data_9BX3
# 
_entry.id   9BX3 
# 
_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   9BX3         pdb_00009bx3 10.2210/pdb9bx3/pdb 
WWPDB D_1000284317 ?            ?                   
EMDB  EMD-44992    ?            ?                   
# 
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                        9BX3 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-22 
_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 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
EMDB .                                                                                               EMD-44985 
'consensus EM volume'  
EMDB 'Class 5 model for preturnover condition of Bacillus subtilis ribonucleotide reductase complex' EMD-44992 
'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 'MANGANESE (II) ION'                                 54.938    4 ?        ? ? ? 
# 
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 'MANGANESE (II) ION'        MN  
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   GLN n 
1 4   ASN n 
1 5   GLN n 
1 6   VAL n 
1 7   PRO n 
1 8   LYS n 
1 9   TRP n 
1 10  ILE n 
1 11  GLN n 
1 12  LEU n 
1 13  ASN n 
1 14  ASN n 
1 15  GLU n 
1 16  ILE n 
1 17  MET n 
1 18  ILE n 
1 19  GLN n 
1 20  LYS n 
1 21  ASP n 
1 22  GLY n 
1 23  LYS n 
1 24  PHE n 
1 25  GLN n 
1 26  PHE n 
1 27  ASP n 
1 28  LYS n 
1 29  ASP n 
1 30  LYS n 
1 31  GLU n 
1 32  ALA n 
1 33  VAL n 
1 34  HIS n 
1 35  SER n 
1 36  TYR n 
1 37  PHE n 
1 38  VAL n 
1 39  ASP n 
1 40  TYR n 
1 41  ILE n 
1 42  ASN n 
1 43  GLN n 
1 44  ASN n 
1 45  THR n 
1 46  VAL n 
1 47  PHE n 
1 48  PHE n 
1 49  HIS n 
1 50  ASN n 
1 51  LEU n 
1 52  LYS n 
1 53  GLU n 
1 54  LYS n 
1 55  LEU n 
1 56  ASP n 
1 57  TYR n 
1 58  LEU n 
1 59  VAL n 
1 60  GLU n 
1 61  ASN n 
1 62  GLN n 
1 63  TYR n 
1 64  TYR n 
1 65  GLU n 
1 66  GLU n 
1 67  GLU n 
1 68  PHE n 
1 69  LEU n 
1 70  SER n 
1 71  LEU n 
1 72  TYR n 
1 73  SER n 
1 74  PHE n 
1 75  GLU n 
1 76  ASP n 
1 77  ILE n 
1 78  LYS n 
1 79  GLU n 
1 80  VAL n 
1 81  PHE n 
1 82  LYS n 
1 83  THR n 
1 84  ALA n 
1 85  TYR n 
1 86  ALA n 
1 87  LYS n 
1 88  LYS n 
1 89  PHE n 
1 90  ARG n 
1 91  PHE n 
1 92  PRO n 
1 93  SER n 
1 94  PHE n 
1 95  MET n 
1 96  SER n 
1 97  ALA n 
1 98  PHE n 
1 99  LYS n 
1 100 PHE n 
1 101 TYR n 
1 102 ASN n 
1 103 ASP n 
1 104 TYR n 
1 105 ALA n 
1 106 LEU n 
1 107 LYS n 
1 108 THR n 
1 109 ASN n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 ILE n 
1 115 LEU n 
1 116 GLU n 
1 117 ARG n 
1 118 TYR n 
1 119 GLU n 
1 120 ASP n 
1 121 ARG n 
1 122 ILE n 
1 123 SER n 
1 124 ILE n 
1 125 VAL n 
1 126 ALA n 
1 127 LEU n 
1 128 PHE n 
1 129 PHE n 
1 130 ALA n 
1 131 ASN n 
1 132 GLY n 
1 133 ASP n 
1 134 THR n 
1 135 GLU n 
1 136 LYS n 
1 137 ALA n 
1 138 LYS n 
1 139 GLU n 
1 140 TYR n 
1 141 VAL n 
1 142 ASN n 
1 143 LEU n 
1 144 MET n 
1 145 ILE n 
1 146 ASN n 
1 147 GLN n 
1 148 GLU n 
1 149 TYR n 
1 150 GLN n 
1 151 PRO n 
1 152 SER n 
1 153 THR n 
1 154 PRO n 
1 155 THR n 
1 156 PHE n 
1 157 LEU n 
1 158 ASN n 
1 159 ALA n 
1 160 GLY n 
1 161 ARG n 
1 162 LYS n 
1 163 ARG n 
1 164 ARG n 
1 165 GLY n 
1 166 GLU n 
1 167 LEU n 
1 168 VAL n 
1 169 SER n 
1 170 CYS n 
1 171 PHE n 
1 172 LEU n 
1 173 LEU n 
1 174 GLU n 
1 175 VAL n 
1 176 ASN n 
1 177 ASP n 
1 178 SER n 
1 179 LEU n 
1 180 ASN n 
1 181 ASP n 
1 182 ILE n 
1 183 SER n 
1 184 ARG n 
1 185 ALA n 
1 186 ILE n 
1 187 ASP n 
1 188 ILE n 
1 189 SER n 
1 190 MET n 
1 191 GLN n 
1 192 LEU n 
1 193 SER n 
1 194 LYS n 
1 195 LEU n 
1 196 GLY n 
1 197 GLY n 
1 198 GLY n 
1 199 VAL n 
1 200 SER n 
1 201 LEU n 
1 202 ASN n 
1 203 LEU n 
1 204 SER n 
1 205 LYS n 
1 206 LEU n 
1 207 ARG n 
1 208 ALA n 
1 209 LYS n 
1 210 GLY n 
1 211 GLU n 
1 212 ALA n 
1 213 ILE n 
1 214 LYS n 
1 215 ASP n 
1 216 VAL n 
1 217 GLU n 
1 218 ASN n 
1 219 ALA n 
1 220 THR n 
1 221 LYS n 
1 222 GLY n 
1 223 VAL n 
1 224 VAL n 
1 225 GLY n 
1 226 VAL n 
1 227 MET n 
1 228 LYS n 
1 229 LEU n 
1 230 LEU n 
1 231 ASP n 
1 232 ASN n 
1 233 ALA n 
1 234 PHE n 
1 235 ARG n 
1 236 TYR n 
1 237 ALA n 
1 238 ASP n 
1 239 GLN n 
1 240 MET n 
1 241 GLY n 
1 242 GLN n 
1 243 ARG n 
1 244 GLN n 
1 245 GLY n 
1 246 SER n 
1 247 GLY n 
1 248 ALA n 
1 249 ALA n 
1 250 TYR n 
1 251 LEU n 
1 252 ASN n 
1 253 ILE n 
1 254 PHE n 
1 255 HIS n 
1 256 ARG n 
1 257 ASP n 
1 258 ILE n 
1 259 ASN n 
1 260 ASP n 
1 261 PHE n 
1 262 LEU n 
1 263 ASP n 
1 264 THR n 
1 265 LYS n 
1 266 LYS n 
1 267 ILE n 
1 268 SER n 
1 269 ALA n 
1 270 ASP n 
1 271 GLU n 
1 272 ASP n 
1 273 VAL n 
1 274 ARG n 
1 275 VAL n 
1 276 LYS n 
1 277 THR n 
1 278 LEU n 
1 279 SER n 
1 280 ILE n 
1 281 GLY n 
1 282 VAL n 
1 283 VAL n 
1 284 ILE n 
1 285 PRO n 
1 286 ASP n 
1 287 LYS n 
1 288 PHE n 
1 289 VAL n 
1 290 GLU n 
1 291 LEU n 
1 292 ALA n 
1 293 ARG n 
1 294 GLU n 
1 295 ASP n 
1 296 LYS n 
1 297 ALA n 
1 298 ALA n 
1 299 TYR n 
1 300 VAL n 
1 301 PHE n 
1 302 TYR n 
1 303 PRO n 
1 304 HIS n 
1 305 THR n 
1 306 ILE n 
1 307 TYR n 
1 308 LYS n 
1 309 GLU n 
1 310 TYR n 
1 311 GLY n 
1 312 GLN n 
1 313 HIS n 
1 314 MET n 
1 315 ASP n 
1 316 GLU n 
1 317 MET n 
1 318 ASP n 
1 319 MET n 
1 320 ASN n 
1 321 GLU n 
1 322 MET n 
1 323 TYR n 
1 324 ASP n 
1 325 LYS n 
1 326 PHE n 
1 327 VAL n 
1 328 ASP n 
1 329 ASN n 
1 330 PRO n 
1 331 ARG n 
1 332 VAL n 
1 333 LYS n 
1 334 LYS n 
1 335 GLU n 
1 336 LYS n 
1 337 ILE n 
1 338 ASN n 
1 339 PRO n 
1 340 ARG n 
1 341 LYS n 
1 342 LEU n 
1 343 LEU n 
1 344 GLU n 
1 345 LYS n 
1 346 LEU n 
1 347 ALA n 
1 348 MET n 
1 349 LEU n 
1 350 ARG n 
1 351 SER n 
1 352 GLU n 
1 353 SER n 
1 354 GLY n 
1 355 TYR n 
1 356 PRO n 
1 357 TYR n 
1 358 ILE n 
1 359 MET n 
1 360 PHE n 
1 361 GLN n 
1 362 ASP n 
1 363 ASN n 
1 364 VAL n 
1 365 ASN n 
1 366 LYS n 
1 367 VAL n 
1 368 HIS n 
1 369 ALA n 
1 370 ASN n 
1 371 ASN n 
1 372 HIS n 
1 373 ILE n 
1 374 SER n 
1 375 LYS n 
1 376 VAL n 
1 377 LYS n 
1 378 PHE n 
1 379 SER n 
1 380 ASN n 
1 381 LEU n 
1 382 CYS n 
1 383 SER n 
1 384 GLU n 
1 385 VAL n 
1 386 LEU n 
1 387 GLN n 
1 388 ALA n 
1 389 SER n 
1 390 GLN n 
1 391 VAL n 
1 392 SER n 
1 393 SER n 
1 394 TYR n 
1 395 THR n 
1 396 ASP n 
1 397 TYR n 
1 398 ASP n 
1 399 GLU n 
1 400 GLU n 
1 401 ASP n 
1 402 GLU n 
1 403 ILE n 
1 404 GLY n 
1 405 LEU n 
1 406 ASP n 
1 407 ILE n 
1 408 SER n 
1 409 CYS n 
1 410 ASN n 
1 411 LEU n 
1 412 GLY n 
1 413 SER n 
1 414 LEU n 
1 415 ASN n 
1 416 ILE n 
1 417 LEU n 
1 418 ASN n 
1 419 VAL n 
1 420 MET n 
1 421 GLU n 
1 422 HIS n 
1 423 LYS n 
1 424 SER n 
1 425 ILE n 
1 426 GLU n 
1 427 LYS n 
1 428 THR n 
1 429 VAL n 
1 430 LYS n 
1 431 LEU n 
1 432 ALA n 
1 433 THR n 
1 434 ASP n 
1 435 SER n 
1 436 LEU n 
1 437 THR n 
1 438 HIS n 
1 439 VAL n 
1 440 SER n 
1 441 GLU n 
1 442 THR n 
1 443 THR n 
1 444 ASP n 
1 445 ILE n 
1 446 ARG n 
1 447 ASN n 
1 448 ALA n 
1 449 PRO n 
1 450 ALA n 
1 451 VAL n 
1 452 ARG n 
1 453 ARG n 
1 454 ALA n 
1 455 ASN n 
1 456 LYS n 
1 457 ALA n 
1 458 MET n 
1 459 LYS n 
1 460 SER n 
1 461 ILE n 
1 462 GLY n 
1 463 LEU n 
1 464 GLY n 
1 465 ALA n 
1 466 MET n 
1 467 ASN n 
1 468 LEU n 
1 469 HIS n 
1 470 GLY n 
1 471 TYR n 
1 472 LEU n 
1 473 ALA n 
1 474 GLN n 
1 475 ASN n 
1 476 GLY n 
1 477 ILE n 
1 478 ALA n 
1 479 TYR n 
1 480 GLU n 
1 481 SER n 
1 482 PRO n 
1 483 GLU n 
1 484 ALA n 
1 485 ARG n 
1 486 ASP n 
1 487 PHE n 
1 488 ALA n 
1 489 ASN n 
1 490 THR n 
1 491 PHE n 
1 492 PHE n 
1 493 MET n 
1 494 MET n 
1 495 VAL n 
1 496 ASN n 
1 497 PHE n 
1 498 TYR n 
1 499 SER n 
1 500 ILE n 
1 501 GLN n 
1 502 ARG n 
1 503 SER n 
1 504 ALA n 
1 505 GLU n 
1 506 ILE n 
1 507 ALA n 
1 508 LYS n 
1 509 GLU n 
1 510 LYS n 
1 511 GLY n 
1 512 GLU n 
1 513 THR n 
1 514 PHE n 
1 515 ASP n 
1 516 GLN n 
1 517 TYR n 
1 518 GLU n 
1 519 GLY n 
1 520 SER n 
1 521 THR n 
1 522 TYR n 
1 523 ALA n 
1 524 THR n 
1 525 GLY n 
1 526 GLU n 
1 527 TYR n 
1 528 PHE n 
1 529 ASP n 
1 530 LYS n 
1 531 TYR n 
1 532 VAL n 
1 533 SER n 
1 534 THR n 
1 535 ASP n 
1 536 PHE n 
1 537 SER n 
1 538 PRO n 
1 539 LYS n 
1 540 TYR n 
1 541 GLU n 
1 542 LYS n 
1 543 ILE n 
1 544 ALA n 
1 545 ASN n 
1 546 LEU n 
1 547 PHE n 
1 548 GLU n 
1 549 GLY n 
1 550 MET n 
1 551 HIS n 
1 552 ILE n 
1 553 PRO n 
1 554 THR n 
1 555 THR n 
1 556 GLU n 
1 557 ASP n 
1 558 TRP n 
1 559 LYS n 
1 560 LYS n 
1 561 LEU n 
1 562 LYS n 
1 563 ALA n 
1 564 PHE n 
1 565 VAL n 
1 566 ALA n 
1 567 GLU n 
1 568 HIS n 
1 569 GLY n 
1 570 MET n 
1 571 TYR n 
1 572 HIS n 
1 573 SER n 
1 574 TYR n 
1 575 ARG n 
1 576 LEU n 
1 577 CYS n 
1 578 ILE n 
1 579 ALA n 
1 580 PRO n 
1 581 THR n 
1 582 GLY n 
1 583 SER n 
1 584 ILE n 
1 585 SER n 
1 586 TYR n 
1 587 VAL n 
1 588 GLN n 
1 589 SER n 
1 590 SER n 
1 591 THR n 
1 592 ALA n 
1 593 SER n 
1 594 VAL n 
1 595 MET n 
1 596 PRO n 
1 597 ILE n 
1 598 MET n 
1 599 GLU n 
1 600 ARG n 
1 601 ILE n 
1 602 GLU n 
1 603 GLU n 
1 604 ARG n 
1 605 THR n 
1 606 TYR n 
1 607 GLY n 
1 608 ASN n 
1 609 SER n 
1 610 LYS n 
1 611 THR n 
1 612 TYR n 
1 613 TYR n 
1 614 PRO n 
1 615 MET n 
1 616 PRO n 
1 617 GLY n 
1 618 LEU n 
1 619 ALA n 
1 620 SER n 
1 621 ASN n 
1 622 ASN n 
1 623 TRP n 
1 624 PHE n 
1 625 PHE n 
1 626 TYR n 
1 627 LYS n 
1 628 GLU n 
1 629 ALA n 
1 630 TYR n 
1 631 ASP n 
1 632 MET n 
1 633 ASP n 
1 634 MET n 
1 635 PHE n 
1 636 LYS n 
1 637 VAL n 
1 638 VAL n 
1 639 ASP n 
1 640 MET n 
1 641 ILE n 
1 642 ALA n 
1 643 THR n 
1 644 ILE n 
1 645 GLN n 
1 646 GLN n 
1 647 HIS n 
1 648 ILE n 
1 649 ASP n 
1 650 GLN n 
1 651 GLY n 
1 652 ILE n 
1 653 SER n 
1 654 PHE n 
1 655 THR n 
1 656 LEU n 
1 657 PHE n 
1 658 LEU n 
1 659 LYS n 
1 660 ASP n 
1 661 THR n 
1 662 MET n 
1 663 THR n 
1 664 THR n 
1 665 ARG n 
1 666 ASP n 
1 667 LEU n 
1 668 ASN n 
1 669 ARG n 
1 670 ILE n 
1 671 ASP n 
1 672 LEU n 
1 673 TYR n 
1 674 ALA n 
1 675 HIS n 
1 676 HIS n 
1 677 ARG n 
1 678 GLY n 
1 679 ILE n 
1 680 LYS n 
1 681 THR n 
1 682 ILE n 
1 683 TYR n 
1 684 TYR n 
1 685 ALA n 
1 686 ARG n 
1 687 THR n 
1 688 LYS n 
1 689 ASP n 
1 690 THR n 
1 691 GLY n 
1 692 GLN n 
1 693 ASP n 
1 694 SER n 
1 695 CYS n 
1 696 LEU n 
1 697 SER n 
1 698 CYS n 
1 699 VAL n 
1 700 VAL n 
2 1   MET n 
2 2   GLY n 
2 3   SER n 
2 4   SER n 
2 5   HIS n 
2 6   HIS n 
2 7   HIS n 
2 8   HIS n 
2 9   HIS n 
2 10  HIS n 
2 11  SER n 
2 12  SER n 
2 13  GLY n 
2 14  LEU n 
2 15  VAL n 
2 16  PRO n 
2 17  ARG n 
2 18  GLY n 
2 19  SER n 
2 20  HIS n 
2 21  MET n 
2 22  MET n 
2 23  THR n 
2 24  LYS n 
2 25  ILE n 
2 26  TYR n 
2 27  ASP n 
2 28  ALA n 
2 29  ALA n 
2 30  ASN n 
2 31  TRP n 
2 32  SER n 
2 33  LYS n 
2 34  HIS n 
2 35  GLU n 
2 36  ASP n 
2 37  ASP n 
2 38  PHE n 
2 39  THR n 
2 40  GLN n 
2 41  MET n 
2 42  PHE n 
2 43  TYR n 
2 44  ASN n 
2 45  GLN n 
2 46  ASN n 
2 47  VAL n 
2 48  LYS n 
2 49  GLN n 
2 50  PHE n 
2 51  TRP n 
2 52  LEU n 
2 53  PRO n 
2 54  GLU n 
2 55  GLU n 
2 56  ILE n 
2 57  ALA n 
2 58  LEU n 
2 59  ASN n 
2 60  GLY n 
2 61  ASP n 
2 62  LEU n 
2 63  LEU n 
2 64  THR n 
2 65  TRP n 
2 66  LYS n 
2 67  TYR n 
2 68  LEU n 
2 69  GLY n 
2 70  LYS n 
2 71  ASN n 
2 72  GLU n 
2 73  GLN n 
2 74  ASP n 
2 75  THR n 
2 76  TYR n 
2 77  MET n 
2 78  LYS n 
2 79  VAL n 
2 80  LEU n 
2 81  ALA n 
2 82  GLY n 
2 83  LEU n 
2 84  THR n 
2 85  LEU n 
2 86  LEU n 
2 87  ASP n 
2 88  THR n 
2 89  GLU n 
2 90  GLN n 
2 91  GLY n 
2 92  ASN n 
2 93  THR n 
2 94  GLY n 
2 95  MET n 
2 96  PRO n 
2 97  ILE n 
2 98  VAL n 
2 99  ALA n 
2 100 GLU n 
2 101 HIS n 
2 102 VAL n 
2 103 ASP n 
2 104 GLY n 
2 105 HIS n 
2 106 GLN n 
2 107 ARG n 
2 108 LYS n 
2 109 ALA n 
2 110 VAL n 
2 111 LEU n 
2 112 ASN n 
2 113 PHE n 
2 114 MET n 
2 115 ALA n 
2 116 MET n 
2 117 MET n 
2 118 GLU n 
2 119 ASN n 
2 120 ALA n 
2 121 VAL n 
2 122 HIS n 
2 123 ALA n 
2 124 LYS n 
2 125 SER n 
2 126 TYR n 
2 127 SER n 
2 128 ASN n 
2 129 ILE n 
2 130 PHE n 
2 131 MET n 
2 132 THR n 
2 133 LEU n 
2 134 ALA n 
2 135 PRO n 
2 136 THR n 
2 137 GLU n 
2 138 THR n 
2 139 ILE n 
2 140 ASN n 
2 141 GLU n 
2 142 VAL n 
2 143 PHE n 
2 144 GLU n 
2 145 TRP n 
2 146 VAL n 
2 147 LYS n 
2 148 GLN n 
2 149 ASN n 
2 150 LYS n 
2 151 TYR n 
2 152 LEU n 
2 153 GLN n 
2 154 LYS n 
2 155 LYS n 
2 156 ALA n 
2 157 GLN n 
2 158 MET n 
2 159 ILE n 
2 160 VAL n 
2 161 GLY n 
2 162 LEU n 
2 163 TYR n 
2 164 LYS n 
2 165 ALA n 
2 166 ILE n 
2 167 GLN n 
2 168 LYS n 
2 169 ASP n 
2 170 ASP n 
2 171 GLU n 
2 172 ILE n 
2 173 SER n 
2 174 LEU n 
2 175 PHE n 
2 176 LYS n 
2 177 ALA n 
2 178 MET n 
2 179 VAL n 
2 180 ALA n 
2 181 SER n 
2 182 VAL n 
2 183 TYR n 
2 184 LEU n 
2 185 GLU n 
2 186 SER n 
2 187 PHE n 
2 188 LEU n 
2 189 PHE n 
2 190 TYR n 
2 191 SER n 
2 192 GLY n 
2 193 PHE n 
2 194 TYR n 
2 195 TYR n 
2 196 PRO n 
2 197 LEU n 
2 198 TYR n 
2 199 PHE n 
2 200 TYR n 
2 201 GLY n 
2 202 GLN n 
2 203 GLY n 
2 204 LYS n 
2 205 LEU n 
2 206 MET n 
2 207 GLN n 
2 208 SER n 
2 209 GLY n 
2 210 GLU n 
2 211 ILE n 
2 212 ILE n 
2 213 ASN n 
2 214 LEU n 
2 215 ILE n 
2 216 LEU n 
2 217 ARG n 
2 218 ASP n 
2 219 GLU n 
2 220 ALA n 
2 221 ILE n 
2 222 HIS n 
2 223 GLY n 
2 224 VAL n 
2 225 TYR n 
2 226 VAL n 
2 227 GLY n 
2 228 LEU n 
2 229 LEU n 
2 230 ALA n 
2 231 GLN n 
2 232 GLU n 
2 233 ILE n 
2 234 TYR n 
2 235 ASN n 
2 236 LYS n 
2 237 GLN n 
2 238 THR n 
2 239 GLU n 
2 240 GLU n 
2 241 LYS n 
2 242 LYS n 
2 243 ALA n 
2 244 GLU n 
2 245 LEU n 
2 246 ARG n 
2 247 GLU n 
2 248 PHE n 
2 249 ALA n 
2 250 ILE n 
2 251 ASP n 
2 252 LEU n 
2 253 LEU n 
2 254 ASN n 
2 255 GLN n 
2 256 LEU n 
2 257 TYR n 
2 258 GLU n 
2 259 ASN n 
2 260 GLU n 
2 261 LEU n 
2 262 GLU n 
2 263 TYR n 
2 264 THR n 
2 265 GLU n 
2 266 ASP n 
2 267 LEU n 
2 268 TYR n 
2 269 ASP n 
2 270 GLN n 
2 271 VAL n 
2 272 GLY n 
2 273 LEU n 
2 274 SER n 
2 275 HIS n 
2 276 ASP n 
2 277 VAL n 
2 278 LYS n 
2 279 LYS n 
2 280 PHE n 
2 281 ILE n 
2 282 ARG n 
2 283 TYR n 
2 284 ASN n 
2 285 ALA n 
2 286 ASN n 
2 287 LYS n 
2 288 ALA n 
2 289 LEU n 
2 290 MET n 
2 291 ASN n 
2 292 LEU n 
2 293 GLY n 
2 294 PHE n 
2 295 ASP n 
2 296 PRO n 
2 297 TYR n 
2 298 PHE n 
2 299 GLU n 
2 300 GLU n 
2 301 GLU n 
2 302 ASP n 
2 303 ILE n 
2 304 ASN n 
2 305 PRO n 
2 306 ILE n 
2 307 VAL n 
2 308 LEU n 
2 309 ASN n 
2 310 GLY n 
2 311 LEU n 
2 312 ASN n 
2 313 THR n 
2 314 LYS n 
2 315 THR n 
2 316 LYS n 
2 317 SER n 
2 318 HIS n 
2 319 ASP n 
2 320 PHE n 
2 321 PHE n 
2 322 SER n 
2 323 MET n 
