1 205 ? 116.815 149.952 137.006 1.00 24.56 ? 205 LYS B CE    1 
ATOM   7220  N  NZ    . LYS B 1 205 ? 116.945 149.499 138.414 1.00 18.27 ? 205 LYS B NZ    1 
ATOM   7221  N  N     . LEU B 1 206 ? 116.953 143.790 133.414 1.00 19.40 ? 206 LEU B N     1 
ATOM   7222  C  CA    . LEU B 1 206 ? 117.146 143.059 132.170 1.00 14.10 ? 206 LEU B CA    1 
ATOM   7223  C  C     . LEU B 1 206 ? 115.843 142.408 131.731 1.00 19.49 ? 206 LEU B C     1 
ATOM   7224  O  O     . LEU B 1 206 ? 115.148 141.778 132.533 1.00 23.94 ? 206 LEU B O     1 
ATOM   7225  C  CB    . LEU B 1 206 ? 118.231 141.999 132.346 1.00 20.00 ? 206 LEU B CB    1 
ATOM   7226  C  CG    . LEU B 1 206 ? 119.569 142.491 132.891 1.00 22.05 ? 206 LEU B CG    1 
ATOM   7227  C  CD1   . LEU B 1 206 ? 120.503 141.321 133.117 1.00 18.79 ? 206 LEU B CD1   1 
ATOM   7228  C  CD2   . LEU B 1 206 ? 120.185 143.500 131.943 1.00 24.78 ? 206 LEU B CD2   1 
ATOM   7229  N  N     . ARG B 1 207 ? 115.515 142.560 130.452 1.00 24.37 ? 207 ARG B N     1 
ATOM   7230  C  CA    . ARG B 1 207 ? 114.281 141.991 129.936 1.00 23.98 ? 207 ARG B CA    1 
ATOM   7231  C  C     . ARG B 1 207 ? 114.375 140.470 129.880 1.00 25.89 ? 207 ARG B C     1 
ATOM   7232  O  O     . ARG B 1 207 ? 115.453 139.893 129.720 1.00 27.97 ? 207 ARG B O     1 
ATOM   7233  C  CB    . ARG B 1 207 ? 113.957 142.565 128.557 1.00 23.17 ? 207 ARG B CB    1 
ATOM   7234  C  CG    . ARG B 1 207 ? 114.969 142.265 127.473 1.00 22.87 ? 207 ARG B CG    1 
ATOM   7235  C  CD    . ARG B 1 207 ? 114.664 143.080 126.227 1.00 22.48 ? 207 ARG B CD    1 
ATOM   7236  N  NE    . ARG B 1 207 ? 115.049 144.476 126.389 1.00 26.21 ? 207 ARG B NE    1 
ATOM   7237  C  CZ    . ARG B 1 207 ? 115.276 145.315 125.388 1.00 21.36 ? 207 ARG B CZ    1 
ATOM   7238  N  NH1   . ARG B 1 207 ? 115.124 144.944 124.128 1.00 26.61 ? 207 ARG B NH1   1 
ATOM   7239  N  NH2   . ARG B 1 207 ? 115.665 146.557 125.658 1.00 16.74 ? 207 ARG B NH2   1 
ATOM   7240  N  N     . ALA B 1 208 ? 113.222 139.824 130.023 1.00 29.74 ? 208 ALA B N     1 
ATOM   7241  C  CA    . ALA B 1 208 ? 113.168 138.380 130.167 1.00 29.00 ? 208 ALA B CA    1 
ATOM   7242  C  C     . ALA B 1 208 ? 113.494 137.681 128.848 1.00 31.96 ? 208 ALA B C     1 
ATOM   7243  O  O     . ALA B 1 208 ? 113.692 138.307 127.804 1.00 33.48 ? 208 ALA B O     1 
ATOM   7244  C  CB    . ALA B 1 208 ? 111.792 137.949 130.665 1.00 26.48 ? 208 ALA B CB    1 
ATOM   7245  N  N     . LYS B 1 209 ? 113.553 136.354 128.917 1.00 28.47 ? 209 LYS B N     1 
ATOM   7246  C  CA    . LYS B 1 209 ? 113.802 135.547 127.733 1.00 25.21 ? 209 LYS B CA    1 
ATOM   7247  C  C     . LYS B 1 209 ? 112.614 135.612 126.783 1.00 33.69 ? 209 LYS B C     1 
ATOM   7248  O  O     . LYS B 1 209 ? 111.456 135.606 127.207 1.00 34.82 ? 209 LYS B O     1 
ATOM   7249  C  CB    . LYS B 1 209 ? 114.078 134.098 128.130 1.00 28.74 ? 209 LYS B CB    1 
ATOM   7250  C  CG    . LYS B 1 209 ? 114.885 133.315 127.108 1.00 33.20 ? 209 LYS B CG    1 
ATOM   7251  C  CD    . LYS B 1 209 ? 114.841 131.819 127.380 1.00 31.95 ? 209 LYS B CD    1 
ATOM   7252  C  CE    . LYS B 1 209 ? 113.553 131.408 128.079 1.00 34.67 ? 209 LYS B CE    1 
ATOM   7253  N  NZ    . LYS B 1 209 ? 113.395 129.929 128.133 1.00 34.26 ? 209 LYS B NZ    1 
ATOM   7254  N  N     . GLY B 1 210 ? 112.908 135.664 125.488 1.00 36.83 ? 210 GLY B N     1 
ATOM   7255  C  CA    . GLY B 1 210 ? 111.860 135.775 124.496 1.00 33.78 ? 210 GLY B CA    1 
ATOM   7256  C  C     . GLY B 1 210 ? 111.277 137.159 124.344 1.00 36.80 ? 210 GLY B C     1 
ATOM   7257  O  O     . GLY B 1 210 ? 110.090 137.293 124.030 1.00 39.54 ? 210 GLY B O     1 
ATOM   7258  N  N     . GLU B 1 211 ? 112.072 138.198 124.568 1.00 37.52 ? 211 GLU B N     1 
ATOM   7259  C  CA    . GLU B 1 211 ? 111.645 139.574 124.373 1.00 33.69 ? 211 GLU B CA    1 
ATOM   7260  C  C     . GLU B 1 211 ? 112.264 140.137 123.100 1.00 37.82 ? 211 GLU B C     1 
ATOM   7261  O  O     . GLU B 1 211 ? 113.235 139.604 122.559 1.00 40.02 ? 211 GLU B O     1 
ATOM   7262  C  CB    . GLU B 1 211 ? 112.015 140.440 125.582 1.00 35.25 ? 211 GLU B CB    1 
ATOM   7263  C  CG    . GLU B 1 211 ? 111.159 140.174 126.803 1.00 35.52 ? 211 GLU B CG    1 
ATOM   7264  C  CD    . GLU B 1 211 ? 110.588 141.441 127.403 1.00 39.85 ? 211 GLU B CD    1 
ATOM   7265  O  OE1   . GLU B 1 211 ? 109.819 142.135 126.706 1.00 41.36 ? 211 GLU B OE1   1 
ATOM   7266  O  OE2   . GLU B 1 211 ? 110.894 141.738 128.575 1.00 39.08 ? 211 GLU B OE2   1 
ATOM   7267  N  N     . ALA B 1 212 ? 111.681 141.231 122.623 1.00 39.46 ? 212 ALA B N     1 
ATOM   7268  C  CA    . ALA B 1 212 ? 112.088 141.836 121.365 1.00 36.41 ? 212 ALA B CA    1 
ATOM   7269  C  C     . ALA B 1 212 ? 113.308 142.725 121.558 1.00 40.07 ? 212 ALA B C     1 
ATOM   7270  O  O     . ALA B 1 212 ? 113.420 143.443 122.555 1.00 41.75 ? 212 ALA B O     1 
ATOM   7271  C  CB    . ALA B 1 212 ? 110.941 142.651 120.766 1.00 39.41 ? 212 ALA B CB    1 
ATOM   7272  N  N     . ILE B 1 213 ? 114.222 142.671 120.593 1.00 39.16 ? 213 ILE B N     1 
ATOM   7273  C  CA    . ILE B 1 213 ? 115.377 143.560 120.538 1.00 40.18 ? 213 ILE B CA    1 
ATOM   7274  C  C     . ILE B 1 213 ? 115.216 144.400 119.278 1.00 40.07 ? 213 ILE B C     1 
ATOM   7275  O  O     . ILE B 1 213 ? 115.494 143.926 118.170 1.00 44.48 ? 213 ILE B O     1 
ATOM   7276  C  CB    . ILE B 1 213 ? 116.706 142.796 120.533 1.00 39.87 ? 213 ILE B CB    1 
ATOM   7277  C  CG1   . ILE B 1 213 ? 116.785 141.844 121.727 1.00 39.54 ? 213 ILE B CG1   1 
ATOM   7278  C  CG2   . ILE B 1 213 ? 117.876 143.764 120.555 1.00 36.97 ? 213 ILE B CG2   1 
ATOM   7279  C  CD1   . ILE B 1 213 ? 117.954 140.889 121.665 1.00 37.16 ? 213 ILE B CD1   1 
ATOM   7280  N  N     . LYS B 1 214 ? 114.760 145.646 119.448 1.00 45.60 ? 214 LYS B N     1 
ATOM   7281  C  CA    . LYS B 1 214 ? 114.537 146.617 118.375 1.00 46.35 ? 214 LYS B CA    1 
ATOM   7282  C  C     . LYS B 1 214 ? 113.859 145.993 117.158 1.00 49.36 ? 214 LYS B C     1 
ATOM   7283  O  O     . LYS B 1 214 ? 114.463 145.888 116.086 1.00 49.53 ? 214 LYS B O     1 
ATOM   7284  C  CB    . LYS B 1 214 ? 115.838 147.339 117.977 1.00 46.20 ? 214 LYS B CB    1 
ATOM   7285  C  CG    . LYS B 1 214 ? 117.065 146.491 117.674 1.00 47.60 ? 214 LYS B CG    1 
ATOM   7286  C  CD    . LYS B 1 214 ? 118.113 147.306 116.938 1.00 46.60 ? 214 LYS B CD    1 
ATOM   7287  C  CE    . LYS B 1 214 ? 119.449 146.590 116.905 1.00 47.57 ? 214 LYS B CE    1 
ATOM   7288  N  NZ    . LYS B 1 214 ? 120.585 147.551 116.944 1.00 48.57 ? 214 LYS B NZ    1 
ATOM   7289  N  N     . ASP B 1 215 ? 112.610 145.559 117.335 1.00 54.87 ? 215 ASP B N     1 
ATOM   7290  C  CA    . ASP B 1 215 ? 111.684 145.024 116.341 1.00 55.45 ? 215 ASP B CA    1 
ATOM   7291  C  C     . ASP B 1 215 ? 111.952 143.559 116.005 1.00 55.52 ? 215 ASP B C     1 
ATOM   7292  O  O     . ASP B 1 215 ? 111.222 142.992 115.191 1.00 57.05 ? 215 ASP B O     1 
ATOM   7293  C  CB    . ASP B 1 215 ? 111.661 145.834 115.028 1.00 55.00 ? 215 ASP B CB    1 
ATOM   7294  C  CG    . ASP B 1 215 ? 110.988 147.181 115.187 1.00 59.43 ? 215 ASP B CG    1 
ATOM   7295  O  OD1   . ASP B 1 215 ? 109.754 147.212 115.378 1.00 57.86 ? 215 ASP B OD1   1 
ATOM   7296  O  OD2   . ASP B 1 215 ? 111.693 148.210 115.118 1.00 57.37 ? 215 ASP B OD2   1 
ATOM   7297  N  N     . VAL B 1 216 ? 112.959 142.923 116.592 1.00 50.78 ? 216 VAL B N     1 
ATOM   7298  C  CA    . VAL B 1 216 ? 113.172 141.493 116.398 1.00 47.61 ? 216 VAL B CA    1 
ATOM   7299  C  C     . VAL B 1 216 ? 112.651 140.763 117.629 1.00 49.99 ? 216 VAL B C     1 
ATOM   7300  O  O     . VAL B 1 216 ? 113.335 140.690 118.656 1.00 52.91 ? 216 VAL B O     1 
ATOM   7301  C  CB    . VAL B 1 216 ? 114.653 141.180 116.147 1.00 48.58 ? 216 VAL B CB    1 
ATOM   7302  C  CG1   . VAL B 1 216 ? 114.867 139.680 116.012 1.00 48.25 ? 216 VAL B CG1   1 
ATOM   7303  C  CG2   . VAL B 1 216 ? 115.140 141.905 114.905 1.00 47.02 ? 216 VAL B CG2   1 
ATOM   7304  N  N     . GLU B 1 217 ? 111.442 140.223 117.529 1.00 50.92 ? 217 GLU B N     1 
ATOM   7305  C  CA    . GLU B 1 217 ? 110.768 139.607 118.661 1.00 51.16 ? 217 GLU B CA    1 
ATOM   7306  C  C     . GLU B 1 217 ? 111.416 138.278 119.030 1.00 47.58 ? 217 GLU B C     1 
ATOM   7307  O  O     . GLU B 1 217 ? 112.019 137.603 118.197 1.00 48.52 ? 217 GLU B O     1 
ATOM   7308  C  CB    . GLU B 1 217 ? 109.286 139.391 118.352 1.00 48.62 ? 217 GLU B CB    1 
ATOM   7309  C  CG    . GLU B 1 217 ? 108.709 140.388 117.369 1.00 50.65 ? 217 GLU B CG    1 
ATOM   7310  C  CD    . GLU B 1 217 ? 108.384 141.716 118.019 1.00 53.02 ? 217 GLU B CD    1 
ATOM   7311  O  OE1   . GLU B 1 217 ? 108.738 142.765 117.441 1.00 55.51 ? 217 GLU B OE1   1 
ATOM   7312  O  OE2   . GLU B 1 217 ? 107.777 141.711 119.110 1.00 51.66 ? 217 GLU B OE2   1 
ATOM   7313  N  N     . ASN B 1 218 ? 111.271 137.910 120.305 1.00 44.13 ? 218 ASN B N     1 
ATOM   7314  C  CA    . ASN B 1 218 ? 111.743 136.625 120.824 1.00 44.44 ? 218 ASN B CA    1 
ATOM   7315  C  C     . ASN B 1 218 ? 113.238 136.432 120.576 1.00 46.68 ? 218 ASN B C     1 
ATOM   7316  O  O     . ASN B 1 218 ? 113.691 135.356 120.182 1.00 47.95 ? 218 ASN B O     1 
ATOM   7317  C  CB    . ASN B 1 218 ? 110.938 135.469 120.226 1.00 43.59 ? 218 ASN B CB    1 
ATOM   7318  C  CG    . ASN B 1 218 ? 110.859 134.275 121.150 1.00 46.40 ? 218 ASN B CG    1 
ATOM   7319  O  OD1   . ASN B 1 218 ? 111.674 133.356 121.065 1.00 49.28 ? 218 ASN B OD1   1 
ATOM   7320  N  ND2   . ASN B 1 218 ? 109.873 134.277 122.038 1.00 47.26 ? 218 ASN B ND2   1 
ATOM   7321  N  N     . ALA B 1 219 ? 114.017 137.489 120.816 1.00 37.68 ? 219 ALA B N     1 
ATOM   7322  C  CA    . ALA B 1 219 ? 115.445 137.470 120.538 1.00 35.54 ? 219 ALA B CA    1 
ATOM   7323  C  C     . ALA B 1 219 ? 116.325 137.520 121.778 1.00 38.12 ? 219 ALA B C     1 
ATOM   7324  O  O     . ALA B 1 219 ? 117.533 137.295 121.664 1.00 37.43 ? 219 ALA B O     1 
ATOM   7325  C  CB    . ALA B 1 219 ? 115.823 138.643 119.622 1.00 35.75 ? 219 ALA B CB    1 
ATOM   7326  N  N     . THR B 1 220 ? 115.761 137.804 122.948 1.00 35.62 ? 220 THR B N     1 
ATOM   7327  C  CA    . THR B 1 220 ? 116.545 137.980 124.162 1.00 34.37 ? 220 THR B CA    1 
ATOM   7328  C  C     . THR B 1 220 ? 116.706 136.649 124.886 1.00 35.31 ? 220 THR B C     1 
ATOM   7329  O  O     . THR B 1 220 ? 115.735 135.904 125.053 1.00 34.05 ? 220 THR B O     1 
ATOM   7330  C  CB    . THR B 1 220 ? 115.881 139.007 125.082 1.00 30.29 ? 220 THR B CB    1 
ATOM   7331  O  OG1   . THR B 1 220 ? 115.724 140.246 124.381 1.00 33.74 ? 220 THR B OG1   1 
ATOM   7332  C  CG2   . THR B 1 220 ? 116.724 139.244 126.320 1.00 33.59 ? 220 THR B CG2   1 
ATOM   7333  N  N     . LYS B 1 221 ? 117.936 136.354 125.311 1.00 34.69 ? 221 LYS B N     1 
ATOM   7334  C  CA    . LYS B 1 221 ? 118.208 135.157 126.095 1.00 31.82 ? 221 LYS B CA    1 
ATOM   7335  C  C     . LYS B 1 221 ? 117.774 135.289 127.547 1.00 35.21 ? 221 LYS B C     1 
ATOM   7336  O  O     . LYS B 1 221 ? 117.810 134.296 128.280 1.00 38.14 ? 221 LYS B O     1 
ATOM   7337  C  CB    . LYS B 1 221 ? 119.698 134.813 126.048 1.00 32.39 ? 221 LYS B CB    1 
ATOM   7338  C  CG    . LYS B 1 221 ? 120.424 135.332 124.827 1.00 31.36 ? 221 LYS B CG    1 
ATOM   7339  C  CD    . LYS B 1 221 ? 121.758 134.633 124.660 1.00 35.20 ? 221 LYS B CD    1 
ATOM   7340  C  CE    . LYS B 1 221 ? 121.579 133.194 124.216 1.00 36.64 ? 221 LYS B CE    1 
ATOM   7341  N  NZ    . LYS B 1 221 ? 120.840 133.105 122.930 1.00 35.94 ? 221 LYS B NZ    1 
ATOM   7342  N  N     . GLY B 1 222 ? 117.375 136.478 127.975 1.00 33.72 ? 222 GLY B N     1 
ATOM   7343  C  CA    . GLY B 1 222 ? 116.922 136.679 129.332 1.00 32.83 ? 222 GLY B CA    1 
ATOM   7344  C  C     . GLY B 1 222 ? 118.063 136.925 130.297 1.00 30.91 ? 222 GLY B C     1 
ATOM   7345  O  O     . GLY B 1 222 ? 119.200 137.223 129.919 1.00 32.45 ? 222 GLY B O     1 
ATOM   7346  N  N     . VAL B 1 223 ? 117.738 136.798 131.586 1.00 28.14 ? 223 VAL B N     1 
ATOM   7347  C  CA    . VAL B 1 223 ? 118.731 137.021 132.632 1.00 29.98 ? 223 VAL B CA    1 
ATOM   7348  C  C     . VAL B 1 223 ? 119.706 135.866 132.776 1.00 22.11 ? 223 VAL B C     1 
ATOM   7349  O  O     . VAL B 1 223 ? 120.755 136.038 133.402 1.00 25.47 ? 223 VAL B O     1 
ATOM   7350  C  CB    . VAL B 1 223 ? 118.062 137.286 133.995 1.00 26.70 ? 223 VAL B CB    1 
ATOM   7351  C  CG1   . VAL B 1 223 ? 116.985 138.346 133.858 1.00 22.45 ? 223 VAL B CG1   1 
ATOM   7352  C  CG2   . VAL B 1 223 ? 117.486 136.001 134.571 1.00 26.33 ? 223 VAL B CG2   1 
ATOM   7353  N  N     . VAL B 1 224 ? 119.403 134.700 132.205 1.00 26.61 ? 224 VAL B N     1 
ATOM   7354  C  CA    . VAL B 1 224 ? 120.284 133.549 132.374 1.00 26.60 ? 224 VAL B CA    1 
ATOM   7355  C  C     . VAL B 1 224 ? 121.523 133.653 131.486 1.00 30.37 ? 224 VAL B C     1 
ATOM   7356  O  O     . VAL B 1 224 ? 122.605 133.200 131.873 1.00 33.95 ? 224 VAL B O     1 
ATOM   7357  C  CB    . VAL B 1 224 ? 119.510 132.247 132.115 1.00 31.23 ? 224 VAL B CB    1 
ATOM   7358  C  CG1   . VAL B 1 224 ? 120.379 131.040 132.417 1.00 29.48 ? 224 VAL B CG1   1 
ATOM   7359  C  CG2   . VAL B 1 224 ? 118.248 132.216 132.957 1.00 31.35 ? 224 VAL B CG2   1 
ATOM   7360  N  N     . GLY B 1 225 ? 121.404 134.244 130.296 1.00 22.22 ? 225 GLY B N     1 
ATOM   7361  C  CA    . GLY B 1 225 ? 122.593 134.496 129.497 1.00 20.33 ? 225 GLY B CA    1 
ATOM   7362  C  C     . GLY B 1 225 ? 123.546 135.460 130.177 1.00 22.59 ? 225 GLY B C     1 
ATOM   7363  O  O     . GLY B 1 225 ? 124.763 135.241 130.202 1.00 30.33 ? 225 GLY B O     1 
ATOM   7364  N  N     . VAL B 1 226 ? 123.003 136.536 130.750 1.00 19.10 ? 226 VAL B N     1 
ATOM   7365  C  CA    . VAL B 1 226 ? 123.815 137.457 131.536 1.00 22.26 ? 226 VAL B CA    1 
ATOM   7366  C  C     . VAL B 1 226 ? 124.377 136.755 132.763 1.00 19.76 ? 226 VAL B C     1 
ATOM   7367  O  O     . VAL B 1 226 ? 125.498 137.041 133.191 1.00 23.72 ? 226 VAL B O     1 
ATOM   7368  C  CB    . VAL B 1 226 ? 122.989 138.699 131.921 1.00 21.63 ? 226 VAL B CB    1 
ATOM   7369  C  CG1   . VAL B 1 226 ? 123.854 139.710 132.654 1.00 27.07 ? 226 VAL B CG1   1 
ATOM   7370  C  CG2   . VAL B 1 226 ? 122.370 139.319 130.684 1.00 24.18 ? 226 VAL B CG2   1 
ATOM   7371  N  N     . MET B 1 227 ? 123.613 135.831 133.345 1.00 22.11 ? 227 MET B N     1 
ATOM   7372  C  CA    . MET B 1 227 ? 124.102 135.060 134.483 1.00 23.92 ? 227 MET B CA    1 
ATOM   7373  C  C     . MET B 1 227 ? 125.315 134.222 134.103 1.00 26.21 ? 227 MET B C     1 
ATOM   7374  O  O     . MET B 1 227 ? 126.291 134.157 134.855 1.00 28.60 ? 227 MET B O     1 
ATOM   7375  C  CB    . MET B 1 227 ? 122.986 134.168 135.018 1.00 19.03 ? 227 MET B CB    1 
ATOM   7376  C  CG    . MET B 1 227 ? 122.058 134.843 136.001 1.00 20.52 ? 227 MET B CG    1 
ATOM   7377  S  SD    . MET B 1 227 ? 120.982 133.644 136.792 1.00 33.06 ? 227 MET B SD    1 
ATOM   7378  C  CE    . MET B 1 227 ? 122.030 133.119 138.133 1.00 28.58 ? 227 MET B CE    1 
ATOM   7379  N  N     . LYS B 1 228 ? 125.265 133.566 132.943 1.00 25.92 ? 228 LYS B N     1 
ATOM   7380  C  CA    . LYS B 1 228 ? 126.413 132.797 132.469 1.00 21.63 ? 228 LYS B CA    1 
ATOM   7381  C  C     . LYS B 1 228 ? 127.608 133.700 132.195 1.00 22.06 ? 228 LYS B C     1 
ATOM   7382  O  O     . LYS B 1 228 ? 128.750 133.360 132.537 1.00 26.78 ? 228 LYS B O     1 
ATOM   7383  C  CB    . LYS B 1 228 ? 126.042 132.019 131.209 1.00 24.16 ? 228 LYS B CB    1 
ATOM   7384  C  CG    . LYS B 1 228 ? 124.908 131.034 131.387 1.00 25.42 ? 228 LYS B CG    1 
ATOM   7385  C  CD    . LYS B 1 228 ? 124.896 130.025 130.256 1.00 32.20 ? 228 LYS B CD    1 
ATOM   7386  C  CE    . LYS B 1 228 ? 123.965 130.461 129.135 1.00 36.25 ? 228 LYS B CE    1 
ATOM   7387  N  NZ    . LYS B 1 228 ? 122.540 130.172 129.451 1.00 35.35 ? 228 LYS B NZ    1 
ATOM   7388  N  N     . LEU B 1 229 ? 127.363 134.854 131.567 1.00 23.10 ? 229 LEU B N     1 
ATOM   7389  C  CA    . LEU B 1 229 ? 128.442 135.803 131.314 1.00 21.72 ? 229 LEU B CA    1 
ATOM   7390  C  C     . LEU B 1 229 ? 129.099 136.241 132.615 1.00 24.21 ? 229 LEU B C     1 
ATOM   7391  O  O     . LEU B 1 229 ? 130.328 136.279 132.723 1.00 27.69 ? 229 LEU B O     1 
ATOM   7392  C  CB    . LEU B 1 229 ? 127.911 137.019 130.558 1.00 24.18 ? 229 LEU B CB    1 
ATOM   7393  C  CG    . LEU B 1 229 ? 127.672 136.914 129.056 1.00 21.02 ? 229 LEU B CG    1 
ATOM   7394  C  CD1   . LEU B 1 229 ? 126.803 138.072 128.609 1.00 24.06 ? 229 LEU B CD1   1 
ATOM   7395  C  CD2   . LEU B 1 229 ? 128.988 136.911 128.307 1.00 21.17 ? 229 LEU B CD2   1 
ATOM   7396  N  N     . LEU B 1 230 ? 128.286 136.563 133.623 1.00 26.53 ? 230 LEU B N     1 
ATOM   7397  C  CA    . LEU B 1 230 ? 128.817 137.014 134.903 1.00 21.56 ? 230 LEU B CA    1 
ATOM   7398  C  C     . LEU B 1 230 ? 129.532 135.888 135.636 1.00 17.36 ? 230 LEU B C     1 
ATOM   7399  O  O     . LEU B 1 230 ? 130.545 136.122 136.300 1.00 30.36 ? 230 LEU B O     1 
ATOM   7400  C  CB    . LEU B 1 230 ? 127.692 137.585 135.764 1.00 20.98 ? 230 LEU B CB    1 
ATOM   7401  C  CG    . LEU B 1 230 ? 127.076 138.895 135.277 1.00 24.24 ? 230 LEU B CG    1 
ATOM   7402  C  CD1   . LEU B 1 230 ? 125.845 139.237 136.097 1.00 28.01 ? 230 LEU B CD1   1 
ATOM   7403  C  CD2   . LEU B 1 230 ? 128.096 140.021 135.328 1.00 24.85 ? 230 LEU B CD2   1 
ATOM   7404  N  N     . ASP B 1 231 ? 129.016 134.662 135.538 1.00 24.26 ? 231 ASP B N     1 
ATOM   7405  C  CA    . ASP B 1 231 ? 129.677 133.532 136.178 1.00 26.74 ? 231 ASP B CA    1 
ATOM   7406  C  C     . ASP B 1 231 ? 131.060 133.303 135.587 1.00 28.96 ? 231 ASP B C     1 
ATOM   7407  O  O     . ASP B 1 231 ? 132.033 133.100 136.322 1.00 33.38 ? 231 ASP B O     1 
ATOM   7408  C  CB    . ASP B 1 231 ? 128.816 132.277 136.042 1.00 26.55 ? 231 ASP B CB    1 
ATOM   7409  C  CG    . ASP B 1 231 ? 129.353 131.113 136.848 1.00 39.19 ? 231 ASP B CG    1 
ATOM   7410  O  OD1   . ASP B 1 231 ? 129.185 131.118 138.084 1.00 42.43 ? 231 ASP B OD1   1 
ATOM   7411  O  OD2   . ASP B 1 231 ? 129.943 130.192 136.246 1.00 38.45 ? 231 ASP B OD2   1 
ATOM   7412  N  N     . ASN B 1 232 ? 131.173 133.354 134.259 1.00 28.91 ? 232 ASN B N     1 
ATOM   7413  C  CA    . ASN B 1 232 ? 132.487 133.213 133.637 1.00 28.91 ? 232 ASN B CA    1 
ATOM   7414  C  C     . ASN B 1 232 ? 133.383 134.409 133.936 1.00 24.80 ? 232 ASN B C     1 
ATOM   7415  O  O     . ASN B 1 232 ? 134.601 134.254 134.083 1.00 31.67 ? 232 ASN B O     1 
ATOM   7416  C  CB    . ASN B 1 232 ? 132.333 132.999 132.136 1.00 27.16 ? 232 ASN B CB    1 
ATOM   7417  C  CG    . ASN B 1 232 ? 132.283 131.535 131.772 1.00 31.16 ? 232 ASN B CG    1 
ATOM   7418  O  OD1   . ASN B 1 232 ? 133.070 130.735 132.274 1.00 35.95 ? 232 ASN B OD1   1 
ATOM   7419  N  ND2   . ASN B 1 232 ? 131.332 131.167 130.937 1.00 33.29 ? 232 ASN B ND2   1 
ATOM   7420  N  N     . ALA B 1 233 ? 132.805 135.606 134.033 1.00 20.91 ? 233 ALA B N     1 
ATOM   7421  C  CA    . ALA B 1 233 ? 133.594 136.781 134.384 1.00 18.26 ? 233 ALA B CA    1 
ATOM   7422  C  C     . ALA B 1 233 ? 134.172 136.658 135.788 1.00 26.20 ? 233 ALA B C     1 
ATOM   7423  O  O     . ALA B 1 233 ? 135.326 137.030 136.028 1.00 29.46 ? 233 ALA B O     1 
ATOM   7424  C  CB    . ALA B 1 233 ? 132.734 138.038 134.261 1.00 21.35 ? 233 ALA B CB    1 
ATOM   7425  N  N     . PHE B 1 234 ? 133.380 136.145 136.731 1.00 29.49 ? 234 PHE B N     1 
ATOM   7426  C  CA    . PHE B 1 234 ? 133.866 135.955 138.093 1.00 24.87 ? 234 PHE B CA    1 
ATOM   7427  C  C     . PHE B 1 234 ? 134.853 134.801 138.181 1.00 25.21 ? 234 PHE B C     1 
ATOM   7428  O  O     . PHE B 1 234 ? 135.787 134.849 138.988 1.00 28.18 ? 234 PHE B O     1 
ATOM   7429  C  CB    . PHE B 1 234 ? 132.693 135.725 139.044 1.00 23.54 ? 234 PHE B CB    1 
ATOM   7430  C  CG    . PHE B 1 234 ? 131.964 136.980 139.416 1.00 23.83 ? 234 PHE B CG    1 
ATOM   7431  C  CD1   . PHE B 1 234 ? 132.632 138.034 140.012 1.00 25.55 ? 234 PHE B CD1   1 
ATOM   7432  C  CD2   . PHE B 1 234 ? 130.610 137.109 139.169 1.00 24.39 ? 234 PHE B CD2   1 
ATOM   7433  C  CE1   . PHE B 1 234 ? 131.961 139.190 140.350 1.00 24.37 ? 234 PHE B CE1   1 
ATOM   7434  C  CE2   . PHE B 1 234 ? 129.939 138.263 139.503 1.00 24.49 ? 234 PHE B CE2   1 
ATOM   7435  C  CZ    . PHE B 1 234 ? 130.614 139.302 140.096 1.00 25.25 ? 234 PHE B CZ    1 
ATOM   7436  N  N     . ARG B 1 235 ? 134.660 133.756 137.373 1.00 30.56 ? 235 ARG B N     1 
ATOM   7437  C  CA    . ARG B 1 235 ? 135.633 132.670 137.330 1.00 26.74 ? 235 ARG B CA    1 
ATOM   7438  C  C     . ARG B 1 235 ? 136.970 133.148 136.780 1.00 32.12 ? 235 ARG B C     1 
ATOM   7439  O  O     . ARG B 1 235 ? 138.028 132.720 137.253 1.00 38.44 ? 235 ARG B O     1 
ATOM   7440  C  CB    . ARG B 1 235 ? 135.092 131.507 136.499 1.00 28.69 ? 235 ARG B CB    1 
ATOM   7441  C  CG    . ARG B 1 235 ? 134.334 130.477 137.317 1.00 37.15 ? 235 ARG B CG    1 
ATOM   7442  C  CD    . ARG B 1 235 ? 134.068 129.203 136.534 1.00 32.60 ? 235 ARG B CD    1 
ATOM   7443  N  NE    . ARG B 1 235 ? 132.723 129.177 135.974 1.00 36.53 ? 235 ARG B NE    1 
ATOM   7444  C  CZ    . ARG B 1 235 ? 132.454 129.081 134.680 1.00 38.76 ? 235 ARG B CZ    1 
ATOM   7445  N  NH1   . ARG B 1 235 ? 133.417 128.985 133.779 1.00 40.17 ? 235 ARG B NH1   1 
ATOM   7446  N  NH2   . ARG B 1 235 ? 131.186 129.084 134.278 1.00 34.66 ? 235 ARG B NH2   1 
ATOM   7447  N  N     . TYR B 1 236 ? 136.946 134.024 135.775 1.00 23.30 ? 236 TYR B N     1 
ATOM   7448  C  CA    . TYR B 1 236 ? 138.194 134.538 135.224 1.00 24.12 ? 236 TYR B CA    1 
ATOM   7449  C  C     . TYR B 1 236 ? 138.882 135.479 136.206 1.00 24.27 ? 236 TYR B C     1 
ATOM   7450  O  O     . TYR B 1 236 ? 140.087 135.361 136.455 1.00 25.29 ? 236 TYR B O     1 
ATOM   7451  C  CB    . TYR B 1 236 ? 137.935 135.248 133.898 1.00 23.80 ? 236 TYR B CB    1 
ATOM   7452  C  CG    . TYR B 1 236 ? 139.198 135.739 133.238 1.00 23.16 ? 236 TYR B CG    1 
ATOM   7453  C  CD1   . TYR B 1 236 ? 140.072 134.848 132.636 1.00 20.24 ? 236 TYR B CD1   1 
ATOM   7454  C  CD2   . TYR B 1 236 ? 139.525 137.088 133.227 1.00 19.57 ? 236 TYR B CD2   1 
ATOM   7455  C  CE1   . TYR B 1 236 ? 141.227 135.282 132.036 1.00 22.35 ? 236 TYR B CE1   1 
ATOM   7456  C  CE2   . TYR B 1 236 ? 140.683 137.533 132.625 1.00 15.40 ? 236 TYR B CE2   1 
ATOM   7457  C  CZ    . TYR B 1 236 ? 141.529 136.622 132.032 1.00 21.65 ? 236 TYR B CZ    1 
ATOM   7458  O  OH    . TYR B 1 236 ? 142.684 137.046 131.429 1.00 28.30 ? 236 TYR B OH    1 
ATOM   7459  N  N     . ALA B 1 237 ? 138.130 136.423 136.773 1.00 30.44 ? 237 ALA B N     1 
ATOM   7460  C  CA    . ALA B 1 237 ? 138.672 137.374 137.742 1.00 29.93 ? 237 ALA B CA    1 
ATOM   7461  C  C     . ALA B 1 237 ? 138.695 136.714 139.120 1.00 36.55 ? 237 ALA B C     1 
ATOM   7462  O  O     . ALA B 1 237 ? 137.923 137.035 140.026 1.00 36.12 ? 237 ALA B O     1 
ATOM   7463  C  CB    . ALA B 1 237 ? 137.861 138.661 137.744 1.00 30.63 ? 237 ALA B CB    1 
ATOM   7464  N  N     . ASP B 1 238 ? 139.618 135.763 139.265 1.00 51.96 ? 238 ASP B N     1 
ATOM   7465  C  CA    . ASP B 1 238 ? 139.707 134.924 140.453 1.00 51.85 ? 238 ASP B CA    1 
ATOM   7466  C  C     . ASP B 1 238 ? 140.710 135.451 141.471 1.00 55.86 ? 238 ASP B C     1 
ATOM   7467  O  O     . ASP B 1 238 ? 141.333 134.654 142.186 1.00 57.60 ? 238 ASP B O     1 
ATOM   7468  C  CB    . ASP B 1 238 ? 140.060 133.491 140.055 1.00 50.78 ? 238 ASP B CB    1 
ATOM   7469  C  CG    . ASP B 1 238 ? 138.906 132.533 140.258 1.00 54.55 ? 238 ASP B CG    1 
ATOM   7470  O  OD1   . ASP B 1 238 ? 138.899 131.464 139.612 1.00 53.78 ? 238 ASP B OD1   1 
ATOM   7471  O  OD2   . ASP B 1 238 ? 137.996 132.859 141.047 1.00 53.37 ? 238 ASP B OD2   1 
ATOM   7472  N  N     . GLN B 1 239 ? 140.890 136.771 141.542 1.00 64.71 ? 239 GLN B N     1 
ATOM   7473  C  CA    . GLN B 1 239 ? 141.780 137.404 142.517 1.00 65.88 ? 239 GLN B CA    1 
ATOM   7474  C  C     . GLN B 1 239 ? 143.207 136.869 142.397 1.00 67.13 ? 239 GLN B C     1 
ATOM   7475  O  O     . GLN B 1 239 ? 143.810 136.418 143.373 1.00 64.92 ? 239 GLN B O     1 
ATOM   7476  C  CB    . GLN B 1 239 ? 141.247 137.227 143.941 1.00 64.69 ? 239 GLN B CB    1 
ATOM   7477  C  CG    . GLN B 1 239 ? 139.801 137.649 144.116 1.00 64.11 ? 239 GLN B CG    1 
ATOM   7478  C  CD    . GLN B 1 239 ? 139.248 137.281 145.476 1.00 66.38 ? 239 GLN B CD    1 
ATOM   7479  O  OE1   . GLN B 1 239 ? 138.055 137.021 145.624 1.00 65.19 ? 239 GLN B OE1   1 
ATOM   7480  N  NE2   . GLN B 1 239 ? 140.116 137.260 146.481 1.00 66.14 ? 239 GLN B NE2   1 
ATOM   7481  N  N     . MET B 1 240 ? 143.741 136.916 141.175 1.00 68.97 ? 240 MET B N     1 
ATOM   7482  C  CA    . MET B 1 240 ? 145.100 136.462 140.878 1.00 68.20 ? 240 MET B CA    1 
ATOM   7483  C  C     . MET B 1 240 ? 145.318 135.007 141.286 1.00 69.25 ? 240 MET B C     1 
ATOM   7484  O  O     . MET B 1 240 ? 146.408 134.631 141.726 1.00 69.11 ? 240 MET B O     1 
ATOM   7485  C  CB    . MET B 1 240 ? 146.145 137.362 141.545 1.00 68.80 ? 240 MET B CB    1 
ATOM   7486  C  CG    . MET B 1 240 ? 146.232 138.763 140.966 1.00 69.62 ? 240 MET B CG    1 
ATOM   7487  S  SD    . MET B 1 240 ? 144.632 139.472 140.542 1.00 75.09 ? 240 MET B SD    1 
ATOM   7488  C  CE    . MET B 1 240 ? 145.084 141.194 140.363 1.00 67.48 ? 240 MET B CE    1 
ATOM   7489  N  N     . GLY B 1 241 ? 144.286 134.178 141.146 1.00 72.10 ? 241 GLY B N     1 
ATOM   7490  C  CA    . GLY B 1 241 ? 144.399 132.780 141.507 1.00 71.25 ? 241 GLY B CA    1 
ATOM   7491  C  C     . GLY B 1 241 ? 144.549 132.506 142.984 1.00 73.22 ? 241 GLY B C     1 
ATOM   7492  O  O     . GLY B 1 241 ? 144.976 131.408 143.354 1.00 73.27 ? 241 GLY B O     1 
ATOM   7493  N  N     . GLN B 1 242 ? 144.215 133.468 143.844 1.00 74.70 ? 242 GLN B N     1 
ATOM   7494  C  CA    . GLN B 1 242 ? 144.353 133.295 145.287 1.00 74.42 ? 242 GLN B CA    1 
ATOM   7495  C  C     . GLN B 1 242 ? 143.060 132.780 145.913 1.00 74.96 ? 242 GLN B C     1 
ATOM   7496  O  O     . GLN B 1 242 ? 143.043 131.712 146.533 1.00 73.99 ? 242 GLN B O     1 
ATOM   7497  C  CB    . GLN B 1 242 ? 144.773 134.619 145.936 1.00 73.22 ? 242 GLN B CB    1 
ATOM   7498  C  CG    . GLN B 1 242 ? 146.159 135.102 145.534 1.00 74.87 ? 242 GLN B CG    1 
ATOM   7499  C  CD    . GLN B 1 242 ? 146.714 136.141 146.490 1.00 76.14 ? 242 GLN B CD    1 
ATOM   7500  O  OE1   . GLN B 1 242 ? 146.146 136.391 147.553 1.00 76.27 ? 242 GLN B OE1   1 
ATOM   7501  N  NE2   . GLN B 1 242 ? 147.832 136.752 146.115 1.00 73.67 ? 242 GLN B NE2   1 
ATOM   7502  N  N     . ARG B 1 243 ? 141.973 133.529 145.754 1.00 69.14 ? 243 ARG B N     1 
ATOM   7503  C  CA    . ARG B 1 243 ? 140.673 133.171 146.301 1.00 67.91 ? 243 ARG B CA    1 
ATOM   7504  C  C     . ARG B 1 243 ? 139.640 133.222 145.187 1.00 67.28 ? 243 ARG B C     1 
ATOM   7505  O  O     . ARG B 1 243 ? 139.659 134.133 144.355 1.00 66.72 ? 243 ARG B O     1 
ATOM   7506  C  CB    . ARG B 1 243 ? 140.281 134.112 147.448 1.00 67.40 ? 243 ARG B CB    1 
ATOM   7507  C  CG    . ARG B 1 243 ? 138.914 133.848 148.056 1.00 68.21 ? 243 ARG B CG    1 
ATOM   7508  C  CD    . ARG B 1 243 ? 138.427 135.061 148.835 1.00 68.47 ? 243 ARG B CD    1 
ATOM   7509  N  NE    . ARG B 1 243 ? 137.720 136.015 147.988 1.00 69.47 ? 243 ARG B NE    1 
ATOM   7510  C  CZ    . ARG B 1 243 ? 136.555 136.569 148.295 1.00 69.34 ? 243 ARG B CZ    1 
ATOM   7511  N  NH1   . ARG B 1 243 ? 135.935 136.292 149.430 1.00 67.75 ? 243 ARG B NH1   1 
ATOM   7512  N  NH2   . ARG B 1 243 ? 136.001 137.427 147.443 1.00 65.49 ? 243 ARG B NH2   1 
ATOM   7513  N  N     . GLN B 1 244 ? 138.744 132.237 145.175 1.00 64.12 ? 244 GLN B N     1 
ATOM   7514  C  CA    . GLN B 1 244 ? 137.775 132.113 144.094 1.00 63.68 ? 244 GLN B CA    1 
ATOM   7515  C  C     . GLN B 1 244 ? 136.877 133.343 144.023 1.00 63.93 ? 244 GLN B C     1 
ATOM   7516  O  O     . GLN B 1 244 ? 136.384 133.829 145.045 1.00 62.27 ? 244 GLN B O     1 
ATOM   7517  C  CB    . GLN B 1 244 ? 136.933 130.852 144.285 1.00 62.20 ? 244 GLN B CB    1 
ATOM   7518  C  CG    . GLN B 1 244 ? 137.740 129.563 144.279 1.00 62.76 ? 244 GLN B CG    1 
ATOM   7519  C  CD    . GLN B 1 244 ? 136.864 128.326 144.296 1.00 62.73 ? 244 GLN B CD    1 
ATOM   7520  O  OE1   . GLN B 1 244 ? 135.841 128.284 144.979 1.00 61.97 ? 244 GLN B OE1   1 
ATOM   7521  N  NE2   . GLN B 1 244 ? 137.263 127.309 143.541 1.00 60.87 ? 244 GLN B NE2   1 
ATOM   7522  N  N     . GLY B 1 245 ? 136.673 133.846 142.806 1.00 48.17 ? 245 GLY B N     1 
ATOM   7523  C  CA    . GLY B 1 245 ? 135.826 135.003 142.588 1.00 44.68 ? 245 GLY B CA    1 
ATOM   7524  C  C     . GLY B 1 245 ? 134.377 134.745 142.940 1.00 44.66 ? 245 GLY B C     1 
ATOM   7525  O  O     . GLY B 1 245 ? 133.748 133.837 142.390 1.00 41.96 ? 245 GLY B O     1 
ATOM   7526  N  N     . SER B 1 246 ? 133.834 135.544 143.852 1.00 38.16 ? 246 SER B N     1 
ATOM   7527  C  CA    . SER B 1 246 ? 132.482 135.361 144.359 1.00 33.06 ? 246 SER B CA    1 
ATOM   7528  C  C     . SER B 1 246 ? 131.606 136.521 143.910 1.00 29.91 ? 246 SER B C     1 
ATOM   7529  O  O     . SER B 1 246 ? 131.968 137.688 144.093 1.00 24.70 ? 246 SER B O     1 
ATOM   7530  C  CB    . SER B 1 246 ? 132.480 135.255 145.885 1.00 32.69 ? 246 SER B CB    1 
ATOM   7531  O  OG    . SER B 1 246 ? 133.153 136.355 146.472 1.00 37.75 ? 246 SER B OG    1 
ATOM   7532  N  N     . GLY B 1 247 ? 130.458 136.194 143.324 1.00 26.58 ? 247 GLY B N     1 
ATOM   7533  C  CA    . GLY B 1 247 ? 129.511 137.203 142.908 1.00 12.75 ? 247 GLY B CA    1 
ATOM   7534  C  C     . GLY B 1 247 ? 128.097 136.748 143.196 1.00 13.82 ? 247 GLY B C     1 
ATOM   7535  O  O     . GLY B 1 247 ? 127.828 135.563 143.397 1.00 22.85 ? 247 GLY B O     1 
ATOM   7536  N  N     . ALA B 1 248 ? 127.191 137.719 143.215 1.00 18.00 ? 248 ALA B N     1 
ATOM   7537  C  CA    . ALA B 1 248 ? 125.787 137.462 143.484 1.00 17.58 ? 248 ALA B CA    1 
ATOM   7538  C  C     . ALA B 1 248 ? 124.931 138.138 142.426 1.00 16.32 ? 248 ALA B C     1 
ATOM   7539  O  O     . ALA B 1 248 ? 125.275 139.203 141.910 1.00 20.93 ? 248 ALA B O     1 
ATOM   7540  C  CB    . ALA B 1 248 ? 125.377 137.952 144.879 1.00 7.82  ? 248 ALA B CB    1 
ATOM   7541  N  N     . ALA B 1 249 ? 123.813 137.498 142.102 1.00 16.35 ? 249 ALA B N     1 
ATOM   7542  C  CA    . ALA B 1 249 ? 122.831 138.040 141.177 1.00 14.89 ? 249 ALA B CA    1 
ATOM   7543  C  C     . ALA B 1 249 ? 121.483 138.089 141.875 1.00 16.50 ? 249 ALA B C     1 
ATOM   7544  O  O     . ALA B 1 249 ? 121.084 137.123 142.532 1.00 22.75 ? 249 ALA B O     1 
ATOM   7545  C  CB    . ALA B 1 249 ? 122.743 137.199 139.902 1.00 13.18 ? 249 ALA B CB    1 
ATOM   7546  N  N     . TYR B 1 250 ? 120.788 139.211 141.741 1.00 17.07 ? 250 TYR B N     1 
ATOM   7547  C  CA    . TYR B 1 250 ? 119.489 139.396 142.365 1.00 8.22  ? 250 TYR B CA    1 
ATOM   7548  C  C     . TYR B 1 250 ? 118.432 139.606 141.295 1.00 9.54  ? 250 TYR B C     1 
ATOM   7549  O  O     . TYR B 1 250 ? 118.650 140.340 140.327 1.00 20.18 ? 250 TYR B O     1 
ATOM   7550  C  CB    . TYR B 1 250 ? 119.499 140.580 143.332 1.00 12.83 ? 250 TYR B CB    1 
ATOM   7551  C  CG    . TYR B 1 250 ? 119.979 140.225 144.718 1.00 16.21 ? 250 TYR B CG    1 
ATOM   7552  C  CD1   . TYR B 1 250 ? 121.322 139.981 144.967 1.00 9.14  ? 250 TYR B CD1   1 
ATOM   7553  C  CD2   . TYR B 1 250 ? 119.087 140.121 145.776 1.00 13.50 ? 250 TYR B CD2   1 
ATOM   7554  C  CE1   . TYR B 1 250 ? 121.764 139.651 146.229 1.00 3.41  ? 250 TYR B CE1   1 
ATOM   7555  C  CE2   . TYR B 1 250 ? 119.522 139.790 147.043 1.00 9.69  ? 250 TYR B CE2   1 
ATOM   7556  C  CZ    . TYR B 1 250 ? 120.861 139.557 147.263 1.00 11.32 ? 250 TYR B CZ    1 
ATOM   7557  O  OH    . TYR B 1 250 ? 121.302 139.230 148.523 1.00 19.93 ? 250 TYR B OH    1 
ATOM   7558  N  N     . LEU B 1 251 ? 117.290 138.951 141.473 1.00 15.09 ? 251 LEU B N     1 
ATOM   7559  C  CA    . LEU B 1 251 ? 116.163 139.097 140.567 1.00 16.22 ? 251 LEU B CA    1 
ATOM   7560  C  C     . LEU B 1 251 ? 114.889 139.253 141.376 1.00 11.77 ? 251 LEU B C     1 
ATOM   7561  O  O     . LEU B 1 251 ? 114.703 138.574 142.389 1.00 17.74 ? 251 LEU B O     1 
ATOM   7562  C  CB    . LEU B 1 251 ? 116.039 137.896 139.625 1.00 14.00 ? 251 LEU B CB    1 
ATOM   7563  C  CG    . LEU B 1 251 ? 115.208 138.125 138.364 1.00 15.05 ? 251 LEU B CG    1 
ATOM   7564  C  CD1   . LEU B 1 251 ? 115.939 139.031 137.397 1.00 8.89  ? 251 LEU B CD1   1 
ATOM   7565  C  CD2   . LEU B 1 251 ? 114.860 136.807 137.706 1.00 12.21 ? 251 LEU B CD2   1 
ATOM   7566  N  N     . ASN B 1 252 ? 114.017 140.150 140.927 1.00 13.42 ? 252 ASN B N     1 
ATOM   7567  C  CA    . ASN B 1 252 ? 112.710 140.293 141.548 1.00 12.09 ? 252 ASN B CA    1 
ATOM   7568  C  C     . ASN B 1 252 ? 111.870 139.048 141.298 1.00 17.35 ? 252 ASN B C     1 
ATOM   7569  O  O     . ASN B 1 252 ? 111.950 138.428 140.234 1.00 25.53 ? 252 ASN B O     1 
ATOM   7570  C  CB    . ASN B 1 252 ? 111.997 141.530 141.006 1.00 14.83 ? 252 ASN B CB    1 
ATOM   7571  C  CG    . ASN B 1 252 ? 111.022 142.121 142.001 1.00 20.57 ? 252 ASN B CG    1 
ATOM   7572  O  OD1   . ASN B 1 252 ? 109.959 141.557 142.254 1.00 29.70 ? 252 ASN B OD1   1 
ATOM   7573  N  ND2   . ASN B 1 252 ? 111.379 143.263 142.571 1.00 16.18 ? 252 ASN B ND2   1 
ATOM   7574  N  N     . ILE B 1 253 ? 111.063 138.675 142.293 1.00 13.79 ? 253 ILE B N     1 
ATOM   7575  C  CA    . ILE B 1 253 ? 110.224 137.493 142.157 1.00 17.26 ? 253 ILE B CA    1 
ATOM   7576  C  C     . ILE B 1 253 ? 109.143 137.683 141.101 1.00 22.87 ? 253 ILE B C     1 
ATOM   7577  O  O     . ILE B 1 253 ? 108.614 136.696 140.577 1.00 24.22 ? 253 ILE B O     1 
ATOM   7578  C  CB    . ILE B 1 253 ? 109.612 137.117 143.520 1.00 19.75 ? 253 ILE B CB    1 
ATOM   7579  C  CG1   . ILE B 1 253 ? 109.199 135.644 143.530 1.00 16.60 ? 253 ILE B CG1   1 
ATOM   7580  C  CG2   . ILE B 1 253 ? 108.442 138.028 143.859 1.00 15.10 ? 253 ILE B CG2   1 
ATOM   7581  C  CD1   . ILE B 1 253 ? 109.323 134.989 144.877 1.00 18.36 ? 253 ILE B CD1   1 
ATOM   7582  N  N     . PHE B 1 254 ? 108.806 138.924 140.762 1.00 28.65 ? 254 PHE B N     1 
ATOM   7583  C  CA    . PHE B 1 254 ? 107.829 139.205 139.720 1.00 19.52 ? 254 PHE B CA    1 
ATOM   7584  C  C     . PHE B 1 254 ? 108.460 139.309 138.339 1.00 22.34 ? 254 PHE B C     1 
ATOM   7585  O  O     . PHE B 1 254 ? 107.742 139.535 137.360 1.00 26.77 ? 254 PHE B O     1 
ATOM   7586  C  CB    . PHE B 1 254 ? 107.064 140.489 140.047 1.00 22.62 ? 254 PHE B CB    1 
ATOM   7587  C  CG    . PHE B 1 254 ? 105.987 140.301 141.075 1.00 25.67 ? 254 PHE B CG    1 
ATOM   7588  C  CD1   . PHE B 1 254 ? 104.888 139.508 140.804 1.00 25.37 ? 254 PHE B CD1   1 
ATOM   7589  C  CD2   . PHE B 1 254 ? 106.081 140.904 142.316 1.00 25.12 ? 254 PHE B CD2   1 
ATOM   7590  C  CE1   . PHE B 1 254 ? 103.897 139.329 141.746 1.00 27.60 ? 254 PHE B CE1   1 
ATOM   7591  C  CE2   . PHE B 1 254 ? 105.093 140.727 143.262 1.00 26.13 ? 254 PHE B CE2   1 
ATOM   7592  C  CZ    . PHE B 1 254 ? 104.000 139.939 142.976 1.00 24.66 ? 254 PHE B CZ    1 
ATOM   7593  N  N     . HIS B 1 255 ? 109.776 139.156 138.240 1.00 27.24 ? 255 HIS B N     1 
ATOM   7594  C  CA    . HIS B 1 255 ? 110.428 139.053 136.945 1.00 21.06 ? 255 HIS B CA    1 
ATOM   7595  C  C     . HIS B 1 255 ? 110.006 137.761 136.258 1.00 23.38 ? 255 HIS B C     1 
ATOM   7596  O  O     . HIS B 1 255 ? 109.836 136.724 136.903 1.00 28.93 ? 255 HIS B O     1 
ATOM   7597  C  CB    . HIS B 1 255 ? 111.945 139.092 137.117 1.00 18.17 ? 255 HIS B CB    1 
ATOM   7598  C  CG    . HIS B 1 255 ? 112.696 139.422 135.865 1.00 21.41 ? 255 HIS B CG    1 
ATOM   7599  N  ND1   . HIS B 1 255 ? 112.882 138.513 134.846 1.00 16.91 ? 255 HIS B ND1   1 
ATOM   7600  C  CD2   . HIS B 1 255 ? 113.334 140.552 135.481 1.00 20.23 ? 255 HIS B CD2   1 
ATOM   7601  C  CE1   . HIS B 1 255 ? 113.587 139.075 133.881 1.00 16.21 ? 255 HIS B CE1   1 
ATOM   7602  N  NE2   . HIS B 1 255 ? 113.877 140.311 134.243 1.00 15.29 ? 255 HIS B NE2   1 
ATOM   7603  N  N     . ARG B 1 256 ? 109.836 137.830 134.938 1.00 26.29 ? 256 ARG B N     1 
ATOM   7604  C  CA    . ARG B 1 256 ? 109.360 136.671 134.191 1.00 23.23 ? 256 ARG B CA    1 
ATOM   7605  C  C     . ARG B 1 256 ? 110.354 135.519 134.255 1.00 25.16 ? 256 ARG B C     1 
ATOM   7606  O  O     . ARG B 1 256 ? 109.959 134.348 134.292 1.00 31.49 ? 256 ARG B O     1 
ATOM   7607  C  CB    . ARG B 1 256 ? 109.086 137.068 132.743 1.00 26.94 ? 256 ARG B CB    1 
ATOM   7608  C  CG    . ARG B 1 256 ? 107.890 136.383 132.130 1.00 34.93 ? 256 ARG B CG    1 
ATOM   7609  C  CD    . ARG B 1 256 ? 108.238 134.988 131.659 1.00 31.39 ? 256 ARG B CD    1 
ATOM   7610  N  NE    . ARG B 1 256 ? 109.607 134.890 131.173 1.00 29.68 ? 256 ARG B NE    1 
ATOM   7611  C  CZ    . ARG B 1 256 ? 110.166 133.766 130.747 1.00 31.54 ? 256 ARG B CZ    1 
ATOM   7612  N  NH1   . ARG B 1 256 ? 109.497 132.625 130.732 1.00 29.43 ? 256 ARG B NH1   1 
ATOM   7613  N  NH2   . ARG B 1 256 ? 111.427 133.786 130.328 1.00 31.09 ? 256 ARG B NH2   1 
ATOM   7614  N  N     . ASP B 1 257 ? 111.647 135.828 134.277 1.00 24.30 ? 257 ASP B N     1 
ATOM   7615  C  CA    . ASP B 1 257 ? 112.691 134.814 134.299 1.00 22.12 ? 257 ASP B CA    1 
ATOM   7616  C  C     . ASP B 1 257 ? 112.971 134.273 135.691 1.00 23.23 ? 257 ASP B C     1 
ATOM   7617  O  O     . ASP B 1 257 ? 114.047 133.704 135.902 1.00 26.90 ? 257 ASP B O     1 
ATOM   7618  C  CB    . ASP B 1 257 ? 113.982 135.376 133.704 1.00 25.52 ? 257 ASP B CB    1 
ATOM   7619  C  CG    . ASP B 1 257 ? 113.982 135.363 132.196 1.00 30.92 ? 257 ASP B CG    1 
ATOM   7620  O  OD1   . ASP B 1 257 ? 113.086 134.730 131.602 1.00 30.77 ? 257 ASP B OD1   1 
ATOM   7621  O  OD2   . ASP B 1 257 ? 114.885 135.983 131.603 1.00 32.66 ? 257 ASP B OD2   1 
ATOM   7622  N  N     . ILE B 1 258 ? 112.049 134.436 136.642 1.00 26.09 ? 258 ILE B N     1 
ATOM   7623  C  CA    . ILE B 1 258 ? 112.323 134.019 138.013 1.00 22.72 ? 258 ILE B CA    1 
ATOM   7624  C  C     . ILE B 1 258 ? 112.502 132.508 138.093 1.00 22.47 ? 258 ILE B C     1 
ATOM   7625  O  O     . ILE B 1 258 ? 113.359 132.014 138.834 1.00 31.95 ? 258 ILE B O     1 
ATOM   7626  C  CB    . ILE B 1 258 ? 111.218 134.523 138.963 1.00 26.29 ? 258 ILE B CB    1 
ATOM   7627  C  CG1   . ILE B 1 258 ? 111.561 134.177 140.414 1.00 24.18 ? 258 ILE B CG1   1 
ATOM   7628  C  CG2   . ILE B 1 258 ? 109.854 133.969 138.573 1.00 21.60 ? 258 ILE B CG2   1 
ATOM   7629  C  CD1   . ILE B 1 258 ? 112.871 134.765 140.887 1.00 18.12 ? 258 ILE B CD1   1 
ATOM   7630  N  N     . ASN B 1 259 ? 111.720 131.748 137.324 1.00 29.32 ? 259 ASN B N     1 
ATOM   7631  C  CA    . ASN B 1 259 ? 111.852 130.295 137.359 1.00 27.12 ? 259 ASN B CA    1 
ATOM   7632  C  C     . ASN B 1 259 ? 113.153 129.844 136.710 1.00 28.00 ? 259 ASN B C     1 
ATOM   7633  O  O     . ASN B 1 259 ? 113.830 128.946 137.223 1.00 29.85 ? 259 ASN B O     1 
ATOM   7634  C  CB    . ASN B 1 259 ? 110.649 129.642 136.683 1.00 28.10 ? 259 ASN B CB    1 
ATOM   7635  C  CG    . ASN B 1 259 ? 109.434 129.594 137.585 1.00 31.34 ? 259 ASN B CG    1 
ATOM   7636  O  OD1   . ASN B 1 259 ? 109.477 129.020 138.671 1.00 32.70 ? 259 ASN B OD1   1 
ATOM   7637  N  ND2   . ASN B 1 259 ? 108.342 130.202 137.140 1.00 32.58 ? 259 ASN B ND2   1 
ATOM   7638  N  N     . ASP B 1 260 ? 113.522 130.456 135.583 1.00 30.57 ? 260 ASP B N     1 
ATOM   7639  C  CA    . ASP B 1 260 ? 114.827 130.189 134.987 1.00 25.31 ? 260 ASP B CA    1 
ATOM   7640  C  C     . ASP B 1 260 ? 115.949 130.630 135.918 1.00 28.56 ? 260 ASP B C     1 
ATOM   7641  O  O     . ASP B 1 260 ? 116.995 129.976 135.999 1.00 32.10 ? 260 ASP B O     1 
ATOM   7642  C  CB    . ASP B 1 260 ? 114.941 130.899 133.639 1.00 27.90 ? 260 ASP B CB    1 
ATOM   7643  C  CG    . ASP B 1 260 ? 113.858 130.481 132.668 1.00 36.98 ? 260 ASP B CG    1 
ATOM   7644  O  OD1   . ASP B 1 260 ? 113.730 131.128 131.607 1.00 35.15 ? 260 ASP B OD1   1 
ATOM   7645  O  OD2   . ASP B 1 260 ? 113.135 129.506 132.962 1.00 38.76 ? 260 ASP B OD2   1 
ATOM   7646  N  N     . PHE B 1 261 ? 115.747 131.748 136.618 1.00 30.66 ? 261 PHE B N     1 
ATOM   7647  C  CA    . PHE B 1 261 ? 116.723 132.227 137.590 1.00 20.77 ? 261 PHE B CA    1 
ATOM   7648  C  C     . PHE B 1 261 ? 116.954 131.200 138.690 1.00 23.79 ? 261 PHE B C     1 
ATOM   7649  O  O     . PHE B 1 261 ? 118.096 130.959 139.099 1.00 26.32 ? 261 PHE B O     1 
ATOM   7650  C  CB    . PHE B 1 261 ? 116.233 133.551 138.176 1.00 16.48 ? 261 PHE B CB    1 
ATOM   7651  C  CG    . PHE B 1 261 ? 117.214 134.232 139.081 1.00 26.31 ? 261 PHE B CG    1 
ATOM   7652  C  CD1   . PHE B 1 261 ? 118.296 134.915 138.560 1.00 22.25 ? 261 PHE B CD1   1 
ATOM   7653  C  CD2   . PHE B 1 261 ? 117.033 134.223 140.453 1.00 21.37 ? 261 PHE B CD2   1 
ATOM   7654  C  CE1   . PHE B 1 261 ? 119.191 135.554 139.389 1.00 17.02 ? 261 PHE B CE1   1 
ATOM   7655  C  CE2   . PHE B 1 261 ? 117.925 134.862 141.285 1.00 13.53 ? 261 PHE B CE2   1 
ATOM   7656  C  CZ    . PHE B 1 261 ? 119.005 135.526 140.751 1.00 17.24 ? 261 PHE B CZ    1 
ATOM   7657  N  N     . LEU B 1 262 ? 115.878 130.583 139.182 1.00 30.23 ? 262 LEU B N     1 
ATOM   7658  C  CA    . LEU B 1 262 ? 116.004 129.595 140.246 1.00 25.80 ? 262 LEU B CA    1 
ATOM   7659  C  C     . LEU B 1 262 ? 116.545 128.268 139.733 1.00 29.61 ? 262 LEU B C     1 
ATOM   7660  O  O     . LEU B 1 262 ? 117.240 127.560 140.471 1.00 30.82 ? 262 LEU B O     1 
ATOM   7661  C  CB    . LEU B 1 262 ? 114.654 129.388 140.924 1.00 30.48 ? 262 LEU B CB    1 
ATOM   7662  C  CG    . LEU B 1 262 ? 114.022 130.632 141.541 1.00 23.84 ? 262 LEU B CG    1 
ATOM   7663  C  CD1   . LEU B 1 262 ? 112.642 130.315 142.085 1.00 28.90 ? 262 LEU B CD1   1 
ATOM   7664  C  CD2   . LEU B 1 262 ? 114.922 131.193 142.623 1.00 23.09 ? 262 LEU B CD2   1 
ATOM   7665  N  N     . ASP B 1 263 ? 116.243 127.910 138.484 1.00 40.18 ? 263 ASP B N     1 
ATOM   7666  C  CA    . ASP B 1 263 ? 116.696 126.640 137.930 1.00 32.45 ? 263 ASP B CA    1 
ATOM   7667  C  C     . ASP B 1 263 ? 118.206 126.567 137.767 1.00 35.23 ? 263 ASP B C     1 
ATOM   7668  O  O     . ASP B 1 263 ? 118.736 125.469 137.569 1.00 45.06 ? 263 ASP B O     1 
ATOM   7669  C  CB    . ASP B 1 263 ? 116.025 126.382 136.581 1.00 36.38 ? 263 ASP B CB    1 
ATOM   7670  C  CG    . ASP B 1 263 ? 114.544 126.102 136.710 1.00 43.46 ? 263 ASP B CG    1 
ATOM   7671  O  OD1   . ASP B 1 263 ? 114.078 125.878 137.846 1.00 40.57 ? 263 ASP B OD1   1 
ATOM   7672  O  OD2   . ASP B 1 263 ? 113.844 126.108 135.676 1.00 43.73 ? 263 ASP B OD2   1 
ATOM   7673  N  N     . THR B 1 264 ? 118.909 127.698 137.836 1.00 38.48 ? 264 THR B N     1 
ATOM   7674  C  CA    . THR B 1 264 ? 120.363 127.689 137.740 1.00 36.79 ? 264 THR B CA    1 
ATOM   7675  C  C     . THR B 1 264 ? 121.030 127.067 138.960 1.00 39.54 ? 264 THR B C     1 
ATOM   7676  O  O     . THR B 1 264 ? 122.227 126.766 138.901 1.00 40.93 ? 264 THR B O     1 
ATOM   7677  C  CB    . THR B 1 264 ? 120.888 129.112 137.540 1.00 35.80 ? 264 THR B CB    1 
ATOM   7678  O  OG1   . THR B 1 264 ? 120.499 129.929 138.650 1.00 37.61 ? 264 THR B OG1   1 
ATOM   7679  C  CG2   . THR B 1 264 ? 120.329 129.710 136.262 1.00 35.69 ? 264 THR B CG2   1 
ATOM   7680  N  N     . LYS B 1 265 ? 120.296 126.865 140.052 1.00 35.34 ? 265 LYS B N     1 
ATOM   7681  C  CA    . LYS B 1 265 ? 120.851 126.306 141.276 1.00 36.35 ? 265 LYS B CA    1 
ATOM   7682  C  C     . LYS B 1 265 ? 120.396 124.880 141.550 1.00 40.35 ? 265 LYS B C     1 
ATOM   7683  O  O     . LYS B 1 265 ? 120.779 124.313 142.578 1.00 42.67 ? 265 LYS B O     1 
ATOM   7684  C  CB    . LYS B 1 265 ? 120.494 127.196 142.470 1.00 35.36 ? 265 LYS B CB    1 
ATOM   7685  C  CG    . LYS B 1 265 ? 121.319 128.460 142.553 1.00 37.22 ? 265 LYS B CG    1 
ATOM   7686  C  CD    . LYS B 1 265 ? 122.796 128.146 142.453 1.00 40.74 ? 265 LYS B CD    1 
ATOM   7687  C  CE    . LYS B 1 265 ? 123.619 129.411 142.418 1.00 37.82 ? 265 LYS B CE    1 
ATOM   7688  N  NZ    . LYS B 1 265 ? 125.043 129.131 142.096 1.00 40.60 ? 265 LYS B NZ    1 
ATOM   7689  N  N     . LYS B 1 266 ? 119.594 124.288 140.672 1.00 46.20 ? 266 LYS B N     1 
ATOM   7690  C  CA    . LYS B 1 266 ? 119.183 122.906 140.860 1.00 48.22 ? 266 LYS B CA    1 
ATOM   7691  C  C     . LYS B 1 266 ? 120.362 121.965 140.643 1.00 53.54 ? 266 LYS B C     1 
ATOM   7692  O  O     . LYS B 1 266 ? 121.262 122.232 139.842 1.00 54.01 ? 266 LYS B O     1 
ATOM   7693  C  CB    . LYS B 1 266 ? 118.043 122.550 139.907 1.00 48.02 ? 266 LYS B CB    1 
ATOM   7694  C  CG    . LYS B 1 266 ? 116.690 123.091 140.332 1.00 49.21 ? 266 LYS B CG    1 
ATOM   7695  C  CD    . LYS B 1 266 ? 115.623 122.772 139.300 1.00 50.74 ? 266 LYS B CD    1 
ATOM   7696  C  CE    . LYS B 1 266 ? 114.238 123.143 139.803 1.00 49.67 ? 266 LYS B CE    1 
ATOM   7697  N  NZ    . LYS B 1 266 ? 113.215 123.057 138.724 1.00 48.97 ? 266 LYS B NZ    1 
ATOM   7698  N  N     . ILE B 1 267 ? 120.357 120.853 141.382 1.00 58.00 ? 267 ILE B N     1 
ATOM   7699  C  CA    . ILE B 1 267 ? 121.432 119.876 141.252 1.00 59.61 ? 267 ILE B CA    1 
ATOM   7700  C  C     . ILE B 1 267 ? 121.396 119.214 139.881 1.00 61.26 ? 267 ILE B C     1 
ATOM   7701  O  O     . ILE B 1 267 ? 122.439 118.817 139.347 1.00 60.40 ? 267 ILE B O     1 
ATOM   7702  C  CB    . ILE B 1 267 ? 121.354 118.831 142.382 1.00 60.74 ? 267 ILE B CB    1 
ATOM   7703  C  CG1   . ILE B 1 267 ? 121.603 119.483 143.745 1.00 60.91 ? 267 ILE B CG1   1 
ATOM   7704  C  CG2   . ILE B 1 267 ? 122.355 117.714 142.141 1.00 58.65 ? 267 ILE B CG2   1 
ATOM   7705  C  CD1   . ILE B 1 267 ? 120.339 119.772 144.531 1.00 59.48 ? 267 ILE B CD1   1 
ATOM   7706  N  N     . SER B 1 268 ? 120.211 119.086 139.291 1.00 62.14 ? 268 SER B N     1 
ATOM   7707  C  CA    . SER B 1 268 ? 120.040 118.485 137.976 1.00 63.21 ? 268 SER B CA    1 
ATOM   7708  C  C     . SER B 1 268 ? 120.124 119.502 136.845 1.00 64.42 ? 268 SER B C     1 
ATOM   7709  O  O     . SER B 1 268 ? 119.758 119.179 135.711 1.00 64.12 ? 268 SER B O     1 
ATOM   7710  C  CB    . SER B 1 268 ? 118.700 117.748 137.909 1.00 64.84 ? 268 SER B CB    1 
ATOM   7711  O  OG    . SER B 1 268 ? 117.632 118.608 138.268 1.00 61.57 ? 268 SER B OG    1 
ATOM   7712  N  N     . ALA B 1 269 ? 120.585 120.719 137.128 1.00 68.18 ? 269 ALA B N     1 
ATOM   7713  C  CA    . ALA B 1 269 ? 120.610 121.765 136.116 1.00 68.46 ? 269 ALA B CA    1 
ATOM   7714  C  C     . ALA B 1 269 ? 121.576 121.417 134.991 1.00 69.28 ? 269 ALA B C     1 
ATOM   7715  O  O     . ALA B 1 269 ? 122.656 120.866 135.221 1.00 67.39 ? 269 ALA B O     1 
ATOM   7716  C  CB    . ALA B 1 269 ? 120.998 123.103 136.747 1.00 65.53 ? 269 ALA B CB    1 
ATOM   7717  N  N     . ASP B 1 270 ? 121.176 121.743 133.765 1.00 73.95 ? 270 ASP B N     1 
ATOM   7718  C  CA    . ASP B 1 270 ? 122.028 121.526 132.607 1.00 74.36 ? 270 ASP B CA    1 
ATOM   7719  C  C     . ASP B 1 270 ? 123.247 122.440 132.662 1.00 73.99 ? 270 ASP B C     1 
ATOM   7720  O  O     . ASP B 1 270 ? 123.206 123.535 133.230 1.00 75.02 ? 270 ASP B O     1 
ATOM   7721  C  CB    . ASP B 1 270 ? 121.244 121.769 131.317 1.00 73.89 ? 270 ASP B CB    1 
ATOM   7722  C  CG    . ASP B 1 270 ? 121.857 121.070 130.119 1.00 76.21 ? 270 ASP B CG    1 
ATOM   7723  O  OD1   . ASP B 1 270 ? 123.046 121.314 129.825 1.00 75.47 ? 270 ASP B OD1   1 
ATOM   7724  O  OD2   . ASP B 1 270 ? 121.147 120.275 129.467 1.00 75.19 ? 270 ASP B OD2   1 
ATOM   7725  N  N     . GLU B 1 271 ? 124.347 121.975 132.064 1.00 74.39 ? 271 GLU B N     1 
ATOM   7726  C  CA    . GLU B 1 271 ? 125.591 122.734 132.098 1.00 75.07 ? 271 GLU B CA    1 
ATOM   7727  C  C     . GLU B 1 271 ? 125.500 124.046 131.328 1.00 73.69 ? 271 GLU B C     1 
ATOM   7728  O  O     . GLU B 1 271 ? 126.306 124.949 131.574 1.00 73.29 ? 271 GLU B O     1 
ATOM   7729  C  CB    . GLU B 1 271 ? 126.740 121.887 131.549 1.00 73.98 ? 271 GLU B CB    1 
ATOM   7730  C  CG    . GLU B 1 271 ? 127.150 120.740 132.458 1.00 73.71 ? 271 GLU B CG    1 
ATOM   7731  C  CD    . GLU B 1 271 ? 127.688 121.218 133.793 1.00 75.05 ? 271 GLU B CD    1 
ATOM   7732  O  OE1   . GLU B 1 271 ? 128.396 122.246 133.819 1.00 75.05 ? 271 GLU B OE1   1 
ATOM   7733  O  OE2   . GLU B 1 271 ? 127.402 120.565 134.818 1.00 74.91 ? 271 GLU B OE2   1 
ATOM   7734  N  N     . ASP B 1 272 ? 124.548 124.174 130.407 1.00 69.91 ? 272 ASP B N     1 
ATOM   7735  C  CA    . ASP B 1 272 ? 124.317 125.435 129.715 1.00 71.27 ? 272 ASP B CA    1 
ATOM   7736  C  C     . ASP B 1 272 ? 123.366 126.352 130.473 1.00 70.48 ? 272 ASP B C     1 
ATOM   7737  O  O     . ASP B 1 272 ? 123.079 127.455 129.999 1.00 67.60 ? 272 ASP B O     1 
ATOM   7738  C  CB    . ASP B 1 272 ? 123.786 125.180 128.298 1.00 70.78 ? 272 ASP B CB    1 
ATOM   7739  C  CG    . ASP B 1 272 ? 122.331 124.749 128.282 1.00 72.72 ? 272 ASP B CG    1 
ATOM   7740  O  OD1   . ASP B 1 272 ? 121.879 124.112 129.255 1.00 72.58 ? 272 ASP B OD1   1 
ATOM   7741  O  OD2   . ASP B 1 272 ? 121.636 125.050 127.288 1.00 70.62 ? 272 ASP B OD2   1 
ATOM   7742  N  N     . VAL B 1 273 ? 122.858 125.911 131.626 1.00 66.27 ? 273 VAL B N     1 
ATOM   7743  C  CA    . VAL B 1 273 ? 122.012 126.725 132.484 1.00 66.17 ? 273 VAL B CA    1 
ATOM   7744  C  C     . VAL B 1 273 ? 122.645 126.949 133.851 1.00 64.63 ? 273 VAL B C     1 
ATOM   7745  O  O     . VAL B 1 273 ? 122.561 128.050 134.408 1.00 65.19 ? 273 VAL B O     1 
ATOM   7746  C  CB    . VAL B 1 273 ? 120.609 126.097 132.635 1.00 67.27 ? 273 VAL B CB    1 
ATOM   7747  C  CG1   . VAL B 1 273 ? 119.737 126.938 133.557 1.00 62.77 ? 273 VAL B CG1   1 
ATOM   7748  C  CG2   . VAL B 1 273 ? 119.952 125.931 131.273 1.00 65.20 ? 273 VAL B CG2   1 
ATOM   7749  N  N     . ARG B 1 274 ? 123.291 125.924 134.403 1.00 62.69 ? 274 ARG B N     1 
ATOM   7750  C  CA    . ARG B 1 274 ? 123.832 125.998 135.753 1.00 61.26 ? 274 ARG B CA    1 
ATOM   7751  C  C     . ARG B 1 274 ? 124.946 127.035 135.851 1.00 61.46 ? 274 ARG B C     1 
ATOM   7752  O  O     . ARG B 1 274 ? 125.795 127.150 134.963 1.00 62.17 ? 274 ARG B O     1 
ATOM   7753  C  CB    . ARG B 1 274 ? 124.357 124.623 136.176 1.00 63.99 ? 274 ARG B CB    1 
ATOM   7754  C  CG    . ARG B 1 274 ? 125.495 124.663 137.183 1.00 62.28 ? 274 ARG B CG    1 
ATOM   7755  C  CD    . ARG B 1 274 ? 125.508 123.427 138.065 1.00 63.07 ? 274 ARG B CD    1 
ATOM   7756  N  NE    . ARG B 1 274 ? 125.921 122.239 137.328 1.00 65.20 ? 274 ARG B NE    1 