2 324 LYS n 
2 325 GLY n 
2 326 ASN n 
2 327 GLY n 
2 328 TYR n 
2 329 LYS n 
2 330 LYS n 
2 331 ALA n 
2 332 THR n 
2 333 VAL n 
2 334 GLU n 
2 335 PRO n 
2 336 LEU n 
2 337 LYS n 
2 338 ASP n 
2 339 ASP n 
2 340 ASP n 
2 341 PHE n 
2 342 TYR n 
2 343 PHE n 
2 344 GLU n 
2 345 ASP n 
2 346 GLU n 
2 347 LYS n 
2 348 GLU n 
2 349 GLN n 
2 350 ILE n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 700 ? ? 'nrdE, nrdA, BSU17380' ? ? ? ? ? ? 'Bacillus subtilis' 1423 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 350 ? ? 'nrdF, BSU17390'       ? ? ? ? ? ? 'Bacillus subtilis' 1423 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                     ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                    ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                  ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'             ? 'C4 H7 N O4'        133.103 
ATP non-polymer         . "ADENOSINE-5'-TRIPHOSPHATE" ? 'C10 H16 N5 O13 P3' 507.181 
CYS 'L-peptide linking' y CYSTEINE                    ? 'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE                   ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'             ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                     ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                   ? 'C6 H10 N3 O2 1'    156.162 
ILE 'L-peptide linking' y ISOLEUCINE                  ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                     ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                      ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                  ? 'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION'             ? 'Mg 2'              24.305  
MN  non-polymer         . 'MANGANESE (II) ION'        ? 'Mn 2'              54.938  
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  16  ASP ASP C . n 
C 2 38  PHE 38  17  17  PHE PHE C . n 
C 2 39  THR 39  18  18  THR THR C . n 
C 2 40  GLN 40  19  19  GLN GLN C . n 
C 2 41  MET 41  20  20  MET MET C . n 
C 2 42  PHE 42  21  21  PHE PHE C . n 
C 2 43  TYR 43  22  22  TYR TYR C . n 
C 2 44  ASN 44  23  23  ASN ASN C . n 
C 2 45  GLN 45  24  24  GLN GLN C . n 
C 2 46  ASN 46  25  25  ASN ASN C . n 
C 2 47  VAL 47  26  26  VAL VAL C . n 
C 2 48  LYS 48  27  27  LYS LYS C . n 
C 2 49  GLN 49  28  28  GLN GLN C . n 
C 2 50  PHE 50  29  29  PHE PHE C . n 
C 2 51  TRP 51  30  30  TRP TRP C . n 
C 2 52  LEU 52  31  31  LEU LEU C . n 
C 2 53  PRO 53  32  32  PRO PRO C . n 
C 2 54  GLU 54  33  33  GLU GLU C . n 
C 2 55  GLU 55  34  34  GLU GLU C . n 
C 2 56  ILE 56  35  35  ILE ILE C . n 
C 2 57  ALA 57  36  36  ALA ALA C . n 
C 2 58  LEU 58  37  37  LEU LEU C . n 
C 2 59  ASN 59  38  38  ASN ASN C . n 
C 2 60  GLY 60  39  39  GLY GLY C . n 
C 2 61  ASP 61  40  40  ASP ASP C . n 
C 2 62  LEU 62  41  41  LEU LEU C . n 
C 2 63  LEU 63  42  42  LEU LEU C . n 
C 2 64  THR 64  43  43  THR THR C . n 
C 2 65  TRP 65  44  44  TRP TRP C . n 
C 2 66  LYS 66  45  45  LYS LYS C . n 
C 2 67  TYR 67  46  46  TYR TYR C . n 
C 2 68  LEU 68  47  47  LEU LEU C . n 
C 2 69  GLY 69  48  48  GLY GLY C . n 
C 2 70  LYS 70  49  49  LYS LYS C . n 
C 2 71  ASN 71  50  50  ASN ASN C . n 
C 2 72  GLU 72  51  51  GLU GLU C . n 
C 2 73  GLN 73  52  52  GLN GLN C . n 
C 2 74  ASP 74  53  53  ASP ASP C . n 
C 2 75  THR 75  54  54  THR THR C . n 
C 2 76  TYR 76  55  55  TYR TYR C . n 
C 2 77  MET 77  56  56  MET MET C . n 
C 2 78  LYS 78  57  57  LYS LYS C . n 
C 2 79  VAL 79  58  58  VAL VAL C . n 
C 2 80  LEU 80  59  59  LEU LEU C . n 
C 2 81  ALA 81  60  60  ALA ALA C . n 
C 2 82  GLY 82  61  61  GLY GLY C . n 
C 2 83  LEU 83  62  62  LEU LEU C . n 
C 2 84  THR 84  63  63  THR THR C . n 
C 2 85  LEU 85  64  64  LEU LEU C . n 
C 2 86  LEU 86  65  65  LEU LEU C . n 
C 2 87  ASP 87  66  66  ASP ASP C . n 
C 2 88  THR 88  67  67  THR THR C . n 
C 2 89  GLU 89  68  68  GLU GLU C . n 
C 2 90  GLN 90  69  69  GLN GLN C . n 
C 2 91  GLY 91  70  70  GLY GLY C . n 
C 2 92  ASN 92  71  71  ASN ASN C . n 
C 2 93  THR 93  72  72  THR THR C . n 
C 2 94  GLY 94  73  73  GLY GLY C . n 
C 2 95  MET 95  74  74  MET MET C . n 
C 2 96  PRO 96  75  75  PRO PRO C . n 
C 2 97  ILE 97  76  76  ILE ILE C . n 
C 2 98  VAL 98  77  77  VAL VAL C . n 
C 2 99  ALA 99  78  78  ALA ALA C . n 
C 2 100 GLU 100 79  79  GLU GLU C . n 
C 2 101 HIS 101 80  80  HIS HIS C . n 
C 2 102 VAL 102 81  81  VAL VAL C . n 
C 2 103 ASP 103 82  82  ASP ASP C . n 
C 2 104 GLY 104 83  83  GLY GLY C . n 
C 2 105 HIS 105 84  84  HIS HIS C . n 
C 2 106 GLN 106 85  85  GLN GLN C . n 
C 2 107 ARG 107 86  86  ARG ARG C . n 
C 2 108 LYS 108 87  87  LYS LYS C . n 
C 2 109 ALA 109 88  88  ALA ALA C . n 
C 2 110 VAL 110 89  89  VAL VAL C . n 
C 2 111 LEU 111 90  90  LEU LEU C . n 
C 2 112 ASN 112 91  91  ASN ASN C . n 
C 2 113 PHE 113 92  92  PHE PHE C . n 
C 2 114 MET 114 93  93  MET MET C . n 
C 2 115 ALA 115 94  94  ALA ALA C . n 
C 2 116 MET 116 95  95  MET MET C . n 
C 2 117 MET 117 96  96  MET MET C . n 
C 2 118 GLU 118 97  97  GLU GLU C . n 
C 2 119 ASN 119 98  98  ASN ASN C . n 
C 2 120 ALA 120 99  99  ALA ALA C . n 
C 2 121 VAL 121 100 100 VAL VAL C . n 
C 2 122 HIS 122 101 101 HIS HIS C . n 
C 2 123 ALA 123 102 102 ALA ALA C . n 
C 2 124 LYS 124 103 103 LYS LYS C . n 
C 2 125 SER 125 104 104 SER SER C . n 
C 2 126 TYR 126 105 105 TYR TYR C . n 
C 2 127 SER 127 106 106 SER SER C . n 
C 2 128 ASN 128 107 107 ASN ASN C . n 
C 2 129 ILE 129 108 108 ILE ILE C . n 
C 2 130 PHE 130 109 109 PHE PHE C . n 
C 2 131 MET 131 110 110 MET MET C . n 
C 2 132 THR 132 111 111 THR THR C . n 
C 2 133 LEU 133 112 112 LEU LEU C . n 
C 2 134 ALA 134 113 113 ALA ALA C . n 
C 2 135 PRO 135 114 114 PRO PRO C . n 
C 2 136 THR 136 115 115 THR THR C . n 
C 2 137 GLU 137 116 116 GLU GLU C . n 
C 2 138 THR 138 117 117 THR THR C . n 
C 2 139 ILE 139 118 118 ILE ILE C . n 
C 2 140 ASN 140 119 119 ASN ASN C . n 
C 2 141 GLU 141 120 120 GLU GLU C . n 
C 2 142 VAL 142 121 121 VAL VAL C . n 
C 2 143 PHE 143 122 122 PHE PHE C . n 
C 2 144 GLU 144 123 123 GLU GLU C . n 
C 2 145 TRP 145 124 124 TRP TRP C . n 
C 2 146 VAL 146 125 125 VAL VAL C . n 
C 2 147 LYS 147 126 126 LYS LYS C . n 
C 2 148 GLN 148 127 127 GLN GLN C . n 
C 2 149 ASN 149 128 128 ASN ASN C . n 
C 2 150 LYS 150 129 129 LYS LYS C . n 
C 2 151 TYR 151 130 130 TYR TYR C . n 
C 2 152 LEU 152 131 131 LEU LEU C . n 
C 2 153 GLN 153 132 132 GLN GLN C . n 
C 2 154 LYS 154 133 133 LYS LYS C . n 
C 2 155 LYS 155 134 134 LYS LYS C . n 
C 2 156 ALA 156 135 135 ALA ALA C . n 
C 2 157 GLN 157 136 136 GLN GLN C . n 
C 2 158 MET 158 137 137 MET MET C . n 
C 2 159 ILE 159 138 138 ILE ILE C . n 
C 2 160 VAL 160 139 139 VAL VAL C . n 
C 2 161 GLY 161 140 140 GLY GLY C . n 
C 2 162 LEU 162 141 141 LEU LEU C . n 
C 2 163 TYR 163 142 142 TYR TYR C . n 
C 2 164 LYS 164 143 143 LYS LYS C . n 
C 2 165 ALA 165 144 144 ALA ALA C . n 
C 2 166 ILE 166 145 145 ILE ILE C . n 
C 2 167 GLN 167 146 146 GLN GLN C . n 
C 2 168 LYS 168 147 147 LYS LYS C . n 
C 2 169 ASP 169 148 148 ASP ASP C . n 
C 2 170 ASP 170 149 149 ASP ASP C . n 
C 2 171 GLU 171 150 150 GLU GLU C . n 
C 2 172 ILE 172 151 151 ILE ILE C . n 
C 2 173 SER 173 152 152 SER SER C . n 
C 2 174 LEU 174 153 153 LEU LEU C . n 
C 2 175 PHE 175 154 154 PHE PHE C . n 
C 2 176 LYS 176 155 155 LYS LYS C . n 
C 2 177 ALA 177 156 156 ALA ALA C . n 
C 2 178 MET 178 157 157 MET MET C . n 
C 2 179 VAL 179 158 158 VAL VAL C . n 
C 2 180 ALA 180 159 159 ALA ALA C . n 
C 2 181 SER 181 160 160 SER SER C . n 
C 2 182 VAL 182 161 161 VAL VAL C . n 
C 2 183 TYR 183 162 162 TYR TYR C . n 
C 2 184 LEU 184 163 163 LEU LEU C . n 
C 2 185 GLU 185 164 164 GLU GLU C . n 
C 2 186 SER 186 165 165 SER SER C . n 
C 2 187 PHE 187 166 166 PHE PHE C . n 
C 2 188 LEU 188 167 167 LEU LEU C . n 
C 2 189 PHE 189 168 168 PHE PHE C . n 
C 2 190 TYR 190 169 169 TYR TYR C . n 
C 2 191 SER 191 170 170 SER SER C . n 
C 2 192 GLY 192 171 171 GLY GLY C . n 
C 2 193 PHE 193 172 172 PHE PHE C . n 
C 2 194 TYR 194 173 173 TYR TYR C . n 
C 2 195 TYR 195 174 174 TYR TYR C . n 
C 2 196 PRO 196 175 175 PRO PRO C . n 
C 2 197 LEU 197 176 176 LEU LEU C . n 
C 2 198 TYR 198 177 177 TYR TYR C . n 
C 2 199 PHE 199 178 178 PHE PHE C . n 
C 2 200 TYR 200 179 179 TYR TYR C . n 
C 2 201 GLY 201 180 180 GLY GLY C . n 
C 2 202 GLN 202 181 181 GLN GLN C . n 
C 2 203 GLY 203 182 182 GLY GLY C . n 
C 2 204 LYS 204 183 183 LYS LYS C . n 
C 2 205 LEU 205 184 184 LEU LEU C . n 
C 2 206 MET 206 185 185 MET MET C . n 
C 2 207 GLN 207 186 186 GLN GLN C . n 
C 2 208 SER 208 187 187 SER SER C . n 
C 2 209 GLY 209 188 188 GLY GLY C . n 
C 2 210 GLU 210 189 189 GLU GLU C . n 
C 2 211 ILE 211 190 190 ILE ILE C . n 
C 2 212 ILE 212 191 191 ILE ILE C . n 
C 2 213 ASN 213 192 192 ASN ASN C . n 
C 2 214 LEU 214 193 193 LEU LEU C . n 
C 2 215 ILE 215 194 194 ILE ILE C . n 
C 2 216 LEU 216 195 195 LEU LEU C . n 
C 2 217 ARG 217 196 196 ARG ARG C . n 
C 2 218 ASP 218 197 197 ASP ASP C . n 
C 2 219 GLU 219 198 198 GLU GLU C . n 
C 2 220 ALA 220 199 199 ALA ALA C . n 
C 2 221 ILE 221 200 200 ILE ILE C . n 
C 2 222 HIS 222 201 201 HIS HIS C . n 
C 2 223 GLY 223 202 202 GLY GLY C . n 
C 2 224 VAL 224 203 203 VAL VAL C . n 
C 2 225 TYR 225 204 204 TYR TYR C . n 
C 2 226 VAL 226 205 205 VAL VAL C . n 
C 2 227 GLY 227 206 206 GLY GLY C . n 
C 2 228 LEU 228 207 207 LEU LEU C . n 
C 2 229 LEU 229 208 208 LEU LEU C . n 
C 2 230 ALA 230 209 209 ALA ALA C . n 
C 2 231 GLN 231 210 210 GLN GLN C . n 
C 2 232 GLU 232 211 211 GLU GLU C . n 
C 2 233 ILE 233 212 212 ILE ILE C . n 
C 2 234 TYR 234 213 213 TYR TYR C . n 
C 2 235 ASN 235 214 214 ASN ASN C . n 
C 2 236 LYS 236 215 215 LYS LYS C . n 
C 2 237 GLN 237 216 216 GLN GLN C . n 
C 2 238 THR 238 217 217 THR THR C . n 
C 2 239 GLU 239 218 218 GLU GLU C . n 
C 2 240 GLU 240 219 219 GLU GLU C . n 
C 2 241 LYS 241 220 220 LYS LYS C . n 
C 2 242 LYS 242 221 221 LYS LYS C . n 
C 2 243 ALA 243 222 222 ALA ALA C . n 
C 2 244 GLU 244 223 223 GLU GLU C . n 
C 2 245 LEU 245 224 224 LEU LEU C . n 
C 2 246 ARG 246 225 225 ARG ARG C . n 
C 2 247 GLU 247 226 226 GLU GLU C . n 
C 2 248 PHE 248 227 227 PHE PHE C . n 
C 2 249 ALA 249 228 228 ALA ALA C . n 
C 2 250 ILE 250 229 229 ILE ILE C . n 
C 2 251 ASP 251 230 230 ASP ASP C . n 
C 2 252 LEU 252 231 231 LEU LEU C . n 
C 2 253 LEU 253 232 232 LEU LEU C . n 
C 2 254 ASN 254 233 233 ASN ASN C . n 
C 2 255 GLN 255 234 234 GLN GLN C . n 
C 2 256 LEU 256 235 235 LEU LEU C . n 
C 2 257 TYR 257 236 236 TYR TYR C . n 
C 2 258 GLU 258 237 237 GLU GLU C . n 
C 2 259 ASN 259 238 238 ASN ASN C . n 
C 2 260 GLU 260 239 239 GLU GLU C . n 
C 2 261 LEU 261 240 240 LEU LEU C . n 
C 2 262 GLU 262 241 241 GLU GLU C . n 
C 2 263 TYR 263 242 242 TYR TYR C . n 
C 2 264 THR 264 243 243 THR THR C . n 
C 2 265 GLU 265 244 244 GLU GLU C . n 
C 2 266 ASP 266 245 245 ASP ASP C . n 
C 2 267 LEU 267 246 246 LEU LEU C . n 
C 2 268 TYR 268 247 247 TYR TYR C . n 
C 2 269 ASP 269 248 248 ASP ASP C . n 
C 2 270 GLN 270 249 249 GLN GLN C . n 
C 2 271 VAL 271 250 250 VAL VAL C . n 
C 2 272 GLY 272 251 251 GLY GLY C . n 
C 2 273 LEU 273 252 252 LEU LEU C . n 
C 2 274 SER 274 253 253 SER SER C . n 
C 2 275 HIS 275 254 254 HIS HIS C . n 
C 2 276 ASP 276 255 255 ASP ASP C . n 
C 2 277 VAL 277 256 256 VAL VAL C . n 
C 2 278 LYS 278 257 257 LYS LYS C . n 
C 2 279 LYS 279 258 258 LYS LYS C . n 
C 2 280 PHE 280 259 259 PHE PHE C . n 
C 2 281 ILE 281 260 260 ILE ILE C . n 
C 2 282 ARG 282 261 261 ARG ARG C . n 
C 2 283 TYR 283 262 262 TYR TYR C . n 
C 2 284 ASN 284 263 263 ASN ASN C . n 
C 2 285 ALA 285 264 264 ALA ALA C . n 
C 2 286 ASN 286 265 265 ASN ASN C . n 
C 2 287 LYS 287 266 266 LYS LYS C . n 
C 2 288 ALA 288 267 267 ALA ALA C . n 
C 2 289 LEU 289 268 268 LEU LEU C . n 
C 2 290 MET 290 269 269 MET MET C . n 
C 2 291 ASN 291 270 270 ASN ASN C . n 
C 2 292 LEU 292 271 271 LEU LEU C . n 
C 2 293 GLY 293 272 272 GLY GLY C . n 
C 2 294 PHE 294 273 273 PHE PHE C . n 
C 2 295 ASP 295 274 274 ASP ASP C . n 
C 2 296 PRO 296 275 275 PRO PRO C . n 
C 2 297 TYR 297 276 276 TYR TYR C . n 
C 2 298 PHE 298 277 277 PHE PHE C . n 
C 2 299 GLU 299 278 278 GLU GLU C . n 
C 2 300 GLU 300 279 279 GLU GLU C . n 
C 2 301 GLU 301 280 280 GLU GLU C . n 
C 2 302 ASP 302 281 281 ASP ASP C . n 
C 2 303 ILE 303 282 282 ILE ILE C . n 
C 2 304 ASN 304 283 283 ASN ASN C . n 
C 2 305 PRO 305 284 284 PRO PRO C . n 
C 2 306 ILE 306 285 285 ILE ILE C . n 
C 2 307 VAL 307 286 286 VAL VAL C . n 
C 2 308 LEU 308 287 287 LEU LEU C . n 
C 2 309 ASN 309 288 288 ASN ASN C . n 
C 2 310 GLY 310 289 289 GLY GLY C . n 
C 2 311 LEU 311 290 290 LEU LEU C . n 
C 2 312 ASN 312 291 ?   ?   ?   C . n 
C 2 313 THR 313 292 ?   ?   ?   C . n 
C 2 314 LYS 314 293 ?   ?   ?   C . n 
C 2 315 THR 315 294 ?   ?   ?   C . n 
C 2 316 LYS 316 295 ?   ?   ?   C . n 
C 2 317 SER 317 296 ?   ?   ?   C . n 
C 2 318 HIS 318 297 ?   ?   ?   C . n 
C 2 319 ASP 319 298 ?   ?   ?   C . n 
C 2 320 PHE 320 299 ?   ?   ?   C . n 
C 2 321 PHE 321 300 ?   ?   ?   C . n 
C 2 322 SER 322 301 ?   ?   ?   C . n 
C 2 323 MET 323 302 ?   ?   ?   C . n 
C 2 324 LYS 324 303 ?   ?   ?   C . n 
C 2 325 GLY 325 304 ?   ?   ?   C . n 
C 2 326 ASN 326 305 ?   ?   ?   C . n 
C 2 327 GLY 327 306 ?   ?   ?   C . n 
C 2 328 TYR 328 307 ?   ?   ?   C . n 
C 2 329 LYS 329 308 ?   ?   ?   C . n 
C 2 330 LYS 330 309 ?   ?   ?   C . n 
C 2 331 ALA 331 310 ?   ?   ?   C . n 
C 2 332 THR 332 311 311 THR THR C . n 
C 2 333 VAL 333 312 312 VAL VAL C . n 
C 2 334 GLU 334 313 313 GLU GLU C . n 
C 2 335 PRO 335 314 314 PRO PRO C . n 
C 2 336 LEU 336 315 315 LEU LEU C . n 
C 2 337 LYS 337 316 316 LYS LYS C . n 
C 2 338 ASP 338 317 317 ASP ASP C . n 
C 2 339 ASP 339 318 318 ASP ASP C . n 
C 2 340 ASP 340 319 319 ASP ASP C . n 
C 2 341 PHE 341 320 320 PHE PHE C . n 
C 2 342 TYR 342 321 321 TYR TYR C . n 
C 2 343 PHE 343 322 322 PHE PHE C . n 
C 2 344 GLU 344 323 ?   ?   ?   C . n 
C 2 345 ASP 345 324 ?   ?   ?   C . n 
C 2 346 GLU 346 325 ?   ?   ?   C . n 
C 2 347 LYS 347 326 ?   ?   ?   C . n 
C 2 348 GLU 348 327 ?   ?   ?   C . n 
C 2 349 GLN 349 328 ?   ?   ?   C . n 
C 2 350 ILE 350 329 ?   ?   ?   C . n 
D 2 1   MET 1   -20 ?   ?   ?   D . n 
D 2 2   GLY 2   -19 ?   ?   ?   D . n 
D 2 3   SER 3   -18 ?   ?   ?   D . n 
D 2 4   SER 4   -17 ?   ?   ?   D . n 
D 2 5   HIS 5   -16 ?   ?   ?   D . n 
D 2 6   HIS 6   -15 ?   ?   ?   D . n 
D 2 7   HIS 7   -14 ?   ?   ?   D . n 
D 2 8   HIS 8   -13 ?   ?   ?   D . n 
D 2 9   HIS 9   -12 ?   ?   ?   D . n 
D 2 10  HIS 10  -11 ?   ?   ?   D . n 
D 2 11  SER 11  -10 ?   ?   ?   D . n 
D 2 12  SER 12  -9  ?   ?   ?   D . n 
D 2 13  GLY 13  -8  ?   ?   ?   D . n 
D 2 14  LEU 14  -7  ?   ?   ?   D . n 
D 2 15  VAL 15  -6  ?   ?   ?   D . n 
D 2 16  PRO 16  -5  ?   ?   ?   D . n 
D 2 17  ARG 17  -4  ?   ?   ?   D . n 
D 2 18  GLY 18  -3  ?   ?   ?   D . n 
D 2 19  SER 19  -2  ?   ?   ?   D . n 
D 2 20  HIS 20  -1  ?   ?   ?   D . n 
D 2 21  MET 21  0   ?   ?   ?   D . n 
D 2 22  MET 22  1   ?   ?   ?   D . n 
D 2 23  THR 23  2   ?   ?   ?   D . n 
D 2 24  LYS 24  3   ?   ?   ?   D . n 
D 2 25  ILE 25  4   ?   ?   ?   D . n 
D 2 26  TYR 26  5   ?   ?   ?   D . n 
D 2 27  ASP 27  6   ?   ?   ?   D . n 
D 2 28  ALA 28  7   ?   ?   ?   D . n 
D 2 29  ALA 29  8   ?   ?   ?   D . n 
D 2 30  ASN 30  9   ?   ?   ?   D . n 
D 2 31  TRP 31  10  ?   ?   ?   D . n 
D 2 32  SER 32  11  ?   ?   ?   D . n 
D 2 33  LYS 33  12  ?   ?   ?   D . n 
D 2 34  HIS 34  13  ?   ?   ?   D . n 
D 2 35  GLU 35  14  ?   ?   ?   D . n 
D 2 36  ASP 36  15  ?   ?   ?   D . n 
D 2 37  ASP 37  16  16  ASP ASP D . n 
D 2 38  PHE 38  17  17  PHE PHE D . n 
D 2 39  THR 39  18  18  THR THR D . n 
D 2 40  GLN 40  19  19  GLN GLN D . n 
D 2 41  MET 41  20  20  MET MET D . n 
D 2 42  PHE 42  21  21  PHE PHE D . n 
D 2 43  TYR 43  22  22  TYR TYR D . n 
D 2 44  ASN 44  23  23  ASN ASN D . n 
D 2 45  GLN 45  24  24  GLN GLN D . n 
D 2 46  ASN 46  25  25  ASN ASN D . n 
D 2 47  VAL 47  26  26  VAL VAL D . n 
D 2 48  LYS 48  27  27  LYS LYS D . n 
D 2 49  GLN 49  28  28  GLN GLN D . n 
D 2 50  PHE 50  29  29  PHE PHE D . n 
D 2 51  TRP 51  30  30  TRP TRP D . n 
D 2 52  LEU 52  31  31  LEU LEU D . n 
D 2 53  PRO 53  32  32  PRO PRO D . n 
D 2 54  GLU 54  33  33  GLU GLU D . n 
D 2 55  GLU 55  34  34  GLU GLU D . n 
D 2 56  ILE 56  35  35  ILE ILE D . n 
D 2 57  ALA 57  36  36  ALA ALA D . n 
D 2 58  LEU 58  37  37  LEU LEU D . n 
D 2 59  ASN 59  38  38  ASN ASN D . n 
D 2 60  GLY 60  39  39  GLY GLY D . n 
D 2 61  ASP 61  40  40  ASP ASP D . n 
D 2 62  LEU 62  41  41  LEU LEU D . n 
D 2 63  LEU 63  42  42  LEU LEU D . n 
D 2 64  THR 64  43  43  THR THR D . n 
D 2 65  TRP 65  44  44  TRP TRP D . n 
D 2 66  LYS 66  45  45  LYS LYS D . n 
D 2 67  TYR 67  46  46  TYR TYR D . n 
D 2 68  LEU 68  47  47  LEU LEU D . n 
D 2 69  GLY 69  48  48  GLY GLY D . n 
D 2 70  LYS 70  49  49  LYS LYS D . n 
D 2 71  ASN 71  50  50  ASN ASN D . n 
D 2 72  GLU 72  51  51  GLU GLU D . n 
D 2 73  GLN 73  52  52  GLN GLN D . n 
D 2 74  ASP 74  53  53  ASP ASP D . n 
D 2 75  THR 75  54  54  THR THR D . n 
D 2 76  TYR 76  55  55  TYR TYR D . n 
D 2 77  MET 77  56  56  MET MET D . n 
D 2 78  LYS 78  57  57  LYS LYS D . n 
D 2 79  VAL 79  58  58  VAL VAL D . n 
D 2 80  LEU 80  59  59  LEU LEU D . n 
D 2 81  ALA 81  60  60  ALA ALA D . n 
D 2 82  GLY 82  61  61  GLY GLY D . n 
D 2 83  LEU 83  62  62  LEU LEU D . n 
D 2 84  THR 84  63  63  THR THR D . n 
D 2 85  LEU 85  64  64  LEU LEU D . n 
D 2 86  LEU 86  65  65  LEU LEU D . n 
D 2 87  ASP 87  66  66  ASP ASP D . n 
D 2 88  THR 88  67  67  THR THR D . n 
D 2 89  GLU 89  68  68  GLU GLU D . n 
D 2 90  GLN 90  69  69  GLN GLN D . n 
D 2 91  GLY 91  70  70  GLY GLY D . n 
D 2 92  ASN 92  71  71  ASN ASN D . n 
D 2 93  THR 93  72  72  THR THR D . n 
D 2 94  GLY 94  73  73  GLY GLY D . n 
D 2 95  MET 95  74  74  MET MET D . n 
D 2 96  PRO 96  75  75  PRO PRO D . n 
D 2 97  ILE 97  76  76  ILE ILE D . n 
D 2 98  VAL 98  77  77  VAL VAL D . n 
D 2 99  ALA 99  78  78  ALA ALA D . n 
D 2 100 GLU 100 79  79  GLU GLU D . n 
D 2 101 HIS 101 80  80  HIS HIS D . n 
D 2 102 VAL 102 81  81  VAL VAL D . n 
D 2 103 ASP 103 82  82  ASP ASP D . n 
D 2 104 GLY 104 83  83  GLY GLY D . n 
D 2 105 HIS 105 84  84  HIS HIS D . n 
D 2 106 GLN 106 85  85  GLN GLN D . n 
D 2 107 ARG 107 86  86  ARG ARG D . n 
D 2 108 LYS 108 87  87  LYS LYS D . n 
D 2 109 ALA 109 88  88  ALA ALA D . n 
D 2 110 VAL 110 89  89  VAL VAL D . n 
D 2 111 LEU 111 90  90  LEU LEU D . n 
D 2 112 ASN 112 91  91  ASN ASN D . n 
D 2 113 PHE 113 92  92  PHE PHE D . n 
D 2 114 MET 114 93  93  MET MET D . n 
D 2 115 ALA 115 94  94  ALA ALA D . n 
D 2 116 MET 116 95  95  MET MET D . n 
D 2 117 MET 117 96  96  MET MET D . n 
D 2 118 GLU 118 97  97  GLU GLU D . n 
D 2 119 ASN 119 98  98  ASN ASN D . n 
D 2 120 ALA 120 99  99  ALA ALA D . n 
D 2 121 VAL 121 100 100 VAL VAL D . n 
D 2 122 HIS 122 101 101 HIS HIS D . n 
D 2 123 ALA 123 102 102 ALA ALA D . n 
D 2 124 LYS 124 103 103 LYS LYS D . n 
D 2 125 SER 125 104 104 SER SER D . n 
D 2 126 TYR 126 105 105 TYR TYR D . n 
D 2 127 SER 127 106 106 SER SER D . n 
D 2 128 ASN 128 107 107 ASN ASN D . n 
D 2 129 ILE 129 108 108 ILE ILE D . n 
D 2 130 PHE 130 109 109 PHE PHE D . n 
D 2 131 MET 131 110 110 MET MET D . n 
D 2 132 THR 132 111 111 THR THR D . n 
D 2 133 LEU 133 112 112 LEU LEU D . n 
D 2 134 ALA 134 113 113 ALA ALA D . n 
D 2 135 PRO 135 114 114 PRO PRO D . n 
D 2 136 THR 136 115 115 THR THR D . n 
D 2 137 GLU 137 116 116 GLU GLU D . n 
D 2 138 THR 138 117 117 THR THR D . n 
D 2 139 ILE 139 118 118 ILE ILE D . n 
D 2 140 ASN 140 119 119 ASN ASN D . n 
D 2 141 GLU 141 120 120 GLU GLU D . n 
D 2 142 VAL 142 121 121 VAL VAL D . n 
D 2 143 PHE 143 122 122 PHE PHE D . n 
D 2 144 GLU 144 123 123 GLU GLU D . n 
D 2 145 TRP 145 124 124 TRP TRP D . n 
D 2 146 VAL 146 125 125 VAL VAL D . n 
D 2 147 LYS 147 126 126 LYS LYS D . n 
D 2 148 GLN 148 127 127 GLN GLN D . n 
D 2 149 ASN 149 128 128 ASN ASN D . n 
D 2 150 LYS 150 129 129 LYS LYS D . n 
D 2 151 TYR 151 130 130 TYR TYR D . n 
D 2 152 LEU 152 131 131 LEU LEU D . n 
D 2 153 GLN 153 132 132 GLN GLN D . n 
D 2 154 LYS 154 133 133 LYS LYS D . n 
D 2 155 LYS 155 134 134 LYS LYS D . n 
D 2 156 ALA 156 135 135 ALA ALA D . n 
D 2 157 GLN 157 136 136 GLN GLN D . n 
D 2 158 MET 158 137 137 MET MET D . n 
D 2 159 ILE 159 138 138 ILE ILE D . n 
D 2 160 VAL 160 139 139 VAL VAL D . n 
D 2 161 GLY 161 140 140 GLY GLY D . n 
D 2 162 LEU 162 141 141 LEU LEU D . n 
D 2 163 TYR 163 142 142 TYR TYR D . n 
D 2 164 LYS 164 143 143 LYS LYS D . n 
D 2 165 ALA 165 144 144 ALA ALA D . n 
D 2 166 ILE 166 145 145 ILE ILE D . n 
D 2 167 GLN 167 146 146 GLN GLN D . n 
D 2 168 LYS 168 147 147 LYS LYS D . n 
D 2 169 ASP 169 148 148 ASP ASP D . n 
D 2 170 ASP 170 149 149 ASP ASP D . n 
D 2 171 GLU 171 150 150 GLU GLU D . n 
D 2 172 ILE 172 151 151 ILE ILE D . n 
D 2 173 SER 173 152 152 SER SER D . n 
D 2 174 LEU 174 153 153 LEU LEU D . n 
D 2 175 PHE 175 154 154 PHE PHE D . n 
D 2 176 LYS 176 155 155 LYS LYS D . n 
D 2 177 ALA 177 156 156 ALA ALA D . n 
D 2 178 MET 178 157 157 MET MET D . n 
D 2 179 VAL 179 158 158 VAL VAL D . n 
D 2 180 ALA 180 159 159 ALA ALA D . n 
D 2 181 SER 181 160 160 SER SER D . n 
D 2 182 VAL 182 161 161 VAL VAL D . n 
D 2 183 TYR 183 162 162 TYR TYR D . n 
D 2 184 LEU 184 163 163 LEU LEU D . n 
D 2 185 GLU 185 164 164 GLU GLU D . n 
D 2 186 SER 186 165 165 SER SER D . n 
D 2 187 PHE 187 166 166 PHE PHE D . n 
D 2 188 LEU 188 167 167 LEU LEU D . n 
D 2 189 PHE 189 168 168 PHE PHE D . n 
D 2 190 TYR 190 169 169 TYR TYR D . n 
D 2 191 SER 191 170 170 SER SER D . n 
D 2 192 GLY 192 171 171 GLY GLY D . n 
D 2 193 PHE 193 172 172 PHE PHE D . n 
D 2 194 TYR 194 173 173 TYR TYR D . n 
D 2 195 TYR 195 174 174 TYR TYR D . n 
D 2 196 PRO 196 175 175 PRO PRO D . n 
D 2 197 LEU 197 176 176 LEU LEU D . n 
D 2 198 TYR 198 177 177 TYR TYR D . n 
D 2 199 PHE 199 178 178 PHE PHE D . n 
D 2 200 TYR 200 179 179 TYR TYR D . n 
D 2 201 GLY 201 180 180 GLY GLY D . n 
D 2 202 GLN 202 181 181 GLN GLN D . n 
D 2 203 GLY 203 182 182 GLY GLY D . n 
D 2 204 LYS 204 183 183 LYS LYS D . n 
D 2 205 LEU 205 184 184 LEU LEU D . n 
D 2 206 MET 206 185 185 MET MET D . n 
D 2 207 GLN 207 186 186 GLN GLN D . n 
D 2 208 SER 208 187 187 SER SER D . n 
D 2 209 GLY 209 188 188 GLY GLY D . n 
D 2 210 GLU 210 189 189 GLU GLU D . n 
D 2 211 ILE 211 190 190 ILE ILE D . n 
D 2 212 ILE 212 191 191 ILE ILE D . n 
D 2 213 ASN 213 192 192 ASN ASN D . n 
D 2 214 LEU 214 193 193 LEU LEU D . n 
D 2 215 ILE 215 194 194 ILE ILE D . n 
D 2 216 LEU 216 195 195 LEU LEU D . n 
D 2 217 ARG 217 196 196 ARG ARG D . n 
D 2 218 ASP 218 197 197 ASP ASP D . n 
D 2 219 GLU 219 198 198 GLU GLU D . n 
D 2 220 ALA 220 199 199 ALA ALA D . n 
D 2 221 ILE 221 200 200 ILE ILE D . n 
D 2 222 HIS 222 201 201 HIS HIS D . n 
D 2 223 GLY 223 202 202 GLY GLY D . n 
D 2 224 VAL 224 203 203 VAL VAL D . n 
D 2 225 TYR 225 204 204 TYR TYR D . n 
D 2 226 VAL 226 205 205 VAL VAL D . n 
D 2 227 GLY 227 206 206 GLY GLY D . n 
D 2 228 LEU 228 207 207 LEU LEU D . n 
D 2 229 LEU 229 208 208 LEU LEU D . n 
D 2 230 ALA 230 209 209 ALA ALA D . n 
D 2 231 GLN 231 210 210 GLN GLN D . n 
D 2 232 GLU 232 211 211 GLU GLU D . n 
D 2 233 ILE 233 212 212 ILE ILE D . n 
D 2 234 TYR 234 213 213 TYR TYR D . n 
D 2 235 ASN 235 214 214 ASN ASN D . n 
D 2 236 LYS 236 215 215 LYS LYS D . n 
D 2 237 GLN 237 216 216 GLN GLN D . n 
D 2 238 THR 238 217 217 THR THR D . n 
D 2 239 GLU 239 218 218 GLU GLU D . n 
D 2 240 GLU 240 219 219 GLU GLU D . n 
D 2 241 LYS 241 220 220 LYS LYS D . n 
D 2 242 LYS 242 221 221 LYS LYS D . n 
D 2 243 ALA 243 222 222 ALA ALA D . n 
D 2 244 GLU 244 223 223 GLU GLU D . n 
D 2 245 LEU 245 224 224 LEU LEU D . n 
D 2 246 ARG 246 225 225 ARG ARG D . n 
D 2 247 GLU 247 226 226 GLU GLU D . n 
D 2 248 PHE 248 227 227 PHE PHE D . n 
D 2 249 ALA 249 228 228 ALA ALA D . n 
D 2 250 ILE 250 229 229 ILE ILE D . n 
D 2 251 ASP 251 230 230 ASP ASP D . n 
D 2 252 LEU 252 231 231 LEU LEU D . n 
D 2 253 LEU 253 232 232 LEU LEU D . n 
D 2 254 ASN 254 233 233 ASN ASN D . n 
D 2 255 GLN 255 234 234 GLN GLN D . n 
D 2 256 LEU 256 235 235 LEU LEU D . n 
D 2 257 TYR 257 236 236 TYR TYR D . n 
D 2 258 GLU 258 237 237 GLU GLU D . n 
D 2 259 ASN 259 238 238 ASN ASN D . n 
D 2 260 GLU 260 239 239 GLU GLU D . n 
D 2 261 LEU 261 240 240 LEU LEU D . n 
D 2 262 GLU 262 241 241 GLU GLU D . n 
D 2 263 TYR 263 242 242 TYR TYR D . n 
D 2 264 THR 264 243 243 THR THR D . n 
D 2 265 GLU 265 244 244 GLU GLU D . n 
D 2 266 ASP 266 245 245 ASP ASP D . n 
D 2 267 LEU 267 246 246 LEU LEU D . n 
D 2 268 TYR 268 247 247 TYR TYR D . n 
D 2 269 ASP 269 248 248 ASP ASP D . n 
D 2 270 GLN 270 249 249 GLN GLN D . n 
D 2 271 VAL 271 250 250 VAL VAL D . n 
D 2 272 GLY 272 251 251 GLY GLY D . n 
D 2 273 LEU 273 252 252 LEU LEU D . n 
D 2 274 SER 274 253 253 SER SER D . n 
D 2 275 HIS 275 254 254 HIS HIS D . n 
D 2 276 ASP 276 255 255 ASP ASP D . n 
D 2 277 VAL 277 256 256 VAL VAL D . n 
D 2 278 LYS 278 257 257 LYS LYS D . n 
D 2 279 LYS 279 258 258 LYS LYS D . n 
D 2 280 PHE 280 259 259 PHE PHE D . n 
D 2 281 ILE 281 260 260 ILE ILE D . n 
D 2 282 ARG 282 261 261 ARG ARG D . n 
D 2 283 TYR 283 262 262 TYR TYR D . n 
D 2 284 ASN 284 263 263 ASN ASN D . n 
D 2 285 ALA 285 264 264 ALA ALA D . n 
D 2 286 ASN 286 265 265 ASN ASN D . n 
D 2 287 LYS 287 266 266 LYS LYS D . n 
D 2 288 ALA 288 267 267 ALA ALA D . n 
D 2 289 LEU 289 268 268 LEU LEU D . n 
D 2 290 MET 290 269 269 MET MET D . n 
D 2 291 ASN 291 270 270 ASN ASN D . n 
D 2 292 LEU 292 271 271 LEU LEU D . n 
D 2 293 GLY 293 272 272 GLY GLY D . n 
D 2 294 PHE 294 273 273 PHE PHE D . n 
D 2 295 ASP 295 274 274 ASP ASP D . n 
D 2 296 PRO 296 275 275 PRO PRO D . n 
D 2 297 TYR 297 276 276 TYR TYR D . n 
D 2 298 PHE 298 277 277 PHE PHE D . n 
D 2 299 GLU 299 278 278 GLU GLU D . n 
D 2 300 GLU 300 279 279 GLU GLU D . n 
D 2 301 GLU 301 280 280 GLU GLU D . n 
D 2 302 ASP 302 281 281 ASP ASP D . n 
D 2 303 ILE 303 282 282 ILE ILE D . n 
D 2 304 ASN 304 283 283 ASN ASN D . n 
D 2 305 PRO 305 284 284 PRO PRO D . n 
D 2 306 ILE 306 285 285 ILE ILE D . n 
D 2 307 VAL 307 286 286 VAL VAL D . n 
D 2 308 LEU 308 287 287 LEU LEU D . n 
D 2 309 ASN 309 288 288 ASN ASN D . n 
D 2 310 GLY 310 289 289 GLY GLY D . n 
D 2 311 LEU 311 290 290 LEU LEU D . n 
D 2 312 ASN 312 291 ?   ?   ?   D . n 
D 2 313 THR 313 292 ?   ?   ?   D . n 
D 2 314 LYS 314 293 ?   ?   ?   D . n 
D 2 315 THR 315 294 ?   ?   ?   D . n 
D 2 316 LYS 316 295 ?   ?   ?   D . n 
D 2 317 SER 317 296 ?   ?   ?   D . n 
D 2 318 HIS 318 297 ?   ?   ?   D . n 
D 2 319 ASP 319 298 ?   ?   ?   D . n 
D 2 320 PHE 320 299 ?   ?   ?   D . n 
D 2 321 PHE 321 300 ?   ?   ?   D . n 
D 2 322 SER 322 301 ?   ?   ?   D . n 
D 2 323 MET 323 302 ?   ?   ?   D . n 
D 2 324 LYS 324 303 ?   ?   ?   D . n 
D 2 325 GLY 325 304 ?   ?   ?   D . n 
D 2 326 ASN 326 305 ?   ?   ?   D . n 
D 2 327 GLY 327 306 ?   ?   ?   D . n 
D 2 328 TYR 328 307 ?   ?   ?   D . n 
D 2 329 LYS 329 308 ?   ?   ?   D . n 
D 2 330 LYS 330 309 ?   ?   ?   D . n 
D 2 331 ALA 331 310 ?   ?   ?   D . n 
D 2 332 THR 332 311 311 THR THR D . n 
D 2 333 VAL 333 312 312 VAL VAL D . n 
D 2 334 GLU 334 313 313 GLU GLU D . n 
D 2 335 PRO 335 314 314 PRO PRO D . n 
D 2 336 LEU 336 315 315 LEU LEU D . n 
D 2 337 LYS 337 316 316 LYS LYS D . n 
D 2 338 ASP 338 317 317 ASP ASP D . n 
D 2 339 ASP 339 318 318 ASP ASP D . n 
D 2 340 ASP 340 319 319 ASP ASP D . n 
D 2 341 PHE 341 320 320 PHE PHE D . n 
D 2 342 TYR 342 321 321 TYR TYR D . n 
D 2 343 PHE 343 322 322 PHE PHE D . n 
D 2 344 GLU 344 323 ?   ?   ?   D . n 
D 2 345 ASP 345 324 ?   ?   ?   D . n 
D 2 346 GLU 346 325 ?   ?   ?   D . n 
D 2 347 LYS 347 326 ?   ?   ?   D . n 
D 2 348 GLU 348 327 ?   ?   ?   D . n 
D 2 349 GLN 349 328 ?   ?   ?   D . n 
D 2 350 ILE 350 329 ?   ?   ?   D . n 
# 
loop_
_pdbx_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 MN  ? ? MN  ? ? '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 3 TTP 1 801 801 TTP TTP B . 
I 4 MG  1 802 802 MG  MG  B . 
J 5 ATP 1 803 803 ATP ATP B . 
K 6 MN  1 401 401 MN  MN  C . 
L 6 MN  1 402 402 MN  MN  C . 
M 6 MN  1 401 401 MN  MN  D . 
N 6 MN  1 402 402 MN  MN  D . 
# 
_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                   9BX3 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9BX3 
_struct.title                        
'Class 5 model for preturnover condition of Bacillus subtilis ribonucleotide reductase complex' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9BX3 
_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 3 ? 
I N N 4 ? 
J N N 5 ? 
K N N 6 ? 
L N N 6 ? 
M N N 6 ? 