ATOM   7757  C  CZ    . ARG B 1 274 ? 125.144 121.189 137.100 1.00 66.95 ? 274 ARG B CZ    1 
ATOM   7758  N  NH1   . ARG B 1 274 ? 123.899 121.141 137.545 1.00 66.38 ? 274 ARG B NH1   1 
ATOM   7759  N  NH2   . ARG B 1 274 ? 125.628 120.161 136.409 1.00 65.43 ? 274 ARG B NH2   1 
ATOM   7760  N  N     . VAL B 1 275 ? 124.930 127.798 136.943 1.00 49.05 ? 275 VAL B N     1 
ATOM   7761  C  CA    . VAL B 1 275 ? 126.006 128.716 137.299 1.00 46.72 ? 275 VAL B CA    1 
ATOM   7762  C  C     . VAL B 1 275 ? 126.623 128.230 138.603 1.00 48.42 ? 275 VAL B C     1 
ATOM   7763  O  O     . VAL B 1 275 ? 125.909 127.802 139.517 1.00 52.80 ? 275 VAL B O     1 
ATOM   7764  C  CB    . VAL B 1 275 ? 125.505 130.169 137.424 1.00 45.78 ? 275 VAL B CB    1 
ATOM   7765  C  CG1   . VAL B 1 275 ? 125.143 130.725 136.056 1.00 42.57 ? 275 VAL B CG1   1 
ATOM   7766  C  CG2   . VAL B 1 275 ? 124.314 130.249 138.361 1.00 47.28 ? 275 VAL B CG2   1 
ATOM   7767  N  N     . LYS B 1 276 ? 127.952 128.278 138.682 1.00 43.69 ? 276 LYS B N     1 
ATOM   7768  C  CA    . LYS B 1 276 ? 128.685 127.690 139.798 1.00 44.28 ? 276 LYS B CA    1 
ATOM   7769  C  C     . LYS B 1 276 ? 129.148 128.724 140.818 1.00 42.21 ? 276 LYS B C     1 
ATOM   7770  O  O     . LYS B 1 276 ? 128.974 128.524 142.023 1.00 47.54 ? 276 LYS B O     1 
ATOM   7771  C  CB    . LYS B 1 276 ? 129.902 126.883 139.304 1.00 45.34 ? 276 LYS B CB    1 
ATOM   7772  C  CG    . LYS B 1 276 ? 129.626 125.621 138.455 1.00 46.57 ? 276 LYS B CG    1 
ATOM   7773  C  CD    . LYS B 1 276 ? 128.928 125.847 137.115 1.00 47.91 ? 276 LYS B CD    1 
ATOM   7774  C  CE    . LYS B 1 276 ? 129.546 126.993 136.328 1.00 44.89 ? 276 LYS B CE    1 
ATOM   7775  N  NZ    . LYS B 1 276 ? 129.153 126.948 134.893 1.00 47.62 ? 276 LYS B NZ    1 
ATOM   7776  N  N     . THR B 1 277 ? 129.742 129.825 140.365 1.00 37.29 ? 277 THR B N     1 
ATOM   7777  C  CA    . THR B 1 277 ? 130.326 130.817 141.257 1.00 38.46 ? 277 THR B CA    1 
ATOM   7778  C  C     . THR B 1 277 ? 129.443 132.042 141.446 1.00 38.43 ? 277 THR B C     1 
ATOM   7779  O  O     . THR B 1 277 ? 129.917 133.060 141.961 1.00 37.45 ? 277 THR B O     1 
ATOM   7780  C  CB    . THR B 1 277 ? 131.700 131.245 140.741 1.00 40.53 ? 277 THR B CB    1 
ATOM   7781  O  OG1   . THR B 1 277 ? 131.541 132.109 139.609 1.00 33.82 ? 277 THR B OG1   1 
ATOM   7782  C  CG2   . THR B 1 277 ? 132.513 130.027 140.341 1.00 39.78 ? 277 THR B CG2   1 
ATOM   7783  N  N     . LEU B 1 278 ? 128.177 131.971 141.047 1.00 34.16 ? 278 LEU B N     1 
ATOM   7784  C  CA    . LEU B 1 278 ? 127.260 133.103 141.122 1.00 28.50 ? 278 LEU B CA    1 
ATOM   7785  C  C     . LEU B 1 278 ? 126.140 132.763 142.095 1.00 26.17 ? 278 LEU B C     1 
ATOM   7786  O  O     . LEU B 1 278 ? 125.244 131.981 141.765 1.00 34.95 ? 278 LEU B O     1 
ATOM   7787  C  CB    . LEU B 1 278 ? 126.702 133.441 139.740 1.00 29.69 ? 278 LEU B CB    1 
ATOM   7788  C  CG    . LEU B 1 278 ? 126.183 134.864 139.533 1.00 29.21 ? 278 LEU B CG    1 
ATOM   7789  C  CD1   . LEU B 1 278 ? 127.336 135.823 139.328 1.00 25.24 ? 278 LEU B CD1   1 
ATOM   7790  C  CD2   . LEU B 1 278 ? 125.234 134.914 138.351 1.00 28.67 ? 278 LEU B CD2   1 
ATOM   7791  N  N     . SER B 1 279 ? 126.196 133.344 143.289 1.00 24.24 ? 279 SER B N     1 
ATOM   7792  C  CA    . SER B 1 279 ? 125.094 133.227 144.232 1.00 19.39 ? 279 SER B CA    1 
ATOM   7793  C  C     . SER B 1 279 ? 123.877 133.972 143.702 1.00 22.06 ? 279 SER B C     1 
ATOM   7794  O  O     . SER B 1 279 ? 123.993 134.915 142.917 1.00 29.30 ? 279 SER B O     1 
ATOM   7795  C  CB    . SER B 1 279 ? 125.494 133.785 145.596 1.00 19.44 ? 279 SER B CB    1 
ATOM   7796  O  OG    . SER B 1 279 ? 126.668 133.160 146.079 1.00 28.20 ? 279 SER B OG    1 
ATOM   7797  N  N     . ILE B 1 280 ? 122.696 133.537 144.129 1.00 19.84 ? 280 ILE B N     1 
ATOM   7798  C  CA    . ILE B 1 280 ? 121.448 134.124 143.661 1.00 19.91 ? 280 ILE B CA    1 
ATOM   7799  C  C     . ILE B 1 280 ? 120.635 134.595 144.856 1.00 14.53 ? 280 ILE B C     1 
ATOM   7800  O  O     . ILE B 1 280 ? 120.609 133.941 145.904 1.00 24.67 ? 280 ILE B O     1 
ATOM   7801  C  CB    . ILE B 1 280 ? 120.634 133.140 142.793 1.00 16.48 ? 280 ILE B CB    1 
ATOM   7802  C  CG1   . ILE B 1 280 ? 120.257 131.882 143.572 1.00 21.60 ? 280 ILE B CG1   1 
ATOM   7803  C  CG2   . ILE B 1 280 ? 121.412 132.765 141.557 1.00 17.62 ? 280 ILE B CG2   1 
ATOM   7804  C  CD1   . ILE B 1 280 ? 119.032 131.187 143.022 1.00 16.46 ? 280 ILE B CD1   1 
ATOM   7805  N  N     . GLY B 1 281 ? 120.004 135.744 144.704 1.00 8.94  ? 281 GLY B N     1 
ATOM   7806  C  CA    . GLY B 1 281 ? 119.070 136.241 145.700 1.00 7.23  ? 281 GLY B CA    1 
ATOM   7807  C  C     . GLY B 1 281 ? 117.780 136.664 145.038 1.00 7.83  ? 281 GLY B C     1 
ATOM   7808  O  O     . GLY B 1 281 ? 117.786 137.231 143.948 1.00 19.37 ? 281 GLY B O     1 
ATOM   7809  N  N     . VAL B 1 282 ? 116.668 136.375 145.704 1.00 14.14 ? 282 VAL B N     1 
ATOM   7810  C  CA    . VAL B 1 282 ? 115.340 136.696 145.200 1.00 15.93 ? 282 VAL B CA    1 
ATOM   7811  C  C     . VAL B 1 282 ? 114.772 137.838 146.028 1.00 13.39 ? 282 VAL B C     1 
ATOM   7812  O  O     . VAL B 1 282 ? 114.805 137.796 147.263 1.00 19.91 ? 282 VAL B O     1 
ATOM   7813  C  CB    . VAL B 1 282 ? 114.412 135.470 145.227 1.00 15.65 ? 282 VAL B CB    1 
ATOM   7814  C  CG1   . VAL B 1 282 ? 112.974 135.883 144.985 1.00 18.73 ? 282 VAL B CG1   1 
ATOM   7815  C  CG2   . VAL B 1 282 ? 114.846 134.473 144.176 1.00 20.84 ? 282 VAL B CG2   1 
ATOM   7816  N  N     . VAL B 1 283 ? 114.265 138.860 145.348 1.00 4.30  ? 283 VAL B N     1 
ATOM   7817  C  CA    . VAL B 1 283 ? 113.616 139.996 145.986 1.00 10.80 ? 283 VAL B CA    1 
ATOM   7818  C  C     . VAL B 1 283 ? 112.114 139.766 145.955 1.00 13.20 ? 283 VAL B C     1 
ATOM   7819  O  O     . VAL B 1 283 ? 111.532 139.558 144.884 1.00 21.31 ? 283 VAL B O     1 
ATOM   7820  C  CB    . VAL B 1 283 ? 113.991 141.312 145.287 1.00 9.19  ? 283 VAL B CB    1 
ATOM   7821  C  CG1   . VAL B 1 283 ? 113.535 142.494 146.114 1.00 11.04 ? 283 VAL B CG1   1 
ATOM   7822  C  CG2   . VAL B 1 283 ? 115.488 141.365 145.047 1.00 11.16 ? 283 VAL B CG2   1 
ATOM   7823  N  N     . ILE B 1 284 ? 111.487 139.798 147.126 1.00 14.88 ? 284 ILE B N     1 
ATOM   7824  C  CA    . ILE B 1 284 ? 110.065 139.486 147.244 1.00 17.24 ? 284 ILE B CA    1 
ATOM   7825  C  C     . ILE B 1 284 ? 109.313 140.687 147.805 1.00 19.52 ? 284 ILE B C     1 
ATOM   7826  O  O     . ILE B 1 284 ? 109.459 141.009 148.993 1.00 22.61 ? 284 ILE B O     1 
ATOM   7827  C  CB    . ILE B 1 284 ? 109.841 138.246 148.122 1.00 15.42 ? 284 ILE B CB    1 
ATOM   7828  C  CG1   . ILE B 1 284 ? 110.684 137.075 147.616 1.00 16.96 ? 284 ILE B CG1   1 
ATOM   7829  C  CG2   . ILE B 1 284 ? 108.370 137.875 148.150 1.00 16.48 ? 284 ILE B CG2   1 
ATOM   7830  C  CD1   . ILE B 1 284 ? 110.450 135.789 148.365 1.00 18.38 ? 284 ILE B CD1   1 
ATOM   7831  N  N     . PRO B 1 285 ? 108.511 141.375 147.000 1.00 20.37 ? 285 PRO B N     1 
ATOM   7832  C  CA    . PRO B 1 285 ? 107.633 142.414 147.545 1.00 28.39 ? 285 PRO B CA    1 
ATOM   7833  C  C     . PRO B 1 285 ? 106.496 141.805 148.352 1.00 27.29 ? 285 PRO B C     1 
ATOM   7834  O  O     . PRO B 1 285 ? 106.216 140.607 148.284 1.00 22.95 ? 285 PRO B O     1 
ATOM   7835  C  CB    . PRO B 1 285 ? 107.103 143.130 146.298 1.00 22.86 ? 285 PRO B CB    1 
ATOM   7836  C  CG    . PRO B 1 285 ? 108.029 142.734 145.194 1.00 20.81 ? 285 PRO B CG    1 
ATOM   7837  C  CD    . PRO B 1 285 ? 108.497 141.359 145.530 1.00 16.61 ? 285 PRO B CD    1 
ATOM   7838  N  N     . ASP B 1 286 ? 105.834 142.663 149.132 1.00 31.35 ? 286 ASP B N     1 
ATOM   7839  C  CA    . ASP B 1 286 ? 104.685 142.216 149.913 1.00 26.57 ? 286 ASP B CA    1 
ATOM   7840  C  C     . ASP B 1 286 ? 103.545 141.732 149.029 1.00 32.03 ? 286 ASP B C     1 
ATOM   7841  O  O     . ASP B 1 286 ? 102.707 140.952 149.492 1.00 34.77 ? 286 ASP B O     1 
ATOM   7842  C  CB    . ASP B 1 286 ? 104.187 143.343 150.817 1.00 29.02 ? 286 ASP B CB    1 
ATOM   7843  C  CG    . ASP B 1 286 ? 104.766 143.271 152.213 1.00 38.76 ? 286 ASP B CG    1 
ATOM   7844  O  OD1   . ASP B 1 286 ? 105.670 142.442 152.443 1.00 35.25 ? 286 ASP B OD1   1 
ATOM   7845  O  OD2   . ASP B 1 286 ? 104.321 144.049 153.082 1.00 41.08 ? 286 ASP B OD2   1 
ATOM   7846  N  N     . LYS B 1 287 ? 103.495 142.181 147.773 1.00 34.71 ? 287 LYS B N     1 
ATOM   7847  C  CA    . LYS B 1 287 ? 102.437 141.747 146.868 1.00 29.31 ? 287 LYS B CA    1 
ATOM   7848  C  C     . LYS B 1 287 ? 102.504 140.247 146.616 1.00 31.12 ? 287 LYS B C     1 
ATOM   7849  O  O     . LYS B 1 287 ? 101.471 139.571 146.574 1.00 35.53 ? 287 LYS B O     1 
ATOM   7850  C  CB    . LYS B 1 287 ? 102.526 142.515 145.550 1.00 29.67 ? 287 LYS B CB    1 
ATOM   7851  C  CG    . LYS B 1 287 ? 101.291 142.383 144.679 1.00 29.90 ? 287 LYS B CG    1 
ATOM   7852  C  CD    . LYS B 1 287 ? 100.049 142.802 145.441 1.00 34.81 ? 287 LYS B CD    1 
ATOM   7853  C  CE    . LYS B 1 287 ? 98.827  142.822 144.545 1.00 34.11 ? 287 LYS B CE    1 
ATOM   7854  N  NZ    . LYS B 1 287 ? 97.667  143.467 145.215 1.00 35.24 ? 287 LYS B NZ    1 
ATOM   7855  N  N     . PHE B 1 288 ? 103.712 139.708 146.439 1.00 31.15 ? 288 PHE B N     1 
ATOM   7856  C  CA    . PHE B 1 288 ? 103.852 138.274 146.210 1.00 25.99 ? 288 PHE B CA    1 
ATOM   7857  C  C     . PHE B 1 288 ? 103.404 137.472 147.425 1.00 26.79 ? 288 PHE B C     1 
ATOM   7858  O  O     . PHE B 1 288 ? 102.729 136.446 147.285 1.00 33.87 ? 288 PHE B O     1 
ATOM   7859  C  CB    . PHE B 1 288 ? 105.298 137.939 145.852 1.00 26.08 ? 288 PHE B CB    1 
ATOM   7860  C  CG    . PHE B 1 288 ? 105.493 136.524 145.395 1.00 26.64 ? 288 PHE B CG    1 
ATOM   7861  C  CD1   . PHE B 1 288 ? 105.774 135.521 146.306 1.00 23.98 ? 288 PHE B CD1   1 
ATOM   7862  C  CD2   . PHE B 1 288 ? 105.391 136.196 144.055 1.00 24.46 ? 288 PHE B CD2   1 
ATOM   7863  C  CE1   . PHE B 1 288 ? 105.951 134.221 145.889 1.00 23.77 ? 288 PHE B CE1   1 
ATOM   7864  C  CE2   . PHE B 1 288 ? 105.570 134.897 143.633 1.00 29.05 ? 288 PHE B CE2   1 
ATOM   7865  C  CZ    . PHE B 1 288 ? 105.850 133.909 144.552 1.00 29.68 ? 288 PHE B CZ    1 
ATOM   7866  N  N     . VAL B 1 289 ? 103.776 137.920 148.624 1.00 33.38 ? 289 VAL B N     1 
ATOM   7867  C  CA    . VAL B 1 289 ? 103.371 137.216 149.835 1.00 31.15 ? 289 VAL B CA    1 
ATOM   7868  C  C     . VAL B 1 289 ? 101.862 137.301 150.017 1.00 33.23 ? 289 VAL B C     1 
ATOM   7869  O  O     . VAL B 1 289 ? 101.225 136.348 150.478 1.00 35.22 ? 289 VAL B O     1 
ATOM   7870  C  CB    . VAL B 1 289 ? 104.128 137.774 151.053 1.00 32.70 ? 289 VAL B CB    1 
ATOM   7871  C  CG1   . VAL B 1 289 ? 103.716 137.042 152.320 1.00 30.94 ? 289 VAL B CG1   1 
ATOM   7872  C  CG2   . VAL B 1 289 ? 105.627 137.668 150.835 1.00 27.95 ? 289 VAL B CG2   1 
ATOM   7873  N  N     . GLU B 1 290 ? 101.265 138.437 149.654 1.00 37.20 ? 290 GLU B N     1 
ATOM   7874  C  CA    . GLU B 1 290 ? 99.814  138.568 149.730 1.00 34.17 ? 290 GLU B CA    1 
ATOM   7875  C  C     . GLU B 1 290 ? 99.120  137.639 148.740 1.00 37.91 ? 290 GLU B C     1 
ATOM   7876  O  O     . GLU B 1 290 ? 98.097  137.028 149.068 1.00 43.68 ? 290 GLU B O     1 
ATOM   7877  C  CB    . GLU B 1 290 ? 99.409  140.020 149.482 1.00 36.37 ? 290 GLU B CB    1 
ATOM   7878  C  CG    . GLU B 1 290 ? 97.912  140.264 149.499 1.00 39.64 ? 290 GLU B CG    1 
ATOM   7879  C  CD    . GLU B 1 290 ? 97.563  141.737 149.425 1.00 46.69 ? 290 GLU B CD    1 
ATOM   7880  O  OE1   . GLU B 1 290 ? 98.009  142.406 148.470 1.00 45.09 ? 290 GLU B OE1   1 
ATOM   7881  O  OE2   . GLU B 1 290 ? 96.841  142.225 150.320 1.00 46.61 ? 290 GLU B OE2   1 
ATOM   7882  N  N     . LEU B 1 291 ? 99.657  137.526 147.523 1.00 31.65 ? 291 LEU B N     1 
ATOM   7883  C  CA    . LEU B 1 291 ? 99.067  136.632 146.532 1.00 29.35 ? 291 LEU B CA    1 
ATOM   7884  C  C     . LEU B 1 291 ? 99.192  135.175 146.955 1.00 35.49 ? 291 LEU B C     1 
ATOM   7885  O  O     . LEU B 1 291 ? 98.254  134.389 146.778 1.00 37.71 ? 291 LEU B O     1 
ATOM   7886  C  CB    . LEU B 1 291 ? 99.722  136.850 145.168 1.00 33.16 ? 291 LEU B CB    1 
ATOM   7887  C  CG    . LEU B 1 291 ? 99.476  138.199 144.491 1.00 33.92 ? 291 LEU B CG    1 
ATOM   7888  C  CD1   . LEU B 1 291 ? 100.477 138.417 143.373 1.00 28.08 ? 291 LEU B CD1   1 
ATOM   7889  C  CD2   . LEU B 1 291 ? 98.053  138.291 143.971 1.00 32.15 ? 291 LEU B CD2   1 
ATOM   7890  N  N     . ALA B 1 292 ? 100.345 134.792 147.506 1.00 40.48 ? 292 ALA B N     1 
ATOM   7891  C  CA    . ALA B 1 292 ? 100.523 133.422 147.977 1.00 32.33 ? 292 ALA B CA    1 
ATOM   7892  C  C     . ALA B 1 292 ? 99.659  133.129 149.196 1.00 32.71 ? 292 ALA B C     1 
ATOM   7893  O  O     . ALA B 1 292 ? 99.180  132.002 149.359 1.00 37.81 ? 292 ALA B O     1 
ATOM   7894  C  CB    . ALA B 1 292 ? 101.994 133.163 148.295 1.00 28.83 ? 292 ALA B CB    1 
ATOM   7895  N  N     . ARG B 1 293 ? 99.454  134.125 150.060 1.00 36.41 ? 293 ARG B N     1 
ATOM   7896  C  CA    . ARG B 1 293 ? 98.639  133.929 151.253 1.00 36.57 ? 293 ARG B CA    1 
ATOM   7897  C  C     . ARG B 1 293 ? 97.199  133.596 150.891 1.00 41.26 ? 293 ARG B C     1 
ATOM   7898  O  O     . ARG B 1 293 ? 96.582  132.717 151.505 1.00 45.20 ? 293 ARG B O     1 
ATOM   7899  C  CB    . ARG B 1 293 ? 98.703  135.182 152.126 1.00 38.02 ? 293 ARG B CB    1 
ATOM   7900  C  CG    . ARG B 1 293 ? 97.729  135.210 153.286 1.00 38.05 ? 293 ARG B CG    1 
ATOM   7901  C  CD    . ARG B 1 293 ? 97.708  136.590 153.915 1.00 38.31 ? 293 ARG B CD    1 
ATOM   7902  N  NE    . ARG B 1 293 ? 99.057  137.108 154.104 1.00 43.52 ? 293 ARG B NE    1 
ATOM   7903  C  CZ    . ARG B 1 293 ? 99.456  138.316 153.733 1.00 41.65 ? 293 ARG B CZ    1 
ATOM   7904  N  NH1   . ARG B 1 293 ? 98.628  139.172 153.157 1.00 40.60 ? 293 ARG B NH1   1 
ATOM   7905  N  NH2   . ARG B 1 293 ? 100.719 138.676 153.943 1.00 38.83 ? 293 ARG B NH2   1 
ATOM   7906  N  N     . GLU B 1 294 ? 96.649  134.281 149.894 1.00 47.18 ? 294 GLU B N     1 
ATOM   7907  C  CA    . GLU B 1 294 ? 95.279  134.058 149.456 1.00 46.40 ? 294 GLU B CA    1 
ATOM   7908  C  C     . GLU B 1 294 ? 95.174  133.023 148.345 1.00 45.09 ? 294 GLU B C     1 
ATOM   7909  O  O     . GLU B 1 294 ? 94.071  132.790 147.839 1.00 46.78 ? 294 GLU B O     1 
ATOM   7910  C  CB    . GLU B 1 294 ? 94.657  135.378 148.996 1.00 44.47 ? 294 GLU B CB    1 
ATOM   7911  C  CG    . GLU B 1 294 ? 94.561  136.428 150.088 1.00 47.13 ? 294 GLU B CG    1 
ATOM   7912  C  CD    . GLU B 1 294 ? 94.653  137.837 149.544 1.00 52.49 ? 294 GLU B CD    1 
ATOM   7913  O  OE1   . GLU B 1 294 ? 94.827  137.989 148.316 1.00 54.05 ? 294 GLU B OE1   1 
ATOM   7914  O  OE2   . GLU B 1 294 ? 94.553  138.793 150.341 1.00 51.51 ? 294 GLU B OE2   1 
ATOM   7915  N  N     . ASP B 1 295 ? 96.291  132.412 147.949 1.00 45.01 ? 295 ASP B N     1 
ATOM   7916  C  CA    . ASP B 1 295 ? 96.343  131.359 146.935 1.00 44.69 ? 295 ASP B CA    1 
ATOM   7917  C  C     . ASP B 1 295 ? 95.856  131.831 145.569 1.00 48.61 ? 295 ASP B C     1 
ATOM   7918  O  O     . ASP B 1 295 ? 95.544  131.008 144.703 1.00 47.45 ? 295 ASP B O     1 
ATOM   7919  C  CB    . ASP B 1 295 ? 95.555  130.119 147.374 1.00 45.93 ? 295 ASP B CB    1 
ATOM   7920  C  CG    . ASP B 1 295 ? 96.270  128.824 147.036 1.00 51.65 ? 295 ASP B CG    1 
ATOM   7921  O  OD1   . ASP B 1 295 ? 97.189  128.854 146.192 1.00 51.92 ? 295 ASP B OD1   1 
ATOM   7922  O  OD2   . ASP B 1 295 ? 95.910  127.775 147.611 1.00 49.29 ? 295 ASP B OD2   1 
ATOM   7923  N  N     . LYS B 1 296 ? 95.779  133.141 145.354 1.00 49.01 ? 296 LYS B N     1 
ATOM   7924  C  CA    . LYS B 1 296 ? 95.446  133.657 144.035 1.00 47.01 ? 296 LYS B CA    1 
ATOM   7925  C  C     . LYS B 1 296 ? 96.596  133.404 143.070 1.00 45.78 ? 296 LYS B C     1 
ATOM   7926  O  O     . LYS B 1 296 ? 97.768  133.529 143.433 1.00 49.85 ? 296 LYS B O     1 
ATOM   7927  C  CB    . LYS B 1 296 ? 95.142  135.154 144.103 1.00 46.11 ? 296 LYS B CB    1 
ATOM   7928  C  CG    . LYS B 1 296 ? 94.598  135.621 145.437 1.00 47.30 ? 296 LYS B CG    1 
ATOM   7929  C  CD    . LYS B 1 296 ? 93.615  136.766 145.266 1.00 48.09 ? 296 LYS B CD    1 
ATOM   7930  C  CE    . LYS B 1 296 ? 92.226  136.257 144.922 1.00 50.33 ? 296 LYS B CE    1 
ATOM   7931  N  NZ    . LYS B 1 296 ? 91.660  135.405 146.004 1.00 49.53 ? 296 LYS B NZ    1 
ATOM   7932  N  N     . ALA B 1 297 ? 96.258  133.044 141.836 1.00 45.63 ? 297 ALA B N     1 
ATOM   7933  C  CA    . ALA B 1 297 ? 97.281  132.822 140.824 1.00 45.65 ? 297 ALA B CA    1 
ATOM   7934  C  C     . ALA B 1 297 ? 97.947  134.143 140.462 1.00 45.14 ? 297 ALA B C     1 
ATOM   7935  O  O     . ALA B 1 297 ? 97.270  135.131 140.164 1.00 50.95 ? 297 ALA B O     1 
ATOM   7936  C  CB    . ALA B 1 297 ? 96.671  132.170 139.586 1.00 43.75 ? 297 ALA B CB    1 
ATOM   7937  N  N     . ALA B 1 298 ? 99.274  134.157 140.489 1.00 39.25 ? 298 ALA B N     1 
ATOM   7938  C  CA    . ALA B 1 298 ? 100.048 135.373 140.295 1.00 39.37 ? 298 ALA B CA    1 
ATOM   7939  C  C     . ALA B 1 298 ? 100.582 135.456 138.870 1.00 37.90 ? 298 ALA B C     1 
ATOM   7940  O  O     . ALA B 1 298 ? 100.533 134.497 138.098 1.00 39.55 ? 298 ALA B O     1 
ATOM   7941  C  CB    . ALA B 1 298 ? 101.200 135.442 141.301 1.00 41.24 ? 298 ALA B CB    1 
ATOM   7942  N  N     . TYR B 1 299 ? 101.103 136.631 138.533 1.00 37.93 ? 299 TYR B N     1 
ATOM   7943  C  CA    . TYR B 1 299 ? 101.646 136.913 137.213 1.00 32.90 ? 299 TYR B CA    1 
ATOM   7944  C  C     . TYR B 1 299 ? 103.079 137.402 137.346 1.00 33.59 ? 299 TYR B C     1 
ATOM   7945  O  O     . TYR B 1 299 ? 103.368 138.269 138.176 1.00 39.35 ? 299 TYR B O     1 
ATOM   7946  C  CB    . TYR B 1 299 ? 100.806 137.967 136.488 1.00 33.34 ? 299 TYR B CB    1 
ATOM   7947  C  CG    . TYR B 1 299 ? 99.527  137.440 135.886 1.00 34.82 ? 299 TYR B CG    1 
ATOM   7948  C  CD1   . TYR B 1 299 ? 99.552  136.608 134.776 1.00 36.71 ? 299 TYR B CD1   1 
ATOM   7949  C  CD2   . TYR B 1 299 ? 98.294  137.777 136.425 1.00 36.32 ? 299 TYR B CD2   1 
ATOM   7950  C  CE1   . TYR B 1 299 ? 98.386  136.127 134.221 1.00 39.66 ? 299 TYR B CE1   1 
ATOM   7951  C  CE2   . TYR B 1 299 ? 97.123  137.301 135.878 1.00 38.59 ? 299 TYR B CE2   1 
ATOM   7952  C  CZ    . TYR B 1 299 ? 97.173  136.476 134.776 1.00 42.19 ? 299 TYR B CZ    1 
ATOM   7953  O  OH    . TYR B 1 299 ? 96.006  136.000 134.226 1.00 41.85 ? 299 TYR B OH    1 
ATOM   7954  N  N     . VAL B 1 300 ? 103.969 136.844 136.535 1.00 31.98 ? 300 VAL B N     1 
ATOM   7955  C  CA    . VAL B 1 300 ? 105.309 137.385 136.348 1.00 28.69 ? 300 VAL B CA    1 
ATOM   7956  C  C     . VAL B 1 300 ? 105.314 138.150 135.036 1.00 28.77 ? 300 VAL B C     1 
ATOM   7957  O  O     . VAL B 1 300 ? 104.676 137.736 134.061 1.00 32.35 ? 300 VAL B O     1 
ATOM   7958  C  CB    . VAL B 1 300 ? 106.380 136.279 136.360 1.00 25.48 ? 300 VAL B CB    1 
ATOM   7959  C  CG1   . VAL B 1 300 ? 106.626 135.804 137.781 1.00 27.58 ? 300 VAL B CG1   1 
ATOM   7960  C  CG2   . VAL B 1 300 ? 105.965 135.124 135.469 1.00 31.49 ? 300 VAL B CG2   1 
ATOM   7961  N  N     . PHE B 1 301 ? 106.024 139.270 135.005 1.00 29.86 ? 301 PHE B N     1 
ATOM   7962  C  CA    . PHE B 1 301 ? 105.908 140.221 133.912 1.00 24.82 ? 301 PHE B CA    1 
ATOM   7963  C  C     . PHE B 1 301 ? 107.208 140.319 133.132 1.00 31.31 ? 301 PHE B C     1 
ATOM   7964  O  O     . PHE B 1 301 ? 108.300 140.150 133.681 1.00 33.45 ? 301 PHE B O     1 
ATOM   7965  C  CB    . PHE B 1 301 ? 105.514 141.602 134.435 1.00 26.18 ? 301 PHE B CB    1 
ATOM   7966  C  CG    . PHE B 1 301 ? 104.331 141.580 135.353 1.00 30.92 ? 301 PHE B CG    1 
ATOM   7967  C  CD1   . PHE B 1 301 ? 103.045 141.599 134.844 1.00 28.92 ? 301 PHE B CD1   1 
ATOM   7968  C  CD2   . PHE B 1 301 ? 104.502 141.528 136.724 1.00 28.90 ? 301 PHE B CD2   1 
ATOM   7969  C  CE1   . PHE B 1 301 ? 101.954 141.570 135.683 1.00 30.92 ? 301 PHE B CE1   1 
ATOM   7970  C  CE2   . PHE B 1 301 ? 103.413 141.501 137.567 1.00 29.01 ? 301 PHE B CE2   1 
ATOM   7971  C  CZ    . PHE B 1 301 ? 102.138 141.524 137.045 1.00 33.10 ? 301 PHE B CZ    1 
ATOM   7972  N  N     . TYR B 1 302 ? 107.073 140.586 131.839 1.00 31.18 ? 302 TYR B N     1 
ATOM   7973  C  CA    . TYR B 1 302 ? 108.224 140.888 131.006 1.00 28.48 ? 302 TYR B CA    1 
ATOM   7974  C  C     . TYR B 1 302 ? 108.628 142.339 131.236 1.00 29.14 ? 302 TYR B C     1 
ATOM   7975  O  O     . TYR B 1 302 ? 107.836 143.242 130.947 1.00 31.12 ? 302 TYR B O     1 
ATOM   7976  C  CB    . TYR B 1 302 ? 107.899 140.651 129.537 1.00 29.04 ? 302 TYR B CB    1 
ATOM   7977  C  CG    . TYR B 1 302 ? 107.692 139.196 129.170 1.00 30.00 ? 302 TYR B CG    1 
ATOM   7978  C  CD1   . TYR B 1 302 ? 106.521 138.533 129.510 1.00 30.16 ? 302 TYR B CD1   1 
ATOM   7979  C  CD2   . TYR B 1 302 ? 108.666 138.488 128.481 1.00 29.43 ? 302 TYR B CD2   1 
ATOM   7980  C  CE1   . TYR B 1 302 ? 106.327 137.208 129.176 1.00 30.00 ? 302 TYR B CE1   1 
ATOM   7981  C  CE2   . TYR B 1 302 ? 108.481 137.163 128.142 1.00 30.47 ? 302 TYR B CE2   1 
ATOM   7982  C  CZ    . TYR B 1 302 ? 107.310 136.528 128.493 1.00 33.23 ? 302 TYR B CZ    1 
ATOM   7983  O  OH    . TYR B 1 302 ? 107.120 135.208 128.159 1.00 31.85 ? 302 TYR B OH    1 
ATOM   7984  N  N     . PRO B 1 303 ? 109.823 142.604 131.765 1.00 27.07 ? 303 PRO B N     1 
ATOM   7985  C  CA    . PRO B 1 303 ? 110.168 143.984 132.147 1.00 28.71 ? 303 PRO B CA    1 
ATOM   7986  C  C     . PRO B 1 303 ? 110.171 144.973 130.996 1.00 28.29 ? 303 PRO B C     1 
ATOM   7987  O  O     . PRO B 1 303 ? 109.836 146.146 131.206 1.00 33.07 ? 303 PRO B O     1 
ATOM   7988  C  CB    . PRO B 1 303 ? 111.567 143.830 132.760 1.00 29.17 ? 303 PRO B CB    1 
ATOM   7989  C  CG    . PRO B 1 303 ? 111.624 142.417 133.205 1.00 27.83 ? 303 PRO B CG    1 
ATOM   7990  C  CD    . PRO B 1 303 ? 110.854 141.643 132.186 1.00 23.92 ? 303 PRO B CD    1 
ATOM   7991  N  N     . HIS B 1 304 ? 110.549 144.551 129.787 1.00 28.60 ? 304 HIS B N     1 
ATOM   7992  C  CA    . HIS B 1 304 ? 110.642 145.507 128.689 1.00 27.96 ? 304 HIS B CA    1 
ATOM   7993  C  C     . HIS B 1 304 ? 109.271 146.003 128.254 1.00 33.05 ? 304 HIS B C     1 
ATOM   7994  O  O     . HIS B 1 304 ? 109.138 147.162 127.852 1.00 39.30 ? 304 HIS B O     1 
ATOM   7995  C  CB    . HIS B 1 304 ? 111.384 144.897 127.503 1.00 29.90 ? 304 HIS B CB    1 
ATOM   7996  C  CG    . HIS B 1 304 ? 111.778 145.902 126.467 1.00 32.16 ? 304 HIS B CG    1 
ATOM   7997  N  ND1   . HIS B 1 304 ? 112.409 147.086 126.783 1.00 32.50 ? 304 HIS B ND1   1 
ATOM   7998  C  CD2   . HIS B 1 304 ? 111.619 145.907 125.123 1.00 33.29 ? 304 HIS B CD2   1 
ATOM   7999  C  CE1   . HIS B 1 304 ? 112.628 147.774 125.677 1.00 31.67 ? 304 HIS B CE1   1 
ATOM   8000  N  NE2   . HIS B 1 304 ? 112.158 147.081 124.656 1.00 32.14 ? 304 HIS B NE2   1 
ATOM   8001  N  N     . THR B 1 305 ? 108.246 145.154 128.326 1.00 33.01 ? 305 THR B N     1 
ATOM   8002  C  CA    . THR B 1 305 ? 106.894 145.613 128.028 1.00 31.29 ? 305 THR B CA    1 
ATOM   8003  C  C     . THR B 1 305 ? 106.452 146.686 129.014 1.00 29.90 ? 305 THR B C     1 
ATOM   8004  O  O     . THR B 1 305 ? 105.848 147.692 128.622 1.00 33.98 ? 305 THR B O     1 
ATOM   8005  C  CB    . THR B 1 305 ? 105.921 144.436 128.045 1.00 29.68 ? 305 THR B CB    1 
ATOM   8006  O  OG1   . THR B 1 305 ? 105.768 143.962 129.388 1.00 29.86 ? 305 THR B OG1   1 
ATOM   8007  C  CG2   . THR B 1 305 ? 106.442 143.309 127.173 1.00 30.12 ? 305 THR B CG2   1 
ATOM   8008  N  N     . ILE B 1 306 ? 106.757 146.494 130.299 1.00 33.72 ? 306 ILE B N     1 
ATOM   8009  C  CA    . ILE B 1 306 ? 106.416 147.491 131.308 1.00 30.18 ? 306 ILE B CA    1 
ATOM   8010  C  C     . ILE B 1 306 ? 107.186 148.782 131.065 1.00 30.21 ? 306 ILE B C     1 
ATOM   8011  O  O     . ILE B 1 306 ? 106.633 149.882 131.184 1.00 36.00 ? 306 ILE B O     1 
ATOM   8012  C  CB    . ILE B 1 306 ? 106.676 146.924 132.715 1.00 28.57 ? 306 ILE B CB    1 
ATOM   8013  C  CG1   . ILE B 1 306 ? 105.588 145.915 133.082 1.00 28.34 ? 306 ILE B CG1   1 
ATOM   8014  C  CG2   . ILE B 1 306 ? 106.746 148.040 133.746 1.00 30.39 ? 306 ILE B CG2   1 
ATOM   8015  C  CD1   . ILE B 1 306 ? 105.835 145.198 134.374 1.00 29.43 ? 306 ILE B CD1   1 
ATOM   8016  N  N     . TYR B 1 307 ? 108.471 148.672 130.721 1.00 30.57 ? 307 TYR B N     1 
ATOM   8017  C  CA    . TYR B 1 307 ? 109.268 149.862 130.445 1.00 31.48 ? 307 TYR B CA    1 
ATOM   8018  C  C     . TYR B 1 307 ? 108.734 150.619 129.236 1.00 34.33 ? 307 TYR B C     1 
ATOM   8019  O  O     . TYR B 1 307 ? 108.713 151.855 129.226 1.00 37.53 ? 307 TYR B O     1 
ATOM   8020  C  CB    . TYR B 1 307 ? 110.730 149.476 130.232 1.00 28.14 ? 307 TYR B CB    1 
ATOM   8021  C  CG    . TYR B 1 307 ? 111.641 150.659 130.011 1.00 35.37 ? 307 TYR B CG    1 
ATOM   8022  C  CD1   . TYR B 1 307 ? 112.067 151.440 131.075 1.00 31.30 ? 307 TYR B CD1   1 
ATOM   8023  C  CD2   . TYR B 1 307 ? 112.069 151.000 128.736 1.00 36.18 ? 307 TYR B CD2   1 
ATOM   8024  C  CE1   . TYR B 1 307 ? 112.896 152.523 130.877 1.00 30.92 ? 307 TYR B CE1   1 
ATOM   8025  C  CE2   . TYR B 1 307 ? 112.898 152.081 128.527 1.00 34.98 ? 307 TYR B CE2   1 
ATOM   8026  C  CZ    . TYR B 1 307 ? 113.309 152.839 129.601 1.00 35.38 ? 307 TYR B CZ    1 
ATOM   8027  O  OH    . TYR B 1 307 ? 114.136 153.918 129.396 1.00 38.89 ? 307 TYR B OH    1 
ATOM   8028  N  N     . LYS B 1 308 ? 108.309 149.895 128.201 1.00 37.11 ? 308 LYS B N     1 
ATOM   8029  C  CA    . LYS B 1 308 ? 107.752 150.543 127.019 1.00 33.06 ? 308 LYS B CA    1 
ATOM   8030  C  C     . LYS B 1 308 ? 106.408 151.191 127.323 1.00 30.18 ? 308 LYS B C     1 
ATOM   8031  O  O     . LYS B 1 308 ? 106.100 152.269 126.802 1.00 35.93 ? 308 LYS B O     1 
ATOM   8032  C  CB    . LYS B 1 308 ? 107.613 149.526 125.888 1.00 31.85 ? 308 LYS B CB    1 
ATOM   8033  C  CG    . LYS B 1 308 ? 108.839 149.410 124.999 1.00 33.57 ? 308 LYS B CG    1 
ATOM   8034  C  CD    . LYS B 1 308 ? 108.917 148.048 124.321 1.00 37.17 ? 308 LYS B CD    1 
ATOM   8035  C  CE    . LYS B 1 308 ? 107.544 147.419 124.143 1.00 36.00 ? 308 LYS B CE    1 
ATOM   8036  N  NZ    . LYS B 1 308 ? 107.616 145.935 124.067 1.00 37.01 ? 308 LYS B NZ    1 
ATOM   8037  N  N     . GLU B 1 309 ? 105.593 150.549 128.161 1.00 32.25 ? 309 GLU B N     1 
ATOM   8038  C  CA    . GLU B 1 309 ? 104.260 151.072 128.439 1.00 35.47 ? 309 GLU B CA    1 
ATOM   8039  C  C     . GLU B 1 309 ? 104.308 152.286 129.360 1.00 38.40 ? 309 GLU B C     1 
ATOM   8040  O  O     . GLU B 1 309 ? 103.576 153.259 129.147 1.00 41.09 ? 309 GLU B O     1 
ATOM   8041  C  CB    . GLU B 1 309 ? 103.387 149.974 129.045 1.00 34.10 ? 309 GLU B CB    1 
ATOM   8042  C  CG    . GLU B 1 309 ? 102.005 150.441 129.470 1.00 37.97 ? 309 GLU B CG    1 
ATOM   8043  C  CD    . GLU B 1 309 ? 101.134 150.851 128.300 1.00 43.10 ? 309 GLU B CD    1 
ATOM   8044  O  OE1   . GLU B 1 309 ? 101.481 150.518 127.148 1.00 43.21 ? 309 GLU B OE1   1 
ATOM   8045  O  OE2   . GLU B 1 309 ? 100.100 151.510 128.534 1.00 41.98 ? 309 GLU B OE2   1 
ATOM   8046  N  N     . TYR B 1 310 ? 105.157 152.253 130.386 1.00 37.38 ? 310 TYR B N     1 
ATOM   8047  C  CA    . TYR B 1 310 ? 105.139 153.277 131.419 1.00 33.84 ? 310 TYR B CA    1 
ATOM   8048  C  C     . TYR B 1 310 ? 106.369 154.170 131.429 1.00 32.84 ? 310 TYR B C     1 
ATOM   8049  O  O     . TYR B 1 310 ? 106.377 155.170 132.155 1.00 36.52 ? 310 TYR B O     1 
ATOM   8050  C  CB    . TYR B 1 310 ? 104.981 152.626 132.801 1.00 35.15 ? 310 TYR B CB    1 
ATOM   8051  C  CG    . TYR B 1 310 ? 103.729 151.791 132.935 1.00 35.66 ? 310 TYR B CG    1 
ATOM   8052  C  CD1   . TYR B 1 310 ? 102.508 152.379 133.229 1.00 33.22 ? 310 TYR B CD1   1 
ATOM   8053  C  CD2   . TYR B 1 310 ? 103.768 150.415 132.760 1.00 32.20 ? 310 TYR B CD2   1 
ATOM   8054  C  CE1   . TYR B 1 310 ? 101.362 151.621 133.348 1.00 35.79 ? 310 TYR B CE1   1 
ATOM   8055  C  CE2   . TYR B 1 310 ? 102.627 149.648 132.876 1.00 32.16 ? 310 TYR B CE2   1 
ATOM   8056  C  CZ    . TYR B 1 310 ? 101.427 150.257 133.172 1.00 36.41 ? 310 TYR B CZ    1 
ATOM   8057  O  OH    . TYR B 1 310 ? 100.287 149.498 133.289 1.00 36.89 ? 310 TYR B OH    1 
ATOM   8058  N  N     . GLY B 1 311 ? 107.401 153.848 130.655 1.00 28.93 ? 311 GLY B N     1 
ATOM   8059  C  CA    . GLY B 1 311 ? 108.622 154.622 130.684 1.00 30.37 ? 311 GLY B CA    1 
ATOM   8060  C  C     . GLY B 1 311 ? 109.479 154.407 131.908 1.00 31.48 ? 311 GLY B C     1 
ATOM   8061  O  O     . GLY B 1 311 ? 110.503 155.083 132.053 1.00 38.54 ? 311 GLY B O     1 
ATOM   8062  N  N     . GLN B 1 312 ? 109.095 153.492 132.793 1.00 32.81 ? 312 GLN B N     1 
ATOM   8063  C  CA    . GLN B 1 312 ? 109.840 153.194 134.003 1.00 30.35 ? 312 GLN B CA    1 
ATOM   8064  C  C     . GLN B 1 312 ? 110.080 151.696 134.083 1.00 31.03 ? 312 GLN B C     1 
ATOM   8065  O  O     . GLN B 1 312 ? 109.275 150.897 133.600 1.00 37.11 ? 312 GLN B O     1 
ATOM   8066  C  CB    . GLN B 1 312 ? 109.093 153.664 135.256 1.00 33.62 ? 312 GLN B CB    1 
ATOM   8067  C  CG    . GLN B 1 312 ? 108.755 155.140 135.264 1.00 35.61 ? 312 GLN B CG    1 
ATOM   8068  C  CD    . GLN B 1 312 ? 107.665 155.475 136.261 1.00 38.30 ? 312 GLN B CD    1 
ATOM   8069  O  OE1   . GLN B 1 312 ? 106.498 155.615 135.897 1.00 37.79 ? 312 GLN B OE1   1 
ATOM   8070  N  NE2   . GLN B 1 312 ? 108.041 155.603 137.527 1.00 36.35 ? 312 GLN B NE2   1 
ATOM   8071  N  N     . HIS B 1 313 ? 111.197 151.322 134.698 1.00 28.60 ? 313 HIS B N     1 
ATOM   8072  C  CA    . HIS B 1 313 ? 111.502 149.914 134.891 1.00 29.53 ? 313 HIS B CA    1 
ATOM   8073  C  C     . HIS B 1 313 ? 110.522 149.290 135.877 1.00 31.98 ? 313 HIS B C     1 
ATOM   8074  O  O     . HIS B 1 313 ? 109.990 149.959 136.765 1.00 33.05 ? 313 HIS B O     1 
ATOM   8075  C  CB    . HIS B 1 313 ? 112.935 149.742 135.390 1.00 27.10 ? 313 HIS B CB    1 
ATOM   8076  C  CG    . HIS B 1 313 ? 113.974 150.105 134.377 1.00 28.38 ? 313 HIS B CG    1 
ATOM   8077  N  ND1   . HIS B 1 313 ? 114.240 149.326 133.272 1.00 31.09 ? 313 HIS B ND1   1 
ATOM   8078  C  CD2   . HIS B 1 313 ? 114.814 151.164 134.302 1.00 28.96 ? 313 HIS B CD2   1 
ATOM   8079  C  CE1   . HIS B 1 313 ? 115.199 149.890 132.560 1.00 28.99 ? 313 HIS B CE1   1 
ATOM   8080  N  NE2   . HIS B 1 313 ? 115.565 151.006 133.164 1.00 32.24 ? 313 HIS B NE2   1 
ATOM   8081  N  N     . MET B 1 314 ? 110.280 147.989 135.705 1.00 34.96 ? 314 MET B N     1 
ATOM   8082  C  CA    . MET B 1 314 ? 109.336 147.295 136.574 1.00 29.66 ? 314 MET B CA    1 
ATOM   8083  C  C     . MET B 1 314 ? 109.809 147.306 138.022 1.00 34.52 ? 314 MET B C     1 
ATOM   8084  O  O     . MET B 1 314 ? 109.001 147.464 138.946 1.00 38.20 ? 314 MET B O     1 
ATOM   8085  C  CB    . MET B 1 314 ? 109.124 145.864 136.079 1.00 27.85 ? 314 MET B CB    1 
ATOM   8086  C  CG    . MET B 1 314 ? 108.345 144.977 137.029 1.00 27.91 ? 314 MET B CG    1 
ATOM   8087  S  SD    . MET B 1 314 ? 108.824 143.244 136.904 1.00 41.91 ? 314 MET B SD    1 
ATOM   8088  C  CE    . MET B 1 314 ? 110.564 143.335 137.318 1.00 35.01 ? 314 MET B CE    1 
ATOM   8089  N  N     . ASP B 1 315 ? 111.113 147.149 138.243 1.00 33.65 ? 315 ASP B N     1 
ATOM   8090  C  CA    . ASP B 1 315 ? 111.656 147.190 139.594 1.00 33.60 ? 315 ASP B CA    1 
ATOM   8091  C  C     . ASP B 1 315 ? 111.792 148.605 140.145 1.00 29.43 ? 315 ASP B C     1 
ATOM   8092  O  O     . ASP B 1 315 ? 112.075 148.762 141.337 1.00 36.46 ? 315 ASP B O     1 
ATOM   8093  C  CB    . ASP B 1 315 ? 112.984 146.400 139.640 1.00 29.57 ? 315 ASP B CB    1 
ATOM   8094  C  CG    . ASP B 1 315 ? 114.234 147.231 139.298 1.00 32.08 ? 315 ASP B CG    1 
ATOM   8095  O  OD1   . ASP B 1 315 ? 114.178 148.453 139.052 1.00 37.15 ? 315 ASP B OD1   1 
ATOM   8096  O  OD2   . ASP B 1 315 ? 115.324 146.622 139.282 1.00 33.40 ? 315 ASP B OD2   1 
ATOM   8097  N  N     . GLU B 1 316 ? 111.595 149.628 139.315 1.00 27.63 ? 316 GLU B N     1 
ATOM   8098  C  CA    . GLU B 1 316 ? 111.575 151.009 139.778 1.00 28.93 ? 316 GLU B CA    1 
ATOM   8099  C  C     . GLU B 1 316 ? 110.207 151.450 140.277 1.00 35.68 ? 316 GLU B C     1 
ATOM   8100  O  O     . GLU B 1 316 ? 110.088 152.559 140.807 1.00 35.95 ? 316 GLU B O     1 
ATOM   8101  C  CB    . GLU B 1 316 ? 112.028 151.945 138.655 1.00 31.52 ? 316 GLU B CB    1 
ATOM   8102  C  CG    . GLU B 1 316 ? 112.974 153.040 139.106 1.00 34.09 ? 316 GLU B CG    1 
ATOM   8103  C  CD    . GLU B 1 316 ? 114.338 152.512 139.478 1.00 37.51 ? 316 GLU B CD    1 
ATOM   8104  O  OE1   . GLU B 1 316 ? 114.779 151.524 138.858 1.00 37.74 ? 316 GLU B OE1   1 
ATOM   8105  O  OE2   . GLU B 1 316 ? 114.970 153.084 140.390 1.00 36.61 ? 316 GLU B OE2   1 
ATOM   8106  N  N     . MET B 1 317 ? 109.181 150.619 140.125 1.00 38.49 ? 317 MET B N     1 
ATOM   8107  C  CA    . MET B 1 317 ? 107.819 150.970 140.490 1.00 36.01 ? 317 MET B CA    1 
ATOM   8108  C  C     . MET B 1 317 ? 107.344 150.119 141.660 1.00 38.49 ? 317 MET B C     1 
ATOM   8109  O  O     . MET B 1 317 ? 107.845 149.019 141.906 1.00 39.19 ? 317 MET B O     1 
ATOM   8110  C  CB    . MET B 1 317 ? 106.874 150.801 139.296 1.00 36.75 ? 317 MET B CB    1 
ATOM   8111  C  CG    . MET B 1 317 ? 107.411 151.384 138.000 1.00 36.74 ? 317 MET B CG    1 
ATOM   8112  S  SD    . MET B 1 317 ? 106.688 150.633 136.531 1.00 46.03 ? 317 MET B SD    1 
ATOM   8113  C  CE    . MET B 1 317 ? 105.220 151.637 136.332 1.00 40.29 ? 317 MET B CE    1 
ATOM   8114  N  N     . ASP B 1 318 ? 106.360 150.649 142.382 1.00 40.76 ? 318 ASP B N     1 
ATOM   8115  C  CA    . ASP B 1 318 ? 105.797 149.969 143.544 1.00 39.14 ? 318 ASP B CA    1 
ATOM   8116  C  C     . ASP B 1 318 ? 104.842 148.884 143.063 1.00 42.56 ? 318 ASP B C     1 
ATOM   8117  O  O     . ASP B 1 318 ? 103.781 149.184 142.506 1.00 44.34 ? 318 ASP B O     1 
ATOM   8118  C  CB    . ASP B 1 318 ? 105.085 150.969 144.450 1.00 40.88 ? 318 ASP B CB    1 
ATOM   8119  C  CG    . ASP B 1 318 ? 104.626 150.350 145.754 1.00 48.06 ? 318 ASP B CG    1 
ATOM   8120  O  OD1   . ASP B 1 318 ? 105.315 149.439 146.259 1.00 45.81 ? 318 ASP B OD1   1 
ATOM   8121  O  OD2   . ASP B 1 318 ? 103.573 150.775 146.274 1.00 49.29 ? 318 ASP B OD2   1 
ATOM   8122  N  N     . MET B 1 319 ? 105.215 147.621 143.278 1.00 40.65 ? 319 MET B N     1 
ATOM   8123  C  CA    . MET B 1 319 ? 104.382 146.517 142.815 1.00 36.15 ? 319 MET B CA    1 
ATOM   8124  C  C     . MET B 1 319 ? 103.049 146.465 143.546 1.00 38.29 ? 319 MET B C     1 
ATOM   8125  O  O     . MET B 1 319 ? 102.058 145.992 142.982 1.00 41.85 ? 319 MET B O     1 
ATOM   8126  C  CB    . MET B 1 319 ? 105.121 145.191 142.976 1.00 35.86 ? 319 MET B CB    1 
ATOM   8127  C  CG    . MET B 1 319 ? 104.568 144.074 142.110 1.00 38.23 ? 319 MET B CG    1 
ATOM   8128  S  SD    . MET B 1 319 ? 104.716 144.414 140.346 1.00 45.63 ? 319 MET B SD    1 
ATOM   8129  C  CE    . MET B 1 319 ? 106.494 144.415 140.159 1.00 40.88 ? 319 MET B CE    1 
ATOM   8130  N  N     . ASN B 1 320 ? 102.997 146.956 144.785 1.00 40.75 ? 320 ASN B N     1 
ATOM   8131  C  CA    . ASN B 1 320 ? 101.756 146.903 145.550 1.00 40.87 ? 320 ASN B CA    1 
ATOM   8132  C  C     . ASN B 1 320 ? 100.655 147.714 144.879 1.00 45.43 ? 320 ASN B C     1 
ATOM   8133  O  O     . ASN B 1 320 ? 99.493  147.291 144.848 1.00 44.52 ? 320 ASN B O     1 
ATOM   8134  C  CB    . ASN B 1 320 ? 102.001 147.395 146.975 1.00 40.86 ? 320 ASN B CB    1 
ATOM   8135  C  CG    . ASN B 1 320 ? 103.039 146.566 147.704 1.00 42.56 ? 320 ASN B CG    1 
ATOM   8136  O  OD1   . ASN B 1 320 ? 102.817 145.391 147.995 1.00 42.41 ? 320 ASN B OD1   1 
ATOM   8137  N  ND2   . ASN B 1 320 ? 104.182 147.173 147.999 1.00 43.38 ? 320 ASN B ND2   1 
ATOM   8138  N  N     . GLU B 1 321 ? 100.998 148.880 144.336 1.00 46.51 ? 321 GLU B N     1 
ATOM   8139  C  CA    . GLU B 1 321 ? 100.019 149.704 143.638 1.00 45.90 ? 321 GLU B CA    1 
ATOM   8140  C  C     . GLU B 1 321 ? 99.968  149.429 142.142 1.00 45.17 ? 321 GLU B C     1 
ATOM   8141  O  O     . GLU B 1 321 ? 98.921  149.637 141.519 1.00 47.22 ? 321 GLU B O     1 
ATOM   8142  C  CB    . GLU B 1 321 ? 100.317 151.188 143.862 1.00 44.77 ? 321 GLU B CB    1 
ATOM   8143  C  CG    . GLU B 1 321 ? 101.665 151.635 143.324 1.00 48.21 ? 321 GLU B CG    1 
ATOM   8144  C  CD    . GLU B 1 321 ? 101.614 153.008 142.682 1.00 51.19 ? 321 GLU B CD    1 
ATOM   8145  O  OE1   . GLU B 1 321 ? 100.498 153.507 142.430 1.00 50.18 ? 321 GLU B OE1   1 
ATOM   8146  O  OE2   . GLU B 1 321 ? 102.691 153.588 142.430 1.00 50.86 ? 321 GLU B OE2   1 
ATOM   8147  N  N     . MET B 1 322 ? 101.066 148.966 141.549 1.00 41.58 ? 322 MET B N     1 
ATOM   8148  C  CA    . MET B 1 322 ? 101.143 148.848 140.102 1.00 37.98 ? 322 MET B CA    1 
ATOM   8149  C  C     . MET B 1 322 ? 100.860 147.440 139.594 1.00 37.87 ? 322 MET B C     1 
ATOM   8150  O  O     . MET B 1 322 ? 100.796 147.248 138.377 1.00 46.18 ? 322 MET B O     1 
ATOM   8151  C  CB    . MET B 1 322 ? 102.526 149.288 139.608 1.00 38.18 ? 322 MET B CB    1 
ATOM   8152  C  CG    . MET B 1 322 ? 102.695 150.797 139.476 1.00 40.51 ? 322 MET B CG    1 
ATOM   8153  S  SD    . MET B 1 322 ? 101.502 151.628 138.411 1.00 49.67 ? 322 MET B SD    1 
ATOM   8154  C  CE    . MET B 1 322 ? 101.604 150.654 136.918 1.00 40.38 ? 322 MET B CE    1 
ATOM   8155  N  N     . TYR B 1 323 ? 100.699 146.455 140.481 1.00 37.96 ? 323 TYR B N     1 
ATOM   8156  C  CA    . TYR B 1 323 ? 100.509 145.076 140.039 1.00 34.89 ? 323 TYR B CA    1 
ATOM   8157  C  C     . TYR B 1 323 ? 99.190  144.908 139.295 1.00 39.41 ? 323 TYR B C     1 
ATOM   8158  O  O     . TYR B 1 323 ? 99.134  144.251 138.249 1.00 41.79 ? 323 TYR B O     1 
ATOM   8159  C  CB    . TYR B 1 323 ? 100.576 144.129 141.238 1.00 35.78 ? 323 TYR B CB    1 
ATOM   8160  C  CG    . TYR B 1 323 ? 100.265 142.687 140.905 1.00 38.20 ? 323 TYR B CG    1 
ATOM   8161  C  CD1   . TYR B 1 323 ? 101.242 141.843 140.396 1.00 33.19 ? 323 TYR B CD1   1 
ATOM   8162  C  CD2   . TYR B 1 323 ? 98.992  142.168 141.106 1.00 37.78 ? 323 TYR B CD2   1 
ATOM   8163  C  CE1   . TYR B 1 323 ? 100.958 140.526 140.095 1.00 30.45 ? 323 TYR B CE1   1 
ATOM   8164  C  CE2   . TYR B 1 323 ? 98.701  140.855 140.806 1.00 33.79 ? 323 TYR B CE2   1 
ATOM   8165  C  CZ    . TYR B 1 323 ? 99.687  140.039 140.302 1.00 33.87 ? 323 TYR B CZ    1 
ATOM   8166  O  OH    . TYR B 1 323 ? 99.398  138.730 140.002 1.00 37.46 ? 323 TYR B OH    1 
ATOM   8167  N  N     . ASP B 1 324 ? 98.114  145.489 139.827 1.00 43.12 ? 324 ASP B N     1 
ATOM   8168  C  CA    . ASP B 1 324 ? 96.821  145.391 139.160 1.00 40.21 ? 324 ASP B CA    1 
ATOM   8169  C  C     . ASP B 1 324 ? 96.843  146.104 137.816 1.00 42.31 ? 324 ASP B C     1 
ATOM   8170  O  O     . ASP B 1 324 ? 96.245  145.631 136.844 1.00 46.15 ? 324 ASP B O     1 
ATOM   8171  C  CB    . ASP B 1 324 ? 95.724  145.959 140.057 1.00 42.68 ? 324 ASP B CB    1 
ATOM   8172  C  CG    . ASP B 1 324 ? 95.501  145.124 141.300 1.00 45.14 ? 324 ASP B CG    1 
ATOM   8173  O  OD1   . ASP B 1 324 ? 95.599  143.883 141.206 1.00 44.49 ? 324 ASP B OD1   1 
ATOM   8174  O  OD2   . ASP B 1 324 ? 95.227  145.705 142.370 1.00 45.82 ? 324 ASP B OD2   1 
ATOM   8175  N  N     . LYS B 1 325 ? 97.522  147.251 137.744 1.00 42.42 ? 325 LYS B N     1 
ATOM   8176  C  CA    . LYS B 1 325 ? 97.634  147.968 136.479 1.00 42.13 ? 325 LYS B CA    1 
ATOM   8177  C  C     . LYS B 1 325 ? 98.449  147.175 135.464 1.00 41.27 ? 325 LYS B C     1 
ATOM   8178  O  O     . LYS B 1 325 ? 98.128  147.172 134.271 1.00 45.94 ? 325 LYS B O     1 
ATOM   8179  C  CB    . LYS B 1 325 ? 98.249  149.345 136.716 1.00 40.03 ? 325 LYS B CB    1 
ATOM   8180  C  CG    . LYS B 1 325 ? 97.480  150.187 137.718 1.00 38.94 ? 325 LYS B CG    1 
ATOM   8181  C  CD    . LYS B 1 325 ? 97.413  151.641 137.291 1.00 43.93 ? 325 LYS B CD    1 
ATOM   8182  C  CE    . LYS B 1 325 ? 98.046  152.550 138.329 1.00 44.07 ? 325 LYS B CE    1 
ATOM   8183  N  NZ    . LYS B 1 325 ? 97.271  152.567 139.598 1.00 45.07 ? 325 LYS B NZ    1 
ATOM   8184  N  N     . PHE B 1 326 ? 99.514  146.508 135.917 1.00 39.06 ? 326 PHE B N     1 
ATOM   8185  C  CA    . PHE B 1 326 ? 100.265 145.615 135.039 1.00 36.63 ? 326 PHE B CA    1 
ATOM   8186  C  C     . PHE B 1 326 ? 99.385  144.491 134.513 1.00 36.96 ? 326 PHE B C     1 
ATOM   8187  O  O     . PHE B 1 326 ? 99.400  144.190 133.315 1.00 42.61 ? 326 PHE B O     1 
ATOM   8188  C  CB    . PHE B 1 326 ? 101.467 145.027 135.782 1.00 35.81 ? 326 PHE B CB    1 
ATOM   8189  C  CG    . PHE B 1 326 ? 102.541 146.022 136.110 1.00 33.78 ? 326 PHE B CG    1 
ATOM   8190  C  CD1   . PHE B 1 326 ? 102.595 147.249 135.476 1.00 35.17 ? 326 PHE B CD1   1 
ATOM   8191  C  CD2   . PHE B 1 326 ? 103.499 145.724 137.065 1.00 36.38 ? 326 PHE B CD2   1 
ATOM   8192  C  CE1   . PHE B 1 326 ? 103.591 148.154 135.779 1.00 34.31 ? 326 PHE B CE1   1 
ATOM   8193  C  CE2   . PHE B 1 326 ? 104.492 146.628 137.376 1.00 38.89 ? 326 PHE B CE2   1 
ATOM   8194  C  CZ    . PHE B 1 326 ? 104.537 147.845 136.732 1.00 38.73 ? 326 PHE B CZ    1 
ATOM   8195  N  N     . VAL B 1 327 ? 98.612  143.859 135.397 1.00 40.84 ? 327 VAL B N     1 
ATOM   8196  C  CA    . VAL B 1 327 ? 97.799  142.715 134.993 1.00 42.78 ? 327 VAL B CA    1 
ATOM   8197  C  C     . VAL B 1 327 ? 96.702  143.147 134.026 1.00 42.46 ? 327 VAL B C     1 
ATOM   8198  O  O     . VAL B 1 327 ? 96.443  142.475 133.021 1.00 44.18 ? 327 VAL B O     1 
ATOM   8199  C  CB    . VAL B 1 327 ? 97.224  142.007 136.233 1.00 38.73 ? 327 VAL B CB    1 
ATOM   8200  C  CG1   . VAL B 1 327 ? 96.207  140.955 135.824 1.00 40.60 ? 327 VAL B CG1   1 
ATOM   8201  C  CG2   . VAL B 1 327 ? 98.341  141.378 137.045 1.00 33.71 ? 327 VAL B CG2   1 
ATOM   8202  N  N     . ASP B 1 328 ? 96.050  144.274 134.305 1.00 43.82 ? 328 ASP B N     1 
ATOM   8203  C  CA    . ASP B 1 328 ? 94.958  144.753 133.470 1.00 44.54 ? 328 ASP B CA    1 
ATOM   8204  C  C     . ASP B 1 328 ? 95.433  145.435 132.195 1.00 44.14 ? 328 ASP B C     1 
ATOM   8205  O  O     . ASP B 1 328 ? 94.606  145.717 131.322 1.00 47.88 ? 328 ASP B O     1 
ATOM   8206  C  CB    . ASP B 1 328 ? 94.074  145.718 134.263 1.00 45.16 ? 328 ASP B CB    1 
ATOM   8207  C  CG    . ASP B 1 328 ? 93.221  145.010 135.295 1.00 50.58 ? 328 ASP B CG    1 
ATOM   8208  O  OD1   . ASP B 1 328 ? 93.086  143.772 135.207 1.00 49.99 ? 328 ASP B OD1   1 
ATOM   8209  O  OD2   . ASP B 1 328 ? 92.685  145.691 136.194 1.00 49.40 ? 328 ASP B OD2   1 
ATOM   8210  N  N     . ASN B 1 329 ? 96.724  145.710 132.065 1.00 39.43 ? 329 ASN B N     1 
ATOM   8211  C  CA    . ASN B 1 329 ? 97.235  146.351 130.861 1.00 39.38 ? 329 ASN B CA    1 
ATOM   8212  C  C     . ASN B 1 329 ? 97.440  145.308 129.771 1.00 45.15 ? 329 ASN B C     1 
ATOM   8213  O  O     . ASN B 1 329 ? 98.257  144.397 129.946 1.00 42.97 ? 329 ASN B O     1 
ATOM   8214  C  CB    . ASN B 1 329 ? 98.545  147.068 131.151 1.00 36.90 ? 329 ASN B CB    1 
ATOM   8215  C  CG    . ASN B 1 329 ? 98.833  148.177 130.162 1.00 41.00 ? 329 ASN B CG    1 
ATOM   8216  O  OD1   . ASN B 1 329 ? 99.207  147.922 129.019 1.00 44.11 ? 329 ASN B OD1   1 
ATOM   8217  N  ND2   . ASN B 1 329 ? 98.662  149.418 130.598 1.00 39.31 ? 329 ASN B ND2   1 
ATOM   8218  N  N     . PRO B 1 330 ? 96.725  145.393 128.645 1.00 46.47 ? 330 PRO B N     1 
ATOM   8219  C  CA    . PRO B 1 330 ? 96.950  144.425 127.561 1.00 42.62 ? 330 PRO B CA    1 
ATOM   8220  C  C     . PRO B 1 330 ? 98.312  144.551 126.907 1.00 40.34 ? 330 PRO B C     1 
ATOM   8221  O  O     . PRO B 1 330 ? 98.801  143.565 126.341 1.00 43.15 ? 330 PRO B O     1 
ATOM   8222  C  CB    . PRO B 1 330 ? 95.824  144.741 126.569 1.00 43.87 ? 330 PRO B CB    1 
ATOM   8223  C  CG    . PRO B 1 330 ? 95.484  146.166 126.836 1.00 42.73 ? 330 PRO B CG    1 
ATOM   8224  C  CD    . PRO B 1 330 ? 95.675  146.369 128.309 1.00 41.04 ? 330 PRO B CD    1 
ATOM   8225  N  N     . ARG B 1 331 ? 98.939  145.725 126.962 1.00 38.46 ? 331 ARG B N     1 
ATOM   8226  C  CA    . ARG B 1 331 ? 100.242 145.934 126.347 1.00 41.37 ? 331 ARG B CA    1 
ATOM   8227  C  C     . ARG B 1 331 ? 101.392 145.460 127.224 1.00 40.66 ? 331 ARG B C     1 
ATOM   8228  O  O     . ARG B 1 331 ? 102.545 145.498 126.782 1.00 39.97 ? 331 ARG B O     1 
ATOM   8229  C  CB    . ARG B 1 331 ? 100.425 147.413 126.001 1.00 39.61 ? 331 ARG B CB    1 
ATOM   8230  C  CG    . ARG B 1 331 ? 99.314  147.975 125.130 1.00 39.47 ? 331 ARG B CG    1 
ATOM   8231  C  CD    . ARG B 1 331 ? 99.391  149.494 125.037 1.00 39.72 ? 331 ARG B CD    1 
ATOM   8232  N  NE    . ARG B 1 331 ? 98.667  150.203 126.091 1.00 39.26 ? 331 ARG B NE    1 
ATOM   8233  C  CZ    . ARG B 1 331 ? 97.411  149.982 126.462 1.00 42.33 ? 331 ARG B CZ    1 
ATOM   8234  N  NH1   . ARG B 1 331 ? 96.633  149.125 125.821 1.00 42.93 ? 331 ARG B NH1   1 
ATOM   8235  N  NH2   . ARG B 1 331 ? 96.912  150.662 127.490 1.00 40.12 ? 331 ARG B NH2   1 
ATOM   8236  N  N     . VAL B 1 332 ? 101.110 145.023 128.446 1.00 37.22 ? 332 VAL B N     1 
ATOM   8237  C  CA    . VAL B 1 332 ? 102.109 144.436 129.330 1.00 34.25 ? 332 VAL B CA    1 
ATOM   8238  C  C     . VAL B 1 332 ? 101.992 142.923 129.220 1.00 37.72 ? 332 VAL B C     1 
ATOM   8239  O  O     . VAL B 1 332 ? 100.916 142.358 129.449 1.00 39.09 ? 332 VAL B O     1 
ATOM   8240  C  CB    . VAL B 1 332 ? 101.923 144.907 130.781 1.00 34.76 ? 332 VAL B CB    1 
ATOM   8241  C  CG1   . VAL B 1 332 ? 102.717 144.027 131.731 1.00 36.47 ? 332 VAL B CG1   1 
ATOM   8242  C  CG2   . VAL B 1 332 ? 102.338 146.362 130.925 1.00 34.06 ? 332 VAL B CG2   1 
ATOM   8243  N  N     . LYS B 1 333 ? 103.089 142.266 128.860 1.00 34.00 ? 333 LYS B N     1 
ATOM   8244  C  CA    . LYS B 1 333 ? 103.100 140.822 128.688 1.00 30.44 ? 333 LYS B CA    1 
ATOM   8245  C  C     . LYS B 1 333 ? 103.399 140.137 130.015 1.00 33.51 ? 333 LYS B C     1 
ATOM   8246  O  O     . LYS B 1 333 ? 104.261 140.581 130.778 1.00 34.54 ? 333 LYS B O     1 
ATOM   8247  C  CB    . LYS B 1 333 ? 104.131 140.414 127.636 1.00 30.09 ? 333 LYS B CB    1 
ATOM   8248  C  CG    . LYS B 1 333 ? 103.947 139.007 127.100 1.00 35.83 ? 333 LYS B CG    1 
ATOM   8249  C  CD    . LYS B 1 333 ? 105.092 138.615 126.183 1.00 36.12 ? 333 LYS B CD    1 
ATOM   8250  C  CE    . LYS B 1 333 ? 104.972 137.167 125.745 1.00 36.73 ? 333 LYS B CE    1 
ATOM   8251  N  NZ    . LYS B 1 333 ? 106.076 136.775 124.830 1.00 38.17 ? 333 LYS B NZ    1 
ATOM   8252  N  N     . LYS B 1 334 ? 102.679 139.050 130.285 1.00 36.10 ? 334 LYS B N     1 
ATOM   8253  C  CA    . LYS B 1 334 ? 102.806 138.350 131.554 1.00 33.33 ? 334 LYS B CA    1 
ATOM   8254  C  C     . LYS B 1 334 ? 102.479 136.878 131.357 1.00 35.06 ? 334 LYS B C     1 
ATOM   8255  O  O     . LYS B 1 334 ? 101.828 136.492 130.384 1.00 39.90 ? 334 LYS B O     1 
ATOM   8256  C  CB    . LYS B 1 334 ? 101.884 138.954 132.617 1.00 34.20 ? 334 LYS B CB    1 
ATOM   8257  C  CG    . LYS B 1 334 ? 100.425 138.989 132.205 1.00 34.68 ? 334 LYS B CG    1 
ATOM   8258  C  CD    . LYS B 1 334 ? 99.667  140.070 132.942 1.00 33.88 ? 334 LYS B CD    1 
ATOM   8259  C  CE    . LYS B 1 334 ? 99.544  141.318 132.093 1.00 37.07 ? 334 LYS B CE    1 
ATOM   8260  N  NZ    . LYS B 1 334 ? 98.567  141.156 130.984 1.00 37.72 ? 334 LYS B NZ    1 
ATOM   8261  N  N     . GLU B 1 335 ? 102.947 136.056 132.295 1.00 37.98 ? 335 GLU B N     1 
ATOM   8262  C  CA    . GLU B 1 335 ? 102.590 134.646 132.348 1.00 40.04 ? 335 GLU B CA    1 
ATOM   8263  C  C     . GLU B 1 335 ? 102.101 134.291 133.742 1.00 40.51 ? 335 GLU B C     1 
ATOM   8264  O  O     . GLU B 1 335 ? 102.655 134.754 134.742 1.00 44.14 ? 335 GLU B O     1 
ATOM   8265  C  CB    . GLU B 1 335 ? 103.761 133.733 131.973 1.00 37.26 ? 335 GLU B CB    1 
ATOM   8266  C  CG    . GLU B 1 335 ? 104.776 134.348 131.041 1.00 44.07 ? 335 GLU B CG    1 
ATOM   8267  C  CD    . GLU B 1 335 ? 105.613 133.298 130.340 1.00 45.15 ? 335 GLU B CD    1 
ATOM   8268  O  OE1   . GLU B 1 335 ? 106.344 132.558 131.031 1.00 42.70 ? 335 GLU B OE1   1 
ATOM   8269  O  OE2   . GLU B 1 335 ? 105.540 133.214 129.096 1.00 42.19 ? 335 GLU B OE2   1 
ATOM   8270  N  N     . LYS B 1 336 ? 101.059 133.467 133.797 1.00 38.14 ? 336 LYS B N     1 
ATOM   8271  C  CA    . LYS B 1 336 ? 100.512 133.027 135.071 1.00 31.84 ? 336 LYS B CA    1 
ATOM   8272  C  C     . LYS B 1 336 ? 101.500 132.125 135.798 1.00 36.47 ? 336 LYS B C     1 
ATOM   8273  O  O     . LYS B 1 336 ? 102.154 131.273 135.191 1.00 39.12 ? 336 LYS B O     1 
ATOM   8274  C  CB    . LYS B 1 336 ? 99.195  132.284 134.856 1.00 39.50 ? 336 LYS B CB    1 
ATOM   8275  C  CG    . LYS B 1 336 ? 98.349  132.149 136.108 1.00 40.69 ? 336 LYS B CG    1 
ATOM   8276  C  CD    . LYS B 1 336 ? 97.463  133.362 136.305 1.00 42.23 ? 336 LYS B CD    1 
ATOM   8277  C  CE    . LYS B 1 336 ? 96.111  133.165 135.642 1.00 40.57 ? 336 LYS B CE    1 
ATOM   8278  N  NZ    . LYS B 1 336 ? 95.177  132.392 136.505 1.00 40.73 ? 336 LYS B NZ    1 
ATOM   8279  N  N     . ILE B 1 337 ? 101.608 132.323 137.111 1.00 37.59 ? 337 ILE B N     1 
ATOM   8280  C  CA    . ILE B 1 337 ? 102.383 131.456 137.986 1.00 37.13 ? 337 ILE B CA    1 
ATOM   8281  C  C     . ILE B 1 337 ? 101.547 131.161 139.223 1.00 38.78 ? 337 ILE B C     1 
ATOM   8282  O  O     . ILE B 1 337 ? 100.553 131.830 139.505 1.00 43.11 ? 337 ILE B O     1 
ATOM   8283  C  CB    . ILE B 1 337 ? 103.739 132.072 138.390 1.00 35.79 ? 337 ILE B CB    1 
ATOM   8284  C  CG1   . ILE B 1 337 ? 103.528 133.428 139.066 1.00 36.00 ? 337 ILE B CG1   1 
ATOM   8285  C  CG2   . ILE B 1 337 ? 104.660 132.191 137.188 1.00 37.09 ? 337 ILE B CG2   1 
ATOM   8286  C  CD1   . ILE B 1 337 ? 104.521 133.725 140.162 1.00 33.72 ? 337 ILE B CD1   1 
ATOM   8287  N  N     . ASN B 1 338 ? 101.963 130.138 139.962 1.00 37.91 ? 338 ASN B N     1 
ATOM   8288  C  CA    . ASN B 1 338 ? 101.372 129.856 141.258 1.00 34.63 ? 338 ASN B CA    1 
ATOM   8289  C  C     . ASN B 1 338 ? 102.315 130.373 142.331 1.00 35.37 ? 338 ASN B C     1 
ATOM   8290  O  O     . ASN B 1 338 ? 103.399 129.798 142.514 1.00 40.26 ? 338 ASN B O     1 
ATOM   8291  C  CB    . ASN B 1 338 ? 101.127 128.360 141.433 1.00 35.38 ? 338 ASN B CB    1 
ATOM   8292  C  CG    . ASN B 1 338 ? 100.102 128.058 142.507 1.00 38.03 ? 338 ASN B CG    1 
ATOM   8293  O  OD1   . ASN B 1 338 ? 99.651  128.954 143.220 1.00 39.71 ? 338 ASN B OD1   1 
ATOM   8294  N  ND2   . ASN B 1 338 ? 99.726  126.791 142.627 1.00 38.46 ? 338 ASN B ND2   1 
ATOM   8295  N  N     . PRO B 1 339 ? 101.974 131.451 143.040 1.00 35.97 ? 339 PRO B N     1 
ATOM   8296  C  CA    . PRO B 1 339 ? 102.905 131.989 144.044 1.00 34.72 ? 339 PRO B CA    1 
ATOM   8297  C  C     . PRO B 1 339 ? 103.227 131.013 145.159 1.00 33.48 ? 339 PRO B C     1 
ATOM   8298  O  O     . PRO B 1 339 ? 104.356 131.017 145.664 1.00 35.85 ? 339 PRO B O     1 
ATOM   8299  C  CB    . PRO B 1 339 ? 102.173 133.231 144.569 1.00 33.29 ? 339 PRO B CB    1 
ATOM   8300  C  CG    . PRO B 1 339 ? 100.742 132.976 144.277 1.00 36.57 ? 339 PRO B CG    1 
ATOM   8301  C  CD    . PRO B 1 339 ? 100.715 132.210 142.993 1.00 36.20 ? 339 PRO B CD    1 
ATOM   8302  N  N     . ARG B 1 340 ? 102.272 130.173 145.563 1.00 33.87 ? 340 ARG B N     1 
ATOM   8303  C  CA    . ARG B 1 340 ? 102.566 129.166 146.577 1.00 32.28 ? 340 ARG B CA    1 
ATOM   8304  C  C     . ARG B 1 340 ? 103.527 128.115 146.042 1.00 33.08 ? 340 ARG B C     1 
ATOM   8305  O  O     . ARG B 1 340 ? 104.425 127.663 146.760 1.00 38.27 ? 340 ARG B O     1 
ATOM   8306  C  CB    . ARG B 1 340 ? 101.275 128.517 147.069 1.00 31.67 ? 340 ARG B CB    1 
ATOM   8307  C  CG    . ARG B 1 340 ? 100.454 129.414 147.969 1.00 30.84 ? 340 ARG B CG    1 
ATOM   8308  C  CD    . ARG B 1 340 ? 99.524  128.616 148.860 1.00 32.16 ? 340 ARG B CD    1 
ATOM   8309  N  NE    . ARG B 1 340 ? 98.609  129.487 149.586 1.00 33.87 ? 340 ARG B NE    1 
ATOM   8310  C  CZ    . ARG B 1 340 ? 97.694  129.064 150.446 1.00 35.36 ? 340 ARG B CZ    1 
ATOM   8311  N  NH1   . ARG B 1 340 ? 97.545  127.779 150.720 1.00 34.83 ? 340 ARG B NH1   1 
ATOM   8312  N  NH2   . ARG B 1 340 ? 96.909  129.953 151.047 1.00 35.92 ? 340 ARG B NH2   1 
ATOM   8313  N  N     . LYS B 1 341 ? 103.357 127.715 144.780 1.00 34.38 ? 341 LYS B N     1 
ATOM   8314  C  CA    . LYS B 1 341 ? 104.302 126.786 144.173 1.00 33.81 ? 341 LYS B CA    1 
ATOM   8315  C  C     . LYS B 1 341 ? 105.683 127.414 144.050 1.00 31.86 ? 341 LYS B C     1 
ATOM   8316  O  O     . LYS B 1 341 ? 106.696 126.734 144.238 1.00 33.01 ? 341 LYS B O     1 
ATOM   8317  C  CB    . LYS B 1 341 ? 103.792 126.328 142.807 1.00 36.28 ? 341 LYS B CB    1 
ATOM   8318  C  CG    . LYS B 1 341 ? 102.697 125.272 142.869 1.00 38.18 ? 341 LYS B CG    1 
ATOM   8319  C  CD    . LYS B 1 341 ? 102.802 124.424 144.128 1.00 39.43 ? 341 LYS B CD    1 
ATOM   8320  C  CE    . LYS B 1 341 ? 101.797 123.286 144.117 1.00 40.53 ? 341 LYS B CE    1 
ATOM   8321  N  NZ    . LYS B 1 341 ? 102.443 121.978 144.409 1.00 39.32 ? 341 LYS B NZ    1 
ATOM   8322  N  N     . LEU B 1 342 ? 105.745 128.710 143.737 1.00 31.77 ? 342 LEU B N     1 
ATOM   8323  C  CA    . LEU B 1 342 ? 107.033 129.394 143.689 1.00 29.22 ? 342 LEU B CA    1 
ATOM   8324  C  C     . LEU B 1 342 ? 107.680 129.451 145.069 1.00 30.35 ? 342 LEU B C     1 
ATOM   8325  O  O     . LEU B 1 342 ? 108.897 129.283 145.195 1.00 36.89 ? 342 LEU B O     1 
ATOM   8326  C  CB    . LEU B 1 342 ? 106.863 130.798 143.111 1.00 29.48 ? 342 LEU B CB    1 
ATOM   8327  C  CG    . LEU B 1 342 ? 108.134 131.464 142.580 1.00 29.06 ? 342 LEU B CG    1 
ATOM   8328  C  CD1   . LEU B 1 342 ? 108.955 130.480 141.766 1.00 28.67 ? 342 LEU B CD1   1 
ATOM   8329  C  CD2   . LEU B 1 342 ? 107.795 132.690 141.750 1.00 27.16 ? 342 LEU B CD2   1 
ATOM   8330  N  N     . LEU B 1 343 ? 106.884 129.688 146.114 1.00 28.31 ? 343 LEU B N     1 
ATOM   8331  C  CA    . LEU B 1 343 ? 107.417 129.676 147.474 1.00 30.02 ? 343 LEU B CA    1 
ATOM   8332  C  C     . LEU B 1 343 ? 107.939 128.295 147.852 1.00 28.74 ? 343 LEU B C     1 
ATOM   8333  O  O     . LEU B 1 343 ? 108.998 128.170 148.481 1.00 31.19 ? 343 LEU B O     1 
ATOM   8334  C  CB    . LEU B 1 343 ? 106.340 130.124 148.460 1.00 31.35 ? 343 LEU B CB    1 
ATOM   8335  C  CG    . LEU B 1 343 ? 106.317 131.602 148.841 1.00 31.68 ? 343 LEU B CG    1 
ATOM   8336  C  CD1   . LEU B 1 343 ? 105.165 131.880 149.788 1.00 26.65 ? 343 LEU B CD1   1 
ATOM   8337  C  CD2   . LEU B 1 343 ? 107.638 132.015 149.465 1.00 32.39 ? 343 LEU B CD2   1 
ATOM   8338  N  N     . GLU B 1 344 ? 107.200 127.246 147.490 1.00 33.76 ? 344 GLU B N     1 
ATOM   8339  C  CA    . GLU B 1 344 ? 107.657 125.889 147.770 1.00 33.11 ? 344 GLU B CA    1 
ATOM   8340  C  C     . GLU B 1 344 ? 108.928 125.568 146.997 1.00 30.28 ? 344 GLU B C     1 
ATOM   8341  O  O     . GLU B 1 344 ? 109.816 124.881 147.512 1.00 34.25 ? 344 GLU B O     1 
ATOM   8342  C  CB    . GLU B 1 344 ? 106.553 124.885 147.444 1.00 33.83 ? 344 GLU B CB    1 
ATOM   8343  C  CG    . GLU B 1 344 ? 105.302 125.052 148.288 1.00 35.22 ? 344 GLU B CG    1 
ATOM   8344  C  CD    . GLU B 1 344 ? 104.166 124.165 147.824 1.00 42.95 ? 344 GLU B CD    1 
ATOM   8345  O  OE1   . GLU B 1 344 ? 104.446 123.084 147.266 1.00 42.65 ? 344 GLU B OE1   1 
ATOM   8346  O  OE2   . GLU B 1 344 ? 102.993 124.550 148.015 1.00 40.70 ? 344 GLU B OE2   1 
ATOM   8347  N  N     . LYS B 1 345 ? 109.032 126.054 145.760 1.00 29.85 ? 345 LYS B N     1 
ATOM   8348  C  CA    . LYS B 1 345 ? 110.258 125.879 144.989 1.00 27.81 ? 345 LYS B CA    1 
ATOM   8349  C  C     . LYS B 1 345 ? 111.425 126.607 145.642 1.00 32.02 ? 345 LYS B C     1 
ATOM   8350  O  O     . LYS B 1 345 ? 112.547 126.089 145.677 1.00 34.31 ? 345 LYS B O     1 
ATOM   8351  C  CB    . LYS B 1 345 ? 110.047 126.370 143.558 1.00 29.42 ? 345 LYS B CB    1 
ATOM   8352  C  CG    . LYS B 1 345 ? 111.245 126.184 142.651 1.00 30.39 ? 345 LYS B CG    1 
ATOM   8353  C  CD    . LYS B 1 345 ? 110.952 126.678 141.248 1.00 30.22 ? 345 LYS B CD    1 
ATOM   8354  C  CE    . LYS B 1 345 ? 112.182 126.579 140.367 1.00 33.31 ? 345 LYS B CE    1 
ATOM   8355  N  NZ    . LYS B 1 345 ? 111.938 127.136 139.011 1.00 33.41 ? 345 LYS B NZ    1 
ATOM   8356  N  N     . LEU B 1 346 ? 111.178 127.809 146.167 1.00 31.48 ? 346 LEU B N     1 
ATOM   8357  C  CA    . LEU B 1 346 ? 112.213 128.535 146.895 1.00 26.92 ? 346 LEU B CA    1 
ATOM   8358  C  C     . LEU B 1 346 ? 112.682 127.743 148.106 1.00 26.20 ? 346 LEU B C     1 
ATOM   8359  O  O     . LEU B 1 346 ? 113.886 127.609 148.347 1.00 27.55 ? 346 LEU B O     1 
ATOM   8360  C  CB    . LEU B 1 346 ? 111.691 129.904 147.332 1.00 27.04 ? 346 LEU B CB    1 
ATOM   8361  C  CG    . LEU B 1 346 ? 111.441 130.972 146.270 1.00 26.52 ? 346 LEU B CG    1 
ATOM   8362  C  CD1   . LEU B 1 346 ? 110.822 132.203 146.905 1.00 29.36 ? 346 LEU B CD1   1 
ATOM   8363  C  CD2   . LEU B 1 346 ? 112.729 131.327 145.564 1.00 27.17 ? 346 LEU B CD2   1 
ATOM   8364  N  N     . ALA B 1 347 ? 111.737 127.208 148.881 1.00 26.80 ? 347 ALA B N     1 
ATOM   8365  C  CA    . ALA B 1 347 ? 112.102 126.445 150.071 1.00 21.70 ? 347 ALA B CA    1 
ATOM   8366  C  C     . ALA B 1 347 ? 112.859 125.174 149.705 1.00 27.52 ? 347 ALA B C     1 
ATOM   8367  O  O     . ALA B 1 347 ? 113.823 124.801 150.381 1.00 33.07 ? 347 ALA B O     1 
ATOM   8368  C  CB    . ALA B 1 347 ? 110.855 126.113 150.886 1.00 21.51 ? 347 ALA B CB    1 
ATOM   8369  N  N     . MET B 1 348 ? 112.433 124.494 148.638 1.00 32.08 ? 348 MET B N     1 
ATOM   8370  C  CA    . MET B 1 348 ? 113.133 123.296 148.187 1.00 30.91 ? 348 MET B CA    1 
ATOM   8371  C  C     . MET B 1 348 ? 114.554 123.621 147.750 1.00 31.93 ? 348 MET B C     1 
ATOM   8372  O  O     . MET B 1 348 ? 115.498 122.894 148.083 1.00 36.77 ? 348 MET B O     1 
ATOM   8373  C  CB    . MET B 1 348 ? 112.348 122.640 147.050 1.00 33.57 ? 348 MET B CB    1 
ATOM   8374  C  CG    . MET B 1 348 ? 113.075 121.513 146.335 1.00 38.43 ? 348 MET B CG    1 
ATOM   8375  S  SD    . MET B 1 348 ? 113.839 122.036 144.786 1.00 54.46 ? 348 MET B SD    1 
ATOM   8376  C  CE    . MET B 1 348 ? 112.518 122.993 144.049 1.00 36.42 ? 348 MET B CE    1 
ATOM   8377  N  N     . LEU B 1 349 ? 114.729 124.719 147.014 1.00 28.07 ? 349 LEU B N     1 
ATOM   8378  C  CA    . LEU B 1 349 ? 116.061 125.116 146.577 1.00 27.22 ? 349 LEU B CA    1 
ATOM   8379  C  C     . LEU B 1 349 ? 116.945 125.485 147.761 1.00 28.40 ? 349 LEU B C     1 
ATOM   8380  O  O     . LEU B 1 349 ? 118.138 125.167 147.774 1.00 31.89 ? 349 LEU B O     1 
ATOM   8381  C  CB    . LEU B 1 349 ? 115.959 126.281 145.598 1.00 28.44 ? 349 LEU B CB    1 
ATOM   8382  C  CG    . LEU B 1 349 ? 115.898 125.890 144.125 1.00 32.55 ? 349 LEU B CG    1 
ATOM   8383  C  CD1   . LEU B 1 349 ? 115.101 126.918 143.359 1.00 33.02 ? 349 LEU B CD1   1 
ATOM   8384  C  CD2   . LEU B 1 349 ? 117.295 125.752 143.550 1.00 32.50 ? 349 LEU B CD2   1 
ATOM   8385  N  N     . ARG B 1 350 ? 116.382 126.171 148.758 1.00 27.14 ? 350 ARG B N     1 
ATOM   8386  C  CA    . ARG B 1 350 ? 117.167 126.521 149.938 1.00 23.59 ? 350 ARG B CA    1 
ATOM   8387  C  C     . ARG B 1 350 ? 117.539 125.290 150.751 1.00 29.96 ? 350 ARG B C     1 
ATOM   8388  O  O     . ARG B 1 350 ? 118.640 125.228 151.309 1.00 38.33 ? 350 ARG B O     1 
ATOM   8389  C  CB    . ARG B 1 350 ? 116.408 127.525 150.805 1.00 25.41 ? 350 ARG B CB    1 
ATOM   8390  C  CG    . ARG B 1 350 ? 116.048 128.814 150.092 1.00 25.34 ? 350 ARG B CG    1 
ATOM   8391  C  CD    . ARG B 1 350 ? 115.673 129.899 151.074 1.00 26.00 ? 350 ARG B CD    1 
ATOM   8392  N  NE    . ARG B 1 350 ? 116.787 130.806 151.317 1.00 32.21 ? 350 ARG B NE    1 
ATOM   8393  C  CZ    . ARG B 1 350 ? 117.166 131.219 152.517 1.00 28.27 ? 350 ARG B CZ    1 
ATOM   8394  N  NH1   . ARG B 1 350 ? 116.556 130.805 153.614 1.00 26.80 ? 350 ARG B NH1   1 
ATOM   8395  N  NH2   . ARG B 1 350 ? 118.188 132.064 152.619 1.00 30.25 ? 350 ARG B NH2   1 
ATOM   8396  N  N     . SER B 1 351 ? 116.639 124.309 150.842 1.00 32.86 ? 351 SER B N     1 
ATOM   8397  C  CA    . SER B 1 351 ? 116.986 123.055 151.501 1.00 32.72 ? 351 SER B CA    1 
ATOM   8398  C  C     . SER B 1 351 ? 118.103 122.337 150.756 1.00 33.32 ? 351 SER B C     1 
ATOM   8399  O  O     . SER B 1 351 ? 119.030 121.802 151.375 1.00 40.69 ? 351 SER B O     1 
ATOM   8400  C  CB    . SER B 1 351 ? 115.754 122.157 151.606 1.00 34.03 ? 351 SER B CB    1 
ATOM   8401  O  OG    . SER B 1 351 ? 114.784 122.714 152.473 1.00 42.35 ? 351 SER B OG    1 
ATOM   8402  N  N     . GLU B 1 352 ? 118.033 122.316 149.424 1.00 33.63 ? 352 GLU B N     1 
ATOM   8403  C  CA    . GLU B 1 352 ? 119.004 121.552 148.648 1.00 33.43 ? 352 GLU B CA    1 
ATOM   8404  C  C     . GLU B 1 352 ? 120.374 122.220 148.631 1.00 34.74 ? 352 GLU B C     1 
ATOM   8405  O  O     . GLU B 1 352 ? 121.396 121.549 148.817 1.00 42.37 ? 352 GLU B O     1 
ATOM   8406  C  CB    . GLU B 1 352 ? 118.487 121.353 147.225 1.00 34.82 ? 352 GLU B CB    1 
ATOM   8407  C  CG    . GLU B 1 352 ? 117.365 120.341 147.126 1.00 37.45 ? 352 GLU B CG    1 
ATOM   8408  C  CD    . GLU B 1 352 ? 116.638 120.409 145.802 1.00 44.40 ? 352 GLU B CD    1 
ATOM   8409  O  OE1   . GLU B 1 352 ? 116.956 121.306 144.993 1.00 41.86 ? 352 GLU B OE1   1 
ATOM   8410  O  OE2   . GLU B 1 352 ? 115.745 119.569 145.572 1.00 42.87 ? 352 GLU B OE2   1 
ATOM   8411  N  N     . SER B 1 353 ? 120.423 123.535 148.413 1.00 34.80 ? 353 SER B N     1 
ATOM   8412  C  CA    . SER B 1 353 ? 121.686 124.225 148.188 1.00 35.45 ? 353 SER B CA    1 
ATOM   8413  C  C     . SER B 1 353 ? 121.888 125.484 149.018 1.00 30.68 ? 353 SER B C     1 
ATOM   8414  O  O     . SER B 1 353 ? 122.954 126.099 148.908 1.00 31.53 ? 353 SER B O     1 
ATOM   8415  C  CB    . SER B 1 353 ? 121.831 124.596 146.704 1.00 35.41 ? 353 SER B CB    1 
ATOM   8416  O  OG    . SER B 1 353 ? 120.912 125.612 146.343 1.00 34.19 ? 353 SER B OG    1 
ATOM   8417  N  N     . GLY B 1 354 ? 120.916 125.894 149.831 1.00 25.65 ? 354 GLY B N     1 
ATOM   8418  C  CA    . GLY B 1 354 ? 121.033 127.114 150.599 1.00 27.27 ? 354 GLY B CA    1 
ATOM   8419  C  C     . GLY B 1 354 ? 120.668 128.377 149.854 1.00 24.15 ? 354 GLY B C     1 
ATOM   8420  O  O     . GLY B 1 354 ? 120.672 129.456 150.460 1.00 25.45 ? 354 GLY B O     1 
ATOM   8421  N  N     . TYR B 1 355 ? 120.348 128.283 148.572 1.00 26.76 ? 355 TYR B N     1 
ATOM   8422  C  CA    . TYR B 1 355 ? 119.996 129.407 147.726 1.00 18.06 ? 355 TYR B CA    1 
ATOM   8423  C  C     . TYR B 1 355 ? 118.519 129.353 147.364 1.00 24.03 ? 355 TYR B C     1 
ATOM   8424  O  O     . TYR B 1 355 ? 117.909 128.280 147.368 1.00 28.04 ? 355 TYR B O     1 
ATOM   8425  C  CB    . TYR B 1 355 ? 120.842 129.400 146.446 1.00 19.94 ? 355 TYR B CB    1 
ATOM   8426  C  CG    . TYR B 1 355 ? 122.297 129.726 146.674 1.00 26.81 ? 355 TYR B CG    1 
ATOM   8427  C  CD1   . TYR B 1 355 ? 122.672 130.892 147.325 1.00 24.52 ? 355 TYR B CD1   1 
ATOM   8428  C  CD2   . TYR B 1 355 ? 123.296 128.867 146.242 1.00 29.27 ? 355 TYR B CD2   1 
ATOM   8429  C  CE1   . TYR B 1 355 ? 124.000 131.193 147.537 1.00 26.85 ? 355 TYR B CE1   1 
ATOM   8430  C  CE2   . TYR B 1 355 ? 124.628 129.160 146.449 1.00 28.40 ? 355 TYR B CE2   1 
ATOM   8431  C  CZ    . TYR B 1 355 ? 124.974 130.324 147.098 1.00 28.70 ? 355 TYR B CZ    1 
ATOM   8432  O  OH    . TYR B 1 355 ? 126.299 130.624 147.309 1.00 31.15 ? 355 TYR B OH    1 
ATOM   8433  N  N     . PRO B 1 356 ? 117.904 130.494 147.035 1.00 25.36 ? 356 PRO B N     1 
ATOM   8434  C  CA    . PRO B 1 356 ? 118.453 131.854 146.968 1.00 17.21 ? 356 PRO B CA    1 
ATOM   8435  C  C     . PRO B 1 356 ? 118.418 132.603 148.290 1.00 16.71 ? 356 PRO B C     1 
ATOM   8436  O  O     . PRO B 1 356 ? 117.783 132.176 149.247 1.00 22.71 ? 356 PRO B O     1 
ATOM   8437  C  CB    . PRO B 1 356 ? 117.536 132.524 145.944 1.00 18.58 ? 356 PRO B CB    1 
ATOM   8438  C  CG    . PRO B 1 356 ? 116.209 131.900 146.226 1.00 22.30 ? 356 PRO B CG    1 
ATOM   8439  C  CD    . PRO B 1 356 ? 116.514 130.458 146.548 1.00 15.82 ? 356 PRO B CD    1 
ATOM   8440  N  N     . TYR B 1 357 ? 119.107 133.736 148.366 1.00 20.65 ? 357 TYR B N     1 
ATOM   8441  C  CA    . TYR B 1 357 ? 118.841 134.685 149.434 1.00 16.25 ? 357 TYR B CA    1 
ATOM   8442  C  C     . TYR B 1 357 ? 117.447 135.264 149.240 1.00 17.83 ? 357 TYR B C     1 
ATOM   8443  O  O     . TYR B 1 357 ? 117.003 135.484 148.111 1.00 24.45 ? 357 TYR B O     1 
ATOM   8444  C  CB    . TYR B 1 357 ? 119.874 135.813 149.444 1.00 13.52 ? 357 TYR B CB    1 
ATOM   8445  C  CG    . TYR B 1 357 ? 121.315 135.392 149.257 1.00 16.76 ? 357 TYR B CG    1 
ATOM   8446  C  CD1   . TYR B 1 357 ? 121.779 134.178 149.739 1.00 17.24 ? 357 TYR B CD1   1 
ATOM   8447  C  CD2   . TYR B 1 357 ? 122.217 136.220 148.603 1.00 18.17 ? 357 TYR B CD2   1 
ATOM   8448  C  CE1   . TYR B 1 357 ? 123.092 133.799 149.576 1.00 19.02 ? 357 TYR B CE1   1 
ATOM   8449  C  CE2   . TYR B 1 357 ? 123.532 135.848 148.433 1.00 15.77 ? 357 TYR B CE2   1 
ATOM   8450  C  CZ    . TYR B 1 357 ? 123.965 134.637 148.921 1.00 22.21 ? 357 TYR B CZ    1 
ATOM   8451  O  OH    . TYR B 1 357 ? 125.276 134.259 148.756 1.00 29.32 ? 357 TYR B OH    1 
ATOM   8452  N  N     . ILE B 1 358 ? 116.749 135.503 150.343 1.00 23.77 ? 358 ILE B N     1 
ATOM   8453  C  CA    . ILE B 1 358 ? 115.417 136.091 150.307 1.00 17.92 ? 358 ILE B CA    1 
ATOM   8454  C  C     . ILE B 1 358 ? 115.521 137.509 150.841 1.00 18.09 ? 358 ILE B C     1 
ATOM   8455  O  O     . ILE B 1 358 ? 115.939 137.719 151.985 1.00 22.69 ? 358 ILE B O     1 
ATOM   8456  C  CB    . ILE B 1 358 ? 114.405 135.271 151.121 1.00 18.93 ? 358 ILE B CB    1 
ATOM   8457  C  CG1   . ILE B 1 358 ? 114.375 133.818 150.640 1.00 15.91 ? 358 ILE B CG1   1 
ATOM   8458  C  CG2   . ILE B 1 358 ? 113.026 135.897 151.027 1.00 16.74 ? 358 ILE B CG2   1 
ATOM   8459  C  CD1   . ILE B 1 358 ? 113.935 133.654 149.207 1.00 20.22 ? 358 ILE B CD1   1 
ATOM   8460  N  N     . MET B 1 359 ? 115.146 138.480 150.017 1.00 13.32 ? 359 MET B N     1 
ATOM   8461  C  CA    . MET B 1 359 ? 115.076 139.877 150.422 1.00 5.76  ? 359 MET B CA    1 
ATOM   8462  C  C     . MET B 1 359 ? 113.623 140.321 150.352 1.00 9.92  ? 359 MET B C     1 
ATOM   8463  O  O     . MET B 1 359 ? 113.029 140.341 149.270 1.00 19.21 ? 359 MET B O     1 
ATOM   8464  C  CB    . MET B 1 359 ? 115.963 140.753 149.539 1.00 11.69 ? 359 MET B CB    1 
ATOM   8465  C  CG    . MET B 1 359 ? 115.944 142.226 149.910 1.00 11.03 ? 359 MET B CG    1 
ATOM   8466  S  SD    . MET B 1 359 ? 115.986 143.311 148.478 1.00 35.25 ? 359 MET B SD    1 
ATOM   8467  C  CE    . MET B 1 359 ? 115.263 144.799 149.150 1.00 14.50 ? 359 MET B CE    1 
ATOM   8468  N  N     . PHE B 1 360 ? 113.052 140.661 151.502 1.00 14.14 ? 360 PHE B N     1 
ATOM   8469  C  CA    . PHE B 1 360 ? 111.667 141.117 151.568 1.00 8.14  ? 360 PHE B CA    1 
ATOM   8470  C  C     . PHE B 1 360 ? 111.651 142.604 151.249 1.00 13.89 ? 360 PHE B C     1 
ATOM   8471  O  O     . PHE B 1 360 ? 111.992 143.437 152.091 1.00 20.59 ? 360 PHE B O     1 
ATOM   8472  C  CB    . PHE B 1 360 ? 111.072 140.815 152.937 1.00 13.03 ? 360 PHE B CB    1 
ATOM   8473  C  CG    . PHE B 1 360 ? 110.987 139.347 153.241 1.00 16.29 ? 360 PHE B CG    1 
ATOM   8474  C  CD1   . PHE B 1 360 ? 110.176 138.515 152.488 1.00 18.06 ? 360 PHE B CD1   1 
ATOM   8475  C  CD2   . PHE B 1 360 ? 111.735 138.794 154.265 1.00 14.48 ? 360 PHE B CD2   1 
ATOM   8476  C  CE1   . PHE B 1 360 ? 110.104 137.164 152.759 1.00 17.56 ? 360 PHE B CE1   1 
ATOM   8477  C  CE2   . PHE B 1 360 ? 111.667 137.445 154.541 1.00 17.50 ? 360 PHE B CE2   1 
ATOM   8478  C  CZ    . PHE B 1 360 ? 110.850 136.629 153.787 1.00 14.06 ? 360 PHE B CZ    1 
ATOM   8479  N  N     . GLN B 1 361 ? 111.238 142.935 150.022 1.00 18.63 ? 361 GLN B N     1 
ATOM   8480  C  CA    . GLN B 1 361 ? 111.406 144.288 149.498 1.00 12.01 ? 361 GLN B CA    1 
ATOM   8481  C  C     . GLN B 1 361 ? 110.678 145.321 150.349 1.00 10.21 ? 361 GLN B C     1 
ATOM   8482  O  O     . GLN B 1 361 ? 111.228 146.387 150.647 1.00 13.46 ? 361 GLN B O     1 
ATOM   8483  C  CB    . GLN B 1 361 ? 110.912 144.343 148.052 1.00 18.61 ? 361 GLN B CB    1 
ATOM   8484  C  CG    . GLN B 1 361 ? 110.821 145.740 147.466 1.00 19.78 ? 361 GLN B CG    1 
ATOM   8485  C  CD    . GLN B 1 361 ? 111.820 145.972 146.353 1.00 19.93 ? 361 GLN B CD    1 
ATOM   8486  O  OE1   . GLN B 1 361 ? 111.908 145.186 145.413 1.00 27.15 ? 361 GLN B OE1   1 
ATOM   8487  N  NE2   . GLN B 1 361 ? 112.581 147.053 146.455 1.00 19.68 ? 361 GLN B NE2   1 
ATOM   8488  N  N     . ASP B 1 362 ? 109.439 145.032 150.744 1.00 22.07 ? 362 ASP B N     1 
ATOM   8489  C  CA    . ASP B 1 362 ? 108.658 146.007 151.492 1.00 15.51 ? 362 ASP B CA    1 
ATOM   8490  C  C     . ASP B 1 362 ? 109.056 146.087 152.959 1.00 15.08 ? 362 ASP B C     1 
ATOM   8491  O  O     . ASP B 1 362 ? 108.815 147.118 153.593 1.00 21.61 ? 362 ASP B O     1 
ATOM   8492  C  CB    . ASP B 1 362 ? 107.167 145.695 151.364 1.00 17.52 ? 362 ASP B CB    1 
ATOM   8493  C  CG    . ASP B 1 362 ? 106.682 145.767 149.929 1.00 26.53 ? 362 ASP B CG    1 
ATOM   8494  O  OD1   . ASP B 1 362 ? 107.517 145.644 149.009 1.00 25.14 ? 362 ASP B OD1   1 
ATOM   8495  O  OD2   . ASP B 1 362 ? 105.469 145.970 149.717 1.00 34.49 ? 362 ASP B OD2   1 
ATOM   8496  N  N     . ASN B 1 363 ? 109.651 145.029 153.513 1.00 25.43 ? 363 ASN B N     1 
ATOM   8497  C  CA    . ASN B 1 363 ? 110.220 145.131 154.852 1.00 13.37 ? 363 ASN B CA    1 
ATOM   8498  C  C     . ASN B 1 363 ? 111.402 146.091 154.869 1.00 18.11 ? 363 ASN B C     1 
ATOM   8499  O  O     . ASN B 1 363 ? 111.574 146.858 155.822 1.00 23.04 ? 363 ASN B O     1 
ATOM   8500  C  CB    . ASN B 1 363 ? 110.646 143.752 155.354 1.00 11.47 ? 363 ASN B CB    1 
ATOM   8501  C  CG    . ASN B 1 363 ? 109.485 142.941 155.883 1.00 17.55 ? 363 ASN B CG    1 
ATOM   8502  O  OD1   . ASN B 1 363 ? 108.379 143.452 156.041 1.00 20.52 ? 363 ASN B OD1   1 
ATOM   8503  N  ND2   . ASN B 1 363 ? 109.733 141.669 156.163 1.00 19.70 ? 363 ASN B ND2   1 
ATOM   8504  N  N     . VAL B 1 364 ? 112.228 146.055 153.824 1.00 15.33 ? 364 VAL B N     1 
ATOM   8505  C  CA    . VAL B 1 364 ? 113.364 146.965 153.735 1.00 11.04 ? 364 VAL B CA    1 
ATOM   8506  C  C     . VAL B 1 364 ? 112.887 148.400 153.559 1.00 18.60 ? 364 VAL B C     1 
ATOM   8507  O  O     . VAL B 1 364 ? 113.345 149.316 154.252 1.00 22.84 ? 364 VAL B O     1 
ATOM   8508  C  CB    . VAL B 1 364 ? 114.298 146.545 152.587 1.00 3.87  ? 364 VAL B CB    1 
ATOM   8509  C  CG1   . VAL B 1 364 ? 115.535 147.415 152.573 1.00 8.25  ? 364 VAL B CG1   1 
ATOM   8510  C  CG2   . VAL B 1 364 ? 114.667 145.082 152.708 1.00 5.98  ? 364 VAL B CG2   1 
ATOM   8511  N  N     . ASN B 1 365 ? 111.956 148.617 152.631 1.00 14.53 ? 365 ASN B N     1 
ATOM   8512  C  CA    . ASN B 1 365 ? 111.607 149.964 152.204 1.00 7.47  ? 365 ASN B CA    1 
ATOM   8513  C  C     . ASN B 1 365 ? 110.590 150.648 153.106 1.00 14.43 ? 365 ASN B C     1 
ATOM   8514  O  O     . ASN B 1 365 ? 110.433 151.869 153.009 1.00 23.04 ? 365 ASN B O     1 
ATOM   8515  C  CB    . ASN B 1 365 ? 111.082 149.928 150.770 1.00 18.59 ? 365 ASN B CB    1 
ATOM   8516  C  CG    . ASN B 1 365 ? 112.149 149.529 149.776 1.00 16.90 ? 365 ASN B CG    1 
ATOM   8517  O  OD1   . ASN B 1 365 ? 113.208 150.148 149.708 1.00 14.02 ? 365 ASN B OD1   1 
ATOM   8518  N  ND2   . ASN B 1 365 ? 111.878 148.488 149.003 1.00 18.97 ? 365 ASN B ND2   1 
ATOM   8519  N  N     . LYS B 1 366 ? 109.899 149.908 153.974 1.00 17.48 ? 366 LYS B N     1 
ATOM   8520  C  CA    . LYS B 1 366 ? 108.975 150.551 154.900 1.00 19.54 ? 366 LYS B CA    1 
ATOM   8521  C  C     . LYS B 1 366 ? 109.706 151.298 156.006 1.00 19.20 ? 366 LYS B C     1 
ATOM   8522  O  O     . LYS B 1 366 ? 109.124 152.199 156.619 1.00 28.19 ? 366 LYS B O     1 
ATOM   8523  C  CB    . LYS B 1 366 ? 108.018 149.520 155.499 1.00 17.16 ? 366 LYS B CB    1 
ATOM   8524  C  CG    . LYS B 1 366 ? 108.604 148.689 156.624 1.00 24.63 ? 366 LYS B CG    1 
ATOM   8525  C  CD    . LYS B 1 366 ? 107.509 147.993 157.410 1.00 26.44 ? 366 LYS B CD    1 
ATOM   8526  C  CE    . LYS B 1 366 ? 106.599 147.191 156.493 1.00 22.33 ? 366 LYS B CE    1 
ATOM   8527  N  NZ    . LYS B 1 366 ? 105.651 146.339 157.260 1.00 26.54 ? 366 LYS B NZ    1 
ATOM   8528  N  N     . VAL B 1 367 ? 110.964 150.949 156.267 1.00 23.73 ? 367 VAL B N     1 
ATOM   8529  C  CA    . VAL B 1 367 ? 111.797 151.630 157.246 1.00 18.23 ? 367 VAL B CA    1 
ATOM   8530  C  C     . VAL B 1 367 ? 113.020 152.266 156.602 1.00 18.05 ? 367 VAL B C     1 
ATOM   8531  O  O     . VAL B 1 367 ? 113.887 152.784 157.304 1.00 20.44 ? 367 VAL B O     1 
ATOM   8532  C  CB    . VAL B 1 367 ? 112.213 150.674 158.381 1.00 15.60 ? 367 VAL B CB    1 
ATOM   8533  C  CG1   . VAL B 1 367 ? 111.006 150.289 159.216 1.00 16.86 ? 367 VAL B CG1   1 
ATOM   8534  C  CG2   . VAL B 1 367 ? 112.880 149.445 157.806 1.00 10.48 ? 367 VAL B CG2   1 
ATOM   8535  N  N     . HIS B 1 368 ? 113.110 152.227 155.276 1.00 16.88 ? 368 HIS B N     1 
ATOM   8536  C  CA    . HIS B 1 368 ? 114.233 152.829 154.574 1.00 6.22  ? 368 HIS B CA    1 
ATOM   8537  C  C     . HIS B 1 368 ? 114.184 154.344 154.715 1.00 17.16 ? 368 HIS B C     1 
ATOM   8538  O  O     . HIS B 1 368 ? 113.132 154.963 154.530 1.00 27.24 ? 368 HIS B O     1 
ATOM   8539  C  CB    . HIS B 1 368 ? 114.206 152.429 153.101 1.00 12.41 ? 368 HIS B CB    1 
ATOM   8540  C  CG    . HIS B 1 368 ? 115.406 152.876 152.328 1.00 8.82  ? 368 HIS B CG    1 
ATOM   8541  N  ND1   . HIS B 1 368 ? 115.338 153.251 151.005 1.00 17.96 ? 368 HIS B ND1   1 
ATOM   8542  C  CD2   . HIS B 1 368 ? 116.703 153.006 152.690 1.00 8.92  ? 368 HIS B CD2   1 
ATOM   8543  C  CE1   . HIS B 1 368 ? 116.542 153.592 150.584 1.00 17.05 ? 368 HIS B CE1   1 
ATOM   8544  N  NE2   . HIS B 1 368 ? 117.388 153.455 151.588 1.00 16.00 ? 368 HIS B NE2   1 
ATOM   8545  N  N     . ALA B 1 369 ? 115.325 154.940 155.049 1.00 19.73 ? 369 ALA B N     1 
ATOM   8546  C  CA    . ALA B 1 369 ? 115.400 156.370 155.302 1.00 13.96 ? 369 ALA B CA    1 
ATOM   8547  C  C     . ALA B 1 369 ? 115.695 157.189 154.055 1.00 22.99 ? 369 ALA B C     1 
ATOM   8548  O  O     . ALA B 1 369 ? 115.650 158.420 154.121 1.00 29.50 ? 369 ALA B O     1 
ATOM   8549  C  CB    . ALA B 1 369 ? 116.467 156.660 156.361 1.00 13.07 ? 369 ALA B CB    1 
ATOM   8550  N  N     . ASN B 1 370 ? 115.982 156.547 152.927 1.00 18.22 ? 370 ASN B N     1 
ATOM   8551  C  CA    . ASN B 1 370 ? 116.382 157.239 151.710 1.00 12.99 ? 370 ASN B CA    1 
ATOM   8552  C  C     . ASN B 1 370 ? 115.544 156.783 150.527 1.00 13.47 ? 370 ASN B C     1 
ATOM   8553  O  O     . ASN B 1 370 ? 116.055 156.580 149.424 1.00 23.39 ? 370 ASN B O     1 
ATOM   8554  C  CB    . ASN B 1 370 ? 117.868 157.030 151.430 1.00 14.82 ? 370 ASN B CB    1 
ATOM   8555  C  CG    . ASN B 1 370 ? 118.752 157.612 152.513 1.00 13.38 ? 370 ASN B CG    1 
ATOM   8556  O  OD1   . ASN B 1 370 ? 118.744 158.818 152.755 1.00 27.62 ? 370 ASN B OD1   1 
ATOM   8557  N  ND2   . ASN B 1 370 ? 119.521 156.756 153.172 1.00 11.85 ? 370 ASN B ND2   1 
ATOM   8558  N  N     . ASN B 1 371 ? 114.236 156.618 150.739 1.00 18.88 ? 371 ASN B N     1 
ATOM   8559  C  CA    . ASN B 1 371 ? 113.350 156.236 149.645 1.00 13.14 ? 371 ASN B CA    1 
ATOM   8560  C  C     . ASN B 1 371 ? 113.230 157.328 148.593 1.00 16.99 ? 371 ASN B C     1 
ATOM   8561  O  O     . ASN B 1 371 ? 112.889 157.028 147.444 1.00 25.10 ? 371 ASN B O     1 
ATOM   8562  C  CB    . ASN B 1 371 ? 111.963 155.883 150.184 1.00 9.73  ? 371 ASN B CB    1 
ATOM   8563  C  CG    . ASN B 1 371 ? 111.883 154.462 150.696 1.00 16.84 ? 371 ASN B CG    1 
ATOM   8564  O  OD1   . ASN B 1 371 ? 112.701 153.616 150.341 1.00 21.56 ? 371 ASN B OD1   1 
ATOM   8565  N  ND2   . ASN B 1 371 ? 110.894 154.192 151.537 1.00 22.52 ? 371 ASN B ND2   1 
ATOM   8566  N  N     . HIS B 1 372 ? 113.494 158.584 148.961 1.00 19.83 ? 372 HIS B N     1 
ATOM   8567  C  CA    . HIS B 1 372 ? 113.484 159.664 147.980 1.00 20.09 ? 372 HIS B CA    1 
ATOM   8568  C  C     . HIS B 1 372 ? 114.586 159.476 146.946 1.00 21.53 ? 372 HIS B C     1 
ATOM   8569  O  O     . HIS B 1 372 ? 114.379 159.729 145.754 1.00 24.93 ? 372 HIS B O     1 
ATOM   8570  C  CB    . HIS B 1 372 ? 113.633 161.012 148.685 1.00 23.22 ? 372 HIS B CB    1 
ATOM   8571  C  CG    . HIS B 1 372 ? 114.962 161.202 149.346 1.00 21.42 ? 372 HIS B CG    1 
ATOM   8572  N  ND1   . HIS B 1 372 ? 115.389 160.422 150.398 1.00 21.13 ? 372 HIS B ND1   1 
ATOM   8573  C  CD2   . HIS B 1 372 ? 115.963 162.078 149.097 1.00 23.07 ? 372 HIS B CD2   1 
ATOM   8574  C  CE1   . HIS B 1 372 ? 116.595 160.809 150.769 1.00 19.35 ? 372 HIS B CE1   1 
ATOM   8575  N  NE2   . HIS B 1 372 ? 116.965 161.815 149.998 1.00 22.88 ? 372 HIS B NE2   1 
ATOM   8576  N  N     . ILE B 1 373 ? 115.770 159.045 147.387 1.00 16.94 ? 373 ILE B N     1 
ATOM   8577  C  CA    . ILE B 1 373 ? 116.855 158.763 146.451 1.00 19.18 ? 373 ILE B CA    1 
ATOM   8578  C  C     . ILE B 1 373 ? 116.477 157.597 145.551 1.00 21.41 ? 373 ILE B C     1 
ATOM   8579  O  O     . ILE B 1 373 ? 116.569 157.681 144.320 1.00 33.99 ? 373 ILE B O     1 
ATOM   8580  C  CB    . ILE B 1 373 ? 118.160 158.481 147.216 1.00 23.03 ? 373 ILE B CB    1 
ATOM   8581  C  CG1   . ILE B 1 373 ? 118.597 159.714 148.004 1.00 21.29 ? 373 ILE B CG1   1 
ATOM   8582  C  CG2   . ILE B 1 373 ? 119.254 158.035 146.261 1.00 20.95 ? 373 ILE B CG2   1 
ATOM   8583  C  CD1   . ILE B 1 373 ? 119.608 159.420 149.079 1.00 18.62 ? 373 ILE B CD1   1 
ATOM   8584  N  N     . SER B 1 374 ? 116.029 156.501 146.155 1.00 15.55 ? 374 SER B N     1 
ATOM   8585  C  CA    . SER B 1 374 ? 115.592 155.299 145.463 1.00 12.17 ? 374 SER B CA    1 
ATOM   8586  C  C     . SER B 1 374 ? 115.106 154.315 146.514 1.00 18.98 ? 374 SER B C     1 
ATOM   8587  O  O     . SER B 1 374 ? 115.459 154.418 147.692 1.00 21.60 ? 374 SER B O     1 
ATOM   8588  C  CB    . SER B 1 374 ? 116.714 154.669 144.634 1.00 21.21 ? 374 SER B CB    1 
ATOM   8589  O  OG    . SER B 1 374 ? 116.214 153.648 143.793 1.00 32.58 ? 374 SER B OG    1 
ATOM   8590  N  N     . LYS B 1 375 ? 114.289 153.365 146.078 1.00 23.38 ? 375 LYS B N     1 
ATOM   8591  C  CA    . LYS B 1 375 ? 113.975 152.229 146.924 1.00 12.93 ? 375 LYS B CA    1 
ATOM   8592  C  C     . LYS B 1 375 ? 115.140 151.244 146.915 1.00 14.50 ? 375 LYS B C     1 
ATOM   8593  O  O     . LYS B 1 375 ? 115.946 151.203 145.982 1.00 25.54 ? 375 LYS B O     1 
ATOM   8594  C  CB    . LYS B 1 375 ? 112.698 151.539 146.447 1.00 15.11 ? 375 LYS B CB    1 
ATOM   8595  C  CG    . LYS B 1 375 ? 111.469 152.427 146.445 1.00 16.71 ? 375 LYS B CG    1 
ATOM   8596  C  CD    . LYS B 1 375 ? 110.885 152.555 147.836 1.00 19.95 ? 375 LYS B CD    1 
ATOM   8597  C  CE    . LYS B 1 375 ? 109.372 152.637 147.792 1.00 21.33 ? 375 LYS B CE    1 
ATOM   8598  N  NZ    . LYS B 1 375 ? 108.904 154.046 147.702 1.00 23.93 ? 375 LYS B NZ    1 
ATOM   8599  N  N     . VAL B 1 376 ? 115.234 150.452 147.976 1.00 12.54 ? 376 VAL B N     1 
ATOM   8600  C  CA    . VAL B 1 376 ? 116.212 149.372 148.020 1.00 13.88 ? 376 VAL B CA    1 
ATOM   8601  C  C     . VAL B 1 376 ? 115.672 148.218 147.187 1.00 14.05 ? 376 VAL B C     1 
ATOM   8602  O  O     . VAL B 1 376 ? 114.632 147.636 147.513 1.00 22.59 ? 376 VAL B O     1 
ATOM   8603  C  CB    . VAL B 1 376 ? 116.498 148.932 149.462 1.00 10.47 ? 376 VAL B CB    1 
ATOM   8604  C  CG1   . VAL B 1 376 ? 117.535 147.819 149.483 1.00 7.68  ? 376 VAL B CG1   1 
ATOM   8605  C  CG2   . VAL B 1 376 ? 116.955 150.113 150.297 1.00 7.95  ? 376 VAL B CG2   1 
ATOM   8606  N  N     . LYS B 1 377 ? 116.372 147.889 146.103 1.00 13.50 ? 377 LYS B N     1 
ATOM   8607  C  CA    . LYS B 1 377 ? 115.900 146.877 145.172 1.00 13.94 ? 377 LYS B CA    1 
ATOM   8608  C  C     . LYS B 1 377 ? 116.581 145.529 145.341 1.00 10.33 ? 377 LYS B C     1 
ATOM   8609  O  O     . LYS B 1 377 ? 116.022 144.517 144.909 1.00 22.86 ? 377 LYS B O     1 
ATOM   8610  C  CB    . LYS B 1 377 ? 116.097 147.349 143.728 1.00 16.69 ? 377 LYS B CB    1 
ATOM   8611  C  CG    . LYS B 1 377 ? 115.350 148.616 143.384 1.00 10.88 ? 377 LYS B CG    1 
ATOM   8612  C  CD    . LYS B 1 377 ? 116.024 149.329 142.233 1.00 19.72 ? 377 LYS B CD    1 
ATOM   8613  C  CE    . LYS B 1 377 ? 115.960 150.828 142.407 1.00 23.72 ? 377 LYS B CE    1 
ATOM   8614  N  NZ    . LYS B 1 377 ? 116.932 151.530 141.527 1.00 21.57 ? 377 LYS B NZ    1 
ATOM   8615  N  N     . PHE B 1 378 ? 117.762 145.490 145.948 1.00 8.67  ? 378 PHE B N     1 
ATOM   8616  C  CA    . PHE B 1 378 ? 118.502 144.246 146.095 1.00 7.82  ? 378 PHE B CA    1 
ATOM   8617  C  C     . PHE B 1 378 ? 119.553 144.432 147.179 1.00 11.30 ? 378 PHE B C     1 
ATOM   8618  O  O     . PHE B 1 378 ? 119.751 145.531 147.700 1.00 14.61 ? 378 PHE B O     1 
ATOM   8619  C  CB    . PHE B 1 378 ? 119.132 143.804 144.769 1.00 6.67  ? 378 PHE B CB    1 
ATOM   8620  C  CG    . PHE B 1 378 ? 120.278 144.663 144.309 1.00 9.68  ? 378 PHE B CG    1 
ATOM   8621  C  CD1   . PHE B 1 378 ? 120.115 146.023 144.108 1.00 15.39 ? 378 PHE B CD1   1 
ATOM   8622  C  CD2   . PHE B 1 378 ? 121.515 144.101 144.049 1.00 6.65  ? 378 PHE B CD2   1 
ATOM   8623  C  CE1   . PHE B 1 378 ? 121.165 146.804 143.678 1.00 9.44  ? 378 PHE B CE1   1 
ATOM   8624  C  CE2   . PHE B 1 378 ? 122.566 144.880 143.615 1.00 9.39  ? 378 PHE B CE2   1 
ATOM   8625  C  CZ    . PHE B 1 378 ? 122.390 146.232 143.429 1.00 11.49 ? 378 PHE B CZ    1 
ATOM   8626  N  N     . SER B 1 379 ? 120.222 143.337 147.511 1.00 5.79  ? 379 SER B N     1 
ATOM   8627  C  CA    . SER B 1 379 ? 121.208 143.295 148.579 1.00 9.57  ? 379 SER B CA    1 
ATOM   8628  C  C     . SER B 1 379 ? 122.553 142.850 148.018 1.00 9.63  ? 379 SER B C     1 
ATOM   8629  O  O     . SER B 1 379 ? 122.719 142.662 146.812 1.00 18.06 ? 379 SER B O     1 
ATOM   8630  C  CB    . SER B 1 379 ? 120.749 142.364 149.704 1.00 7.65  ? 379 SER B CB    1 
ATOM   8631  O  OG    . SER B 1 379 ? 121.237 142.805 150.955 1.00 11.11 ? 379 SER B OG    1 
ATOM   8632  N  N     . ASN B 1 380 ? 123.521 142.687 148.913 1.00 12.05 ? 380 ASN B N     1 
ATOM   8633  C  CA    . ASN B 1 380 ? 124.876 142.332 148.528 1.00 9.82  ? 380 ASN B CA    1 
ATOM   8634  C  C     . ASN B 1 380 ? 125.037 140.814 148.526 1.00 14.69 ? 380 ASN B C     1 
ATOM   8635  O  O     . ASN B 1 380 ? 124.065 140.059 148.603 1.00 18.76 ? 380 ASN B O     1 
ATOM   8636  C  CB    . ASN B 1 380 ? 125.885 143.013 149.450 1.00 9.20  ? 380 ASN B CB    1 
ATOM   8637  C  CG    . ASN B 1 380 ? 125.787 142.534 150.879 1.00 10.78 ? 380 ASN B CG    1 
ATOM   8638  O  OD1   . ASN B 1 380 ? 124.694 142.357 151.411 1.00 20.44 ? 380 ASN B OD1   1 
ATOM   8639  N  ND2   . ASN B 1 380 ? 126.932 142.337 151.516 1.00 15.99 ? 380 ASN B ND2   1 
ATOM   8640  N  N     . LEU B 1 381 ? 126.284 140.354 148.423 1.00 18.50 ? 381 LEU B N     1 
ATOM   8641  C  CA    . LEU B 1 381 ? 126.569 138.926 148.428 1.00 11.44 ? 381 LEU B CA    1 
ATOM   8642  C  C     . LEU B 1 381 ? 126.321 138.293 149.792 1.00 9.73  ? 381 LEU B C     1 
ATOM   8643  O  O     . LEU B 1 381 ? 126.096 137.082 149.867 1.00 20.28 ? 381 LEU B O     1 
ATOM   8644  C  CB    . LEU B 1 381 ? 128.015 138.698 147.981 1.00 17.24 ? 381 LEU B CB    1 
ATOM   8645  C  CG    . LEU B 1 381 ? 128.625 137.295 147.997 1.00 19.87 ? 381 LEU B CG    1 
ATOM   8646  C  CD1   . LEU B 1 381 ? 127.885 136.359 147.062 1.00 21.62 ? 381 LEU B CD1   1 
ATOM   8647  C  CD2   . LEU B 1 381 ? 130.092 137.371 147.629 1.00 16.93 ? 381 LEU B CD2   1 
ATOM   8648  N  N     . CYS B 1 382 ? 126.344 139.082 150.864 1.00 20.14 ? 382 CYS B N     1 
ATOM   8649  C  CA    . CYS B 1 382 ? 126.118 138.579 152.210 1.00 7.72  ? 382 CYS B CA    1 
ATOM   8650  C  C     . CYS B 1 382 ? 124.750 138.953 152.763 1.00 13.77 ? 382 CYS B C     1 
ATOM   8651  O  O     . CYS B 1 382 ? 124.453 138.619 153.914 1.00 22.02 ? 382 CYS B O     1 
ATOM   8652  C  CB    . CYS B 1 382 ? 127.218 139.082 153.151 1.00 20.41 ? 382 CYS B CB    1 
ATOM   8653  S  SG    . CYS B 1 382 ? 128.901 138.720 152.595 1.00 34.53 ? 382 CYS B SG    1 
ATOM   8654  N  N     . SER B 1 383 ? 123.922 139.652 151.982 1.00 15.70 ? 383 SER B N     1 
ATOM   8655  C  CA    . SER B 1 383 ? 122.509 139.882 152.287 1.00 12.60 ? 383 SER B CA    1 
ATOM   8656  C  C     . SER B 1 383 ? 122.298 140.796 153.492 1.00 18.20 ? 383 SER B C     1 
ATOM   8657  O  O     . SER B 1 383 ? 121.294 140.677 154.194 1.00 25.08 ? 383 SER B O     1 
ATOM   8658  C  CB    . SER B 1 383 ? 121.762 138.561 152.498 1.00 11.23 ? 383 SER B CB    1 
ATOM   8659  O  OG    . SER B 1 383 ? 121.800 137.767 151.328 1.00 32.77 ? 383 SER B OG    1 
ATOM   8660  N  N     . GLU B 1 384 ? 123.220 141.718 153.755 1.00 12.98 ? 384 GLU B N     1 
ATOM   8661  C  CA    . GLU B 1 384 ? 123.027 142.683 154.826 1.00 10.50 ? 384 GLU B CA    1 
ATOM   8662  C  C     . GLU B 1 384 ? 123.083 144.131 154.367 1.00 16.04 ? 384 GLU B C     1 
ATOM   8663  O  O     . GLU B 1 384 ? 122.636 145.012 155.109 1.00 23.33 ? 384 GLU B O     1 
ATOM   8664  C  CB    . GLU B 1 384 ? 124.059 142.466 155.946 1.00 11.06 ? 384 GLU B CB    1 
ATOM   8665  C  CG    . GLU B 1 384 ? 125.273 143.372 155.886 1.00 11.82 ? 384 GLU B CG    1 
ATOM   8666  C  CD    . GLU B 1 384 ? 126.323 142.871 154.927 1.00 20.82 ? 384 GLU B CD    1 
ATOM   8667  O  OE1   . GLU B 1 384 ? 126.202 141.719 154.472 1.00 21.31 ? 384 GLU B OE1   1 
ATOM   8668  O  OE2   . GLU B 1 384 ? 127.274 143.623 154.635 1.00 26.90 ? 384 GLU B OE2   1 
ATOM   8669  N  N     . VAL B 1 385 ? 123.601 144.407 153.177 1.00 12.17 ? 385 VAL B N     1 
ATOM   8670  C  CA    . VAL B 1 385 ? 123.686 145.769 152.667 1.00 5.50  ? 385 VAL B CA    1 
ATOM   8671  C  C     . VAL B 1 385 ? 122.387 146.093 151.944 1.00 16.26 ? 385 VAL B C     1 
ATOM   8672  O  O     . VAL B 1 385 ? 122.041 145.446 150.951 1.00 22.03 ? 385 VAL B O     1 
ATOM   8673  C  CB    . VAL B 1 385 ? 124.894 145.942 151.737 1.00 6.74  ? 385 VAL B CB    1 
ATOM   8674  C  CG1   . VAL B 1 385 ? 124.873 147.317 151.118 1.00 10.16 ? 385 VAL B CG1   1 
ATOM   8675  C  CG2   . VAL B 1 385 ? 126.179 145.731 152.504 1.00 10.21 ? 385 VAL B CG2   1 
ATOM   8676  N  N     . LEU B 1 386 ? 121.664 147.094 152.446 1.00 17.73 ? 386 LEU B N     1 
ATOM   8677  C  CA    . LEU B 1 386 ? 120.361 147.488 151.910 1.00 4.25  ? 386 LEU B CA    1 
ATOM   8678  C  C     . LEU B 1 386 ? 120.355 149.004 151.758 1.00 6.34  ? 386 LEU B C     1 
ATOM   8679  O  O     . LEU B 1 386 ? 119.999 149.729 152.689 1.00 12.95 ? 386 LEU B O     1 
ATOM   8680  C  CB    . LEU B 1 386 ? 119.238 147.001 152.814 1.00 6.94  ? 386 LEU B CB    1 
ATOM   8681  C  CG    . LEU B 1 386 ? 119.120 145.481 152.902 1.00 3.34  ? 386 LEU B CG    1 
ATOM   8682  C  CD1   . LEU B 1 386 ? 118.084 145.091 153.920 1.00 8.47  ? 386 LEU B CD1   1 
ATOM   8683  C  CD2   . LEU B 1 386 ? 118.783 144.899 151.541 1.00 6.13  ? 386 LEU B CD2   1 
ATOM   8684  N  N     . GLN B 1 387 ? 120.749 149.479 150.580 1.00 13.05 ? 387 GLN B N     1 
ATOM   8685  C  CA    . GLN B 1 387 ? 120.888 150.901 150.317 1.00 5.31  ? 387 GLN B CA    1 
ATOM   8686  C  C     . GLN B 1 387 ? 120.224 151.256 148.995 1.00 10.22 ? 387 GLN B C     1 
ATOM   8687  O  O     . GLN B 1 387 ? 120.006 150.401 148.134 1.00 20.16 ? 387 GLN B O     1 
ATOM   8688  C  CB    . GLN B 1 387 ? 122.363 151.321 150.294 1.00 3.93  ? 387 GLN B CB    1 
ATOM   8689  C  CG    . GLN B 1 387 ? 123.132 150.913 151.532 1.00 6.73  ? 387 GLN B CG    1 
ATOM   8690  C  CD    . GLN B 1 387 ? 124.553 151.412 151.526 1.00 10.83 ? 387 GLN B CD    1 
ATOM   8691  O  OE1   . GLN B 1 387 ? 124.915 152.278 150.733 1.00 18.82 ? 387 GLN B OE1   1 
ATOM   8692  N  NE2   . GLN B 1 387 ? 125.373 150.864 152.409 1.00 11.64 ? 387 GLN B NE2   1 
ATOM   8693  N  N     . ALA B 1 388 ? 119.893 152.535 148.853 1.00 10.58 ? 388 ALA B N     1 
ATOM   8694  C  CA    . ALA B 1 388 ? 119.320 153.031 147.610 1.00 9.15  ? 388 ALA B CA    1 
ATOM   8695  C  C     . ALA B 1 388 ? 120.359 153.012 146.497 1.00 15.10 ? 388 ALA B C     1 
ATOM   8696  O  O     . ALA B 1 388 ? 121.525 153.360 146.705 1.00 23.39 ? 388 ALA B O     1 
ATOM   8697  C  CB    . ALA B 1 388 ? 118.784 154.448 147.801 1.00 12.86 ? 388 ALA B CB    1 
ATOM   8698  N  N     . SER B 1 389 ? 119.930 152.606 145.307 1.00 19.41 ? 389 SER B N     1 
ATOM   8699  C  CA    . SER B 1 389 ? 120.797 152.550 144.143 1.00 10.37 ? 389 SER B CA    1 
ATOM   8700  C  C     . SER B 1 389 ? 120.100 153.190 142.954 1.00 14.55 ? 389 SER B C     1 
ATOM   8701  O  O     . SER B 1 389 ? 118.871 153.176 142.850 1.00 22.86 ? 389 SER B O     1 
ATOM   8702  C  CB    . SER B 1 389 ? 121.187 151.108 143.797 1.00 16.66 ? 389 SER B CB    1 
ATOM   8703  O  OG    . SER B 1 389 ? 120.047 150.268 143.756 1.00 22.68 ? 389 SER B OG    1 
ATOM   8704  N  N     . GLN B 1 390 ? 120.901 153.752 142.056 1.00 21.79 ? 390 GLN B N     1 
ATOM   8705  C  CA    . GLN B 1 390 ? 120.412 154.310 140.804 1.00 13.94 ? 390 GLN B CA    1 
ATOM   8706  C  C     . GLN B 1 390 ? 121.178 153.661 139.665 1.00 15.32 ? 390 GLN B C     1 
ATOM   8707  O  O     . GLN B 1 390 ? 122.410 153.597 139.701 1.00 23.30 ? 390 GLN B O     1 
ATOM   8708  C  CB    . GLN B 1 390 ? 120.576 155.831 140.770 1.00 12.82 ? 390 GLN B CB    1 
ATOM   8709  C  CG    . GLN B 1 390 ? 119.627 156.565 141.695 1.00 14.85 ? 390 GLN B CG    1 
ATOM   8710  C  CD    . GLN B 1 390 ? 119.857 158.058 141.703 1.00 25.03 ? 390 GLN B CD    1 
ATOM   8711  O  OE1   . GLN B 1 390 ? 120.814 158.555 141.109 1.00 28.68 ? 390 GLN B OE1   1 
ATOM   8712  N  NE2   . GLN B 1 390 ? 118.979 158.787 142.380 1.00 17.67 ? 390 GLN B NE2   1 
ATOM   8713  N  N     . VAL B 1 391 ? 120.450 153.175 138.661 1.00 25.39 ? 391 VAL B N     1 
ATOM   8714  C  CA    . VAL B 1 391 ? 121.087 152.472 137.558 1.00 20.63 ? 391 VAL B CA    1 
ATOM   8715  C  C     . VAL B 1 391 ? 121.822 153.467 136.671 1.00 25.33 ? 391 VAL B C     1 
ATOM   8716  O  O     . VAL B 1 391 ? 121.371 154.602 136.462 1.00 22.55 ? 391 VAL B O     1 
ATOM   8717  C  CB    . VAL B 1 391 ? 120.050 151.655 136.767 1.00 16.98 ? 391 VAL B CB    1 
ATOM   8718  C  CG1   . VAL B 1 391 ? 119.120 152.564 135.975 1.00 17.56 ? 391 VAL B CG1   1 
ATOM   8719  C  CG2   . VAL B 1 391 ? 120.742 150.651 135.858 1.00 17.74 ? 391 VAL B CG2   1 
ATOM   8720  N  N     . SER B 1 392 ? 122.980 153.055 136.169 1.00 31.37 ? 392 SER B N     1 
ATOM   8721  C  CA    . SER B 1 392 ? 123.766 153.880 135.269 1.00 22.29 ? 392 SER B CA    1 
ATOM   8722  C  C     . SER B 1 392 ? 123.393 153.586 133.824 1.00 28.46 ? 392 SER B C     1 
ATOM   8723  O  O     . SER B 1 392 ? 123.056 152.455 133.464 1.00 30.88 ? 392 SER B O     1 
ATOM   8724  C  CB    . SER B 1 392 ? 125.261 153.642 135.479 1.00 26.53 ? 392 SER B CB    1 
ATOM   8725  O  OG    . SER B 1 392 ? 125.625 153.841 136.832 1.00 34.92 ? 392 SER B OG    1 
ATOM   8726  N  N     . SER B 1 393 ? 123.456 154.620 132.995 1.00 35.07 ? 393 SER B N     1 
ATOM   8727  C  CA    . SER B 1 393 ? 123.177 154.511 131.567 1.00 29.81 ? 393 SER B CA    1 
ATOM   8728  C  C     . SER B 1 393 ? 124.514 154.600 130.837 1.00 32.89 ? 393 SER B C     1 
ATOM   8729  O  O     . SER B 1 393 ? 124.965 155.683 130.462 1.00 35.42 ? 393 SER B O     1 
ATOM   8730  C  CB    . SER B 1 393 ? 122.210 155.597 131.110 1.00 31.41 ? 393 SER B CB    1 
ATOM   8731  O  OG    . SER B 1 393 ? 121.119 155.713 132.005 1.00 39.55 ? 393 SER B OG    1 
ATOM   8732  N  N     . TYR B 1 394 ? 125.147 153.447 130.640 1.00 32.71 ? 394 TYR B N     1 
ATOM   8733  C  CA    . TYR B 1 394 ? 126.405 153.381 129.907 1.00 29.35 ? 394 TYR B CA    1 
ATOM   8734  C  C     . TYR B 1 394 ? 126.092 153.377 128.418 1.00 31.41 ? 394 TYR B C     1 
ATOM   8735  O  O     . TYR B 1 394 ? 125.527 152.411 127.896 1.00 34.47 ? 394 TYR B O     1 
ATOM   8736  C  CB    . TYR B 1 394 ? 127.200 152.144 130.314 1.00 29.21 ? 394 TYR B CB    1 
ATOM   8737  C  CG    . TYR B 1 394 ? 127.606 152.140 131.769 1.00 29.76 ? 394 TYR B CG    1 
ATOM   8738  C  CD1   . TYR B 1 394 ? 128.600 152.990 132.234 1.00 30.32 ? 394 TYR B CD1   1 
ATOM   8739  C  CD2   . TYR B 1 394 ? 126.992 151.291 132.678 1.00 26.24 ? 394 TYR B CD2   1 
ATOM   8740  C  CE1   . TYR B 1 394 ? 128.974 152.989 133.562 1.00 29.54 ? 394 TYR B CE1   1 
ATOM   8741  C  CE2   . TYR B 1 394 ? 127.358 151.283 134.007 1.00 27.91 ? 394 TYR B CE2   1 
ATOM   8742  C  CZ    . TYR B 1 394 ? 128.348 152.134 134.445 1.00 35.20 ? 394 TYR B CZ    1 
ATOM   8743  O  OH    . TYR B 1 394 ? 128.715 152.128 135.771 1.00 37.09 ? 394 TYR B OH    1 
ATOM   8744  N  N     . THR B 1 395 ? 126.451 154.458 127.739 1.00 37.14 ? 395 THR B N     1 
ATOM   8745  C  CA    . THR B 1 395 ? 126.112 154.657 126.340 1.00 34.49 ? 395 THR B CA    1 
ATOM   8746  C  C     . THR B 1 395 ? 127.228 154.107 125.453 1.00 37.28 ? 395 THR B C     1 
ATOM   8747  O  O     . THR B 1 395 ? 128.116 153.381 125.909 1.00 35.81 ? 395 THR B O     1 
ATOM   8748  C  CB    . THR B 1 395 ? 125.851 156.137 126.078 1.00 36.71 ? 395 THR B CB    1 
ATOM   8749  O  OG1   . THR B 1 395 ? 127.041 156.884 126.353 1.00 37.17 ? 395 THR B OG1   1 
ATOM   8750  C  CG2   . THR B 1 395 ? 124.732 156.640 126.973 1.00 36.17 ? 395 THR B CG2   1 
ATOM   8751  N  N     . ASP B 1 396 ? 127.188 154.446 124.167 1.00 40.94 ? 396 ASP B N     1 
ATOM   8752  C  CA    . ASP B 1 396 ? 128.228 154.021 123.246 1.00 36.98 ? 396 ASP B CA    1 
ATOM   8753  C  C     . ASP B 1 396 ? 129.566 154.653 123.625 1.00 39.50 ? 396 ASP B C     1 
ATOM   8754  O  O     . ASP B 1 396 ? 129.652 155.540 124.477 1.00 45.27 ? 396 ASP B O     1 
ATOM   8755  C  CB    . ASP B 1 396 ? 127.853 154.382 121.810 1.00 40.48 ? 396 ASP B CB    1 
ATOM   8756  C  CG    . ASP B 1 396 ? 126.620 153.644 121.327 1.00 44.58 ? 396 ASP B CG    1 
ATOM   8757  O  OD1   . ASP B 1 396 ? 126.540 152.416 121.537 1.00 42.43 ? 396 ASP B OD1   1 
ATOM   8758  O  OD2   . ASP B 1 396 ? 125.733 154.292 120.734 1.00 45.64 ? 396 ASP B OD2   1 
ATOM   8759  N  N     . TYR B 1 397 ? 130.626 154.174 122.971 1.00 34.31 ? 397 TYR B N     1 
ATOM   8760  C  CA    . TYR B 1 397 ? 131.975 154.601 123.327 1.00 35.86 ? 397 TYR B CA    1 
ATOM   8761  C  C     . TYR B 1 397 ? 132.162 156.099 123.116 1.00 36.12 ? 397 TYR B C     1 
ATOM   8762  O  O     . TYR B 1 397 ? 132.793 156.774 123.938 1.00 41.04 ? 397 TYR B O     1 
ATOM   8763  C  CB    . TYR B 1 397 ? 133.002 153.806 122.519 1.00 33.57 ? 397 TYR B CB    1 
ATOM   8764  C  CG    . TYR B 1 397 ? 134.435 154.226 122.751 1.00 33.49 ? 397 TYR B CG    1 
ATOM   8765  C  CD1   . TYR B 1 397 ? 135.014 155.242 122.001 1.00 33.79 ? 397 TYR B CD1   1 
ATOM   8766  C  CD2   . TYR B 1 397 ? 135.211 153.605 123.720 1.00 30.65 ? 397 TYR B CD2   1 
ATOM   8767  C  CE1   . TYR B 1 397 ? 136.318 155.628 122.210 1.00 34.51 ? 397 TYR B CE1   1 
ATOM   8768  C  CE2   . TYR B 1 397 ? 136.519 153.985 123.935 1.00 33.41 ? 397 TYR B CE2   1 
ATOM   8769  C  CZ    . TYR B 1 397 ? 137.067 154.997 123.177 1.00 36.73 ? 397 TYR B CZ    1 
ATOM   8770  O  OH    . TYR B 1 397 ? 138.369 155.381 123.387 1.00 38.38 ? 397 TYR B OH    1 
ATOM   8771  N  N     . ASP B 1 398 ? 131.627 156.636 122.020 1.00 43.37 ? 398 ASP B N     1 
ATOM   8772  C  CA    . ASP B 1 398 ? 131.820 158.052 121.723 1.00 44.01 ? 398 ASP B CA    1 
ATOM   8773  C  C     . ASP B 1 398 ? 130.969 158.944 122.618 1.00 46.46 ? 398 ASP B C     1 
ATOM   8774  O  O     . ASP B 1 398 ? 131.337 160.097 122.868 1.00 48.15 ? 398 ASP B O     1 
ATOM   8775  C  CB    . ASP B 1 398 ? 131.507 158.323 120.252 1.00 45.11 ? 398 ASP B CB    1 
ATOM   8776  C  CG    . ASP B 1 398 ? 130.256 157.607 119.781 1.00 48.58 ? 398 ASP B CG    1 
ATOM   8777  O  OD1   . ASP B 1 398 ? 130.179 156.373 119.952 1.00 47.76 ? 398 ASP B OD1   1 
ATOM   8778  O  OD2   . ASP B 1 398 ? 129.354 158.275 119.237 1.00 49.12 ? 398 ASP B OD2   1 
ATOM   8779  N  N     . GLU B 1 399 ? 129.842 158.439 123.106 1.00 46.66 ? 399 GLU B N     1 
ATOM   8780  C  CA    . GLU B 1 399 ? 128.909 159.238 123.883 1.00 43.51 ? 399 GLU B CA    1 
ATOM   8781  C  C     . GLU B 1 399 ? 129.329 159.300 125.350 1.00 47.90 ? 399 GLU B C     1 
ATOM   8782  O  O     . GLU B 1 399 ? 130.227 158.587 125.803 1.00 46.78 ? 399 GLU B O     1 
ATOM   8783  C  CB    . GLU B 1 399 ? 127.495 158.674 123.758 1.00 44.38 ? 399 GLU B CB    1 
ATOM   8784  C  CG    . GLU B 1 399 ? 126.851 158.912 122.406 1.00 47.83 ? 399 GLU B CG    1 
ATOM   8785  C  CD    . GLU B 1 399 ? 125.809 157.867 122.069 1.00 50.18 ? 399 GLU B CD    1 
ATOM   8786  O  OE1   . GLU B 1 399 ? 125.198 157.313 123.007 1.00 48.92 ? 399 GLU B OE1   1 
ATOM   8787  O  OE2   . GLU B 1 399 ? 125.600 157.601 120.866 1.00 51.38 ? 399 GLU B OE2   1 
ATOM   8788  N  N     . GLU B 1 400 ? 128.658 160.175 126.096 1.00 47.70 ? 400 GLU B N     1 
ATOM   8789  C  CA    . GLU B 1 400 ? 128.916 160.351 127.519 1.00 41.57 ? 400 GLU B CA    1 
ATOM   8790  C  C     . GLU B 1 400 ? 127.962 159.485 128.330 1.00 43.76 ? 400 GLU B C     1 
ATOM   8791  O  O     . GLU B 1 400 ? 126.749 159.501 128.098 1.00 42.18 ? 400 GLU B O     1 
ATOM   8792  C  CB    . GLU B 1 400 ? 128.762 161.820 127.916 1.00 41.97 ? 400 GLU B CB    1 
ATOM   8793  C  CG    . GLU B 1 400 ? 129.998 162.671 127.672 1.00 46.86 ? 400 GLU B CG    1 
ATOM   8794  C  CD    . GLU B 1 400 ? 131.205 162.187 128.453 1.00 50.33 ? 400 GLU B CD    1 
ATOM   8795  O  OE1   . GLU B 1 400 ? 131.033 161.756 129.613 1.00 50.55 ? 400 GLU B OE1   1 
ATOM   8796  O  OE2   . GLU B 1 400 ? 132.326 162.239 127.908 1.00 47.63 ? 400 GLU B OE2   1 
ATOM   8797  N  N     . ASP B 1 401 ? 128.512 158.733 129.277 1.00 42.40 ? 401 ASP B N     1 
ATOM   8798  C  CA    . ASP B 1 401 ? 127.704 157.859 130.113 1.00 37.92 ? 401 ASP B CA    1 
ATOM   8799  C  C     . ASP B 1 401 ? 126.973 158.655 131.186 1.00 38.63 ? 401 ASP B C     1 
ATOM   8800  O  O     . ASP B 1 401 ? 127.440 159.703 131.643 1.00 40.98 ? 401 ASP B O     1 
ATOM   8801  C  CB    . ASP B 1 401 ? 128.574 156.790 130.773 1.00 37.06 ? 401 ASP B CB    1 
ATOM   8802  C  CG    . ASP B 1 401 ? 129.240 155.877 129.769 1.00 39.60 ? 401 ASP B CG    1 
ATOM   8803  O  OD1   . ASP B 1 401 ? 128.619 155.578 128.729 1.00 42.83 ? 401 ASP B OD1   1 
ATOM   8804  O  OD2   . ASP B 1 401 ? 130.387 155.457 130.021 1.00 40.34 ? 401 ASP B OD2   1 
ATOM   8805  N  N     . GLU B 1 402 ? 125.812 158.143 131.586 1.00 37.75 ? 402 GLU B N     1 
ATOM   8806  C  CA    . GLU B 1 402 ? 125.026 158.714 132.677 1.00 33.47 ? 402 GLU B CA    1 
ATOM   8807  C  C     . GLU B 1 402 ? 125.284 157.867 133.916 1.00 34.71 ? 402 GLU B C     1 
ATOM   8808  O  O     . GLU B 1 402 ? 124.697 156.796 134.084 1.00 38.18 ? 402 GLU B O     1 
ATOM   8809  C  CB    . GLU B 1 402 ? 123.544 158.756 132.320 1.00 36.33 ? 402 GLU B CB    1 
ATOM   8810  C  CG    . GLU B 1 402 ? 122.918 160.154 132.185 1.00 39.63 ? 402 GLU B CG    1 
ATOM   8811  C  CD    . GLU B 1 402 ? 123.002 161.039 133.434 1.00 45.56 ? 402 GLU B CD    1 
ATOM   8812  O  OE1   . GLU B 1 402 ? 122.250 162.035 133.480 1.00 44.36 ? 402 GLU B OE1   1 
ATOM   8813  O  OE2   . GLU B 1 402 ? 123.778 160.758 134.371 1.00 46.66 ? 402 GLU B OE2   1 
ATOM   8814  N  N     . ILE B 1 403 ? 126.163 158.352 134.784 1.00 32.26 ? 403 ILE B N     1 
ATOM   8815  C  CA    . ILE B 1 403 ? 126.607 157.582 135.939 1.00 29.09 ? 403 ILE B CA    1 
ATOM   8816  C  C     . ILE B 1 403 ? 125.569 157.687 137.048 1.00 30.45 ? 403 ILE B C     1 
ATOM   8817  O  O     . ILE B 1 403 ? 125.145 158.788 137.419 1.00 31.60 ? 403 ILE B O     1 
ATOM   8818  C  CB    . ILE B 1 403 ? 127.983 158.070 136.415 1.00 25.16 ? 403 ILE B CB    1 
ATOM   8819  C  CG1   . ILE B 1 403 ? 129.042 157.801 135.343 1.00 27.13 ? 403 ILE B CG1   1 
ATOM   8820  C  CG2   . ILE B 1 403 ? 128.357 157.406 137.722 1.00 25.46 ? 403 ILE B CG2   1 
ATOM   8821  C  CD1   . ILE B 1 403 ? 129.062 156.375 134.850 1.00 30.54 ? 403 ILE B CD1   1 
ATOM   8822  N  N     . GLY B 1 404 ? 125.157 156.542 137.575 1.00 25.65 ? 404 GLY B N     1 
ATOM   8823  C  CA    . GLY B 1 404 ? 124.231 156.455 138.684 1.00 16.69 ? 404 GLY B CA    1 
ATOM   8824  C  C     . GLY B 1 404 ? 124.933 156.222 140.004 1.00 22.51 ? 404 GLY B C     1 
ATOM   8825  O  O     . GLY B 1 404 ? 126.072 156.654 140.216 1.00 31.98 ? 404 GLY B O     1 
ATOM   8826  N  N     . LEU B 1 405 ? 124.247 155.529 140.909 1.00 24.46 ? 405 LEU B N     1 
ATOM   8827  C  CA    . LEU B 1 405 ? 124.778 155.214 142.230 1.00 11.61 ? 405 LEU B CA    1 
ATOM   8828  C  C     . LEU B 1 405 ? 124.802 153.704 142.411 1.00 14.43 ? 405 LEU B C     1 
ATOM   8829  O  O     . LEU B 1 405 ? 123.751 153.056 142.371 1.00 20.50 ? 405 LEU B O     1 
ATOM   8830  C  CB    . LEU B 1 405 ? 123.941 155.870 143.330 1.00 19.53 ? 405 LEU B CB    1 
ATOM   8831  C  CG    . LEU B 1 405 ? 123.820 157.393 143.291 1.00 18.09 ? 405 LEU B CG    1 
ATOM   8832  C  CD1   . LEU B 1 405 ? 122.852 157.871 144.355 1.00 23.25 ? 405 LEU B CD1   1 