N 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 9BX3 A 1  ? 700 ? P50620 1 ? 700 ? 1 700 
2 1 9BX3 B 1  ? 700 ? P50620 1 ? 700 ? 1 700 
3 2 9BX3 C 22 ? 350 ? P50621 1 ? 329 ? 1 329 
4 2 9BX3 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 9BX3 MET C 1  ? UNP P50621 ? ? 'initiating methionine' -20 1  
3 9BX3 GLY C 2  ? UNP P50621 ? ? 'expression tag'        -19 2  
3 9BX3 SER C 3  ? UNP P50621 ? ? 'expression tag'        -18 3  
3 9BX3 SER C 4  ? UNP P50621 ? ? 'expression tag'        -17 4  
3 9BX3 HIS C 5  ? UNP P50621 ? ? 'expression tag'        -16 5  
3 9BX3 HIS C 6  ? UNP P50621 ? ? 'expression tag'        -15 6  
3 9BX3 HIS C 7  ? UNP P50621 ? ? 'expression tag'        -14 7  
3 9BX3 HIS C 8  ? UNP P50621 ? ? 'expression tag'        -13 8  
3 9BX3 HIS C 9  ? UNP P50621 ? ? 'expression tag'        -12 9  
3 9BX3 HIS C 10 ? UNP P50621 ? ? 'expression tag'        -11 10 
3 9BX3 SER C 11 ? UNP P50621 ? ? 'expression tag'        -10 11 
3 9BX3 SER C 12 ? UNP P50621 ? ? 'expression tag'        -9  12 
3 9BX3 GLY C 13 ? UNP P50621 ? ? 'expression tag'        -8  13 
3 9BX3 LEU C 14 ? UNP P50621 ? ? 'expression tag'        -7  14 
3 9BX3 VAL C 15 ? UNP P50621 ? ? 'expression tag'        -6  15 
3 9BX3 PRO C 16 ? UNP P50621 ? ? 'expression tag'        -5  16 
3 9BX3 ARG C 17 ? UNP P50621 ? ? 'expression tag'        -4  17 
3 9BX3 GLY C 18 ? UNP P50621 ? ? 'expression tag'        -3  18 
3 9BX3 SER C 19 ? UNP P50621 ? ? 'expression tag'        -2  19 
3 9BX3 HIS C 20 ? UNP P50621 ? ? 'expression tag'        -1  20 
3 9BX3 MET C 21 ? UNP P50621 ? ? 'expression tag'        0   21 
4 9BX3 MET D 1  ? UNP P50621 ? ? 'initiating methionine' -20 22 
4 9BX3 GLY D 2  ? UNP P50621 ? ? 'expression tag'        -19 23 
4 9BX3 SER D 3  ? UNP P50621 ? ? 'expression tag'        -18 24 
4 9BX3 SER D 4  ? UNP P50621 ? ? 'expression tag'        -17 25 
4 9BX3 HIS D 5  ? UNP P50621 ? ? 'expression tag'        -16 26 
4 9BX3 HIS D 6  ? UNP P50621 ? ? 'expression tag'        -15 27 
4 9BX3 HIS D 7  ? UNP P50621 ? ? 'expression tag'        -14 28 
4 9BX3 HIS D 8  ? UNP P50621 ? ? 'expression tag'        -13 29 
4 9BX3 HIS D 9  ? UNP P50621 ? ? 'expression tag'        -12 30 
4 9BX3 HIS D 10 ? UNP P50621 ? ? 'expression tag'        -11 31 
4 9BX3 SER D 11 ? UNP P50621 ? ? 'expression tag'        -10 32 
4 9BX3 SER D 12 ? UNP P50621 ? ? 'expression tag'        -9  33 
4 9BX3 GLY D 13 ? UNP P50621 ? ? 'expression tag'        -8  34 
4 9BX3 LEU D 14 ? UNP P50621 ? ? 'expression tag'        -7  35 
4 9BX3 VAL D 15 ? UNP P50621 ? ? 'expression tag'        -6  36 
4 9BX3 PRO D 16 ? UNP P50621 ? ? 'expression tag'        -5  37 
4 9BX3 ARG D 17 ? UNP P50621 ? ? 'expression tag'        -4  38 
4 9BX3 GLY D 18 ? UNP P50621 ? ? 'expression tag'        -3  39 
4 9BX3 SER D 19 ? UNP P50621 ? ? 'expression tag'        -2  40 
4 9BX3 HIS D 20 ? UNP P50621 ? ? 'expression tag'        -1  41 
4 9BX3 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,M,N 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 7   ? GLU A 15  ? PRO A 7   GLU A 15  1 ? 9  
HELX_P HELX_P2  AA2 ASP A 27  ? ILE A 41  ? ASP A 27  ILE A 41  1 ? 15 
HELX_P HELX_P3  AA3 ASN A 50  ? ASN A 61  ? ASN A 50  ASN A 61  1 ? 12 
HELX_P HELX_P4  AA4 GLU A 65  ? SER A 70  ? GLU A 65  SER A 70  1 ? 6  
HELX_P HELX_P5  AA5 SER A 73  ? LYS A 87  ? SER A 73  LYS A 87  1 ? 15 
HELX_P HELX_P6  AA6 SER A 93  ? TYR A 104 ? SER A 93  TYR A 104 1 ? 12 
HELX_P HELX_P7  AA7 ARG A 117 ? ASN A 131 ? ARG A 117 ASN A 131 1 ? 15 
HELX_P HELX_P8  AA8 ASP A 133 ? ASN A 146 ? ASP A 133 ASN A 146 1 ? 14 
HELX_P HELX_P9  AA9 SER A 152 ? ALA A 159 ? SER A 152 ALA A 159 1 ? 8  
HELX_P HELX_P10 AB1 SER A 178 ? LEU A 195 ? SER A 178 LEU A 195 1 ? 18 
HELX_P HELX_P11 AB2 GLY A 222 ? ALA A 237 ? GLY A 222 ALA A 237 1 ? 16 
HELX_P HELX_P12 AB3 ASP A 238 ? GLN A 242 ? ASP A 238 GLN A 242 5 ? 5  
HELX_P HELX_P13 AB4 ASP A 257 ? THR A 264 ? ASP A 257 THR A 264 1 ? 8  
HELX_P HELX_P14 AB5 PRO A 285 ? GLU A 294 ? PRO A 285 GLU A 294 1 ? 10 
HELX_P HELX_P15 AB6 TYR A 302 ? GLY A 311 ? TYR A 302 GLY A 311 1 ? 10 
HELX_P HELX_P16 AB7 HIS A 313 ? MET A 317 ? HIS A 313 MET A 317 5 ? 5  
HELX_P HELX_P17 AB8 ASP A 318 ? ASN A 329 ? ASP A 318 ASN A 329 1 ? 12 
HELX_P HELX_P18 AB9 ASN A 338 ? GLY A 354 ? ASN A 338 GLY A 354 1 ? 17 
HELX_P HELX_P19 AC1 GLN A 361 ? LYS A 366 ? GLN A 361 LYS A 366 1 ? 6  
HELX_P HELX_P20 AC2 ILE A 416 ? LYS A 423 ? ILE A 416 LYS A 423 1 ? 8  
HELX_P HELX_P21 AC3 SER A 424 ? THR A 442 ? SER A 424 THR A 442 1 ? 19 
HELX_P HELX_P22 AC4 ALA A 448 ? LYS A 459 ? ALA A 448 LYS A 459 1 ? 12 
HELX_P HELX_P23 AC5 ASN A 467 ? GLN A 474 ? ASN A 467 GLN A 474 1 ? 8  
HELX_P HELX_P24 AC6 SER A 481 ? GLY A 511 ? SER A 481 GLY A 511 1 ? 31 
HELX_P HELX_P25 AC7 SER A 520 ? GLY A 525 ? SER A 520 GLY A 525 1 ? 6  
HELX_P HELX_P26 AC8 PHE A 528 ? THR A 534 ? PHE A 528 THR A 534 1 ? 7  
HELX_P HELX_P27 AC9 TYR A 540 ? PHE A 547 ? TYR A 540 PHE A 547 1 ? 8  
HELX_P HELX_P28 AD1 THR A 554 ? GLY A 569 ? THR A 554 GLY A 569 1 ? 16 
HELX_P HELX_P29 AD2 SER A 583 ? SER A 589 ? SER A 583 SER A 589 1 ? 7  
HELX_P HELX_P30 AD3 GLU A 628 ? MET A 632 ? GLU A 628 MET A 632 5 ? 5  
HELX_P HELX_P31 AD4 ASP A 633 ? GLN A 646 ? ASP A 633 GLN A 646 1 ? 14 
HELX_P HELX_P32 AD5 THR A 663 ? ARG A 677 ? THR A 663 ARG A 677 1 ? 15 
HELX_P HELX_P33 AD6 PRO B 7   ? GLU B 15  ? PRO B 7   GLU B 15  1 ? 9  
HELX_P HELX_P34 AD7 ASP B 27  ? ILE B 41  ? ASP B 27  ILE B 41  1 ? 15 
HELX_P HELX_P35 AD8 ASN B 50  ? ASN B 61  ? ASN B 50  ASN B 61  1 ? 12 
HELX_P HELX_P36 AD9 GLU B 65  ? SER B 70  ? GLU B 65  SER B 70  1 ? 6  
HELX_P HELX_P37 AE1 SER B 73  ? LYS B 87  ? SER B 73  LYS B 87  1 ? 15 
HELX_P HELX_P38 AE2 SER B 93  ? TYR B 104 ? SER B 93  TYR B 104 1 ? 12 
HELX_P HELX_P39 AE3 ARG B 117 ? ASN B 131 ? ARG B 117 ASN B 131 1 ? 15 
HELX_P HELX_P40 AE4 ASP B 133 ? ASN B 146 ? ASP B 133 ASN B 146 1 ? 14 
HELX_P HELX_P41 AE5 SER B 152 ? ALA B 159 ? SER B 152 ALA B 159 1 ? 8  
HELX_P HELX_P42 AE6 SER B 178 ? LEU B 195 ? SER B 178 LEU B 195 1 ? 18 
HELX_P HELX_P43 AE7 GLY B 222 ? ALA B 237 ? GLY B 222 ALA B 237 1 ? 16 
HELX_P HELX_P44 AE8 ASP B 238 ? GLN B 242 ? ASP B 238 GLN B 242 5 ? 5  
HELX_P HELX_P45 AE9 ASP B 257 ? THR B 264 ? ASP B 257 THR B 264 1 ? 8  
HELX_P HELX_P46 AF1 PRO B 285 ? ASP B 295 ? PRO B 285 ASP B 295 1 ? 11 
HELX_P HELX_P47 AF2 TYR B 302 ? GLY B 311 ? TYR B 302 GLY B 311 1 ? 10 
HELX_P HELX_P48 AF3 HIS B 313 ? MET B 317 ? HIS B 313 MET B 317 5 ? 5  
HELX_P HELX_P49 AF4 ASP B 318 ? ASN B 329 ? ASP B 318 ASN B 329 1 ? 12 
HELX_P HELX_P50 AF5 ASN B 338 ? GLY B 354 ? ASN B 338 GLY B 354 1 ? 17 
HELX_P HELX_P51 AF6 GLN B 361 ? VAL B 367 ? GLN B 361 VAL B 367 1 ? 7  
HELX_P HELX_P52 AF7 ILE B 416 ? LYS B 423 ? ILE B 416 LYS B 423 1 ? 8  
HELX_P HELX_P53 AF8 SER B 424 ? THR B 443 ? SER B 424 THR B 443 1 ? 20 
HELX_P HELX_P54 AF9 ALA B 448 ? LYS B 459 ? ALA B 448 LYS B 459 1 ? 12 
HELX_P HELX_P55 AG1 ASN B 467 ? GLN B 474 ? ASN B 467 GLN B 474 1 ? 8  
HELX_P HELX_P56 AG2 SER B 481 ? GLY B 511 ? SER B 481 GLY B 511 1 ? 31 
HELX_P HELX_P57 AG3 SER B 520 ? GLY B 525 ? SER B 520 GLY B 525 1 ? 6  
HELX_P HELX_P58 AG4 PHE B 528 ? THR B 534 ? PHE B 528 THR B 534 1 ? 7  
HELX_P HELX_P59 AG5 TYR B 540 ? PHE B 547 ? TYR B 540 PHE B 547 1 ? 8  
HELX_P HELX_P60 AG6 THR B 554 ? GLY B 569 ? THR B 554 GLY B 569 1 ? 16 
HELX_P HELX_P61 AG7 SER B 583 ? SER B 589 ? SER B 583 SER B 589 1 ? 7  
HELX_P HELX_P62 AG8 GLU B 628 ? MET B 632 ? GLU B 628 MET B 632 5 ? 5  
HELX_P HELX_P63 AG9 ASP B 633 ? GLN B 646 ? ASP B 633 GLN B 646 1 ? 14 
HELX_P HELX_P64 AH1 THR B 663 ? ARG B 677 ? THR B 663 ARG B 677 1 ? 15 
HELX_P HELX_P65 AH2 PHE C 38  ? GLN C 49  ? PHE C 17  GLN C 28  1 ? 12 
HELX_P HELX_P66 AH3 LEU C 52  ? ILE C 56  ? LEU C 31  ILE C 35  5 ? 5  
HELX_P HELX_P67 AH4 LEU C 58  ? GLY C 60  ? LEU C 37  GLY C 39  5 ? 3  
HELX_P HELX_P68 AH5 ASP C 61  ? TYR C 67  ? ASP C 40  TYR C 46  1 ? 7  
HELX_P HELX_P69 AH6 GLY C 69  ? THR C 93  ? GLY C 48  THR C 72  1 ? 25 
HELX_P HELX_P70 AH7 THR C 93  ? VAL C 102 ? THR C 72  VAL C 81  1 ? 10 
HELX_P HELX_P71 AH8 GLY C 104 ? VAL C 121 ? GLY C 83  VAL C 100 1 ? 18 
HELX_P HELX_P72 AH9 VAL C 121 ? ALA C 134 ? VAL C 100 ALA C 113 1 ? 14 
HELX_P HELX_P73 AI1 PRO C 135 ? ASN C 149 ? PRO C 114 ASN C 128 1 ? 15 
HELX_P HELX_P74 AI2 ASN C 149 ? ALA C 165 ? ASN C 128 ALA C 144 1 ? 17 
HELX_P HELX_P75 AI3 ASP C 170 ? PHE C 187 ? ASP C 149 PHE C 166 1 ? 18 
HELX_P HELX_P76 AI4 PHE C 189 ? GLY C 201 ? PHE C 168 GLY C 180 1 ? 13 
HELX_P HELX_P77 AI5 LEU C 205 ? ASN C 235 ? LEU C 184 ASN C 214 1 ? 31 
HELX_P HELX_P78 AI6 THR C 238 ? ASP C 269 ? THR C 217 ASP C 248 1 ? 32 
HELX_P HELX_P79 AI7 GLN C 270 ? GLY C 272 ? GLN C 249 GLY C 251 5 ? 3  
HELX_P HELX_P80 AI8 LEU C 273 ? LEU C 292 ? LEU C 252 LEU C 271 1 ? 20 
HELX_P HELX_P81 AI9 ASN C 304 ? GLY C 310 ? ASN C 283 GLY C 289 1 ? 7  
HELX_P HELX_P82 AJ1 LYS C 337 ? TYR C 342 ? LYS C 316 TYR C 321 5 ? 6  
HELX_P HELX_P83 AJ2 PHE D 38  ? GLN D 49  ? PHE D 17  GLN D 28  1 ? 12 
HELX_P HELX_P84 AJ3 LEU D 52  ? ILE D 56  ? LEU D 31  ILE D 35  5 ? 5  
HELX_P HELX_P85 AJ4 LEU D 58  ? GLY D 60  ? LEU D 37  GLY D 39  5 ? 3  
HELX_P HELX_P86 AJ5 ASP D 61  ? LYS D 66  ? ASP D 40  LYS D 45  1 ? 6  
HELX_P HELX_P87 AJ6 GLY D 69  ? THR D 93  ? GLY D 48  THR D 72  1 ? 25 
HELX_P HELX_P88 AJ7 THR D 93  ? VAL D 102 ? THR D 72  VAL D 81  1 ? 10 
HELX_P HELX_P89 AJ8 GLY D 104 ? VAL D 121 ? GLY D 83  VAL D 100 1 ? 18 
HELX_P HELX_P90 AJ9 VAL D 121 ? ALA D 134 ? VAL D 100 ALA D 113 1 ? 14 
HELX_P HELX_P91 AK1 PRO D 135 ? ASN D 149 ? PRO D 114 ASN D 128 1 ? 15 
HELX_P HELX_P92 AK2 ASN D 149 ? ALA D 165 ? ASN D 128 ALA D 144 1 ? 17 
HELX_P HELX_P93 AK3 ASP D 170 ? PHE D 187 ? ASP D 149 PHE D 166 1 ? 18 
HELX_P HELX_P94 AK4 PHE D 189 ? GLY D 201 ? PHE D 168 GLY D 180 1 ? 13 
HELX_P HELX_P95 AK5 LEU D 205 ? ASN D 235 ? LEU D 184 ASN D 214 1 ? 31 
HELX_P HELX_P96 AK6 THR D 238 ? ASP D 269 ? THR D 217 ASP D 248 1 ? 32 
HELX_P HELX_P97 AK7 GLN D 270 ? GLY D 272 ? GLN D 249 GLY D 251 5 ? 3  
HELX_P HELX_P98 AK8 LEU D 273 ? LEU D 292 ? LEU D 252 LEU D 271 1 ? 20 
HELX_P HELX_P99 AK9 ASN D 304 ? LEU D 311 ? ASN D 283 LEU D 290 1 ? 8  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? E TTP .   O2A ? ? ? 1_555 F MG . MG ? ? A TTP 801 A MG 802 1_555 ? ? ? ? ? ? ? 2.300 ? ? 
metalc2  metalc ? ? E TTP .   O1B ? ? ? 1_555 F MG . MG ? ? A TTP 801 A MG 802 1_555 ? ? ? ? ? ? ? 1.919 ? ? 
metalc3  metalc ? ? H TTP .   O2A ? ? ? 1_555 I MG . MG ? ? B TTP 801 B MG 802 1_555 ? ? ? ? ? ? ? 1.928 ? ? 
metalc4  metalc ? ? H TTP .   O1B ? ? ? 1_555 I MG . MG ? ? B TTP 801 B MG 802 1_555 ? ? ? ? ? ? ? 2.397 ? ? 
metalc5  metalc ? ? H TTP .   O3G ? ? ? 1_555 I MG . MG ? ? B TTP 801 B MG 802 1_555 ? ? ? ? ? ? ? 2.348 ? ? 
metalc6  metalc ? ? C ASP 87  OD1 ? ? ? 1_555 L MN . MN ? ? C ASP 66  C MN 402 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
metalc7  metalc ? ? C GLU 118 OE2 ? ? ? 1_555 K MN . MN ? ? C GLU 97  C MN 401 1_555 ? ? ? ? ? ? ? 1.961 ? ? 
metalc8  metalc ? ? C GLU 118 OE1 ? ? ? 1_555 L MN . MN ? ? C GLU 97  C MN 402 1_555 ? ? ? ? ? ? ? 2.113 ? ? 
metalc9  metalc ? ? C HIS 122 ND1 ? ? ? 1_555 L MN . MN ? ? C HIS 101 C MN 402 1_555 ? ? ? ? ? ? ? 2.176 ? ? 
metalc10 metalc ? ? C GLU 185 OE1 ? ? ? 1_555 K MN . MN ? ? C GLU 164 C MN 401 1_555 ? ? ? ? ? ? ? 2.129 ? ? 
metalc11 metalc ? ? C GLU 185 OE2 ? ? ? 1_555 K MN . MN ? ? C GLU 164 C MN 401 1_555 ? ? ? ? ? ? ? 1.965 ? ? 
metalc12 metalc ? ? C GLU 219 OE1 ? ? ? 1_555 K MN . MN ? ? C GLU 198 C MN 401 1_555 ? ? ? ? ? ? ? 2.173 ? ? 
metalc13 metalc ? ? C GLU 219 OE1 ? ? ? 1_555 L MN . MN ? ? C GLU 198 C MN 402 1_555 ? ? ? ? ? ? ? 2.711 ? ? 
metalc14 metalc ? ? C GLU 219 OE2 ? ? ? 1_555 L MN . MN ? ? C GLU 198 C MN 402 1_555 ? ? ? ? ? ? ? 2.095 ? ? 
metalc15 metalc ? ? C HIS 222 ND1 ? ? ? 1_555 K MN . MN ? ? C HIS 201 C MN 401 1_555 ? ? ? ? ? ? ? 2.408 ? ? 
metalc16 metalc ? ? D ASP 87  OD1 ? ? ? 1_555 N MN . MN ? ? D ASP 66  D MN 402 1_555 ? ? ? ? ? ? ? 2.326 ? ? 
metalc17 metalc ? ? D ASP 87  OD2 ? ? ? 1_555 N MN . MN ? ? D ASP 66  D MN 402 1_555 ? ? ? ? ? ? ? 2.156 ? ? 
metalc18 metalc ? ? D GLU 118 OE2 ? ? ? 1_555 M MN . MN ? ? D GLU 97  D MN 401 1_555 ? ? ? ? ? ? ? 1.912 ? ? 
metalc19 metalc ? ? D GLU 118 OE1 ? ? ? 1_555 N MN . MN ? ? D GLU 97  D MN 402 1_555 ? ? ? ? ? ? ? 1.990 ? ? 
metalc20 metalc ? ? D HIS 122 ND1 ? ? ? 1_555 N MN . MN ? ? D HIS 101 D MN 402 1_555 ? ? ? ? ? ? ? 2.147 ? ? 
metalc21 metalc ? ? D GLU 185 OE1 ? ? ? 1_555 M MN . MN ? ? D GLU 164 D MN 401 1_555 ? ? ? ? ? ? ? 2.304 ? ? 
metalc22 metalc ? ? D GLU 185 OE2 ? ? ? 1_555 M MN . MN ? ? D GLU 164 D MN 401 1_555 ? ? ? ? ? ? ? 2.318 ? ? 
metalc23 metalc ? ? D GLU 219 OE1 ? ? ? 1_555 M MN . MN ? ? D GLU 198 D MN 401 1_555 ? ? ? ? ? ? ? 2.082 ? ? 
metalc24 metalc ? ? D GLU 219 OE2 ? ? ? 1_555 N MN . MN ? ? D GLU 198 D MN 402 1_555 ? ? ? ? ? ? ? 2.085 ? ? 
metalc25 metalc ? ? D HIS 222 ND1 ? ? ? 1_555 M MN . MN ? ? D HIS 201 D MN 401 1_555 ? ? ? ? ? ? ? 2.331 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O2A ? E TTP .   ? A TTP 801 ? 1_555 MG ? F MG . ? A MG 802 ? 1_555 O1B ? E TTP .   ? A TTP 801 ? 1_555 71.4  ? 
2  O2A ? H TTP .   ? B TTP 801 ? 1_555 MG ? I MG . ? B MG 802 ? 1_555 O1B ? H TTP .   ? B TTP 801 ? 1_555 69.5  ? 
3  O2A ? H TTP .   ? B TTP 801 ? 1_555 MG ? I MG . ? B MG 802 ? 1_555 O3G ? H TTP .   ? B TTP 801 ? 1_555 93.9  ? 
4  O1B ? H TTP .   ? B TTP 801 ? 1_555 MG ? I MG . ? B MG 802 ? 1_555 O3G ? H TTP .   ? B TTP 801 ? 1_555 69.8  ? 
5  OD1 ? C ASP 87  ? C ASP 66  ? 1_555 MN ? L MN . ? C MN 402 ? 1_555 OE1 ? C GLU 118 ? C GLU 97  ? 1_555 89.6  ? 
6  OD1 ? C ASP 87  ? C ASP 66  ? 1_555 MN ? L MN . ? C MN 402 ? 1_555 ND1 ? C HIS 122 ? C HIS 101 ? 1_555 120.6 ? 
7  OE1 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? L MN . ? C MN 402 ? 1_555 ND1 ? C HIS 122 ? C HIS 101 ? 1_555 90.1  ? 
8  OD1 ? C ASP 87  ? C ASP 66  ? 1_555 MN ? L MN . ? C MN 402 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 138.4 ? 
9  OE1 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? L MN . ? C MN 402 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 85.1  ? 
10 ND1 ? C HIS 122 ? C HIS 101 ? 1_555 MN ? L MN . ? C MN 402 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 100.7 ? 
11 OD1 ? C ASP 87  ? C ASP 66  ? 1_555 MN ? L MN . ? C MN 402 ? 1_555 OE2 ? C GLU 219 ? C GLU 198 ? 1_555 117.3 ? 
12 OE1 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? L MN . ? C MN 402 ? 1_555 OE2 ? C GLU 219 ? C GLU 198 ? 1_555 137.9 ? 
13 ND1 ? C HIS 122 ? C HIS 101 ? 1_555 MN ? L MN . ? C MN 402 ? 1_555 OE2 ? C GLU 219 ? C GLU 198 ? 1_555 101.2 ? 
14 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 MN ? L MN . ? C MN 402 ? 1_555 OE2 ? C GLU 219 ? C GLU 198 ? 1_555 53.0  ? 
15 OE2 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? K MN . ? C MN 401 ? 1_555 OE1 ? C GLU 185 ? C GLU 164 ? 1_555 141.6 ? 
16 OE2 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? K MN . ? C MN 401 ? 1_555 OE2 ? C GLU 185 ? C GLU 164 ? 1_555 87.2  ? 
17 OE1 ? C GLU 185 ? C GLU 164 ? 1_555 MN ? K MN . ? C MN 401 ? 1_555 OE2 ? C GLU 185 ? C GLU 164 ? 1_555 64.8  ? 
18 OE2 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? K MN . ? C MN 401 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 120.1 ? 
19 OE1 ? C GLU 185 ? C GLU 164 ? 1_555 MN ? K MN . ? C MN 401 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 78.3  ? 
20 OE2 ? C GLU 185 ? C GLU 164 ? 1_555 MN ? K MN . ? C MN 401 ? 1_555 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 142.1 ? 
21 OE2 ? C GLU 118 ? C GLU 97  ? 1_555 MN ? K MN . ? C MN 401 ? 1_555 ND1 ? C HIS 222 ? C HIS 201 ? 1_555 97.1  ? 
22 OE1 ? C GLU 185 ? C GLU 164 ? 1_555 MN ? K MN . ? C MN 401 ? 1_555 ND1 ? C HIS 222 ? C HIS 201 ? 1_555 114.2 ? 
23 OE2 ? C GLU 185 ? C GLU 164 ? 1_555 MN ? K MN . ? C MN 401 ? 1_555 ND1 ? C HIS 222 ? C HIS 201 ? 1_555 104.0 ? 
24 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 MN ? K MN . ? C MN 401 ? 1_555 ND1 ? C HIS 222 ? C HIS 201 ? 1_555 98.4  ? 
25 OD1 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? N MN . ? D MN 402 ? 1_555 OD2 ? D ASP 87  ? D ASP 66  ? 1_555 58.6  ? 
26 OD1 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? N MN . ? D MN 402 ? 1_555 OE1 ? D GLU 118 ? D GLU 97  ? 1_555 93.3  ? 
27 OD2 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? N MN . ? D MN 402 ? 1_555 OE1 ? D GLU 118 ? D GLU 97  ? 1_555 119.5 ? 
28 OD1 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? N MN . ? D MN 402 ? 1_555 ND1 ? D HIS 122 ? D HIS 101 ? 1_555 165.7 ? 
29 OD2 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? N MN . ? D MN 402 ? 1_555 ND1 ? D HIS 122 ? D HIS 101 ? 1_555 107.1 ? 
30 OE1 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? N MN . ? D MN 402 ? 1_555 ND1 ? D HIS 122 ? D HIS 101 ? 1_555 93.8  ? 
31 OD1 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? N MN . ? D MN 402 ? 1_555 OE2 ? D GLU 219 ? D GLU 198 ? 1_555 90.2  ? 
32 OD2 ? D ASP 87  ? D ASP 66  ? 1_555 MN ? N MN . ? D MN 402 ? 1_555 OE2 ? D GLU 219 ? D GLU 198 ? 1_555 111.3 ? 
33 OE1 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? N MN . ? D MN 402 ? 1_555 OE2 ? D GLU 219 ? D GLU 198 ? 1_555 122.0 ? 
34 ND1 ? D HIS 122 ? D HIS 101 ? 1_555 MN ? N MN . ? D MN 402 ? 1_555 OE2 ? D GLU 219 ? D GLU 198 ? 1_555 96.5  ? 
35 OE2 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? M MN . ? D MN 401 ? 1_555 OE1 ? D GLU 185 ? D GLU 164 ? 1_555 153.3 ? 
36 OE2 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? M MN . ? D MN 401 ? 1_555 OE2 ? D GLU 185 ? D GLU 164 ? 1_555 99.6  ? 
37 OE1 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? M MN . ? D MN 401 ? 1_555 OE2 ? D GLU 185 ? D GLU 164 ? 1_555 55.6  ? 
38 OE2 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? M MN . ? D MN 401 ? 1_555 OE1 ? D GLU 219 ? D GLU 198 ? 1_555 121.7 ? 
39 OE1 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? M MN . ? D MN 401 ? 1_555 OE1 ? D GLU 219 ? D GLU 198 ? 1_555 81.3  ? 
40 OE2 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? M MN . ? D MN 401 ? 1_555 OE1 ? D GLU 219 ? D GLU 198 ? 1_555 136.7 ? 
41 OE2 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? M MN . ? D MN 401 ? 1_555 ND1 ? D HIS 222 ? D HIS 201 ? 1_555 91.4  ? 
42 OE1 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? M MN . ? D MN 401 ? 1_555 ND1 ? D HIS 222 ? D HIS 201 ? 1_555 103.0 ? 
43 OE2 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? M MN . ? D MN 401 ? 1_555 ND1 ? D HIS 222 ? D HIS 201 ? 1_555 102.6 ? 
44 OE1 ? D GLU 219 ? D GLU 198 ? 1_555 MN ? M MN . ? D MN 401 ? 1_555 ND1 ? D HIS 222 ? D HIS 201 ? 1_555 89.6  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 TYR 355 A . ? TYR 355 A PRO 356 A ? PRO 356 A 1 -3.79 
2 TYR 355 B . ? TYR 355 B PRO 356 B ? PRO 356 B 1 -1.53 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 8 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 3 ? 
AA7 ? 7 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
AB1 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? parallel      
AA2 7 8 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? parallel      
AA6 1 2 ? anti-parallel 
AA6 2 3 ? parallel      
AA7 1 2 ? anti-parallel 
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA7 4 5 ? parallel      
AA7 5 6 ? parallel      
AA7 6 7 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TYR A 149 ? PRO A 151 ? TYR A 149 PRO A 151 
AA1 2 ILE A 407 ? ASN A 415 ? ILE A 407 ASN A 415 
AA1 3 ILE A 461 ? MET A 466 ? ILE A 461 MET A 466 
AA2 1 TYR A 149 ? PRO A 151 ? TYR A 149 PRO A 151 
AA2 2 ILE A 407 ? ASN A 415 ? ILE A 407 ASN A 415 
AA2 3 CYS A 170 ? GLU A 174 ? CYS A 170 GLU A 174 
AA2 4 GLY A 198 ? ASN A 202 ? GLY A 198 ASN A 202 
AA2 5 GLY A 247 ? ASN A 252 ? GLY A 247 ASN A 252 
AA2 6 LEU A 278 ? ILE A 284 ? LEU A 278 ILE A 284 
AA2 7 TYR A 357 ? PHE A 360 ? TYR A 357 PHE A 360 
AA2 8 THR A 681 ? ILE A 682 ? THR A 681 ILE A 682 
AA3 1 ALA A 298 ? PHE A 301 ? ALA A 298 PHE A 301 
AA3 2 LYS A 334 ? ILE A 337 ? LYS A 334 ILE A 337 
AA4 1 ILE A 601 ? TYR A 606 ? ILE A 601 TYR A 606 
AA4 2 SER A 609 ? PRO A 614 ? SER A 609 PRO A 614 
AA5 1 THR A 655 ? LEU A 658 ? THR A 655 LEU A 658 
AA5 2 TYR A 684 ? THR A 687 ? TYR A 684 THR A 687 
AA6 1 TYR B 149 ? PRO B 151 ? TYR B 149 PRO B 151 
AA6 2 ASN B 410 ? ASN B 415 ? ASN B 410 ASN B 415 
AA6 3 ILE B 461 ? MET B 466 ? ILE B 461 MET B 466 
AA7 1 ILE B 407 ? SER B 408 ? ILE B 407 SER B 408 
AA7 2 CYS B 170 ? GLU B 174 ? CYS B 170 GLU B 174 
AA7 3 GLY B 198 ? ASN B 202 ? GLY B 198 ASN B 202 
AA7 4 GLY B 247 ? ASN B 252 ? GLY B 247 ASN B 252 
AA7 5 LEU B 278 ? ILE B 284 ? LEU B 278 ILE B 284 
AA7 6 TYR B 357 ? PHE B 360 ? TYR B 357 PHE B 360 
AA7 7 THR B 681 ? ILE B 682 ? THR B 681 ILE B 682 
AA8 1 ALA B 298 ? PHE B 301 ? ALA B 298 PHE B 301 
AA8 2 LYS B 334 ? ILE B 337 ? LYS B 334 ILE B 337 
AA9 1 ILE B 601 ? TYR B 606 ? ILE B 601 TYR B 606 
AA9 2 SER B 609 ? PRO B 614 ? SER B 609 PRO B 614 
AB1 1 THR B 655 ? LYS B 659 ? THR B 655 LYS B 659 
AB1 2 TYR B 684 ? LYS B 688 ? TYR B 684 LYS B 688 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLN A 150 ? N GLN A 150 O SER A 413 ? O SER A 413 
AA1 2 3 N GLY A 412 ? N GLY A 412 O GLY A 464 ? O GLY A 464 
AA2 1 2 N GLN A 150 ? N GLN A 150 O SER A 413 ? O SER A 413 
AA2 2 3 O ILE A 407 ? O ILE A 407 N LEU A 172 ? N LEU A 172 
AA2 3 4 N LEU A 173 ? N LEU A 173 O SER A 200 ? O SER A 200 
AA2 4 5 N LEU A 201 ? N LEU A 201 O ALA A 248 ? O ALA A 248 
AA2 5 6 N ALA A 249 ? N ALA A 249 O SER A 279 ? O SER A 279 
AA2 6 7 N VAL A 282 ? N VAL A 282 O TYR A 357 ? O TYR A 357 
AA2 7 8 N ILE A 358 ? N ILE A 358 O ILE A 682 ? O ILE A 682 
AA3 1 2 N ALA A 298 ? N ALA A 298 O ILE A 337 ? O ILE A 337 
AA4 1 2 N ARG A 604 ? N ARG A 604 O THR A 611 ? O THR A 611 
AA5 1 2 N LEU A 656 ? N LEU A 656 O TYR A 684 ? O TYR A 684 
AA6 1 2 N GLN B 150 ? N GLN B 150 O SER B 413 ? O SER B 413 
AA6 2 3 N GLY B 412 ? N GLY B 412 O GLY B 464 ? O GLY B 464 
AA7 1 2 O ILE B 407 ? O ILE B 407 N LEU B 172 ? N LEU B 172 
AA7 2 3 N LEU B 173 ? N LEU B 173 O SER B 200 ? O SER B 200 
AA7 3 4 N LEU B 201 ? N LEU B 201 O ALA B 248 ? O ALA B 248 
AA7 4 5 N GLY B 247 ? N GLY B 247 O SER B 279 ? O SER B 279 
AA7 5 6 N VAL B 282 ? N VAL B 282 O TYR B 357 ? O TYR B 357 
AA7 6 7 N ILE B 358 ? N ILE B 358 O ILE B 682 ? O ILE B 682 
AA8 1 2 N ALA B 298 ? N ALA B 298 O ILE B 337 ? O ILE B 337 
AA9 1 2 N GLU B 602 ? N GLU B 602 O TYR B 613 ? O TYR B 613 
AB1 1 2 N LEU B 658 ? N LEU B 658 O ARG B 686 ? O ARG B 686 
# 
_pdbx_entry_details.entry_id                   9BX3 
_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 ? ? 1.99 
2  1 OG1 A THR 663 ? ? OE2   C GLU 313 ? ? 2.02 
3  1 OH  B TYR 64  ? ? OE2   B GLU 116 ? ? 2.02 
4  1 OE2 A GLU 148 ? ? OG    A SER 424 ? ? 2.04 
5  1 OH  B TYR 63  ? ? OD1   B ASN 109 ? ? 2.06 
6  1 O   A PRO 616 ? ? OH    A TYR 626 ? ? 2.07 
7  1 NZ  A LYS 530 ? ? O     A GLN 646 ? ? 2.11 
8  1 OH  A TYR 64  ? ? OE2   A GLU 116 ? ? 2.13 
9  1 NZ  B LYS 214 ? ? O1G   B TTP 801 ? ? 2.13 
10 1 O   A ILE 41  ? ? OG1   A THR 45  ? ? 2.15 
11 1 NH2 A ARG 121 ? ? O     A ALA 159 ? ? 2.16 
12 1 OE2 B GLU 441 ? ? NZ    B LYS 510 ? ? 2.16 
13 1 NZ  A LYS 377 ? ? O     A SER 389 ? ? 2.17 
14 1 NE2 A HIS 372 ? ? O     A GLN 516 ? ? 2.17 
15 1 OD1 B ASP 177 ? ? "O3'" B TTP 801 ? ? 2.18 
16 1 NH2 D ARG 86  ? ? OE1   D GLU 211 ? ? 2.18 
17 1 NE2 B HIS 372 ? ? O     B GLN 516 ? ? 2.19 
18 1 OH  A TYR 63  ? ? OD1   A ASN 109 ? ? 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 MET A 240 ? ? 74.68   -5.71   
2  1 ASP A 398 ? ? 77.16   -4.40   
3  1 SER A 593 ? ? 52.92   -147.91 
4  1 LYS B 214 ? ? 60.13   61.82   
5  1 ASP B 238 ? ? -94.40  31.22   
6  1 ARG B 243 ? ? -160.38 114.29  
7  1 ASP B 398 ? ? 79.07   -2.89   
8  1 SER B 593 ? ? 52.84   -146.25 
9  1 THR C 72  ? ? -128.08 -59.10  
10 1 ASP C 148 ? ? 58.07   15.70   
11 1 PHE C 166 ? ? -125.67 -60.80  
12 1 THR D 72  ? ? -128.24 -58.44  
13 1 PHE D 166 ? ? -144.17 -61.25  
14 1 ASP D 317 ? ? 69.47   -4.52   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BX3 
_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      'RIGID BODY FIT' 
# 
loop_
_em_3d_fitting_list.id 
_em_3d_fitting_list.3d_fitting_id 
_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 
_em_3d_fitting_list.chain_id 
_em_3d_fitting_list.chain_residue_range 
_em_3d_fitting_list.source_name 
_em_3d_fitting_list.type 
_em_3d_fitting_list.accession_code 
_em_3d_fitting_list.initial_refinement_model_id 
1 1 9BW3 ? ?      'Rigid-body docking of consensus model 9BW3 containing alpha subunits and beta C-terminal tails' ? ?      PDB 
'experimental model' 9BW3 1 
2 1 4DR0 ? 16-290 'Rigid-body docking of residues 16-290 from beta dimer model 4DR0'                               ? 16-290 PDB 
'experimental model' 4DR0 2 
# 
_em_3d_reconstruction.entry_id                    9BX3 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.9 
_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               27000 
_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                        9BX3 
_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              9BX3 
_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                9BX3 
_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              9BX3 
_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 ASN 291 ? C ASN 312 
72  1 Y 1 C THR 292 ? C THR 313 
73  1 Y 1 C LYS 293 ? C LYS 314 
74  1 Y 1 C THR 294 ? C THR 315 
75  1 Y 1 C LYS 295 ? C LYS 316 
76  1 Y 1 C SER 296 ? C SER 317 
77  1 Y 1 C HIS 297 ? C HIS 318 
78  1 Y 1 C ASP 298 ? C ASP 319 
79  1 Y 1 C PHE 299 ? C PHE 320 
80  1 Y 1 C PHE 300 ? C PHE 321 
81  1 Y 1 C SER 301 ? C SER 322 
82  1 Y 1 C MET 302 ? C MET 323 
83  1 Y 1 C LYS 303 ? C LYS 324 
84  1 Y 1 C GLY 304 ? C GLY 325 
85  1 Y 1 C ASN 305 ? C ASN 326 
86  1 Y 1 C GLY 306 ? C GLY 327 
87  1 Y 1 C TYR 307 ? C TYR 328 
88  1 Y 1 C LYS 308 ? C LYS 329 
89  1 Y 1 C LYS 309 ? C LYS 330 
90  1 Y 1 C ALA 310 ? C ALA 331 
91  1 Y 1 C GLU 323 ? C GLU 344 
92  1 Y 1 C ASP 324 ? C ASP 345 
93  1 Y 1 C GLU 325 ? C GLU 346 
94  1 Y 1 C LYS 326 ? C LYS 347 
95  1 Y 1 C GLU 327 ? C GLU 348 
96  1 Y 1 C GLN 328 ? C GLN 349 
97  1 Y 1 C ILE 329 ? C ILE 350 
98  1 Y 1 D MET -20 ? D MET 1   
99  1 Y 1 D GLY -19 ? D GLY 2   
100 1 Y 1 D SER -18 ? D SER 3   
101 1 Y 1 D SER -17 ? D SER 4   
102 1 Y 1 D HIS -16 ? D HIS 5   
103 1 Y 1 D HIS -15 ? D HIS 6   
104 1 Y 1 D HIS -14 ? D HIS 7   
105 1 Y 1 D HIS -13 ? D HIS 8   
106 1 Y 1 D HIS -12 ? D HIS 9   
107 1 Y 1 D HIS -11 ? D HIS 10  
108 1 Y 1 D SER -10 ? D SER 11  
109 1 Y 1 D SER -9  ? D SER 12  
110 1 Y 1 D GLY -8  ? D GLY 13  
111 1 Y 1 D LEU -7  ? D LEU 14  
112 1 Y 1 D VAL -6  ? D VAL 15  
113 1 Y 1 D PRO -5  ? D PRO 16  
114 1 Y 1 D ARG -4  ? D ARG 17  
115 1 Y 1 D GLY -3  ? D GLY 18  
116 1 Y 1 D SER -2  ? D SER 19  
117 1 Y 1 D HIS -1  ? D HIS 20  
118 1 Y 1 D MET 0   ? D MET 21  
119 1 Y 1 D MET 1   ? D MET 22  
120 1 Y 1 D THR 2   ? D THR 23  
121 1 Y 1 D LYS 3   ? D LYS 24  
122 1 Y 1 D ILE 4   ? D ILE 25  
123 1 Y 1 D TYR 5   ? D TYR 26  
124 1 Y 1 D ASP 6   ? D ASP 27  
125 1 Y 1 D ALA 7   ? D ALA 28  
126 1 Y 1 D ALA 8   ? D ALA 29  
127 1 Y 1 D ASN 9   ? D ASN 30  
128 1 Y 1 D TRP 10  ? D TRP 31  
129 1 Y 1 D SER 11  ? D SER 32  
130 1 Y 1 D LYS 12  ? D LYS 33  
131 1 Y 1 D HIS 13  ? D HIS 34  
132 1 Y 1 D GLU 14  ? D GLU 35  
133 1 Y 1 D ASP 15  ? D ASP 36  
134 1 Y 1 D ASN 291 ? D ASN 312 
135 1 Y 1 D THR 292 ? D THR 313 
136 1 Y 1 D LYS 293 ? D LYS 314 
137 1 Y 1 D THR 294 ? D THR 315 
138 1 Y 1 D LYS 295 ? D LYS 316 
139 1 Y 1 D SER 296 ? D SER 317 
140 1 Y 1 D HIS 297 ? D HIS 318 
141 1 Y 1 D ASP 298 ? D ASP 319 
142 1 Y 1 D PHE 299 ? D PHE 320 
143 1 Y 1 D PHE 300 ? D PHE 321 
144 1 Y 1 D SER 301 ? D SER 322 
145 1 Y 1 D MET 302 ? D MET 323 
146 1 Y 1 D LYS 303 ? D LYS 324 
147 1 Y 1 D GLY 304 ? D GLY 325 
148 1 Y 1 D ASN 305 ? D ASN 326 
149 1 Y 1 D GLY 306 ? D GLY 327 
150 1 Y 1 D TYR 307 ? D TYR 328 
151 1 Y 1 D LYS 308 ? D LYS 329 
152 1 Y 1 D LYS 309 ? D LYS 330 
153 1 Y 1 D ALA 310 ? D ALA 331 
154 1 Y 1 D GLU 323 ? D GLU 344 
155 1 Y 1 D ASP 324 ? D ASP 345 
156 1 Y 1 D GLU 325 ? D GLU 346 
157 1 Y 1 D LYS 326 ? D LYS 347 
158 1 Y 1 D GLU 327 ? D GLU 348 
159 1 Y 1 D GLN 328 ? D GLN 349 
160 1 Y 1 D ILE 329 ? D ILE 350 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
ATP PG     P  N N 74  
ATP O1G    O  N N 75  
ATP O2G    O  N N 76  
ATP O3G    O  N N 77  
ATP PB     P  N R 78  
ATP O1B    O  N N 79  
ATP O2B    O  N N 80  
ATP O3B    O  N N 81  
ATP PA     P  N R 82  
ATP O1A    O  N N 83  
ATP O2A    O  N N 84  
ATP O3A    O  N N 85  
ATP "O5'"  O  N N 86  
ATP "C5'"  C  N N 87  
ATP "C4'"  C  N R 88  
ATP "O4'"  O  N N 89  
ATP "C3'"  C  N S 90  
ATP "O3'"  O  N N 91  
ATP "C2'"  C  N R 92  
ATP "O2'"  O  N N 93  
ATP "C1'"  C  N R 94  
ATP N9     N  Y N 95  
ATP C8     C  Y N 96  
ATP N7     N  Y N 97  
ATP C5     C  Y N 98  
ATP C6     C  Y N 99  
ATP N6     N  N N 100 
ATP N1     N  Y N 101 
ATP C2     C  Y N 102 
ATP N3     N  Y N 103 
ATP C4     C  Y N 104 
ATP HOG2   H  N N 105 
ATP HOG3   H  N N 106 
ATP HOB2   H  N N 107 
ATP HOA2   H  N N 108 
ATP "H5'1" H  N N 109 
ATP "H5'2" H  N N 110 
ATP "H4'"  H  N N 111 
ATP "H3'"  H  N N 112 
ATP "HO3'" H  N N 113 
ATP "H2'"  H  N N 114 
ATP "HO2'" H  N N 115 
ATP "H1'"  H  N N 116 
ATP H8     H  N N 117 
ATP HN61   H  N N 118 
ATP HN62   H  N N 119 
ATP H2     H  N N 120 
CYS N      N  N N 121 
CYS CA     C  N R 122 
CYS C      C  N N 123 
CYS O      O  N N 124 
CYS CB     C  N N 125 
CYS SG     S  N N 126 
CYS OXT    O  N N 127 
CYS H      H  N N 128 
CYS H2     H  N N 129 
CYS HA     H  N N 130 
CYS HB2    H  N N 131 
CYS HB3    H  N N 132 
CYS HG     H  N N 133 
CYS HXT    H  N N 134 
GLN N      N  N N 135 
GLN CA     C  N S 136 
GLN C      C  N N 137 
GLN O      O  N N 138 
GLN CB     C  N N 139 
GLN CG     C  N N 140 
GLN CD     C  N N 141 
GLN OE1    O  N N 142 
GLN NE2    N  N N 143 
GLN OXT    O  N N 144 
GLN H      H  N N 145 
GLN H2     H  N N 146 
GLN HA     H  N N 147 
GLN HB2    H  N N 148 
GLN HB3    H  N N 149 
GLN HG2    H  N N 150 
GLN HG3    H  N N 151 
GLN HE21   H  N N 152 
GLN HE22   H  N N 153 
GLN HXT    H  N N 154 
GLU N      N  N N 155 
GLU CA     C  N S 156 
GLU C      C  N N 157 
GLU O      O  N N 158 
GLU CB     C  N N 159 
GLU CG     C  N N 160 
GLU CD     C  N N 161 
GLU OE1    O  N N 162 
GLU OE2    O  N N 163 
GLU OXT    O  N N 164 
GLU H      H  N N 165 
GLU H2     H  N N 166 
GLU HA     H  N N 167 
GLU HB2    H  N N 168 
GLU HB3    H  N N 169 
GLU HG2    H  N N 170 
GLU HG3    H  N N 171 
GLU HE2    H  N N 172 
GLU HXT    H  N N 173 
GLY N      N  N N 174 
GLY CA     C  N N 175 
GLY C      C  N N 176 
GLY O      O  N N 177 
GLY OXT    O  N N 178 
GLY H      H  N N 179 
GLY H2     H  N N 180 
GLY HA2    H  N N 181 
GLY HA3    H  N N 182 
GLY HXT    H  N N 183 
HIS N      N  N N 184 
HIS CA     C  N S 185 
HIS C      C  N N 186 
HIS O      O  N N 187 
HIS CB     C  N N 188 
HIS CG     C  Y N 189 
HIS ND1    N  Y N 190 
HIS CD2    C  Y N 191 
HIS CE1    C  Y N 192 
HIS NE2    N  Y N 193 
HIS OXT    O  N N 194 
HIS H      H  N N 195 
HIS H2     H  N N 196 
HIS HA     H  N N 197 
HIS HB2    H  N N 198 
HIS HB3    H  N N 199 
HIS HD1    H  N N 200 
HIS HD2    H  N N 201 
HIS HE1    H  N N 202 
HIS HE2    H  N N 203 
HIS HXT    H  N N 204 
ILE N      N  N N 205 
ILE CA     C  N S 206 
ILE C      C  N N 207 
ILE O      O  N N 208 
ILE CB     C  N S 209 
ILE CG1    C  N N 210 
ILE CG2    C  N N 211 
ILE CD1    C  N N 212 
ILE OXT    O  N N 213 
ILE H      H  N N 214 
ILE H2     H  N N 215 
ILE HA     H  N N 216 
ILE HB     H  N N 217 
ILE HG12   H  N N 218 
ILE HG13   H  N N 219 
ILE HG21   H  N N 220 
ILE HG22   H  N N 221 
ILE HG23   H  N N 222 
ILE HD11   H  N N 223 
ILE HD12   H  N N 224 
ILE HD13   H  N N 225 
ILE HXT    H  N N 226 
LEU N      N  N N 227 
LEU CA     C  N S 228 
LEU C      C  N N 229 
LEU O      O  N N 230 
LEU CB     C  N N 231 
LEU CG     C  N N 232 
LEU CD1    C  N N 233 
LEU CD2    C  N N 234 
LEU OXT    O  N N 235 
LEU H      H  N N 236 
LEU H2     H  N N 237 
LEU HA     H  N N 238 
LEU HB2    H  N N 239 
LEU HB3    H  N N 240 
LEU HG     H  N N 241 
LEU HD11   H  N N 242 
LEU HD12   H  N N 243 
LEU HD13   H  N N 244 
LEU HD21   H  N N 245 
LEU HD22   H  N N 246 
LEU HD23   H  N N 247 
LEU HXT    H  N N 248 
LYS N      N  N N 249 
LYS CA     C  N S 250 
LYS C      C  N N 251 
LYS O      O  N N 252 
LYS CB     C  N N 253 
LYS CG     C  N N 254 