ATOM   8833  C  CD2   . LEU B 1 405 ? 125.178 158.045 143.467 1.00 19.52 ? 405 LEU B CD2   1 
ATOM   8834  N  N     . ASP B 1 406 ? 125.993 153.152 142.618 1.00 23.90 ? 406 ASP B N     1 
ATOM   8835  C  CA    . ASP B 1 406 ? 126.169 151.739 142.920 1.00 15.08 ? 406 ASP B CA    1 
ATOM   8836  C  C     . ASP B 1 406 ? 126.688 151.590 144.343 1.00 23.15 ? 406 ASP B C     1 
ATOM   8837  O  O     . ASP B 1 406 ? 127.623 152.285 144.749 1.00 31.60 ? 406 ASP B O     1 
ATOM   8838  C  CB    . ASP B 1 406 ? 127.130 151.074 141.935 1.00 19.15 ? 406 ASP B CB    1 
ATOM   8839  C  CG    . ASP B 1 406 ? 126.479 150.765 140.601 1.00 31.61 ? 406 ASP B CG    1 
ATOM   8840  O  OD1   . ASP B 1 406 ? 125.252 150.958 140.472 1.00 34.31 ? 406 ASP B OD1   1 
ATOM   8841  O  OD2   . ASP B 1 406 ? 127.198 150.327 139.679 1.00 30.62 ? 406 ASP B OD2   1 
ATOM   8842  N  N     . ILE B 1 407 ? 126.093 150.670 145.086 1.00 27.77 ? 407 ILE B N     1 
ATOM   8843  C  CA    . ILE B 1 407 ? 126.290 150.599 146.528 1.00 17.80 ? 407 ILE B CA    1 
ATOM   8844  C  C     . ILE B 1 407 ? 127.634 149.960 146.851 1.00 18.30 ? 407 ILE B C     1 
ATOM   8845  O  O     . ILE B 1 407 ? 128.045 148.975 146.227 1.00 23.86 ? 407 ILE B O     1 
ATOM   8846  C  CB    . ILE B 1 407 ? 125.135 149.826 147.185 1.00 13.12 ? 407 ILE B CB    1 
ATOM   8847  C  CG1   . ILE B 1 407 ? 123.795 150.467 146.833 1.00 7.20  ? 407 ILE B CG1   1 
ATOM   8848  C  CG2   . ILE B 1 407 ? 125.315 149.779 148.674 1.00 18.32 ? 407 ILE B CG2   1 
ATOM   8849  C  CD1   . ILE B 1 407 ? 122.707 149.465 146.575 1.00 18.19 ? 407 ILE B CD1   1 
ATOM   8850  N  N     . SER B 1 408 ? 128.322 150.531 147.837 1.00 26.15 ? 408 SER B N     1 
ATOM   8851  C  CA    . SER B 1 408 ? 129.544 149.952 148.390 1.00 24.91 ? 408 SER B CA    1 
ATOM   8852  C  C     . SER B 1 408 ? 129.770 150.578 149.755 1.00 27.48 ? 408 SER B C     1 
ATOM   8853  O  O     . SER B 1 408 ? 130.008 151.786 149.844 1.00 36.29 ? 408 SER B O     1 
ATOM   8854  C  CB    . SER B 1 408 ? 130.738 150.205 147.473 1.00 29.29 ? 408 SER B CB    1 
ATOM   8855  O  OG    . SER B 1 408 ? 131.434 151.378 147.856 1.00 31.92 ? 408 SER B OG    1 
ATOM   8856  N  N     . CYS B 1 409 ? 129.696 149.775 150.812 1.00 22.81 ? 409 CYS B N     1 
ATOM   8857  C  CA    . CYS B 1 409 ? 129.828 150.285 152.167 1.00 29.25 ? 409 CYS B CA    1 
ATOM   8858  C  C     . CYS B 1 409 ? 130.984 149.601 152.886 1.00 26.43 ? 409 CYS B C     1 
ATOM   8859  O  O     . CYS B 1 409 ? 131.385 148.484 152.551 1.00 25.09 ? 409 CYS B O     1 
ATOM   8860  C  CB    . CYS B 1 409 ? 128.523 150.112 152.961 1.00 26.21 ? 409 CYS B CB    1 
ATOM   8861  S  SG    . CYS B 1 409 ? 128.382 148.592 153.917 1.00 36.43 ? 409 CYS B SG    1 
ATOM   8862  N  N     . ASN B 1 410 ? 131.516 150.301 153.883 1.00 23.11 ? 410 ASN B N     1 
ATOM   8863  C  CA    . ASN B 1 410 ? 132.674 149.854 154.644 1.00 22.25 ? 410 ASN B CA    1 
ATOM   8864  C  C     . ASN B 1 410 ? 132.199 149.143 155.901 1.00 23.62 ? 410 ASN B C     1 
ATOM   8865  O  O     . ASN B 1 410 ? 131.301 149.631 156.593 1.00 28.99 ? 410 ASN B O     1 
ATOM   8866  C  CB    . ASN B 1 410 ? 133.563 151.041 155.011 1.00 26.61 ? 410 ASN B CB    1 
ATOM   8867  C  CG    . ASN B 1 410 ? 133.455 152.171 154.012 1.00 33.58 ? 410 ASN B CG    1 
ATOM   8868  O  OD1   . ASN B 1 410 ? 132.739 153.142 154.240 1.00 33.93 ? 410 ASN B OD1   1 
ATOM   8869  N  ND2   . ASN B 1 410 ? 134.157 152.046 152.893 1.00 32.89 ? 410 ASN B ND2   1 
ATOM   8870  N  N     . LEU B 1 411 ? 132.808 148.002 156.200 1.00 18.04 ? 411 LEU B N     1 
ATOM   8871  C  CA    . LEU B 1 411 ? 132.339 147.124 157.261 1.00 12.46 ? 411 LEU B CA    1 
ATOM   8872  C  C     . LEU B 1 411 ? 133.202 147.257 158.507 1.00 14.35 ? 411 LEU B C     1 
ATOM   8873  O  O     . LEU B 1 411 ? 134.426 147.388 158.423 1.00 23.17 ? 411 LEU B O     1 
ATOM   8874  C  CB    . LEU B 1 411 ? 132.332 145.669 156.793 1.00 21.34 ? 411 LEU B CB    1 
ATOM   8875  C  CG    . LEU B 1 411 ? 131.488 145.325 155.569 1.00 18.70 ? 411 LEU B CG    1 
ATOM   8876  C  CD1   . LEU B 1 411 ? 131.229 143.838 155.521 1.00 23.25 ? 411 LEU B CD1   1 
ATOM   8877  C  CD2   . LEU B 1 411 ? 130.179 146.082 155.608 1.00 18.89 ? 411 LEU B CD2   1 
ATOM   8878  N  N     . GLY B 1 412 ? 132.547 147.229 159.662 1.00 19.27 ? 412 GLY B N     1 
ATOM   8879  C  CA    . GLY B 1 412 ? 133.230 147.151 160.938 1.00 9.70  ? 412 GLY B CA    1 
ATOM   8880  C  C     . GLY B 1 412 ? 132.301 146.509 161.942 1.00 13.65 ? 412 GLY B C     1 
ATOM   8881  O  O     . GLY B 1 412 ? 131.075 146.597 161.824 1.00 28.24 ? 412 GLY B O     1 
ATOM   8882  N  N     . SER B 1 413 ? 132.892 145.854 162.936 1.00 13.87 ? 413 SER B N     1 
ATOM   8883  C  CA    . SER B 1 413 ? 132.119 145.087 163.903 1.00 15.44 ? 413 SER B CA    1 
ATOM   8884  C  C     . SER B 1 413 ? 132.502 145.467 165.322 1.00 17.34 ? 413 SER B C     1 
ATOM   8885  O  O     . SER B 1 413 ? 133.682 145.431 165.683 1.00 22.58 ? 413 SER B O     1 
ATOM   8886  C  CB    . SER B 1 413 ? 132.315 143.584 163.699 1.00 12.70 ? 413 SER B CB    1 
ATOM   8887  O  OG    . SER B 1 413 ? 131.611 143.143 162.557 1.00 27.90 ? 413 SER B OG    1 
ATOM   8888  N  N     . LEU B 1 414 ? 131.502 145.825 166.119 1.00 18.00 ? 414 LEU B N     1 
ATOM   8889  C  CA    . LEU B 1 414 ? 131.693 145.929 167.556 1.00 12.84 ? 414 LEU B CA    1 
ATOM   8890  C  C     . LEU B 1 414 ? 131.699 144.541 168.177 1.00 21.22 ? 414 LEU B C     1 
ATOM   8891  O  O     . LEU B 1 414 ? 130.905 143.673 167.805 1.00 25.86 ? 414 LEU B O     1 
ATOM   8892  C  CB    . LEU B 1 414 ? 130.585 146.767 168.189 1.00 18.95 ? 414 LEU B CB    1 
ATOM   8893  C  CG    . LEU B 1 414 ? 130.209 148.093 167.536 1.00 20.76 ? 414 LEU B CG    1 
ATOM   8894  C  CD1   . LEU B 1 414 ? 128.957 148.642 168.185 1.00 22.42 ? 414 LEU B CD1   1 
ATOM   8895  C  CD2   . LEU B 1 414 ? 131.348 149.084 167.655 1.00 23.82 ? 414 LEU B CD2   1 
ATOM   8896  N  N     . ASN B 1 415 ? 132.603 144.329 169.124 1.00 27.87 ? 415 ASN B N     1 
ATOM   8897  C  CA    . ASN B 1 415 ? 132.584 143.129 169.949 1.00 25.52 ? 415 ASN B CA    1 
ATOM   8898  C  C     . ASN B 1 415 ? 131.655 143.401 171.125 1.00 24.57 ? 415 ASN B C     1 
ATOM   8899  O  O     . ASN B 1 415 ? 131.997 144.171 172.026 1.00 28.36 ? 415 ASN B O     1 
ATOM   8900  C  CB    . ASN B 1 415 ? 133.990 142.768 170.412 1.00 22.33 ? 415 ASN B CB    1 
ATOM   8901  C  CG    . ASN B 1 415 ? 134.094 141.346 170.918 1.00 21.93 ? 415 ASN B CG    1 
ATOM   8902  O  OD1   . ASN B 1 415 ? 133.315 140.918 171.767 1.00 34.00 ? 415 ASN B OD1   1 
ATOM   8903  N  ND2   . ASN B 1 415 ? 135.064 140.606 170.399 1.00 28.20 ? 415 ASN B ND2   1 
ATOM   8904  N  N     . ILE B 1 416 ? 130.476 142.777 171.107 1.00 19.41 ? 416 ILE B N     1 
ATOM   8905  C  CA    . ILE B 1 416 ? 129.455 143.079 172.106 1.00 21.88 ? 416 ILE B CA    1 
ATOM   8906  C  C     . ILE B 1 416 ? 129.950 142.730 173.504 1.00 27.27 ? 416 ILE B C     1 
ATOM   8907  O  O     . ILE B 1 416 ? 129.698 143.464 174.466 1.00 26.38 ? 416 ILE B O     1 
ATOM   8908  C  CB    . ILE B 1 416 ? 128.142 142.350 171.761 1.00 26.02 ? 416 ILE B CB    1 
ATOM   8909  C  CG1   . ILE B 1 416 ? 127.521 142.952 170.500 1.00 20.98 ? 416 ILE B CG1   1 
ATOM   8910  C  CG2   . ILE B 1 416 ? 127.159 142.425 172.913 1.00 12.75 ? 416 ILE B CG2   1 
ATOM   8911  C  CD1   . ILE B 1 416 ? 126.315 142.204 169.991 1.00 16.91 ? 416 ILE B CD1   1 
ATOM   8912  N  N     . LEU B 1 417 ? 130.675 141.618 173.639 1.00 21.31 ? 417 LEU B N     1 
ATOM   8913  C  CA    . LEU B 1 417 ? 131.191 141.227 174.947 1.00 25.64 ? 417 LEU B CA    1 
ATOM   8914  C  C     . LEU B 1 417 ? 132.195 142.245 175.476 1.00 29.16 ? 417 LEU B C     1 
ATOM   8915  O  O     . LEU B 1 417 ? 132.106 142.679 176.630 1.00 35.93 ? 417 LEU B O     1 
ATOM   8916  C  CB    . LEU B 1 417 ? 131.825 139.839 174.864 1.00 29.24 ? 417 LEU B CB    1 
ATOM   8917  C  CG    . LEU B 1 417 ? 132.619 139.366 176.082 1.00 29.51 ? 417 LEU B CG    1 
ATOM   8918  C  CD1   . LEU B 1 417 ? 131.697 138.766 177.128 1.00 27.46 ? 417 LEU B CD1   1 
ATOM   8919  C  CD2   . LEU B 1 417 ? 133.684 138.368 175.669 1.00 32.92 ? 417 LEU B CD2   1 
ATOM   8920  N  N     . ASN B 1 418 ? 133.152 142.650 174.640 1.00 29.31 ? 418 ASN B N     1 
ATOM   8921  C  CA    . ASN B 1 418 ? 134.187 143.577 175.083 1.00 27.60 ? 418 ASN B CA    1 
ATOM   8922  C  C     . ASN B 1 418 ? 133.660 144.997 175.233 1.00 28.60 ? 418 ASN B C     1 
ATOM   8923  O  O     . ASN B 1 418 ? 134.097 145.723 176.132 1.00 33.46 ? 418 ASN B O     1 
ATOM   8924  C  CB    . ASN B 1 418 ? 135.364 143.551 174.110 1.00 26.91 ? 418 ASN B CB    1 
ATOM   8925  C  CG    . ASN B 1 418 ? 136.154 142.265 174.194 1.00 27.73 ? 418 ASN B CG    1 
ATOM   8926  O  OD1   . ASN B 1 418 ? 136.303 141.687 175.268 1.00 32.57 ? 418 ASN B OD1   1 
ATOM   8927  N  ND2   . ASN B 1 418 ? 136.660 141.806 173.059 1.00 30.43 ? 418 ASN B ND2   1 
ATOM   8928  N  N     . VAL B 1 419 ? 132.737 145.412 174.366 1.00 31.07 ? 419 VAL B N     1 
ATOM   8929  C  CA    . VAL B 1 419 ? 132.117 146.724 174.511 1.00 31.05 ? 419 VAL B CA    1 
ATOM   8930  C  C     . VAL B 1 419 ? 131.268 146.771 175.775 1.00 31.11 ? 419 VAL B C     1 
ATOM   8931  O  O     . VAL B 1 419 ? 131.233 147.784 176.483 1.00 33.74 ? 419 VAL B O     1 
ATOM   8932  C  CB    . VAL B 1 419 ? 131.293 147.057 173.253 1.00 28.93 ? 419 VAL B CB    1 
ATOM   8933  C  CG1   . VAL B 1 419 ? 130.317 148.179 173.526 1.00 33.11 ? 419 VAL B CG1   1 
ATOM   8934  C  CG2   . VAL B 1 419 ? 132.210 147.420 172.104 1.00 25.62 ? 419 VAL B CG2   1 
ATOM   8935  N  N     . MET B 1 420 ? 130.588 145.668 176.089 1.00 35.38 ? 420 MET B N     1 
ATOM   8936  C  CA    . MET B 1 420 ? 129.716 145.632 177.255 1.00 33.04 ? 420 MET B CA    1 
ATOM   8937  C  C     . MET B 1 420 ? 130.523 145.571 178.546 1.00 31.79 ? 420 MET B C     1 
ATOM   8938  O  O     . MET B 1 420 ? 130.158 146.203 179.543 1.00 34.92 ? 420 MET B O     1 
ATOM   8939  C  CB    . MET B 1 420 ? 128.772 144.436 177.150 1.00 32.66 ? 420 MET B CB    1 
ATOM   8940  C  CG    . MET B 1 420 ? 127.401 144.764 176.581 1.00 26.09 ? 420 MET B CG    1 
ATOM   8941  S  SD    . MET B 1 420 ? 126.865 146.444 176.931 1.00 39.47 ? 420 MET B SD    1 
ATOM   8942  C  CE    . MET B 1 420 ? 126.088 146.205 178.521 1.00 32.75 ? 420 MET B CE    1 
ATOM   8943  N  N     . GLU B 1 421 ? 131.626 144.816 178.546 1.00 38.20 ? 421 GLU B N     1 
ATOM   8944  C  CA    . GLU B 1 421 ? 132.454 144.720 179.744 1.00 37.44 ? 421 GLU B CA    1 
ATOM   8945  C  C     . GLU B 1 421 ? 133.219 146.012 180.009 1.00 36.46 ? 421 GLU B C     1 
ATOM   8946  O  O     . GLU B 1 421 ? 133.529 146.317 181.166 1.00 38.73 ? 421 GLU B O     1 
ATOM   8947  C  CB    . GLU B 1 421 ? 133.415 143.535 179.624 1.00 33.23 ? 421 GLU B CB    1 
ATOM   8948  C  CG    . GLU B 1 421 ? 134.711 143.840 178.890 1.00 38.11 ? 421 GLU B CG    1 
ATOM   8949  C  CD    . GLU B 1 421 ? 135.736 142.731 179.018 1.00 44.10 ? 421 GLU B CD    1 
ATOM   8950  O  OE1   . GLU B 1 421 ? 136.497 142.733 180.008 1.00 41.37 ? 421 GLU B OE1   1 
ATOM   8951  O  OE2   . GLU B 1 421 ? 135.785 141.860 178.124 1.00 41.59 ? 421 GLU B OE2   1 
ATOM   8952  N  N     . HIS B 1 422 ? 133.529 146.779 178.965 1.00 36.06 ? 422 HIS B N     1 
ATOM   8953  C  CA    . HIS B 1 422 ? 134.202 148.060 179.121 1.00 36.33 ? 422 HIS B CA    1 
ATOM   8954  C  C     . HIS B 1 422 ? 133.238 149.215 179.349 1.00 40.01 ? 422 HIS B C     1 
ATOM   8955  O  O     . HIS B 1 422 ? 133.692 150.329 179.630 1.00 41.91 ? 422 HIS B O     1 
ATOM   8956  C  CB    . HIS B 1 422 ? 135.065 148.364 177.891 1.00 34.84 ? 422 HIS B CB    1 
ATOM   8957  C  CG    . HIS B 1 422 ? 136.407 147.702 177.913 1.00 37.15 ? 422 HIS B CG    1 
ATOM   8958  N  ND1   . HIS B 1 422 ? 136.565 146.335 177.834 1.00 38.78 ? 422 HIS B ND1   1 
ATOM   8959  C  CD2   . HIS B 1 422 ? 137.655 148.220 178.001 1.00 38.92 ? 422 HIS B CD2   1 
ATOM   8960  C  CE1   . HIS B 1 422 ? 137.852 146.039 177.874 1.00 40.11 ? 422 HIS B CE1   1 
ATOM   8961  N  NE2   . HIS B 1 422 ? 138.535 147.165 177.975 1.00 41.10 ? 422 HIS B NE2   1 
ATOM   8962  N  N     . LYS B 1 423 ? 131.930 148.973 179.239 1.00 43.02 ? 423 LYS B N     1 
ATOM   8963  C  CA    . LYS B 1 423 ? 130.912 150.011 179.403 1.00 43.77 ? 423 LYS B CA    1 
ATOM   8964  C  C     . LYS B 1 423 ? 131.169 151.184 178.462 1.00 46.29 ? 423 LYS B C     1 
ATOM   8965  O  O     . LYS B 1 423 ? 131.020 152.351 178.828 1.00 47.45 ? 423 LYS B O     1 
ATOM   8966  C  CB    . LYS B 1 423 ? 130.837 150.483 180.856 1.00 42.53 ? 423 LYS B CB    1 
ATOM   8967  C  CG    . LYS B 1 423 ? 130.192 149.485 181.801 1.00 44.37 ? 423 LYS B CG    1 
ATOM   8968  C  CD    . LYS B 1 423 ? 131.168 149.042 182.878 1.00 47.20 ? 423 LYS B CD    1 
ATOM   8969  C  CE    . LYS B 1 423 ? 130.632 147.851 183.655 1.00 46.20 ? 423 LYS B CE    1 
ATOM   8970  N  NZ    . LYS B 1 423 ? 131.074 146.555 183.067 1.00 42.07 ? 423 LYS B NZ    1 
ATOM   8971  N  N     . SER B 1 424 ? 131.556 150.868 177.230 1.00 32.91 ? 424 SER B N     1 
ATOM   8972  C  CA    . SER B 1 424 ? 132.004 151.858 176.257 1.00 32.65 ? 424 SER B CA    1 
ATOM   8973  C  C     . SER B 1 424 ? 131.240 151.717 174.949 1.00 35.86 ? 424 SER B C     1 
ATOM   8974  O  O     . SER B 1 424 ? 131.825 151.654 173.868 1.00 36.88 ? 424 SER B O     1 
ATOM   8975  C  CB    . SER B 1 424 ? 133.504 151.734 176.014 1.00 36.12 ? 424 SER B CB    1 
ATOM   8976  O  OG    . SER B 1 424 ? 133.811 150.532 175.330 1.00 35.13 ? 424 SER B OG    1 
ATOM   8977  N  N     . ILE B 1 425 ? 129.910 151.653 175.027 1.00 34.82 ? 425 ILE B N     1 
ATOM   8978  C  CA    . ILE B 1 425 ? 129.109 151.618 173.805 1.00 29.28 ? 425 ILE B CA    1 
ATOM   8979  C  C     . ILE B 1 425 ? 129.287 152.912 173.022 1.00 33.98 ? 425 ILE B C     1 
ATOM   8980  O  O     . ILE B 1 425 ? 129.550 152.897 171.815 1.00 38.47 ? 425 ILE B O     1 
ATOM   8981  C  CB    . ILE B 1 425 ? 127.628 151.358 174.131 1.00 33.96 ? 425 ILE B CB    1 
ATOM   8982  C  CG1   . ILE B 1 425 ? 127.430 149.930 174.637 1.00 33.91 ? 425 ILE B CG1   1 
ATOM   8983  C  CG2   . ILE B 1 425 ? 126.765 151.601 172.904 1.00 30.59 ? 425 ILE B CG2   1 
ATOM   8984  C  CD1   . ILE B 1 425 ? 125.990 149.583 174.927 1.00 34.59 ? 425 ILE B CD1   1 
ATOM   8985  N  N     . GLU B 1 426 ? 129.171 154.051 173.706 1.00 31.78 ? 426 GLU B N     1 
ATOM   8986  C  CA    . GLU B 1 426 ? 129.244 155.340 173.026 1.00 30.88 ? 426 GLU B CA    1 
ATOM   8987  C  C     . GLU B 1 426 ? 130.614 155.562 172.395 1.00 31.17 ? 426 GLU B C     1 
ATOM   8988  O  O     . GLU B 1 426 ? 130.718 155.887 171.206 1.00 39.01 ? 426 GLU B O     1 
ATOM   8989  C  CB    . GLU B 1 426 ? 128.917 156.462 174.010 1.00 32.16 ? 426 GLU B CB    1 
ATOM   8990  C  CG    . GLU B 1 426 ? 129.346 157.842 173.552 1.00 31.96 ? 426 GLU B CG    1 
ATOM   8991  C  CD    . GLU B 1 426 ? 129.166 158.889 174.631 1.00 38.84 ? 426 GLU B CD    1 
ATOM   8992  O  OE1   . GLU B 1 426 ? 128.810 158.515 175.767 1.00 39.75 ? 426 GLU B OE1   1 
ATOM   8993  O  OE2   . GLU B 1 426 ? 129.380 160.085 174.345 1.00 42.48 ? 426 GLU B OE2   1 
ATOM   8994  N  N     . LYS B 1 427 ? 131.679 155.389 173.181 1.00 32.20 ? 427 LYS B N     1 
ATOM   8995  C  CA    . LYS B 1 427 ? 133.023 155.667 172.686 1.00 31.05 ? 427 LYS B CA    1 
ATOM   8996  C  C     . LYS B 1 427 ? 133.407 154.714 171.563 1.00 31.95 ? 427 LYS B C     1 
ATOM   8997  O  O     . LYS B 1 427 ? 133.953 155.143 170.539 1.00 35.32 ? 427 LYS B O     1 
ATOM   8998  C  CB    . LYS B 1 427 ? 134.058 155.595 173.820 1.00 33.28 ? 427 LYS B CB    1 
ATOM   8999  C  CG    . LYS B 1 427 ? 134.048 156.742 174.859 1.00 38.58 ? 427 LYS B CG    1 
ATOM   9000  C  CD    . LYS B 1 427 ? 132.783 156.906 175.720 1.00 37.25 ? 427 LYS B CD    1 
ATOM   9001  C  CE    . LYS B 1 427 ? 132.157 155.574 176.130 1.00 35.00 ? 427 LYS B CE    1 
ATOM   9002  N  NZ    . LYS B 1 427 ? 131.039 155.750 177.096 1.00 38.09 ? 427 LYS B NZ    1 
ATOM   9003  N  N     . THR B 1 428 ? 133.130 153.419 171.733 1.00 29.42 ? 428 THR B N     1 
ATOM   9004  C  CA    . THR B 1 428 ? 133.452 152.456 170.686 1.00 25.12 ? 428 THR B CA    1 
ATOM   9005  C  C     . THR B 1 428 ? 132.655 152.729 169.420 1.00 26.69 ? 428 THR B C     1 
ATOM   9006  O  O     . THR B 1 428 ? 133.202 152.670 168.315 1.00 33.18 ? 428 THR B O     1 
ATOM   9007  C  CB    . THR B 1 428 ? 133.203 151.029 171.171 1.00 23.73 ? 428 THR B CB    1 
ATOM   9008  O  OG1   . THR B 1 428 ? 133.842 150.834 172.438 1.00 26.74 ? 428 THR B OG1   1 
ATOM   9009  C  CG2   . THR B 1 428 ? 133.758 150.031 170.173 1.00 27.40 ? 428 THR B CG2   1 
ATOM   9010  N  N     . VAL B 1 429 ? 131.362 153.036 169.558 1.00 25.83 ? 429 VAL B N     1 
ATOM   9011  C  CA    . VAL B 1 429 ? 130.538 153.302 168.384 1.00 24.48 ? 429 VAL B CA    1 
ATOM   9012  C  C     . VAL B 1 429 ? 131.048 154.530 167.642 1.00 24.71 ? 429 VAL B C     1 
ATOM   9013  O  O     . VAL B 1 429 ? 131.166 154.524 166.412 1.00 29.24 ? 429 VAL B O     1 
ATOM   9014  C  CB    . VAL B 1 429 ? 129.058 153.456 168.787 1.00 25.49 ? 429 VAL B CB    1 
ATOM   9015  C  CG1   . VAL B 1 429 ? 128.296 154.221 167.725 1.00 23.57 ? 429 VAL B CG1   1 
ATOM   9016  C  CG2   . VAL B 1 429 ? 128.424 152.097 168.995 1.00 25.65 ? 429 VAL B CG2   1 
ATOM   9017  N  N     . LYS B 1 430 ? 131.377 155.595 168.375 1.00 28.04 ? 430 LYS B N     1 
ATOM   9018  C  CA    . LYS B 1 430 ? 131.820 156.822 167.721 1.00 25.18 ? 430 LYS B CA    1 
ATOM   9019  C  C     . LYS B 1 430 ? 133.188 156.651 167.068 1.00 24.00 ? 430 LYS B C     1 
ATOM   9020  O  O     . LYS B 1 430 ? 133.409 157.130 165.949 1.00 29.82 ? 430 LYS B O     1 
ATOM   9021  C  CB    . LYS B 1 430 ? 131.827 157.972 168.725 1.00 26.98 ? 430 LYS B CB    1 
ATOM   9022  C  CG    . LYS B 1 430 ? 130.432 158.368 169.178 1.00 24.33 ? 430 LYS B CG    1 
ATOM   9023  C  CD    . LYS B 1 430 ? 130.424 159.690 169.913 1.00 30.27 ? 430 LYS B CD    1 
ATOM   9024  C  CE    . LYS B 1 430 ? 129.005 160.120 170.235 1.00 32.80 ? 430 LYS B CE    1 
ATOM   9025  N  NZ    . LYS B 1 430 ? 128.971 161.376 171.028 1.00 33.73 ? 430 LYS B NZ    1 
ATOM   9026  N  N     . LEU B 1 431 ? 134.116 155.963 167.738 1.00 29.62 ? 431 LEU B N     1 
ATOM   9027  C  CA    . LEU B 1 431 ? 135.425 155.728 167.135 1.00 23.11 ? 431 LEU B CA    1 
ATOM   9028  C  C     . LEU B 1 431 ? 135.321 154.814 165.920 1.00 24.31 ? 431 LEU B C     1 
ATOM   9029  O  O     . LEU B 1 431 ? 136.018 155.022 164.919 1.00 30.99 ? 431 LEU B O     1 
ATOM   9030  C  CB    . LEU B 1 431 ? 136.381 155.143 168.171 1.00 29.90 ? 431 LEU B CB    1 
ATOM   9031  C  CG    . LEU B 1 431 ? 137.258 156.142 168.925 1.00 31.80 ? 431 LEU B CG    1 
ATOM   9032  C  CD1   . LEU B 1 431 ? 138.014 155.443 170.040 1.00 28.71 ? 431 LEU B CD1   1 
ATOM   9033  C  CD2   . LEU B 1 431 ? 138.216 156.839 167.977 1.00 33.53 ? 431 LEU B CD2   1 
ATOM   9034  N  N     . ALA B 1 432 ? 134.463 153.793 165.988 1.00 24.77 ? 432 ALA B N     1 
ATOM   9035  C  CA    . ALA B 1 432 ? 134.245 152.927 164.837 1.00 19.70 ? 432 ALA B CA    1 
ATOM   9036  C  C     . ALA B 1 432 ? 133.630 153.701 163.681 1.00 25.37 ? 432 ALA B C     1 
ATOM   9037  O  O     . ALA B 1 432 ? 133.983 153.477 162.518 1.00 28.28 ? 432 ALA B O     1 
ATOM   9038  C  CB    . ALA B 1 432 ? 133.356 151.750 165.232 1.00 23.82 ? 432 ALA B CB    1 
ATOM   9039  N  N     . THR B 1 433 ? 132.704 154.613 163.981 1.00 27.20 ? 433 THR B N     1 
ATOM   9040  C  CA    . THR B 1 433 ? 132.130 155.463 162.945 1.00 19.83 ? 433 THR B CA    1 
ATOM   9041  C  C     . THR B 1 433 ? 133.198 156.337 162.303 1.00 24.59 ? 433 THR B C     1 
ATOM   9042  O  O     . THR B 1 433 ? 133.223 156.500 161.080 1.00 30.38 ? 433 THR B O     1 
ATOM   9043  C  CB    . THR B 1 433 ? 131.012 156.324 163.535 1.00 24.74 ? 433 THR B CB    1 
ATOM   9044  O  OG1   . THR B 1 433 ? 130.021 155.478 164.129 1.00 29.90 ? 433 THR B OG1   1 
ATOM   9045  C  CG2   . THR B 1 433 ? 130.360 157.173 162.457 1.00 23.55 ? 433 THR B CG2   1 
ATOM   9046  N  N     . ASP B 1 434 ? 134.094 156.903 163.115 1.00 23.83 ? 434 ASP B N     1 
ATOM   9047  C  CA    . ASP B 1 434 ? 135.178 157.715 162.568 1.00 20.93 ? 434 ASP B CA    1 
ATOM   9048  C  C     . ASP B 1 434 ? 136.094 156.890 161.672 1.00 20.95 ? 434 ASP B C     1 
ATOM   9049  O  O     . ASP B 1 434 ? 136.492 157.342 160.591 1.00 26.85 ? 434 ASP B O     1 
ATOM   9050  C  CB    . ASP B 1 434 ? 135.977 158.355 163.703 1.00 25.92 ? 434 ASP B CB    1 
ATOM   9051  C  CG    . ASP B 1 434 ? 135.204 159.435 164.423 1.00 30.34 ? 434 ASP B CG    1 
ATOM   9052  O  OD1   . ASP B 1 434 ? 134.319 160.051 163.794 1.00 34.46 ? 434 ASP B OD1   1 
ATOM   9053  O  OD2   . ASP B 1 434 ? 135.481 159.669 165.617 1.00 31.98 ? 434 ASP B OD2   1 
ATOM   9054  N  N     . SER B 1 435 ? 136.440 155.675 162.104 1.00 22.47 ? 435 SER B N     1 
ATOM   9055  C  CA    . SER B 1 435 ? 137.315 154.825 161.301 1.00 17.85 ? 435 SER B CA    1 
ATOM   9056  C  C     . SER B 1 435 ? 136.648 154.412 159.994 1.00 23.45 ? 435 SER B C     1 
ATOM   9057  O  O     . SER B 1 435 ? 137.289 154.406 158.936 1.00 29.96 ? 435 SER B O     1 
ATOM   9058  C  CB    . SER B 1 435 ? 137.732 153.595 162.105 1.00 21.95 ? 435 SER B CB    1 
ATOM   9059  O  OG    . SER B 1 435 ? 136.638 152.722 162.313 1.00 22.58 ? 435 SER B OG    1 
ATOM   9060  N  N     . LEU B 1 436 ? 135.362 154.059 160.048 1.00 19.52 ? 436 LEU B N     1 
ATOM   9061  C  CA    . LEU B 1 436 ? 134.640 153.696 158.834 1.00 15.16 ? 436 LEU B CA    1 
ATOM   9062  C  C     . LEU B 1 436 ? 134.509 154.887 157.896 1.00 20.31 ? 436 LEU B C     1 
ATOM   9063  O  O     . LEU B 1 436 ? 134.600 154.734 156.673 1.00 27.03 ? 436 LEU B O     1 
ATOM   9064  C  CB    . LEU B 1 436 ? 133.266 153.136 159.195 1.00 22.36 ? 436 LEU B CB    1 
ATOM   9065  C  CG    . LEU B 1 436 ? 133.265 151.765 159.868 1.00 19.68 ? 436 LEU B CG    1 
ATOM   9066  C  CD1   . LEU B 1 436 ? 131.949 151.523 160.582 1.00 17.09 ? 436 LEU B CD1   1 
ATOM   9067  C  CD2   . LEU B 1 436 ? 133.536 150.678 158.851 1.00 20.43 ? 436 LEU B CD2   1 
ATOM   9068  N  N     . THR B 1 437 ? 134.299 156.082 158.449 1.00 22.17 ? 437 THR B N     1 
ATOM   9069  C  CA    . THR B 1 437 ? 134.280 157.287 157.630 1.00 19.91 ? 437 THR B CA    1 
ATOM   9070  C  C     . THR B 1 437 ? 135.622 157.506 156.946 1.00 25.04 ? 437 THR B C     1 
ATOM   9071  O  O     . THR B 1 437 ? 135.672 157.843 155.760 1.00 32.96 ? 437 THR B O     1 
ATOM   9072  C  CB    . THR B 1 437 ? 133.915 158.497 158.489 1.00 16.76 ? 437 THR B CB    1 
ATOM   9073  O  OG1   . THR B 1 437 ? 132.663 158.259 159.141 1.00 18.22 ? 437 THR B OG1   1 
ATOM   9074  C  CG2   . THR B 1 437 ? 133.805 159.744 157.635 1.00 21.50 ? 437 THR B CG2   1 
ATOM   9075  N  N     . HIS B 1 438 ? 136.722 157.318 157.680 1.00 20.91 ? 438 HIS B N     1 
ATOM   9076  C  CA    . HIS B 1 438 ? 138.042 157.463 157.074 1.00 20.68 ? 438 HIS B CA    1 
ATOM   9077  C  C     . HIS B 1 438 ? 138.247 156.454 155.952 1.00 22.54 ? 438 HIS B C     1 
ATOM   9078  O  O     . HIS B 1 438 ? 138.779 156.795 154.889 1.00 31.48 ? 438 HIS B O     1 
ATOM   9079  C  CB    . HIS B 1 438 ? 139.132 157.309 158.135 1.00 25.62 ? 438 HIS B CB    1 
ATOM   9080  C  CG    . HIS B 1 438 ? 140.519 157.310 157.573 1.00 28.38 ? 438 HIS B CG    1 
ATOM   9081  N  ND1   . HIS B 1 438 ? 141.219 158.470 157.324 1.00 26.21 ? 438 HIS B ND1   1 
ATOM   9082  C  CD2   . HIS B 1 438 ? 141.330 156.293 157.199 1.00 30.44 ? 438 HIS B CD2   1 
ATOM   9083  C  CE1   . HIS B 1 438 ? 142.405 158.167 156.826 1.00 27.43 ? 438 HIS B CE1   1 
ATOM   9084  N  NE2   . HIS B 1 438 ? 142.497 156.853 156.740 1.00 30.44 ? 438 HIS B NE2   1 
ATOM   9085  N  N     . VAL B 1 439 ? 137.832 155.205 156.172 1.00 24.36 ? 439 VAL B N     1 
ATOM   9086  C  CA    . VAL B 1 439 ? 137.950 154.188 155.128 1.00 19.62 ? 439 VAL B CA    1 
ATOM   9087  C  C     . VAL B 1 439 ? 137.124 154.581 153.910 1.00 28.11 ? 439 VAL B C     1 
ATOM   9088  O  O     . VAL B 1 439 ? 137.546 154.383 152.764 1.00 33.06 ? 439 VAL B O     1 
ATOM   9089  C  CB    . VAL B 1 439 ? 137.536 152.809 155.675 1.00 23.14 ? 439 VAL B CB    1 
ATOM   9090  C  CG1   . VAL B 1 439 ? 137.484 151.782 154.555 1.00 25.40 ? 439 VAL B CG1   1 
ATOM   9091  C  CG2   . VAL B 1 439 ? 138.496 152.362 156.758 1.00 21.71 ? 439 VAL B CG2   1 
ATOM   9092  N  N     . SER B 1 440 ? 135.935 155.142 154.137 1.00 27.64 ? 440 SER B N     1 
ATOM   9093  C  CA    . SER B 1 440 ? 135.098 155.588 153.029 1.00 20.12 ? 440 SER B CA    1 
ATOM   9094  C  C     . SER B 1 440 ? 135.770 156.703 152.236 1.00 25.54 ? 440 SER B C     1 
ATOM   9095  O  O     . SER B 1 440 ? 135.775 156.678 151.000 1.00 33.35 ? 440 SER B O     1 
ATOM   9096  C  CB    . SER B 1 440 ? 133.740 156.049 153.558 1.00 25.91 ? 440 SER B CB    1 
ATOM   9097  O  OG    . SER B 1 440 ? 132.811 156.228 152.504 1.00 32.69 ? 440 SER B OG    1 
ATOM   9098  N  N     . GLU B 1 441 ? 136.342 157.691 152.930 1.00 26.18 ? 441 GLU B N     1 
ATOM   9099  C  CA    . GLU B 1 441 ? 136.978 158.806 152.231 1.00 22.77 ? 441 GLU B CA    1 
ATOM   9100  C  C     . GLU B 1 441 ? 138.226 158.361 151.478 1.00 30.91 ? 441 GLU B C     1 
ATOM   9101  O  O     . GLU B 1 441 ? 138.490 158.844 150.371 1.00 39.17 ? 441 GLU B O     1 
ATOM   9102  C  CB    . GLU B 1 441 ? 137.323 159.938 153.200 1.00 24.04 ? 441 GLU B CB    1 
ATOM   9103  C  CG    . GLU B 1 441 ? 136.237 160.294 154.193 1.00 30.79 ? 441 GLU B CG    1 
ATOM   9104  C  CD    . GLU B 1 441 ? 135.012 160.898 153.536 1.00 39.12 ? 441 GLU B CD    1 
ATOM   9105  O  OE1   . GLU B 1 441 ? 134.036 160.156 153.299 1.00 43.14 ? 441 GLU B OE1   1 
ATOM   9106  O  OE2   . GLU B 1 441 ? 135.024 162.115 153.260 1.00 37.00 ? 441 GLU B OE2   1 
ATOM   9107  N  N     . THR B 1 442 ? 139.005 157.450 152.052 1.00 32.22 ? 442 THR B N     1 
ATOM   9108  C  CA    . THR B 1 442 ? 140.257 157.045 151.424 1.00 30.02 ? 442 THR B CA    1 
ATOM   9109  C  C     . THR B 1 442 ? 140.068 155.996 150.337 1.00 29.24 ? 442 THR B C     1 
ATOM   9110  O  O     . THR B 1 442 ? 141.054 155.601 149.706 1.00 36.35 ? 442 THR B O     1 
ATOM   9111  C  CB    . THR B 1 442 ? 141.238 156.521 152.476 1.00 31.51 ? 442 THR B CB    1 
ATOM   9112  O  OG1   . THR B 1 442 ? 140.677 155.379 153.133 1.00 35.95 ? 442 THR B OG1   1 
ATOM   9113  C  CG2   . THR B 1 442 ? 141.538 157.599 153.501 1.00 28.75 ? 442 THR B CG2   1 
ATOM   9114  N  N     . THR B 1 443 ? 138.843 155.540 150.098 1.00 32.82 ? 443 THR B N     1 
ATOM   9115  C  CA    . THR B 1 443 ? 138.572 154.558 149.058 1.00 37.51 ? 443 THR B CA    1 
ATOM   9116  C  C     . THR B 1 443 ? 138.270 155.278 147.750 1.00 38.48 ? 443 THR B C     1 
ATOM   9117  O  O     . THR B 1 443 ? 137.360 156.110 147.688 1.00 38.38 ? 443 THR B O     1 
ATOM   9118  C  CB    . THR B 1 443 ? 137.403 153.656 149.452 1.00 35.05 ? 443 THR B CB    1 
ATOM   9119  O  OG1   . THR B 1 443 ? 137.714 152.976 150.674 1.00 39.88 ? 443 THR B OG1   1 
ATOM   9120  C  CG2   . THR B 1 443 ? 137.136 152.631 148.365 1.00 29.68 ? 443 THR B CG2   1 
ATOM   9121  N  N     . ASP B 1 444 ? 139.036 154.958 146.709 1.00 45.20 ? 444 ASP B N     1 
ATOM   9122  C  CA    . ASP B 1 444 ? 138.813 155.505 145.374 1.00 43.86 ? 444 ASP B CA    1 
ATOM   9123  C  C     . ASP B 1 444 ? 138.990 154.373 144.373 1.00 46.64 ? 444 ASP B C     1 
ATOM   9124  O  O     . ASP B 1 444 ? 140.089 153.824 144.243 1.00 47.46 ? 444 ASP B O     1 
ATOM   9125  C  CB    . ASP B 1 444 ? 139.771 156.658 145.075 1.00 45.86 ? 444 ASP B CB    1 
ATOM   9126  C  CG    . ASP B 1 444 ? 139.192 157.654 144.089 1.00 48.57 ? 444 ASP B CG    1 
ATOM   9127  O  OD1   . ASP B 1 444 ? 138.082 158.165 144.344 1.00 47.16 ? 444 ASP B OD1   1 
ATOM   9128  O  OD2   . ASP B 1 444 ? 139.847 157.927 143.062 1.00 49.71 ? 444 ASP B OD2   1 
ATOM   9129  N  N     . ILE B 1 445 ? 137.916 154.023 143.673 1.00 39.17 ? 445 ILE B N     1 
ATOM   9130  C  CA    . ILE B 1 445 ? 137.923 152.924 142.716 1.00 40.09 ? 445 ILE B CA    1 
ATOM   9131  C  C     . ILE B 1 445 ? 137.837 153.522 141.318 1.00 43.81 ? 445 ILE B C     1 
ATOM   9132  O  O     . ILE B 1 445 ? 136.886 154.247 140.999 1.00 45.25 ? 445 ILE B O     1 
ATOM   9133  C  CB    . ILE B 1 445 ? 136.774 151.942 142.985 1.00 38.44 ? 445 ILE B CB    1 
ATOM   9134  C  CG1   . ILE B 1 445 ? 137.198 150.927 144.046 1.00 37.70 ? 445 ILE B CG1   1 
ATOM   9135  C  CG2   . ILE B 1 445 ? 136.387 151.208 141.717 1.00 40.00 ? 445 ILE B CG2   1 
ATOM   9136  C  CD1   . ILE B 1 445 ? 136.088 150.518 144.973 1.00 37.28 ? 445 ILE B CD1   1 
ATOM   9137  N  N     . ARG B 1 446 ? 138.835 153.227 140.488 1.00 44.52 ? 446 ARG B N     1 
ATOM   9138  C  CA    . ARG B 1 446 ? 139.017 153.924 139.223 1.00 45.80 ? 446 ARG B CA    1 
ATOM   9139  C  C     . ARG B 1 446 ? 138.294 153.270 138.053 1.00 45.99 ? 446 ARG B C     1 
ATOM   9140  O  O     . ARG B 1 446 ? 138.282 153.845 136.960 1.00 42.53 ? 446 ARG B O     1 
ATOM   9141  C  CB    . ARG B 1 446 ? 140.511 154.033 138.897 1.00 43.26 ? 446 ARG B CB    1 
ATOM   9142  C  CG    . ARG B 1 446 ? 141.409 154.194 140.117 1.00 41.70 ? 446 ARG B CG    1 
ATOM   9143  C  CD    . ARG B 1 446 ? 141.186 155.479 140.930 1.00 45.33 ? 446 ARG B CD    1 
ATOM   9144  N  NE    . ARG B 1 446 ? 141.439 156.712 140.190 1.00 46.84 ? 446 ARG B NE    1 
ATOM   9145  C  CZ    . ARG B 1 446 ? 140.536 157.395 139.498 1.00 47.51 ? 446 ARG B CZ    1 
ATOM   9146  N  NH1   . ARG B 1 446 ? 139.264 157.035 139.472 1.00 44.19 ? 446 ARG B NH1   1 
ATOM   9147  N  NH2   . ARG B 1 446 ? 140.915 158.485 138.838 1.00 42.15 ? 446 ARG B NH2   1 
ATOM   9148  N  N     . ASN B 1 447 ? 137.692 152.098 138.245 1.00 35.50 ? 447 ASN B N     1 
ATOM   9149  C  CA    . ASN B 1 447 ? 137.043 151.393 137.151 1.00 29.62 ? 447 ASN B CA    1 
ATOM   9150  C  C     . ASN B 1 447 ? 135.566 151.123 137.393 1.00 32.08 ? 447 ASN B C     1 
ATOM   9151  O  O     . ASN B 1 447 ? 134.933 150.450 136.573 1.00 39.09 ? 447 ASN B O     1 
ATOM   9152  C  CB    . ASN B 1 447 ? 137.768 150.072 136.869 1.00 33.76 ? 447 ASN B CB    1 
ATOM   9153  C  CG    . ASN B 1 447 ? 138.870 150.226 135.844 1.00 32.04 ? 447 ASN B CG    1 
ATOM   9154  O  OD1   . ASN B 1 447 ? 138.606 150.398 134.655 1.00 36.82 ? 447 ASN B OD1   1 
ATOM   9155  N  ND2   . ASN B 1 447 ? 140.113 150.172 136.301 1.00 27.94 ? 447 ASN B ND2   1 
ATOM   9156  N  N     . ALA B 1 448 ? 135.000 151.624 138.490 1.00 33.07 ? 448 ALA B N     1 
ATOM   9157  C  CA    . ALA B 1 448 ? 133.568 151.539 138.770 1.00 29.06 ? 448 ALA B CA    1 
ATOM   9158  C  C     . ALA B 1 448 ? 133.076 152.956 139.023 1.00 32.54 ? 448 ALA B C     1 
ATOM   9159  O  O     . ALA B 1 448 ? 133.067 153.424 140.172 1.00 32.32 ? 448 ALA B O     1 
ATOM   9160  C  CB    . ALA B 1 448 ? 133.286 150.627 139.960 1.00 25.89 ? 448 ALA B CB    1 
ATOM   9161  N  N     . PRO B 1 449 ? 132.674 153.684 137.976 1.00 31.65 ? 449 PRO B N     1 
ATOM   9162  C  CA    . PRO B 1 449 ? 132.313 155.097 138.179 1.00 25.54 ? 449 PRO B CA    1 
ATOM   9163  C  C     . PRO B 1 449 ? 131.108 155.286 139.080 1.00 29.36 ? 449 PRO B C     1 
ATOM   9164  O  O     . PRO B 1 449 ? 131.075 156.238 139.868 1.00 28.52 ? 449 PRO B O     1 
ATOM   9165  C  CB    . PRO B 1 449 ? 132.047 155.608 136.754 1.00 26.83 ? 449 PRO B CB    1 
ATOM   9166  C  CG    . PRO B 1 449 ? 132.213 154.434 135.837 1.00 28.74 ? 449 PRO B CG    1 
ATOM   9167  C  CD    . PRO B 1 449 ? 132.298 153.192 136.643 1.00 24.89 ? 449 PRO B CD    1 
ATOM   9168  N  N     . ALA B 1 450 ? 130.116 154.399 138.991 1.00 30.97 ? 450 ALA B N     1 
ATOM   9169  C  CA    . ALA B 1 450 ? 128.940 154.520 139.844 1.00 20.98 ? 450 ALA B CA    1 
ATOM   9170  C  C     . ALA B 1 450 ? 129.274 154.199 141.294 1.00 26.03 ? 450 ALA B C     1 
ATOM   9171  O  O     . ALA B 1 450 ? 128.778 154.862 142.210 1.00 30.30 ? 450 ALA B O     1 
ATOM   9172  C  CB    . ALA B 1 450 ? 127.824 153.614 139.329 1.00 23.93 ? 450 ALA B CB    1 
ATOM   9173  N  N     . VAL B 1 451 ? 130.124 153.195 141.520 1.00 28.08 ? 451 VAL B N     1 
ATOM   9174  C  CA    . VAL B 1 451 ? 130.550 152.869 142.879 1.00 20.81 ? 451 VAL B CA    1 
ATOM   9175  C  C     . VAL B 1 451 ? 131.303 154.042 143.491 1.00 24.59 ? 451 VAL B C     1 
ATOM   9176  O  O     . VAL B 1 451 ? 131.067 154.423 144.642 1.00 33.67 ? 451 VAL B O     1 
ATOM   9177  C  CB    . VAL B 1 451 ? 131.405 151.589 142.882 1.00 27.31 ? 451 VAL B CB    1 
ATOM   9178  C  CG1   . VAL B 1 451 ? 132.211 151.485 144.165 1.00 28.63 ? 451 VAL B CG1   1 
ATOM   9179  C  CG2   . VAL B 1 451 ? 130.533 150.364 142.701 1.00 22.99 ? 451 VAL B CG2   1 
ATOM   9180  N  N     . ARG B 1 452 ? 132.221 154.636 142.724 1.00 27.05 ? 452 ARG B N     1 
ATOM   9181  C  CA    . ARG B 1 452 ? 132.984 155.775 143.222 1.00 24.41 ? 452 ARG B CA    1 
ATOM   9182  C  C     . ARG B 1 452 ? 132.083 156.975 143.490 1.00 23.07 ? 452 ARG B C     1 
ATOM   9183  O  O     . ARG B 1 452 ? 132.222 157.650 144.519 1.00 33.29 ? 452 ARG B O     1 
ATOM   9184  C  CB    . ARG B 1 452 ? 134.085 156.133 142.223 1.00 24.96 ? 452 ARG B CB    1 
ATOM   9185  C  CG    . ARG B 1 452 ? 134.938 157.321 142.619 1.00 30.79 ? 452 ARG B CG    1 
ATOM   9186  C  CD    . ARG B 1 452 ? 135.288 158.169 141.409 1.00 29.51 ? 452 ARG B CD    1 
ATOM   9187  N  NE    . ARG B 1 452 ? 134.276 158.071 140.364 1.00 38.16 ? 452 ARG B NE    1 
ATOM   9188  C  CZ    . ARG B 1 452 ? 133.259 158.909 140.220 1.00 38.86 ? 452 ARG B CZ    1 
ATOM   9189  N  NH1   . ARG B 1 452 ? 133.092 159.941 141.032 1.00 33.10 ? 452 ARG B NH1   1 
ATOM   9190  N  NH2   . ARG B 1 452 ? 132.386 158.707 139.237 1.00 28.27 ? 452 ARG B NH2   1 
ATOM   9191  N  N     . ARG B 1 453 ? 131.144 157.250 142.581 1.00 23.52 ? 453 ARG B N     1 
ATOM   9192  C  CA    . ARG B 1 453 ? 130.232 158.372 142.774 1.00 23.35 ? 453 ARG B CA    1 
ATOM   9193  C  C     . ARG B 1 453 ? 129.363 158.172 144.008 1.00 28.84 ? 453 ARG B C     1 
ATOM   9194  O  O     . ARG B 1 453 ? 129.159 159.108 144.789 1.00 30.51 ? 453 ARG B O     1 
ATOM   9195  C  CB    . ARG B 1 453 ? 129.365 158.564 141.529 1.00 25.11 ? 453 ARG B CB    1 
ATOM   9196  C  CG    . ARG B 1 453 ? 128.206 159.525 141.724 1.00 24.31 ? 453 ARG B CG    1 
ATOM   9197  C  CD    . ARG B 1 453 ? 127.617 159.963 140.397 1.00 23.84 ? 453 ARG B CD    1 
ATOM   9198  N  NE    . ARG B 1 453 ? 126.206 159.615 140.285 1.00 27.28 ? 453 ARG B NE    1 
ATOM   9199  C  CZ    . ARG B 1 453 ? 125.212 160.348 140.767 1.00 27.93 ? 453 ARG B CZ    1 
ATOM   9200  N  NH1   . ARG B 1 453 ? 125.437 161.482 141.409 1.00 29.49 ? 453 ARG B NH1   1 
ATOM   9201  N  NH2   . ARG B 1 453 ? 123.960 159.931 140.602 1.00 25.61 ? 453 ARG B NH2   1 
ATOM   9202  N  N     . ALA B 1 454 ? 128.850 156.955 144.207 1.00 30.56 ? 454 ALA B N     1 
ATOM   9203  C  CA    . ALA B 1 454 ? 128.017 156.692 145.373 1.00 21.41 ? 454 ALA B CA    1 
ATOM   9204  C  C     . ALA B 1 454 ? 128.828 156.708 146.660 1.00 21.40 ? 454 ALA B C     1 
ATOM   9205  O  O     . ALA B 1 454 ? 128.314 157.115 147.703 1.00 28.49 ? 454 ALA B O     1 
ATOM   9206  C  CB    . ALA B 1 454 ? 127.293 155.359 145.215 1.00 22.76 ? 454 ALA B CB    1 
ATOM   9207  N  N     . ASN B 1 455 ? 130.086 156.270 146.614 1.00 26.26 ? 455 ASN B N     1 
ATOM   9208  C  CA    . ASN B 1 455 ? 130.936 156.371 147.793 1.00 21.97 ? 455 ASN B CA    1 
ATOM   9209  C  C     . ASN B 1 455 ? 131.193 157.826 148.157 1.00 26.15 ? 455 ASN B C     1 
ATOM   9210  O  O     . ASN B 1 455 ? 131.192 158.187 149.339 1.00 35.82 ? 455 ASN B O     1 
ATOM   9211  C  CB    . ASN B 1 455 ? 132.253 155.632 147.555 1.00 21.39 ? 455 ASN B CB    1 
ATOM   9212  C  CG    . ASN B 1 455 ? 133.135 155.601 148.785 1.00 28.95 ? 455 ASN B CG    1 
ATOM   9213  O  OD1   . ASN B 1 455 ? 132.825 154.930 149.767 1.00 36.69 ? 455 ASN B OD1   1 
ATOM   9214  N  ND2   . ASN B 1 455 ? 134.242 156.331 148.738 1.00 29.14 ? 455 ASN B ND2   1 
ATOM   9215  N  N     . LYS B 1 456 ? 131.416 158.676 147.154 1.00 26.98 ? 456 LYS B N     1 
ATOM   9216  C  CA    . LYS B 1 456 ? 131.656 160.088 147.427 1.00 25.99 ? 456 LYS B CA    1 
ATOM   9217  C  C     . LYS B 1 456 ? 130.394 160.805 147.895 1.00 26.49 ? 456 LYS B C     1 
ATOM   9218  O  O     . LYS B 1 456 ? 130.473 161.705 148.737 1.00 29.00 ? 456 LYS B O     1 
ATOM   9219  C  CB    . LYS B 1 456 ? 132.222 160.772 146.183 1.00 24.19 ? 456 LYS B CB    1 
ATOM   9220  C  CG    . LYS B 1 456 ? 133.232 161.862 146.485 1.00 28.50 ? 456 LYS B CG    1 
ATOM   9221  C  CD    . LYS B 1 456 ? 132.580 163.235 146.470 1.00 33.48 ? 456 LYS B CD    1 
ATOM   9222  C  CE    . LYS B 1 456 ? 133.524 164.302 147.001 1.00 33.85 ? 456 LYS B CE    1 
ATOM   9223  N  NZ    . LYS B 1 456 ? 133.435 164.440 148.481 1.00 30.18 ? 456 LYS B NZ    1 
ATOM   9224  N  N     . ALA B 1 457 ? 129.231 160.427 147.368 1.00 25.60 ? 457 ALA B N     1 
ATOM   9225  C  CA    . ALA B 1 457 ? 127.991 161.139 147.651 1.00 19.23 ? 457 ALA B CA    1 
ATOM   9226  C  C     . ALA B 1 457 ? 127.294 160.633 148.909 1.00 23.62 ? 457 ALA B C     1 
ATOM   9227  O  O     . ALA B 1 457 ? 126.983 161.418 149.810 1.00 27.20 ? 457 ALA B O     1 
ATOM   9228  C  CB    . ALA B 1 457 ? 127.047 161.027 146.452 1.00 21.43 ? 457 ALA B CB    1 
ATOM   9229  N  N     . MET B 1 458 ? 127.040 159.327 148.981 1.00 31.75 ? 458 MET B N     1 
ATOM   9230  C  CA    . MET B 1 458 ? 126.271 158.755 150.078 1.00 18.53 ? 458 MET B CA    1 
ATOM   9231  C  C     . MET B 1 458 ? 127.079 158.689 151.367 1.00 25.66 ? 458 MET B C     1 
ATOM   9232  O  O     . MET B 1 458 ? 126.527 158.885 152.454 1.00 32.07 ? 458 MET B O     1 
ATOM   9233  C  CB    . MET B 1 458 ? 125.776 157.363 149.690 1.00 20.51 ? 458 MET B CB    1 
ATOM   9234  C  CG    . MET B 1 458 ? 125.058 157.305 148.350 1.00 22.87 ? 458 MET B CG    1 
ATOM   9235  S  SD    . MET B 1 458 ? 123.276 157.541 148.481 1.00 34.00 ? 458 MET B SD    1 
ATOM   9236  C  CE    . MET B 1 458 ? 123.158 159.324 148.380 1.00 26.94 ? 458 MET B CE    1 
ATOM   9237  N  N     . LYS B 1 459 ? 128.380 158.411 151.263 1.00 18.08 ? 459 LYS B N     1 
ATOM   9238  C  CA    . LYS B 1 459 ? 129.253 158.261 152.428 1.00 20.51 ? 459 LYS B CA    1 
ATOM   9239  C  C     . LYS B 1 459 ? 128.702 157.215 153.393 1.00 22.09 ? 459 LYS B C     1 
ATOM   9240  O  O     . LYS B 1 459 ? 128.769 157.366 154.614 1.00 29.66 ? 459 LYS B O     1 
ATOM   9241  C  CB    . LYS B 1 459 ? 129.463 159.600 153.139 1.00 24.70 ? 459 LYS B CB    1 
ATOM   9242  C  CG    . LYS B 1 459 ? 129.969 160.714 152.243 1.00 29.66 ? 459 LYS B CG    1 
ATOM   9243  C  CD    . LYS B 1 459 ? 129.278 162.025 152.568 1.00 24.38 ? 459 LYS B CD    1 
ATOM   9244  C  CE    . LYS B 1 459 ? 129.672 163.115 151.592 1.00 27.34 ? 459 LYS B CE    1 
ATOM   9245  N  NZ    . LYS B 1 459 ? 128.987 164.400 151.894 1.00 31.32 ? 459 LYS B NZ    1 
ATOM   9246  N  N     . SER B 1 460 ? 128.149 156.142 152.838 1.00 17.65 ? 460 SER B N     1 
ATOM   9247  C  CA    . SER B 1 460 ? 127.532 155.105 153.649 1.00 12.92 ? 460 SER B CA    1 
ATOM   9248  C  C     . SER B 1 460 ? 128.590 154.192 154.252 1.00 20.62 ? 460 SER B C     1 
ATOM   9249  O  O     . SER B 1 460 ? 129.580 153.845 153.603 1.00 31.64 ? 460 SER B O     1 
ATOM   9250  C  CB    . SER B 1 460 ? 126.552 154.284 152.813 1.00 17.72 ? 460 SER B CB    1 
ATOM   9251  O  OG    . SER B 1 460 ? 127.237 153.490 151.864 1.00 25.48 ? 460 SER B OG    1 
ATOM   9252  N  N     . ILE B 1 461 ? 128.370 153.802 155.506 1.00 18.90 ? 461 ILE B N     1 
ATOM   9253  C  CA    . ILE B 1 461 ? 129.248 152.885 156.215 1.00 16.16 ? 461 ILE B CA    1 
ATOM   9254  C  C     . ILE B 1 461 ? 128.395 151.771 156.802 1.00 19.70 ? 461 ILE B C     1 
ATOM   9255  O  O     . ILE B 1 461 ? 127.178 151.896 156.943 1.00 21.68 ? 461 ILE B O     1 
ATOM   9256  C  CB    . ILE B 1 461 ? 130.060 153.582 157.328 1.00 14.79 ? 461 ILE B CB    1 
ATOM   9257  C  CG1   . ILE B 1 461 ? 129.121 154.260 158.326 1.00 9.20  ? 461 ILE B CG1   1 
ATOM   9258  C  CG2   . ILE B 1 461 ? 131.023 154.593 156.729 1.00 17.99 ? 461 ILE B CG2   1 
ATOM   9259  C  CD1   . ILE B 1 461 ? 129.786 154.673 159.610 1.00 14.62 ? 461 ILE B CD1   1 
ATOM   9260  N  N     . GLY B 1 462 ? 129.046 150.659 157.119 1.00 20.30 ? 462 GLY B N     1 
ATOM   9261  C  CA    . GLY B 1 462 ? 128.363 149.599 157.829 1.00 11.53 ? 462 GLY B CA    1 
ATOM   9262  C  C     . GLY B 1 462 ? 129.058 149.234 159.121 1.00 12.72 ? 462 GLY B C     1 
ATOM   9263  O  O     . GLY B 1 462 ? 130.146 148.654 159.104 1.00 25.23 ? 462 GLY B O     1 
ATOM   9264  N  N     . LEU B 1 463 ? 128.433 149.552 160.249 1.00 13.49 ? 463 LEU B N     1 
ATOM   9265  C  CA    . LEU B 1 463 ? 128.961 149.206 161.562 1.00 11.57 ? 463 LEU B CA    1 
ATOM   9266  C  C     . LEU B 1 463 ? 128.138 148.048 162.110 1.00 19.92 ? 463 LEU B C     1 
ATOM   9267  O  O     . LEU B 1 463 ? 126.984 148.232 162.510 1.00 25.71 ? 463 LEU B O     1 
ATOM   9268  C  CB    . LEU B 1 463 ? 128.924 150.405 162.504 1.00 18.45 ? 463 LEU B CB    1 
ATOM   9269  C  CG    . LEU B 1 463 ? 129.345 150.115 163.945 1.00 17.09 ? 463 LEU B CG    1 
ATOM   9270  C  CD1   . LEU B 1 463 ? 130.751 149.543 163.978 1.00 5.88  ? 463 LEU B CD1   1 
ATOM   9271  C  CD2   . LEU B 1 463 ? 129.250 151.368 164.797 1.00 17.39 ? 463 LEU B CD2   1 
ATOM   9272  N  N     . GLY B 1 464 ? 128.733 146.857 162.127 1.00 21.34 ? 464 GLY B N     1 
ATOM   9273  C  CA    . GLY B 1 464 ? 128.073 145.670 162.616 1.00 13.60 ? 464 GLY B CA    1 
ATOM   9274  C  C     . GLY B 1 464 ? 128.413 145.371 164.064 1.00 10.64 ? 464 GLY B C     1 
ATOM   9275  O  O     . GLY B 1 464 ? 129.075 146.142 164.760 1.00 16.99 ? 464 GLY B O     1 
ATOM   9276  N  N     . ALA B 1 465 ? 127.939 144.215 164.515 1.00 15.37 ? 465 ALA B N     1 
ATOM   9277  C  CA    . ALA B 1 465 ? 128.215 143.727 165.854 1.00 10.99 ? 465 ALA B CA    1 
ATOM   9278  C  C     . ALA B 1 465 ? 128.440 142.226 165.786 1.00 16.38 ? 465 ALA B C     1 
ATOM   9279  O  O     . ALA B 1 465 ? 127.989 141.551 164.858 1.00 30.36 ? 465 ALA B O     1 
ATOM   9280  C  CB    . ALA B 1 465 ? 127.076 144.057 166.826 1.00 19.28 ? 465 ALA B CB    1 
ATOM   9281  N  N     . MET B 1 466 ? 129.154 141.711 166.780 1.00 22.96 ? 466 MET B N     1 
ATOM   9282  C  CA    . MET B 1 466 ? 129.436 140.288 166.867 1.00 20.83 ? 466 MET B CA    1 
ATOM   9283  C  C     . MET B 1 466 ? 129.528 139.908 168.338 1.00 19.05 ? 466 MET B C     1 
ATOM   9284  O  O     . MET B 1 466 ? 129.449 140.763 169.224 1.00 22.94 ? 466 MET B O     1 
ATOM   9285  C  CB    . MET B 1 466 ? 130.719 139.933 166.112 1.00 25.34 ? 466 MET B CB    1 
ATOM   9286  C  CG    . MET B 1 466 ? 131.980 140.355 166.831 1.00 26.92 ? 466 MET B CG    1 
ATOM   9287  S  SD    . MET B 1 466 ? 133.436 140.346 165.778 1.00 39.30 ? 466 MET B SD    1 
ATOM   9288  C  CE    . MET B 1 466 ? 134.409 141.601 166.594 1.00 25.18 ? 466 MET B CE    1 
ATOM   9289  N  N     . ASN B 1 467 ? 129.692 138.610 168.589 1.00 18.43 ? 467 ASN B N     1 
ATOM   9290  C  CA    . ASN B 1 467 ? 129.794 138.063 169.943 1.00 23.64 ? 467 ASN B CA    1 
ATOM   9291  C  C     . ASN B 1 467 ? 128.527 138.313 170.754 1.00 26.11 ? 467 ASN B C     1 
ATOM   9292  O  O     . ASN B 1 467 ? 128.586 138.493 171.972 1.00 25.94 ? 467 ASN B O     1 
ATOM   9293  C  CB    . ASN B 1 467 ? 131.015 138.616 170.683 1.00 22.14 ? 467 ASN B CB    1 
ATOM   9294  C  CG    . ASN B 1 467 ? 131.680 137.581 171.562 1.00 26.43 ? 467 ASN B CG    1 
ATOM   9295  O  OD1   . ASN B 1 467 ? 131.297 136.413 171.562 1.00 27.88 ? 467 ASN B OD1   1 
ATOM   9296  N  ND2   . ASN B 1 467 ? 132.688 138.003 172.312 1.00 28.81 ? 467 ASN B ND2   1 
ATOM   9297  N  N     . LEU B 1 468 ? 127.373 138.342 170.088 1.00 18.75 ? 468 LEU B N     1 
ATOM   9298  C  CA    . LEU B 1 468 ? 126.112 138.444 170.815 1.00 16.16 ? 468 LEU B CA    1 
ATOM   9299  C  C     . LEU B 1 468 ? 125.840 137.174 171.609 1.00 27.13 ? 468 LEU B C     1 
ATOM   9300  O  O     . LEU B 1 468 ? 125.558 137.227 172.812 1.00 30.32 ? 468 LEU B O     1 
ATOM   9301  C  CB    . LEU B 1 468 ? 124.966 138.725 169.844 1.00 23.96 ? 468 LEU B CB    1 
ATOM   9302  C  CG    . LEU B 1 468 ? 123.577 138.825 170.476 1.00 19.91 ? 468 LEU B CG    1 
ATOM   9303  C  CD1   . LEU B 1 468 ? 123.539 139.939 171.507 1.00 18.04 ? 468 LEU B CD1   1 
ATOM   9304  C  CD2   . LEU B 1 468 ? 122.512 139.032 169.416 1.00 17.10 ? 468 LEU B CD2   1 
ATOM   9305  N  N     . HIS B 1 469 ? 125.942 136.017 170.951 1.00 30.43 ? 469 HIS B N     1 
ATOM   9306  C  CA    . HIS B 1 469 ? 125.699 134.756 171.641 1.00 18.94 ? 469 HIS B CA    1 
ATOM   9307  C  C     . HIS B 1 469 ? 126.775 134.480 172.679 1.00 26.13 ? 469 HIS B C     1 
ATOM   9308  O  O     . HIS B 1 469 ? 126.481 133.948 173.752 1.00 36.08 ? 469 HIS B O     1 
ATOM   9309  C  CB    . HIS B 1 469 ? 125.615 133.607 170.639 1.00 19.07 ? 469 HIS B CB    1 
ATOM   9310  C  CG    . HIS B 1 469 ? 125.003 132.365 171.206 1.00 21.74 ? 469 HIS B CG    1 
ATOM   9311  N  ND1   . HIS B 1 469 ? 125.017 131.157 170.544 1.00 31.57 ? 469 HIS B ND1   1 
ATOM   9312  C  CD2   . HIS B 1 469 ? 124.359 132.144 172.376 1.00 27.07 ? 469 HIS B CD2   1 
ATOM   9313  C  CE1   . HIS B 1 469 ? 124.407 130.246 171.280 1.00 26.73 ? 469 HIS B CE1   1 
ATOM   9314  N  NE2   . HIS B 1 469 ? 123.999 130.819 172.397 1.00 25.76 ? 469 HIS B NE2   1 
ATOM   9315  N  N     . GLY B 1 470 ? 128.026 134.827 172.378 1.00 21.03 ? 470 GLY B N     1 
ATOM   9316  C  CA    . GLY B 1 470 ? 129.079 134.662 173.366 1.00 23.59 ? 470 GLY B CA    1 
ATOM   9317  C  C     . GLY B 1 470 ? 128.846 135.507 174.602 1.00 18.45 ? 470 GLY B C     1 
ATOM   9318  O  O     . GLY B 1 470 ? 128.986 135.028 175.730 1.00 33.48 ? 470 GLY B O     1 
ATOM   9319  N  N     . TYR B 1 471 ? 128.467 136.772 174.406 1.00 17.77 ? 471 TYR B N     1 
ATOM   9320  C  CA    . TYR B 1 471 ? 128.190 137.644 175.541 1.00 20.35 ? 471 TYR B CA    1 
ATOM   9321  C  C     . TYR B 1 471 ? 126.999 137.140 176.346 1.00 25.38 ? 471 TYR B C     1 
ATOM   9322  O  O     . TYR B 1 471 ? 127.013 137.183 177.581 1.00 29.06 ? 471 TYR B O     1 
ATOM   9323  C  CB    . TYR B 1 471 ? 127.938 139.073 175.064 1.00 24.46 ? 471 TYR B CB    1 
ATOM   9324  C  CG    . TYR B 1 471 ? 127.376 139.966 176.142 1.00 23.67 ? 471 TYR B CG    1 
ATOM   9325  C  CD1   . TYR B 1 471 ? 128.198 140.492 177.127 1.00 25.09 ? 471 TYR B CD1   1 
ATOM   9326  C  CD2   . TYR B 1 471 ? 126.022 140.262 176.193 1.00 17.83 ? 471 TYR B CD2   1 
ATOM   9327  C  CE1   . TYR B 1 471 ? 127.691 141.299 178.122 1.00 23.31 ? 471 TYR B CE1   1 
ATOM   9328  C  CE2   . TYR B 1 471 ? 125.506 141.061 177.188 1.00 21.06 ? 471 TYR B CE2   1 
ATOM   9329  C  CZ    . TYR B 1 471 ? 126.344 141.581 178.146 1.00 25.86 ? 471 TYR B CZ    1 
ATOM   9330  O  OH    . TYR B 1 471 ? 125.831 142.384 179.135 1.00 33.23 ? 471 TYR B OH    1 
ATOM   9331  N  N     . LEU B 1 472 ? 125.951 136.671 175.664 1.00 27.98 ? 472 LEU B N     1 
ATOM   9332  C  CA    . LEU B 1 472 ? 124.761 136.209 176.371 1.00 22.20 ? 472 LEU B CA    1 
ATOM   9333  C  C     . LEU B 1 472 ? 125.036 134.921 177.140 1.00 28.02 ? 472 LEU B C     1 
ATOM   9334  O  O     . LEU B 1 472 ? 124.641 134.785 178.303 1.00 34.34 ? 472 LEU B O     1 
ATOM   9335  C  CB    . LEU B 1 472 ? 123.607 136.015 175.387 1.00 23.93 ? 472 LEU B CB    1 
ATOM   9336  C  CG    . LEU B 1 472 ? 123.031 137.281 174.752 1.00 25.54 ? 472 LEU B CG    1 
ATOM   9337  C  CD1   . LEU B 1 472 ? 122.086 136.922 173.617 1.00 23.84 ? 472 LEU B CD1   1 
ATOM   9338  C  CD2   . LEU B 1 472 ? 122.329 138.142 175.789 1.00 24.44 ? 472 LEU B CD2   1 
ATOM   9339  N  N     . ALA B 1 473 ? 125.712 133.961 176.504 1.00 25.80 ? 473 ALA B N     1 
ATOM   9340  C  CA    . ALA B 1 473 ? 126.004 132.694 177.159 1.00 26.58 ? 473 ALA B CA    1 
ATOM   9341  C  C     . ALA B 1 473 ? 126.999 132.863 178.299 1.00 31.75 ? 473 ALA B C     1 
ATOM   9342  O  O     . ALA B 1 473 ? 126.913 132.147 179.303 1.00 37.73 ? 473 ALA B O     1 
ATOM   9343  C  CB    . ALA B 1 473 ? 126.527 131.688 176.137 1.00 27.21 ? 473 ALA B CB    1 
ATOM   9344  N  N     . GLN B 1 474 ? 127.943 133.794 178.169 1.00 30.77 ? 474 GLN B N     1 
ATOM   9345  C  CA    . GLN B 1 474 ? 128.868 134.067 179.259 1.00 28.76 ? 474 GLN B CA    1 
ATOM   9346  C  C     . GLN B 1 474 ? 128.236 134.888 180.374 1.00 29.26 ? 474 GLN B C     1 
ATOM   9347  O  O     . GLN B 1 474 ? 128.867 135.073 181.419 1.00 37.90 ? 474 GLN B O     1 
ATOM   9348  C  CB    . GLN B 1 474 ? 130.112 134.781 178.728 1.00 31.07 ? 474 GLN B CB    1 
ATOM   9349  C  CG    . GLN B 1 474 ? 131.047 133.872 177.953 1.00 29.14 ? 474 GLN B CG    1 
ATOM   9350  C  CD    . GLN B 1 474 ? 132.201 134.621 177.326 1.00 33.84 ? 474 GLN B CD    1 
ATOM   9351  O  OE1   . GLN B 1 474 ? 133.078 135.127 178.023 1.00 39.78 ? 474 GLN B OE1   1 
ATOM   9352  N  NE2   . GLN B 1 474 ? 132.210 134.692 176.000 1.00 34.56 ? 474 GLN B NE2   1 
ATOM   9353  N  N     . ASN B 1 475 ? 127.015 135.384 180.177 1.00 31.35 ? 475 ASN B N     1 
ATOM   9354  C  CA    . ASN B 1 475 ? 126.277 136.099 181.208 1.00 33.32 ? 475 ASN B CA    1 
ATOM   9355  C  C     . ASN B 1 475 ? 125.049 135.331 181.679 1.00 34.24 ? 475 ASN B C     1 
ATOM   9356  O  O     . ASN B 1 475 ? 124.184 135.910 182.344 1.00 36.10 ? 475 ASN B O     1 
ATOM   9357  C  CB    . ASN B 1 475 ? 125.869 137.484 180.703 1.00 32.88 ? 475 ASN B CB    1 
ATOM   9358  C  CG    . ASN B 1 475 ? 127.045 138.429 180.591 1.00 31.55 ? 475 ASN B CG    1 
ATOM   9359  O  OD1   . ASN B 1 475 ? 127.319 139.208 181.503 1.00 37.29 ? 475 ASN B OD1   1 
ATOM   9360  N  ND2   . ASN B 1 475 ? 127.755 138.358 179.473 1.00 27.86 ? 475 ASN B ND2   1 
ATOM   9361  N  N     . GLY B 1 476 ? 124.953 134.048 181.350 1.00 34.34 ? 476 GLY B N     1 
ATOM   9362  C  CA    . GLY B 1 476 ? 123.838 133.227 181.785 1.00 32.09 ? 476 GLY B CA    1 
ATOM   9363  C  C     . GLY B 1 476 ? 122.497 133.612 181.201 1.00 34.35 ? 476 GLY B C     1 
ATOM   9364  O  O     . GLY B 1 476 ? 121.488 133.600 181.917 1.00 40.49 ? 476 GLY B O     1 
ATOM   9365  N  N     . ILE B 1 477 ? 122.457 133.954 179.916 1.00 31.60 ? 477 ILE B N     1 
ATOM   9366  C  CA    . ILE B 1 477 ? 121.222 134.320 179.234 1.00 30.60 ? 477 ILE B CA    1 
ATOM   9367  C  C     . ILE B 1 477 ? 121.076 133.443 178.000 1.00 32.33 ? 477 ILE B C     1 
ATOM   9368  O  O     . ILE B 1 477 ? 121.984 133.385 177.164 1.00 35.76 ? 477 ILE B O     1 
ATOM   9369  C  CB    . ILE B 1 477 ? 121.199 135.811 178.847 1.00 27.23 ? 477 ILE B CB    1 
ATOM   9370  C  CG1   . ILE B 1 477 ? 121.198 136.688 180.100 1.00 30.33 ? 477 ILE B CG1   1 