LYS CD     C  N N 255 
LYS CE     C  N N 256 
LYS NZ     N  N N 257 
LYS OXT    O  N N 258 
LYS H      H  N N 259 
LYS H2     H  N N 260 
LYS HA     H  N N 261 
LYS HB2    H  N N 262 
LYS HB3    H  N N 263 
LYS HG2    H  N N 264 
LYS HG3    H  N N 265 
LYS HD2    H  N N 266 
LYS HD3    H  N N 267 
LYS HE2    H  N N 268 
LYS HE3    H  N N 269 
LYS HZ1    H  N N 270 
LYS HZ2    H  N N 271 
LYS HZ3    H  N N 272 
LYS HXT    H  N N 273 
MET N      N  N N 274 
MET CA     C  N S 275 
MET C      C  N N 276 
MET O      O  N N 277 
MET CB     C  N N 278 
MET CG     C  N N 279 
MET SD     S  N N 280 
MET CE     C  N N 281 
MET OXT    O  N N 282 
MET H      H  N N 283 
MET H2     H  N N 284 
MET HA     H  N N 285 
MET HB2    H  N N 286 
MET HB3    H  N N 287 
MET HG2    H  N N 288 
MET HG3    H  N N 289 
MET HE1    H  N N 290 
MET HE2    H  N N 291 
MET HE3    H  N N 292 
MET HXT    H  N N 293 
MG  MG     MG N N 294 
MN  MN     MN N N 295 
PHE N      N  N N 296 
PHE CA     C  N S 297 
PHE C      C  N N 298 
PHE O      O  N N 299 
PHE CB     C  N N 300 
PHE CG     C  Y N 301 
PHE CD1    C  Y N 302 
PHE CD2    C  Y N 303 
PHE CE1    C  Y N 304 
PHE CE2    C  Y N 305 
PHE CZ     C  Y N 306 
PHE OXT    O  N N 307 
PHE H      H  N N 308 
PHE H2     H  N N 309 
PHE HA     H  N N 310 
PHE HB2    H  N N 311 
PHE HB3    H  N N 312 
PHE HD1    H  N N 313 
PHE HD2    H  N N 314 
PHE HE1    H  N N 315 
PHE HE2    H  N N 316 
PHE HZ     H  N N 317 
PHE HXT    H  N N 318 
PRO N      N  N N 319 
PRO CA     C  N S 320 
PRO C      C  N N 321 
PRO O      O  N N 322 
PRO CB     C  N N 323 
PRO CG     C  N N 324 
PRO CD     C  N N 325 
PRO OXT    O  N N 326 
PRO H      H  N N 327 
PRO HA     H  N N 328 
PRO HB2    H  N N 329 
PRO HB3    H  N N 330 
PRO HG2    H  N N 331 
PRO HG3    H  N N 332 
PRO HD2    H  N N 333 
PRO HD3    H  N N 334 
PRO HXT    H  N N 335 
SER N      N  N N 336 
SER CA     C  N S 337 
SER C      C  N N 338 
SER O      O  N N 339 
SER CB     C  N N 340 
SER OG     O  N N 341 
SER OXT    O  N N 342 
SER H      H  N N 343 
SER H2     H  N N 344 
SER HA     H  N N 345 
SER HB2    H  N N 346 
SER HB3    H  N N 347 
SER HG     H  N N 348 
SER HXT    H  N N 349 
THR N      N  N N 350 
THR CA     C  N S 351 
THR C      C  N N 352 
THR O      O  N N 353 
THR CB     C  N R 354 
THR OG1    O  N N 355 
THR CG2    C  N N 356 
THR OXT    O  N N 357 
THR H      H  N N 358 
THR H2     H  N N 359 
THR HA     H  N N 360 
THR HB     H  N N 361 
THR HG1    H  N N 362 
THR HG21   H  N N 363 
THR HG22   H  N N 364 
THR HG23   H  N N 365 
THR HXT    H  N N 366 
TRP N      N  N N 367 
TRP CA     C  N S 368 
TRP C      C  N N 369 
TRP O      O  N N 370 
TRP CB     C  N N 371 
TRP CG     C  Y N 372 
TRP CD1    C  Y N 373 
TRP CD2    C  Y N 374 
TRP NE1    N  Y N 375 
TRP CE2    C  Y N 376 
TRP CE3    C  Y N 377 
TRP CZ2    C  Y N 378 
TRP CZ3    C  Y N 379 
TRP CH2    C  Y N 380 
TRP OXT    O  N N 381 
TRP H      H  N N 382 
TRP H2     H  N N 383 
TRP HA     H  N N 384 
TRP HB2    H  N N 385 
TRP HB3    H  N N 386 
TRP HD1    H  N N 387 
TRP HE1    H  N N 388 
TRP HE3    H  N N 389 
TRP HZ2    H  N N 390 
TRP HZ3    H  N N 391 
TRP HH2    H  N N 392 
TRP HXT    H  N N 393 
TTP PA     P  N S 394 
TTP O1A    O  N N 395 
TTP O2A    O  N N 396 
TTP O3A    O  N N 397 
TTP PB     P  N S 398 
TTP O1B    O  N N 399 
TTP O2B    O  N N 400 
TTP O3B    O  N N 401 
TTP PG     P  N N 402 
TTP O1G    O  N N 403 
TTP O2G    O  N N 404 
TTP O3G    O  N N 405 
TTP "O5'"  O  N N 406 
TTP "C5'"  C  N N 407 
TTP "C4'"  C  N R 408 
TTP "O4'"  O  N N 409 
TTP "C3'"  C  N S 410 
TTP "O3'"  O  N N 411 
TTP "C2'"  C  N N 412 
TTP "C1'"  C  N R 413 
TTP N1     N  N N 414 
TTP C2     C  N N 415 
TTP O2     O  N N 416 
TTP N3     N  N N 417 
TTP C4     C  N N 418 
TTP O4     O  N N 419 
TTP C5     C  N N 420 
TTP C5M    C  N N 421 
TTP C6     C  N N 422 
TTP HOA2   H  N N 423 
TTP HOB2   H  N N 424 
TTP HOG2   H  N N 425 
TTP HOG3   H  N N 426 
TTP "H5'1" H  N N 427 
TTP "H5'2" H  N N 428 
TTP "H4'"  H  N N 429 
TTP "H3'"  H  N N 430 
TTP "HO3'" H  N N 431 
TTP "H2'1" H  N N 432 
TTP "H2'2" H  N N 433 
TTP "H1'"  H  N N 434 
TTP HN3    H  N N 435 
TTP HM51   H  N N 436 
TTP HM52   H  N N 437 
TTP HM53   H  N N 438 
TTP H6     H  N N 439 
TYR N      N  N N 440 
TYR CA     C  N S 441 
TYR C      C  N N 442 
TYR O      O  N N 443 
TYR CB     C  N N 444 
TYR CG     C  Y N 445 
TYR CD1    C  Y N 446 
TYR CD2    C  Y N 447 
TYR CE1    C  Y N 448 
TYR CE2    C  Y N 449 
TYR CZ     C  Y N 450 
TYR OH     O  N N 451 
TYR OXT    O  N N 452 
TYR H      H  N N 453 
TYR H2     H  N N 454 
TYR HA     H  N N 455 
TYR HB2    H  N N 456 
TYR HB3    H  N N 457 
TYR HD1    H  N N 458 
TYR HD2    H  N N 459 
TYR HE1    H  N N 460 
TYR HE2    H  N N 461 
TYR HH     H  N N 462 
TYR HXT    H  N N 463 
VAL N      N  N N 464 
VAL CA     C  N S 465 
VAL C      C  N N 466 
VAL O      O  N N 467 
VAL CB     C  N N 468 
VAL CG1    C  N N 469 
VAL CG2    C  N N 470 
VAL OXT    O  N N 471 
VAL H      H  N N 472 
VAL H2     H  N N 473 
VAL HA     H  N N 474 
VAL HB     H  N N 475 
VAL HG11   H  N N 476 
VAL HG12   H  N N 477 
VAL HG13   H  N N 478 
VAL HG21   H  N N 479 
VAL HG22   H  N N 480 
VAL HG23   H  N N 481 
VAL HXT    H  N N 482 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
ATP PG    O1G    doub N N 70  
ATP PG    O2G    sing N N 71  
ATP PG    O3G    sing N N 72  
ATP PG    O3B    sing N N 73  
ATP O2G   HOG2   sing N N 74  
ATP O3G   HOG3   sing N N 75  
ATP PB    O1B    doub N N 76  
ATP PB    O2B    sing N N 77  
ATP PB    O3B    sing N N 78  
ATP PB    O3A    sing N N 79  
ATP O2B   HOB2   sing N N 80  
ATP PA    O1A    doub N N 81  
ATP PA    O2A    sing N N 82  
ATP PA    O3A    sing N N 83  
ATP PA    "O5'"  sing N N 84  
ATP O2A   HOA2   sing N N 85  
ATP "O5'" "C5'"  sing N N 86  
ATP "C5'" "C4'"  sing N N 87  
ATP "C5'" "H5'1" sing N N 88  
ATP "C5'" "H5'2" sing N N 89  
ATP "C4'" "O4'"  sing N N 90  
ATP "C4'" "C3'"  sing N N 91  
ATP "C4'" "H4'"  sing N N 92  
ATP "O4'" "C1'"  sing N N 93  
ATP "C3'" "O3'"  sing N N 94  
ATP "C3'" "C2'"  sing N N 95  
ATP "C3'" "H3'"  sing N N 96  
ATP "O3'" "HO3'" sing N N 97  
ATP "C2'" "O2'"  sing N N 98  
ATP "C2'" "C1'"  sing N N 99  
ATP "C2'" "H2'"  sing N N 100 
ATP "O2'" "HO2'" sing N N 101 
ATP "C1'" N9     sing N N 102 
ATP "C1'" "H1'"  sing N N 103 
ATP N9    C8     sing Y N 104 
ATP N9    C4     sing Y N 105 
ATP C8    N7     doub Y N 106 
ATP C8    H8     sing N N 107 
ATP N7    C5     sing Y N 108 
ATP C5    C6     sing Y N 109 
ATP C5    C4     doub Y N 110 
ATP C6    N6     sing N N 111 
ATP C6    N1     doub Y N 112 
ATP N6    HN61   sing N N 113 
ATP N6    HN62   sing N N 114 
ATP N1    C2     sing Y N 115 
ATP C2    N3     doub Y N 116 
ATP C2    H2     sing N N 117 
ATP N3    C4     sing Y N 118 
CYS N     CA     sing N N 119 
CYS N     H      sing N N 120 
CYS N     H2     sing N N 121 
CYS CA    C      sing N N 122 
CYS CA    CB     sing N N 123 
CYS CA    HA     sing N N 124 
CYS C     O      doub N N 125 
CYS C     OXT    sing N N 126 
CYS CB    SG     sing N N 127 
CYS CB    HB2    sing N N 128 
CYS CB    HB3    sing N N 129 
CYS SG    HG     sing N N 130 
CYS OXT   HXT    sing N N 131 
GLN N     CA     sing N N 132 
GLN N     H      sing N N 133 
GLN N     H2     sing N N 134 
GLN CA    C      sing N N 135 
GLN CA    CB     sing N N 136 
GLN CA    HA     sing N N 137 
GLN C     O      doub N N 138 
GLN C     OXT    sing N N 139 
GLN CB    CG     sing N N 140 
GLN CB    HB2    sing N N 141 
GLN CB    HB3    sing N N 142 
GLN CG    CD     sing N N 143 
GLN CG    HG2    sing N N 144 
GLN CG    HG3    sing N N 145 
GLN CD    OE1    doub N N 146 
GLN CD    NE2    sing N N 147 
GLN NE2   HE21   sing N N 148 
GLN NE2   HE22   sing N N 149 
GLN OXT   HXT    sing N N 150 
GLU N     CA     sing N N 151 
GLU N     H      sing N N 152 
GLU N     H2     sing N N 153 
GLU CA    C      sing N N 154 
GLU CA    CB     sing N N 155 
GLU CA    HA     sing N N 156 
GLU C     O      doub N N 157 
GLU C     OXT    sing N N 158 
GLU CB    CG     sing N N 159 
GLU CB    HB2    sing N N 160 
GLU CB    HB3    sing N N 161 
GLU CG    CD     sing N N 162 
GLU CG    HG2    sing N N 163 
GLU CG    HG3    sing N N 164 
GLU CD    OE1    doub N N 165 
GLU CD    OE2    sing N N 166 
GLU OE2   HE2    sing N N 167 
GLU OXT   HXT    sing N N 168 
GLY N     CA     sing N N 169 
GLY N     H      sing N N 170 
GLY N     H2     sing N N 171 
GLY CA    C      sing N N 172 
GLY CA    HA2    sing N N 173 
GLY CA    HA3    sing N N 174 
GLY C     O      doub N N 175 
GLY C     OXT    sing N N 176 
GLY OXT   HXT    sing N N 177 
HIS N     CA     sing N N 178 
HIS N     H      sing N N 179 
HIS N     H2     sing N N 180 
HIS CA    C      sing N N 181 
HIS CA    CB     sing N N 182 
HIS CA    HA     sing N N 183 
HIS C     O      doub N N 184 
HIS C     OXT    sing N N 185 
HIS CB    CG     sing N N 186 
HIS CB    HB2    sing N N 187 
HIS CB    HB3    sing N N 188 
HIS CG    ND1    sing Y N 189 
HIS CG    CD2    doub Y N 190 
HIS ND1   CE1    doub Y N 191 
HIS ND1   HD1    sing N N 192 
HIS CD2   NE2    sing Y N 193 
HIS CD2   HD2    sing N N 194 
HIS CE1   NE2    sing Y N 195 
HIS CE1   HE1    sing N N 196 
HIS NE2   HE2    sing N N 197 
HIS OXT   HXT    sing N N 198 
ILE N     CA     sing N N 199 
ILE N     H      sing N N 200 
ILE N     H2     sing N N 201 
ILE CA    C      sing N N 202 
ILE CA    CB     sing N N 203 
ILE CA    HA     sing N N 204 
ILE C     O      doub N N 205 
ILE C     OXT    sing N N 206 
ILE CB    CG1    sing N N 207 
ILE CB    CG2    sing N N 208 
ILE CB    HB     sing N N 209 
ILE CG1   CD1    sing N N 210 
ILE CG1   HG12   sing N N 211 
ILE CG1   HG13   sing N N 212 
ILE CG2   HG21   sing N N 213 
ILE CG2   HG22   sing N N 214 
ILE CG2   HG23   sing N N 215 
ILE CD1   HD11   sing N N 216 
ILE CD1   HD12   sing N N 217 
ILE CD1   HD13   sing N N 218 
ILE OXT   HXT    sing N N 219 
LEU N     CA     sing N N 220 
LEU N     H      sing N N 221 
LEU N     H2     sing N N 222 
LEU CA    C      sing N N 223 
LEU CA    CB     sing N N 224 
LEU CA    HA     sing N N 225 
LEU C     O      doub N N 226 
LEU C     OXT    sing N N 227 
LEU CB    CG     sing N N 228 
LEU CB    HB2    sing N N 229 
LEU CB    HB3    sing N N 230 
LEU CG    CD1    sing N N 231 
LEU CG    CD2    sing N N 232 
LEU CG    HG     sing N N 233 
LEU CD1   HD11   sing N N 234 
LEU CD1   HD12   sing N N 235 
LEU CD1   HD13   sing N N 236 
LEU CD2   HD21   sing N N 237 
LEU CD2   HD22   sing N N 238 
LEU CD2   HD23   sing N N 239 
LEU OXT   HXT    sing N N 240 
LYS N     CA     sing N N 241 
LYS N     H      sing N N 242 
LYS N     H2     sing N N 243 
LYS CA    C      sing N N 244 
LYS CA    CB     sing N N 245 
LYS CA    HA     sing N N 246 
LYS C     O      doub N N 247 
LYS C     OXT    sing N N 248 
LYS CB    CG     sing N N 249 
LYS CB    HB2    sing N N 250 
LYS CB    HB3    sing N N 251 
LYS CG    CD     sing N N 252 
LYS CG    HG2    sing N N 253 
LYS CG    HG3    sing N N 254 
LYS CD    CE     sing N N 255 
LYS CD    HD2    sing N N 256 
LYS CD    HD3    sing N N 257 
LYS CE    NZ     sing N N 258 
LYS CE    HE2    sing N N 259 
LYS CE    HE3    sing N N 260 
LYS NZ    HZ1    sing N N 261 
LYS NZ    HZ2    sing N N 262 
LYS NZ    HZ3    sing N N 263 
LYS OXT   HXT    sing N N 264 
MET N     CA     sing N N 265 
MET N     H      sing N N 266 
MET N     H2     sing N N 267 
MET CA    C      sing N N 268 
MET CA    CB     sing N N 269 
MET CA    HA     sing N N 270 
MET C     O      doub N N 271 
MET C     OXT    sing N N 272 
MET CB    CG     sing N N 273 
MET CB    HB2    sing N N 274 
MET CB    HB3    sing N N 275 
MET CG    SD     sing N N 276 
MET CG    HG2    sing N N 277 
MET CG    HG3    sing N N 278 
MET SD    CE     sing N N 279 
MET CE    HE1    sing N N 280 
MET CE    HE2    sing N N 281 
MET CE    HE3    sing N N 282 
MET OXT   HXT    sing N N 283 
PHE N     CA     sing N N 284 
PHE N     H      sing N N 285 
PHE N     H2     sing N N 286 
PHE CA    C      sing N N 287 
PHE CA    CB     sing N N 288 
PHE CA    HA     sing N N 289 
PHE C     O      doub N N 290 
PHE C     OXT    sing N N 291 
PHE CB    CG     sing N N 292 
PHE CB    HB2    sing N N 293 
PHE CB    HB3    sing N N 294 
PHE CG    CD1    doub Y N 295 
PHE CG    CD2    sing Y N 296 
PHE CD1   CE1    sing Y N 297 
PHE CD1   HD1    sing N N 298 
PHE CD2   CE2    doub Y N 299 
PHE CD2   HD2    sing N N 300 
PHE CE1   CZ     doub Y N 301 
PHE CE1   HE1    sing N N 302 
PHE CE2   CZ     sing Y N 303 
PHE CE2   HE2    sing N N 304 
PHE CZ    HZ     sing N N 305 
PHE OXT   HXT    sing N N 306 
PRO N     CA     sing N N 307 
PRO N     CD     sing N N 308 
PRO N     H      sing N N 309 
PRO CA    C      sing N N 310 
PRO CA    CB     sing N N 311 
PRO CA    HA     sing N N 312 
PRO C     O      doub N N 313 
PRO C     OXT    sing N N 314 
PRO CB    CG     sing N N 315 
PRO CB    HB2    sing N N 316 
PRO CB    HB3    sing N N 317 
PRO CG    CD     sing N N 318 
PRO CG    HG2    sing N N 319 
PRO CG    HG3    sing N N 320 
PRO CD    HD2    sing N N 321 
PRO CD    HD3    sing N N 322 
PRO OXT   HXT    sing N N 323 
SER N     CA     sing N N 324 
SER N     H      sing N N 325 
SER N     H2     sing N N 326 
SER CA    C      sing N N 327 
SER CA    CB     sing N N 328 
SER CA    HA     sing N N 329 
SER C     O      doub N N 330 
SER C     OXT    sing N N 331 
SER CB    OG     sing N N 332 
SER CB    HB2    sing N N 333 
SER CB    HB3    sing N N 334 
SER OG    HG     sing N N 335 
SER OXT   HXT    sing N N 336 
THR N     CA     sing N N 337 
THR N     H      sing N N 338 
THR N     H2     sing N N 339 
THR CA    C      sing N N 340 
THR CA    CB     sing N N 341 
THR CA    HA     sing N N 342 
THR C     O      doub N N 343 
THR C     OXT    sing N N 344 
THR CB    OG1    sing N N 345 
THR CB    CG2    sing N N 346 
THR CB    HB     sing N N 347 
THR OG1   HG1    sing N N 348 
THR CG2   HG21   sing N N 349 
THR CG2   HG22   sing N N 350 
THR CG2   HG23   sing N N 351 
THR OXT   HXT    sing N N 352 
TRP N     CA     sing N N 353 
TRP N     H      sing N N 354 
TRP N     H2     sing N N 355 
TRP CA    C      sing N N 356 
TRP CA    CB     sing N N 357 
TRP CA    HA     sing N N 358 
TRP C     O      doub N N 359 
TRP C     OXT    sing N N 360 
TRP CB    CG     sing N N 361 
TRP CB    HB2    sing N N 362 
TRP CB    HB3    sing N N 363 
TRP CG    CD1    doub Y N 364 
TRP CG    CD2    sing Y N 365 
TRP CD1   NE1    sing Y N 366 
TRP CD1   HD1    sing N N 367 
TRP CD2   CE2    doub Y N 368 
TRP CD2   CE3    sing Y N 369 
TRP NE1   CE2    sing Y N 370 
TRP NE1   HE1    sing N N 371 
TRP CE2   CZ2    sing Y N 372 
TRP CE3   CZ3    doub Y N 373 
TRP CE3   HE3    sing N N 374 
TRP CZ2   CH2    doub Y N 375 
TRP CZ2   HZ2    sing N N 376 
TRP CZ3   CH2    sing Y N 377 
TRP CZ3   HZ3    sing N N 378 
TRP CH2   HH2    sing N N 379 
TRP OXT   HXT    sing N N 380 
TTP PA    O1A    doub N N 381 
TTP PA    O2A    sing N N 382 
TTP PA    O3A    sing N N 383 
TTP PA    "O5'"  sing N N 384 
TTP O2A   HOA2   sing N N 385 
TTP O3A   PB     sing N N 386 
TTP PB    O1B    doub N N 387 
TTP PB    O2B    sing N N 388 
TTP PB    O3B    sing N N 389 
TTP O2B   HOB2   sing N N 390 
TTP O3B   PG     sing N N 391 
TTP PG    O1G    doub N N 392 
TTP PG    O2G    sing N N 393 
TTP PG    O3G    sing N N 394 
TTP O2G   HOG2   sing N N 395 
TTP O3G   HOG3   sing N N 396 
TTP "O5'" "C5'"  sing N N 397 
TTP "C5'" "C4'"  sing N N 398 
TTP "C5'" "H5'1" sing N N 399 
TTP "C5'" "H5'2" sing N N 400 
TTP "C4'" "O4'"  sing N N 401 
TTP "C4'" "C3'"  sing N N 402 
TTP "C4'" "H4'"  sing N N 403 
TTP "O4'" "C1'"  sing N N 404 
TTP "C3'" "O3'"  sing N N 405 
TTP "C3'" "C2'"  sing N N 406 
TTP "C3'" "H3'"  sing N N 407 
TTP "O3'" "HO3'" sing N N 408 
TTP "C2'" "C1'"  sing N N 409 
TTP "C2'" "H2'1" sing N N 410 
TTP "C2'" "H2'2" sing N N 411 
TTP "C1'" N1     sing N N 412 
TTP "C1'" "H1'"  sing N N 413 
TTP N1    C2     sing N N 414 
TTP N1    C6     sing N N 415 
TTP C2    O2     doub N N 416 
TTP C2    N3     sing N N 417 
TTP N3    C4     sing N N 418 
TTP N3    HN3    sing N N 419 
TTP C4    O4     doub N N 420 
TTP C4    C5     sing N N 421 
TTP C5    C5M    sing N N 422 
TTP C5    C6     doub N N 423 
TTP C5M   HM51   sing N N 424 
TTP C5M   HM52   sing N N 425 
TTP C5M   HM53   sing N N 426 
TTP C6    H6     sing N N 427 
TYR N     CA     sing N N 428 
TYR N     H      sing N N 429 
TYR N     H2     sing N N 430 
TYR CA    C      sing N N 431 
TYR CA    CB     sing N N 432 
TYR CA    HA     sing N N 433 
TYR C     O      doub N N 434 
TYR C     OXT    sing N N 435 
TYR CB    CG     sing N N 436 
TYR CB    HB2    sing N N 437 
TYR CB    HB3    sing N N 438 
TYR CG    CD1    doub Y N 439 
TYR CG    CD2    sing Y N 440 
TYR CD1   CE1    sing Y N 441 
TYR CD1   HD1    sing N N 442 
TYR CD2   CE2    doub Y N 443 
TYR CD2   HD2    sing N N 444 
TYR CE1   CZ     doub Y N 445 
TYR CE1   HE1    sing N N 446 
TYR CE2   CZ     sing Y N 447 
TYR CE2   HE2    sing N N 448 
TYR CZ    OH     sing N N 449 
TYR OH    HH     sing N N 450 
TYR OXT   HXT    sing N N 451 
VAL N     CA     sing N N 452 
VAL N     H      sing N N 453 
VAL N     H2     sing N N 454 
VAL CA    C      sing N N 455 
VAL CA    CB     sing N N 456 
VAL CA    HA     sing N N 457 
VAL C     O      doub N N 458 
VAL C     OXT    sing N N 459 
VAL CB    CG1    sing N N 460 
VAL CB    CG2    sing N N 461 
VAL CB    HB     sing N N 462 
VAL CG1   HG11   sing N N 463 
VAL CG1   HG12   sing N N 464 
VAL CG1   HG13   sing N N 465 
VAL CG2   HG21   sing N N 466 
VAL CG2   HG22   sing N N 467 
VAL CG2   HG23   sing N N 468 
VAL OXT   HXT    sing N N 469 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-05-22 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9BX3 
_em_admin.last_update        2025-03-26 
_em_admin.map_release_date   2025-03-19 
_em_admin.title              'Class 5 model for preturnover condition of Bacillus subtilis ribonucleotide reductase complex' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          1423 
_em_entity_assembly_naturalsource.organism             'Bacillus subtilis' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          562 
_em_entity_assembly_recombinant.organism             'Escherichia coli' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         50 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       COUNTING 
_em_image_recording.film_or_detector_model              'GATAN K3 BIOQUANTUM (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
_em_imaging_optics.chr_aberration_corrector   ? 