ATOM   9371  C  CG2   . ILE B 1 477 ? 119.989 136.119 177.989 1.00 26.30 ? 477 ILE B CG2   1 
ATOM   9372  C  CD1   . ILE B 1 477 ? 121.857 138.031 179.904 1.00 32.57 ? 477 ILE B CD1   1 
ATOM   9373  N  N     . ALA B 1 478 ? 119.941 132.758 177.891 1.00 32.43 ? 478 ALA B N     1 
ATOM   9374  C  CA    . ALA B 1 478 ? 119.669 131.948 176.714 1.00 28.48 ? 478 ALA B CA    1 
ATOM   9375  C  C     . ALA B 1 478 ? 119.396 132.841 175.512 1.00 32.91 ? 478 ALA B C     1 
ATOM   9376  O  O     . ALA B 1 478 ? 118.780 133.902 175.637 1.00 36.81 ? 478 ALA B O     1 
ATOM   9377  C  CB    . ALA B 1 478 ? 118.480 131.023 176.967 1.00 29.42 ? 478 ALA B CB    1 
ATOM   9378  N  N     . TYR B 1 479 ? 119.858 132.402 174.340 1.00 29.21 ? 479 TYR B N     1 
ATOM   9379  C  CA    . TYR B 1 479 ? 119.714 133.210 173.133 1.00 23.03 ? 479 TYR B CA    1 
ATOM   9380  C  C     . TYR B 1 479 ? 118.247 133.419 172.774 1.00 32.26 ? 479 TYR B C     1 
ATOM   9381  O  O     . TYR B 1 479 ? 117.857 134.510 172.340 1.00 35.83 ? 479 TYR B O     1 
ATOM   9382  C  CB    . TYR B 1 479 ? 120.466 132.550 171.978 1.00 21.87 ? 479 TYR B CB    1 
ATOM   9383  C  CG    . TYR B 1 479 ? 120.602 133.405 170.740 1.00 27.41 ? 479 TYR B CG    1 
ATOM   9384  C  CD1   . TYR B 1 479 ? 119.643 133.367 169.737 1.00 30.03 ? 479 TYR B CD1   1 
ATOM   9385  C  CD2   . TYR B 1 479 ? 121.696 134.242 170.570 1.00 25.57 ? 479 TYR B CD2   1 
ATOM   9386  C  CE1   . TYR B 1 479 ? 119.766 134.145 168.603 1.00 24.71 ? 479 TYR B CE1   1 
ATOM   9387  C  CE2   . TYR B 1 479 ? 121.828 135.022 169.439 1.00 23.76 ? 479 TYR B CE2   1 
ATOM   9388  C  CZ    . TYR B 1 479 ? 120.860 134.969 168.460 1.00 29.05 ? 479 TYR B CZ    1 
ATOM   9389  O  OH    . TYR B 1 479 ? 120.988 135.745 167.333 1.00 33.82 ? 479 TYR B OH    1 
ATOM   9390  N  N     . GLU B 1 480 ? 117.419 132.388 172.945 1.00 34.44 ? 480 GLU B N     1 
ATOM   9391  C  CA    . GLU B 1 480 ? 115.998 132.494 172.638 1.00 31.28 ? 480 GLU B CA    1 
ATOM   9392  C  C     . GLU B 1 480 ? 115.193 133.142 173.754 1.00 33.19 ? 480 GLU B C     1 
ATOM   9393  O  O     . GLU B 1 480 ? 113.995 133.378 173.571 1.00 37.19 ? 480 GLU B O     1 
ATOM   9394  C  CB    . GLU B 1 480 ? 115.409 131.113 172.350 1.00 34.08 ? 480 GLU B CB    1 
ATOM   9395  C  CG    . GLU B 1 480 ? 116.122 130.325 171.277 1.00 34.89 ? 480 GLU B CG    1 
ATOM   9396  C  CD    . GLU B 1 480 ? 116.014 128.833 171.506 1.00 41.06 ? 480 GLU B CD    1 
ATOM   9397  O  OE1   . GLU B 1 480 ? 116.755 128.310 172.362 1.00 41.09 ? 480 GLU B OE1   1 
ATOM   9398  O  OE2   . GLU B 1 480 ? 115.186 128.183 170.835 1.00 38.50 ? 480 GLU B OE2   1 
ATOM   9399  N  N     . SER B 1 481 ? 115.809 133.422 174.897 1.00 31.34 ? 481 SER B N     1 
ATOM   9400  C  CA    . SER B 1 481 ? 115.071 133.961 176.024 1.00 32.36 ? 481 SER B CA    1 
ATOM   9401  C  C     . SER B 1 481 ? 114.602 135.385 175.730 1.00 35.57 ? 481 SER B C     1 
ATOM   9402  O  O     . SER B 1 481 ? 115.230 136.108 174.952 1.00 36.28 ? 481 SER B O     1 
ATOM   9403  C  CB    . SER B 1 481 ? 115.936 133.946 177.280 1.00 30.53 ? 481 SER B CB    1 
ATOM   9404  O  OG    . SER B 1 481 ? 116.789 135.075 177.325 1.00 34.30 ? 481 SER B OG    1 
ATOM   9405  N  N     . PRO B 1 482 ? 113.483 135.805 176.327 1.00 39.63 ? 482 PRO B N     1 
ATOM   9406  C  CA    . PRO B 1 482 ? 113.064 137.207 176.182 1.00 36.81 ? 482 PRO B CA    1 
ATOM   9407  C  C     . PRO B 1 482 ? 114.075 138.195 176.733 1.00 33.30 ? 482 PRO B C     1 
ATOM   9408  O  O     . PRO B 1 482 ? 114.127 139.339 176.267 1.00 35.33 ? 482 PRO B O     1 
ATOM   9409  C  CB    . PRO B 1 482 ? 111.741 137.258 176.959 1.00 35.41 ? 482 PRO B CB    1 
ATOM   9410  C  CG    . PRO B 1 482 ? 111.257 135.849 176.976 1.00 36.30 ? 482 PRO B CG    1 
ATOM   9411  C  CD    . PRO B 1 482 ? 112.488 135.003 177.056 1.00 36.39 ? 482 PRO B CD    1 
ATOM   9412  N  N     . GLU B 1 483 ? 114.878 137.787 177.718 1.00 35.97 ? 483 GLU B N     1 
ATOM   9413  C  CA    . GLU B 1 483 ? 115.909 138.673 178.249 1.00 34.41 ? 483 GLU B CA    1 
ATOM   9414  C  C     . GLU B 1 483 ? 116.998 138.935 177.216 1.00 31.72 ? 483 GLU B C     1 
ATOM   9415  O  O     . GLU B 1 483 ? 117.556 140.036 177.160 1.00 36.39 ? 483 GLU B O     1 
ATOM   9416  C  CB    . GLU B 1 483 ? 116.506 138.077 179.523 1.00 36.21 ? 483 GLU B CB    1 
ATOM   9417  C  CG    . GLU B 1 483 ? 115.522 137.971 180.674 1.00 38.23 ? 483 GLU B CG    1 
ATOM   9418  C  CD    . GLU B 1 483 ? 114.850 136.615 180.742 1.00 43.63 ? 483 GLU B CD    1 
ATOM   9419  O  OE1   . GLU B 1 483 ? 114.960 135.846 179.765 1.00 41.23 ? 483 GLU B OE1   1 
ATOM   9420  O  OE2   . GLU B 1 483 ? 114.207 136.317 181.770 1.00 42.96 ? 483 GLU B OE2   1 
ATOM   9421  N  N     . ALA B 1 484 ? 117.319 137.933 176.395 1.00 29.32 ? 484 ALA B N     1 
ATOM   9422  C  CA    . ALA B 1 484 ? 118.286 138.141 175.324 1.00 29.40 ? 484 ALA B CA    1 
ATOM   9423  C  C     . ALA B 1 484 ? 117.780 139.164 174.317 1.00 28.75 ? 484 ALA B C     1 
ATOM   9424  O  O     . ALA B 1 484 ? 118.533 140.040 173.877 1.00 30.83 ? 484 ALA B O     1 
ATOM   9425  C  CB    . ALA B 1 484 ? 118.593 136.818 174.630 1.00 23.36 ? 484 ALA B CB    1 
ATOM   9426  N  N     . ARG B 1 485 ? 116.502 139.071 173.942 1.00 27.25 ? 485 ARG B N     1 
ATOM   9427  C  CA    . ARG B 1 485 ? 115.928 140.063 173.043 1.00 26.17 ? 485 ARG B CA    1 
ATOM   9428  C  C     . ARG B 1 485 ? 115.856 141.433 173.698 1.00 25.32 ? 485 ARG B C     1 
ATOM   9429  O  O     . ARG B 1 485 ? 116.025 142.448 173.020 1.00 31.39 ? 485 ARG B O     1 
ATOM   9430  C  CB    . ARG B 1 485 ? 114.542 139.617 172.582 1.00 27.34 ? 485 ARG B CB    1 
ATOM   9431  C  CG    . ARG B 1 485 ? 114.570 138.524 171.535 1.00 24.93 ? 485 ARG B CG    1 
ATOM   9432  C  CD    . ARG B 1 485 ? 113.198 138.311 170.925 1.00 25.73 ? 485 ARG B CD    1 
ATOM   9433  N  NE    . ARG B 1 485 ? 112.226 137.849 171.907 1.00 28.80 ? 485 ARG B NE    1 
ATOM   9434  C  CZ    . ARG B 1 485 ? 112.129 136.597 172.333 1.00 31.92 ? 485 ARG B CZ    1 
ATOM   9435  N  NH1   . ARG B 1 485 ? 112.931 135.648 171.879 1.00 32.98 ? 485 ARG B NH1   1 
ATOM   9436  N  NH2   . ARG B 1 485 ? 111.200 136.289 173.233 1.00 29.45 ? 485 ARG B NH2   1 
ATOM   9437  N  N     . ASP B 1 486 ? 115.613 141.483 175.008 1.00 31.58 ? 486 ASP B N     1 
ATOM   9438  C  CA    . ASP B 1 486 ? 115.624 142.756 175.721 1.00 30.91 ? 486 ASP B CA    1 
ATOM   9439  C  C     . ASP B 1 486 ? 117.006 143.399 175.671 1.00 30.18 ? 486 ASP B C     1 
ATOM   9440  O  O     . ASP B 1 486 ? 117.142 144.604 175.408 1.00 32.81 ? 486 ASP B O     1 
ATOM   9441  C  CB    . ASP B 1 486 ? 115.173 142.533 177.164 1.00 33.43 ? 486 ASP B CB    1 
ATOM   9442  C  CG    . ASP B 1 486 ? 114.920 143.824 177.902 1.00 40.19 ? 486 ASP B CG    1 
ATOM   9443  O  OD1   . ASP B 1 486 ? 114.239 144.709 177.344 1.00 41.37 ? 486 ASP B OD1   1 
ATOM   9444  O  OD2   . ASP B 1 486 ? 115.396 143.947 179.048 1.00 35.13 ? 486 ASP B OD2   1 
ATOM   9445  N  N     . PHE B 1 487 ? 118.050 142.601 175.911 1.00 26.70 ? 487 PHE B N     1 
ATOM   9446  C  CA    . PHE B 1 487 ? 119.405 143.128 175.815 1.00 23.76 ? 487 PHE B CA    1 
ATOM   9447  C  C     . PHE B 1 487 ? 119.721 143.583 174.400 1.00 27.23 ? 487 PHE B C     1 
ATOM   9448  O  O     . PHE B 1 487 ? 120.352 144.624 174.209 1.00 29.87 ? 487 PHE B O     1 
ATOM   9449  C  CB    . PHE B 1 487 ? 120.442 142.099 176.255 1.00 25.19 ? 487 PHE B CB    1 
ATOM   9450  C  CG    . PHE B 1 487 ? 121.830 142.441 175.795 1.00 28.07 ? 487 PHE B CG    1 
ATOM   9451  C  CD1   . PHE B 1 487 ? 122.547 143.443 176.423 1.00 22.88 ? 487 PHE B CD1   1 
ATOM   9452  C  CD2   . PHE B 1 487 ? 122.397 141.804 174.705 1.00 27.41 ? 487 PHE B CD2   1 
ATOM   9453  C  CE1   . PHE B 1 487 ? 123.809 143.786 175.992 1.00 24.40 ? 487 PHE B CE1   1 
ATOM   9454  C  CE2   . PHE B 1 487 ? 123.660 142.147 174.271 1.00 25.51 ? 487 PHE B CE2   1 
ATOM   9455  C  CZ    . PHE B 1 487 ? 124.365 143.140 174.915 1.00 24.65 ? 487 PHE B CZ    1 
ATOM   9456  N  N     . ALA B 1 488 ? 119.334 142.793 173.397 1.00 25.46 ? 488 ALA B N     1 
ATOM   9457  C  CA    . ALA B 1 488 ? 119.598 143.186 172.018 1.00 21.69 ? 488 ALA B CA    1 
ATOM   9458  C  C     . ALA B 1 488 ? 118.897 144.494 171.686 1.00 28.38 ? 488 ALA B C     1 
ATOM   9459  O  O     . ALA B 1 488 ? 119.492 145.391 171.077 1.00 34.96 ? 488 ALA B O     1 
ATOM   9460  C  CB    . ALA B 1 488 ? 119.157 142.080 171.062 1.00 22.04 ? 488 ALA B CB    1 
ATOM   9461  N  N     . ASN B 1 489 ? 117.638 144.627 172.106 1.00 28.00 ? 489 ASN B N     1 
ATOM   9462  C  CA    . ASN B 1 489 ? 116.893 145.861 171.902 1.00 26.15 ? 489 ASN B CA    1 
ATOM   9463  C  C     . ASN B 1 489 ? 117.634 147.051 172.492 1.00 22.39 ? 489 ASN B C     1 
ATOM   9464  O  O     . ASN B 1 489 ? 117.908 148.034 171.793 1.00 29.49 ? 489 ASN B O     1 
ATOM   9465  C  CB    . ASN B 1 489 ? 115.506 145.721 172.531 1.00 22.00 ? 489 ASN B CB    1 
ATOM   9466  C  CG    . ASN B 1 489 ? 114.502 146.691 171.960 1.00 30.45 ? 489 ASN B CG    1 
ATOM   9467  O  OD1   . ASN B 1 489 ? 114.264 146.722 170.754 1.00 35.96 ? 489 ASN B OD1   1 
ATOM   9468  N  ND2   . ASN B 1 489 ? 113.890 147.483 172.830 1.00 30.08 ? 489 ASN B ND2   1 
ATOM   9469  N  N     . THR B 1 490 ? 118.006 146.963 173.771 1.00 22.68 ? 490 THR B N     1 
ATOM   9470  C  CA    . THR B 1 490 ? 118.653 148.099 174.423 1.00 23.33 ? 490 THR B CA    1 
ATOM   9471  C  C     . THR B 1 490 ? 120.020 148.391 173.812 1.00 24.51 ? 490 THR B C     1 
ATOM   9472  O  O     . THR B 1 490 ? 120.343 149.547 173.512 1.00 21.84 ? 490 THR B O     1 
ATOM   9473  C  CB    . THR B 1 490 ? 118.782 147.842 175.924 1.00 31.74 ? 490 THR B CB    1 
ATOM   9474  O  OG1   . THR B 1 490 ? 117.507 147.457 176.451 1.00 37.19 ? 490 THR B OG1   1 
ATOM   9475  C  CG2   . THR B 1 490 ? 119.263 149.095 176.636 1.00 27.10 ? 490 THR B CG2   1 
ATOM   9476  N  N     . PHE B 1 491 ? 120.828 147.350 173.605 1.00 25.38 ? 491 PHE B N     1 
ATOM   9477  C  CA    . PHE B 1 491 ? 122.187 147.530 173.108 1.00 19.82 ? 491 PHE B CA    1 
ATOM   9478  C  C     . PHE B 1 491 ? 122.187 148.147 171.720 1.00 24.30 ? 491 PHE B C     1 
ATOM   9479  O  O     . PHE B 1 491 ? 122.940 149.089 171.447 1.00 30.86 ? 491 PHE B O     1 
ATOM   9480  C  CB    . PHE B 1 491 ? 122.918 146.186 173.099 1.00 22.89 ? 491 PHE B CB    1 
ATOM   9481  C  CG    . PHE B 1 491 ? 124.317 146.254 172.551 1.00 23.81 ? 491 PHE B CG    1 
ATOM   9482  C  CD1   . PHE B 1 491 ? 125.386 146.520 173.386 1.00 22.29 ? 491 PHE B CD1   1 
ATOM   9483  C  CD2   . PHE B 1 491 ? 124.563 146.041 171.204 1.00 19.95 ? 491 PHE B CD2   1 
ATOM   9484  C  CE1   . PHE B 1 491 ? 126.672 146.583 172.890 1.00 16.52 ? 491 PHE B CE1   1 
ATOM   9485  C  CE2   . PHE B 1 491 ? 125.846 146.106 170.703 1.00 16.61 ? 491 PHE B CE2   1 
ATOM   9486  C  CZ    . PHE B 1 491 ? 126.901 146.377 171.547 1.00 19.31 ? 491 PHE B CZ    1 
ATOM   9487  N  N     . PHE B 1 492 ? 121.349 147.633 170.821 1.00 22.18 ? 492 PHE B N     1 
ATOM   9488  C  CA    . PHE B 1 492 ? 121.351 148.159 169.469 1.00 15.51 ? 492 PHE B CA    1 
ATOM   9489  C  C     . PHE B 1 492 ? 120.619 149.487 169.360 1.00 13.22 ? 492 PHE B C     1 
ATOM   9490  O  O     . PHE B 1 492 ? 120.950 150.279 168.474 1.00 23.48 ? 492 PHE B O     1 
ATOM   9491  C  CB    . PHE B 1 492 ? 120.777 147.119 168.510 1.00 15.66 ? 492 PHE B CB    1 
ATOM   9492  C  CG    . PHE B 1 492 ? 121.725 145.990 168.235 1.00 16.95 ? 492 PHE B CG    1 
ATOM   9493  C  CD1   . PHE B 1 492 ? 122.766 146.150 167.340 1.00 11.41 ? 492 PHE B CD1   1 
ATOM   9494  C  CD2   . PHE B 1 492 ? 121.602 144.784 168.902 1.00 18.37 ? 492 PHE B CD2   1 
ATOM   9495  C  CE1   . PHE B 1 492 ? 123.650 145.121 167.096 1.00 11.12 ? 492 PHE B CE1   1 
ATOM   9496  C  CE2   . PHE B 1 492 ? 122.484 143.752 168.663 1.00 13.86 ? 492 PHE B CE2   1 
ATOM   9497  C  CZ    . PHE B 1 492 ? 123.508 143.920 167.759 1.00 15.77 ? 492 PHE B CZ    1 
ATOM   9498  N  N     . MET B 1 493 ? 119.680 149.783 170.264 1.00 16.41 ? 493 MET B N     1 
ATOM   9499  C  CA    . MET B 1 493 ? 119.168 151.144 170.345 1.00 19.01 ? 493 MET B CA    1 
ATOM   9500  C  C     . MET B 1 493 ? 120.275 152.116 170.726 1.00 22.82 ? 493 MET B C     1 
ATOM   9501  O  O     . MET B 1 493 ? 120.384 153.200 170.145 1.00 27.61 ? 493 MET B O     1 
ATOM   9502  C  CB    . MET B 1 493 ? 118.027 151.227 171.355 1.00 20.31 ? 493 MET B CB    1 
ATOM   9503  C  CG    . MET B 1 493 ? 117.396 152.606 171.442 1.00 20.64 ? 493 MET B CG    1 
ATOM   9504  S  SD    . MET B 1 493 ? 117.983 153.571 172.849 1.00 35.70 ? 493 MET B SD    1 
ATOM   9505  C  CE    . MET B 1 493 ? 118.095 152.315 174.115 1.00 27.02 ? 493 MET B CE    1 
ATOM   9506  N  N     . MET B 1 494 ? 121.111 151.743 171.701 1.00 23.39 ? 494 MET B N     1 
ATOM   9507  C  CA    . MET B 1 494 ? 122.231 152.601 172.077 1.00 18.06 ? 494 MET B CA    1 
ATOM   9508  C  C     . MET B 1 494 ? 123.225 152.749 170.932 1.00 19.67 ? 494 MET B C     1 
ATOM   9509  O  O     . MET B 1 494 ? 123.747 153.845 170.690 1.00 29.06 ? 494 MET B O     1 
ATOM   9510  C  CB    . MET B 1 494 ? 122.930 152.047 173.318 1.00 23.25 ? 494 MET B CB    1 
ATOM   9511  C  CG    . MET B 1 494 ? 122.041 151.924 174.540 1.00 22.88 ? 494 MET B CG    1 
ATOM   9512  S  SD    . MET B 1 494 ? 122.971 151.544 176.034 1.00 39.62 ? 494 MET B SD    1 
ATOM   9513  C  CE    . MET B 1 494 ? 124.253 152.789 175.954 1.00 30.52 ? 494 MET B CE    1 
ATOM   9514  N  N     . VAL B 1 495 ? 123.505 151.653 170.227 1.00 19.47 ? 495 VAL B N     1 
ATOM   9515  C  CA    . VAL B 1 495 ? 124.426 151.705 169.096 1.00 14.83 ? 495 VAL B CA    1 
ATOM   9516  C  C     . VAL B 1 495 ? 123.891 152.634 168.016 1.00 19.14 ? 495 VAL B C     1 
ATOM   9517  O  O     . VAL B 1 495 ? 124.628 153.462 167.470 1.00 29.32 ? 495 VAL B O     1 
ATOM   9518  C  CB    . VAL B 1 495 ? 124.684 150.289 168.550 1.00 16.03 ? 495 VAL B CB    1 
ATOM   9519  C  CG1   . VAL B 1 495 ? 125.352 150.354 167.187 1.00 13.82 ? 495 VAL B CG1   1 
ATOM   9520  C  CG2   . VAL B 1 495 ? 125.533 149.496 169.524 1.00 15.53 ? 495 VAL B CG2   1 
ATOM   9521  N  N     . ASN B 1 496 ? 122.598 152.519 167.698 1.00 24.23 ? 496 ASN B N     1 
ATOM   9522  C  CA    . ASN B 1 496 ? 121.990 153.403 166.711 1.00 16.79 ? 496 ASN B CA    1 
ATOM   9523  C  C     . ASN B 1 496 ? 122.026 154.852 167.174 1.00 18.73 ? 496 ASN B C     1 
ATOM   9524  O  O     . ASN B 1 496 ? 122.322 155.756 166.385 1.00 26.38 ? 496 ASN B O     1 
ATOM   9525  C  CB    . ASN B 1 496 ? 120.553 152.963 166.435 1.00 15.32 ? 496 ASN B CB    1 
ATOM   9526  C  CG    . ASN B 1 496 ? 120.014 153.514 165.134 1.00 15.70 ? 496 ASN B CG    1 
ATOM   9527  O  OD1   . ASN B 1 496 ? 120.724 153.575 164.133 1.00 23.19 ? 496 ASN B OD1   1 
ATOM   9528  N  ND2   . ASN B 1 496 ? 118.752 153.915 165.140 1.00 17.58 ? 496 ASN B ND2   1 
ATOM   9529  N  N     . PHE B 1 497 ? 121.729 155.091 168.452 1.00 19.01 ? 497 PHE B N     1 
ATOM   9530  C  CA    . PHE B 1 497 ? 121.748 156.447 168.989 1.00 15.26 ? 497 PHE B CA    1 
ATOM   9531  C  C     . PHE B 1 497 ? 123.119 157.078 168.823 1.00 23.45 ? 497 PHE B C     1 
ATOM   9532  O  O     . PHE B 1 497 ? 123.246 158.199 168.317 1.00 28.10 ? 497 PHE B O     1 
ATOM   9533  C  CB    . PHE B 1 497 ? 121.345 156.422 170.465 1.00 17.85 ? 497 PHE B CB    1 
ATOM   9534  C  CG    . PHE B 1 497 ? 121.290 157.777 171.106 1.00 21.03 ? 497 PHE B CG    1 
ATOM   9535  C  CD1   . PHE B 1 497 ? 120.134 158.534 171.054 1.00 27.37 ? 497 PHE B CD1   1 
ATOM   9536  C  CD2   . PHE B 1 497 ? 122.390 158.291 171.772 1.00 23.16 ? 497 PHE B CD2   1 
ATOM   9537  C  CE1   . PHE B 1 497 ? 120.078 159.777 171.644 1.00 25.54 ? 497 PHE B CE1   1 
ATOM   9538  C  CE2   . PHE B 1 497 ? 122.338 159.535 172.363 1.00 24.93 ? 497 PHE B CE2   1 
ATOM   9539  C  CZ    . PHE B 1 497 ? 121.181 160.278 172.300 1.00 27.27 ? 497 PHE B CZ    1 
ATOM   9540  N  N     . TYR B 1 498 ? 124.166 156.360 169.224 1.00 27.37 ? 498 TYR B N     1 
ATOM   9541  C  CA    . TYR B 1 498 ? 125.497 156.946 169.186 1.00 20.30 ? 498 TYR B CA    1 
ATOM   9542  C  C     . TYR B 1 498 ? 126.058 157.004 167.772 1.00 23.50 ? 498 TYR B C     1 
ATOM   9543  O  O     . TYR B 1 498 ? 126.838 157.909 167.466 1.00 32.43 ? 498 TYR B O     1 
ATOM   9544  C  CB    . TYR B 1 498 ? 126.424 156.186 170.132 1.00 20.31 ? 498 TYR B CB    1 
ATOM   9545  C  CG    . TYR B 1 498 ? 126.089 156.474 171.574 1.00 25.59 ? 498 TYR B CG    1 
ATOM   9546  C  CD1   . TYR B 1 498 ? 126.096 157.776 172.055 1.00 28.19 ? 498 TYR B CD1   1 
ATOM   9547  C  CD2   . TYR B 1 498 ? 125.729 155.456 172.445 1.00 25.95 ? 498 TYR B CD2   1 
ATOM   9548  C  CE1   . TYR B 1 498 ? 125.775 158.055 173.366 1.00 28.21 ? 498 TYR B CE1   1 
ATOM   9549  C  CE2   . TYR B 1 498 ? 125.405 155.725 173.760 1.00 25.75 ? 498 TYR B CE2   1 
ATOM   9550  C  CZ    . TYR B 1 498 ? 125.430 157.027 174.214 1.00 31.40 ? 498 TYR B CZ    1 
ATOM   9551  O  OH    . TYR B 1 498 ? 125.111 157.305 175.523 1.00 33.70 ? 498 TYR B OH    1 
ATOM   9552  N  N     . SER B 1 499 ? 125.641 156.099 166.883 1.00 18.31 ? 499 SER B N     1 
ATOM   9553  C  CA    . SER B 1 499 ? 126.054 156.214 165.489 1.00 12.53 ? 499 SER B CA    1 
ATOM   9554  C  C     . SER B 1 499 ? 125.397 157.415 164.818 1.00 18.40 ? 499 SER B C     1 
ATOM   9555  O  O     . SER B 1 499 ? 126.052 158.145 164.067 1.00 24.79 ? 499 SER B O     1 
ATOM   9556  C  CB    . SER B 1 499 ? 125.735 154.925 164.733 1.00 11.37 ? 499 SER B CB    1 
ATOM   9557  O  OG    . SER B 1 499 ? 124.354 154.824 164.446 1.00 23.72 ? 499 SER B OG    1 
ATOM   9558  N  N     . ILE B 1 500 ? 124.110 157.650 165.094 1.00 17.67 ? 500 ILE B N     1 
ATOM   9559  C  CA    . ILE B 1 500 ? 123.444 158.842 164.574 1.00 20.76 ? 500 ILE B CA    1 
ATOM   9560  C  C     . ILE B 1 500 ? 124.088 160.098 165.141 1.00 21.06 ? 500 ILE B C     1 
ATOM   9561  O  O     . ILE B 1 500 ? 124.297 161.085 164.425 1.00 25.80 ? 500 ILE B O     1 
ATOM   9562  C  CB    . ILE B 1 500 ? 121.936 158.799 164.885 1.00 23.76 ? 500 ILE B CB    1 
ATOM   9563  C  CG1   . ILE B 1 500 ? 121.254 157.668 164.123 1.00 21.33 ? 500 ILE B CG1   1 
ATOM   9564  C  CG2   . ILE B 1 500 ? 121.280 160.119 164.526 1.00 19.81 ? 500 ILE B CG2   1 
ATOM   9565  C  CD1   . ILE B 1 500 ? 119.885 157.340 164.651 1.00 19.40 ? 500 ILE B CD1   1 
ATOM   9566  N  N     . GLN B 1 501 ? 124.400 160.087 166.439 1.00 27.50 ? 501 GLN B N     1 
ATOM   9567  C  CA    . GLN B 1 501 ? 125.027 161.248 167.058 1.00 25.48 ? 501 GLN B CA    1 
ATOM   9568  C  C     . GLN B 1 501 ? 126.395 161.530 166.452 1.00 27.10 ? 501 GLN B C     1 
ATOM   9569  O  O     . GLN B 1 501 ? 126.722 162.684 166.159 1.00 36.35 ? 501 GLN B O     1 
ATOM   9570  C  CB    . GLN B 1 501 ? 125.144 161.038 168.567 1.00 29.12 ? 501 GLN B CB    1 
ATOM   9571  C  CG    . GLN B 1 501 ? 125.039 162.318 169.369 1.00 29.06 ? 501 GLN B CG    1 
ATOM   9572  C  CD    . GLN B 1 501 ? 125.160 162.081 170.856 1.00 32.00 ? 501 GLN B CD    1 
ATOM   9573  O  OE1   . GLN B 1 501 ? 126.144 161.512 171.325 1.00 36.71 ? 501 GLN B OE1   1 
ATOM   9574  N  NE2   . GLN B 1 501 ? 124.157 162.514 171.608 1.00 32.58 ? 501 GLN B NE2   1 
ATOM   9575  N  N     . ARG B 1 502 ? 127.204 160.490 166.245 1.00 29.68 ? 502 ARG B N     1 
ATOM   9576  C  CA    . ARG B 1 502 ? 128.517 160.686 165.641 1.00 23.73 ? 502 ARG B CA    1 
ATOM   9577  C  C     . ARG B 1 502 ? 128.400 161.153 164.198 1.00 22.55 ? 502 ARG B C     1 
ATOM   9578  O  O     . ARG B 1 502 ? 129.191 161.986 163.747 1.00 29.38 ? 502 ARG B O     1 
ATOM   9579  C  CB    . ARG B 1 502 ? 129.335 159.399 165.722 1.00 22.67 ? 502 ARG B CB    1 
ATOM   9580  C  CG    . ARG B 1 502 ? 130.803 159.594 165.393 1.00 25.89 ? 502 ARG B CG    1 
ATOM   9581  C  CD    . ARG B 1 502 ? 131.404 160.711 166.224 1.00 27.44 ? 502 ARG B CD    1 
ATOM   9582  N  NE    . ARG B 1 502 ? 132.715 161.115 165.733 1.00 26.51 ? 502 ARG B NE    1 
ATOM   9583  C  CZ    . ARG B 1 502 ? 133.161 162.364 165.731 1.00 25.97 ? 502 ARG B CZ    1 
ATOM   9584  N  NH1   . ARG B 1 502 ? 132.424 163.362 166.188 1.00 30.53 ? 502 ARG B NH1   1 
ATOM   9585  N  NH2   . ARG B 1 502 ? 134.378 162.617 165.259 1.00 28.72 ? 502 ARG B NH2   1 
ATOM   9586  N  N     . SER B 1 503 ? 127.428 160.625 163.453 1.00 22.93 ? 503 SER B N     1 
ATOM   9587  C  CA    . SER B 1 503 ? 127.237 161.061 162.075 1.00 22.98 ? 503 SER B CA    1 
ATOM   9588  C  C     . SER B 1 503 ? 126.829 162.528 162.012 1.00 26.88 ? 503 SER B C     1 
ATOM   9589  O  O     . SER B 1 503 ? 127.334 163.287 161.177 1.00 32.98 ? 503 SER B O     1 
ATOM   9590  C  CB    . SER B 1 503 ? 126.197 160.174 161.398 1.00 17.84 ? 503 SER B CB    1 
ATOM   9591  O  OG    . SER B 1 503 ? 126.353 160.171 159.993 1.00 23.93 ? 503 SER B OG    1 
ATOM   9592  N  N     . ALA B 1 504 ? 125.926 162.950 162.900 1.00 24.84 ? 504 ALA B N     1 
ATOM   9593  C  CA    . ALA B 1 504 ? 125.538 164.355 162.943 1.00 22.86 ? 504 ALA B CA    1 
ATOM   9594  C  C     . ALA B 1 504 ? 126.696 165.237 163.395 1.00 30.90 ? 504 ALA B C     1 
ATOM   9595  O  O     . ALA B 1 504 ? 126.850 166.363 162.912 1.00 37.04 ? 504 ALA B O     1 
ATOM   9596  C  CB    . ALA B 1 504 ? 124.329 164.537 163.858 1.00 23.61 ? 504 ALA B CB    1 
ATOM   9597  N  N     . GLU B 1 505 ? 127.524 164.743 164.319 1.00 30.09 ? 505 GLU B N     1 
ATOM   9598  C  CA    . GLU B 1 505 ? 128.702 165.493 164.743 1.00 27.04 ? 505 GLU B CA    1 
ATOM   9599  C  C     . GLU B 1 505 ? 129.695 165.658 163.599 1.00 33.82 ? 505 GLU B C     1 
ATOM   9600  O  O     . GLU B 1 505 ? 130.284 166.731 163.433 1.00 38.64 ? 505 GLU B O     1 
ATOM   9601  C  CB    . GLU B 1 505 ? 129.366 164.798 165.930 1.00 27.66 ? 505 GLU B CB    1 
ATOM   9602  C  CG    . GLU B 1 505 ? 128.657 165.012 167.255 1.00 30.49 ? 505 GLU B CG    1 
ATOM   9603  C  CD    . GLU B 1 505 ? 129.016 163.959 168.284 1.00 36.09 ? 505 GLU B CD    1 
ATOM   9604  O  OE1   . GLU B 1 505 ? 129.890 163.115 167.995 1.00 37.38 ? 505 GLU B OE1   1 
ATOM   9605  O  OE2   . GLU B 1 505 ? 128.425 163.975 169.383 1.00 38.84 ? 505 GLU B OE2   1 
ATOM   9606  N  N     . ILE B 1 506 ? 129.899 164.605 162.806 1.00 30.85 ? 506 ILE B N     1 
ATOM   9607  C  CA    . ILE B 1 506 ? 130.779 164.701 161.646 1.00 27.06 ? 506 ILE B CA    1 
ATOM   9608  C  C     . ILE B 1 506 ? 130.205 165.672 160.623 1.00 27.70 ? 506 ILE B C     1 
ATOM   9609  O  O     . ILE B 1 506 ? 130.940 166.454 160.008 1.00 35.70 ? 506 ILE B O     1 
ATOM   9610  C  CB    . ILE B 1 506 ? 131.017 163.306 161.038 1.00 27.55 ? 506 ILE B CB    1 
ATOM   9611  C  CG1   . ILE B 1 506 ? 131.791 162.421 162.015 1.00 31.08 ? 506 ILE B CG1   1 
ATOM   9612  C  CG2   . ILE B 1 506 ? 131.767 163.410 159.722 1.00 25.45 ? 506 ILE B CG2   1 
ATOM   9613  C  CD1   . ILE B 1 506 ? 131.793 160.956 161.643 1.00 25.02 ? 506 ILE B CD1   1 
ATOM   9614  N  N     . ALA B 1 507 ? 128.886 165.640 160.422 1.00 29.92 ? 507 ALA B N     1 
ATOM   9615  C  CA    . ALA B 1 507 ? 128.255 166.585 159.507 1.00 29.80 ? 507 ALA B CA    1 
ATOM   9616  C  C     . ALA B 1 507 ? 128.439 168.021 159.983 1.00 31.32 ? 507 ALA B C     1 
ATOM   9617  O  O     . ALA B 1 507 ? 128.698 168.922 159.178 1.00 35.84 ? 507 ALA B O     1 
ATOM   9618  C  CB    . ALA B 1 507 ? 126.772 166.256 159.351 1.00 26.51 ? 507 ALA B CB    1 
ATOM   9619  N  N     . LYS B 1 508 ? 128.301 168.253 161.289 1.00 36.17 ? 508 LYS B N     1 
ATOM   9620  C  CA    . LYS B 1 508 ? 128.523 169.585 161.842 1.00 36.74 ? 508 LYS B CA    1 
ATOM   9621  C  C     . LYS B 1 508 ? 129.976 170.018 161.689 1.00 38.98 ? 508 LYS B C     1 
ATOM   9622  O  O     . LYS B 1 508 ? 130.254 171.179 161.366 1.00 42.25 ? 508 LYS B O     1 
ATOM   9623  C  CB    . LYS B 1 508 ? 128.106 169.612 163.312 1.00 40.21 ? 508 LYS B CB    1 
ATOM   9624  C  CG    . LYS B 1 508 ? 128.360 170.932 164.013 1.00 38.77 ? 508 LYS B CG    1 
ATOM   9625  C  CD    . LYS B 1 508 ? 128.151 170.804 165.511 1.00 38.44 ? 508 LYS B CD    1 
ATOM   9626  C  CE    . LYS B 1 508 ? 128.245 172.153 166.201 1.00 40.54 ? 508 LYS B CE    1 
ATOM   9627  N  NZ    . LYS B 1 508 ? 127.397 172.212 167.422 1.00 43.88 ? 508 LYS B NZ    1 
ATOM   9628  N  N     . GLU B 1 509 ? 130.916 169.101 161.924 1.00 41.57 ? 509 GLU B N     1 
ATOM   9629  C  CA    . GLU B 1 509 ? 132.332 169.439 161.825 1.00 40.44 ? 509 GLU B CA    1 
ATOM   9630  C  C     . GLU B 1 509 ? 132.727 169.768 160.391 1.00 42.71 ? 509 GLU B C     1 
ATOM   9631  O  O     . GLU B 1 509 ? 133.434 170.752 160.146 1.00 48.57 ? 509 GLU B O     1 
ATOM   9632  C  CB    . GLU B 1 509 ? 133.182 168.287 162.360 1.00 38.79 ? 509 GLU B CB    1 
ATOM   9633  C  CG    . GLU B 1 509 ? 133.457 168.357 163.853 1.00 45.93 ? 509 GLU B CG    1 
ATOM   9634  C  CD    . GLU B 1 509 ? 133.660 166.986 164.473 1.00 48.54 ? 509 GLU B CD    1 
ATOM   9635  O  OE1   . GLU B 1 509 ? 134.225 166.103 163.795 1.00 47.73 ? 509 GLU B OE1   1 
ATOM   9636  O  OE2   . GLU B 1 509 ? 133.252 166.791 165.638 1.00 44.46 ? 509 GLU B OE2   1 
ATOM   9637  N  N     . LYS B 1 510 ? 132.282 168.960 159.432 1.00 38.05 ? 510 LYS B N     1 
ATOM   9638  C  CA    . LYS B 1 510 ? 132.609 169.175 158.031 1.00 33.36 ? 510 LYS B CA    1 
ATOM   9639  C  C     . LYS B 1 510 ? 131.642 170.118 157.331 1.00 37.16 ? 510 LYS B C     1 
ATOM   9640  O  O     . LYS B 1 510 ? 131.907 170.516 156.191 1.00 44.08 ? 510 LYS B O     1 
ATOM   9641  C  CB    . LYS B 1 510 ? 132.640 167.836 157.286 1.00 31.19 ? 510 LYS B CB    1 
ATOM   9642  C  CG    . LYS B 1 510 ? 133.534 166.792 157.927 1.00 32.50 ? 510 LYS B CG    1 
ATOM   9643  C  CD    . LYS B 1 510 ? 133.703 165.584 157.026 1.00 35.81 ? 510 LYS B CD    1 
ATOM   9644  C  CE    . LYS B 1 510 ? 134.629 164.555 157.649 1.00 37.75 ? 510 LYS B CE    1 
ATOM   9645  N  NZ    . LYS B 1 510 ? 135.331 163.743 156.620 1.00 38.73 ? 510 LYS B NZ    1 
ATOM   9646  N  N     . GLY B 1 511 ? 130.538 170.486 157.977 1.00 36.25 ? 511 GLY B N     1 
ATOM   9647  C  CA    . GLY B 1 511 ? 129.563 171.360 157.359 1.00 37.78 ? 511 GLY B CA    1 
ATOM   9648  C  C     . GLY B 1 511 ? 128.820 170.760 156.190 1.00 39.01 ? 511 GLY B C     1 
ATOM   9649  O  O     . GLY B 1 511 ? 128.154 171.495 155.457 1.00 41.73 ? 511 GLY B O     1 
ATOM   9650  N  N     . GLU B 1 512 ? 128.910 169.447 155.992 1.00 33.86 ? 512 GLU B N     1 
ATOM   9651  C  CA    . GLU B 1 512 ? 128.287 168.790 154.855 1.00 31.35 ? 512 GLU B CA    1 
ATOM   9652  C  C     . GLU B 1 512 ? 127.587 167.520 155.309 1.00 31.79 ? 512 GLU B C     1 
ATOM   9653  O  O     . GLU B 1 512 ? 128.067 166.822 156.206 1.00 35.51 ? 512 GLU B O     1 
ATOM   9654  C  CB    . GLU B 1 512 ? 129.320 168.451 153.774 1.00 33.75 ? 512 GLU B CB    1 
ATOM   9655  C  CG    . GLU B 1 512 ? 130.542 167.724 154.300 1.00 33.32 ? 512 GLU B CG    1 
ATOM   9656  C  CD    . GLU B 1 512 ? 131.336 167.048 153.203 1.00 37.16 ? 512 GLU B CD    1 
ATOM   9657  O  OE1   . GLU B 1 512 ? 130.751 166.757 152.138 1.00 37.00 ? 512 GLU B OE1   1 
ATOM   9658  O  OE2   . GLU B 1 512 ? 132.544 166.804 153.405 1.00 38.21 ? 512 GLU B OE2   1 
ATOM   9659  N  N     . THR B 1 513 ? 126.453 167.231 154.684 1.00 33.35 ? 513 THR B N     1 
ATOM   9660  C  CA    . THR B 1 513 ? 125.715 165.993 154.869 1.00 31.50 ? 513 THR B CA    1 
ATOM   9661  C  C     . THR B 1 513 ? 125.916 165.111 153.643 1.00 28.99 ? 513 THR B C     1 
ATOM   9662  O  O     . THR B 1 513 ? 126.669 165.448 152.726 1.00 36.43 ? 513 THR B O     1 
ATOM   9663  C  CB    . THR B 1 513 ? 124.232 166.282 155.109 1.00 31.51 ? 513 THR B CB    1 
ATOM   9664  O  OG1   . THR B 1 513 ? 123.644 166.793 153.907 1.00 33.07 ? 513 THR B OG1   1 
ATOM   9665  C  CG2   . THR B 1 513 ? 124.073 167.308 156.210 1.00 30.29 ? 513 THR B CG2   1 
ATOM   9666  N  N     . PHE B 1 514 ? 125.239 163.968 153.622 1.00 23.00 ? 514 PHE B N     1 
ATOM   9667  C  CA    . PHE B 1 514 ? 125.310 163.156 152.421 1.00 25.55 ? 514 PHE B CA    1 
ATOM   9668  C  C     . PHE B 1 514 ? 124.377 163.721 151.356 1.00 26.09 ? 514 PHE B C     1 
ATOM   9669  O  O     . PHE B 1 514 ? 123.466 164.501 151.642 1.00 30.94 ? 514 PHE B O     1 
ATOM   9670  C  CB    . PHE B 1 514 ? 124.983 161.689 152.713 1.00 21.30 ? 514 PHE B CB    1 
ATOM   9671  C  CG    . PHE B 1 514 ? 123.580 161.444 153.194 1.00 22.23 ? 514 PHE B CG    1 
ATOM   9672  C  CD1   . PHE B 1 514 ? 123.260 161.562 154.533 1.00 20.89 ? 514 PHE B CD1   1 
ATOM   9673  C  CD2   . PHE B 1 514 ? 122.588 161.056 152.309 1.00 22.12 ? 514 PHE B CD2   1 
ATOM   9674  C  CE1   . PHE B 1 514 ? 121.977 161.318 154.977 1.00 15.90 ? 514 PHE B CE1   1 
ATOM   9675  C  CE2   . PHE B 1 514 ? 121.303 160.813 152.748 1.00 18.72 ? 514 PHE B CE2   1 
ATOM   9676  C  CZ    . PHE B 1 514 ? 120.999 160.944 154.084 1.00 18.69 ? 514 PHE B CZ    1 
ATOM   9677  N  N     . ASP B 1 515 ? 124.633 163.337 150.109 1.00 27.73 ? 515 ASP B N     1 
ATOM   9678  C  CA    . ASP B 1 515 ? 123.864 163.877 148.999 1.00 30.03 ? 515 ASP B CA    1 
ATOM   9679  C  C     . ASP B 1 515 ? 122.401 163.473 149.114 1.00 32.30 ? 515 ASP B C     1 
ATOM   9680  O  O     . ASP B 1 515 ? 122.079 162.326 149.433 1.00 41.06 ? 515 ASP B O     1 
ATOM   9681  C  CB    . ASP B 1 515 ? 124.446 163.403 147.669 1.00 31.39 ? 515 ASP B CB    1 
ATOM   9682  C  CG    . ASP B 1 515 ? 125.716 164.142 147.295 1.00 33.46 ? 515 ASP B CG    1 
ATOM   9683  O  OD1   . ASP B 1 515 ? 126.331 164.758 148.189 1.00 33.87 ? 515 ASP B OD1   1 
ATOM   9684  O  OD2   . ASP B 1 515 ? 126.098 164.110 146.107 1.00 35.03 ? 515 ASP B OD2   1 
ATOM   9685  N  N     . GLN B 1 516 ? 121.516 164.436 148.853 1.00 31.55 ? 516 GLN B N     1 
ATOM   9686  C  CA    . GLN B 1 516 ? 120.070 164.244 148.962 1.00 30.03 ? 516 GLN B CA    1 
ATOM   9687  C  C     . GLN B 1 516 ? 119.665 163.846 150.380 1.00 32.09 ? 516 GLN B C     1 
ATOM   9688  O  O     . GLN B 1 516 ? 118.749 163.047 150.582 1.00 38.48 ? 516 GLN B O     1 
ATOM   9689  C  CB    . GLN B 1 516 ? 119.569 163.217 147.944 1.00 27.42 ? 516 GLN B CB    1 
ATOM   9690  C  CG    . GLN B 1 516 ? 119.937 163.538 146.508 1.00 30.23 ? 516 GLN B CG    1 
ATOM   9691  C  CD    . GLN B 1 516 ? 119.787 162.343 145.592 1.00 36.61 ? 516 GLN B CD    1 
ATOM   9692  O  OE1   . GLN B 1 516 ? 118.686 162.022 145.148 1.00 35.66 ? 516 GLN B OE1   1 
ATOM   9693  N  NE2   . GLN B 1 516 ? 120.898 161.674 145.308 1.00 36.44 ? 516 GLN B NE2   1 
ATOM   9694  N  N     . TYR B 1 517 ? 120.359 164.403 151.374 1.00 28.40 ? 517 TYR B N     1 
ATOM   9695  C  CA    . TYR B 1 517 ? 119.965 164.177 152.760 1.00 25.83 ? 517 TYR B CA    1 
ATOM   9696  C  C     . TYR B 1 517 ? 118.644 164.866 153.076 1.00 32.91 ? 517 TYR B C     1 
ATOM   9697  O  O     . TYR B 1 517 ? 117.844 164.355 153.867 1.00 40.07 ? 517 TYR B O     1 
ATOM   9698  C  CB    . TYR B 1 517 ? 121.057 164.665 153.714 1.00 23.28 ? 517 TYR B CB    1 
ATOM   9699  C  CG    . TYR B 1 517 ? 120.534 165.076 155.073 1.00 29.78 ? 517 TYR B CG    1 
ATOM   9700  C  CD1   . TYR B 1 517 ? 120.322 164.134 156.069 1.00 24.13 ? 517 TYR B CD1   1 
ATOM   9701  C  CD2   . TYR B 1 517 ? 120.250 166.407 155.359 1.00 31.50 ? 517 TYR B CD2   1 
ATOM   9702  C  CE1   . TYR B 1 517 ? 119.840 164.502 157.308 1.00 29.75 ? 517 TYR B CE1   1 
ATOM   9703  C  CE2   . TYR B 1 517 ? 119.766 166.783 156.593 1.00 29.06 ? 517 TYR B CE2   1 
ATOM   9704  C  CZ    . TYR B 1 517 ? 119.562 165.827 157.564 1.00 32.13 ? 517 TYR B CZ    1 
ATOM   9705  O  OH    . TYR B 1 517 ? 119.083 166.200 158.797 1.00 36.74 ? 517 TYR B OH    1 
ATOM   9706  N  N     . GLU B 1 518 ? 118.403 166.030 152.468 1.00 31.58 ? 518 GLU B N     1 
ATOM   9707  C  CA    . GLU B 1 518 ? 117.245 166.848 152.812 1.00 34.46 ? 518 GLU B CA    1 
ATOM   9708  C  C     . GLU B 1 518 ? 115.925 166.133 152.562 1.00 36.21 ? 518 GLU B C     1 
ATOM   9709  O  O     . GLU B 1 518 ? 114.929 166.451 153.220 1.00 39.99 ? 518 GLU B O     1 
ATOM   9710  C  CB    . GLU B 1 518 ? 117.282 168.162 152.028 1.00 33.43 ? 518 GLU B CB    1 
ATOM   9711  C  CG    . GLU B 1 518 ? 118.651 168.831 151.981 1.00 36.10 ? 518 GLU B CG    1 
ATOM   9712  C  CD    . GLU B 1 518 ? 119.538 168.287 150.875 1.00 43.03 ? 518 GLU B CD    1 
ATOM   9713  O  OE1   . GLU B 1 518 ? 119.071 168.212 149.718 1.00 41.17 ? 518 GLU B OE1   1 
ATOM   9714  O  OE2   . GLU B 1 518 ? 120.699 167.929 151.163 1.00 38.87 ? 518 GLU B OE2   1 
ATOM   9715  N  N     . GLY B 1 519 ? 115.890 165.184 151.631 1.00 27.98 ? 519 GLY B N     1 
ATOM   9716  C  CA    . GLY B 1 519 ? 114.696 164.395 151.413 1.00 23.67 ? 519 GLY B CA    1 
ATOM   9717  C  C     . GLY B 1 519 ? 114.550 163.184 152.300 1.00 25.52 ? 519 GLY B C     1 
ATOM   9718  O  O     . GLY B 1 519 ? 113.507 162.527 152.267 1.00 31.29 ? 519 GLY B O     1 
ATOM   9719  N  N     . SER B 1 520 ? 115.566 162.873 153.100 1.00 25.63 ? 520 SER B N     1 
ATOM   9720  C  CA    . SER B 1 520 ? 115.552 161.668 153.912 1.00 23.49 ? 520 SER B CA    1 
ATOM   9721  C  C     . SER B 1 520 ? 114.624 161.823 155.112 1.00 26.02 ? 520 SER B C     1 
ATOM   9722  O  O     . SER B 1 520 ? 114.207 162.926 155.477 1.00 27.00 ? 520 SER B O     1 
ATOM   9723  C  CB    . SER B 1 520 ? 116.965 161.325 154.385 1.00 22.23 ? 520 SER B CB    1 
ATOM   9724  O  OG    . SER B 1 520 ? 117.528 162.391 155.127 1.00 26.26 ? 520 SER B OG    1 
ATOM   9725  N  N     . THR B 1 521 ? 114.293 160.685 155.726 1.00 24.42 ? 521 THR B N     1 
ATOM   9726  C  CA    . THR B 1 521 ? 113.476 160.696 156.932 1.00 24.19 ? 521 THR B CA    1 
ATOM   9727  C  C     . THR B 1 521 ? 114.223 161.277 158.123 1.00 27.67 ? 521 THR B C     1 
ATOM   9728  O  O     . THR B 1 521 ? 113.586 161.704 159.090 1.00 31.26 ? 521 THR B O     1 
ATOM   9729  C  CB    . THR B 1 521 ? 112.992 159.284 157.256 1.00 28.17 ? 521 THR B CB    1 
ATOM   9730  O  OG1   . THR B 1 521 ? 114.108 158.471 157.635 1.00 29.14 ? 521 THR B OG1   1 
ATOM   9731  C  CG2   . THR B 1 521 ? 112.320 158.668 156.046 1.00 21.08 ? 521 THR B CG2   1 
ATOM   9732  N  N     . TYR B 1 522 ? 115.557 161.291 158.078 1.00 27.12 ? 522 TYR B N     1 
ATOM   9733  C  CA    . TYR B 1 522 ? 116.324 161.994 159.099 1.00 20.67 ? 522 TYR B CA    1 
ATOM   9734  C  C     . TYR B 1 522 ? 116.035 163.487 159.069 1.00 26.50 ? 522 TYR B C     1 
ATOM   9735  O  O     . TYR B 1 522 ? 115.884 164.121 160.120 1.00 30.46 ? 522 TYR B O     1 
ATOM   9736  C  CB    . TYR B 1 522 ? 117.817 161.745 158.899 1.00 21.86 ? 522 TYR B CB    1 
ATOM   9737  C  CG    . TYR B 1 522 ? 118.229 160.296 158.958 1.00 22.62 ? 522 TYR B CG    1 
ATOM   9738  C  CD1   . TYR B 1 522 ? 118.121 159.573 160.136 1.00 20.85 ? 522 TYR B CD1   1 
ATOM   9739  C  CD2   . TYR B 1 522 ? 118.741 159.655 157.840 1.00 23.84 ? 522 TYR B CD2   1 
ATOM   9740  C  CE1   . TYR B 1 522 ? 118.509 158.253 160.198 1.00 24.10 ? 522 TYR B CE1   1 
ATOM   9741  C  CE2   . TYR B 1 522 ? 119.126 158.334 157.892 1.00 20.87 ? 522 TYR B CE2   1 
ATOM   9742  C  CZ    . TYR B 1 522 ? 119.006 157.637 159.073 1.00 25.43 ? 522 TYR B CZ    1 
ATOM   9743  O  OH    . TYR B 1 522 ? 119.389 156.320 159.131 1.00 28.91 ? 522 TYR B OH    1 
ATOM   9744  N  N     . ALA B 1 523 ? 115.966 164.068 157.869 1.00 31.69 ? 523 ALA B N     1 
ATOM   9745  C  CA    . ALA B 1 523 ? 115.717 165.499 157.744 1.00 26.91 ? 523 ALA B CA    1 
ATOM   9746  C  C     . ALA B 1 523 ? 114.309 165.860 158.198 1.00 30.56 ? 523 ALA B C     1 
ATOM   9747  O  O     . ALA B 1 523 ? 114.109 166.883 158.863 1.00 32.97 ? 523 ALA B O     1 
ATOM   9748  C  CB    . ALA B 1 523 ? 115.948 165.943 156.302 1.00 26.39 ? 523 ALA B CB    1 
ATOM   9749  N  N     . THR B 1 524 ? 113.322 165.036 157.850 1.00 30.97 ? 524 THR B N     1 
ATOM   9750  C  CA    . THR B 1 524 ? 111.939 165.310 158.212 1.00 27.87 ? 524 THR B CA    1 
ATOM   9751  C  C     . THR B 1 524 ? 111.595 164.873 159.628 1.00 33.44 ? 524 THR B C     1 
ATOM   9752  O  O     . THR B 1 524 ? 110.514 165.219 160.118 1.00 39.19 ? 524 THR B O     1 
ATOM   9753  C  CB    . THR B 1 524 ? 110.990 164.626 157.226 1.00 32.52 ? 524 THR B CB    1 
ATOM   9754  O  OG1   . THR B 1 524 ? 110.882 163.235 157.549 1.00 33.43 ? 524 THR B OG1   1 
ATOM   9755  C  CG2   . THR B 1 524 ? 111.508 164.768 155.805 1.00 31.32 ? 524 THR B CG2   1 
ATOM   9756  N  N     . GLY B 1 525 ? 112.475 164.129 160.294 1.00 28.91 ? 525 GLY B N     1 
ATOM   9757  C  CA    . GLY B 1 525 ? 112.215 163.659 161.636 1.00 27.73 ? 525 GLY B CA    1 
ATOM   9758  C  C     . GLY B 1 525 ? 111.352 162.421 161.726 1.00 33.06 ? 525 GLY B C     1 
ATOM   9759  O  O     . GLY B 1 525 ? 111.119 161.930 162.837 1.00 33.26 ? 525 GLY B O     1 
ATOM   9760  N  N     . GLU B 1 526 ? 110.870 161.900 160.596 1.00 35.34 ? 526 GLU B N     1 
ATOM   9761  C  CA    . GLU B 1 526 ? 110.056 160.691 160.611 1.00 33.68 ? 526 GLU B CA    1 
ATOM   9762  C  C     . GLU B 1 526 ? 110.850 159.480 161.083 1.00 33.48 ? 526 GLU B C     1 
ATOM   9763  O  O     . GLU B 1 526 ? 110.262 158.531 161.613 1.00 39.41 ? 526 GLU B O     1 
ATOM   9764  C  CB    . GLU B 1 526 ? 109.471 160.456 159.214 1.00 34.69 ? 526 GLU B CB    1 
ATOM   9765  C  CG    . GLU B 1 526 ? 108.808 159.106 159.001 1.00 35.43 ? 526 GLU B CG    1 
ATOM   9766  C  CD    . GLU B 1 526 ? 108.810 158.682 157.547 1.00 40.82 ? 526 GLU B CD    1 
ATOM   9767  O  OE1   . GLU B 1 526 ? 108.808 159.570 156.668 1.00 39.78 ? 526 GLU B OE1   1 
ATOM   9768  O  OE2   . GLU B 1 526 ? 108.816 157.462 157.281 1.00 40.12 ? 526 GLU B OE2   1 
ATOM   9769  N  N     . TYR B 1 527 ? 112.175 159.507 160.927 1.00 33.29 ? 527 TYR B N     1 
ATOM   9770  C  CA    . TYR B 1 527 ? 113.005 158.403 161.395 1.00 26.73 ? 527 TYR B CA    1 
ATOM   9771  C  C     . TYR B 1 527 ? 112.921 158.247 162.909 1.00 28.09 ? 527 TYR B C     1 
ATOM   9772  O  O     . TYR B 1 527 ? 112.888 157.124 163.425 1.00 32.77 ? 527 TYR B O     1 
ATOM   9773  C  CB    . TYR B 1 527 ? 114.453 158.622 160.959 1.00 24.62 ? 527 TYR B CB    1 
ATOM   9774  C  CG    . TYR B 1 527 ? 115.392 157.513 161.367 1.00 27.69 ? 527 TYR B CG    1 
ATOM   9775  C  CD1   . TYR B 1 527 ? 115.601 156.419 160.541 1.00 23.87 ? 527 TYR B CD1   1 
ATOM   9776  C  CD2   . TYR B 1 527 ? 116.071 157.559 162.578 1.00 28.67 ? 527 TYR B CD2   1 
ATOM   9777  C  CE1   . TYR B 1 527 ? 116.456 155.404 160.908 1.00 24.43 ? 527 TYR B CE1   1 
ATOM   9778  C  CE2   . TYR B 1 527 ? 116.926 156.547 162.953 1.00 24.02 ? 527 TYR B CE2   1 
ATOM   9779  C  CZ    . TYR B 1 527 ? 117.116 155.473 162.115 1.00 23.66 ? 527 TYR B CZ    1 
ATOM   9780  O  OH    . TYR B 1 527 ? 117.970 154.462 162.484 1.00 30.33 ? 527 TYR B OH    1 
ATOM   9781  N  N     . PHE B 1 528 ? 112.886 159.361 163.635 1.00 32.32 ? 528 PHE B N     1 
ATOM   9782  C  CA    . PHE B 1 528 ? 112.985 159.361 165.087 1.00 28.48 ? 528 PHE B CA    1 
ATOM   9783  C  C     . PHE B 1 528 ? 111.645 159.163 165.783 1.00 35.02 ? 528 PHE B C     1 
ATOM   9784  O  O     . PHE B 1 528 ? 111.586 159.268 167.011 1.00 43.25 ? 528 PHE B O     1 
ATOM   9785  C  CB    . PHE B 1 528 ? 113.619 160.668 165.567 1.00 30.99 ? 528 PHE B CB    1 
ATOM   9786  C  CG    . PHE B 1 528 ? 114.991 160.918 165.014 1.00 32.95 ? 528 PHE B CG    1 
ATOM   9787  C  CD1   . PHE B 1 528 ? 116.112 160.435 165.665 1.00 27.52 ? 528 PHE B CD1   1 
ATOM   9788  C  CD2   . PHE B 1 528 ? 115.161 161.642 163.846 1.00 33.84 ? 528 PHE B CD2   1 
ATOM   9789  C  CE1   . PHE B 1 528 ? 117.375 160.665 165.161 1.00 29.80 ? 528 PHE B CE1   1 
ATOM   9790  C  CE2   . PHE B 1 528 ? 116.423 161.873 163.337 1.00 33.75 ? 528 PHE B CE2   1 
ATOM   9791  C  CZ    . PHE B 1 528 ? 117.530 161.384 163.996 1.00 31.29 ? 528 PHE B CZ    1 
ATOM   9792  N  N     . ASP B 1 529 ? 110.575 158.884 165.037 1.00 37.66 ? 529 ASP B N     1 
ATOM   9793  C  CA    . ASP B 1 529 ? 109.245 158.814 165.638 1.00 35.56 ? 529 ASP B CA    1 
ATOM   9794  C  C     . ASP B 1 529 ? 109.167 157.720 166.697 1.00 37.55 ? 529 ASP B C     1 
ATOM   9795  O  O     . ASP B 1 529 ? 108.748 157.967 167.835 1.00 40.83 ? 529 ASP B O     1 
ATOM   9796  C  CB    . ASP B 1 529 ? 108.196 158.584 164.550 1.00 32.90 ? 529 ASP B CB    1 
ATOM   9797  C  CG    . ASP B 1 529 ? 108.071 159.760 163.605 1.00 41.19 ? 529 ASP B CG    1 
ATOM   9798  O  OD1   . ASP B 1 529 ? 108.581 160.850 163.940 1.00 40.54 ? 529 ASP B OD1   1 
ATOM   9799  O  OD2   . ASP B 1 529 ? 107.464 159.593 162.527 1.00 46.08 ? 529 ASP B OD2   1 
ATOM   9800  N  N     . LYS B 1 530 ? 109.577 156.501 166.342 1.00 38.18 ? 530 LYS B N     1 
ATOM   9801  C  CA    . LYS B 1 530 ? 109.529 155.396 167.291 1.00 35.64 ? 530 LYS B CA    1 
ATOM   9802  C  C     . LYS B 1 530 ? 110.514 155.575 168.436 1.00 37.89 ? 530 LYS B C     1 
ATOM   9803  O  O     . LYS B 1 530 ? 110.338 154.957 169.490 1.00 41.35 ? 530 LYS B O     1 
ATOM   9804  C  CB    . LYS B 1 530 ? 109.798 154.074 166.575 1.00 36.92 ? 530 LYS B CB    1 
ATOM   9805  C  CG    . LYS B 1 530 ? 111.247 153.629 166.611 1.00 33.36 ? 530 LYS B CG    1 
ATOM   9806  C  CD    . LYS B 1 530 ? 111.443 152.360 165.811 1.00 36.71 ? 530 LYS B CD    1 
ATOM   9807  C  CE    . LYS B 1 530 ? 112.851 151.832 165.960 1.00 34.20 ? 530 LYS B CE    1 
ATOM   9808  N  NZ    . LYS B 1 530 ? 113.396 151.429 164.641 1.00 41.51 ? 530 LYS B NZ    1 
ATOM   9809  N  N     . TYR B 1 531 ? 111.541 156.400 168.257 1.00 37.55 ? 531 TYR B N     1 
ATOM   9810  C  CA    . TYR B 1 531 ? 112.511 156.636 169.315 1.00 32.32 ? 531 TYR B CA    1 
ATOM   9811  C  C     . TYR B 1 531 ? 112.083 157.747 170.259 1.00 31.74 ? 531 TYR B C     1 
ATOM   9812  O  O     . TYR B 1 531 ? 112.396 157.688 171.454 1.00 39.64 ? 531 TYR B O     1 
ATOM   9813  C  CB    . TYR B 1 531 ? 113.875 156.965 168.710 1.00 27.97 ? 531 TYR B CB    1 
ATOM   9814  C  CG    . TYR B 1 531 ? 114.588 155.763 168.140 1.00 31.77 ? 531 TYR B CG    1 
ATOM   9815  C  CD1   . TYR B 1 531 ? 114.914 154.682 168.946 1.00 26.59 ? 531 TYR B CD1   1 
ATOM   9816  C  CD2   . TYR B 1 531 ? 114.935 155.708 166.798 1.00 29.27 ? 531 TYR B CD2   1 
ATOM   9817  C  CE1   . TYR B 1 531 ? 115.568 153.582 168.432 1.00 31.54 ? 531 TYR B CE1   1 
ATOM   9818  C  CE2   . TYR B 1 531 ? 115.589 154.613 166.276 1.00 26.00 ? 531 TYR B CE2   1 
ATOM   9819  C  CZ    . TYR B 1 531 ? 115.903 153.553 167.097 1.00 30.83 ? 531 TYR B CZ    1 
ATOM   9820  O  OH    . TYR B 1 531 ? 116.554 152.458 166.584 1.00 30.82 ? 531 TYR B OH    1 
ATOM   9821  N  N     . VAL B 1 532 ? 111.377 158.761 169.751 1.00 37.66 ? 532 VAL B N     1 
ATOM   9822  C  CA    . VAL B 1 532 ? 110.826 159.801 170.615 1.00 35.29 ? 532 VAL B CA    1 
ATOM   9823  C  C     . VAL B 1 532 ? 109.473 159.420 171.191 1.00 39.56 ? 532 VAL B C     1 
ATOM   9824  O  O     . VAL B 1 532 ? 108.949 160.147 172.043 1.00 45.27 ? 532 VAL B O     1 
ATOM   9825  C  CB    . VAL B 1 532 ? 110.684 161.140 169.866 1.00 39.05 ? 532 VAL B CB    1 
ATOM   9826  C  CG1   . VAL B 1 532 ? 112.015 161.556 169.261 1.00 36.63 ? 532 VAL B CG1   1 
ATOM   9827  C  CG2   . VAL B 1 532 ? 109.607 161.041 168.798 1.00 37.52 ? 532 VAL B CG2   1 
ATOM   9828  N  N     . SER B 1 533 ? 108.888 158.308 170.747 1.00 40.72 ? 533 SER B N     1 
ATOM   9829  C  CA    . SER B 1 533 ? 107.613 157.846 171.278 1.00 40.69 ? 533 SER B CA    1 
ATOM   9830  C  C     . SER B 1 533 ? 107.724 156.622 172.172 1.00 41.57 ? 533 SER B C     1 
ATOM   9831  O  O     . SER B 1 533 ? 106.934 156.487 173.107 1.00 44.67 ? 533 SER B O     1 
ATOM   9832  C  CB    . SER B 1 533 ? 106.643 157.531 170.133 1.00 43.77 ? 533 SER B CB    1 
ATOM   9833  O  OG    . SER B 1 533 ? 106.884 156.240 169.603 1.00 44.50 ? 533 SER B OG    1 
ATOM   9834  N  N     . THR B 1 534 ? 108.679 155.733 171.914 1.00 44.31 ? 534 THR B N     1 
ATOM   9835  C  CA    . THR B 1 534 ? 108.824 154.491 172.658 1.00 41.10 ? 534 THR B CA    1 
ATOM   9836  C  C     . THR B 1 534 ? 110.126 154.507 173.446 1.00 40.47 ? 534 THR B C     1 
ATOM   9837  O  O     . THR B 1 534 ? 111.145 155.018 172.970 1.00 46.48 ? 534 THR B O     1 
ATOM   9838  C  CB    . THR B 1 534 ? 108.799 153.277 171.719 1.00 42.42 ? 534 THR B CB    1 
ATOM   9839  O  OG1   . THR B 1 534 ? 107.684 153.384 170.826 1.00 41.39 ? 534 THR B OG1   1 
ATOM   9840  C  CG2   . THR B 1 534 ? 108.683 151.982 172.508 1.00 42.66 ? 534 THR B CG2   1 
ATOM   9841  N  N     . ASP B 1 535 ? 110.085 153.949 174.652 1.00 42.06 ? 535 ASP B N     1 
ATOM   9842  C  CA    . ASP B 1 535 ? 111.262 153.812 175.498 1.00 41.72 ? 535 ASP B CA    1 
ATOM   9843  C  C     . ASP B 1 535 ? 111.884 152.442 175.270 1.00 43.42 ? 535 ASP B C     1 
ATOM   9844  O  O     . ASP B 1 535 ? 111.186 151.424 175.313 1.00 45.06 ? 535 ASP B O     1 
ATOM   9845  C  CB    . ASP B 1 535 ? 110.898 153.992 176.972 1.00 41.16 ? 535 ASP B CB    1 
ATOM   9846  C  CG    . ASP B 1 535 ? 112.117 154.079 177.866 1.00 46.23 ? 535 ASP B CG    1 
ATOM   9847  O  OD1   . ASP B 1 535 ? 112.896 155.044 177.720 1.00 47.22 ? 535 ASP B OD1   1 
ATOM   9848  O  OD2   . ASP B 1 535 ? 112.295 153.182 178.715 1.00 47.11 ? 535 ASP B OD2   1 
ATOM   9849  N  N     . PHE B 1 536 ? 113.195 152.420 175.028 1.00 38.38 ? 536 PHE B N     1 
ATOM   9850  C  CA    . PHE B 1 536 ? 113.910 151.188 174.723 1.00 34.05 ? 536 PHE B CA    1 
ATOM   9851  C  C     . PHE B 1 536 ? 114.850 150.767 175.847 1.00 35.01 ? 536 PHE B C     1 
ATOM   9852  O  O     . PHE B 1 536 ? 115.818 150.040 175.602 1.00 39.56 ? 536 PHE B O     1 
ATOM   9853  C  CB    . PHE B 1 536 ? 114.677 151.336 173.409 1.00 33.94 ? 536 PHE B CB    1 
ATOM   9854  C  CG    . PHE B 1 536 ? 113.793 151.429 172.200 1.00 31.29 ? 536 PHE B CG    1 
ATOM   9855  C  CD1   . PHE B 1 536 ? 113.385 150.288 171.534 1.00 32.18 ? 536 PHE B CD1   1 
ATOM   9856  C  CD2   . PHE B 1 536 ? 113.365 152.658 171.732 1.00 32.11 ? 536 PHE B CD2   1 
ATOM   9857  C  CE1   . PHE B 1 536 ? 112.569 150.369 170.423 1.00 30.14 ? 536 PHE B CE1   1 
ATOM   9858  C  CE2   . PHE B 1 536 ? 112.549 152.745 170.621 1.00 37.79 ? 536 PHE B CE2   1 
ATOM   9859  C  CZ    . PHE B 1 536 ? 112.151 151.599 169.967 1.00 30.95 ? 536 PHE B CZ    1 
ATOM   9860  N  N     . SER B 1 537 ? 114.589 151.216 177.072 1.00 35.86 ? 537 SER B N     1 
ATOM   9861  C  CA    . SER B 1 537 ? 115.334 150.740 178.222 1.00 34.21 ? 537 SER B CA    1 
ATOM   9862  C  C     . SER B 1 537 ? 114.978 149.282 178.503 1.00 37.89 ? 537 SER B C     1 
ATOM   9863  O  O     . SER B 1 537 ? 113.900 148.816 178.127 1.00 40.38 ? 537 SER B O     1 
ATOM   9864  C  CB    . SER B 1 537 ? 115.035 151.608 179.442 1.00 35.04 ? 537 SER B CB    1 
ATOM   9865  O  OG    . SER B 1 537 ? 113.666 151.533 179.797 1.00 37.87 ? 537 SER B OG    1 
ATOM   9866  N  N     . PRO B 1 538 ? 115.876 148.534 179.145 1.00 36.64 ? 538 PRO B N     1 
ATOM   9867  C  CA    . PRO B 1 538 ? 115.589 147.121 179.415 1.00 35.24 ? 538 PRO B CA    1 
ATOM   9868  C  C     . PRO B 1 538 ? 114.368 146.954 180.307 1.00 39.29 ? 538 PRO B C     1 
ATOM   9869  O  O     . PRO B 1 538 ? 114.137 147.736 181.231 1.00 37.91 ? 538 PRO B O     1 
ATOM   9870  C  CB    . PRO B 1 538 ? 116.864 146.624 180.108 1.00 35.08 ? 538 PRO B CB    1 
ATOM   9871  C  CG    . PRO B 1 538 ? 117.914 147.614 179.750 1.00 33.98 ? 538 PRO B CG    1 
ATOM   9872  C  CD    . PRO B 1 538 ? 117.207 148.924 179.636 1.00 35.41 ? 538 PRO B CD    1 
ATOM   9873  N  N     . LYS B 1 539 ? 113.582 145.920 180.016 1.00 44.95 ? 539 LYS B N     1 
ATOM   9874  C  CA    . LYS B 1 539 ? 112.396 145.592 180.794 1.00 44.66 ? 539 LYS B CA    1 
ATOM   9875  C  C     . LYS B 1 539 ? 112.667 144.549 181.868 1.00 46.96 ? 539 LYS B C     1 
ATOM   9876  O  O     . LYS B 1 539 ? 111.745 144.184 182.604 1.00 47.74 ? 539 LYS B O     1 
ATOM   9877  C  CB    . LYS B 1 539 ? 111.277 145.101 179.871 1.00 45.20 ? 539 LYS B CB    1 
ATOM   9878  C  CG    . LYS B 1 539 ? 111.307 145.702 178.477 1.00 43.60 ? 539 LYS B CG    1 
ATOM   9879  C  CD    . LYS B 1 539 ? 110.801 147.135 178.478 1.00 46.65 ? 539 LYS B CD    1 
ATOM   9880  C  CE    . LYS B 1 539 ? 110.037 147.451 177.202 1.00 47.98 ? 539 LYS B CE    1 
ATOM   9881  N  NZ    . LYS B 1 539 ? 110.927 147.472 176.008 1.00 47.62 ? 539 LYS B NZ    1 
ATOM   9882  N  N     . TYR B 1 540 ? 113.899 144.063 181.974 1.00 45.21 ? 540 TYR B N     1 
ATOM   9883  C  CA    . TYR B 1 540 ? 114.269 143.042 182.941 1.00 43.27 ? 540 TYR B CA    1 
ATOM   9884  C  C     . TYR B 1 540 ? 115.367 143.575 183.848 1.00 45.30 ? 540 TYR B C     1 
ATOM   9885  O  O     . TYR B 1 540 ? 116.282 144.267 183.390 1.00 46.25 ? 540 TYR B O     1 
ATOM   9886  C  CB    . TYR B 1 540 ? 114.737 141.762 182.242 1.00 44.01 ? 540 TYR B CB    1 
ATOM   9887  C  CG    . TYR B 1 540 ? 113.644 141.059 181.470 1.00 46.56 ? 540 TYR B CG    1 
ATOM   9888  C  CD1   . TYR B 1 540 ? 113.368 141.400 180.153 1.00 43.88 ? 540 TYR B CD1   1 
ATOM   9889  C  CD2   . TYR B 1 540 ? 112.885 140.058 182.060 1.00 46.63 ? 540 TYR B CD2   1 
ATOM   9890  C  CE1   . TYR B 1 540 ? 112.369 140.762 179.445 1.00 43.65 ? 540 TYR B CE1   1 
ATOM   9891  C  CE2   . TYR B 1 540 ? 111.885 139.415 181.360 1.00 44.42 ? 540 TYR B CE2   1 
ATOM   9892  C  CZ    . TYR B 1 540 ? 111.631 139.770 180.053 1.00 44.13 ? 540 TYR B CZ    1 
ATOM   9893  O  OH    . TYR B 1 540 ? 110.634 139.132 179.353 1.00 47.95 ? 540 TYR B OH    1 
ATOM   9894  N  N     . GLU B 1 541 ? 115.265 143.254 185.140 1.00 49.42 ? 541 GLU B N     1 
ATOM   9895  C  CA    . GLU B 1 541 ? 116.249 143.735 186.105 1.00 46.21 ? 541 GLU B CA    1 
ATOM   9896  C  C     . GLU B 1 541 ? 117.637 143.183 185.804 1.00 46.13 ? 541 GLU B C     1 
ATOM   9897  O  O     . GLU B 1 541 ? 118.641 143.887 185.966 1.00 46.05 ? 541 GLU B O     1 
ATOM   9898  C  CB    . GLU B 1 541 ? 115.817 143.363 187.523 1.00 46.84 ? 541 GLU B CB    1 
ATOM   9899  C  CG    . GLU B 1 541 ? 116.660 143.998 188.616 1.00 47.64 ? 541 GLU B CG    1 
ATOM   9900  C  CD    . GLU B 1 541 ? 117.469 142.979 189.393 1.00 51.25 ? 541 GLU B CD    1 
ATOM   9901  O  OE1   . GLU B 1 541 ? 117.248 141.766 189.192 1.00 49.36 ? 541 GLU B OE1   1 
ATOM   9902  O  OE2   . GLU B 1 541 ? 118.326 143.390 190.203 1.00 51.55 ? 541 GLU B OE2   1 
ATOM   9903  N  N     . LYS B 1 542 ? 117.715 141.921 185.375 1.00 42.73 ? 542 LYS B N     1 
ATOM   9904  C  CA    . LYS B 1 542 ? 119.006 141.336 185.030 1.00 40.19 ? 542 LYS B CA    1 
ATOM   9905  C  C     . LYS B 1 542 ? 119.646 142.063 183.855 1.00 43.32 ? 542 LYS B C     1 
ATOM   9906  O  O     . LYS B 1 542 ? 120.851 142.340 183.867 1.00 41.99 ? 542 LYS B O     1 
ATOM   9907  C  CB    . LYS B 1 542 ? 118.841 139.850 184.713 1.00 41.41 ? 542 LYS B CB    1 
ATOM   9908  C  CG    . LYS B 1 542 ? 120.112 139.178 184.222 1.00 43.11 ? 542 LYS B CG    1 
ATOM   9909  C  CD    . LYS B 1 542 ? 119.933 137.677 184.088 1.00 41.86 ? 542 LYS B CD    1 
ATOM   9910  C  CE    . LYS B 1 542 ? 121.254 136.993 183.778 1.00 43.70 ? 542 LYS B CE    1 
ATOM   9911  N  NZ    . LYS B 1 542 ? 121.146 135.512 183.866 1.00 44.01 ? 542 LYS B NZ    1 
ATOM   9912  N  N     . ILE B 1 543 ? 118.855 142.380 182.828 1.00 42.50 ? 543 ILE B N     1 
ATOM   9913  C  CA    . ILE B 1 543 ? 119.388 143.098 181.675 1.00 38.14 ? 543 ILE B CA    1 
ATOM   9914  C  C     . ILE B 1 543 ? 119.744 144.530 182.053 1.00 37.34 ? 543 ILE B C     1 
ATOM   9915  O  O     . ILE B 1 543 ? 120.773 145.062 181.619 1.00 38.13 ? 543 ILE B O     1 
ATOM   9916  C  CB    . ILE B 1 543 ? 118.388 143.051 180.507 1.00 37.16 ? 543 ILE B CB    1 
ATOM   9917  C  CG1   . ILE B 1 543 ? 118.012 141.605 180.180 1.00 37.87 ? 543 ILE B CG1   1 
ATOM   9918  C  CG2   . ILE B 1 543 ? 118.970 143.737 179.289 1.00 36.18 ? 543 ILE B CG2   1 
ATOM   9919  C  CD1   . ILE B 1 543 ? 119.199 140.686 180.003 1.00 34.87 ? 543 ILE B CD1   1 
ATOM   9920  N  N     . ALA B 1 544 ? 118.901 145.179 182.860 1.00 36.59 ? 544 ALA B N     1 
ATOM   9921  C  CA    . ALA B 1 544 ? 119.199 146.539 183.296 1.00 38.88 ? 544 ALA B CA    1 
ATOM   9922  C  C     . ALA B 1 544 ? 120.466 146.592 184.137 1.00 42.26 ? 544 ALA B C     1 
ATOM   9923  O  O     . ALA B 1 544 ? 121.145 147.625 184.172 1.00 45.80 ? 544 ALA B O     1 
ATOM   9924  C  CB    . ALA B 1 544 ? 118.018 147.112 184.078 1.00 39.78 ? 544 ALA B CB    1 
ATOM   9925  N  N     . ASN B 1 545 ? 120.801 145.495 184.820 1.00 44.09 ? 545 ASN B N     1 
ATOM   9926  C  CA    . ASN B 1 545 ? 122.049 145.447 185.573 1.00 46.22 ? 545 ASN B CA    1 
ATOM   9927  C  C     . ASN B 1 545 ? 123.252 145.306 184.651 1.00 45.01 ? 545 ASN B C     1 
ATOM   9928  O  O     . ASN B 1 545 ? 124.361 145.710 185.018 1.00 45.25 ? 545 ASN B O     1 
ATOM   9929  C  CB    . ASN B 1 545 ? 122.013 144.296 186.578 1.00 46.28 ? 545 ASN B CB    1 
ATOM   9930  C  CG    . ASN B 1 545 ? 121.181 144.619 187.801 1.00 48.38 ? 545 ASN B CG    1 
ATOM   9931  O  OD1   . ASN B 1 545 ? 121.006 145.784 188.157 1.00 47.47 ? 545 ASN B OD1   1 
ATOM   9932  N  ND2   . ASN B 1 545 ? 120.663 143.585 188.454 1.00 44.99 ? 545 ASN B ND2   1 
ATOM   9933  N  N     . LEU B 1 546 ? 123.058 144.732 183.462 1.00 43.93 ? 546 LEU B N     1 
ATOM   9934  C  CA    . LEU B 1 546 ? 124.158 144.606 182.512 1.00 37.66 ? 546 LEU B CA    1 
ATOM   9935  C  C     . LEU B 1 546 ? 124.637 145.967 182.027 1.00 38.68 ? 546 LEU B C     1 
ATOM   9936  O  O     . LEU B 1 546 ? 125.815 146.126 181.688 1.00 40.27 ? 546 LEU B O     1 
ATOM   9937  C  CB    . LEU B 1 546 ? 123.731 143.743 181.324 1.00 36.45 ? 546 LEU B CB    1 
ATOM   9938  C  CG    . LEU B 1 546 ? 123.326 142.299 181.619 1.00 38.21 ? 546 LEU B CG    1 
ATOM   9939  C  CD1   . LEU B 1 546 ? 122.840 141.618 180.352 1.00 37.57 ? 546 LEU B CD1   1 
ATOM   9940  C  CD2   . LEU B 1 546 ? 124.482 141.528 182.233 1.00 37.43 ? 546 LEU B CD2   1 
ATOM   9941  N  N     . PHE B 1 547 ? 123.748 146.959 181.996 1.00 39.42 ? 547 PHE B N     1 
ATOM   9942  C  CA    . PHE B 1 547 ? 124.072 148.297 181.526 1.00 39.22 ? 547 PHE B CA    1 
ATOM   9943  C  C     . PHE B 1 547 ? 124.411 149.248 182.668 1.00 40.37 ? 547 PHE B C     1 
ATOM   9944  O  O     . PHE B 1 547 ? 124.365 150.468 182.483 1.00 42.96 ? 547 PHE B O     1 
ATOM   9945  C  CB    . PHE B 1 547 ? 122.917 148.862 180.699 1.00 37.65 ? 547 PHE B CB    1 
ATOM   9946  C  CG    . PHE B 1 547 ? 122.702 148.156 179.391 1.00 38.42 ? 547 PHE B CG    1 
ATOM   9947  C  CD1   . PHE B 1 547 ? 121.874 147.051 179.312 1.00 37.52 ? 547 PHE B CD1   1 
ATOM   9948  C  CD2   . PHE B 1 547 ? 123.327 148.600 178.239 1.00 38.05 ? 547 PHE B CD2   1 
ATOM   9949  C  CE1   . PHE B 1 547 ? 121.674 146.402 178.109 1.00 37.12 ? 547 PHE B CE1   1 
ATOM   9950  C  CE2   . PHE B 1 547 ? 123.131 147.955 177.035 1.00 34.52 ? 547 PHE B CE2   1 
ATOM   9951  C  CZ    . PHE B 1 547 ? 122.304 146.855 176.970 1.00 35.12 ? 547 PHE B CZ    1 
ATOM   9952  N  N     . GLU B 1 548 ? 124.737 148.714 183.843 1.00 47.77 ? 548 GLU B N     1 
ATOM   9953  C  CA    . GLU B 1 548 ? 125.088 149.555 184.978 1.00 48.41 ? 548 GLU B CA    1 
ATOM   9954  C  C     . GLU B 1 548 ? 126.349 150.355 184.677 1.00 51.76 ? 548 GLU B C     1 
ATOM   9955  O  O     . GLU B 1 548 ? 127.291 149.853 184.058 1.00 51.78 ? 548 GLU B O     1 
ATOM   9956  C  CB    . GLU B 1 548 ? 125.291 148.699 186.228 1.00 47.98 ? 548 GLU B CB    1 
ATOM   9957  C  CG    . GLU B 1 548 ? 124.041 148.522 187.073 1.00 50.23 ? 548 GLU B CG    1 
ATOM   9958  C  CD    . GLU B 1 548 ? 124.195 147.433 188.117 1.00 54.34 ? 548 GLU B CD    1 
ATOM   9959  O  OE1   . GLU B 1 548 ? 125.066 146.555 187.937 1.00 54.25 ? 548 GLU B OE1   1 
ATOM   9960  O  OE2   . GLU B 1 548 ? 123.447 147.453 189.116 1.00 53.30 ? 548 GLU B OE2   1 
ATOM   9961  N  N     . GLY B 1 549 ? 126.363 151.609 185.120 1.00 50.59 ? 549 GLY B N     1 
ATOM   9962  C  CA    . GLY B 1 549 ? 127.465 152.495 184.815 1.00 49.86 ? 549 GLY B CA    1 
ATOM   9963  C  C     . GLY B 1 549 ? 127.466 153.035 183.405 1.00 51.92 ? 549 GLY B C     1 
ATOM   9964  O  O     . GLY B 1 549 ? 128.481 153.591 182.971 1.00 53.53 ? 549 GLY B O     1 
ATOM   9965  N  N     . MET B 1 550 ? 126.363 152.886 182.677 1.00 49.29 ? 550 MET B N     1 
ATOM   9966  C  CA    . MET B 1 550 ? 126.270 153.311 181.289 1.00 45.25 ? 550 MET B CA    1 
ATOM   9967  C  C     . MET B 1 550 ? 124.919 153.969 181.068 1.00 46.66 ? 550 MET B C     1 
ATOM   9968  O  O     . MET B 1 550 ? 123.881 153.376 181.375 1.00 51.11 ? 550 MET B O     1 
ATOM   9969  C  CB    . MET B 1 550 ? 126.446 152.121 180.343 1.00 45.49 ? 550 MET B CB    1 
ATOM   9970  C  CG    . MET B 1 550 ? 127.185 152.445 179.065 1.00 50.47 ? 550 MET B CG    1 
ATOM   9971  S  SD    . MET B 1 550 ? 127.216 151.043 177.937 1.00 56.75 ? 550 MET B SD    1 
ATOM   9972  C  CE    . MET B 1 550 ? 127.196 149.670 179.086 1.00 47.76 ? 550 MET B CE    1 
ATOM   9973  N  N     . HIS B 1 551 ? 124.931 155.188 180.537 1.00 42.77 ? 551 HIS B N     1 
ATOM   9974  C  CA    . HIS B 1 551 ? 123.698 155.935 180.327 1.00 43.01 ? 551 HIS B CA    1 
ATOM   9975  C  C     . HIS B 1 551 ? 122.967 155.393 179.106 1.00 45.22 ? 551 HIS B C     1 
ATOM   9976  O  O     . HIS B 1 551 ? 123.470 155.483 177.981 1.00 44.00 ? 551 HIS B O     1 
ATOM   9977  C  CB    . HIS B 1 551 ? 123.990 157.423 180.158 1.00 42.08 ? 551 HIS B CB    1 
ATOM   9978  C  CG    . HIS B 1 551 ? 122.800 158.221 179.728 1.00 45.26 ? 551 HIS B CG    1 
ATOM   9979  N  ND1   . HIS B 1 551 ? 121.829 158.645 180.610 1.00 47.31 ? 551 HIS B ND1   1 
ATOM   9980  C  CD2   . HIS B 1 551 ? 122.421 158.669 178.508 1.00 45.64 ? 551 HIS B CD2   1 
ATOM   9981  C  CE1   . HIS B 1 551 ? 120.904 159.320 179.952 1.00 45.32 ? 551 HIS B CE1   1 
ATOM   9982  N  NE2   . HIS B 1 551 ? 121.239 159.350 178.675 1.00 44.90 ? 551 HIS B NE2   1 
ATOM   9983  N  N     . ILE B 1 552 ? 121.784 154.833 179.328 1.00 40.04 ? 552 ILE B N     1 
ATOM   9984  C  CA    . ILE B 1 552 ? 120.931 154.343 178.252 1.00 37.32 ? 552 ILE B CA    1 
ATOM   9985  C  C     . ILE B 1 552 ? 120.123 155.525 177.722 1.00 37.11 ? 552 ILE B C     1 
ATOM   9986  O  O     . ILE B 1 552 ? 119.435 156.188 178.514 1.00 37.36 ? 552 ILE B O     1 
ATOM   9987  C  CB    . ILE B 1 552 ? 120.009 153.219 178.737 1.00 35.82 ? 552 ILE B CB    1 
ATOM   9988  C  CG1   . ILE B 1 552 ? 120.841 152.050 179.263 1.00 35.18 ? 552 ILE B CG1   1 
ATOM   9989  C  CG2   . ILE B 1 552 ? 119.085 152.764 177.620 1.00 35.99 ? 552 ILE B CG2   1 
ATOM   9990  C  CD1   . ILE B 1 552 ? 120.047 151.052 180.060 1.00 37.96 ? 552 ILE B CD1   1 
ATOM   9991  N  N     . PRO B 1 553 ? 120.192 155.831 176.427 1.00 38.64 ? 553 PRO B N     1 
ATOM   9992  C  CA    . PRO B 1 553 ? 119.445 156.980 175.901 1.00 36.57 ? 553 PRO B CA    1 
ATOM   9993  C  C     . PRO B 1 553 ? 117.952 156.841 176.148 1.00 38.50 ? 553 PRO B C     1 
ATOM   9994  O  O     . PRO B 1 553 ? 117.367 155.770 175.978 1.00 39.28 ? 553 PRO B O     1 
ATOM   9995  C  CB    . PRO B 1 553 ? 119.770 156.955 174.404 1.00 34.30 ? 553 PRO B CB    1 
ATOM   9996  C  CG    . PRO B 1 553 ? 121.069 156.236 174.315 1.00 32.44 ? 553 PRO B CG    1 
ATOM   9997  C  CD    . PRO B 1 553 ? 121.046 155.210 175.403 1.00 33.37 ? 553 PRO B CD    1 
ATOM   9998  N  N     . THR B 1 554 ? 117.337 157.947 176.549 1.00 41.03 ? 554 THR B N     1 
ATOM   9999  C  CA    . THR B 1 554 ? 115.920 157.989 176.860 1.00 39.80 ? 554 THR B CA    1 
ATOM   10000 C  C     . THR B 1 554 ? 115.156 158.652 175.719 1.00 38.36 ? 554 THR B C     1 
ATOM   10001 O  O     . THR B 1 554 ? 115.706 158.968 174.663 1.00 37.34 ? 554 THR B O     1 
ATOM   10002 C  CB    . THR B 1 554 ? 115.682 158.726 178.179 1.00 37.17 ? 554 THR B CB    1 
ATOM   10003 O  OG1   . THR B 1 554 ? 115.871 160.133 177.982 1.00 43.04 ? 554 THR B OG1   1 
ATOM   10004 C  CG2   . THR B 1 554 ? 116.651 158.238 179.243 1.00 36.57 ? 554 THR B CG2   1 
ATOM   10005 N  N     . THR B 1 555 ? 113.857 158.854 175.941 1.00 41.32 ? 555 THR B N     1 
ATOM   10006 C  CA    . THR B 1 555 ? 113.039 159.563 174.964 1.00 38.99 ? 555 THR B CA    1 
ATOM   10007 C  C     . THR B 1 555 ? 113.489 161.013 174.818 1.00 40.10 ? 555 THR B C     1 
ATOM   10008 O  O     . THR B 1 555 ? 113.533 161.545 173.703 1.00 43.09 ? 555 THR B O     1 
ATOM   10009 C  CB    . THR B 1 555 ? 111.566 159.478 175.366 1.00 42.66 ? 555 THR B CB    1 
ATOM   10010 O  OG1   . THR B 1 555 ? 111.047 158.192 175.004 1.00 39.92 ? 555 THR B OG1   1 
ATOM   10011 C  CG2   . THR B 1 555 ? 110.749 160.556 174.680 1.00 41.92 ? 555 THR B CG2   1 
ATOM   10012 N  N     . GLU B 1 556 ? 113.839 161.664 175.930 1.00 36.99 ? 556 GLU B N     1 
ATOM   10013 C  CA    . GLU B 1 556 ? 114.337 163.035 175.860 1.00 40.35 ? 556 GLU B CA    1 
ATOM   10014 C  C     . GLU B 1 556 ? 115.679 163.102 175.141 1.00 39.81 ? 556 GLU B C     1 
ATOM   10015 O  O     . GLU B 1 556 ? 115.932 164.037 174.372 1.00 42.47 ? 556 GLU B O     1 
ATOM   10016 C  CB    . GLU B 1 556 ? 114.446 163.625 177.265 1.00 41.34 ? 556 GLU B CB    1 
ATOM   10017 C  CG    . GLU B 1 556 ? 113.106 163.900 177.932 1.00 41.93 ? 556 GLU B CG    1 
ATOM   10018 C  CD    . GLU B 1 556 ? 112.078 164.477 176.974 1.00 43.99 ? 556 GLU B CD    1 
ATOM   10019 O  OE1   . GLU B 1 556 ? 112.104 165.703 176.742 1.00 42.48 ? 556 GLU B OE1   1 
ATOM   10020 O  OE2   . GLU B 1 556 ? 111.239 163.706 176.461 1.00 44.64 ? 556 GLU B OE2   1 
ATOM   10021 N  N     . ASP B 1 557 ? 116.554 162.122 175.381 1.00 38.88 ? 557 ASP B N     1 
ATOM   10022 C  CA    . ASP B 1 557 ? 117.821 162.071 174.658 1.00 35.51 ? 557 ASP B CA    1 
ATOM   10023 C  C     . ASP B 1 557 ? 117.590 161.894 173.164 1.00 36.21 ? 557 ASP B C     1 
ATOM   10024 O  O     . ASP B 1 557 ? 118.284 162.502 172.342 1.00 38.94 ? 557 ASP B O     1 
ATOM   10025 C  CB    . ASP B 1 557 ? 118.694 160.940 175.201 1.00 34.40 ? 557 ASP B CB    1 
ATOM   10026 C  CG    . ASP B 1 557 ? 119.159 161.192 176.618 1.00 41.34 ? 557 ASP B CG    1 
ATOM   10027 O  OD1   . ASP B 1 557 ? 119.753 162.261 176.868 1.00 43.97 ? 557 ASP B OD1   1 
ATOM   10028 O  OD2   . ASP B 1 557 ? 118.932 160.320 177.482 1.00 41.24 ? 557 ASP B OD2   1 
ATOM   10029 N  N     . TRP B 1 558 ? 116.613 161.066 172.793 1.00 30.95 ? 558 TRP B N     1 
ATOM   10030 C  CA    . TRP B 1 558 ? 116.298 160.886 171.382 1.00 26.64 ? 558 TRP B CA    1 
ATOM   10031 C  C     . TRP B 1 558 ? 115.690 162.142 170.772 1.00 31.85 ? 558 TRP B C     1 
ATOM   10032 O  O     . TRP B 1 558 ? 115.945 162.441 169.603 1.00 36.78 ? 558 TRP B O     1 
ATOM   10033 C  CB    . TRP B 1 558 ? 115.365 159.693 171.204 1.00 31.13 ? 558 TRP B CB    1 
ATOM   10034 C  CG    . TRP B 1 558 ? 116.095 158.400 171.051 1.00 28.80 ? 558 TRP B CG    1 
ATOM   10035 C  CD1   . TRP B 1 558 ? 116.195 157.400 171.970 1.00 26.56 ? 558 TRP B CD1   1 
ATOM   10036 C  CD2   . TRP B 1 558 ? 116.832 157.965 169.903 1.00 29.49 ? 558 TRP B CD2   1 
ATOM   10037 N  NE1   . TRP B 1 558 ? 116.947 156.368 171.467 1.00 31.41 ? 558 TRP B NE1   1 
ATOM   10038 C  CE2   . TRP B 1 558 ? 117.347 156.690 170.197 1.00 29.65 ? 558 TRP B CE2   1 
ATOM   10039 C  CE3   . TRP B 1 558 ? 117.097 158.528 168.652 1.00 30.29 ? 558 TRP B CE3   1 
ATOM   10040 C  CZ2   . TRP B 1 558 ? 118.115 155.969 169.288 1.00 26.15 ? 558 TRP B CZ2   1 
ATOM   10041 C  CZ3   . TRP B 1 558 ? 117.862 157.812 167.753 1.00 27.71 ? 558 TRP B CZ3   1 
ATOM   10042 C  CH2   . TRP B 1 558 ? 118.361 156.547 168.074 1.00 24.22 ? 558 TRP B CH2   1 
ATOM   10043 N  N     . LYS B 1 559 ? 114.888 162.888 171.535 1.00 36.03 ? 559 LYS B N     1 
ATOM   10044 C  CA    . LYS B 1 559 ? 114.384 164.166 171.039 1.00 34.30 ? 559 LYS B CA    1 
ATOM   10045 C  C     . LYS B 1 559 ? 115.519 165.160 170.828 1.00 36.22 ? 559 LYS B C     1 
ATOM   10046 O  O     . LYS B 1 559 ? 115.532 165.901 169.836 1.00 37.45 ? 559 LYS B O     1 
ATOM   10047 C  CB    . LYS B 1 559 ? 113.349 164.736 172.005 1.00 35.89 ? 559 LYS B CB    1 
ATOM   10048 C  CG    . LYS B 1 559 ? 111.992 164.065 171.928 1.00 40.19 ? 559 LYS B CG    1 
ATOM   10049 C  CD    . LYS B 1 559 ? 111.073 164.560 173.029 1.00 36.82 ? 559 LYS B CD    1 
ATOM   10050 C  CE    . LYS B 1 559 ? 109.829 163.701 173.135 1.00 39.56 ? 559 LYS B CE    1 
ATOM   10051 N  NZ    . LYS B 1 559 ? 109.275 163.705 174.516 1.00 37.86 ? 559 LYS B NZ    1 
ATOM   10052 N  N     . LYS B 1 560 ? 116.478 165.194 171.754 1.00 34.26 ? 560 LYS B N     1 
ATOM   10053 C  CA    . LYS B 1 560 ? 117.641 166.058 171.585 1.00 34.38 ? 560 LYS B CA    1 
ATOM   10054 C  C     . LYS B 1 560 ? 118.450 165.655 170.358 1.00 37.78 ? 560 LYS B C     1 
ATOM   10055 O  O     . LYS B 1 560 ? 118.927 166.514 169.609 1.00 40.45 ? 560 LYS B O     1 
ATOM   10056 C  CB    . LYS B 1 560 ? 118.511 166.020 172.840 1.00 36.76 ? 560 LYS B CB    1 
ATOM   10057 C  CG    . LYS B 1 560 ? 118.087 167.003 173.916 1.00 36.74 ? 560 LYS B CG    1 
ATOM   10058 C  CD    . LYS B 1 560 ? 118.826 166.748 175.218 1.00 41.07 ? 560 LYS B CD    1 
ATOM   10059 C  CE    . LYS B 1 560 ? 117.898 166.878 176.415 1.00 38.77 ? 560 LYS B CE    1 
ATOM   10060 N  NZ    . LYS B 1 560 ? 117.968 165.685 177.304 1.00 42.21 ? 560 LYS B NZ    1 
ATOM   10061 N  N     . LEU B 1 561 ? 118.614 164.349 170.137 1.00 35.14 ? 561 LEU B N     1 
ATOM   10062 C  CA    . LEU B 1 561 ? 119.313 163.879 168.945 1.00 30.45 ? 561 LEU B CA    1 
ATOM   10063 C  C     . LEU B 1 561 ? 118.553 164.245 167.676 1.00 33.74 ? 561 LEU B C     1 
ATOM   10064 O  O     . LEU B 1 561 ? 119.163 164.595 166.662 1.00 37.08 ? 561 LEU B O     1 
ATOM   10065 C  CB    . LEU B 1 561 ? 119.530 162.369 169.019 1.00 30.49 ? 561 LEU B CB    1 
ATOM   10066 C  CG    . LEU B 1 561 ? 120.328 161.777 167.858 1.00 31.35 ? 561 LEU B CG    1 
ATOM   10067 C  CD1   . LEU B 1 561 ? 121.664 162.484 167.725 1.00 28.72 ? 561 LEU B CD1   1 
ATOM   10068 C  CD2   . LEU B 1 561 ? 120.523 160.287 168.041 1.00 30.00 ? 561 LEU B CD2   1 
ATOM   10069 N  N     . LYS B 1 562 ? 117.223 164.155 167.710 1.00 31.48 ? 562 LYS B N     1 
ATOM   10070 C  CA    . LYS B 1 562 ? 116.417 164.547 166.559 1.00 32.77 ? 562 LYS B CA    1 
ATOM   10071 C  C     . LYS B 1 562 ? 116.590 166.027 166.246 1.00 36.72 ? 562 LYS B C     1 
ATOM   10072 O  O     . LYS B 1 562 ? 116.741 166.411 165.080 1.00 39.94 ? 562 LYS B O     1 
ATOM   10073 C  CB    . LYS B 1 562 ? 114.949 164.220 166.825 1.00 31.43 ? 562 LYS B CB    1 
ATOM   10074 C  CG    . LYS B 1 562 ? 113.984 164.721 165.771 1.00 31.78 ? 562 LYS B CG    1 
ATOM   10075 C  CD    . LYS B 1 562 ? 112.552 164.458 166.197 1.00 30.60 ? 562 LYS B CD    1 
ATOM   10076 C  CE    . LYS B 1 562 ? 111.570 164.776 165.087 1.00 34.82 ? 562 LYS B CE    1 
ATOM   10077 N  NZ    . LYS B 1 562 ? 110.256 164.120 165.325 1.00 37.92 ? 562 LYS B NZ    1 
ATOM   10078 N  N     . ALA B 1 563 ? 116.580 166.872 167.279 1.00 33.59 ? 563 ALA B N     1 
ATOM   10079 C  CA    . ALA B 1 563 ? 116.813 168.297 167.070 1.00 30.72 ? 563 ALA B CA    1 
ATOM   10080 C  C     . ALA B 1 563 ? 118.214 168.554 166.528 1.00 33.10 ? 563 ALA B C     1 
ATOM   10081 O  O     . ALA B 1 563 ? 118.401 169.388 165.634 1.00 38.58 ? 563 ALA B O     1 
ATOM   10082 C  CB    . ALA B 1 563 ? 116.594 169.061 168.375 1.00 34.29 ? 563 ALA B CB    1 
ATOM   10083 N  N     . PHE B 1 564 ? 119.211 167.839 167.055 1.00 36.49 ? 564 PHE B N     1 
ATOM   10084 C  CA    . PHE B 1 564 ? 120.583 168.002 166.584 1.00 32.94 ? 564 PHE B CA    1 
ATOM   10085 C  C     . PHE B 1 564 ? 120.718 167.597 165.121 1.00 36.22 ? 564 PHE B C     1 
ATOM   10086 O  O     . PHE B 1 564 ? 121.418 168.259 164.347 1.00 39.68 ? 564 PHE B O     1 
ATOM   10087 C  CB    . PHE B 1 564 ? 121.527 167.182 167.462 1.00 33.17 ? 564 PHE B CB    1 
ATOM   10088 C  CG    . PHE B 1 564 ? 122.975 167.531 167.291 1.00 35.70 ? 564 PHE B CG    1 
ATOM   10089 C  CD1   . PHE B 1 564 ? 123.501 168.670 167.875 1.00 35.60 ? 564 PHE B CD1   1 
ATOM   10090 C  CD2   . PHE B 1 564 ? 123.814 166.715 166.554 1.00 38.47 ? 564 PHE B CD2   1 
ATOM   10091 C  CE1   . PHE B 1 564 ? 124.835 168.990 167.722 1.00 40.33 ? 564 PHE B CE1   1 
ATOM   10092 C  CE2   . PHE B 1 564 ? 125.148 167.031 166.395 1.00 37.37 ? 564 PHE B CE2   1 
ATOM   10093 C  CZ    . PHE B 1 564 ? 125.659 168.170 166.980 1.00 37.50 ? 564 PHE B CZ    1 
ATOM   10094 N  N     . VAL B 1 565 ? 120.055 166.510 164.726 1.00 33.98 ? 565 VAL B N     1 
ATOM   10095 C  CA    . VAL B 1 565 ? 120.118 166.054 163.342 1.00 30.47 ? 565 VAL B CA    1 
ATOM   10096 C  C     . VAL B 1 565 ? 119.391 167.028 162.425 1.00 34.46 ? 565 VAL B C     1 
ATOM   10097 O  O     . VAL B 1 565 ? 119.847 167.311 161.311 1.00 37.70 ? 565 VAL B O     1 
ATOM   10098 C  CB    . VAL B 1 565 ? 119.550 164.627 163.229 1.00 31.45 ? 565 VAL B CB    1 
ATOM   10099 C  CG1   . VAL B 1 565 ? 119.202 164.294 161.788 1.00 33.30 ? 565 VAL B CG1   1 
ATOM   10100 C  CG2   . VAL B 1 565 ? 120.543 163.626 163.782 1.00 32.47 ? 565 VAL B CG2   1 
ATOM   10101 N  N     . ALA B 1 566 ? 118.256 167.564 162.877 1.00 36.25 ? 566 ALA B N     1 
ATOM   10102 C  CA    . ALA B 1 566 ? 117.551 168.563 162.082 1.00 34.98 ? 566 ALA B CA    1 
ATOM   10103 C  C     . ALA B 1 566 ? 118.399 169.814 161.896 1.00 36.92 ? 566 ALA B C     1 
ATOM   10104 O  O     . ALA B 1 566 ? 118.399 170.420 160.818 1.00 41.53 ? 566 ALA B O     1 
ATOM   10105 C  CB    . ALA B 1 566 ? 116.217 168.911 162.739 1.00 34.47 ? 566 ALA B CB    1 
ATOM   10106 N  N     . GLU B 1 567 ? 119.126 170.218 162.937 1.00 38.39 ? 567 GLU B N     1 
ATOM   10107 C  CA    . GLU B 1 567 ? 119.932 171.431 162.853 1.00 38.03 ? 567 GLU B CA    1 
ATOM   10108 C  C     . GLU B 1 567 ? 121.167 171.227 161.982 1.00 41.65 ? 567 GLU B C     1 
ATOM   10109 O  O     . GLU B 1 567 ? 121.489 172.070 161.138 1.00 47.92 ? 567 GLU B O     1 
ATOM   10110 C  CB    . GLU B 1 567 ? 120.335 171.884 164.255 1.00 39.35 ? 567 GLU B CB    1 
ATOM   10111 C  CG    . GLU B 1 567 ? 121.096 173.195 164.291 1.00 41.43 ? 567 GLU B CG    1 
ATOM   10112 C  CD    . GLU B 1 567 ? 121.641 173.509 165.669 1.00 47.39 ? 567 GLU B CD    1 
ATOM   10113 O  OE1   . GLU B 1 567 ? 121.169 172.895 166.649 1.00 48.42 ? 567 GLU B OE1   1 
ATOM   10114 O  OE2   . GLU B 1 567 ? 122.538 174.371 165.773 1.00 45.24 ? 567 GLU B OE2   1 
ATOM   10115 N  N     . HIS B 1 568 ? 121.873 170.110 162.168 1.00 43.03 ? 568 HIS B N     1 
ATOM   10116 C  CA    . HIS B 1 568 ? 123.191 169.931 161.577 1.00 39.90 ? 568 HIS B CA    1 
ATOM   10117 C  C     . HIS B 1 568 ? 123.239 168.892 160.467 1.00 35.72 ? 568 HIS B C     1 
ATOM   10118 O  O     . HIS B 1 568 ? 124.243 168.828 159.749 1.00 42.45 ? 568 HIS B O     1 
ATOM   10119 C  CB    . HIS B 1 568 ? 124.207 169.547 162.661 1.00 39.15 ? 568 HIS B CB    1 
ATOM   10120 C  CG    . HIS B 1 568 ? 124.476 170.640 163.646 1.00 39.33 ? 568 HIS B CG    1 
ATOM   10121 N  ND1   . HIS B 1 568 ? 124.074 170.569 164.962 1.00 40.39 ? 568 HIS B ND1   1 
ATOM   10122 C  CD2   . HIS B 1 568 ? 125.092 171.837 163.505 1.00 40.15 ? 568 HIS B CD2   1 
ATOM   10123 C  CE1   . HIS B 1 568 ? 124.441 171.671 165.592 1.00 40.68 ? 568 HIS B CE1   1 
ATOM   10124 N  NE2   . HIS B 1 568 ? 125.060 172.457 164.731 1.00 44.60 ? 568 HIS B NE2   1 
ATOM   10125 N  N     . GLY B 1 569 ? 122.206 168.083 160.306 1.00 30.85 ? 569 GLY B N     1 
ATOM   10126 C  CA    . GLY B 1 569 ? 122.209 167.084 159.264 1.00 29.89 ? 569 GLY B CA    1 
ATOM   10127 C  C     . GLY B 1 569 ? 122.857 165.786 159.693 1.00 30.77 ? 569 GLY B C     1 
ATOM   10128 O  O     . GLY B 1 569 ? 123.211 165.567 160.855 1.00 37.06 ? 569 GLY B O     1 
ATOM   10129 N  N     . MET B 1 570 ? 123.008 164.902 158.713 1.00 28.09 ? 570 MET B N     1 
ATOM   10130 C  CA    . MET B 1 570 ? 123.534 163.562 158.928 1.00 24.38 ? 570 MET B CA    1 
ATOM   10131 C  C     . MET B 1 570 ? 124.581 163.285 157.861 1.00 25.17 ? 570 MET B C     1 
ATOM   10132 O  O     . MET B 1 570 ? 124.320 163.481 156.671 1.00 29.79 ? 570 MET B O     1 
ATOM   10133 C  CB    . MET B 1 570 ? 122.398 162.534 158.875 1.00 30.09 ? 570 MET B CB    1 
ATOM   10134 C  CG    . MET B 1 570 ? 121.757 162.255 160.227 1.00 25.68 ? 570 MET B CG    1 
ATOM   10135 S  SD    . MET B 1 570 ? 121.323 160.532 160.501 1.00 43.15 ? 570 MET B SD    1 
ATOM   10136 C  CE    . MET B 1 570 ? 122.925 159.766 160.528 1.00 26.15 ? 570 MET B CE    1 
ATOM   10137 N  N     . TYR B 1 571 ? 125.769 162.850 158.285 1.00 21.60 ? 571 TYR B N     1 
ATOM   10138 C  CA    . TYR B 1 571 ? 126.873 162.682 157.346 1.00 16.69 ? 571 TYR B CA    1 
ATOM   10139 C  C     . TYR B 1 571 ? 126.771 161.392 156.543 1.00 22.12 ? 571 TYR B C     1 
ATOM   10140 O  O     . TYR B 1 571 ? 127.159 161.368 155.370 1.00 21.68 ? 571 TYR B O     1 
ATOM   10141 C  CB    . TYR B 1 571 ? 128.209 162.722 158.084 1.00 20.04 ? 571 TYR B CB    1 
ATOM   10142 C  CG    . TYR B 1 571 ? 129.403 162.778 157.162 1.00 21.23 ? 571 TYR B CG    1 
ATOM   10143 C  CD1   . TYR B 1 571 ? 129.757 163.960 156.525 1.00 22.64 ? 571 TYR B CD1   1 
ATOM   10144 C  CD2   . TYR B 1 571 ? 130.174 161.650 156.921 1.00 21.61 ? 571 TYR B CD2   1 
ATOM   10145 C  CE1   . TYR B 1 571 ? 130.844 164.015 155.677 1.00 22.48 ? 571 TYR B CE1   1 
ATOM   10146 C  CE2   . TYR B 1 571 ? 131.262 161.696 156.077 1.00 22.91 ? 571 TYR B CE2   1 
ATOM   10147 C  CZ    . TYR B 1 571 ? 131.594 162.881 155.458 1.00 28.09 ? 571 TYR B CZ    1 
ATOM   10148 O  OH    . TYR B 1 571 ? 132.680 162.928 154.616 1.00 29.01 ? 571 TYR B OH    1 
ATOM   10149 N  N     . HIS B 1 572 ? 126.264 160.320 157.143 1.00 24.21 ? 572 HIS B N     1 
ATOM   10150 C  CA    . HIS B 1 572 ? 126.183 159.019 156.495 1.00 14.71 ? 572 HIS B CA    1 
ATOM   10151 C  C     . HIS B 1 572 ? 124.735 158.700 156.160 1.00 17.78 ? 572 HIS B C     1 
ATOM   10152 O  O     . HIS B 1 572 ? 123.862 158.765 157.032 1.00 28.54 ? 572 HIS B O     1 
ATOM   10153 C  CB    . HIS B 1 572 ? 126.769 157.919 157.386 1.00 13.70 ? 572 HIS B CB    1 
ATOM   10154 C  CG    . HIS B 1 572 ? 128.101 158.259 157.976 1.00 11.03 ? 572 HIS B CG    1 
ATOM   10155 N  ND1   . HIS B 1 572 ? 128.239 158.876 159.201 1.00 16.43 ? 572 HIS B ND1   1 
ATOM   10156 C  CD2   . HIS B 1 572 ? 129.358 158.056 157.516 1.00 15.29 ? 572 HIS B CD2   1 
ATOM   10157 C  CE1   . HIS B 1 572 ? 129.521 159.045 159.465 1.00 16.42 ? 572 HIS B CE1   1 
ATOM   10158 N  NE2   . HIS B 1 572 ? 130.221 158.556 158.459 1.00 24.09 ? 572 HIS B NE2   1 
ATOM   10159 N  N     . SER B 1 573 ? 124.484 158.361 154.894 1.00 12.76 ? 573 SER B N     1 
ATOM   10160 C  CA    . SER B 1 573 ? 123.161 157.883 154.509 1.00 11.69 ? 573 SER B CA    1 
ATOM   10161 C  C     . SER B 1 573 ? 122.832 156.579 155.216 1.00 17.81 ? 573 SER B C     1 
ATOM   10162 O  O     . SER B 1 573 ? 121.689 156.354 155.630 1.00 27.83 ? 573 SER B O     1 
ATOM   10163 C  CB    . SER B 1 573 ? 123.087 157.703 152.995 1.00 15.16 ? 573 SER B CB    1 
ATOM   10164 O  OG    . SER B 1 573 ? 124.266 157.097 152.505 1.00 23.25 ? 573 SER B OG    1 
ATOM   10165 N  N     . TYR B 1 574 ? 123.824 155.707 155.359 1.00 15.31 ? 574 TYR B N     1 
ATOM   10166 C  CA    . TYR B 1 574 ? 123.672 154.424 156.022 1.00 3.06  ? 574 TYR B CA    1 
ATOM   10167 C  C     . TYR B 1 574 ? 124.843 154.226 156.969 1.00 10.33 ? 574 TYR B C     1 
ATOM   10168 O  O     . TYR B 1 574 ? 125.978 154.584 156.645 1.00 18.44 ? 574 TYR B O     1 
ATOM   10169 C  CB    . TYR B 1 574 ? 123.601 153.289 155.002 1.00 10.46 ? 574 TYR B CB    1 
ATOM   10170 C  CG    . TYR B 1 574 ? 122.558 153.520 153.936 1.00 2.52  ? 574 TYR B CG    1 
ATOM   10171 C  CD1   . TYR B 1 574 ? 121.253 153.086 154.111 1.00 6.24  ? 574 TYR B CD1   1 
ATOM   10172 C  CD2   . TYR B 1 574 ? 122.874 154.185 152.760 1.00 7.18  ? 574 TYR B CD2   1 
ATOM   10173 C  CE1   . TYR B 1 574 ? 120.297 153.300 153.146 1.00 6.65  ? 574 TYR B CE1   1 
ATOM   10174 C  CE2   . TYR B 1 574 ? 121.923 154.406 151.789 1.00 11.08 ? 574 TYR B CE2   1 
ATOM   10175 C  CZ    . TYR B 1 574 ? 120.637 153.959 151.987 1.00 5.09  ? 574 TYR B CZ    1 
ATOM   10176 O  OH    . TYR B 1 574 ? 119.684 154.172 151.021 1.00 16.31 ? 574 TYR B OH    1 
ATOM   10177 N  N     . ARG B 1 575 ? 124.562 153.667 158.138 1.00 12.43 ? 575 ARG B N     1 
ATOM   10178 C  CA    . ARG B 1 575 ? 125.563 153.552 159.191 1.00 4.82  ? 575 ARG B CA    1 
ATOM   10179 C  C     . ARG B 1 575 ? 125.784 152.132 159.677 1.00 12.50 ? 575 ARG B C     1 
ATOM   10180 O  O     . ARG B 1 575 ? 126.929 151.735 159.898 1.00 20.93 ? 575 ARG B O     1 
ATOM   10181 C  CB    . ARG B 1 575 ? 125.165 154.424 160.384 1.00 13.66 ? 575 ARG B CB    1 
ATOM   10182 C  CG    . ARG B 1 575 ? 125.115 155.901 160.085 1.00 10.39 ? 575 ARG B CG    1 
ATOM   10183 C  CD    . ARG B 1 575 ? 124.277 156.613 161.118 1.00 12.34 ? 575 ARG B CD    1 
ATOM   10184 N  NE    . ARG B 1 575 ? 122.857 156.338 160.941 1.00 17.66 ? 575 ARG B NE    1 
ATOM   10185 C  CZ    . ARG B 1 575 ? 122.150 155.519 161.707 1.00 13.17 ? 575 ARG B CZ    1 
ATOM   10186 N  NH1   . ARG B 1 575 ? 122.701 154.874 162.720 1.00 13.37 ? 575 ARG B NH1   1 
ATOM   10187 N  NH2   . ARG B 1 575 ? 120.857 155.347 161.453 1.00 13.27 ? 575 ARG B NH2   1 
ATOM   10188 N  N     . LEU B 1 576 ? 124.721 151.353 159.852 1.00 19.44 ? 576 LEU B N     1 
ATOM   10189 C  CA    . LEU B 1 576 ? 124.790 150.077 160.547 1.00 12.57 ? 576 LEU B CA    1 
ATOM   10190 C  C     . LEU B 1 576 ? 124.355 148.954 159.620 1.00 6.04  ? 576 LEU B C     1 
ATOM   10191 O  O     . LEU B 1 576 ? 123.281 149.023 159.017 1.00 18.73 ? 576 LEU B O     1 
ATOM   10192 C  CB    . LEU B 1 576 ? 123.910 150.094 161.798 1.00 8.52  ? 576 LEU B CB    1 
ATOM   10193 C  CG    . LEU B 1 576 ? 124.079 151.292 162.734 1.00 8.58  ? 576 LEU B CG    1 
ATOM   10194 C  CD1   . LEU B 1 576 ? 123.041 151.253 163.838 1.00 14.73 ? 576 LEU B CD1   1 
ATOM   10195 C  CD2   . LEU B 1 576 ? 125.478 151.324 163.318 1.00 12.64 ? 576 LEU B CD2   1 
ATOM   10196 N  N     . CYS B 1 577 ? 125.194 147.929 159.508 1.00 10.84 ? 577 CYS B N     1 
ATOM   10197 C  CA    . CYS B 1 577 ? 124.829 146.688 158.840 1.00 9.13  ? 577 CYS B CA    1 
ATOM   10198 C  C     . CYS B 1 577 ? 125.622 145.567 159.491 1.00 19.51 ? 577 CYS B C     1 
ATOM   10199 O  O     . CYS B 1 577 ? 126.829 145.705 159.708 1.00 24.57 ? 577 CYS B O     1 
ATOM   10200 C  CB    . CYS B 1 577 ? 125.095 146.752 157.329 1.00 5.68  ? 577 CYS B CB    1 
ATOM   10201 S  SG    . CYS B 1 577 ? 126.810 146.537 156.796 1.00 31.63 ? 577 CYS B SG    1 
ATOM   10202 N  N     . ILE B 1 578 ? 124.944 144.475 159.819 1.00 14.36 ? 578 ILE B N     1 
ATOM   10203 C  CA    . ILE B 1 578 ? 125.546 143.371 160.555 1.00 13.46 ? 578 ILE B CA    1 
ATOM   10204 C  C     . ILE B 1 578 ? 125.965 142.316 159.538 1.00 8.36  ? 578 ILE B C     1 
ATOM   10205 O  O     . ILE B 1 578 ? 125.155 141.495 159.100 1.00 19.26 ? 578 ILE B O     1 
ATOM   10206 C  CB    . ILE B 1 578 ? 124.595 142.810 161.614 1.00 12.07 ? 578 ILE B CB    1 
ATOM   10207 C  CG1   . ILE B 1 578 ? 124.103 143.937 162.523 1.00 5.97  ? 578 ILE B CG1   1 
ATOM   10208 C  CG2   . ILE B 1 578 ? 125.290 141.750 162.442 1.00 9.26  ? 578 ILE B CG2   1 
ATOM   10209 C  CD1   . ILE B 1 578 ? 123.329 143.459 163.720 1.00 9.92  ? 578 ILE B CD1   1 
ATOM   10210 N  N     . ALA B 1 579 ? 127.239 142.346 159.159 1.00 14.78 ? 579 ALA B N     1 
ATOM   10211 C  CA    . ALA B 1 579 ? 127.832 141.383 158.248 1.00 7.09  ? 579 ALA B CA    1 
ATOM   10212 C  C     . ALA B 1 579 ? 128.109 140.063 158.964 1.00 19.32 ? 579 ALA B C     1 
ATOM   10213 O  O     . ALA B 1 579 ? 128.122 140.007 160.195 1.00 30.00 ? 579 ALA B O     1 
ATOM   10214 C  CB    . ALA B 1 579 ? 129.118 141.955 157.664 1.00 12.27 ? 579 ALA B CB    1 
ATOM   10215 N  N     . PRO B 1 580 ? 128.309 138.974 158.213 1.00 25.48 ? 580 PRO B N     1 
ATOM   10216 C  CA    . PRO B 1 580 ? 128.575 137.679 158.867 1.00 24.03 ? 580 PRO B CA    1 
ATOM   10217 C  C     . PRO B 1 580 ? 129.827 137.653 159.734 1.00 28.95 ? 580 PRO B C     1 
ATOM   10218 O  O     . PRO B 1 580 ? 129.851 136.911 160.725 1.00 34.93 ? 580 PRO B O     1 
ATOM   10219 C  CB    . PRO B 1 580 ? 128.688 136.703 157.685 1.00 23.82 ? 580 PRO B CB    1 
ATOM   10220 C  CG    . PRO B 1 580 ? 128.811 137.550 156.465 1.00 22.98 ? 580 PRO B CG    1 
ATOM   10221 C  CD    . PRO B 1 580 ? 128.102 138.820 156.764 1.00 21.08 ? 580 PRO B CD    1 
ATOM   10222 N  N     . THR B 1 581 ? 130.859 138.429 159.401 1.00 24.79 ? 581 THR B N     1 
ATOM   10223 C  CA    . THR B 1 581 ? 132.119 138.466 160.153 1.00 32.69 ? 581 THR B CA    1 
ATOM   10224 C  C     . THR B 1 581 ? 132.714 137.062 160.293 1.00 31.83 ? 581 THR B C     1 
ATOM   10225 O  O     . THR B 1 581 ? 132.836 136.505 161.384 1.00 33.50 ? 581 THR B O     1 
ATOM   10226 C  CB    . THR B 1 581 ? 131.944 139.113 161.532 1.00 29.27 ? 581 THR B CB    1 
ATOM   10227 O  OG1   . THR B 1 581 ? 131.455 138.140 162.463 1.00 24.95 ? 581 THR B OG1   1 
ATOM   10228 C  CG2   . THR B 1 581 ? 130.985 140.286 161.468 1.00 30.45 ? 581 THR B CG2   1 
ATOM   10229 N  N     . GLY B 1 582 ? 133.079 136.504 159.143 1.00 32.32 ? 582 GLY B N     1 
ATOM   10230 C  CA    . GLY B 1 582 ? 133.515 135.124 159.072 1.00 34.90 ? 582 GLY B CA    1 
ATOM   10231 C  C     . GLY B 1 582 ? 134.792 134.790 159.817 1.00 37.32 ? 582 GLY B C     1 
ATOM   10232 O  O     . GLY B 1 582 ? 134.759 134.045 160.800 1.00 40.01 ? 582 GLY B O     1 
ATOM   10233 N  N     . SER B 1 583 ? 135.923 135.334 159.368 1.00 37.15 ? 583 SER B N     1 
ATOM   10234 C  CA    . SER B 1 583 ? 137.217 134.917 159.895 1.00 41.10 ? 583 SER B CA    1 
ATOM   10235 C  C     . SER B 1 583 ? 137.741 135.821 161.000 1.00 39.09 ? 583 SER B C     1 
ATOM   10236 O  O     . SER B 1 583 ? 138.553 135.373 161.818 1.00 38.80 ? 583 SER B O     1 
ATOM   10237 C  CB    . SER B 1 583 ? 138.247 134.848 158.765 1.00 44.72 ? 583 SER B CB    1 
ATOM   10238 O  OG    . SER B 1 583 ? 138.093 133.660 158.009 1.00 46.25 ? 583 SER B OG    1 
ATOM   10239 N  N     . ILE B 1 584 ? 137.307 137.083 161.048 1.00 32.48 ? 584 ILE B N     1 
ATOM   10240 C  CA    . ILE B 1 584 ? 137.735 137.979 162.117 1.00 29.64 ? 584 ILE B CA    1 
ATOM   10241 C  C     . ILE B 1 584 ? 137.147 137.607 163.467 1.00 31.79 ? 584 ILE B C     1 
ATOM   10242 O  O     . ILE B 1 584 ? 137.607 138.119 164.493 1.00 35.01 ? 584 ILE B O     1 
ATOM   10243 C  CB    . ILE B 1 584 ? 137.372 139.442 161.792 1.00 35.97 ? 584 ILE B CB    1 
ATOM   10244 C  CG1   . ILE B 1 584 ? 135.885 139.561 161.450 1.00 34.84 ? 584 ILE B CG1   1 
ATOM   10245 C  CG2   . ILE B 1 584 ? 138.247 139.976 160.670 1.00 31.81 ? 584 ILE B CG2   1 
ATOM   10246 C  CD1   . ILE B 1 584 ? 135.396 140.987 161.333 1.00 32.94 ? 584 ILE B CD1   1 
ATOM   10247 N  N     . SER B 1 585 ? 136.136 136.736 163.494 1.00 31.86 ? 585 SER B N     1 
ATOM   10248 C  CA    . SER B 1 585 ? 135.556 136.319 164.764 1.00 29.56 ? 585 SER B CA    1 
ATOM   10249 C  C     . SER B 1 585 ? 136.519 135.451 165.563 1.00 29.46 ? 585 SER B C     1 
ATOM   10250 O  O     . SER B 1 585 ? 136.543 135.531 166.795 1.00 29.67 ? 585 SER B O     1 
ATOM   10251 C  CB    . SER B 1 585 ? 134.243 135.577 164.524 1.00 31.84 ? 585 SER B CB    1 
ATOM   10252 O  OG    . SER B 1 585 ? 134.432 134.468 163.664 1.00 35.57 ? 585 SER B OG    1 
ATOM   10253 N  N     . TYR B 1 586 ? 137.309 134.614 164.886 1.00 34.88 ? 586 TYR B N     1 
ATOM   10254 C  CA    . TYR B 1 586 ? 138.302 133.809 165.590 1.00 35.29 ? 586 TYR B CA    1 
ATOM   10255 C  C     . TYR B 1 586 ? 139.359 134.689 166.241 1.00 34.11 ? 586 TYR B C     1 
ATOM   10256 O  O     . TYR B 1 586 ? 139.721 134.480 167.404 1.00 39.21 ? 586 TYR B O     1 
ATOM   10257 C  CB    . TYR B 1 586 ? 138.964 132.822 164.631 1.00 33.13 ? 586 TYR B CB    1 
ATOM   10258 C  CG    . TYR B 1 586 ? 138.016 131.842 163.986 1.00 33.70 ? 586 TYR B CG    1 
ATOM   10259 C  CD1   . TYR B 1 586 ? 137.453 132.105 162.747 1.00 36.01 ? 586 TYR B CD1   1 
ATOM   10260 C  CD2   . TYR B 1 586 ? 137.690 130.649 164.613 1.00 34.94 ? 586 TYR B CD2   1 
ATOM   10261 C  CE1   . TYR B 1 586 ? 136.589 131.211 162.151 1.00 38.19 ? 586 TYR B CE1   1 
ATOM   10262 C  CE2   . TYR B 1 586 ? 136.827 129.747 164.026 1.00 37.41 ? 586 TYR B CE2   1 
ATOM   10263 C  CZ    . TYR B 1 586 ? 136.279 130.034 162.795 1.00 39.02 ? 586 TYR B CZ    1 
ATOM   10264 O  OH    . TYR B 1 586 ? 135.418 129.139 162.205 1.00 42.42 ? 586 TYR B OH    1 
ATOM   10265 N  N     . VAL B 1 587 ? 139.858 135.685 165.505 1.00 30.37 ? 587 VAL B N     1 
ATOM   10266 C  CA    . VAL B 1 587 ? 140.902 136.563 166.026 1.00 25.87 ? 587 VAL B CA    1 
ATOM   10267 C  C     . VAL B 1 587 ? 140.402 137.321 167.247 1.00 30.16 ? 587 VAL B C     1 
ATOM   10268 O  O     . VAL B 1 587 ? 141.142 137.530 168.216 1.00 36.95 ? 587 VAL B O     1 
ATOM   10269 C  CB    . VAL B 1 587 ? 141.385 137.522 164.923 1.00 30.68 ? 587 VAL B CB    1 
ATOM   10270 C  CG1   . VAL B 1 587 ? 142.423 138.484 165.468 1.00 33.04 ? 587 VAL B CG1   1 
ATOM   10271 C  CG2   . VAL B 1 587 ? 141.942 136.737 163.747 1.00 31.08 ? 587 VAL B CG2   1 
ATOM   10272 N  N     . GLN B 1 588 ? 139.139 137.735 167.227 1.00 33.50 ? 588 GLN B N     1 
ATOM   10273 C  CA    . GLN B 1 588 ? 138.552 138.481 168.329 1.00 29.20 ? 588 GLN B CA    1 
ATOM   10274 C  C     . GLN B 1 588 ? 138.042 137.587 169.447 1.00 32.31 ? 588 GLN B C     1 
ATOM   10275 O  O     . GLN B 1 588 ? 137.550 138.111 170.453 1.00 35.45 ? 588 GLN B O     1 
ATOM   10276 C  CB    . GLN B 1 588 ? 137.410 139.359 167.814 1.00 23.70 ? 588 GLN B CB    1 
ATOM   10277 C  CG    . GLN B 1 588 ? 137.871 140.580 167.047 1.00 25.07 ? 588 GLN B CG    1 
ATOM   10278 C  CD    . GLN B 1 588 ? 137.975 141.805 167.927 1.00 28.50 ? 588 GLN B CD    1 
ATOM   10279 O  OE1   . GLN B 1 588 ? 137.128 142.037 168.787 1.00 28.97 ? 588 GLN B OE1   1 
ATOM   10280 N  NE2   . GLN B 1 588 ? 139.016 142.599 167.715 1.00 31.42 ? 588 GLN B NE2   1 
ATOM   10281 N  N     . SER B 1 589 ? 138.154 136.268 169.302 1.00 33.40 ? 589 SER B N     1 
ATOM   10282 C  CA    . SER B 1 589 ? 137.597 135.309 170.252 1.00 29.35 ? 589 SER B CA    1 
ATOM   10283 C  C     . SER B 1 589 ? 136.121 135.612 170.498 1.00 31.49 ? 589 SER B C     1 
ATOM   10284 O  O     . SER B 1 589 ? 135.677 135.863 171.619 1.00 33.28 ? 589 SER B O     1 
ATOM   10285 C  CB    . SER B 1 589 ? 138.392 135.304 171.560 1.00 34.47 ? 589 SER B CB    1 
ATOM   10286 O  OG    . SER B 1 589 ? 138.212 134.087 172.261 1.00 41.70 ? 589 SER B OG    1 
ATOM   10287 N  N     . SER B 1 590 ? 135.362 135.597 169.406 1.00 30.29 ? 590 SER B N     1 
ATOM   10288 C  CA    . SER B 1 590 ? 133.973 136.019 169.421 1.00 24.85 ? 590 SER B CA    1 
ATOM   10289 C  C     . SER B 1 590 ? 133.141 135.075 168.571 1.00 28.38 ? 590 SER B C     1 
ATOM   10290 O  O     . SER B 1 590 ? 133.647 134.439 167.643 1.00 34.13 ? 590 SER B O     1 
ATOM   10291 C  CB    . SER B 1 590 ? 133.826 137.455 168.902 1.00 27.16 ? 590 SER B CB    1 
ATOM   10292 O  OG    . SER B 1 590 ? 133.676 137.473 167.496 1.00 33.16 ? 590 SER B OG    1 
ATOM   10293 N  N     . THR B 1 591 ? 131.857 134.981 168.902 1.00 29.39 ? 591 THR B N     1 
ATOM   10294 C  CA    . THR B 1 591 ? 130.917 134.257 168.062 1.00 27.40 ? 591 THR B CA    1 
ATOM   10295 C  C     . THR B 1 591 ? 130.565 135.102 166.846 1.00 29.66 ? 591 THR B C     1 
ATOM   10296 O  O     . THR B 1 591 ? 130.501 136.332 166.924 1.00 25.49 ? 591 THR B O     1 
ATOM   10297 C  CB    . THR B 1 591 ? 129.655 133.894 168.845 1.00 27.92 ? 591 THR B CB    1 
ATOM   10298 O  OG1   . THR B 1 591 ? 128.901 135.078 169.122 1.00 35.14 ? 591 THR B OG1   1 
ATOM   10299 C  CG2   . THR B 1 591 ? 130.024 133.219 170.153 1.00 25.76 ? 591 THR B CG2   1 
ATOM   10300 N  N     . ALA B 1 592 ? 130.346 134.436 165.717 1.00 26.74 ? 592 ALA B N     1 
ATOM   10301 C  CA    . ALA B 1 592 ? 130.191 135.138 164.451 1.00 26.15 ? 592 ALA B CA    1 
ATOM   10302 C  C     . ALA B 1 592 ? 128.899 135.943 164.427 1.00 25.53 ? 592 ALA B C     1 
ATOM   10303 O  O     . ALA B 1 592 ? 127.806 135.388 164.569 1.00 30.99 ? 592 ALA B O     1 
ATOM   10304 C  CB    . ALA B 1 592 ? 130.212 134.145 163.291 1.00 30.55 ? 592 ALA B CB    1 
ATOM   10305 N  N     . SER B 1 593 ? 129.036 137.253 164.247 1.00 26.98 ? 593 SER B N     1 
ATOM   10306 C  CA    . SER B 1 593 ? 127.913 138.172 164.021 1.00 17.89 ? 593 SER B CA    1 
ATOM   10307 C  C     . SER B 1 593 ? 126.945 138.083 165.203 1.00 16.96 ? 593 SER B C     1 
ATOM   10308 O  O     . SER B 1 593 ? 127.347 137.783 166.334 1.00 29.57 ? 593 SER B O     1 
ATOM   10309 C  CB    . SER B 1 593 ? 127.292 137.870 162.671 1.00 26.95 ? 593 SER B CB    1 
ATOM   10310 O  OG    . SER B 1 593 ? 126.215 138.742 162.394 1.00 23.26 ? 593 SER B OG    1 
ATOM   10311 N  N     . VAL B 1 594 ? 125.662 138.342 164.952 1.00 21.42 ? 594 VAL B N     1 
ATOM   10312 C  CA    . VAL B 1 594 ? 124.624 138.182 165.959 1.00 19.77 ? 594 VAL B CA    1 
ATOM   10313 C  C     . VAL B 1 594 ? 123.973 136.807 165.879 1.00 17.21 ? 594 VAL B C     1 
ATOM   10314 O  O     . VAL B 1 594 ? 123.016 136.532 166.607 1.00 24.45 ? 594 VAL B O     1 
ATOM   10315 C  CB    . VAL B 1 594 ? 123.569 139.294 165.847 1.00 23.72 ? 594 VAL B CB    1 
ATOM   10316 C  CG1   . VAL B 1 594 ? 124.152 140.623 166.300 1.00 16.25 ? 594 VAL B CG1   1 
ATOM   10317 C  CG2   . VAL B 1 594 ? 123.048 139.391 164.425 1.00 22.27 ? 594 VAL B CG2   1 
ATOM   10318 N  N     . MET B 1 595 ? 124.472 135.936 165.006 1.00 24.11 ? 595 MET B N     1 
ATOM   10319 C  CA    . MET B 1 595 ? 123.921 134.601 164.873 1.00 20.62 ? 595 MET B CA    1 
ATOM   10320 C  C     . MET B 1 595 ? 124.293 133.745 166.081 1.00 25.15 ? 595 MET B C     1 
ATOM   10321 O  O     . MET B 1 595 ? 125.327 133.966 166.716 1.00 31.57 ? 595 MET B O     1 
ATOM   10322 C  CB    . MET B 1 595 ? 124.438 133.935 163.600 1.00 23.68 ? 595 MET B CB    1 
ATOM   10323 C  CG    . MET B 1 595 ? 124.038 134.593 162.281 1.00 24.53 ? 595 MET B CG    1 
ATOM   10324 S  SD    . MET B 1 595 ? 122.356 134.275 161.702 1.00 35.05 ? 595 MET B SD    1 
ATOM   10325 C  CE    . MET B 1 595 ? 121.380 135.373 162.722 1.00 19.18 ? 595 MET B CE    1 
ATOM   10326 N  N     . PRO B 1 596 ? 123.465 132.761 166.420 1.00 31.40 ? 596 PRO B N     1 
ATOM   10327 C  CA    . PRO B 1 596 ? 123.866 131.784 167.434 1.00 22.77 ? 596 PRO B CA    1 
ATOM   10328 C  C     . PRO B 1 596 ? 124.899 130.815 166.880 1.00 30.53 ? 596 PRO B C     1 
ATOM   10329 O  O     . PRO B 1 596 ? 125.062 130.656 165.668 1.00 35.98 ? 596 PRO B O     1 
ATOM   10330 C  CB    . PRO B 1 596 ? 122.556 131.073 167.779 1.00 24.71 ? 596 PRO B CB    1 
ATOM   10331 C  CG    . PRO B 1 596 ? 121.737 131.193 166.545 1.00 28.08 ? 596 PRO B CG    1 
ATOM   10332 C  CD    . PRO B 1 596 ? 122.108 132.505 165.908 1.00 31.32 ? 596 PRO B CD    1 
ATOM   10333 N  N     . ILE B 1 597 ? 125.612 130.164 167.799 1.00 29.21 ? 597 ILE B N     1 
ATOM   10334 C  CA    . ILE B 1 597 ? 126.713 129.294 167.410 1.00 30.41 ? 597 ILE B CA    1 
ATOM   10335 C  C     . ILE B 1 597 ? 126.176 128.038 166.739 1.00 37.24 ? 597 ILE B C     1 
ATOM   10336 O  O     . ILE B 1 597 ? 125.156 127.471 167.154 1.00 39.23 ? 597 ILE B O     1 
ATOM   10337 C  CB    . ILE B 1 597 ? 127.583 128.949 168.630 1.00 33.49 ? 597 ILE B CB    1 
ATOM   10338 C  CG1   . ILE B 1 597 ? 126.756 128.237 169.701 1.00 33.99 ? 597 ILE B CG1   1 
ATOM   10339 C  CG2   . ILE B 1 597 ? 128.211 130.204 169.199 1.00 31.56 ? 597 ILE B CG2   1 
ATOM   10340 C  CD1   . ILE B 1 597 ? 127.560 127.308 170.570 1.00 33.73 ? 597 ILE B CD1   1 
ATOM   10341 N  N     . MET B 1 598 ? 126.857 127.607 165.676 1.00 44.02 ? 598 MET B N     1 
ATOM   10342 C  CA    . MET B 1 598 ? 126.476 126.368 165.006 1.00 41.67 ? 598 MET B CA    1 
ATOM   10343 C  C     . MET B 1 598 ? 126.862 125.154 165.841 1.00 39.09 ? 598 MET B C     1 
ATOM   10344 O  O     . MET B 1 598 ? 126.070 124.217 165.999 1.00 45.62 ? 598 MET B O     1 
ATOM   10345 C  CB    . MET B 1 598 ? 127.126 126.301 163.625 1.00 40.29 ? 598 MET B CB    1 
ATOM   10346 C  CG    . MET B 1 598 ? 126.755 127.452 162.711 1.00 39.21 ? 598 MET B CG    1 
ATOM   10347 S  SD    . MET B 1 598 ? 127.160 127.127 160.986 1.00 56.20 ? 598 MET B SD    1 
ATOM   10348 C  CE    . MET B 1 598 ? 128.625 128.139 160.790 1.00 42.02 ? 598 MET B CE    1 
ATOM   10349 N  N     . GLU B 1 599 ? 128.077 125.154 166.384 1.00 41.18 ? 599 GLU B N     1 
ATOM   10350 C  CA    . GLU B 1 599 ? 128.584 124.058 167.196 1.00 41.91 ? 599 GLU B CA    1 
ATOM   10351 C  C     . GLU B 1 599 ? 129.183 124.613 168.478 1.00 40.18 ? 599 GLU B C     1 
ATOM   10352 O  O     . GLU B 1 599 ? 129.707 125.729 168.502 1.00 44.27 ? 599 GLU B O     1 
ATOM   10353 C  CB    . GLU B 1 599 ? 129.647 123.241 166.447 1.00 43.41 ? 599 GLU B CB    1 
ATOM   10354 C  CG    . GLU B 1 599 ? 129.550 123.317 164.935 1.00 42.94 ? 599 GLU B CG    1 
ATOM   10355 C  CD    . GLU B 1 599 ? 130.719 122.650 164.242 1.00 47.80 ? 599 GLU B CD    1 
ATOM   10356 O  OE1   . GLU B 1 599 ? 131.141 121.565 164.695 1.00 48.24 ? 599 GLU B OE1   1 
ATOM   10357 O  OE2   . GLU B 1 599 ? 131.218 123.210 163.243 1.00 46.03 ? 599 GLU B OE2   1 
ATOM   10358 N  N     . ARG B 1 600 ? 129.100 123.825 169.550 1.00 42.05 ? 600 ARG B N     1 
ATOM   10359 C  CA    . ARG B 1 600 ? 129.717 124.234 170.807 1.00 36.82 ? 600 ARG B CA    1 
ATOM   10360 C  C     . ARG B 1 600 ? 131.235 124.194 170.708 1.00 37.53 ? 600 ARG B C     1 
ATOM   10361 O  O     . ARG B 1 600 ? 131.923 125.121 171.151 1.00 40.50 ? 600 ARG B O     1 
ATOM   10362 C  CB    . ARG B 1 600 ? 129.225 123.348 171.948 1.00 38.85 ? 600 ARG B CB    1 
ATOM   10363 C  CG    . ARG B 1 600 ? 127.904 123.793 172.527 1.00 38.71 ? 600 ARG B CG    1 
ATOM   10364 C  CD    . ARG B 1 600 ? 127.612 123.088 173.829 1.00 37.37 ? 600 ARG B CD    1 
ATOM   10365 N  NE    . ARG B 1 600 ? 126.296 123.427 174.353 1.00 36.21 ? 600 ARG B NE    1 
ATOM   10366 C  CZ    . ARG B 1 600 ? 125.168 122.849 173.967 1.00 39.10 ? 600 ARG B CZ    1 
ATOM   10367 N  NH1   . ARG B 1 600 ? 125.157 121.905 173.042 1.00 38.94 ? 600 ARG B NH1   1 
ATOM   10368 N  NH2   . ARG B 1 600 ? 124.022 123.229 174.525 1.00 40.34 ? 600 ARG B NH2   1 
ATOM   10369 N  N     . ILE B 1 601 ? 131.776 123.126 170.131 1.00 47.35 ? 601 ILE B N     1 
ATOM   10370 C  CA    . ILE B 1 601 ? 133.206 122.993 169.888 1.00 43.17 ? 601 ILE B CA    1 
ATOM   10371 C  C     . ILE B 1 601 ? 133.404 122.754 168.400 1.00 44.33 ? 601 ILE B C     1 
ATOM   10372 O  O     . ILE B 1 601 ? 132.799 121.842 167.826 1.00 45.88 ? 601 ILE B O     1 
ATOM   10373 C  CB    . ILE B 1 601 ? 133.825 121.859 170.722 1.00 41.30 ? 601 ILE B CB    1 
ATOM   10374 C  CG1   . ILE B 1 601 ? 133.531 122.083 172.206 1.00 43.06 ? 601 ILE B CG1   1 
ATOM   10375 C  CG2   . ILE B 1 601 ? 135.318 121.787 170.475 1.00 42.28 ? 601 ILE B CG2   1 
ATOM   10376 C  CD1   . ILE B 1 601 ? 133.683 120.852 173.057 1.00 45.28 ? 601 ILE B CD1   1 
ATOM   10377 N  N     . GLU B 1 602 ? 134.248 123.571 167.782 1.00 52.85 ? 602 GLU B N     1 
ATOM   10378 C  CA    . GLU B 1 602 ? 134.421 123.584 166.337 1.00 49.91 ? 602 GLU B CA    1 
ATOM   10379 C  C     . GLU B 1 602 ? 135.559 122.646 165.956 1.00 52.79 ? 602 GLU B C     1 
ATOM   10380 O  O     . GLU B 1 602 ? 136.698 122.834 166.396 1.00 56.02 ? 602 GLU B O     1 
ATOM   10381 C  CB    . GLU B 1 602 ? 134.702 125.005 165.852 1.00 50.42 ? 602 GLU B CB    1 
ATOM   10382 C  CG    . GLU B 1 602 ? 134.377 125.253 164.400 1.00 50.06 ? 602 GLU B CG    1 
ATOM   10383 C  CD    . GLU B 1 602 ? 134.427 126.724 164.044 1.00 55.28 ? 602 GLU B CD    1 
ATOM   10384 O  OE1   . GLU B 1 602 ? 133.630 127.500 164.611 1.00 54.33 ? 602 GLU B OE1   1 
ATOM   10385 O  OE2   . GLU B 1 602 ? 135.264 127.104 163.199 1.00 56.30 ? 602 GLU B OE2   1 
ATOM   10386 N  N     . GLU B 1 603 ? 135.248 121.639 165.144 1.00 55.68 ? 603 GLU B N     1 
ATOM   10387 C  CA    . GLU B 1 603 ? 136.233 120.678 164.666 1.00 55.81 ? 603 GLU B CA    1 
ATOM   10388 C  C     . GLU B 1 603 ? 136.595 121.016 163.225 1.00 57.33 ? 603 GLU B C     1 
ATOM   10389 O  O     . GLU B 1 603 ? 135.748 120.920 162.330 1.00 57.99 ? 603 GLU B O     1 
ATOM   10390 C  CB    . GLU B 1 603 ? 135.692 119.251 164.758 1.00 58.11 ? 603 GLU B CB    1 
ATOM   10391 C  CG    . GLU B 1 603 ? 135.209 118.849 166.143 1.00 59.57 ? 603 GLU B CG    1 
ATOM   10392 C  CD    . GLU B 1 603 ? 133.706 118.988 166.303 1.00 59.70 ? 603 GLU B CD    1 
ATOM   10393 O  OE1   . GLU B 1 603 ? 133.231 119.041 167.457 1.00 58.68 ? 603 GLU B OE1   1 
ATOM   10394 O  OE2   . GLU B 1 603 ? 133.000 119.046 165.274 1.00 54.78 ? 603 GLU B OE2   1 
ATOM   10395 N  N     . ARG B 1 604 ? 137.846 121.411 163.004 1.00 60.11 ? 604 ARG B N     1 
ATOM   10396 C  CA    . ARG B 1 604 ? 138.341 121.745 161.677 1.00 60.74 ? 604 ARG B CA    1 
ATOM   10397 C  C     . ARG B 1 604 ? 139.710 121.121 161.455 1.00 61.38 ? 604 ARG B C     1 
ATOM   10398 O  O     . ARG B 1 604 ? 140.456 120.861 162.403 1.00 60.34 ? 604 ARG B O     1 
ATOM   10399 C  CB    . ARG B 1 604 ? 138.423 123.263 161.461 1.00 60.60 ? 604 ARG B CB    1 
ATOM   10400 C  CG    . ARG B 1 604 ? 137.122 124.001 161.702 1.00 60.46 ? 604 ARG B CG    1 
ATOM   10401 C  CD    . ARG B 1 604 ? 136.282 124.021 160.430 1.00 59.83 ? 604 ARG B CD    1 
ATOM   10402 N  NE    . ARG B 1 604 ? 134.945 124.563 160.639 1.00 59.90 ? 604 ARG B NE    1 
ATOM   10403 C  CZ    . ARG B 1 604 ? 133.986 123.960 161.329 1.00 61.05 ? 604 ARG B CZ    1 
ATOM   10404 N  NH1   . ARG B 1 604 ? 134.166 122.765 161.867 1.00 60.04 ? 604 ARG B NH1   1 
ATOM   10405 N  NH2   . ARG B 1 604 ? 132.813 124.568 161.477 1.00 61.47 ? 604 ARG B NH2   1 
ATOM   10406 N  N     . THR B 1 605 ? 140.028 120.884 160.187 1.00 67.83 ? 605 THR B N     1 
ATOM   10407 C  CA    . THR B 1 605 ? 141.296 120.295 159.779 1.00 67.95 ? 605 THR B CA    1 
ATOM   10408 C  C     . THR B 1 605 ? 142.083 121.324 158.979 1.00 68.05 ? 605 THR B C     1 
ATOM   10409 O  O     . THR B 1 605 ? 141.588 121.844 157.973 1.00 67.69 ? 605 THR B O     1 
ATOM   10410 C  CB    . THR B 1 605 ? 141.073 119.032 158.947 1.00 67.72 ? 605 THR B CB    1 
ATOM   10411 O  OG1   . THR B 1 605 ? 140.405 118.044 159.741 1.00 67.51 ? 605 THR B OG1   1 
ATOM   10412 C  CG2   . THR B 1 605 ? 142.401 118.474 158.461 1.00 68.23 ? 605 THR B CG2   1 
ATOM   10413 N  N     . TYR B 1 606 ? 143.301 121.615 159.426 1.00 70.15 ? 606 TYR B N     1 
ATOM   10414 C  CA    . TYR B 1 606 ? 144.203 122.522 158.728 1.00 71.39 ? 606 TYR B CA    1 
ATOM   10415 C  C     . TYR B 1 606 ? 145.452 121.745 158.344 1.00 72.76 ? 606 TYR B C     1 
ATOM   10416 O  O     . TYR B 1 606 ? 146.120 121.170 159.210 1.00 71.23 ? 606 TYR B O     1 
ATOM   10417 C  CB    . TYR B 1 606 ? 144.550 123.731 159.597 1.00 70.11 ? 606 TYR B CB    1 
ATOM   10418 C  CG    . TYR B 1 606 ? 143.356 124.603 159.902 1.00 70.47 ? 606 TYR B CG    1 
ATOM   10419 C  CD1   . TYR B 1 606 ? 142.891 125.525 158.974 1.00 68.44 ? 606 TYR B CD1   1 
ATOM   10420 C  CD2   . TYR B 1 606 ? 142.686 124.498 161.113 1.00 70.35 ? 606 TYR B CD2   1 
ATOM   10421 C  CE1   . TYR B 1 606 ? 141.795 126.320 159.246 1.00 69.46 ? 606 TYR B CE1   1 
ATOM   10422 C  CE2   . TYR B 1 606 ? 141.591 125.288 161.394 1.00 68.64 ? 606 TYR B CE2   1 
ATOM   10423 C  CZ    . TYR B 1 606 ? 141.150 126.198 160.458 1.00 71.30 ? 606 TYR B CZ    1 
ATOM   10424 O  OH    . TYR B 1 606 ? 140.058 126.986 160.736 1.00 72.12 ? 606 TYR B OH    1 
ATOM   10425 N  N     . GLY B 1 607 ? 145.769 121.737 157.053 1.00 80.17 ? 607 GLY B N     1 
ATOM   10426 C  CA    . GLY B 1 607 ? 146.826 120.862 156.576 1.00 79.65 ? 607 GLY B CA    1 
ATOM   10427 C  C     . GLY B 1 607 ? 146.434 119.414 156.789 1.00 79.80 ? 607 GLY B C     1 
ATOM   10428 O  O     . GLY B 1 607 ? 145.327 118.989 156.443 1.00 79.51 ? 607 GLY B O     1 
ATOM   10429 N  N     . ASN B 1 608 ? 147.349 118.639 157.368 1.00 82.25 ? 608 ASN B N     1 
ATOM   10430 C  CA    . ASN B 1 608 ? 147.093 117.243 157.693 1.00 83.33 ? 608 ASN B CA    1 
ATOM   10431 C  C     . ASN B 1 608 ? 146.737 117.044 159.161 1.00 84.03 ? 608 ASN B C     1 
ATOM   10432 O  O     . ASN B 1 608 ? 146.551 115.903 159.595 1.00 83.19 ? 608 ASN B O     1 
ATOM   10433 C  CB    . ASN B 1 608 ? 148.304 116.384 157.323 1.00 84.17 ? 608 ASN B CB    1 
ATOM   10434 C  CG    . ASN B 1 608 ? 148.600 116.406 155.835 1.00 84.59 ? 608 ASN B CG    1 
ATOM   10435 O  OD1   . ASN B 1 608 ? 147.794 116.882 155.037 1.00 83.05 ? 608 ASN B OD1   1 
ATOM   10436 N  ND2   . ASN B 1 608 ? 149.762 115.885 155.455 1.00 83.52 ? 608 ASN B ND2   1 
ATOM   10437 N  N     . SER B 1 609 ? 146.633 118.123 159.931 1.00 76.47 ? 609 SER B N     1 
ATOM   10438 C  CA    . SER B 1 609 ? 146.341 118.056 161.355 1.00 75.81 ? 609 SER B CA    1 
ATOM   10439 C  C     . SER B 1 609 ? 144.967 118.648 161.636 1.00 74.14 ? 609 SER B C     1 
ATOM   10440 O  O     . SER B 1 609 ? 144.611 119.701 161.097 1.00 73.89 ? 609 SER B O     1 
ATOM   10441 C  CB    . SER B 1 609 ? 147.406 118.798 162.168 1.00 73.63 ? 609 SER B CB    1 
ATOM   10442 O  OG    . SER B 1 609 ? 147.414 120.179 161.853 1.00 73.45 ? 609 SER B OG    1 
ATOM   10443 N  N     . LYS B 1 610 ? 144.199 117.964 162.479 1.00 64.25 ? 610 LYS B N     1 
ATOM   10444 C  CA    . LYS B 1 610 ? 142.866 118.413 162.852 1.00 63.76 ? 610 LYS B CA    1 
ATOM   10445 C  C     . LYS B 1 610 ? 142.924 119.268 164.112 1.00 63.24 ? 610 LYS B C     1 
ATOM   10446 O  O     . LYS B 1 610 ? 143.721 119.013 165.020 1.00 63.63 ? 610 LYS B O     1 