_em_imaging_optics.energyfilter_lower         ? 
_em_imaging_optics.energyfilter_slit_width    20 
_em_imaging_optics.energyfilter_name          ? 
_em_imaging_optics.energyfilter_upper         ? 
_em_imaging_optics.id                         1 
_em_imaging_optics.imaging_id                 1 
_em_imaging_optics.phase_plate                ? 
_em_imaging_optics.sph_aberration_corrector   ? 
_em_imaging_optics.details                    ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'       ? 1  1 ? ? ?               ? 
'IMAGE ACQUISITION'        ? 2  ? ? ? ?               ? 
MASKING                    ? 3  ? ? ? ?               ? 
'CTF CORRECTION'           ? 4  1 ? ? ?               ? 
'LAYERLINE INDEXING'       ? 5  ? ? ? ?               ? 
'DIFFRACTION INDEXING'     ? 6  ? ? ? ?               ? 
'MODEL FITTING'            ? 7  ? 1 ? 'UCSF ChimeraX' ? 
OTHER                      ? 8  ? ? ? ?               ? 
'INITIAL EULER ASSIGNMENT' ? 9  1 ? ? RELION          ? 
'FINAL EULER ASSIGNMENT'   ? 10 1 ? ? RELION          ? 
CLASSIFICATION             ? 11 1 ? ? ?               ? 
RECONSTRUCTION             ? 12 1 ? ? RELION          ? 
'MODEL REFINEMENT'         ? 13 ? 1 ? ?               ? 
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
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 
# 
loop_
_pdbx_initial_refinement_model.id 
_pdbx_initial_refinement_model.type 
_pdbx_initial_refinement_model.source_name 
_pdbx_initial_refinement_model.accession_code 
1 'experimental model' PDB 9BW3 
2 'experimental model' PDB 4DR0 
# 
_atom_sites.entry_id                    9BX3 
_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 
MN 
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   ? 103.806 120.965 99.810  1.00 57.38 ?  6   VAL A N     1 
ATOM   2     C  CA    . VAL A 1 6   ? 104.974 121.222 98.976  1.00 58.84 ?  6   VAL A CA    1 
ATOM   3     C  C     . VAL A 1 6   ? 104.619 122.188 97.850  1.00 58.88 ?  6   VAL A C     1 
ATOM   4     O  O     . VAL A 1 6   ? 103.782 121.879 97.001  1.00 57.73 ?  6   VAL A O     1 
ATOM   5     C  CB    . VAL A 1 6   ? 105.551 119.915 98.409  1.00 59.47 ?  6   VAL A CB    1 
ATOM   6     C  CG1   . VAL A 1 6   ? 106.738 120.207 97.504  1.00 58.72 ?  6   VAL A CG1   1 
ATOM   7     C  CG2   . VAL A 1 6   ? 105.953 118.981 99.540  1.00 58.99 ?  6   VAL A CG2   1 
ATOM   8     N  N     . PRO A 1 7   ? 105.257 123.355 97.843  1.00 57.06 ?  7   PRO A N     1 
ATOM   9     C  CA    . PRO A 1 7   ? 104.959 124.354 96.812  1.00 50.95 ?  7   PRO A CA    1 
ATOM   10    C  C     . PRO A 1 7   ? 105.393 123.884 95.433  1.00 51.58 ?  7   PRO A C     1 
ATOM   11    O  O     . PRO A 1 7   ? 106.284 123.046 95.276  1.00 54.10 ?  7   PRO A O     1 
ATOM   12    C  CB    . PRO A 1 7   ? 105.752 125.587 97.254  1.00 48.35 ?  7   PRO A CB    1 
ATOM   13    C  CG    . PRO A 1 7   ? 106.756 125.100 98.233  1.00 51.97 ?  7   PRO A CG    1 
ATOM   14    C  CD    . PRO A 1 7   ? 106.292 123.797 98.793  1.00 53.84 ?  7   PRO A CD    1 
ATOM   15    N  N     . LYS A 1 8   ? 104.739 124.451 94.416  1.00 48.70 ?  8   LYS A N     1 
ATOM   16    C  CA    . LYS A 1 8   ? 104.996 124.032 93.042  1.00 47.13 ?  8   LYS A CA    1 
ATOM   17    C  C     . LYS A 1 8   ? 106.438 124.305 92.632  1.00 51.09 ?  8   LYS A C     1 
ATOM   18    O  O     . LYS A 1 8   ? 107.064 123.483 91.953  1.00 51.64 ?  8   LYS A O     1 
ATOM   19    C  CB    . LYS A 1 8   ? 104.029 124.734 92.089  1.00 49.32 ?  8   LYS A CB    1 
ATOM   20    C  CG    . LYS A 1 8   ? 104.357 124.529 90.620  1.00 51.24 ?  8   LYS A CG    1 
ATOM   21    C  CD    . LYS A 1 8   ? 103.444 125.352 89.729  1.00 52.40 ?  8   LYS A CD    1 
ATOM   22    C  CE    . LYS A 1 8   ? 103.863 125.254 88.272  1.00 50.26 ?  8   LYS A CE    1 
ATOM   23    N  NZ    . LYS A 1 8   ? 103.105 126.202 87.410  1.00 50.69 1  8   LYS A NZ    1 
ATOM   24    N  N     . TRP A 1 9   ? 106.979 125.465 93.018  1.00 52.70 ?  9   TRP A N     1 
ATOM   25    C  CA    . TRP A 1 9   ? 108.352 125.785 92.645  1.00 48.35 ?  9   TRP A CA    1 
ATOM   26    C  C     . TRP A 1 9   ? 109.334 124.816 93.286  1.00 49.36 ?  9   TRP A C     1 
ATOM   27    O  O     . TRP A 1 9   ? 110.334 124.434 92.668  1.00 51.99 ?  9   TRP A O     1 
ATOM   28    C  CB    . TRP A 1 9   ? 108.691 127.226 93.027  1.00 47.11 ?  9   TRP A CB    1 
ATOM   29    C  CG    . TRP A 1 9   ? 108.328 127.605 94.427  1.00 42.54 ?  9   TRP A CG    1 
ATOM   30    C  CD1   . TRP A 1 9   ? 109.137 127.557 95.523  1.00 44.10 ?  9   TRP A CD1   1 
ATOM   31    C  CD2   . TRP A 1 9   ? 107.070 128.117 94.878  1.00 45.15 ?  9   TRP A CD2   1 
ATOM   32    N  NE1   . TRP A 1 9   ? 108.457 127.996 96.633  1.00 44.97 ?  9   TRP A NE1   1 
ATOM   33    C  CE2   . TRP A 1 9   ? 107.186 128.345 96.263  1.00 46.11 ?  9   TRP A CE2   1 
ATOM   34    C  CE3   . TRP A 1 9   ? 105.855 128.396 94.248  1.00 46.87 ?  9   TRP A CE3   1 
ATOM   35    C  CZ2   . TRP A 1 9   ? 106.133 128.842 97.026  1.00 46.18 ?  9   TRP A CZ2   1 
ATOM   36    C  CZ3   . TRP A 1 9   ? 104.812 128.889 95.007  1.00 48.58 ?  9   TRP A CZ3   1 
ATOM   37    C  CH2   . TRP A 1 9   ? 104.957 129.106 96.382  1.00 47.62 ?  9   TRP A CH2   1 
ATOM   38    N  N     . ILE A 1 10  ? 109.070 124.407 94.528  1.00 50.06 ?  10  ILE A N     1 
ATOM   39    C  CA    . ILE A 1 10  ? 109.920 123.410 95.169  1.00 51.15 ?  10  ILE A CA    1 
ATOM   40    C  C     . ILE A 1 10  ? 109.826 122.080 94.434  1.00 51.21 ?  10  ILE A C     1 
ATOM   41    O  O     . ILE A 1 10  ? 110.827 121.369 94.277  1.00 53.07 ?  10  ILE A O     1 
ATOM   42    C  CB    . ILE A 1 10  ? 109.550 123.264 96.655  1.00 51.35 ?  10  ILE A CB    1 
ATOM   43    C  CG1   . ILE A 1 10  ? 110.055 124.470 97.448  1.00 49.98 ?  10  ILE A CG1   1 
ATOM   44    C  CG2   . ILE A 1 10  ? 110.120 121.974 97.216  1.00 49.70 ?  10  ILE A CG2   1 
ATOM   45    C  CD1   . ILE A 1 10  ? 111.379 125.008 96.960  1.00 51.52 ?  10  ILE A CD1   1 
ATOM   46    N  N     . GLN A 1 11  ? 108.626 121.715 93.977  1.00 53.37 ?  11  GLN A N     1 
ATOM   47    C  CA    . GLN A 1 11  ? 108.475 120.481 93.214  1.00 53.79 ?  11  GLN A CA    1 
ATOM   48    C  C     . GLN A 1 11  ? 109.275 120.537 91.919  1.00 52.95 ?  11  GLN A C     1 
ATOM   49    O  O     . GLN A 1 11  ? 109.941 119.564 91.549  1.00 56.25 ?  11  GLN A O     1 
ATOM   50    C  CB    . GLN A 1 11  ? 106.998 120.221 92.919  1.00 52.33 ?  11  GLN A CB    1 
ATOM   51    C  CG    . GLN A 1 11  ? 106.262 119.474 94.018  1.00 54.46 ?  11  GLN A CG    1 
ATOM   52    C  CD    . GLN A 1 11  ? 104.828 119.939 94.177  1.00 57.73 ?  11  GLN A CD    1 
ATOM   53    O  OE1   . GLN A 1 11  ? 104.054 119.938 93.220  1.00 56.42 ?  11  GLN A OE1   1 
ATOM   54    N  NE2   . GLN A 1 11  ? 104.467 120.341 95.389  1.00 54.44 ?  11  GLN A NE2   1 
ATOM   55    N  N     . LEU A 1 12  ? 109.217 121.668 91.215  1.00 49.15 ?  12  LEU A N     1 
ATOM   56    C  CA    . LEU A 1 12  ? 109.985 121.808 89.982  1.00 49.66 ?  12  LEU A CA    1 
ATOM   57    C  C     . LEU A 1 12  ? 111.482 121.762 90.258  1.00 50.29 ?  12  LEU A C     1 
ATOM   58    O  O     . LEU A 1 12  ? 112.238 121.113 89.525  1.00 52.22 ?  12  LEU A O     1 
ATOM   59    C  CB    . LEU A 1 12  ? 109.606 123.109 89.275  1.00 48.98 ?  12  LEU A CB    1 
ATOM   60    C  CG    . LEU A 1 12  ? 108.377 123.050 88.370  1.00 47.93 ?  12  LEU A CG    1 
ATOM   61    C  CD1   . LEU A 1 12  ? 107.858 124.447 88.078  1.00 49.80 ?  12  LEU A CD1   1 
ATOM   62    C  CD2   . LEU A 1 12  ? 108.696 122.313 87.080  1.00 50.18 ?  12  LEU A CD2   1 
ATOM   63    N  N     . ASN A 1 13  ? 111.929 122.443 91.315  1.00 47.73 ?  13  ASN A N     1 
ATOM   64    C  CA    . ASN A 1 13  ? 113.350 122.453 91.645  1.00 47.85 ?  13  ASN A CA    1 
ATOM   65    C  C     . ASN A 1 13  ? 113.839 121.061 92.023  1.00 50.76 ?  13  ASN A C     1 
ATOM   66    O  O     . ASN A 1 13  ? 114.940 120.655 91.634  1.00 54.40 ?  13  ASN A O     1 
ATOM   67    C  CB    . ASN A 1 13  ? 113.614 123.444 92.778  1.00 50.68 ?  13  ASN A CB    1 
ATOM   68    C  CG    . ASN A 1 13  ? 115.041 123.391 93.278  1.00 49.14 ?  13  ASN A CG    1 
ATOM   69    O  OD1   . ASN A 1 13  ? 115.338 122.736 94.275  1.00 51.51 ?  13  ASN A OD1   1 
ATOM   70    N  ND2   . ASN A 1 13  ? 115.935 124.087 92.586  1.00 50.96 ?  13  ASN A ND2   1 
ATOM   71    N  N     . ASN A 1 14  ? 113.036 120.314 92.784  1.00 54.17 ?  14  ASN A N     1 
ATOM   72    C  CA    . ASN A 1 14  ? 113.420 118.959 93.158  1.00 54.23 ?  14  ASN A CA    1 
ATOM   73    C  C     . ASN A 1 14  ? 113.511 118.035 91.952  1.00 55.31 ?  14  ASN A C     1 
ATOM   74    O  O     . ASN A 1 14  ? 114.126 116.968 92.050  1.00 59.49 ?  14  ASN A O     1 
ATOM   75    C  CB    . ASN A 1 14  ? 112.431 118.392 94.176  1.00 54.11 ?  14  ASN A CB    1 
ATOM   76    C  CG    . ASN A 1 14  ? 112.673 118.917 95.575  1.00 56.75 ?  14  ASN A CG    1 
ATOM   77    O  OD1   . ASN A 1 14  ? 112.217 118.332 96.558  1.00 58.87 ?  14  ASN A OD1   1 
ATOM   78    N  ND2   . ASN A 1 14  ? 113.394 120.027 95.674  1.00 56.50 ?  14  ASN A ND2   1 
ATOM   79    N  N     . GLU A 1 15  ? 112.914 118.417 90.823  1.00 53.98 ?  15  GLU A N     1 
ATOM   80    C  CA    . GLU A 1 15  ? 113.045 117.643 89.597  1.00 55.74 ?  15  GLU A CA    1 
ATOM   81    C  C     . GLU A 1 15  ? 114.438 117.740 88.994  1.00 56.99 ?  15  GLU A C     1 
ATOM   82    O  O     . GLU A 1 15  ? 114.738 117.003 88.050  1.00 58.83 ?  15  GLU A O     1 
ATOM   83    C  CB    . GLU A 1 15  ? 112.005 118.104 88.575  1.00 56.39 ?  15  GLU A CB    1 
ATOM   84    C  CG    . GLU A 1 15  ? 110.674 117.377 88.676  1.00 57.14 ?  15  GLU A CG    1 
ATOM   85    C  CD    . GLU A 1 15  ? 109.557 118.103 87.952  1.00 61.00 ?  15  GLU A CD    1 
ATOM   86    O  OE1   . GLU A 1 15  ? 109.667 118.294 86.723  1.00 60.78 ?  15  GLU A OE1   1 
ATOM   87    O  OE2   . GLU A 1 15  ? 108.568 118.484 88.614  1.00 60.40 -1 15  GLU A OE2   1 
ATOM   88    N  N     . ILE A 1 16  ? 115.288 118.630 89.509  1.00 57.72 ?  16  ILE A N     1 
ATOM   89    C  CA    . ILE A 1 16  ? 116.657 118.736 89.010  1.00 57.43 ?  16  ILE A CA    1 
ATOM   90    C  C     . ILE A 1 16  ? 117.378 117.405 89.171  1.00 57.92 ?  16  ILE A C     1 
ATOM   91    O  O     . ILE A 1 16  ? 118.029 116.913 88.243  1.00 57.58 ?  16  ILE A O     1 
ATOM   92    C  CB    . ILE A 1 16  ? 117.407 119.867 89.739  1.00 58.11 ?  16  ILE A CB    1 
ATOM   93    C  CG1   . ILE A 1 16  ? 116.804 121.231 89.396  1.00 55.27 ?  16  ILE A CG1   1 
ATOM   94    C  CG2   . ILE A 1 16  ? 118.887 119.834 89.391  1.00 57.10 ?  16  ILE A CG2   1 
ATOM   95    C  CD1   . ILE A 1 16  ? 116.854 121.572 87.933  1.00 55.09 ?  16  ILE A CD1   1 
ATOM   96    N  N     . MET A 1 17  ? 117.266 116.799 90.355  1.00 59.08 ?  17  MET A N     1 
ATOM   97    C  CA    . MET A 1 17  ? 118.004 115.578 90.648  1.00 58.90 ?  17  MET A CA    1 
ATOM   98    C  C     . MET A 1 17  ? 117.375 114.346 90.012  1.00 58.88 ?  17  MET A C     1 
ATOM   99    O  O     . MET A 1 17  ? 118.019 113.292 89.966  1.00 59.27 ?  17  MET A O     1 
ATOM   100   C  CB    . MET A 1 17  ? 118.114 115.385 92.160  1.00 58.46 ?  17  MET A CB    1 
ATOM   101   C  CG    . MET A 1 17  ? 118.782 116.546 92.877  1.00 58.20 ?  17  MET A CG    1 
ATOM   102   S  SD    . MET A 1 17  ? 120.393 116.956 92.183  1.00 64.09 ?  17  MET A SD    1 
ATOM   103   C  CE    . MET A 1 17  ? 121.462 115.913 93.170  1.00 59.51 ?  17  MET A CE    1 
ATOM   104   N  N     . ILE A 1 18  ? 116.141 114.450 89.524  1.00 62.11 ?  18  ILE A N     1 
ATOM   105   C  CA    . ILE A 1 18  ? 115.482 113.336 88.844  1.00 62.69 ?  18  ILE A CA    1 
ATOM   106   C  C     . ILE A 1 18  ? 116.102 113.234 87.455  1.00 63.15 ?  18  ILE A C     1 
ATOM   107   O  O     . ILE A 1 18  ? 115.731 113.969 86.539  1.00 64.19 ?  18  ILE A O     1 
ATOM   108   C  CB    . ILE A 1 18  ? 113.966 113.521 88.778  1.00 62.13 ?  18  ILE A CB    1 
ATOM   109   C  CG1   . ILE A 1 18  ? 113.358 113.428 90.179  1.00 62.42 ?  18  ILE A CG1   1 
ATOM   110   C  CG2   . ILE A 1 18  ? 113.344 112.490 87.849  1.00 61.08 ?  18  ILE A CG2   1 
ATOM   111   C  CD1   . ILE A 1 18  ? 111.861 113.630 90.211  1.00 63.95 ?  18  ILE A CD1   1 
ATOM   112   N  N     . GLN A 1 19  ? 117.054 112.319 87.294  1.00 66.16 ?  19  GLN A N     1 
ATOM   113   C  CA    . GLN A 1 19  ? 117.780 112.208 86.037  1.00 67.05 ?  19  GLN A CA    1 
ATOM   114   C  C     . GLN A 1 19  ? 116.865 111.684 84.939  1.00 66.62 ?  19  GLN A C     1 
ATOM   115   O  O     . GLN A 1 19  ? 116.190 110.664 85.109  1.00 68.63 ?  19  GLN A O     1 
ATOM   116   C  CB    . GLN A 1 19  ? 118.990 111.290 86.206  1.00 68.03 ?  19  GLN A CB    1 
ATOM   117   C  CG    . GLN A 1 19  ? 120.066 111.854 87.120  1.00 67.68 ?  19  GLN A CG    1 
ATOM   118   C  CD    . GLN A 1 19  ? 121.351 111.055 87.073  1.00 69.35 ?  19  GLN A CD    1 
ATOM   119   O  OE1   . GLN A 1 19  ? 121.432 110.026 86.401  1.00 68.61 ?  19  GLN A OE1   1 
ATOM   120   N  NE2   . GLN A 1 19  ? 122.367 111.524 87.789  1.00 66.70 ?  19  GLN A NE2   1 
ATOM   121   N  N     . LYS A 1 20  ? 116.847 112.386 83.809  1.00 67.41 ?  20  LYS A N     1 
ATOM   122   C  CA    . LYS A 1 20  ? 116.085 111.984 82.634  1.00 68.91 ?  20  LYS A CA    1 
ATOM   123   C  C     . LYS A 1 20  ? 117.055 111.810 81.477  1.00 70.42 ?  20  LYS A C     1 
ATOM   124   O  O     . LYS A 1 20  ? 117.824 112.726 81.168  1.00 70.57 ?  20  LYS A O     1 
ATOM   125   C  CB    . LYS A 1 20  ? 115.010 113.017 82.291  1.00 68.12 ?  20  LYS A CB    1 