ATOM   10447 C  CB    . LYS B 1 610 ? 141.934 117.211 163.041 1.00 63.94 ? 610 LYS B CB    1 
ATOM   10448 C  CG    . LYS B 1 610 ? 141.848 116.660 164.453 1.00 62.80 ? 610 LYS B CG    1 
ATOM   10449 C  CD    . LYS B 1 610 ? 141.285 115.247 164.440 1.00 64.24 ? 610 LYS B CD    1 
ATOM   10450 C  CE    . LYS B 1 610 ? 141.920 114.378 165.516 1.00 64.34 ? 610 LYS B CE    1 
ATOM   10451 N  NZ    . LYS B 1 610 ? 141.460 114.720 166.886 1.00 63.33 ? 610 LYS B NZ    1 
ATOM   10452 N  N     . THR B 1 611 ? 142.089 120.304 164.146 1.00 62.49 ? 611 THR B N     1 
ATOM   10453 C  CA    . THR B 1 611 ? 142.093 121.289 165.216 1.00 60.99 ? 611 THR B CA    1 
ATOM   10454 C  C     . THR B 1 611 ? 140.716 121.373 165.859 1.00 57.73 ? 611 THR B C     1 
ATOM   10455 O  O     . THR B 1 611 ? 139.696 121.098 165.220 1.00 60.01 ? 611 THR B O     1 
ATOM   10456 C  CB    . THR B 1 611 ? 142.502 122.673 164.699 1.00 60.32 ? 611 THR B CB    1 
ATOM   10457 O  OG1   . THR B 1 611 ? 143.827 122.612 164.160 1.00 60.09 ? 611 THR B OG1   1 
ATOM   10458 C  CG2   . THR B 1 611 ? 142.478 123.680 165.828 1.00 59.97 ? 611 THR B CG2   1 
ATOM   10459 N  N     . TYR B 1 612 ? 140.697 121.759 167.132 1.00 52.67 ? 612 TYR B N     1 
ATOM   10460 C  CA    . TYR B 1 612 ? 139.472 121.875 167.910 1.00 53.14 ? 612 TYR B CA    1 
ATOM   10461 C  C     . TYR B 1 612 ? 139.353 123.293 168.445 1.00 54.22 ? 612 TYR B C     1 
ATOM   10462 O  O     . TYR B 1 612 ? 140.297 123.816 169.046 1.00 53.80 ? 612 TYR B O     1 
ATOM   10463 C  CB    . TYR B 1 612 ? 139.467 120.866 169.056 1.00 54.34 ? 612 TYR B CB    1 
ATOM   10464 C  CG    . TYR B 1 612 ? 139.417 119.440 168.576 1.00 56.62 ? 612 TYR B CG    1 
ATOM   10465 C  CD1   . TYR B 1 612 ? 138.355 118.983 167.808 1.00 55.32 ? 612 TYR B CD1   1 
ATOM   10466 C  CD2   . TYR B 1 612 ? 140.450 118.560 168.855 1.00 56.48 ? 612 TYR B CD2   1 
ATOM   10467 C  CE1   . TYR B 1 612 ? 138.311 117.682 167.356 1.00 54.90 ? 612 TYR B CE1   1 
ATOM   10468 C  CE2   . TYR B 1 612 ? 140.417 117.259 168.406 1.00 58.59 ? 612 TYR B CE2   1 
ATOM   10469 C  CZ    . TYR B 1 612 ? 139.345 116.824 167.658 1.00 58.64 ? 612 TYR B CZ    1 
ATOM   10470 O  OH    . TYR B 1 612 ? 139.309 115.525 167.209 1.00 59.40 ? 612 TYR B OH    1 
ATOM   10471 N  N     . TYR B 1 613 ? 138.195 123.910 168.229 1.00 48.71 ? 613 TYR B N     1 
ATOM   10472 C  CA    . TYR B 1 613 ? 137.946 125.285 168.658 1.00 44.14 ? 613 TYR B CA    1 
ATOM   10473 C  C     . TYR B 1 613 ? 136.670 125.353 169.483 1.00 42.57 ? 613 TYR B C     1 
ATOM   10474 O  O     . TYR B 1 613 ? 135.566 125.437 168.918 1.00 43.05 ? 613 TYR B O     1 
ATOM   10475 C  CB    . TYR B 1 613 ? 137.860 126.226 167.463 1.00 42.28 ? 613 TYR B CB    1 
ATOM   10476 C  CG    . TYR B 1 613 ? 137.554 127.656 167.841 1.00 42.70 ? 613 TYR B CG    1 
ATOM   10477 C  CD1   . TYR B 1 613 ? 138.303 128.315 168.805 1.00 41.90 ? 613 TYR B CD1   1 
ATOM   10478 C  CD2   . TYR B 1 613 ? 136.516 128.347 167.233 1.00 44.24 ? 613 TYR B CD2   1 
ATOM   10479 C  CE1   . TYR B 1 613 ? 138.028 129.620 169.152 1.00 43.23 ? 613 TYR B CE1   1 
ATOM   10480 C  CE2   . TYR B 1 613 ? 136.233 129.653 167.575 1.00 44.00 ? 613 TYR B CE2   1 
ATOM   10481 C  CZ    . TYR B 1 613 ? 136.992 130.285 168.534 1.00 45.95 ? 613 TYR B CZ    1 
ATOM   10482 O  OH    . TYR B 1 613 ? 136.712 131.586 168.874 1.00 44.80 ? 613 TYR B OH    1 
ATOM   10483 N  N     . PRO B 1 614 ? 136.771 125.315 170.808 1.00 39.53 ? 614 PRO B N     1 
ATOM   10484 C  CA    . PRO B 1 614 ? 135.596 125.590 171.636 1.00 41.54 ? 614 PRO B CA    1 
ATOM   10485 C  C     . PRO B 1 614 ? 135.145 127.029 171.456 1.00 41.21 ? 614 PRO B C     1 
ATOM   10486 O  O     . PRO B 1 614 ? 135.947 127.927 171.190 1.00 41.32 ? 614 PRO B O     1 
ATOM   10487 C  CB    . PRO B 1 614 ? 136.091 125.336 173.066 1.00 38.76 ? 614 PRO B CB    1 
ATOM   10488 C  CG    . PRO B 1 614 ? 137.406 124.632 172.920 1.00 41.55 ? 614 PRO B CG    1 
ATOM   10489 C  CD    . PRO B 1 614 ? 137.974 125.075 171.617 1.00 40.39 ? 614 PRO B CD    1 
ATOM   10490 N  N     . MET B 1 615 ? 133.843 127.242 171.597 1.00 40.14 ? 615 MET B N     1 
ATOM   10491 C  CA    . MET B 1 615 ? 133.314 128.589 171.467 1.00 39.63 ? 615 MET B CA    1 
ATOM   10492 C  C     . MET B 1 615 ? 133.867 129.471 172.583 1.00 43.41 ? 615 MET B C     1 
ATOM   10493 O  O     . MET B 1 615 ? 134.103 128.989 173.696 1.00 42.10 ? 615 MET B O     1 
ATOM   10494 C  CB    . MET B 1 615 ? 131.786 128.576 171.492 1.00 38.21 ? 615 MET B CB    1 
ATOM   10495 C  CG    . MET B 1 615 ? 131.178 128.193 170.154 1.00 40.39 ? 615 MET B CG    1 
ATOM   10496 S  SD    . MET B 1 615 ? 132.252 128.679 168.789 1.00 49.48 ? 615 MET B SD    1 
ATOM   10497 C  CE    . MET B 1 615 ? 131.276 128.191 167.372 1.00 41.03 ? 615 MET B CE    1 
ATOM   10498 N  N     . PRO B 1 616 ? 134.108 130.754 172.316 1.00 43.87 ? 616 PRO B N     1 
ATOM   10499 C  CA    . PRO B 1 616 ? 134.785 131.603 173.305 1.00 38.78 ? 616 PRO B CA    1 
ATOM   10500 C  C     . PRO B 1 616 ? 133.990 131.704 174.597 1.00 40.12 ? 616 PRO B C     1 
ATOM   10501 O  O     . PRO B 1 616 ? 132.809 132.055 174.596 1.00 40.82 ? 616 PRO B O     1 
ATOM   10502 C  CB    . PRO B 1 616 ? 134.885 132.957 172.597 1.00 35.41 ? 616 PRO B CB    1 
ATOM   10503 C  CG    . PRO B 1 616 ? 134.718 132.646 171.146 1.00 39.61 ? 616 PRO B CG    1 
ATOM   10504 C  CD    . PRO B 1 616 ? 133.799 131.483 171.077 1.00 39.15 ? 616 PRO B CD    1 
ATOM   10505 N  N     . GLY B 1 617 ? 134.657 131.402 175.708 1.00 39.67 ? 617 GLY B N     1 
ATOM   10506 C  CA    . GLY B 1 617 ? 134.020 131.404 177.004 1.00 36.49 ? 617 GLY B CA    1 
ATOM   10507 C  C     . GLY B 1 617 ? 133.283 130.134 177.360 1.00 40.37 ? 617 GLY B C     1 
ATOM   10508 O  O     . GLY B 1 617 ? 132.638 130.090 178.415 1.00 43.44 ? 617 GLY B O     1 
ATOM   10509 N  N     . LEU B 1 618 ? 133.350 129.104 176.519 1.00 43.05 ? 618 LEU B N     1 
ATOM   10510 C  CA    . LEU B 1 618 ? 132.685 127.846 176.822 1.00 39.24 ? 618 LEU B CA    1 
ATOM   10511 C  C     . LEU B 1 618 ? 133.334 127.175 178.024 1.00 40.59 ? 618 LEU B C     1 
ATOM   10512 O  O     . LEU B 1 618 ? 134.561 127.116 178.138 1.00 43.84 ? 618 LEU B O     1 
ATOM   10513 C  CB    . LEU B 1 618 ? 132.731 126.913 175.613 1.00 38.44 ? 618 LEU B CB    1 
ATOM   10514 C  CG    . LEU B 1 618 ? 131.989 125.580 175.728 1.00 39.63 ? 618 LEU B CG    1 
ATOM   10515 C  CD1   . LEU B 1 618 ? 130.509 125.809 175.962 1.00 40.71 ? 618 LEU B CD1   1 
ATOM   10516 C  CD2   . LEU B 1 618 ? 132.210 124.742 174.484 1.00 40.77 ? 618 LEU B CD2   1 
ATOM   10517 N  N     . ALA B 1 619 ? 132.498 126.671 178.924 1.00 47.62 ? 619 ALA B N     1 
ATOM   10518 C  CA    . ALA B 1 619 ? 132.958 125.990 180.124 1.00 47.29 ? 619 ALA B CA    1 
ATOM   10519 C  C     . ALA B 1 619 ? 131.862 125.031 180.570 1.00 49.69 ? 619 ALA B C     1 
ATOM   10520 O  O     . ALA B 1 619 ? 130.903 124.773 179.836 1.00 52.56 ? 619 ALA B O     1 
ATOM   10521 C  CB    . ALA B 1 619 ? 133.328 127.002 181.215 1.00 46.44 ? 619 ALA B CB    1 
ATOM   10522 N  N     . SER B 1 620 ? 132.007 124.492 181.780 1.00 55.56 ? 620 SER B N     1 
ATOM   10523 C  CA    . SER B 1 620 ? 130.985 123.603 182.319 1.00 54.57 ? 620 SER B CA    1 
ATOM   10524 C  C     . SER B 1 620 ? 129.769 124.380 182.809 1.00 54.69 ? 620 SER B C     1 
ATOM   10525 O  O     . SER B 1 620 ? 128.634 123.911 182.671 1.00 56.64 ? 620 SER B O     1 
ATOM   10526 C  CB    . SER B 1 620 ? 131.571 122.760 183.450 1.00 56.35 ? 620 SER B CB    1 
ATOM   10527 O  OG    . SER B 1 620 ? 132.791 122.160 183.050 1.00 58.06 ? 620 SER B OG    1 
ATOM   10528 N  N     . ASN B 1 621 ? 129.987 125.566 183.382 1.00 51.75 ? 621 ASN B N     1 
ATOM   10529 C  CA    . ASN B 1 621 ? 128.879 126.333 183.943 1.00 52.95 ? 621 ASN B CA    1 
ATOM   10530 C  C     . ASN B 1 621 ? 127.974 126.894 182.852 1.00 54.73 ? 621 ASN B C     1 
ATOM   10531 O  O     . ASN B 1 621 ? 126.749 126.929 183.013 1.00 56.36 ? 621 ASN B O     1 
ATOM   10532 C  CB    . ASN B 1 621 ? 129.418 127.459 184.823 1.00 54.40 ? 621 ASN B CB    1 
ATOM   10533 C  CG    . ASN B 1 621 ? 130.707 128.049 184.289 1.00 57.77 ? 621 ASN B CG    1 
ATOM   10534 O  OD1   . ASN B 1 621 ? 131.695 127.340 184.103 1.00 59.48 ? 621 ASN B OD1   1 
ATOM   10535 N  ND2   . ASN B 1 621 ? 130.704 129.353 184.040 1.00 55.67 ? 621 ASN B ND2   1 
ATOM   10536 N  N     . ASN B 1 622 ? 128.554 127.339 181.737 1.00 47.45 ? 622 ASN B N     1 
ATOM   10537 C  CA    . ASN B 1 622 ? 127.794 127.943 180.650 1.00 46.15 ? 622 ASN B CA    1 
ATOM   10538 C  C     . ASN B 1 622 ? 127.676 127.022 179.440 1.00 46.89 ? 622 ASN B C     1 
ATOM   10539 O  O     . ASN B 1 622 ? 127.474 127.500 178.320 1.00 51.81 ? 622 ASN B O     1 
ATOM   10540 C  CB    . ASN B 1 622 ? 128.412 129.285 180.248 1.00 46.49 ? 622 ASN B CB    1 
ATOM   10541 C  CG    . ASN B 1 622 ? 129.842 129.156 179.741 1.00 46.77 ? 622 ASN B CG    1 
ATOM   10542 O  OD1   . ASN B 1 622 ? 130.320 128.064 179.439 1.00 50.47 ? 622 ASN B OD1   1 
ATOM   10543 N  ND2   . ASN B 1 622 ? 130.533 130.285 179.648 1.00 43.78 ? 622 ASN B ND2   1 
ATOM   10544 N  N     . TRP B 1 623 ? 127.809 125.710 179.645 1.00 40.70 ? 623 TRP B N     1 
ATOM   10545 C  CA    . TRP B 1 623 ? 127.758 124.777 178.524 1.00 40.15 ? 623 TRP B CA    1 
ATOM   10546 C  C     . TRP B 1 623 ? 126.397 124.798 177.841 1.00 41.21 ? 623 TRP B C     1 
ATOM   10547 O  O     . TRP B 1 623 ? 126.314 124.801 176.607 1.00 41.29 ? 623 TRP B O     1 
ATOM   10548 C  CB    . TRP B 1 623 ? 128.096 123.366 179.003 1.00 44.48 ? 623 TRP B CB    1 
ATOM   10549 C  CG    . TRP B 1 623 ? 127.888 122.308 177.963 1.00 42.92 ? 623 TRP B CG    1 
ATOM   10550 C  CD1   . TRP B 1 623 ? 126.744 121.606 177.725 1.00 40.36 ? 623 TRP B CD1   1 
ATOM   10551 C  CD2   . TRP B 1 623 ? 128.855 121.830 177.021 1.00 41.37 ? 623 TRP B CD2   1 
ATOM   10552 N  NE1   . TRP B 1 623 ? 126.937 120.723 176.692 1.00 41.77 ? 623 TRP B NE1   1 
ATOM   10553 C  CE2   . TRP B 1 623 ? 128.226 120.839 176.244 1.00 39.72 ? 623 TRP B CE2   1 
ATOM   10554 C  CE3   . TRP B 1 623 ? 130.192 122.142 176.760 1.00 39.70 ? 623 TRP B CE3   1 
ATOM   10555 C  CZ2   . TRP B 1 623 ? 128.886 120.160 175.223 1.00 38.28 ? 623 TRP B CZ2   1 
ATOM   10556 C  CZ3   . TRP B 1 623 ? 130.845 121.468 175.746 1.00 42.45 ? 623 TRP B CZ3   1 
ATOM   10557 C  CH2   . TRP B 1 623 ? 130.192 120.490 174.990 1.00 41.42 ? 623 TRP B CH2   1 
ATOM   10558 N  N     . PHE B 1 624 ? 125.319 124.812 178.622 1.00 46.15 ? 624 PHE B N     1 
ATOM   10559 C  CA    . PHE B 1 624 ? 123.980 124.737 178.058 1.00 44.44 ? 624 PHE B CA    1 
ATOM   10560 C  C     . PHE B 1 624 ? 123.418 126.094 177.658 1.00 44.27 ? 624 PHE B C     1 
ATOM   10561 O  O     . PHE B 1 624 ? 122.382 126.142 176.986 1.00 50.27 ? 624 PHE B O     1 
ATOM   10562 C  CB    . PHE B 1 624 ? 123.032 124.048 179.043 1.00 47.92 ? 624 PHE B CB    1 
ATOM   10563 C  CG    . PHE B 1 624 ? 123.217 122.560 179.109 1.00 48.82 ? 624 PHE B CG    1 
ATOM   10564 C  CD1   . PHE B 1 624 ? 122.833 121.755 178.050 1.00 43.66 ? 624 PHE B CD1   1 
ATOM   10565 C  CD2   . PHE B 1 624 ? 123.790 121.967 180.222 1.00 47.11 ? 624 PHE B CD2   1 
ATOM   10566 C  CE1   . PHE B 1 624 ? 123.008 120.387 178.102 1.00 44.17 ? 624 PHE B CE1   1 
ATOM   10567 C  CE2   . PHE B 1 624 ? 123.968 120.599 180.281 1.00 47.93 ? 624 PHE B CE2   1 
ATOM   10568 C  CZ    . PHE B 1 624 ? 123.576 119.808 179.219 1.00 47.04 ? 624 PHE B CZ    1 
ATOM   10569 N  N     . PHE B 1 625 ? 124.067 127.191 178.048 1.00 39.20 ? 625 PHE B N     1 
ATOM   10570 C  CA    . PHE B 1 625 ? 123.731 128.485 177.473 1.00 36.41 ? 625 PHE B CA    1 
ATOM   10571 C  C     . PHE B 1 625 ? 124.314 128.656 176.080 1.00 35.29 ? 625 PHE B C     1 
ATOM   10572 O  O     . PHE B 1 625 ? 123.843 129.512 175.325 1.00 40.30 ? 625 PHE B O     1 
ATOM   10573 C  CB    . PHE B 1 625 ? 124.211 129.616 178.382 1.00 33.96 ? 625 PHE B CB    1 
ATOM   10574 C  CG    . PHE B 1 625 ? 123.408 129.763 179.639 1.00 36.15 ? 625 PHE B CG    1 
ATOM   10575 C  CD1   . PHE B 1 625 ? 122.082 130.157 179.583 1.00 37.16 ? 625 PHE B CD1   1 
ATOM   10576 C  CD2   . PHE B 1 625 ? 123.975 129.509 180.875 1.00 38.27 ? 625 PHE B CD2   1 
ATOM   10577 C  CE1   . PHE B 1 625 ? 121.338 130.295 180.737 1.00 38.73 ? 625 PHE B CE1   1 
ATOM   10578 C  CE2   . PHE B 1 625 ? 123.235 129.646 182.032 1.00 37.64 ? 625 PHE B CE2   1 
ATOM   10579 C  CZ    . PHE B 1 625 ? 121.915 130.040 181.963 1.00 39.75 ? 625 PHE B CZ    1 
ATOM   10580 N  N     . TYR B 1 626 ? 125.320 127.862 175.727 1.00 30.38 ? 626 TYR B N     1 
ATOM   10581 C  CA    . TYR B 1 626 ? 125.861 127.842 174.371 1.00 33.46 ? 626 TYR B CA    1 
ATOM   10582 C  C     . TYR B 1 626 ? 125.093 126.861 173.495 1.00 32.07 ? 626 TYR B C     1 
ATOM   10583 O  O     . TYR B 1 626 ? 125.666 125.993 172.843 1.00 35.66 ? 626 TYR B O     1 
ATOM   10584 C  CB    . TYR B 1 626 ? 127.344 127.495 174.408 1.00 31.64 ? 626 TYR B CB    1 
ATOM   10585 C  CG    . TYR B 1 626 ? 128.244 128.695 174.555 1.00 34.23 ? 626 TYR B CG    1 
ATOM   10586 C  CD1   . TYR B 1 626 ? 128.504 129.528 173.477 1.00 35.19 ? 626 TYR B CD1   1 
ATOM   10587 C  CD2   . TYR B 1 626 ? 128.834 128.997 175.774 1.00 34.53 ? 626 TYR B CD2   1 
ATOM   10588 C  CE1   . TYR B 1 626 ? 129.325 130.627 173.608 1.00 33.80 ? 626 TYR B CE1   1 
ATOM   10589 C  CE2   . TYR B 1 626 ? 129.657 130.093 175.915 1.00 31.72 ? 626 TYR B CE2   1 
ATOM   10590 C  CZ    . TYR B 1 626 ? 129.899 130.903 174.830 1.00 31.13 ? 626 TYR B CZ    1 
ATOM   10591 O  OH    . TYR B 1 626 ? 130.716 131.997 174.965 1.00 37.72 ? 626 TYR B OH    1 
ATOM   10592 N  N     . LYS B 1 627 ? 123.771 127.003 173.483 1.00 33.94 ? 627 LYS B N     1 
ATOM   10593 C  CA    . LYS B 1 627 ? 122.925 126.108 172.709 1.00 33.87 ? 627 LYS B CA    1 
ATOM   10594 C  C     . LYS B 1 627 ? 123.236 126.241 171.225 1.00 36.99 ? 627 LYS B C     1 
ATOM   10595 O  O     . LYS B 1 627 ? 123.373 127.351 170.704 1.00 42.21 ? 627 LYS B O     1 
ATOM   10596 C  CB    . LYS B 1 627 ? 121.456 126.424 172.982 1.00 35.78 ? 627 LYS B CB    1 
ATOM   10597 C  CG    . LYS B 1 627 ? 120.466 125.479 172.335 1.00 36.81 ? 627 LYS B CG    1 
ATOM   10598 C  CD    . LYS B 1 627 ? 119.069 125.727 172.876 1.00 33.43 ? 627 LYS B CD    1 
ATOM   10599 C  CE    . LYS B 1 627 ? 118.047 124.830 172.212 1.00 38.26 ? 627 LYS B CE    1 
ATOM   10600 N  NZ    . LYS B 1 627 ? 116.681 125.073 172.748 1.00 40.12 ? 627 LYS B NZ    1 
ATOM   10601 N  N     . GLU B 1 628 ? 123.368 125.105 170.549 1.00 38.56 ? 628 GLU B N     1 
ATOM   10602 C  CA    . GLU B 1 628 ? 123.680 125.124 169.129 1.00 35.69 ? 628 GLU B CA    1 
ATOM   10603 C  C     . GLU B 1 628 ? 122.507 125.680 168.332 1.00 40.00 ? 628 GLU B C     1 
ATOM   10604 O  O     . GLU B 1 628 ? 121.342 125.534 168.711 1.00 44.04 ? 628 GLU B O     1 
ATOM   10605 C  CB    . GLU B 1 628 ? 124.041 123.724 168.639 1.00 39.47 ? 628 GLU B CB    1 
ATOM   10606 C  CG    . GLU B 1 628 ? 125.189 123.087 169.401 1.00 40.45 ? 628 GLU B CG    1 
ATOM   10607 C  CD    . GLU B 1 628 ? 125.921 122.043 168.584 1.00 45.55 ? 628 GLU B CD    1 
ATOM   10608 O  OE1   . GLU B 1 628 ? 125.395 121.641 167.525 1.00 43.18 ? 628 GLU B OE1   1 
ATOM   10609 O  OE2   . GLU B 1 628 ? 127.022 121.625 168.998 1.00 43.44 ? 628 GLU B OE2   1 
ATOM   10610 N  N     . ALA B 1 629 ? 122.833 126.334 167.215 1.00 39.96 ? 629 ALA B N     1 
ATOM   10611 C  CA    . ALA B 1 629 ? 121.814 127.009 166.419 1.00 33.11 ? 629 ALA B CA    1 
ATOM   10612 C  C     . ALA B 1 629 ? 120.787 126.026 165.871 1.00 36.56 ? 629 ALA B C     1 
ATOM   10613 O  O     . ALA B 1 629 ? 119.592 126.336 165.811 1.00 42.39 ? 629 ALA B O     1 
ATOM   10614 C  CB    . ALA B 1 629 ? 122.474 127.785 165.282 1.00 32.36 ? 629 ALA B CB    1 
ATOM   10615 N  N     . TYR B 1 630 ? 121.234 124.838 165.460 1.00 39.91 ? 630 TYR B N     1 
ATOM   10616 C  CA    . TYR B 1 630 ? 120.309 123.853 164.910 1.00 39.07 ? 630 TYR B CA    1 
ATOM   10617 C  C     . TYR B 1 630 ? 119.324 123.353 165.958 1.00 42.23 ? 630 TYR B C     1 
ATOM   10618 O  O     . TYR B 1 630 ? 118.171 123.057 165.628 1.00 46.77 ? 630 TYR B O     1 
ATOM   10619 C  CB    . TYR B 1 630 ? 121.089 122.686 164.308 1.00 37.17 ? 630 TYR B CB    1 
ATOM   10620 C  CG    . TYR B 1 630 ? 122.071 123.109 163.243 1.00 37.65 ? 630 TYR B CG    1 
ATOM   10621 C  CD1   . TYR B 1 630 ? 121.655 123.330 161.939 1.00 38.52 ? 630 TYR B CD1   1 
ATOM   10622 C  CD2   . TYR B 1 630 ? 123.412 123.295 163.543 1.00 38.05 ? 630 TYR B CD2   1 
ATOM   10623 C  CE1   . TYR B 1 630 ? 122.547 123.720 160.961 1.00 38.72 ? 630 TYR B CE1   1 
ATOM   10624 C  CE2   . TYR B 1 630 ? 124.312 123.685 162.572 1.00 39.80 ? 630 TYR B CE2   1 
ATOM   10625 C  CZ    . TYR B 1 630 ? 123.874 123.895 161.283 1.00 44.18 ? 630 TYR B CZ    1 
ATOM   10626 O  OH    . TYR B 1 630 ? 124.765 124.282 160.311 1.00 48.87 ? 630 TYR B OH    1 
ATOM   10627 N  N     . ASP B 1 631 ? 119.752 123.256 167.217 1.00 41.73 ? 631 ASP B N     1 
ATOM   10628 C  CA    . ASP B 1 631 ? 118.851 122.855 168.290 1.00 37.10 ? 631 ASP B CA    1 
ATOM   10629 C  C     . ASP B 1 631 ? 117.858 123.946 168.663 1.00 41.84 ? 631 ASP B C     1 
ATOM   10630 O  O     . ASP B 1 631 ? 116.925 123.674 169.425 1.00 45.89 ? 631 ASP B O     1 
ATOM   10631 C  CB    . ASP B 1 631 ? 119.656 122.453 169.527 1.00 40.68 ? 631 ASP B CB    1 
ATOM   10632 C  CG    . ASP B 1 631 ? 120.631 121.327 169.248 1.00 46.55 ? 631 ASP B CG    1 
ATOM   10633 O  OD1   . ASP B 1 631 ? 120.298 120.437 168.438 1.00 47.22 ? 631 ASP B OD1   1 
ATOM   10634 O  OD2   . ASP B 1 631 ? 121.730 121.331 169.841 1.00 47.72 ? 631 ASP B OD2   1 
ATOM   10635 N  N     . MET B 1 632 ? 118.030 125.157 168.149 1.00 37.00 ? 632 MET B N     1 
ATOM   10636 C  CA    . MET B 1 632 ? 117.208 126.292 168.533 1.00 37.35 ? 632 MET B CA    1 
ATOM   10637 C  C     . MET B 1 632 ? 115.912 126.333 167.732 1.00 36.25 ? 632 MET B C     1 
ATOM   10638 O  O     . MET B 1 632 ? 115.786 125.724 166.667 1.00 35.56 ? 632 MET B O     1 
ATOM   10639 C  CB    . MET B 1 632 ? 117.973 127.599 168.332 1.00 35.67 ? 632 MET B CB    1 
ATOM   10640 C  CG    . MET B 1 632 ? 118.623 128.134 169.584 1.00 35.33 ? 632 MET B CG    1 
ATOM   10641 S  SD    . MET B 1 632 ? 120.017 129.205 169.225 1.00 42.46 ? 632 MET B SD    1 
ATOM   10642 C  CE    . MET B 1 632 ? 120.831 129.228 170.814 1.00 32.83 ? 632 MET B CE    1 
ATOM   10643 N  N     . ASP B 1 633 ? 114.942 127.069 168.266 1.00 35.38 ? 633 ASP B N     1 
ATOM   10644 C  CA    . ASP B 1 633 ? 113.712 127.360 167.544 1.00 32.00 ? 633 ASP B CA    1 
ATOM   10645 C  C     . ASP B 1 633 ? 113.962 128.529 166.601 1.00 34.56 ? 633 ASP B C     1 
ATOM   10646 O  O     . ASP B 1 633 ? 114.270 129.638 167.050 1.00 39.68 ? 633 ASP B O     1 
ATOM   10647 C  CB    . ASP B 1 633 ? 112.583 127.683 168.520 1.00 30.79 ? 633 ASP B CB    1 
ATOM   10648 C  CG    . ASP B 1 633 ? 111.243 127.848 167.830 1.00 37.25 ? 633 ASP B CG    1 
ATOM   10649 O  OD1   . ASP B 1 633 ? 111.139 127.514 166.632 1.00 39.46 ? 633 ASP B OD1   1 
ATOM   10650 O  OD2   . ASP B 1 633 ? 110.291 128.315 168.488 1.00 38.14 ? 633 ASP B OD2   1 
ATOM   10651 N  N     . MET B 1 634 ? 113.839 128.282 165.295 1.00 30.32 ? 634 MET B N     1 
ATOM   10652 C  CA    . MET B 1 634 ? 114.102 129.330 164.317 1.00 25.27 ? 634 MET B CA    1 
ATOM   10653 C  C     . MET B 1 634 ? 113.141 130.502 164.449 1.00 26.07 ? 634 MET B C     1 
ATOM   10654 O  O     . MET B 1 634 ? 113.485 131.615 164.044 1.00 29.39 ? 634 MET B O     1 
ATOM   10655 C  CB    . MET B 1 634 ? 114.043 128.760 162.901 1.00 27.26 ? 634 MET B CB    1 
ATOM   10656 C  CG    . MET B 1 634 ? 115.349 128.148 162.426 1.00 29.32 ? 634 MET B CG    1 
ATOM   10657 S  SD    . MET B 1 634 ? 116.774 129.216 162.720 1.00 40.99 ? 634 MET B SD    1 
ATOM   10658 C  CE    . MET B 1 634 ? 117.592 128.349 164.058 1.00 29.90 ? 634 MET B CE    1 
ATOM   10659 N  N     . PHE B 1 635 ? 111.950 130.281 165.008 1.00 26.14 ? 635 PHE B N     1 
ATOM   10660 C  CA    . PHE B 1 635 ? 111.037 131.393 165.254 1.00 23.01 ? 635 PHE B CA    1 
ATOM   10661 C  C     . PHE B 1 635 ? 111.612 132.358 166.282 1.00 21.48 ? 635 PHE B C     1 
ATOM   10662 O  O     . PHE B 1 635 ? 111.506 133.579 166.128 1.00 25.40 ? 635 PHE B O     1 
ATOM   10663 C  CB    . PHE B 1 635 ? 109.678 130.866 165.711 1.00 26.45 ? 635 PHE B CB    1 
ATOM   10664 C  CG    . PHE B 1 635 ? 108.715 130.624 164.585 1.00 28.69 ? 635 PHE B CG    1 
ATOM   10665 C  CD1   . PHE B 1 635 ? 109.132 129.998 163.423 1.00 25.47 ? 635 PHE B CD1   1 
ATOM   10666 C  CD2   . PHE B 1 635 ? 107.396 131.025 164.687 1.00 24.89 ? 635 PHE B CD2   1 
ATOM   10667 C  CE1   . PHE B 1 635 ? 108.250 129.774 162.385 1.00 23.44 ? 635 PHE B CE1   1 
ATOM   10668 C  CE2   . PHE B 1 635 ? 106.510 130.804 163.652 1.00 27.66 ? 635 PHE B CE2   1 
ATOM   10669 C  CZ    . PHE B 1 635 ? 106.938 130.176 162.500 1.00 25.49 ? 635 PHE B CZ    1 
ATOM   10670 N  N     . LYS B 1 636 ? 112.237 131.830 167.336 1.00 27.21 ? 636 LYS B N     1 
ATOM   10671 C  CA    . LYS B 1 636 ? 112.842 132.695 168.342 1.00 29.34 ? 636 LYS B CA    1 
ATOM   10672 C  C     . LYS B 1 636 ? 114.078 133.405 167.804 1.00 26.84 ? 636 LYS B C     1 
ATOM   10673 O  O     . LYS B 1 636 ? 114.350 134.550 168.183 1.00 34.36 ? 636 LYS B O     1 
ATOM   10674 C  CB    . LYS B 1 636 ? 113.183 131.883 169.588 1.00 29.40 ? 636 LYS B CB    1 
ATOM   10675 C  CG    . LYS B 1 636 ? 111.984 131.192 170.208 1.00 28.60 ? 636 LYS B CG    1 
ATOM   10676 C  CD    . LYS B 1 636 ? 111.500 131.931 171.442 1.00 32.88 ? 636 LYS B CD    1 
ATOM   10677 C  CE    . LYS B 1 636 ? 110.029 131.657 171.708 1.00 31.63 ? 636 LYS B CE    1 
ATOM   10678 N  NZ    . LYS B 1 636 ? 109.258 132.915 171.904 1.00 33.55 ? 636 LYS B NZ    1 
ATOM   10679 N  N     . VAL B 1 637 ? 114.832 132.754 166.919 1.00 24.20 ? 637 VAL B N     1 
ATOM   10680 C  CA    . VAL B 1 637 ? 115.951 133.427 166.267 1.00 19.02 ? 637 VAL B CA    1 
ATOM   10681 C  C     . VAL B 1 637 ? 115.442 134.549 165.371 1.00 26.67 ? 637 VAL B C     1 
ATOM   10682 O  O     . VAL B 1 637 ? 116.040 135.631 165.302 1.00 29.82 ? 637 VAL B O     1 
ATOM   10683 C  CB    . VAL B 1 637 ? 116.803 132.411 165.486 1.00 21.95 ? 637 VAL B CB    1 
ATOM   10684 C  CG1   . VAL B 1 637 ? 117.995 133.098 164.843 1.00 23.13 ? 637 VAL B CG1   1 
ATOM   10685 C  CG2   . VAL B 1 637 ? 117.259 131.291 166.404 1.00 23.14 ? 637 VAL B CG2   1 
ATOM   10686 N  N     . VAL B 1 638 ? 114.329 134.310 164.672 1.00 24.72 ? 638 VAL B N     1 
ATOM   10687 C  CA    . VAL B 1 638 ? 113.697 135.365 163.884 1.00 22.35 ? 638 VAL B CA    1 
ATOM   10688 C  C     . VAL B 1 638 ? 113.282 136.518 164.787 1.00 19.56 ? 638 VAL B C     1 
ATOM   10689 O  O     . VAL B 1 638 ? 113.453 137.691 164.439 1.00 28.38 ? 638 VAL B O     1 
ATOM   10690 C  CB    . VAL B 1 638 ? 112.493 134.806 163.103 1.00 23.18 ? 638 VAL B CB    1 
ATOM   10691 C  CG1   . VAL B 1 638 ? 111.605 135.938 162.617 1.00 15.82 ? 638 VAL B CG1   1 
ATOM   10692 C  CG2   . VAL B 1 638 ? 112.951 133.953 161.937 1.00 22.27 ? 638 VAL B CG2   1 
ATOM   10693 N  N     . ASP B 1 639 ? 112.721 136.200 165.954 1.00 18.28 ? 639 ASP B N     1 
ATOM   10694 C  CA    . ASP B 1 639 ? 112.322 137.238 166.899 1.00 22.43 ? 639 ASP B CA    1 
ATOM   10695 C  C     . ASP B 1 639 ? 113.519 138.065 167.347 1.00 26.56 ? 639 ASP B C     1 
ATOM   10696 O  O     . ASP B 1 639 ? 113.443 139.297 167.420 1.00 32.05 ? 639 ASP B O     1 
ATOM   10697 C  CB    . ASP B 1 639 ? 111.632 136.605 168.106 1.00 24.76 ? 639 ASP B CB    1 
ATOM   10698 C  CG    . ASP B 1 639 ? 110.173 136.301 167.849 1.00 32.95 ? 639 ASP B CG    1 
ATOM   10699 O  OD1   . ASP B 1 639 ? 109.543 137.029 167.054 1.00 30.83 ? 639 ASP B OD1   1 
ATOM   10700 O  OD2   . ASP B 1 639 ? 109.654 135.333 168.442 1.00 35.83 ? 639 ASP B OD2   1 
ATOM   10701 N  N     . MET B 1 640 ? 114.638 137.402 167.643 1.00 25.32 ? 640 MET B N     1 
ATOM   10702 C  CA    . MET B 1 640 ? 115.848 138.114 168.043 1.00 19.31 ? 640 MET B CA    1 
ATOM   10703 C  C     . MET B 1 640 ? 116.351 139.025 166.929 1.00 23.29 ? 640 MET B C     1 
ATOM   10704 O  O     . MET B 1 640 ? 116.675 140.196 167.163 1.00 30.19 ? 640 MET B O     1 
ATOM   10705 C  CB    . MET B 1 640 ? 116.930 137.112 168.443 1.00 22.74 ? 640 MET B CB    1 
ATOM   10706 C  CG    . MET B 1 640 ? 118.333 137.686 168.429 1.00 26.28 ? 640 MET B CG    1 
ATOM   10707 S  SD    . MET B 1 640 ? 118.645 138.736 169.855 1.00 37.40 ? 640 MET B SD    1 
ATOM   10708 C  CE    . MET B 1 640 ? 118.990 137.502 171.098 1.00 25.35 ? 640 MET B CE    1 
ATOM   10709 N  N     . ILE B 1 641 ? 116.422 138.502 165.703 1.00 27.64 ? 641 ILE B N     1 
ATOM   10710 C  CA    . ILE B 1 641 ? 116.955 139.293 164.600 1.00 21.04 ? 641 ILE B CA    1 
ATOM   10711 C  C     . ILE B 1 641 ? 116.031 140.459 164.274 1.00 19.78 ? 641 ILE B C     1 
ATOM   10712 O  O     . ILE B 1 641 ? 116.498 141.548 163.924 1.00 26.37 ? 641 ILE B O     1 
ATOM   10713 C  CB    . ILE B 1 641 ? 117.210 138.399 163.373 1.00 23.56 ? 641 ILE B CB    1 
ATOM   10714 C  CG1   . ILE B 1 641 ? 118.205 137.295 163.728 1.00 19.08 ? 641 ILE B CG1   1 
ATOM   10715 C  CG2   . ILE B 1 641 ? 117.754 139.217 162.214 1.00 17.75 ? 641 ILE B CG2   1 
ATOM   10716 C  CD1   . ILE B 1 641 ? 119.421 137.793 164.479 1.00 21.14 ? 641 ILE B CD1   1 
ATOM   10717 N  N     . ALA B 1 642 ? 114.716 140.263 164.390 1.00 17.51 ? 642 ALA B N     1 
ATOM   10718 C  CA    . ALA B 1 642 ? 113.781 141.361 164.179 1.00 19.55 ? 642 ALA B CA    1 
ATOM   10719 C  C     . ALA B 1 642 ? 113.878 142.395 165.290 1.00 19.72 ? 642 ALA B C     1 
ATOM   10720 O  O     . ALA B 1 642 ? 113.666 143.587 165.045 1.00 24.18 ? 642 ALA B O     1 
ATOM   10721 C  CB    . ALA B 1 642 ? 112.355 140.824 164.074 1.00 17.12 ? 642 ALA B CB    1 
ATOM   10722 N  N     . THR B 1 643 ? 114.178 141.959 166.515 1.00 21.32 ? 643 THR B N     1 
ATOM   10723 C  CA    . THR B 1 643 ? 114.454 142.909 167.586 1.00 18.93 ? 643 THR B CA    1 
ATOM   10724 C  C     . THR B 1 643 ? 115.688 143.742 167.270 1.00 23.05 ? 643 THR B C     1 
ATOM   10725 O  O     . THR B 1 643 ? 115.700 144.958 167.492 1.00 25.40 ? 643 THR B O     1 
ATOM   10726 C  CB    . THR B 1 643 ? 114.634 142.166 168.909 1.00 17.84 ? 643 THR B CB    1 
ATOM   10727 O  OG1   . THR B 1 643 ? 113.463 141.389 169.182 1.00 21.22 ? 643 THR B OG1   1 
ATOM   10728 C  CG2   . THR B 1 643 ? 114.860 143.145 170.042 1.00 18.46 ? 643 THR B CG2   1 
ATOM   10729 N  N     . ILE B 1 644 ? 116.739 143.103 166.757 1.00 22.13 ? 644 ILE B N     1 
ATOM   10730 C  CA    . ILE B 1 644 ? 117.933 143.844 166.361 1.00 12.74 ? 644 ILE B CA    1 
ATOM   10731 C  C     . ILE B 1 644 ? 117.660 144.678 165.115 1.00 16.58 ? 644 ILE B C     1 
ATOM   10732 O  O     . ILE B 1 644 ? 118.122 145.820 165.003 1.00 20.57 ? 644 ILE B O     1 
ATOM   10733 C  CB    . ILE B 1 644 ? 119.113 142.881 166.148 1.00 13.34 ? 644 ILE B CB    1 
ATOM   10734 C  CG1   . ILE B 1 644 ? 119.363 142.050 167.405 1.00 17.14 ? 644 ILE B CG1   1 
ATOM   10735 C  CG2   . ILE B 1 644 ? 120.362 143.651 165.771 1.00 10.01 ? 644 ILE B CG2   1 
ATOM   10736 C  CD1   . ILE B 1 644 ? 120.177 140.808 167.152 1.00 22.29 ? 644 ILE B CD1   1 
ATOM   10737 N  N     . GLN B 1 645 ? 116.905 144.124 164.160 1.00 13.08 ? 645 GLN B N     1 
ATOM   10738 C  CA    . GLN B 1 645 ? 116.714 144.780 162.869 1.00 14.62 ? 645 GLN B CA    1 
ATOM   10739 C  C     . GLN B 1 645 ? 116.031 146.134 163.005 1.00 18.01 ? 645 GLN B C     1 
ATOM   10740 O  O     . GLN B 1 645 ? 116.245 147.022 162.173 1.00 27.03 ? 645 GLN B O     1 
ATOM   10741 C  CB    . GLN B 1 645 ? 115.905 143.876 161.939 1.00 13.56 ? 645 GLN B CB    1 
ATOM   10742 C  CG    . GLN B 1 645 ? 115.747 144.404 160.526 1.00 7.16  ? 645 GLN B CG    1 
ATOM   10743 C  CD    . GLN B 1 645 ? 117.016 144.280 159.716 1.00 18.38 ? 645 GLN B CD    1 
ATOM   10744 O  OE1   . GLN B 1 645 ? 117.827 145.202 159.669 1.00 13.60 ? 645 GLN B OE1   1 
ATOM   10745 N  NE2   . GLN B 1 645 ? 117.197 143.134 159.073 1.00 16.02 ? 645 GLN B NE2   1 
ATOM   10746 N  N     . GLN B 1 646 ? 115.216 146.320 164.043 1.00 19.43 ? 646 GLN B N     1 
ATOM   10747 C  CA    . GLN B 1 646 ? 114.512 147.584 164.206 1.00 14.03 ? 646 GLN B CA    1 
ATOM   10748 C  C     . GLN B 1 646 ? 115.437 148.736 164.577 1.00 13.53 ? 646 GLN B C     1 
ATOM   10749 O  O     . GLN B 1 646 ? 114.999 149.889 164.546 1.00 15.91 ? 646 GLN B O     1 
ATOM   10750 C  CB    . GLN B 1 646 ? 113.411 147.438 165.256 1.00 20.07 ? 646 GLN B CB    1 
ATOM   10751 C  CG    . GLN B 1 646 ? 113.904 147.467 166.682 1.00 21.84 ? 646 GLN B CG    1 
ATOM   10752 C  CD    . GLN B 1 646 ? 112.802 147.182 167.676 1.00 26.19 ? 646 GLN B CD    1 
ATOM   10753 O  OE1   . GLN B 1 646 ? 112.851 146.196 168.410 1.00 25.89 ? 646 GLN B OE1   1 
ATOM   10754 N  NE2   . GLN B 1 646 ? 111.796 148.047 167.707 1.00 22.44 ? 646 GLN B NE2   1 
ATOM   10755 N  N     . HIS B 1 647 ? 116.694 148.460 164.918 1.00 26.75 ? 647 HIS B N     1 
ATOM   10756 C  CA    . HIS B 1 647 ? 117.668 149.503 165.200 1.00 14.13 ? 647 HIS B CA    1 
ATOM   10757 C  C     . HIS B 1 647 ? 118.793 149.554 164.178 1.00 14.58 ? 647 HIS B C     1 
ATOM   10758 O  O     . HIS B 1 647 ? 119.691 150.393 164.309 1.00 25.48 ? 647 HIS B O     1 
ATOM   10759 C  CB    . HIS B 1 647 ? 118.259 149.317 166.604 1.00 9.16  ? 647 HIS B CB    1 
ATOM   10760 C  CG    . HIS B 1 647 ? 117.228 149.152 167.675 1.00 16.69 ? 647 HIS B CG    1 
ATOM   10761 N  ND1   . HIS B 1 647 ? 116.326 150.142 167.997 1.00 17.55 ? 647 HIS B ND1   1 
ATOM   10762 C  CD2   . HIS B 1 647 ? 116.954 148.111 168.495 1.00 14.86 ? 647 HIS B CD2   1 
ATOM   10763 C  CE1   . HIS B 1 647 ? 115.541 149.719 168.970 1.00 20.66 ? 647 HIS B CE1   1 
ATOM   10764 N  NE2   . HIS B 1 647 ? 115.901 148.490 169.291 1.00 16.54 ? 647 HIS B NE2   1 
ATOM   10765 N  N     . ILE B 1 648 ? 118.770 148.690 163.169 1.00 15.69 ? 648 ILE B N     1 
ATOM   10766 C  CA    . ILE B 1 648 ? 119.783 148.649 162.123 1.00 16.84 ? 648 ILE B CA    1 
ATOM   10767 C  C     . ILE B 1 648 ? 119.156 149.211 160.855 1.00 14.75 ? 648 ILE B C     1 
ATOM   10768 O  O     . ILE B 1 648 ? 118.123 148.712 160.395 1.00 25.72 ? 648 ILE B O     1 
ATOM   10769 C  CB    . ILE B 1 648 ? 120.304 147.220 161.904 1.00 11.36 ? 648 ILE B CB    1 
ATOM   10770 C  CG1   . ILE B 1 648 ? 120.879 146.657 163.206 1.00 11.40 ? 648 ILE B CG1   1 
ATOM   10771 C  CG2   . ILE B 1 648 ? 121.347 147.186 160.805 1.00 6.04  ? 648 ILE B CG2   1 
ATOM   10772 C  CD1   . ILE B 1 648 ? 122.032 147.456 163.761 1.00 7.12  ? 648 ILE B CD1   1 
ATOM   10773 N  N     . ASP B 1 649 ? 119.773 150.256 160.295 1.00 7.81  ? 649 ASP B N     1 
ATOM   10774 C  CA    . ASP B 1 649 ? 119.192 150.901 159.121 1.00 9.72  ? 649 ASP B CA    1 
ATOM   10775 C  C     . ASP B 1 649 ? 119.342 150.045 157.871 1.00 11.81 ? 649 ASP B C     1 
ATOM   10776 O  O     . ASP B 1 649 ? 118.454 150.047 157.012 1.00 29.51 ? 649 ASP B O     1 
ATOM   10777 C  CB    . ASP B 1 649 ? 119.816 152.283 158.910 1.00 20.72 ? 649 ASP B CB    1 
ATOM   10778 C  CG    . ASP B 1 649 ? 121.320 152.279 159.068 1.00 16.63 ? 649 ASP B CG    1 
ATOM   10779 O  OD1   . ASP B 1 649 ? 122.026 152.524 158.071 1.00 23.59 ? 649 ASP B OD1   1 
ATOM   10780 O  OD2   . ASP B 1 649 ? 121.796 152.040 160.195 1.00 21.59 ? 649 ASP B OD2   1 
ATOM   10781 N  N     . GLN B 1 650 ? 120.445 149.321 157.744 1.00 12.10 ? 650 GLN B N     1 
ATOM   10782 C  CA    . GLN B 1 650 ? 120.613 148.338 156.684 1.00 4.55  ? 650 GLN B CA    1 
ATOM   10783 C  C     . GLN B 1 650 ? 120.138 146.979 157.199 1.00 7.88  ? 650 GLN B C     1 
ATOM   10784 O  O     . GLN B 1 650 ? 119.451 146.896 158.219 1.00 21.35 ? 650 GLN B O     1 
ATOM   10785 C  CB    . GLN B 1 650 ? 122.064 148.325 156.204 1.00 10.67 ? 650 GLN B CB    1 
ATOM   10786 C  CG    . GLN B 1 650 ? 122.526 149.639 155.618 1.00 10.85 ? 650 GLN B CG    1 
ATOM   10787 C  CD    . GLN B 1 650 ? 123.904 149.544 155.012 1.00 13.77 ? 650 GLN B CD    1 
ATOM   10788 O  OE1   . GLN B 1 650 ? 124.095 148.901 153.983 1.00 15.61 ? 650 GLN B OE1   1 
ATOM   10789 N  NE2   . GLN B 1 650 ? 124.875 150.189 155.644 1.00 8.75  ? 650 GLN B NE2   1 
ATOM   10790 N  N     . GLY B 1 651 ? 120.468 145.903 156.491 1.00 12.98 ? 651 GLY B N     1 
ATOM   10791 C  CA    . GLY B 1 651 ? 120.026 144.581 156.876 1.00 13.19 ? 651 GLY B CA    1 
ATOM   10792 C  C     . GLY B 1 651 ? 121.004 143.858 157.783 1.00 8.85  ? 651 GLY B C     1 
ATOM   10793 O  O     . GLY B 1 651 ? 122.036 144.382 158.199 1.00 11.60 ? 651 GLY B O     1 
ATOM   10794 N  N     . ILE B 1 652 ? 120.645 142.616 158.095 1.00 19.78 ? 652 ILE B N     1 
ATOM   10795 C  CA    . ILE B 1 652 ? 121.442 141.721 158.924 1.00 7.59  ? 652 ILE B CA    1 
ATOM   10796 C  C     . ILE B 1 652 ? 121.578 140.402 158.182 1.00 13.53 ? 652 ILE B C     1 
ATOM   10797 O  O     . ILE B 1 652 ? 120.594 139.890 157.637 1.00 21.91 ? 652 ILE B O     1 
ATOM   10798 C  CB    . ILE B 1 652 ? 120.801 141.495 160.307 1.00 5.26  ? 652 ILE B CB    1 
ATOM   10799 C  CG1   . ILE B 1 652 ? 120.596 142.823 161.035 1.00 5.91  ? 652 ILE B CG1   1 
ATOM   10800 C  CG2   . ILE B 1 652 ? 121.640 140.545 161.142 1.00 8.77  ? 652 ILE B CG2   1 
ATOM   10801 C  CD1   . ILE B 1 652 ? 119.791 142.697 162.298 1.00 9.48  ? 652 ILE B CD1   1 
ATOM   10802 N  N     . SER B 1 653 ? 122.789 139.856 158.152 1.00 14.51 ? 653 SER B N     1 
ATOM   10803 C  CA    . SER B 1 653 ? 123.019 138.554 157.533 1.00 15.10 ? 653 SER B CA    1 
ATOM   10804 C  C     . SER B 1 653 ? 122.365 137.486 158.398 1.00 19.24 ? 653 SER B C     1 
ATOM   10805 O  O     . SER B 1 653 ? 122.911 137.074 159.422 1.00 25.16 ? 653 SER B O     1 
ATOM   10806 C  CB    . SER B 1 653 ? 124.511 138.298 157.366 1.00 17.21 ? 653 SER B CB    1 
ATOM   10807 O  OG    . SER B 1 653 ? 124.932 138.615 156.054 1.00 21.78 ? 653 SER B OG    1 
ATOM   10808 N  N     . PHE B 1 654 ? 121.185 137.035 157.984 1.00 20.42 ? 654 PHE B N     1 
ATOM   10809 C  CA    . PHE B 1 654 ? 120.361 136.121 158.765 1.00 10.79 ? 654 PHE B CA    1 
ATOM   10810 C  C     . PHE B 1 654 ? 120.433 134.737 158.132 1.00 19.48 ? 654 PHE B C     1 
ATOM   10811 O  O     . PHE B 1 654 ? 119.797 134.483 157.105 1.00 25.40 ? 654 PHE B O     1 
ATOM   10812 C  CB    . PHE B 1 654 ? 118.921 136.625 158.831 1.00 15.01 ? 654 PHE B CB    1 
ATOM   10813 C  CG    . PHE B 1 654 ? 118.038 135.840 159.757 1.00 17.01 ? 654 PHE B CG    1 
ATOM   10814 C  CD1   . PHE B 1 654 ? 118.575 134.964 160.684 1.00 21.22 ? 654 PHE B CD1   1 
ATOM   10815 C  CD2   . PHE B 1 654 ? 116.666 135.984 159.702 1.00 19.56 ? 654 PHE B CD2   1 
ATOM   10816 C  CE1   . PHE B 1 654 ? 117.763 134.246 161.529 1.00 18.97 ? 654 PHE B CE1   1 
ATOM   10817 C  CE2   . PHE B 1 654 ? 115.850 135.269 160.549 1.00 23.70 ? 654 PHE B CE2   1 
ATOM   10818 C  CZ    . PHE B 1 654 ? 116.400 134.399 161.464 1.00 17.55 ? 654 PHE B CZ    1 
ATOM   10819 N  N     . THR B 1 655 ? 121.191 133.844 158.760 1.00 21.94 ? 655 THR B N     1 
ATOM   10820 C  CA    . THR B 1 655 ? 121.316 132.469 158.303 1.00 20.02 ? 655 THR B CA    1 
ATOM   10821 C  C     . THR B 1 655 ? 120.285 131.600 159.009 1.00 21.65 ? 655 THR B C     1 
ATOM   10822 O  O     . THR B 1 655 ? 120.155 131.651 160.236 1.00 27.36 ? 655 THR B O     1 
ATOM   10823 C  CB    . THR B 1 655 ? 122.725 131.938 158.572 1.00 27.37 ? 655 THR B CB    1 
ATOM   10824 O  OG1   . THR B 1 655 ? 123.674 132.687 157.804 1.00 31.45 ? 655 THR B OG1   1 
ATOM   10825 C  CG2   . THR B 1 655 ? 122.826 130.469 158.194 1.00 28.96 ? 655 THR B CG2   1 
ATOM   10826 N  N     . LEU B 1 656 ? 119.547 130.814 158.232 1.00 31.51 ? 656 LEU B N     1 
ATOM   10827 C  CA    . LEU B 1 656 ? 118.618 129.838 158.783 1.00 31.48 ? 656 LEU B CA    1 
ATOM   10828 C  C     . LEU B 1 656 ? 119.365 128.544 159.063 1.00 27.82 ? 656 LEU B C     1 
ATOM   10829 O  O     . LEU B 1 656 ? 120.010 127.986 158.171 1.00 32.43 ? 656 LEU B O     1 
ATOM   10830 C  CB    . LEU B 1 656 ? 117.460 129.578 157.819 1.00 33.15 ? 656 LEU B CB    1 
ATOM   10831 C  CG    . LEU B 1 656 ? 116.556 130.764 157.495 1.00 31.96 ? 656 LEU B CG    1 
ATOM   10832 C  CD1   . LEU B 1 656 ? 115.307 130.293 156.768 1.00 29.81 ? 656 LEU B CD1   1 
ATOM   10833 C  CD2   . LEU B 1 656 ? 116.196 131.530 158.758 1.00 25.09 ? 656 LEU B CD2   1 
ATOM   10834 N  N     . PHE B 1 657 ? 119.285 128.077 160.301 1.00 29.30 ? 657 PHE B N     1 
ATOM   10835 C  CA    . PHE B 1 657 ? 119.931 126.841 160.725 1.00 29.22 ? 657 PHE B CA    1 
ATOM   10836 C  C     . PHE B 1 657 ? 118.845 125.785 160.867 1.00 35.14 ? 657 PHE B C     1 
ATOM   10837 O  O     . PHE B 1 657 ? 118.015 125.860 161.779 1.00 36.94 ? 657 PHE B O     1 
ATOM   10838 C  CB    . PHE B 1 657 ? 120.693 127.047 162.029 1.00 32.64 ? 657 PHE B CB    1 
ATOM   10839 C  CG    . PHE B 1 657 ? 121.671 128.181 161.978 1.00 36.27 ? 657 PHE B CG    1 
ATOM   10840 C  CD1   . PHE B 1 657 ? 122.948 127.987 161.481 1.00 32.10 ? 657 PHE B CD1   1 
ATOM   10841 C  CD2   . PHE B 1 657 ? 121.312 129.445 162.414 1.00 34.08 ? 657 PHE B CD2   1 
ATOM   10842 C  CE1   . PHE B 1 657 ? 123.850 129.028 161.429 1.00 34.42 ? 657 PHE B CE1   1 
ATOM   10843 C  CE2   . PHE B 1 657 ? 122.211 130.490 162.363 1.00 33.64 ? 657 PHE B CE2   1 
ATOM   10844 C  CZ    . PHE B 1 657 ? 123.482 130.281 161.870 1.00 37.09 ? 657 PHE B CZ    1 
ATOM   10845 N  N     . LEU B 1 658 ? 118.853 124.807 159.969 1.00 40.01 ? 658 LEU B N     1 
ATOM   10846 C  CA    . LEU B 1 658 ? 117.754 123.867 159.834 1.00 40.56 ? 658 LEU B CA    1 
ATOM   10847 C  C     . LEU B 1 658 ? 118.217 122.463 160.191 1.00 43.92 ? 658 LEU B C     1 
ATOM   10848 O  O     . LEU B 1 658 ? 119.390 122.117 160.027 1.00 45.48 ? 658 LEU B O     1 
ATOM   10849 C  CB    . LEU B 1 658 ? 117.202 123.869 158.406 1.00 39.96 ? 658 LEU B CB    1 
ATOM   10850 C  CG    . LEU B 1 658 ? 117.082 125.227 157.711 1.00 39.31 ? 658 LEU B CG    1 
ATOM   10851 C  CD1   . LEU B 1 658 ? 117.124 125.037 156.209 1.00 38.13 ? 658 LEU B CD1   1 
ATOM   10852 C  CD2   . LEU B 1 658 ? 115.836 125.990 158.122 1.00 40.15 ? 658 LEU B CD2   1 
ATOM   10853 N  N     . LYS B 1 659 ? 117.286 121.660 160.688 1.00 48.74 ? 659 LYS B N     1 
ATOM   10854 C  CA    . LYS B 1 659 ? 117.534 120.243 160.885 1.00 49.54 ? 659 LYS B CA    1 
ATOM   10855 C  C     . LYS B 1 659 ? 117.211 119.472 159.610 1.00 50.99 ? 659 LYS B C     1 
ATOM   10856 O  O     . LYS B 1 659 ? 116.508 119.956 158.720 1.00 51.82 ? 659 LYS B O     1 
ATOM   10857 C  CB    . LYS B 1 659 ? 116.708 119.704 162.053 1.00 49.13 ? 659 LYS B CB    1 
ATOM   10858 C  CG    . LYS B 1 659 ? 117.065 120.315 163.396 1.00 50.96 ? 659 LYS B CG    1 
ATOM   10859 C  CD    . LYS B 1 659 ? 116.471 119.517 164.543 1.00 51.18 ? 659 LYS B CD    1 
ATOM   10860 C  CE    . LYS B 1 659 ? 116.913 120.071 165.887 1.00 49.75 ? 659 LYS B CE    1 
ATOM   10861 N  NZ    . LYS B 1 659 ? 116.709 119.091 166.988 1.00 50.53 ? 659 LYS B NZ    1 
ATOM   10862 N  N     . ASP B 1 660 ? 117.749 118.254 159.527 1.00 55.60 ? 660 ASP B N     1 
ATOM   10863 C  CA    . ASP B 1 660 ? 117.472 117.404 158.375 1.00 55.35 ? 660 ASP B CA    1 
ATOM   10864 C  C     . ASP B 1 660 ? 116.023 116.933 158.359 1.00 54.56 ? 660 ASP B C     1 
ATOM   10865 O  O     . ASP B 1 660 ? 115.472 116.665 157.286 1.00 54.41 ? 660 ASP B O     1 
ATOM   10866 C  CB    . ASP B 1 660 ? 118.420 116.205 158.367 1.00 55.90 ? 660 ASP B CB    1 
ATOM   10867 C  CG    . ASP B 1 660 ? 118.398 115.436 159.673 1.00 57.36 ? 660 ASP B CG    1 
ATOM   10868 O  OD1   . ASP B 1 660 ? 117.919 115.994 160.683 1.00 56.45 ? 660 ASP B OD1   1 
ATOM   10869 O  OD2   . ASP B 1 660 ? 118.859 114.276 159.692 1.00 57.06 ? 660 ASP B OD2   1 
ATOM   10870 N  N     . THR B 1 661 ? 115.391 116.831 159.528 1.00 52.41 ? 661 THR B N     1 
ATOM   10871 C  CA    . THR B 1 661 ? 114.027 116.327 159.612 1.00 53.29 ? 661 THR B CA    1 
ATOM   10872 C  C     . THR B 1 661 ? 112.978 117.349 159.199 1.00 54.49 ? 661 THR B C     1 
ATOM   10873 O  O     . THR B 1 661 ? 111.840 116.963 158.911 1.00 53.25 ? 661 THR B O     1 
ATOM   10874 C  CB    . THR B 1 661 ? 113.727 115.862 161.035 1.00 53.68 ? 661 THR B CB    1 
ATOM   10875 O  OG1   . THR B 1 661 ? 113.902 116.960 161.939 1.00 51.94 ? 661 THR B OG1   1 
ATOM   10876 C  CG2   . THR B 1 661 ? 114.655 114.731 161.428 1.00 53.72 ? 661 THR B CG2   1 
ATOM   10877 N  N     . MET B 1 662 ? 113.320 118.634 159.176 1.00 54.26 ? 662 MET B N     1 
ATOM   10878 C  CA    . MET B 1 662 ? 112.333 119.660 158.873 1.00 51.19 ? 662 MET B CA    1 
ATOM   10879 C  C     . MET B 1 662 ? 111.955 119.629 157.398 1.00 51.12 ? 662 MET B C     1 
ATOM   10880 O  O     . MET B 1 662 ? 112.762 119.269 156.538 1.00 50.35 ? 662 MET B O     1 
ATOM   10881 C  CB    . MET B 1 662 ? 112.863 121.038 159.261 1.00 50.50 ? 662 MET B CB    1 
ATOM   10882 C  CG    . MET B 1 662 ? 112.680 121.358 160.737 1.00 52.96 ? 662 MET B CG    1 
ATOM   10883 S  SD    . MET B 1 662 ? 113.608 122.801 161.283 1.00 55.86 ? 662 MET B SD    1 
ATOM   10884 C  CE    . MET B 1 662 ? 113.670 123.748 159.768 1.00 50.19 ? 662 MET B CE    1 
ATOM   10885 N  N     . THR B 1 663 ? 110.715 120.012 157.111 1.00 47.61 ? 663 THR B N     1 
ATOM   10886 C  CA    . THR B 1 663 ? 110.144 119.873 155.784 1.00 43.90 ? 663 THR B CA    1 
ATOM   10887 C  C     . THR B 1 663 ? 110.379 121.137 154.958 1.00 45.59 ? 663 THR B C     1 
ATOM   10888 O  O     . THR B 1 663 ? 110.953 122.124 155.423 1.00 47.48 ? 663 THR B O     1 
ATOM   10889 C  CB    . THR B 1 663 ? 108.649 119.581 155.885 1.00 41.72 ? 663 THR B CB    1 
ATOM   10890 O  OG1   . THR B 1 663 ? 108.044 120.521 156.779 1.00 43.89 ? 663 THR B OG1   1 
ATOM   10891 C  CG2   . THR B 1 663 ? 108.422 118.194 156.449 1.00 43.69 ? 663 THR B CG2   1 
ATOM   10892 N  N     . THR B 1 664 ? 109.931 121.096 153.702 1.00 39.86 ? 664 THR B N     1 
ATOM   10893 C  CA    . THR B 1 664 ? 109.835 122.316 152.907 1.00 37.67 ? 664 THR B CA    1 
ATOM   10894 C  C     . THR B 1 664 ? 108.836 123.284 153.527 1.00 37.38 ? 664 THR B C     1 
ATOM   10895 O  O     . THR B 1 664 ? 109.062 124.502 153.549 1.00 40.04 ? 664 THR B O     1 
ATOM   10896 C  CB    . THR B 1 664 ? 109.443 121.962 151.469 1.00 41.20 ? 664 THR B CB    1 
ATOM   10897 O  OG1   . THR B 1 664 ? 110.594 121.483 150.761 1.00 39.08 ? 664 THR B OG1   1 
ATOM   10898 C  CG2   . THR B 1 664 ? 108.852 123.156 150.739 1.00 40.56 ? 664 THR B CG2   1 
ATOM   10899 N  N     . ARG B 1 665 ? 107.729 122.753 154.052 1.00 38.50 ? 665 ARG B N     1 
ATOM   10900 C  CA    . ARG B 1 665 ? 106.738 123.588 154.719 1.00 38.60 ? 665 ARG B CA    1 
ATOM   10901 C  C     . ARG B 1 665 ? 107.333 124.305 155.923 1.00 40.37 ? 665 ARG B C     1 
ATOM   10902 O  O     . ARG B 1 665 ? 106.965 125.445 156.215 1.00 44.63 ? 665 ARG B O     1 
ATOM   10903 C  CB    . ARG B 1 665 ? 105.541 122.740 155.145 1.00 39.29 ? 665 ARG B CB    1 
ATOM   10904 C  CG    . ARG B 1 665 ? 104.271 123.533 155.381 1.00 37.69 ? 665 ARG B CG    1 
ATOM   10905 C  CD    . ARG B 1 665 ? 103.321 122.784 156.296 1.00 40.43 ? 665 ARG B CD    1 
ATOM   10906 N  NE    . ARG B 1 665 ? 103.602 123.048 157.701 1.00 43.76 ? 665 ARG B NE    1 
ATOM   10907 C  CZ    . ARG B 1 665 ? 102.778 122.753 158.698 1.00 45.62 ? 665 ARG B CZ    1 
ATOM   10908 N  NH1   . ARG B 1 665 ? 101.608 122.175 158.480 1.00 41.99 ? 665 ARG B NH1   1 
ATOM   10909 N  NH2   . ARG B 1 665 ? 103.137 123.048 159.944 1.00 43.46 ? 665 ARG B NH2   1 
ATOM   10910 N  N     . ASP B 1 666 ? 108.251 123.653 156.640 1.00 37.79 ? 666 ASP B N     1 
ATOM   10911 C  CA    . ASP B 1 666 ? 108.870 124.297 157.795 1.00 34.64 ? 666 ASP B CA    1 
ATOM   10912 C  C     . ASP B 1 666 ? 109.750 125.469 157.377 1.00 38.97 ? 666 ASP B C     1 
ATOM   10913 O  O     . ASP B 1 666 ? 109.719 126.532 158.008 1.00 40.24 ? 666 ASP B O     1 
ATOM   10914 C  CB    . ASP B 1 666 ? 109.675 123.277 158.598 1.00 40.57 ? 666 ASP B CB    1 
ATOM   10915 C  CG    . ASP B 1 666 ? 108.799 122.223 159.243 1.00 45.59 ? 666 ASP B CG    1 
ATOM   10916 O  OD1   . ASP B 1 666 ? 107.698 122.576 159.715 1.00 42.98 ? 666 ASP B OD1   1 
ATOM   10917 O  OD2   . ASP B 1 666 ? 109.212 121.045 159.285 1.00 47.37 ? 666 ASP B OD2   1 
ATOM   10918 N  N     . LEU B 1 667 ? 110.541 125.296 156.316 1.00 35.55 ? 667 LEU B N     1 
ATOM   10919 C  CA    . LEU B 1 667 ? 111.352 126.401 155.815 1.00 28.78 ? 667 LEU B CA    1 
ATOM   10920 C  C     . LEU B 1 667 ? 110.470 127.542 155.324 1.00 30.44 ? 667 LEU B C     1 
ATOM   10921 O  O     . LEU B 1 667 ? 110.766 128.718 155.571 1.00 31.15 ? 667 LEU B O     1 
ATOM   10922 C  CB    . LEU B 1 667 ? 112.273 125.911 154.698 1.00 30.89 ? 667 LEU B CB    1 
ATOM   10923 C  CG    . LEU B 1 667 ? 113.683 126.504 154.613 1.00 32.48 ? 667 LEU B CG    1 
ATOM   10924 C  CD1   . LEU B 1 667 ? 114.514 125.736 153.604 1.00 32.18 ? 667 LEU B CD1   1 
ATOM   10925 C  CD2   . LEU B 1 667 ? 113.656 127.980 154.261 1.00 37.10 ? 667 LEU B CD2   1 
ATOM   10926 N  N     . ASN B 1 668 ? 109.380 127.213 154.628 1.00 35.25 ? 668 ASN B N     1 
ATOM   10927 C  CA    . ASN B 1 668 ? 108.452 128.245 154.178 1.00 24.13 ? 668 ASN B CA    1 
ATOM   10928 C  C     . ASN B 1 668 ? 107.820 128.972 155.357 1.00 23.45 ? 668 ASN B C     1 
ATOM   10929 O  O     . ASN B 1 668 ? 107.634 130.191 155.314 1.00 29.46 ? 668 ASN B O     1 
ATOM   10930 C  CB    . ASN B 1 668 ? 107.375 127.631 153.287 1.00 27.90 ? 668 ASN B CB    1 
ATOM   10931 C  CG    . ASN B 1 668 ? 107.815 127.507 151.847 1.00 31.90 ? 668 ASN B CG    1 
ATOM   10932 O  OD1   . ASN B 1 668 ? 107.509 126.524 151.175 1.00 37.61 ? 668 ASN B OD1   1 
ATOM   10933 N  ND2   . ASN B 1 668 ? 108.538 128.508 151.362 1.00 29.77 ? 668 ASN B ND2   1 
ATOM   10934 N  N     . ARG B 1 669 ? 107.473 128.237 156.414 1.00 30.18 ? 669 ARG B N     1 
ATOM   10935 C  CA    . ARG B 1 669 ? 106.913 128.863 157.606 1.00 32.01 ? 669 ARG B CA    1 
ATOM   10936 C  C     . ARG B 1 669 ? 107.917 129.803 158.255 1.00 28.46 ? 669 ARG B C     1 
ATOM   10937 O  O     . ARG B 1 669 ? 107.553 130.894 158.706 1.00 26.39 ? 669 ARG B O     1 
ATOM   10938 C  CB    . ARG B 1 669 ? 106.465 127.791 158.598 1.00 31.21 ? 669 ARG B CB    1 
ATOM   10939 C  CG    . ARG B 1 669 ? 104.966 127.598 158.663 1.00 28.17 ? 669 ARG B CG    1 
ATOM   10940 C  CD    . ARG B 1 669 ? 104.585 126.631 159.770 1.00 31.43 ? 669 ARG B CD    1 
ATOM   10941 N  NE    . ARG B 1 669 ? 104.558 127.267 161.082 1.00 32.82 ? 669 ARG B NE    1 
ATOM   10942 C  CZ    . ARG B 1 669 ? 103.670 128.175 161.465 1.00 34.84 ? 669 ARG B CZ    1 
ATOM   10943 N  NH1   . ARG B 1 669 ? 102.703 128.581 160.659 1.00 34.35 ? 669 ARG B NH1   1 
ATOM   10944 N  NH2   . ARG B 1 669 ? 103.750 128.684 162.690 1.00 35.66 ? 669 ARG B NH2   1 
ATOM   10945 N  N     . ILE B 1 670 ? 109.185 129.395 158.316 1.00 26.20 ? 670 ILE B N     1 
ATOM   10946 C  CA    . ILE B 1 670 ? 110.215 130.269 158.872 1.00 24.84 ? 670 ILE B CA    1 
ATOM   10947 C  C     . ILE B 1 670 ? 110.350 131.533 158.032 1.00 24.59 ? 670 ILE B C     1 
ATOM   10948 O  O     . ILE B 1 670 ? 110.441 132.644 158.567 1.00 26.83 ? 670 ILE B O     1 
ATOM   10949 C  CB    . ILE B 1 670 ? 111.555 129.521 158.990 1.00 29.87 ? 670 ILE B CB    1 
ATOM   10950 C  CG1   . ILE B 1 670 ? 111.441 128.376 159.997 1.00 29.99 ? 670 ILE B CG1   1 
ATOM   10951 C  CG2   . ILE B 1 670 ? 112.662 130.473 159.405 1.00 28.14 ? 670 ILE B CG2   1 
ATOM   10952 C  CD1   . ILE B 1 670 ? 112.446 127.272 159.777 1.00 26.60 ? 670 ILE B CD1   1 
ATOM   10953 N  N     . ASP B 1 671 ? 110.356 131.387 156.704 1.00 25.44 ? 671 ASP B N     1 
ATOM   10954 C  CA    . ASP B 1 671 ? 110.464 132.553 155.830 1.00 21.98 ? 671 ASP B CA    1 
ATOM   10955 C  C     . ASP B 1 671 ? 109.268 133.485 155.992 1.00 21.95 ? 671 ASP B C     1 
ATOM   10956 O  O     . ASP B 1 671 ? 109.426 134.711 156.031 1.00 28.53 ? 671 ASP B O     1 
ATOM   10957 C  CB    . ASP B 1 671 ? 110.599 132.112 154.373 1.00 23.19 ? 671 ASP B CB    1 
ATOM   10958 C  CG    . ASP B 1 671 ? 111.788 131.201 154.148 1.00 37.03 ? 671 ASP B CG    1 
ATOM   10959 O  OD1   . ASP B 1 671 ? 112.711 131.208 154.988 1.00 36.87 ? 671 ASP B OD1   1 
ATOM   10960 O  OD2   . ASP B 1 671 ? 111.801 130.476 153.130 1.00 35.95 ? 671 ASP B OD2   1 
ATOM   10961 N  N     . LEU B 1 672 ? 108.063 132.924 156.094 1.00 22.71 ? 672 LEU B N     1 
ATOM   10962 C  CA    . LEU B 1 672 ? 106.868 133.750 156.224 1.00 18.88 ? 672 LEU B CA    1 
ATOM   10963 C  C     . LEU B 1 672 ? 106.788 134.421 157.587 1.00 19.08 ? 672 LEU B C     1 
ATOM   10964 O  O     . LEU B 1 672 ? 106.278 135.540 157.692 1.00 23.68 ? 672 LEU B O     1 
ATOM   10965 C  CB    . LEU B 1 672 ? 105.618 132.909 155.971 1.00 23.75 ? 672 LEU B CB    1 
ATOM   10966 C  CG    . LEU B 1 672 ? 105.457 132.387 154.544 1.00 23.48 ? 672 LEU B CG    1 
ATOM   10967 C  CD1   . LEU B 1 672 ? 104.455 131.247 154.504 1.00 20.15 ? 672 LEU B CD1   1 
ATOM   10968 C  CD2   . LEU B 1 672 ? 105.049 133.509 153.605 1.00 23.60 ? 672 LEU B CD2   1 
ATOM   10969 N  N     . TYR B 1 673 ? 107.276 133.762 158.638 1.00 23.10 ? 673 TYR B N     1 
ATOM   10970 C  CA    . TYR B 1 673 ? 107.321 134.404 159.946 1.00 17.31 ? 673 TYR B CA    1 
ATOM   10971 C  C     . TYR B 1 673 ? 108.380 135.496 159.984 1.00 18.64 ? 673 TYR B C     1 
ATOM   10972 O  O     . TYR B 1 673 ? 108.199 136.521 160.649 1.00 23.54 ? 673 TYR B O     1 
ATOM   10973 C  CB    . TYR B 1 673 ? 107.580 133.367 161.036 1.00 19.66 ? 673 TYR B CB    1 
ATOM   10974 C  CG    . TYR B 1 673 ? 107.604 133.953 162.427 1.00 20.31 ? 673 TYR B CG    1 
ATOM   10975 C  CD1   . TYR B 1 673 ? 106.472 134.541 162.971 1.00 21.36 ? 673 TYR B CD1   1 
ATOM   10976 C  CD2   . TYR B 1 673 ? 108.758 133.919 163.194 1.00 16.85 ? 673 TYR B CD2   1 
ATOM   10977 C  CE1   . TYR B 1 673 ? 106.488 135.077 164.240 1.00 20.53 ? 673 TYR B CE1   1 
ATOM   10978 C  CE2   . TYR B 1 673 ? 108.785 134.453 164.463 1.00 23.10 ? 673 TYR B CE2   1 
ATOM   10979 C  CZ    . TYR B 1 673 ? 107.648 135.030 164.982 1.00 24.25 ? 673 TYR B CZ    1 
ATOM   10980 O  OH    . TYR B 1 673 ? 107.670 135.564 166.249 1.00 28.12 ? 673 TYR B OH    1 
ATOM   10981 N  N     . ALA B 1 674 ? 109.499 135.287 159.288 1.00 20.53 ? 674 ALA B N     1 
ATOM   10982 C  CA    . ALA B 1 674 ? 110.490 136.347 159.150 1.00 13.72 ? 674 ALA B CA    1 
ATOM   10983 C  C     . ALA B 1 674 ? 109.901 137.547 158.422 1.00 18.15 ? 674 ALA B C     1 
ATOM   10984 O  O     . ALA B 1 674 ? 110.096 138.694 158.838 1.00 26.54 ? 674 ALA B O     1 
ATOM   10985 C  CB    . ALA B 1 674 ? 111.721 135.817 158.417 1.00 12.39 ? 674 ALA B CB    1 
ATOM   10986 N  N     . HIS B 1 675 ? 109.162 137.299 157.341 1.00 18.13 ? 675 HIS B N     1 
ATOM   10987 C  CA    . HIS B 1 675 ? 108.487 138.385 156.638 1.00 16.74 ? 675 HIS B CA    1 
ATOM   10988 C  C     . HIS B 1 675 ? 107.478 139.083 157.541 1.00 21.23 ? 675 HIS B C     1 
ATOM   10989 O  O     . HIS B 1 675 ? 107.362 140.314 157.523 1.00 25.84 ? 675 HIS B O     1 
ATOM   10990 C  CB    . HIS B 1 675 ? 107.803 137.846 155.383 1.00 17.43 ? 675 HIS B CB    1 
ATOM   10991 C  CG    . HIS B 1 675 ? 106.947 138.854 154.683 1.00 21.17 ? 675 HIS B CG    1 
ATOM   10992 N  ND1   . HIS B 1 675 ? 105.598 138.982 154.930 1.00 26.15 ? 675 HIS B ND1   1 
ATOM   10993 C  CD2   . HIS B 1 675 ? 107.248 139.784 153.747 1.00 16.46 ? 675 HIS B CD2   1 
ATOM   10994 C  CE1   . HIS B 1 675 ? 105.104 139.948 154.177 1.00 23.84 ? 675 HIS B CE1   1 
ATOM   10995 N  NE2   . HIS B 1 675 ? 106.085 140.450 153.449 1.00 27.44 ? 675 HIS B NE2   1 
ATOM   10996 N  N     . HIS B 1 676 ? 106.736 138.311 158.336 1.00 21.26 ? 676 HIS B N     1 
ATOM   10997 C  CA    . HIS B 1 676 ? 105.737 138.886 159.230 1.00 19.78 ? 676 HIS B CA    1 
ATOM   10998 C  C     . HIS B 1 676 ? 106.382 139.739 160.314 1.00 24.53 ? 676 HIS B C     1 
ATOM   10999 O  O     . HIS B 1 676 ? 105.831 140.773 160.708 1.00 24.01 ? 676 HIS B O     1 
ATOM   11000 C  CB    . HIS B 1 676 ? 104.898 137.770 159.852 1.00 22.70 ? 676 HIS B CB    1 
ATOM   11001 C  CG    . HIS B 1 676 ? 103.969 138.237 160.927 1.00 21.31 ? 676 HIS B CG    1 
ATOM   11002 N  ND1   . HIS B 1 676 ? 102.936 139.116 160.689 1.00 20.46 ? 676 HIS B ND1   1 
ATOM   11003 C  CD2   . HIS B 1 676 ? 103.918 137.945 162.248 1.00 23.95 ? 676 HIS B CD2   1 
ATOM   11004 C  CE1   . HIS B 1 676 ? 102.288 139.347 161.816 1.00 26.90 ? 676 HIS B CE1   1 
ATOM   11005 N  NE2   . HIS B 1 676 ? 102.864 138.648 162.778 1.00 26.32 ? 676 HIS B NE2   1 
ATOM   11006 N  N     . ARG B 1 677 ? 107.545 139.325 160.806 1.00 23.53 ? 677 ARG B N     1 
ATOM   11007 C  CA    . ARG B 1 677 ? 108.208 139.997 161.915 1.00 19.43 ? 677 ARG B CA    1 
ATOM   11008 C  C     . ARG B 1 677 ? 109.065 141.174 161.476 1.00 23.47 ? 677 ARG B C     1 
ATOM   11009 O  O     . ARG B 1 677 ? 109.692 141.814 162.325 1.00 29.20 ? 677 ARG B O     1 
ATOM   11010 C  CB    . ARG B 1 677 ? 109.068 138.999 162.694 1.00 19.57 ? 677 ARG B CB    1 
ATOM   11011 C  CG    . ARG B 1 677 ? 108.285 138.152 163.673 1.00 19.73 ? 677 ARG B CG    1 
ATOM   11012 C  CD    . ARG B 1 677 ? 107.749 138.990 164.816 1.00 23.27 ? 677 ARG B CD    1 
ATOM   11013 N  NE    . ARG B 1 677 ? 108.745 139.173 165.864 1.00 28.19 ? 677 ARG B NE    1 
ATOM   11014 C  CZ    . ARG B 1 677 ? 109.178 140.352 166.286 1.00 31.57 ? 677 ARG B CZ    1 
ATOM   11015 N  NH1   . ARG B 1 677 ? 108.719 141.481 165.771 1.00 27.61 ? 677 ARG B NH1   1 
ATOM   11016 N  NH2   . ARG B 1 677 ? 110.096 140.401 167.247 1.00 27.47 ? 677 ARG B NH2   1 
ATOM   11017 N  N     . GLY B 1 678 ? 109.112 141.475 160.183 1.00 21.12 ? 678 GLY B N     1 
ATOM   11018 C  CA    . GLY B 1 678 ? 109.883 142.595 159.695 1.00 14.82 ? 678 GLY B CA    1 
ATOM   11019 C  C     . GLY B 1 678 ? 111.303 142.279 159.293 1.00 16.43 ? 678 GLY B C     1 
ATOM   11020 O  O     . GLY B 1 678 ? 112.103 143.208 159.136 1.00 22.23 ? 678 GLY B O     1 
ATOM   11021 N  N     . ILE B 1 679 ? 111.647 141.001 159.128 1.00 17.00 ? 679 ILE B N     1 
ATOM   11022 C  CA    . ILE B 1 679 ? 112.983 140.642 158.672 1.00 13.71 ? 679 ILE B CA    1 
ATOM   11023 C  C     . ILE B 1 679 ? 113.174 141.149 157.252 1.00 19.24 ? 679 ILE B C     1 
ATOM   11024 O  O     . ILE B 1 679 ? 112.306 140.972 156.388 1.00 24.93 ? 679 ILE B O     1 
ATOM   11025 C  CB    . ILE B 1 679 ? 113.188 139.123 158.766 1.00 12.69 ? 679 ILE B CB    1 
ATOM   11026 C  CG1   . ILE B 1 679 ? 113.220 138.677 160.229 1.00 14.68 ? 679 ILE B CG1   1 
ATOM   11027 C  CG2   . ILE B 1 679 ? 114.453 138.698 158.042 1.00 15.09 ? 679 ILE B CG2   1 
ATOM   11028 C  CD1   . ILE B 1 679 ? 114.337 139.281 161.025 1.00 17.74 ? 679 ILE B CD1   1 
ATOM   11029 N  N     . LYS B 1 680 ? 114.309 141.800 157.007 1.00 12.13 ? 680 LYS B N     1 
ATOM   11030 C  CA    . LYS B 1 680 ? 114.573 142.393 155.703 1.00 7.27  ? 680 LYS B CA    1 
ATOM   11031 C  C     . LYS B 1 680 ? 115.161 141.388 154.720 1.00 3.29  ? 680 LYS B C     1 
ATOM   11032 O  O     . LYS B 1 680 ? 114.727 141.320 153.567 1.00 16.95 ? 680 LYS B O     1 
ATOM   11033 C  CB    . LYS B 1 680 ? 115.512 143.590 155.857 1.00 11.34 ? 680 LYS B CB    1 
ATOM   11034 C  CG    . LYS B 1 680 ? 114.929 144.744 156.641 1.00 0.00  ? 680 LYS B CG    1 
ATOM   11035 C  CD    . LYS B 1 680 ? 115.869 145.933 156.622 1.00 4.29  ? 680 LYS B CD    1 
ATOM   11036 C  CE    . LYS B 1 680 ? 115.456 146.976 157.634 1.00 12.52 ? 680 LYS B CE    1 
ATOM   11037 N  NZ    . LYS B 1 680 ? 116.320 148.182 157.576 1.00 14.81 ? 680 LYS B NZ    1 
ATOM   11038 N  N     . THR B 1 681 ? 116.150 140.612 155.151 1.00 8.42  ? 681 THR B N     1 
ATOM   11039 C  CA    . THR B 1 681 ? 116.811 139.654 154.279 1.00 8.37  ? 681 THR B CA    1 
ATOM   11040 C  C     . THR B 1 681 ? 117.021 138.345 155.023 1.00 13.41 ? 681 THR B C     1 
ATOM   11041 O  O     . THR B 1 681 ? 117.138 138.321 156.250 1.00 22.95 ? 681 THR B O     1 
ATOM   11042 C  CB    . THR B 1 681 ? 118.165 140.177 153.769 1.00 12.80 ? 681 THR B CB    1 
ATOM   11043 O  OG1   . THR B 1 681 ? 118.923 140.704 154.865 1.00 26.27 ? 681 THR B OG1   1 
ATOM   11044 C  CG2   . THR B 1 681 ? 117.972 141.267 152.731 1.00 8.31  ? 681 THR B CG2   1 
ATOM   11045 N  N     . ILE B 1 682 ? 117.067 137.254 154.265 1.00 15.01 ? 682 ILE B N     1 
ATOM   11046 C  CA    . ILE B 1 682 ? 117.427 135.939 154.780 1.00 10.98 ? 682 ILE B CA    1 
ATOM   11047 C  C     . ILE B 1 682 ? 118.640 135.452 154.003 1.00 17.98 ? 682 ILE B C     1 
ATOM   11048 O  O     . ILE B 1 682 ? 118.603 135.374 152.771 1.00 14.80 ? 682 ILE B O     1 
ATOM   11049 C  CB    . ILE B 1 682 ? 116.262 134.940 154.671 1.00 13.20 ? 682 ILE B CB    1 
ATOM   11050 C  CG1   . ILE B 1 682 ? 115.021 135.490 155.374 1.00 18.92 ? 682 ILE B CG1   1 
ATOM   11051 C  CG2   . ILE B 1 682 ? 116.659 133.615 155.276 1.00 19.03 ? 682 ILE B CG2   1 
ATOM   11052 C  CD1   . ILE B 1 682 ? 113.887 134.501 155.478 1.00 19.82 ? 682 ILE B CD1   1 
ATOM   11053 N  N     . TYR B 1 683 ? 119.715 135.130 154.723 1.00 22.38 ? 683 TYR B N     1 
ATOM   11054 C  CA    . TYR B 1 683 ? 120.989 134.843 154.065 1.00 18.92 ? 683 TYR B CA    1 
ATOM   11055 C  C     . TYR B 1 683 ? 121.070 133.403 153.569 1.00 22.12 ? 683 TYR B C     1 
ATOM   11056 O  O     . TYR B 1 683 ? 121.101 133.149 152.363 1.00 33.47 ? 683 TYR B O     1 
ATOM   11057 C  CB    . TYR B 1 683 ? 122.142 135.149 155.028 1.00 18.88 ? 683 TYR B CB    1 
ATOM   11058 C  CG    . TYR B 1 683 ? 123.512 135.099 154.399 1.00 15.70 ? 683 TYR B CG    1 
ATOM   11059 C  CD1   . TYR B 1 683 ? 123.680 135.283 153.035 1.00 13.39 ? 683 TYR B CD1   1 
ATOM   11060 C  CD2   . TYR B 1 683 ? 124.641 134.876 155.174 1.00 11.44 ? 683 TYR B CD2   1 
ATOM   11061 C  CE1   . TYR B 1 683 ? 124.929 135.241 152.460 1.00 18.79 ? 683 TYR B CE1   1 
ATOM   11062 C  CE2   . TYR B 1 683 ? 125.897 134.834 154.607 1.00 19.36 ? 683 TYR B CE2   1 
ATOM   11063 C  CZ    . TYR B 1 683 ? 126.035 135.017 153.249 1.00 21.17 ? 683 TYR B CZ    1 
ATOM   11064 O  OH    . TYR B 1 683 ? 127.284 134.976 152.676 1.00 22.33 ? 683 TYR B OH    1 
ATOM   11065 N  N     . TYR B 1 684 ? 121.078 132.442 154.485 1.00 27.64 ? 684 TYR B N     1 
ATOM   11066 C  CA    . TYR B 1 684 ? 121.417 131.076 154.125 1.00 22.41 ? 684 TYR B CA    1 
ATOM   11067 C  C     . TYR B 1 684 ? 120.488 130.105 154.827 1.00 34.42 ? 684 TYR B C     1 
ATOM   11068 O  O     . TYR B 1 684 ? 119.998 130.371 155.927 1.00 35.40 ? 684 TYR B O     1 
ATOM   11069 C  CB    . TYR B 1 684 ? 122.869 130.742 154.485 1.00 24.56 ? 684 TYR B CB    1 
ATOM   11070 C  CG    . TYR B 1 684 ? 123.834 130.856 153.331 1.00 25.48 ? 684 TYR B CG    1 
ATOM   11071 C  CD1   . TYR B 1 684 ? 123.480 130.427 152.061 1.00 27.02 ? 684 TYR B CD1   1 
ATOM   11072 C  CD2   . TYR B 1 684 ? 125.101 131.389 153.514 1.00 29.51 ? 684 TYR B CD2   1 
ATOM   11073 C  CE1   . TYR B 1 684 ? 124.360 130.529 151.003 1.00 32.04 ? 684 TYR B CE1   1 
ATOM   11074 C  CE2   . TYR B 1 684 ? 125.988 131.496 152.463 1.00 25.73 ? 684 TYR B CE2   1 
ATOM   11075 C  CZ    . TYR B 1 684 ? 125.613 131.065 151.210 1.00 29.78 ? 684 TYR B CZ    1 
ATOM   11076 O  OH    . TYR B 1 684 ? 126.495 131.169 150.160 1.00 33.98 ? 684 TYR B OH    1 
ATOM   11077 N  N     . ALA B 1 685 ? 120.254 128.976 154.175 1.00 35.91 ? 685 ALA B N     1 
ATOM   11078 C  CA    . ALA B 1 685 ? 119.523 127.855 154.749 1.00 33.13 ? 685 ALA B CA    1 
ATOM   11079 C  C     . ALA B 1 685 ? 120.548 126.752 154.999 1.00 34.36 ? 685 ALA B C     1 
ATOM   11080 O  O     . ALA B 1 685 ? 120.879 125.975 154.102 1.00 40.54 ? 685 ALA B O     1 
ATOM   11081 C  CB    . ALA B 1 685 ? 118.403 127.399 153.826 1.00 30.44 ? 685 ALA B CB    1 
ATOM   11082 N  N     . ARG B 1 686 ? 121.057 126.695 156.225 1.00 33.76 ? 686 ARG B N     1 
ATOM   11083 C  CA    . ARG B 1 686 ? 122.057 125.707 156.606 1.00 38.14 ? 686 ARG B CA    1 
ATOM   11084 C  C     . ARG B 1 686 ? 121.366 124.532 157.282 1.00 41.36 ? 686 ARG B C     1 
ATOM   11085 O  O     . ARG B 1 686 ? 120.690 124.706 158.302 1.00 41.57 ? 686 ARG B O     1 
ATOM   11086 C  CB    . ARG B 1 686 ? 123.103 126.326 157.531 1.00 39.88 ? 686 ARG B CB    1 
ATOM   11087 C  CG    . ARG B 1 686 ? 124.210 127.062 156.804 1.00 40.19 ? 686 ARG B CG    1 
ATOM   11088 C  CD    . ARG B 1 686 ? 125.442 127.205 157.677 1.00 42.85 ? 686 ARG B CD    1 
ATOM   11089 N  NE    . ARG B 1 686 ? 126.261 125.999 157.670 1.00 44.31 ? 686 ARG B NE    1 
ATOM   11090 C  CZ    . ARG B 1 686 ? 127.586 125.996 157.627 1.00 45.64 ? 686 ARG B CZ    1 
ATOM   11091 N  NH1   . ARG B 1 686 ? 128.279 127.122 157.575 1.00 42.12 ? 686 ARG B NH1   1 
ATOM   11092 N  NH2   . ARG B 1 686 ? 128.233 124.834 157.633 1.00 45.78 ? 686 ARG B NH2   1 
ATOM   11093 N  N     . THR B 1 687 ? 121.535 123.341 156.718 1.00 46.51 ? 687 THR B N     1 
ATOM   11094 C  CA    . THR B 1 687 ? 120.902 122.132 157.221 1.00 48.83 ? 687 THR B CA    1 
ATOM   11095 C  C     . THR B 1 687 ? 121.939 121.238 157.886 1.00 48.87 ? 687 THR B C     1 
ATOM   11096 O  O     . THR B 1 687 ? 123.049 121.069 157.372 1.00 50.06 ? 687 THR B O     1 
ATOM   11097 C  CB    . THR B 1 687 ? 120.200 121.367 156.095 1.00 46.79 ? 687 THR B CB    1 
ATOM   11098 O  OG1   . THR B 1 687 ? 119.581 122.296 155.197 1.00 44.28 ? 687 THR B OG1   1 
ATOM   11099 C  CG2   . THR B 1 687 ? 119.141 120.440 156.664 1.00 45.29 ? 687 THR B CG2   1 
ATOM   11100 N  N     . LYS B 1 688 ? 121.573 120.674 159.032 1.00 47.28 ? 688 LYS B N     1 
ATOM   11101 C  CA    . LYS B 1 688 ? 122.458 119.771 159.757 1.00 48.83 ? 688 LYS B CA    1 
ATOM   11102 C  C     . LYS B 1 688 ? 122.268 118.332 159.292 1.00 52.43 ? 688 LYS B C     1 
ATOM   11103 O  O     . LYS B 1 688 ? 121.140 117.863 159.143 1.00 53.11 ? 688 LYS B O     1 
ATOM   11104 C  CB    . LYS B 1 688 ? 122.213 119.873 161.263 1.00 47.66 ? 688 LYS B CB    1 
ATOM   11105 C  CG    . LYS B 1 688 ? 123.273 119.186 162.105 1.00 48.61 ? 688 LYS B CG    1 
ATOM   11106 C  CD    . LYS B 1 688 ? 123.246 119.685 163.538 1.00 49.34 ? 688 LYS B CD    1 
ATOM   11107 C  CE    . LYS B 1 688 ? 124.440 119.171 164.322 1.00 51.07 ? 688 LYS B CE    1 
ATOM   11108 N  NZ    . LYS B 1 688 ? 124.481 119.737 165.698 1.00 51.54 ? 688 LYS B NZ    1 
ATOM   11109 N  N     . LYS C 2 330 ? 139.161 109.094 114.475 1.00 57.38 ? 309 LYS C N     1 
ATOM   11110 C  CA    . LYS C 2 330 ? 140.398 109.841 114.278 1.00 58.57 ? 309 LYS C CA    1 
ATOM   11111 C  C     . LYS C 2 330 ? 141.120 109.389 113.014 1.00 57.73 ? 309 LYS C C     1 
ATOM   11112 O  O     . LYS C 2 330 ? 140.931 108.266 112.547 1.00 59.72 ? 309 LYS C O     1 
ATOM   11113 C  CB    . LYS C 2 330 ? 141.322 109.680 115.487 1.00 55.66 ? 309 LYS C CB    1 
ATOM   11114 C  CG    . LYS C 2 330 ? 141.042 110.644 116.627 1.00 56.05 ? 309 LYS C CG    1 
ATOM   11115 C  CD    . LYS C 2 330 ? 142.177 110.632 117.639 1.00 57.52 ? 309 LYS C CD    1 
ATOM   11116 C  CE    . LYS C 2 330 ? 141.891 111.558 118.809 1.00 58.27 ? 309 LYS C CE    1 
ATOM   11117 N  NZ    . LYS C 2 330 ? 141.068 110.892 119.856 1.00 57.81 ? 309 LYS C NZ    1 
ATOM   11118 N  N     . ALA C 2 331 ? 141.948 110.271 112.464 1.00 46.74 ? 310 ALA C N     1 
ATOM   11119 C  CA    . ALA C 2 331 ? 142.793 109.926 111.333 1.00 47.69 ? 310 ALA C CA    1 
ATOM   11120 C  C     . ALA C 2 331 ? 144.105 109.336 111.831 1.00 44.34 ? 310 ALA C C     1 
ATOM   11121 O  O     . ALA C 2 331 ? 144.619 109.717 112.886 1.00 44.88 ? 310 ALA C O     1 
ATOM   11122 C  CB    . ALA C 2 331 ? 143.065 111.150 110.458 1.00 44.94 ? 310 ALA C CB    1 
ATOM   11123 N  N     . THR C 2 332 ? 144.637 108.388 111.063 1.00 40.86 ? 311 THR C N     1 
ATOM   11124 C  CA    . THR C 2 332 ? 145.855 107.690 111.454 1.00 38.81 ? 311 THR C CA    1 
ATOM   11125 C  C     . THR C 2 332 ? 147.011 108.666 111.611 1.00 36.15 ? 311 THR C C     1 
ATOM   11126 O  O     . THR C 2 332 ? 147.241 109.518 110.749 1.00 43.30 ? 311 THR C O     1 
ATOM   11127 C  CB    . THR C 2 332 ? 146.203 106.616 110.420 1.00 39.78 ? 311 THR C CB    1 
ATOM   11128 O  OG1   . THR C 2 332 ? 145.140 105.658 110.348 1.00 41.99 ? 311 THR C OG1   1 
ATOM   11129 C  CG2   . THR C 2 332 ? 147.495 105.908 110.797 1.00 37.37 ? 311 THR C CG2   1 
ATOM   11130 N  N     . VAL C 2 333 ? 147.734 108.538 112.718 1.00 29.00 ? 312 VAL C N     1 
ATOM   11131 C  CA    . VAL C 2 333 ? 148.857 109.423 113.008 1.00 27.73 ? 312 VAL C CA    1 
ATOM   11132 C  C     . VAL C 2 333 ? 150.133 108.785 112.475 1.00 34.73 ? 312 VAL C C     1 
ATOM   11133 O  O     . VAL C 2 333 ? 150.508 107.683 112.887 1.00 34.24 ? 312 VAL C O     1 
ATOM   11134 C  CB    . VAL C 2 333 ? 148.964 109.703 114.513 1.00 29.67 ? 312 VAL C CB    1 
ATOM   11135 C  CG1   . VAL C 2 333 ? 150.259 110.436 114.826 1.00 33.09 ? 312 VAL C CG1   1 
ATOM   11136 C  CG2   . VAL C 2 333 ? 147.763 110.504 114.987 1.00 33.00 ? 312 VAL C CG2   1 
ATOM   11137 N  N     . GLU C 2 334 ? 150.799 109.477 111.555 1.00 31.99 ? 313 GLU C N     1 
ATOM   11138 C  CA    . GLU C 2 334 ? 152.047 109.016 110.982 1.00 30.19 ? 313 GLU C CA    1 
ATOM   11139 C  C     . GLU C 2 334 ? 153.123 110.069 111.206 1.00 35.47 ? 313 GLU C C     1 
ATOM   11140 O  O     . GLU C 2 334 ? 152.915 111.241 110.858 1.00 39.91 ? 313 GLU C O     1 
ATOM   11141 C  CB    . GLU C 2 334 ? 151.889 108.730 109.480 1.00 31.98 ? 313 GLU C CB    1 
ATOM   11142 C  CG    . GLU C 2 334 ? 152.924 107.770 108.920 1.00 30.40 ? 313 GLU C CG    1 
ATOM   11143 C  CD    . GLU C 2 334 ? 152.952 107.758 107.405 1.00 36.69 ? 313 GLU C CD    1 
ATOM   11144 O  OE1   . GLU C 2 334 ? 151.867 107.750 106.789 1.00 35.22 ? 313 GLU C OE1   1 
ATOM   11145 O  OE2   . GLU C 2 334 ? 154.060 107.738 106.829 1.00 37.50 ? 313 GLU C OE2   1 
ATOM   11146 N  N     . PRO C 2 335 ? 154.265 109.709 111.785 1.00 33.23 ? 314 PRO C N     1 
ATOM   11147 C  CA    . PRO C 2 335 ? 155.282 110.718 112.098 1.00 32.48 ? 314 PRO C CA    1 
ATOM   11148 C  C     . PRO C 2 335 ? 155.861 111.354 110.845 1.00 32.75 ? 314 PRO C C     1 
ATOM   11149 O  O     . PRO C 2 335 ? 155.962 110.729 109.787 1.00 33.62 ? 314 PRO C O     1 
ATOM   11150 C  CB    . PRO C 2 335 ? 156.348 109.921 112.858 1.00 27.14 ? 314 PRO C CB    1 
ATOM   11151 C  CG    . PRO C 2 335 ? 156.188 108.526 112.359 1.00 33.25 ? 314 PRO C CG    1 
ATOM   11152 C  CD    . PRO C 2 335 ? 154.712 108.349 112.133 1.00 31.97 ? 314 PRO C CD    1 
ATOM   11153 N  N     . LEU C 2 336 ? 156.240 112.622 110.981 1.00 31.37 ? 315 LEU C N     1 
ATOM   11154 C  CA    . LEU C 2 336 ? 156.857 113.355 109.887 1.00 25.32 ? 315 LEU C CA    1 
ATOM   11155 C  C     . LEU C 2 336 ? 158.296 112.903 109.689 1.00 30.05 ? 315 LEU C C     1 
ATOM   11156 O  O     . LEU C 2 336 ? 159.050 112.738 110.652 1.00 28.04 ? 315 LEU C O     1 
ATOM   11157 C  CB    . LEU C 2 336 ? 156.825 114.857 110.165 1.00 24.68 ? 315 LEU C CB    1 
ATOM   11158 C  CG    . LEU C 2 336 ? 155.623 115.665 109.681 1.00 29.53 ? 315 LEU C CG    1 
ATOM   11159 C  CD1   . LEU C 2 336 ? 155.571 116.993 110.416 1.00 23.58 ? 315 LEU C CD1   1 
ATOM   11160 C  CD2   . LEU C 2 336 ? 155.686 115.883 108.181 1.00 23.76 ? 315 LEU C CD2   1 
ATOM   11161 N  N     . LYS C 2 337 ? 158.677 112.710 108.432 1.00 29.08 ? 316 LYS C N     1 
ATOM   11162 C  CA    . LYS C 2 337 ? 160.052 112.387 108.095 1.00 24.90 ? 316 LYS C CA    1 
ATOM   11163 C  C     . LYS C 2 337 ? 160.836 113.663 107.800 1.00 25.51 ? 316 LYS C C     1 
ATOM   11164 O  O     . LYS C 2 337 ? 160.274 114.745 107.622 1.00 33.13 ? 316 LYS C O     1 
ATOM   11165 C  CB    . LYS C 2 337 ? 160.108 111.439 106.897 1.00 29.23 ? 316 LYS C CB    1 
ATOM   11166 C  CG    . LYS C 2 337 ? 159.185 110.239 106.998 1.00 29.66 ? 316 LYS C CG    1 
ATOM   11167 C  CD    . LYS C 2 337 ? 159.615 109.140 106.039 1.00 30.93 ? 316 LYS C CD    1 
ATOM   11168 C  CE    . LYS C 2 337 ? 159.020 107.797 106.428 1.00 33.14 ? 316 LYS C CE    1 
ATOM   11169 N  NZ    . LYS C 2 337 ? 157.658 107.941 107.014 1.00 33.67 ? 316 LYS C NZ    1 
ATOM   11170 N  N     . ASP C 2 338 ? 162.162 113.525 107.758 1.00 26.51 ? 317 ASP C N     1 
ATOM   11171 C  CA    . ASP C 2 338 ? 163.004 114.657 107.391 1.00 29.94 ? 317 ASP C CA    1 
ATOM   11172 C  C     . ASP C 2 338 ? 162.754 115.079 105.950 1.00 29.65 ? 317 ASP C C     1 
ATOM   11173 O  O     . ASP C 2 338 ? 162.715 116.275 105.642 1.00 24.94 ? 317 ASP C O     1 
ATOM   11174 C  CB    . ASP C 2 338 ? 164.477 114.309 107.603 1.00 32.12 ? 317 ASP C CB    1 
ATOM   11175 C  CG    . ASP C 2 338 ? 164.951 114.615 109.009 1.00 35.61 ? 317 ASP C CG    1 
ATOM   11176 O  OD1   . ASP C 2 338 ? 164.748 113.767 109.904 1.00 36.45 ? 317 ASP C OD1   1 
ATOM   11177 O  OD2   . ASP C 2 338 ? 165.526 115.703 109.222 1.00 32.88 ? 317 ASP C OD2   1 
ATOM   11178 N  N     . ASP C 2 339 ? 162.571 114.108 105.053 1.00 31.98 ? 318 ASP C N     1 
ATOM   11179 C  CA    . ASP C 2 339 ? 162.343 114.404 103.644 1.00 23.82 ? 318 ASP C CA    1 
ATOM   11180 C  C     . ASP C 2 339 ? 160.994 115.061 103.384 1.00 21.90 ? 318 ASP C C     1 
ATOM   11181 O  O     . ASP C 2 339 ? 160.779 115.572 102.279 1.00 29.62 ? 318 ASP C O     1 
ATOM   11182 C  CB    . ASP C 2 339 ? 162.459 113.122 102.816 1.00 24.61 ? 318 ASP C CB    1 
ATOM   11183 C  CG    . ASP C 2 339 ? 163.890 112.636 102.694 1.00 36.61 ? 318 ASP C CG    1 
ATOM   11184 O  OD1   . ASP C 2 339 ? 164.809 113.481 102.692 1.00 34.94 ? 318 ASP C OD1   1 
ATOM   11185 O  OD2   . ASP C 2 339 ? 164.095 111.407 102.600 1.00 37.02 ? 318 ASP C OD2   1 
ATOM   11186 N  N     . ASP C 2 340 ? 160.083 115.056 104.358 1.00 21.75 ? 319 ASP C N     1 
ATOM   11187 C  CA    . ASP C 2 340 ? 158.793 115.714 104.192 1.00 12.52 ? 319 ASP C CA    1 
ATOM   11188 C  C     . ASP C 2 340 ? 158.902 117.232 104.189 1.00 11.68 ? 319 ASP C C     1 
ATOM   11189 O  O     . ASP C 2 340 ? 157.961 117.901 103.749 1.00 29.94 ? 319 ASP C O     1 
ATOM   11190 C  CB    . ASP C 2 340 ? 157.835 115.276 105.299 1.00 15.38 ? 319 ASP C CB    1 
ATOM   11191 C  CG    . ASP C 2 340 ? 157.343 113.859 105.115 1.00 27.80 ? 319 ASP C CG    1 
ATOM   11192 O  OD1   . ASP C 2 340 ? 156.633 113.358 106.010 1.00 35.11 ? 319 ASP C OD1   1 
ATOM   11193 O  OD2   . ASP C 2 340 ? 157.663 113.246 104.075 1.00 32.85 ? 319 ASP C OD2   1 
ATOM   11194 N  N     . PHE C 2 341 ? 160.013 117.785 104.665 1.00 19.10 ? 320 PHE C N     1 
ATOM   11195 C  CA    . PHE C 2 341 ? 160.195 119.225 104.770 1.00 9.08  ? 320 PHE C CA    1 
ATOM   11196 C  C     . PHE C 2 341 ? 160.883 119.829 103.555 1.00 17.46 ? 320 PHE C C     1 
ATOM   11197 O  O     . PHE C 2 341 ? 161.087 121.046 103.519 1.00 21.47 ? 320 PHE C O     1 
ATOM   11198 C  CB    . PHE C 2 341 ? 160.991 119.557 106.033 1.00 14.57 ? 320 PHE C CB    1 
ATOM   11199 C  CG    . PHE C 2 341 ? 160.221 119.351 107.303 1.00 10.84 ? 320 PHE C CG    1 
ATOM   11200 C  CD1   . PHE C 2 341 ? 159.506 120.389 107.870 1.00 9.48  ? 320 PHE C CD1   1 
ATOM   11201 C  CD2   . PHE C 2 341 ? 160.205 118.115 107.926 1.00 12.36 ? 320 PHE C CD2   1 
ATOM   11202 C  CE1   . PHE C 2 341 ? 158.794 120.201 109.037 1.00 7.91  ? 320 PHE C CE1   1 
ATOM   11203 C  CE2   . PHE C 2 341 ? 159.494 117.922 109.091 1.00 13.16 ? 320 PHE C CE2   1 
ATOM   11204 C  CZ    . PHE C 2 341 ? 158.788 118.966 109.647 1.00 4.56  ? 320 PHE C CZ    1 
ATOM   11205 N  N     . TYR C 2 342 ? 161.245 119.019 102.565 1.00 9.53  ? 321 TYR C N     1 
ATOM   11206 C  CA    . TYR C 2 342 ? 161.865 119.508 101.344 1.00 17.23 ? 321 TYR C CA    1 
ATOM   11207 C  C     . TYR C 2 342 ? 161.054 119.055 100.141 1.00 16.10 ? 321 TYR C C     1 
ATOM   11208 O  O     . TYR C 2 342 ? 160.477 117.965 100.130 1.00 16.88 ? 321 TYR C O     1 
ATOM   11209 C  CB    . TYR C 2 342 ? 163.331 119.048 101.197 1.00 17.88 ? 321 TYR C CB    1 
ATOM   11210 C  CG    . TYR C 2 342 ? 164.154 119.107 102.467 1.00 13.83 ? 321 TYR C CG    1 
ATOM   11211 C  CD1   . TYR C 2 342 ? 163.988 118.176 103.483 1.00 18.12 ? 321 TYR C CD1   1 
ATOM   11212 C  CD2   . TYR C 2 342 ? 165.096 120.109 102.650 1.00 16.03 ? 321 TYR C CD2   1 
ATOM   11213 C  CE1   . TYR C 2 342 ? 164.742 118.240 104.639 1.00 15.48 ? 321 TYR C CE1   1 
ATOM   11214 C  CE2   . TYR C 2 342 ? 165.852 120.180 103.802 1.00 17.80 ? 321 TYR C CE2   1 
ATOM   11215 C  CZ    . TYR C 2 342 ? 165.671 119.244 104.793 1.00 19.62 ? 321 TYR C CZ    1 
ATOM   11216 O  OH    . TYR C 2 342 ? 166.423 119.310 105.943 1.00 28.71 ? 321 TYR C OH    1 
ATOM   11217 N  N     . PHE C 2 343 ? 161.016 119.914 99.128  1.00 7.71  ? 322 PHE C N     1 
ATOM   11218 C  CA    . PHE C 2 343 ? 160.174 119.698 97.960  1.00 20.35 ? 322 PHE C CA    1 
ATOM   11219 C  C     . PHE C 2 343 ? 160.938 119.993 96.674  1.00 25.47 ? 322 PHE C C     1 
ATOM   11220 O  O     . PHE C 2 343 ? 161.920 120.734 96.678  1.00 26.11 ? 322 PHE C O     1 
ATOM   11221 C  CB    . PHE C 2 343 ? 158.922 120.572 98.050  1.00 15.28 ? 322 PHE C CB    1 
ATOM   11222 C  CG    . PHE C 2 343 ? 158.139 120.374 99.315  1.00 13.74 ? 322 PHE C CG    1 
ATOM   11223 C  CD1   . PHE C 2 343 ? 157.229 119.339 99.427  1.00 17.31 ? 322 PHE C CD1   1 
ATOM   11224 C  CD2   . PHE C 2 343 ? 158.329 121.211 100.399 1.00 4.75  ? 322 PHE C CD2   1 
ATOM   11225 C  CE1   . PHE C 2 343 ? 156.515 119.152 100.592 1.00 16.31 ? 322 PHE C CE1   1 
ATOM   11226 C  CE2   . PHE C 2 343 ? 157.621 121.027 101.565 1.00 5.64  ? 322 PHE C CE2   1 
ATOM   11227 C  CZ    . PHE C 2 343 ? 156.711 119.997 101.662 1.00 10.19 ? 322 PHE C CZ    1 
ATOM   11228 N  N     . LYS D 2 330 ? 117.446 117.738 149.167 1.00 61.72 ? 309 LYS D N     1 
ATOM   11229 C  CA    . LYS D 2 330 ? 116.143 117.086 149.152 1.00 61.83 ? 309 LYS D CA    1 
ATOM   11230 C  C     . LYS D 2 330 ? 115.780 116.565 150.535 1.00 62.21 ? 309 LYS D C     1 
ATOM   11231 O  O     . LYS D 2 330 ? 116.017 115.394 150.835 1.00 61.32 ? 309 LYS D O     1 
ATOM   11232 C  CB    . LYS D 2 330 ? 116.128 115.924 148.155 1.00 59.60 ? 309 LYS D CB    1 
ATOM   11233 C  CG    . LYS D 2 330 ? 116.722 116.232 146.794 1.00 60.95 ? 309 LYS D CG    1 
ATOM   11234 C  CD    . LYS D 2 330 ? 115.711 115.992 145.684 1.00 60.77 ? 309 LYS D CD    1 
ATOM   11235 C  CE    . LYS D 2 330 ? 116.150 116.646 144.385 1.00 61.40 ? 309 LYS D CE    1 
ATOM   11236 N  NZ    . LYS D 2 330 ? 115.351 117.861 144.071 1.00 62.04 ? 309 LYS D NZ    1 
ATOM   11237 N  N     . ALA D 2 331 ? 115.217 117.417 151.391 1.00 57.72 ? 310 ALA D N     1 
ATOM   11238 C  CA    . ALA D 2 331 ? 114.813 116.947 152.708 1.00 58.04 ? 310 ALA D CA    1 
ATOM   11239 C  C     . ALA D 2 331 ? 113.453 116.261 152.686 1.00 58.14 ? 310 ALA D C     1 
ATOM   11240 O  O     . ALA D 2 331 ? 113.379 115.040 152.857 1.00 58.87 ? 310 ALA D O     1 
ATOM   11241 C  CB    . ALA D 2 331 ? 114.793 118.116 153.700 1.00 56.57 ? 310 ALA D CB    1 
ATOM   11242 N  N     . THR D 2 332 ? 112.376 117.021 152.473 1.00 46.15 ? 311 THR D N     1 
ATOM   11243 C  CA    . THR D 2 332 ? 111.062 116.479 152.138 1.00 42.78 ? 311 THR D CA    1 
ATOM   11244 C  C     . THR D 2 332 ? 110.122 117.594 151.687 1.00 42.27 ? 311 THR D C     1 
ATOM   11245 O  O     . THR D 2 332 ? 109.795 118.489 152.474 1.00 45.09 ? 311 THR D O     1 
ATOM   11246 C  CB    . THR D 2 332 ? 110.471 115.697 153.318 1.00 46.86 ? 311 THR D CB    1 
ATOM   11247 O  OG1   . THR D 2 332 ? 109.287 115.002 152.904 1.00 46.97 ? 311 THR D OG1   1 
ATOM   11248 C  CG2   . THR D 2 332 ? 110.183 116.605 154.497 1.00 43.65 ? 311 THR D CG2   1 
ATOM   11249 N  N     . VAL D 2 333 ? 109.680 117.554 150.432 1.00 39.49 ? 312 VAL D N     1 
ATOM   11250 C  CA    . VAL D 2 333 ? 108.747 118.552 149.920 1.00 35.97 ? 312 VAL D CA    1 
ATOM   11251 C  C     . VAL D 2 333 ? 107.397 118.382 150.606 1.00 40.19 ? 312 VAL D C     1 
ATOM   11252 O  O     . VAL D 2 333 ? 106.815 117.291 150.591 1.00 43.38 ? 312 VAL D O     1 
ATOM   11253 C  CB    . VAL D 2 333 ? 108.605 118.453 148.390 1.00 38.60 ? 312 VAL D CB    1 
ATOM   11254 C  CG1   . VAL D 2 333 ? 107.284 119.056 147.931 1.00 39.63 ? 312 VAL D CG1   1 
ATOM   11255 C  CG2   . VAL D 2 333 ? 109.774 119.138 147.703 1.00 39.03 ? 312 VAL D CG2   1 
ATOM   11256 N  N     . GLU D 2 334 ? 106.895 119.453 151.218 1.00 39.20 ? 313 GLU D N     1 
ATOM   11257 C  CA    . GLU D 2 334 ? 105.562 119.463 151.813 1.00 36.81 ? 313 GLU D CA    1 
ATOM   11258 C  C     . GLU D 2 334 ? 104.864 120.747 151.385 1.00 37.73 ? 313 GLU D C     1 
ATOM   11259 O  O     . GLU D 2 334 ? 105.460 121.838 151.492 1.00 40.12 ? 313 GLU D O     1 
ATOM   11260 C  CB    . GLU D 2 334 ? 105.617 119.353 153.338 1.00 34.61 ? 313 GLU D CB    1 
ATOM   11261 C  CG    . GLU D 2 334 ? 104.246 119.187 153.976 1.00 37.90 ? 313 GLU D CG    1 
ATOM   11262 C  CD    . GLU D 2 334 ? 104.299 119.052 155.484 1.00 39.43 ? 313 GLU D CD    1 
ATOM   11263 O  OE1   . GLU D 2 334 ? 105.411 118.967 156.037 1.00 37.54 ? 313 GLU D OE1   1 
ATOM   11264 O  OE2   . GLU D 2 334 ? 103.224 119.027 156.117 1.00 39.69 ? 313 GLU D OE2   1 
ATOM   11265 N  N     . PRO D 2 335 ? 103.629 120.679 150.895 1.00 38.18 ? 314 PRO D N     1 
ATOM   11266 C  CA    . PRO D 2 335 ? 102.947 121.895 150.443 1.00 40.62 ? 314 PRO D CA    1 
ATOM   11267 C  C     . PRO D 2 335 ? 102.547 122.793 151.603 1.00 40.02 ? 314 PRO D C     1 
ATOM   11268 O  O     . PRO D 2 335 ? 102.376 122.347 152.739 1.00 41.11 ? 314 PRO D O     1 
ATOM   11269 C  CB    . PRO D 2 335 ? 101.714 121.355 149.713 1.00 37.91 ? 314 PRO D CB    1 
ATOM   11270 C  CG    . PRO D 2 335 ? 101.451 120.042 150.370 1.00 34.58 ? 314 PRO D CG    1 
ATOM   11271 C  CD    . PRO D 2 335 ? 102.806 119.475 150.687 1.00 36.60 ? 314 PRO D CD    1 
ATOM   11272 N  N     . LEU D 2 336 ? 102.408 124.081 151.299 1.00 34.57 ? 315 LEU D N     1 
ATOM   11273 C  CA    . LEU D 2 336 ? 101.853 125.033 152.250 1.00 30.08 ? 315 LEU D CA    1 
ATOM   11274 C  C     . LEU D 2 336 ? 100.337 124.888 152.276 1.00 33.20 ? 315 LEU D C     1 
ATOM   11275 O  O     . LEU D 2 336 ? 99.668  125.100 151.260 1.00 37.22 ? 315 LEU D O     1 
ATOM   11276 C  CB    . LEU D 2 336 ? 102.247 126.460 151.868 1.00 28.04 ? 315 LEU D CB    1 
ATOM   11277 C  CG    . LEU D 2 336 ? 103.664 126.909 152.225 1.00 27.76 ? 315 LEU D CG    1 
ATOM   11278 C  CD1   . LEU D 2 336 ? 104.113 128.034 151.307 1.00 24.11 ? 315 LEU D CD1   1 
ATOM   11279 C  CD2   . LEU D 2 336 ? 103.732 127.343 153.677 1.00 29.08 ? 315 LEU D CD2   1 
ATOM   11280 N  N     . LYS D 2 337 ? 99.795  124.528 153.438 1.00 36.25 ? 316 LYS D N     1 
ATOM   11281 C  CA    . LYS D 2 337 ? 98.385  124.180 153.569 1.00 47.76 ? 316 LYS D CA    1 
ATOM   11282 C  C     . LYS D 2 337 ? 97.587  125.290 154.244 1.00 47.26 ? 316 LYS D C     1 
ATOM   11283 O  O     . LYS D 2 337 ? 96.655  125.014 155.003 1.00 51.37 ? 316 LYS D O     1 
ATOM   11284 C  CB    . LYS D 2 337 ? 98.225  122.869 154.336 1.00 44.37 ? 316 LYS D CB    1 
ATOM   11285 C  CG    . LYS D 2 337 ? 99.172  122.729 155.516 1.00 46.03 ? 316 LYS D CG    1 
ATOM   11286 C  CD    . LYS D 2 337 ? 99.597  121.285 155.720 1.00 46.40 ? 316 LYS D CD    1 
ATOM   11287 C  CE    . LYS D 2 337 ? 100.144 120.686 154.435 1.00 45.29 ? 316 LYS D CE    1 
ATOM   11288 N  NZ    . LYS D 2 337 ? 100.980 119.484 154.694 1.00 42.09 ? 316 LYS D NZ    1 
ATOM   11289 N  N     . ASP D 2 338 ? 97.951  126.546 153.976 1.00 29.55 ? 317 ASP D N     1 
ATOM   11290 C  CA    . ASP D 2 338 ? 97.313  127.719 154.568 1.00 32.48 ? 317 ASP D CA    1 
ATOM   11291 C  C     . ASP D 2 338 ? 97.464  127.738 156.085 1.00 37.94 ? 317 ASP D C     1 
ATOM   11292 O  O     . ASP D 2 338 ? 97.908  126.754 156.687 1.00 40.84 ? 317 ASP D O     1 
ATOM   11293 C  CB    . ASP D 2 338 ? 95.835  127.794 154.177 1.00 36.01 ? 317 ASP D CB    1 
ATOM   11294 C  CG    . ASP D 2 338 ? 95.318  129.216 154.140 1.00 38.86 ? 317 ASP D CG    1 
ATOM   11295 O  OD1   . ASP D 2 338 ? 96.121  130.143 154.378 1.00 36.19 ? 317 ASP D OD1   1 
ATOM   11296 O  OD2   . ASP D 2 338 ? 94.113  129.408 153.874 1.00 34.94 ? 317 ASP D OD2   1 
ATOM   11297 N  N     . ASP D 2 339 ? 97.146  128.881 156.699 1.00 32.37 ? 318 ASP D N     1 
ATOM   11298 C  CA    . ASP D 2 339 ? 97.327  129.120 158.130 1.00 28.49 ? 318 ASP D CA    1 
ATOM   11299 C  C     . ASP D 2 339 ? 98.810  129.157 158.481 1.00 28.80 ? 318 ASP D C     1 
ATOM   11300 O  O     . ASP D 2 339 ? 99.178  129.423 159.629 1.00 36.28 ? 318 ASP D O     1 
ATOM   11301 C  CB    . ASP D 2 339 ? 96.594  128.072 158.972 1.00 30.55 ? 318 ASP D CB    1 
ATOM   11302 C  CG    . ASP D 2 339 ? 95.730  128.694 160.052 1.00 37.05 ? 318 ASP D CG    1 
ATOM   11303 O  OD1   . ASP D 2 339 ? 96.103  129.770 160.566 1.00 32.14 ? 318 ASP D OD1   1 
ATOM   11304 O  OD2   . ASP D 2 339 ? 94.678  128.109 160.386 1.00 39.30 ? 318 ASP D OD2   1 
ATOM   11305 N  N     . ASP D 2 340 ? 99.666  128.891 157.495 1.00 24.72 ? 319 ASP D N     1 
ATOM   11306 C  CA    . ASP D 2 340 ? 101.095 129.127 157.604 1.00 24.52 ? 319 ASP D CA    1 
ATOM   11307 C  C     . ASP D 2 340 ? 101.466 130.556 157.245 1.00 21.51 ? 319 ASP D C     1 
ATOM   11308 O  O     . ASP D 2 340 ? 102.605 130.968 157.485 1.00 32.71 ? 319 ASP D O     1 
ATOM   11309 C  CB    . ASP D 2 340 ? 101.861 128.155 156.701 1.00 23.05 ? 319 ASP D CB    1 
ATOM   11310 C  CG    . ASP D 2 340 ? 101.748 126.716 157.164 1.00 28.00 ? 319 ASP D CG    1 
ATOM   11311 O  OD1   . ASP D 2 340 ? 101.628 126.489 158.386 1.00 34.28 ? 319 ASP D OD1   1 
ATOM   11312 O  OD2   . ASP D 2 340 ? 101.778 125.810 156.306 1.00 31.08 ? 319 ASP D OD2   1 
ATOM   11313 N  N     . PHE D 2 341 ? 100.530 131.310 156.673 1.00 10.52 ? 320 PHE D N     1 
ATOM   11314 C  CA    . PHE D 2 341 ? 100.708 132.720 156.370 1.00 15.27 ? 320 PHE D CA    1 
ATOM   11315 C  C     . PHE D 2 341 ? 100.149 133.618 157.461 1.00 12.85 ? 320 PHE D C     1 
ATOM   11316 O  O     . PHE D 2 341 ? 100.203 134.844 157.327 1.00 22.40 ? 320 PHE D O     1 
ATOM   11317 C  CB    . PHE D 2 341 ? 100.039 133.058 155.034 1.00 21.01 ? 320 PHE D CB    1 
ATOM   11318 C  CG    . PHE D 2 341 ? 100.614 132.317 153.859 1.00 15.79 ? 320 PHE D CG    1 
ATOM   11319 C  CD1   . PHE D 2 341 ? 100.174 131.043 153.547 1.00 11.88 ? 320 PHE D CD1   1 
ATOM   11320 C  CD2   . PHE D 2 341 ? 101.585 132.897 153.064 1.00 9.87  ? 320 PHE D CD2   1 
ATOM   11321 C  CE1   . PHE D 2 341 ? 100.698 130.360 152.470 1.00 13.02 ? 320 PHE D CE1   1 
ATOM   11322 C  CE2   . PHE D 2 341 ? 102.111 132.218 151.984 1.00 10.78 ? 320 PHE D CE2   1 
ATOM   11323 C  CZ    . PHE D 2 341 ? 101.668 130.948 151.688 1.00 4.79  ? 320 PHE D CZ    1 
ATOM   11324 N  N     . TYR D 2 342 ? 99.615  133.037 158.531 1.00 12.46 ? 321 TYR D N     1 
ATOM   11325 C  CA    . TYR D 2 342 ? 99.014  133.783 159.625 1.00 17.95 ? 321 TYR D CA    1 
ATOM   11326 C  C     . TYR D 2 342 ? 99.687  133.380 160.926 1.00 22.41 ? 321 TYR D C     1 
ATOM   11327 O  O     . TYR D 2 342 ? 99.995  132.203 161.136 1.00 24.04 ? 321 TYR D O     1 
ATOM   11328 C  CB    . TYR D 2 342 ? 97.507  133.525 159.707 1.00 13.28 ? 321 TYR D CB    1 
ATOM   11329 C  CG    . TYR D 2 342 ? 96.748  133.982 158.484 1.00 11.63 ? 321 TYR D CG    1 
ATOM   11330 C  CD1   . TYR D 2 342 ? 96.343  135.303 158.346 1.00 16.81 ? 321 TYR D CD1   1 
ATOM   11331 C  CD2   . TYR D 2 342 ? 96.442  133.093 157.463 1.00 15.94 ? 321 TYR D CD2   1 
ATOM   11332 C  CE1   . TYR D 2 342 ? 95.651  135.723 157.227 1.00 20.80 ? 321 TYR D CE1   1 
ATOM   11333 C  CE2   . TYR D 2 342 ? 95.751  133.504 156.341 1.00 15.55 ? 321 TYR D CE2   1 
ATOM   11334 C  CZ    . TYR D 2 342 ? 95.358  134.820 156.228 1.00 24.69 ? 321 TYR D CZ    1 
ATOM   11335 O  OH    . TYR D 2 342 ? 94.668  135.236 155.112 1.00 21.45 ? 321 TYR D OH    1 
ATOM   11336 N  N     . PHE D 2 343 ? 99.920  134.359 161.792 1.00 12.93 ? 322 PHE D N     1 
ATOM   11337 C  CA    . PHE D 2 343 ? 100.625 134.117 163.045 1.00 18.66 ? 322 PHE D CA    1 
ATOM   11338 C  C     . PHE D 2 343 ? 99.954  134.848 164.202 1.00 24.79 ? 322 PHE D C     1 
ATOM   11339 O  O     . PHE D 2 343 ? 99.650  136.036 164.109 1.00 23.91 ? 322 PHE D O     1 
ATOM   11340 C  CB    . PHE D 2 343 ? 102.091 134.548 162.924 1.00 13.99 ? 322 PHE D CB    1 
ATOM   11341 C  CG    . PHE D 2 343 ? 102.748 134.107 161.647 1.00 14.21 ? 322 PHE D CG    1 
ATOM   11342 C  CD1   . PHE D 2 343 ? 102.722 134.913 160.522 1.00 13.48 ? 322 PHE D CD1   1 
ATOM   11343 C  CD2   . PHE D 2 343 ? 103.389 132.884 161.571 1.00 16.65 ? 322 PHE D CD2   1 
ATOM   11344 C  CE1   . PHE D 2 343 ? 103.320 134.505 159.348 1.00 9.34  ? 322 PHE D CE1   1 
ATOM   11345 C  CE2   . PHE D 2 343 ? 103.988 132.473 160.399 1.00 9.50  ? 322 PHE D CE2   1 
ATOM   11346 C  CZ    . PHE D 2 343 ? 103.953 133.285 159.288 1.00 5.03  ? 322 PHE D CZ    1 
HETATM 11347 P  PA    . TTP E 3 .   ? 146.280 143.675 134.203 1.00 19.44 ? 801 TTP A PA    1 
HETATM 11348 O  O1A   . TTP E 3 .   ? 144.865 144.179 134.090 1.00 22.91 ? 801 TTP A O1A   1 
HETATM 11349 O  O2A   . TTP E 3 .   ? 147.203 144.456 133.302 1.00 26.72 ? 801 TTP A O2A   1 
HETATM 11350 O  O3A   . TTP E 3 .   ? 146.762 143.675 135.736 1.00 35.07 ? 801 TTP A O3A   1 
HETATM 11351 P  PB    . TTP E 3 .   ? 147.875 144.700 136.279 1.00 29.75 ? 801 TTP A PB    1 
HETATM 11352 O  O1B   . TTP E 3 .   ? 147.519 145.140 137.676 1.00 34.30 ? 801 TTP A O1B   1 
HETATM 11353 O  O2B   . TTP E 3 .   ? 148.058 145.900 135.387 1.00 25.93 ? 801 TTP A O2B   1 
HETATM 11354 O  O3B   . TTP E 3 .   ? 149.174 143.752 136.289 1.00 28.87 ? 801 TTP A O3B   1 
HETATM 11355 P  PG    . TTP E 3 .   ? 150.548 144.184 135.576 1.00 32.89 ? 801 TTP A PG    1 
HETATM 11356 O  O1G   . TTP E 3 .   ? 150.269 144.699 134.186 1.00 33.74 ? 801 TTP A O1G   1 
HETATM 11357 O  O2G   . TTP E 3 .   ? 151.447 142.978 135.487 1.00 23.90 ? 801 TTP A O2G   1 
HETATM 11358 O  O3G   . TTP E 3 .   ? 151.233 145.260 136.382 1.00 35.17 ? 801 TTP A O3G   1 
HETATM 11359 O  "O5'" . TTP E 3 .   ? 146.362 142.114 133.846 1.00 18.70 ? 801 TTP A "O5'" 1 
HETATM 11360 C  "C5'" . TTP E 3 .   ? 147.268 141.695 132.834 1.00 26.50 ? 801 TTP A "C5'" 1 
HETATM 11361 C  "C4'" . TTP E 3 .   ? 147.032 140.232 132.501 1.00 27.90 ? 801 TTP A "C4'" 1 
HETATM 11362 O  "O4'" . TTP E 3 .   ? 146.694 139.511 133.684 1.00 30.58 ? 801 TTP A "O4'" 1 
HETATM 11363 C  "C3'" . TTP E 3 .   ? 145.871 140.072 131.540 1.00 26.13 ? 801 TTP A "C3'" 1 
HETATM 11364 O  "O3'" . TTP E 3 .   ? 146.351 139.760 130.230 1.00 31.45 ? 801 TTP A "O3'" 1 
HETATM 11365 C  "C2'" . TTP E 3 .   ? 145.059 138.914 132.077 1.00 28.98 ? 801 TTP A "C2'" 1 
HETATM 11366 C  "C1'" . TTP E 3 .   ? 145.705 138.521 133.395 1.00 26.00 ? 801 TTP A "C1'" 1 
HETATM 11367 N  N1    . TTP E 3 .   ? 144.697 138.493 134.453 1.00 26.56 ? 801 TTP A N1    1 
HETATM 11368 C  C2    . TTP E 3 .   ? 144.081 137.270 134.797 1.00 30.84 ? 801 TTP A C2    1 
HETATM 11369 O  O2    . TTP E 3 .   ? 144.412 136.227 134.196 1.00 28.88 ? 801 TTP A O2    1 
HETATM 11370 N  N3    . TTP E 3 .   ? 143.155 137.202 135.761 1.00 28.97 ? 801 TTP A N3    1 
HETATM 11371 C  C4    . TTP E 3 .   ? 142.784 138.301 136.421 1.00 32.59 ? 801 TTP A C4    1 
HETATM 11372 O  O4    . TTP E 3 .   ? 141.919 138.239 137.319 1.00 33.84 ? 801 TTP A O4    1 
HETATM 11373 C  C5    . TTP E 3 .   ? 143.414 139.596 136.077 1.00 26.59 ? 801 TTP A C5    1 
HETATM 11374 C  C5M   . TTP E 3 .   ? 143.025 140.855 136.799 1.00 27.25 ? 801 TTP A C5M   1 
HETATM 11375 C  C6    . TTP E 3 .   ? 144.369 139.628 135.075 1.00 25.72 ? 801 TTP A C6    1 
HETATM 11376 MG MG    . MG  F 4 .   ? 148.504 145.983 132.949 1.00 25.23 ? 802 MG  A MG    1 
HETATM 11377 P  PG    . ATP G 5 .   ? 109.354 133.180 77.529  1.00 73.27 ? 803 ATP A PG    1 
HETATM 11378 O  O1G   . ATP G 5 .   ? 109.846 134.072 76.440  1.00 64.02 ? 803 ATP A O1G   1 
HETATM 11379 O  O2G   . ATP G 5 .   ? 108.819 131.834 77.029  1.00 64.53 ? 803 ATP A O2G   1 
HETATM 11380 O  O3G   . ATP G 5 .   ? 110.388 132.929 78.632  1.00 61.68 ? 803 ATP A O3G   1 
HETATM 11381 P  PB    . ATP G 5 .   ? 107.800 134.687 79.603  1.00 72.64 ? 803 ATP A PB    1 
HETATM 11382 O  O1B   . ATP G 5 .   ? 108.618 135.914 79.681  1.00 64.50 ? 803 ATP A O1B   1 
HETATM 11383 O  O2B   . ATP G 5 .   ? 106.288 134.904 79.654  1.00 63.63 ? 803 ATP A O2B   1 
HETATM 11384 O  O3B   . ATP G 5 .   ? 108.114 133.850 78.286  1.00 67.12 ? 803 ATP A O3B   1 
HETATM 11385 P  PA    . ATP G 5 .   ? 107.406 132.559 81.627  1.00 71.60 ? 803 ATP A PA    1 
HETATM 11386 O  O1A   . ATP G 5 .   ? 108.045 131.231 81.531  1.00 64.62 ? 803 ATP A O1A   1 
HETATM 11387 O  O2A   . ATP G 5 .   ? 105.936 132.590 81.207  1.00 62.50 ? 803 ATP A O2A   1 
HETATM 11388 O  O3A   . ATP G 5 .   ? 108.172 133.646 80.749  1.00 64.21 ? 803 ATP A O3A   1 
HETATM 11389 O  "O5'" . ATP G 5 .   ? 107.516 133.154 83.085  1.00 62.90 ? 803 ATP A "O5'" 1 
HETATM 11390 C  "C5'" . ATP G 5 .   ? 106.630 134.200 83.535  1.00 61.99 ? 803 ATP A "C5'" 1 
HETATM 11391 C  "C4'" . ATP G 5 .   ? 107.335 135.028 84.579  1.00 62.42 ? 803 ATP A "C4'" 1 
HETATM 11392 O  "O4'" . ATP G 5 .   ? 107.808 134.169 85.639  1.00 64.29 ? 803 ATP A "O4'" 1 
HETATM 11393 C  "C3'" . ATP G 5 .   ? 108.571 135.775 84.091  1.00 61.80 ? 803 ATP A "C3'" 1 
HETATM 11394 O  "O3'" . ATP G 5 .   ? 108.220 137.042 83.548  1.00 63.13 ? 803 ATP A "O3'" 1 
HETATM 11395 C  "C2'" . ATP G 5 .   ? 109.389 135.921 85.374  1.00 63.15 ? 803 ATP A "C2'" 1 
HETATM 11396 O  "O2'" . ATP G 5 .   ? 108.951 137.026 86.155  1.00 61.70 ? 803 ATP A "O2'" 1 
HETATM 11397 C  "C1'" . ATP G 5 .   ? 109.082 134.601 86.089  1.00 62.50 ? 803 ATP A "C1'" 1 
HETATM 11398 N  N9    . ATP G 5 .   ? 110.047 133.539 85.828  1.00 60.44 ? 803 ATP A N9    1 
HETATM 11399 C  C8    . ATP G 5 .   ? 109.799 132.315 85.264  1.00 61.14 ? 803 ATP A C8    1 
HETATM 11400 N  N7    . ATP G 5 .   ? 110.859 131.553 85.149  1.00 61.42 ? 803 ATP A N7    1 
HETATM 11401 C  C5    . ATP G 5 .   ? 111.879 132.330 85.675  1.00 61.96 ? 803 ATP A C5    1 
HETATM 11402 C  C6    . ATP G 5 .   ? 113.257 132.099 85.848  1.00 58.56 ? 803 ATP A C6    1 
HETATM 11403 N  N6    . ATP G 5 .   ? 113.874 130.968 85.491  1.00 58.53 ? 803 ATP A N6    1 
HETATM 11404 N  N1    . ATP G 5 .   ? 113.993 133.082 86.410  1.00 58.84 ? 803 ATP A N1    1 
HETATM 11405 C  C2    . ATP G 5 .   ? 113.387 134.217 86.765  1.00 59.03 ? 803 ATP A C2    1 
HETATM 11406 N  N3    . ATP G 5 .   ? 112.099 134.547 86.655  1.00 62.53 ? 803 ATP A N3    1 
HETATM 11407 C  C4    . ATP G 5 .   ? 111.394 133.557 86.099  1.00 62.75 ? 803 ATP A C4    1 
HETATM 11408 O  O1B   . DGI H 6 .   ? 105.498 150.323 83.267  1.00 65.61 ? 804 DGI A O1B   1 
HETATM 11409 P  PB    . DGI H 6 .   ? 105.640 151.794 83.589  1.00 74.57 ? 804 DGI A PB    1 
HETATM 11410 O  O2B   . DGI H 6 .   ? 104.320 152.537 83.562  1.00 66.47 ? 804 DGI A O2B   1 
HETATM 11411 O  O3B   . DGI H 6 .   ? 106.715 152.480 82.772  1.00 66.48 ? 804 DGI A O3B   1 
HETATM 11412 O  O3A   . DGI H 6 .   ? 106.146 151.801 85.135  1.00 67.11 ? 804 DGI A O3A   1 
HETATM 11413 P  PA    . DGI H 6 .   ? 106.021 150.973 86.498  1.00 71.84 ? 804 DGI A PA    1 
HETATM 11414 O  O1A   . DGI H 6 .   ? 106.148 151.903 87.640  1.00 65.23 ? 804 DGI A O1A   1 
HETATM 11415 O  O2A   . DGI H 6 .   ? 104.836 150.087 86.416  1.00 65.26 ? 804 DGI A O2A   1 
HETATM 11416 O  "O5'" . DGI H 6 .   ? 107.345 150.085 86.443  1.00 63.58 ? 804 DGI A "O5'" 1 
HETATM 11417 C  "C5'" . DGI H 6 .   ? 108.617 150.709 86.171  1.00 63.31 ? 804 DGI A "C5'" 1 
HETATM 11418 C  "C4'" . DGI H 6 .   ? 109.721 149.726 86.469  1.00 62.84 ? 804 DGI A "C4'" 1 
HETATM 11419 O  "O4'" . DGI H 6 .   ? 109.632 149.300 87.847  1.00 61.58 ? 804 DGI A "O4'" 1 
HETATM 11420 C  "C3'" . DGI H 6 .   ? 109.704 148.454 85.613  1.00 64.74 ? 804 DGI A "C3'" 1 
HETATM 11421 O  "O3'" . DGI H 6 .   ? 111.010 148.179 85.108  1.00 62.95 ? 804 DGI A "O3'" 1 
HETATM 11422 C  "C2'" . DGI H 6 .   ? 109.265 147.371 86.591  1.00 62.89 ? 804 DGI A "C2'" 1 
HETATM 11423 C  "C1'" . DGI H 6 .   ? 109.787 147.898 87.912  1.00 59.20 ? 804 DGI A "C1'" 1 
HETATM 11424 N  N9    . DGI H 6 .   ? 109.051 147.407 89.093  1.00 62.12 ? 804 DGI A N9    1 
HETATM 11425 C  C8    . DGI H 6 .   ? 109.576 146.781 90.192  1.00 63.30 ? 804 DGI A C8    1 
HETATM 11426 N  N7    . DGI H 6 .   ? 108.670 146.445 91.078  1.00 62.72 ? 804 DGI A N7    1 
HETATM 11427 C  C5    . DGI H 6 .   ? 107.475 146.878 90.530  1.00 64.86 ? 804 DGI A C5    1 
HETATM 11428 C  C4    . DGI H 6 .   ? 107.694 147.474 89.307  1.00 63.79 ? 804 DGI A C4    1 
HETATM 11429 N  N3    . DGI H 6 .   ? 106.789 148.019 88.473  1.00 63.96 ? 804 DGI A N3    1 
HETATM 11430 C  C2    . DGI H 6 .   ? 105.546 147.940 88.943  1.00 62.13 ? 804 DGI A C2    1 
HETATM 11431 N  N2    . DGI H 6 .   ? 104.537 148.438 88.227  1.00 62.79 ? 804 DGI A N2    1 
HETATM 11432 N  N1    . DGI H 6 .   ? 105.231 147.367 90.145  1.00 63.16 ? 804 DGI A N1    1 
HETATM 11433 C  C6    . DGI H 6 .   ? 106.138 146.801 91.020  1.00 64.31 ? 804 DGI A C6    1 
HETATM 11434 O  O6    . DGI H 6 .   ? 105.760 146.304 92.081  1.00 63.24 ? 804 DGI A O6    1 
HETATM 11435 P  PA    . TTP I 3 .   ? 119.934 146.642 123.713 1.00 26.75 ? 801 TTP B PA    1 
HETATM 11436 O  O1A   . TTP I 3 .   ? 121.286 146.129 123.292 1.00 21.64 ? 801 TTP B O1A   1 
HETATM 11437 O  O2A   . TTP I 3 .   ? 120.040 148.037 124.274 1.00 29.08 ? 801 TTP B O2A   1 
HETATM 11438 O  O3A   . TTP I 3 .   ? 118.881 146.604 122.499 1.00 40.59 ? 801 TTP B O3A   1 
HETATM 11439 P  PB    . TTP I 3 .   ? 118.875 147.706 121.329 1.00 29.45 ? 801 TTP B PB    1 
HETATM 11440 O  O1B   . TTP I 3 .   ? 119.714 147.251 120.163 1.00 31.02 ? 801 TTP B O1B   1 
HETATM 11441 O  O2B   . TTP I 3 .   ? 119.336 149.055 121.818 1.00 30.29 ? 801 TTP B O2B   1 
HETATM 11442 O  O3B   . TTP I 3 .   ? 117.321 147.746 120.928 1.00 31.25 ? 801 TTP B O3B   1 
HETATM 11443 P  PG    . TTP I 3 .   ? 116.208 148.013 122.059 1.00 28.17 ? 801 TTP B PG    1 
HETATM 11444 O  O1G   . TTP I 3 .   ? 115.742 146.689 122.606 1.00 28.15 ? 801 TTP B O1G   1 
HETATM 11445 O  O2G   . TTP I 3 .   ? 115.027 148.735 121.462 1.00 34.00 ? 801 TTP B O2G   1 
HETATM 11446 O  O3G   . TTP I 3 .   ? 116.802 148.835 123.176 1.00 27.89 ? 801 TTP B O3G   1 
HETATM 11447 O  "O5'" . TTP I 3 .   ? 119.247 145.652 124.775 1.00 23.35 ? 801 TTP B "O5'" 1 
HETATM 11448 C  "C5'" . TTP I 3 .   ? 118.502 144.532 124.310 1.00 23.28 ? 801 TTP B "C5'" 1 
HETATM 11449 C  "C4'" . TTP I 3 .   ? 118.378 143.509 125.426 1.00 25.98 ? 801 TTP B "C4'" 1 
HETATM 11450 O  "O4'" . TTP I 3 .   ? 118.430 142.211 124.837 1.00 35.74 ? 801 TTP B "O4'" 1 
HETATM 11451 C  "C3'" . TTP I 3 .   ? 119.535 143.628 126.397 1.00 26.00 ? 801 TTP B "C3'" 1 
HETATM 11452 O  "O3'" . TTP I 3 .   ? 119.044 143.800 127.729 1.00 31.43 ? 801 TTP B "O3'" 1 
HETATM 11453 C  "C2'" . TTP I 3 .   ? 120.302 142.328 126.305 1.00 24.04 ? 801 TTP B "C2'" 1 
HETATM 11454 C  "C1'" . TTP I 3 .   ? 119.500 141.433 125.374 1.00 28.66 ? 801 TTP B "C1'" 1 
HETATM 11455 N  N1    . TTP I 3 .   ? 120.343 140.957 124.280 1.00 26.41 ? 801 TTP B N1    1 
HETATM 11456 C  C2    . TTP I 3 .   ? 120.463 139.571 124.038 1.00 27.35 ? 801 TTP B C2    1 
HETATM 11457 O  O2    . TTP I 3 .   ? 119.847 138.766 124.767 1.00 31.78 ? 801 TTP B O2    1 
HETATM 11458 N  N3    . TTP I 3 .   ? 121.227 139.102 123.045 1.00 26.84 ? 801 TTP B N3    1 
HETATM 11459 C  C4    . TTP I 3 .   ? 121.898 139.940 122.251 1.00 32.39 ? 801 TTP B C4    1 
HETATM 11460 O  O4    . TTP I 3 .   ? 122.609 139.500 121.324 1.00 35.38 ? 801 TTP B O4    1 
HETATM 11461 C  C5    . TTP I 3 .   ? 121.787 141.399 122.484 1.00 26.58 ? 801 TTP B C5    1 
HETATM 11462 C  C5M   . TTP I 3 .   ? 122.525 142.377 121.613 1.00 25.79 ? 801 TTP B C5M   1 
HETATM 11463 C  C6    . TTP I 3 .   ? 120.988 141.847 123.522 1.00 25.49 ? 801 TTP B C6    1 
HETATM 11464 MG MG    . MG  J 4 .   ? 118.230 149.499 124.594 1.00 33.73 ? 802 MG  B MG    1 
HETATM 11465 P  PG    . ATP K 5 .   ? 154.827 137.870 179.354 1.00 74.47 ? 803 ATP B PG    1 
HETATM 11466 O  O1G   . ATP K 5 .   ? 154.608 138.377 180.739 1.00 63.53 ? 803 ATP B O1G   1 
HETATM 11467 O  O2G   . ATP K 5 .   ? 153.539 137.744 178.535 1.00 64.78 ? 803 ATP B O2G   1 
HETATM 11468 O  O3G   . ATP K 5 .   ? 155.851 138.683 178.555 1.00 63.68 ? 803 ATP B O3G   1 
HETATM 11469 P  PB    . ATP K 5 .   ? 156.771 135.632 179.770 1.00 71.67 ? 803 ATP B PB    1 
HETATM 11470 O  O1B   . ATP K 5 .   ? 157.922 136.119 178.984 1.00 62.83 ? 803 ATP B O1B   1 
HETATM 11471 O  O2B   . ATP K 5 .   ? 156.919 135.714 181.289 1.00 64.38 ? 803 ATP B O2B   1 
HETATM 11472 O  O3B   . ATP K 5 .   ? 155.427 136.390 179.386 1.00 66.37 ? 803 ATP B O3B   1 
HETATM 11473 P  PA    . ATP K 5 .   ? 155.647 133.363 178.241 1.00 72.27 ? 803 ATP B PA    1 
HETATM 11474 O  O1A   . ATP K 5 .   ? 154.290 132.957 178.656 1.00 64.34 ? 803 ATP B O1A   1 
HETATM 11475 O  O2A   . ATP K 5 .   ? 156.557 132.221 177.789 1.00 65.32 ? 803 ATP B O2A   1 
HETATM 11476 O  O3A   . ATP K 5 .   ? 156.404 134.125 179.413 1.00 65.34 ? 803 ATP B O3A   1 
HETATM 11477 O  "O5'" . ATP K 5 .   ? 155.597 134.442 177.090 1.00 63.31 ? 803 ATP B "O5'" 1 
HETATM 11478 C  "C5'" . ATP K 5 .   ? 156.650 134.540 176.109 1.00 62.12 ? 803 ATP B "C5'" 1 
HETATM 11479 C  "C4'" . ATP K 5 .   ? 156.196 135.448 174.994 1.00 63.57 ? 803 ATP B "C4'" 1 
HETATM 11480 O  "O4'" . ATP K 5 .   ? 155.441 134.685 174.028 1.00 64.97 ? 803 ATP B "O4'" 1 
HETATM 11481 C  "C3'" . ATP K 5 .   ? 155.271 136.583 175.415 1.00 61.60 ? 803 ATP B "C3'" 1 
HETATM 11482 O  "O3'" . ATP K 5 .   ? 156.016 137.722 175.830 1.00 63.94 ? 803 ATP B "O3'" 1 
HETATM 11483 C  "C2'" . ATP K 5 .   ? 154.491 136.860 174.129 1.00 61.77 ? 803 ATP B "C2'" 1 
HETATM 11484 O  "O2'" . ATP K 5 .   ? 155.218 137.701 173.242 1.00 62.70 ? 803 ATP B "O2'" 1 
HETATM 11485 C  "C1'" . ATP K 5 .   ? 154.353 135.452 173.540 1.00 63.06 ? 803 ATP B "C1'" 1 
HETATM 11486 N  N9    . ATP K 5 .   ? 153.111 134.772 173.895 1.00 61.34 ? 803 ATP B N9    1 
HETATM 11487 C  C8    . ATP K 5 .   ? 152.976 133.612 174.612 1.00 59.95 ? 803 ATP B C8    1 
HETATM 11488 N  N7    . ATP K 5 .   ? 151.734 133.227 174.778 1.00 61.22 ? 803 ATP B N7    1 
HETATM 11489 C  C5    . ATP K 5 .   ? 150.998 134.201 174.121 1.00 63.53 ? 803 ATP B C5    1 
HETATM 11490 C  C6    . ATP K 5 .   ? 149.615 134.378 173.924 1.00 59.76 ? 803 ATP B C6    1 
HETATM 11491 N  N6    . ATP K 5 .   ? 148.684 133.541 174.392 1.00 59.24 ? 803 ATP B N6    1 
HETATM 11492 N  N1    . ATP K 5 .   ? 149.214 135.457 173.219 1.00 59.07 ? 803 ATP B N1    1 
HETATM 11493 C  C2    . ATP K 5 .   ? 150.137 136.300 172.752 1.00 58.45 ? 803 ATP B C2    1 
HETATM 11494 N  N3    . ATP K 5 .   ? 151.464 136.237 172.871 1.00 60.85 ? 803 ATP B N3    1 
HETATM 11495 C  C4    . ATP K 5 .   ? 151.834 135.160 173.571 1.00 63.17 ? 803 ATP B C4    1 
HETATM 11496 O  O1B   . DGI L 6 .   ? 162.506 152.826 173.422 1.00 62.28 ? 804 DGI B O1B   1 
HETATM 11497 P  PB    . DGI L 6 .   ? 162.714 151.346 173.175 1.00 74.53 ? 804 DGI B PB    1 
HETATM 11498 O  O2B   . DGI L 6 .   ? 164.152 150.991 172.874 1.00 65.04 ? 804 DGI B O2B   1 
HETATM 11499 O  O3B   . DGI L 6 .   ? 162.102 150.480 174.257 1.00 62.08 ? 804 DGI B O3B   1 
HETATM 11500 O  O3A   . DGI L 6 .   ? 161.931 150.986 171.794 1.00 63.71 ? 804 DGI B O3A   1 
HETATM 11501 P  PA    . DGI L 6 .   ? 161.954 149.951 170.575 1.00 68.86 ? 804 DGI B PA    1 
HETATM 11502 O  O1A   . DGI L 6 .   ? 162.792 148.787 170.952 1.00 63.69 ? 804 DGI B O1A   1 
HETATM 11503 O  O2A   . DGI L 6 .   ? 162.258 150.684 169.328 1.00 62.91 ? 804 DGI B O2A   1 
HETATM 11504 O  "O5'" . DGI L 6 .   ? 160.424 149.502 170.514 1.00 62.99 ? 804 DGI B "O5'" 1 
HETATM 11505 C  "C5'" . DGI L 6 .   ? 159.383 150.500 170.536 1.00 61.09 ? 804 DGI B "C5'" 1 
HETATM 11506 C  "C4'" . DGI L 6 .   ? 158.042 149.821 170.406 1.00 61.52 ? 804 DGI B "C4'" 1 
HETATM 11507 O  "O4'" . DGI L 6 .   ? 157.979 149.109 169.150 1.00 61.55 ? 804 DGI B "O4'" 1 
HETATM 11508 C  "C3'" . DGI L 6 .   ? 157.719 148.804 171.506 1.00 62.17 ? 804 DGI B "C3'" 1 
HETATM 11509 O  "O3'" . DGI L 6 .   ? 156.403 149.024 172.014 1.00 61.09 ? 804 DGI B "O3'" 1 
HETATM 11510 C  "C2'" . DGI L 6 .   ? 157.804 147.461 170.790 1.00 58.70 ? 804 DGI B "C2'" 1 
HETATM 11511 C  "C1'" . DGI L 6 .   ? 157.428 147.828 169.368 1.00 58.07 ? 804 DGI B "C1'" 1 
HETATM 11512 N  N9    . DGI L 6 .   ? 157.966 146.915 168.340 1.00 59.53 ? 804 DGI B N9    1 
HETATM 11513 C  C8    . DGI L 6 .   ? 157.262 146.277 167.354 1.00 61.58 ? 804 DGI B C8    1 
HETATM 11514 N  N7    . DGI L 6 .   ? 158.012 145.523 166.586 1.00 60.62 ? 804 DGI B N7    1 
HETATM 11515 C  C5    . DGI L 6 .   ? 159.289 145.675 167.097 1.00 62.53 ? 804 DGI B C5    1 
HETATM 11516 C  C4    . DGI L 6 .   ? 159.277 146.529 168.179 1.00 61.59 ? 804 DGI B C4    1 
HETATM 11517 N  N3    . DGI L 6 .   ? 160.316 146.923 168.940 1.00 62.26 ? 804 DGI B N3    1 
HETATM 11518 C  C2    . DGI L 6 .   ? 161.470 146.383 168.551 1.00 61.03 ? 804 DGI B C2    1 
HETATM 11519 N  N2    . DGI L 6 .   ? 162.591 146.674 169.213 1.00 61.62 ? 804 DGI B N2    1 
HETATM 11520 N  N1    . DGI L 6 .   ? 161.581 145.524 167.490 1.00 60.49 ? 804 DGI B N1    1 
HETATM 11521 C  C6    . DGI L 6 .   ? 160.534 145.105 166.692 1.00 61.94 ? 804 DGI B C6    1 
HETATM 11522 O  O6    . DGI L 6 .   ? 160.729 144.329 165.757 1.00 60.90 ? 804 DGI B O6    1 
# 