ATOM   126   C  CG    . LYS A 1 20  ? 114.640 113.068 80.818  1.00 68.29 ?  20  LYS A CG    1 
ATOM   127   C  CD    . LYS A 1 20  ? 114.764 114.479 80.267  1.00 68.94 ?  20  LYS A CD    1 
ATOM   128   C  CE    . LYS A 1 20  ? 114.757 114.483 78.746  1.00 70.09 ?  20  LYS A CE    1 
ATOM   129   N  NZ    . LYS A 1 20  ? 114.692 115.863 78.195  1.00 68.36 1  20  LYS A NZ    1 
ATOM   130   N  N     . ASP A 1 21  ? 117.021 110.639 80.845  1.00 71.02 ?  21  ASP A N     1 
ATOM   131   C  CA    . ASP A 1 21  ? 117.945 110.285 79.773  1.00 70.06 ?  21  ASP A CA    1 
ATOM   132   C  C     . ASP A 1 21  ? 119.382 110.169 80.268  1.00 70.99 ?  21  ASP A C     1 
ATOM   133   O  O     . ASP A 1 21  ? 120.324 110.298 79.480  1.00 70.57 ?  21  ASP A O     1 
ATOM   134   C  CB    . ASP A 1 21  ? 117.864 111.295 78.621  1.00 70.71 ?  21  ASP A CB    1 
ATOM   135   C  CG    . ASP A 1 21  ? 118.544 110.799 77.360  1.00 72.79 ?  21  ASP A CG    1 
ATOM   136   O  OD1   . ASP A 1 21  ? 118.472 109.584 77.083  1.00 73.04 ?  21  ASP A OD1   1 
ATOM   137   O  OD2   . ASP A 1 21  ? 119.151 111.626 76.647  1.00 72.01 -1 21  ASP A OD2   1 
ATOM   138   N  N     . GLY A 1 22  ? 119.571 109.928 81.564  1.00 70.01 ?  22  GLY A N     1 
ATOM   139   C  CA    . GLY A 1 22  ? 120.892 109.836 82.145  1.00 69.00 ?  22  GLY A CA    1 
ATOM   140   C  C     . GLY A 1 22  ? 121.513 111.156 82.543  1.00 70.59 ?  22  GLY A C     1 
ATOM   141   O  O     . GLY A 1 22  ? 122.636 111.157 83.066  1.00 71.85 ?  22  GLY A O     1 
ATOM   142   N  N     . LYS A 1 23  ? 120.829 112.274 82.323  1.00 68.91 ?  23  LYS A N     1 
ATOM   143   C  CA    . LYS A 1 23  ? 121.362 113.594 82.614  1.00 65.65 ?  23  LYS A CA    1 
ATOM   144   C  C     . LYS A 1 23  ? 120.411 114.356 83.527  1.00 66.16 ?  23  LYS A C     1 
ATOM   145   O  O     . LYS A 1 23  ? 119.192 114.164 83.481  1.00 67.79 ?  23  LYS A O     1 
ATOM   146   C  CB    . LYS A 1 23  ? 121.594 114.393 81.327  1.00 64.19 ?  23  LYS A CB    1 
ATOM   147   C  CG    . LYS A 1 23  ? 122.704 113.844 80.448  1.00 66.42 ?  23  LYS A CG    1 
ATOM   148   C  CD    . LYS A 1 23  ? 122.919 114.711 79.221  1.00 65.91 ?  23  LYS A CD    1 
ATOM   149   C  CE    . LYS A 1 23  ? 123.989 114.128 78.315  1.00 65.49 ?  23  LYS A CE    1 
ATOM   150   N  NZ    . LYS A 1 23  ? 124.146 114.917 77.062  1.00 66.02 1  23  LYS A NZ    1 
ATOM   151   N  N     . PHE A 1 24  ? 120.983 115.223 84.359  1.00 62.03 ?  24  PHE A N     1 
ATOM   152   C  CA    . PHE A 1 24  ? 120.173 116.068 85.225  1.00 57.74 ?  24  PHE A CA    1 
ATOM   153   C  C     . PHE A 1 24  ? 119.314 117.009 84.391  1.00 57.55 ?  24  PHE A C     1 
ATOM   154   O  O     . PHE A 1 24  ? 119.727 117.477 83.326  1.00 56.57 ?  24  PHE A O     1 
ATOM   155   C  CB    . PHE A 1 24  ? 121.065 116.875 86.169  1.00 55.83 ?  24  PHE A CB    1 
ATOM   156   C  CG    . PHE A 1 24  ? 121.758 116.046 87.206  1.00 57.34 ?  24  PHE A CG    1 
ATOM   157   C  CD1   . PHE A 1 24  ? 121.120 115.718 88.390  1.00 58.06 ?  24  PHE A CD1   1 
ATOM   158   C  CD2   . PHE A 1 24  ? 123.051 115.596 87.002  1.00 57.22 ?  24  PHE A CD2   1 
ATOM   159   C  CE1   . PHE A 1 24  ? 121.757 114.956 89.348  1.00 57.82 ?  24  PHE A CE1   1 
ATOM   160   C  CE2   . PHE A 1 24  ? 123.691 114.834 87.956  1.00 55.59 ?  24  PHE A CE2   1 
ATOM   161   C  CZ    . PHE A 1 24  ? 123.044 114.514 89.131  1.00 56.13 ?  24  PHE A CZ    1 
ATOM   162   N  N     . GLN A 1 25  ? 118.106 117.282 84.880  1.00 59.14 ?  25  GLN A N     1 
ATOM   163   C  CA    . GLN A 1 25  ? 117.185 118.195 84.203  1.00 57.92 ?  25  GLN A CA    1 
ATOM   164   C  C     . GLN A 1 25  ? 117.434 119.620 84.700  1.00 58.07 ?  25  GLN A C     1 
ATOM   165   O  O     . GLN A 1 25  ? 116.669 120.193 85.477  1.00 59.36 ?  25  GLN A O     1 
ATOM   166   C  CB    . GLN A 1 25  ? 115.743 117.762 84.429  1.00 58.55 ?  25  GLN A CB    1 
ATOM   167   C  CG    . GLN A 1 25  ? 115.377 116.449 83.763  1.00 58.49 ?  25  GLN A CG    1 
ATOM   168   C  CD    . GLN A 1 25  ? 114.022 115.936 84.205  1.00 59.66 ?  25  GLN A CD    1 
ATOM   169   O  OE1   . GLN A 1 25  ? 112.988 116.361 83.692  1.00 59.76 ?  25  GLN A OE1   1 
ATOM   170   N  NE2   . GLN A 1 25  ? 114.021 115.016 85.162  1.00 58.81 ?  25  GLN A NE2   1 
ATOM   171   N  N     . PHE A 1 26  ? 118.541 120.190 84.220  1.00 53.84 ?  26  PHE A N     1 
ATOM   172   C  CA    . PHE A 1 26  ? 118.930 121.526 84.656  1.00 50.41 ?  26  PHE A CA    1 
ATOM   173   C  C     . PHE A 1 26  ? 117.918 122.578 84.220  1.00 51.31 ?  26  PHE A C     1 
ATOM   174   O  O     . PHE A 1 26  ? 117.813 123.635 84.853  1.00 50.82 ?  26  PHE A O     1 
ATOM   175   C  CB    . PHE A 1 26  ? 120.320 121.869 84.120  1.00 49.05 ?  26  PHE A CB    1 
ATOM   176   C  CG    . PHE A 1 26  ? 121.419 121.031 84.710  1.00 50.87 ?  26  PHE A CG    1 
ATOM   177   C  CD1   . PHE A 1 26  ? 121.629 121.003 86.077  1.00 49.00 ?  26  PHE A CD1   1 
ATOM   178   C  CD2   . PHE A 1 26  ? 122.237 120.268 83.896  1.00 49.74 ?  26  PHE A CD2   1 
ATOM   179   C  CE1   . PHE A 1 26  ? 122.638 120.231 86.622  1.00 48.13 ?  26  PHE A CE1   1 
ATOM   180   C  CE2   . PHE A 1 26  ? 123.247 119.495 84.436  1.00 48.73 ?  26  PHE A CE2   1 
ATOM   181   C  CZ    . PHE A 1 26  ? 123.447 119.477 85.800  1.00 49.15 ?  26  PHE A CZ    1 
ATOM   182   N  N     . ASP A 1 27  ? 117.167 122.312 83.150  1.00 53.81 ?  27  ASP A N     1 
ATOM   183   C  CA    . ASP A 1 27  ? 116.176 123.271 82.681  1.00 52.97 ?  27  ASP A CA    1 
ATOM   184   C  C     . ASP A 1 27  ? 115.009 123.420 83.648  1.00 53.10 ?  27  ASP A C     1 
ATOM   185   O  O     . ASP A 1 27  ? 114.234 124.374 83.522  1.00 52.04 ?  27  ASP A O     1 
ATOM   186   C  CB    . ASP A 1 27  ? 115.659 122.864 81.301  1.00 54.53 ?  27  ASP A CB    1 
ATOM   187   C  CG    . ASP A 1 27  ? 115.154 121.434 81.266  1.00 57.76 ?  27  ASP A CG    1 
ATOM   188   O  OD1   . ASP A 1 27  ? 115.971 120.510 81.459  1.00 55.72 ?  27  ASP A OD1   1 
ATOM   189   O  OD2   . ASP A 1 27  ? 113.941 121.238 81.046  1.00 57.67 -1 27  ASP A OD2   1 
ATOM   190   N  N     . LYS A 1 28  ? 114.864 122.502 84.606  1.00 49.79 ?  28  LYS A N     1 
ATOM   191   C  CA    . LYS A 1 28  ? 113.793 122.616 85.587  1.00 52.49 ?  28  LYS A CA    1 
ATOM   192   C  C     . LYS A 1 28  ? 113.981 123.805 86.519  1.00 54.07 ?  28  LYS A C     1 
ATOM   193   O  O     . LYS A 1 28  ? 113.008 124.251 87.136  1.00 55.04 ?  28  LYS A O     1 
ATOM   194   C  CB    . LYS A 1 28  ? 113.689 121.328 86.406  1.00 54.50 ?  28  LYS A CB    1 
ATOM   195   C  CG    . LYS A 1 28  ? 112.639 120.353 85.898  1.00 52.75 ?  28  LYS A CG    1 
ATOM   196   C  CD    . LYS A 1 28  ? 112.754 120.153 84.397  1.00 56.69 ?  28  LYS A CD    1 
ATOM   197   C  CE    . LYS A 1 28  ? 111.395 119.902 83.769  1.00 54.64 ?  28  LYS A CE    1 
ATOM   198   N  NZ    . LYS A 1 28  ? 110.586 118.936 84.560  1.00 55.04 1  28  LYS A NZ    1 
ATOM   199   N  N     . ASP A 1 29  ? 115.203 124.329 86.636  1.00 52.08 ?  29  ASP A N     1 
ATOM   200   C  CA    . ASP A 1 29  ? 115.443 125.474 87.505  1.00 50.49 ?  29  ASP A CA    1 
ATOM   201   C  C     . ASP A 1 29  ? 114.849 126.763 86.956  1.00 47.92 ?  29  ASP A C     1 
ATOM   202   O  O     . ASP A 1 29  ? 114.339 127.574 87.736  1.00 46.99 ?  29  ASP A O     1 
ATOM   203   C  CB    . ASP A 1 29  ? 116.944 125.657 87.736  1.00 47.41 ?  29  ASP A CB    1 
ATOM   204   C  CG    . ASP A 1 29  ? 117.269 126.010 89.172  1.00 48.01 ?  29  ASP A CG    1 
ATOM   205   O  OD1   . ASP A 1 29  ? 116.327 126.126 89.984  1.00 48.39 ?  29  ASP A OD1   1 
ATOM   206   O  OD2   . ASP A 1 29  ? 118.466 126.174 89.488  1.00 49.55 -1 29  ASP A OD2   1 
ATOM   207   N  N     . LYS A 1 30  ? 114.907 126.977 85.640  1.00 47.25 ?  30  LYS A N     1 
ATOM   208   C  CA    . LYS A 1 30  ? 114.210 128.113 85.053  1.00 49.43 ?  30  LYS A CA    1 
ATOM   209   C  C     . LYS A 1 30  ? 112.706 128.002 85.257  1.00 50.80 ?  30  LYS A C     1 
ATOM   210   O  O     . LYS A 1 30  ? 112.057 128.988 85.626  1.00 53.07 ?  30  LYS A O     1 
ATOM   211   C  CB    . LYS A 1 30  ? 114.543 128.221 83.562  1.00 49.11 ?  30  LYS A CB    1 
ATOM   212   C  CG    . LYS A 1 30  ? 113.709 129.230 82.787  1.00 49.92 ?  30  LYS A CG    1 
ATOM   213   C  CD    . LYS A 1 30  ? 113.483 130.510 83.578  1.00 55.07 ?  30  LYS A CD    1 
ATOM   214   C  CE    . LYS A 1 30  ? 112.320 131.311 83.014  1.00 53.37 ?  30  LYS A CE    1 
ATOM   215   N  NZ    . LYS A 1 30  ? 111.793 132.300 83.996  1.00 51.67 1  30  LYS A NZ    1 
ATOM   216   N  N     . GLU A 1 31  ? 112.143 126.810 85.045  1.00 49.84 ?  31  GLU A N     1 
ATOM   217   C  CA    . GLU A 1 31  ? 110.739 126.580 85.360  1.00 49.76 ?  31  GLU A CA    1 
ATOM   218   C  C     . GLU A 1 31  ? 110.472 126.755 86.848  1.00 46.63 ?  31  GLU A C     1 
ATOM   219   O  O     . GLU A 1 31  ? 109.444 127.320 87.235  1.00 50.34 ?  31  GLU A O     1 
ATOM   220   C  CB    . GLU A 1 31  ? 110.317 125.183 84.909  1.00 49.44 ?  31  GLU A CB    1 
ATOM   221   C  CG    . GLU A 1 31  ? 109.697 125.132 83.526  1.00 49.18 ?  31  GLU A CG    1 
ATOM   222   C  CD    . GLU A 1 31  ? 109.649 123.726 82.965  1.00 54.68 ?  31  GLU A CD    1 
ATOM   223   O  OE1   . GLU A 1 31  ? 110.618 122.966 83.181  1.00 55.84 ?  31  GLU A OE1   1 
ATOM   224   O  OE2   . GLU A 1 31  ? 108.643 123.379 82.313  1.00 50.92 -1 31  GLU A OE2   1 
ATOM   225   N  N     . ALA A 1 32  ? 111.381 126.268 87.694  1.00 43.42 ?  32  ALA A N     1 
ATOM   226   C  CA    . ALA A 1 32  ? 111.194 126.406 89.132  1.00 43.56 ?  32  ALA A CA    1 
ATOM   227   C  C     . ALA A 1 32  ? 111.150 127.871 89.543  1.00 47.51 ?  32  ALA A C     1 
ATOM   228   O  O     . ALA A 1 32  ? 110.283 128.276 90.324  1.00 48.81 ?  32  ALA A O     1 
ATOM   229   C  CB    . ALA A 1 32  ? 112.304 125.670 89.881  1.00 44.72 ?  32  ALA A CB    1 
ATOM   230   N  N     . VAL A 1 33  ? 112.062 128.687 89.011  1.00 48.98 ?  33  VAL A N     1 
ATOM   231   C  CA    . VAL A 1 33  ? 112.087 130.102 89.371  1.00 45.53 ?  33  VAL A CA    1 
ATOM   232   C  C     . VAL A 1 33  ? 110.873 130.823 88.796  1.00 44.38 ?  33  VAL A C     1 
ATOM   233   O  O     . VAL A 1 33  ? 110.289 131.698 89.447  1.00 45.65 ?  33  VAL A O     1 
ATOM   234   C  CB    . VAL A 1 33  ? 113.410 130.750 88.916  1.00 42.77 ?  33  VAL A CB    1 
ATOM   235   C  CG1   . VAL A 1 33  ? 113.367 131.091 87.436  1.00 41.59 ?  33  VAL A CG1   1 
ATOM   236   C  CG2   . VAL A 1 33  ? 113.704 131.991 89.744  1.00 43.68 ?  33  VAL A CG2   1 
ATOM   237   N  N     . HIS A 1 34  ? 110.472 130.473 87.573  1.00 44.87 ?  34  HIS A N     1 
ATOM   238   C  CA    . HIS A 1 34  ? 109.288 131.089 86.984  1.00 45.97 ?  34  HIS A CA    1 
ATOM   239   C  C     . HIS A 1 34  ? 108.049 130.806 87.824  1.00 45.69 ?  34  HIS A C     1 
ATOM   240   O  O     . HIS A 1 34  ? 107.257 131.712 88.112  1.00 49.21 ?  34  HIS A O     1 
ATOM   241   C  CB    . HIS A 1 34  ? 109.094 130.590 85.554  1.00 48.40 ?  34  HIS A CB    1 
ATOM   242   C  CG    . HIS A 1 34  ? 108.151 131.424 84.745  1.00 49.36 ?  34  HIS A CG    1 
ATOM   243   N  ND1   . HIS A 1 34  ? 106.782 131.350 84.890  1.00 46.93 ?  34  HIS A ND1   1 
ATOM   244   C  CD2   . HIS A 1 34  ? 108.378 132.351 83.786  1.00 50.27 ?  34  HIS A CD2   1 
ATOM   245   C  CE1   . HIS A 1 34  ? 106.207 132.195 84.053  1.00 48.16 ?  34  HIS A CE1   1 
ATOM   246   N  NE2   . HIS A 1 34  ? 107.153 132.815 83.372  1.00 49.60 ?  34  HIS A NE2   1 
ATOM   247   N  N     . SER A 1 35  ? 107.859 129.544 88.217  1.00 46.39 ?  35  SER A N     1 
ATOM   248   C  CA    . SER A 1 35  ? 106.715 129.197 89.051  1.00 46.46 ?  35  SER A CA    1 
ATOM   249   C  C     . SER A 1 35  ? 106.807 129.872 90.412  1.00 45.88 ?  35  SER A C     1 
ATOM   250   O  O     . SER A 1 35  ? 105.809 130.393 90.923  1.00 49.64 ?  35  SER A O     1 
ATOM   251   C  CB    . SER A 1 35  ? 106.618 127.680 89.208  1.00 46.71 ?  35  SER A CB    1 
ATOM   252   O  OG    . SER A 1 35  ? 107.113 127.267 90.469  1.00 48.41 ?  35  SER A OG    1 
ATOM   253   N  N     . TYR A 1 36  ? 107.999 129.879 91.013  1.00 47.65 ?  36  TYR A N     1 
ATOM   254   C  CA    . TYR A 1 36  ? 108.193 130.564 92.284  1.00 48.20 ?  36  TYR A CA    1 
ATOM   255   C  C     . TYR A 1 36  ? 107.714 132.002 92.197  1.00 46.09 ?  36  TYR A C     1 
ATOM   256   O  O     . TYR A 1 36  ? 106.899 132.449 93.008  1.00 47.50 ?  36  TYR A O     1 
ATOM   257   C  CB    . TYR A 1 36  ? 109.670 130.509 92.677  1.00 44.96 ?  36  TYR A CB    1 
ATOM   258   C  CG    . TYR A 1 36  ? 110.035 131.335 93.890  1.00 42.67 ?  36  TYR A CG    1 
ATOM   259   C  CD1   . TYR A 1 36  ? 109.447 131.096 95.123  1.00 41.35 ?  36  TYR A CD1   1 
ATOM   260   C  CD2   . TYR A 1 36  ? 110.977 132.350 93.799  1.00 44.15 ?  36  TYR A CD2   1 
ATOM   261   C  CE1   . TYR A 1 36  ? 109.787 131.847 96.231  1.00 42.72 ?  36  TYR A CE1   1 
ATOM   262   C  CE2   . TYR A 1 36  ? 111.321 133.106 94.899  1.00 43.57 ?  36  TYR A CE2   1 
ATOM   263   C  CZ    . TYR A 1 36  ? 110.724 132.851 96.112  1.00 45.46 ?  36  TYR A CZ    1 
ATOM   264   O  OH    . TYR A 1 36  ? 111.066 133.604 97.211  1.00 47.21 ?  36  TYR A OH    1 
ATOM   265   N  N     . PHE A 1 37  ? 108.185 132.734 91.189  1.00 47.56 ?  37  PHE A N     1 
ATOM   266   C  CA    . PHE A 1 37  ? 107.745 134.112 91.026  1.00 45.84 ?  37  PHE A CA    1 
ATOM   267   C  C     . PHE A 1 37  ? 106.235 134.178 90.851  1.00 47.72 ?  37  PHE A C     1 
ATOM   268   O  O     . PHE A 1 37  ? 105.527 134.709 91.712  1.00 52.74 ?  37  PHE A O     1 
ATOM   269   C  CB    . PHE A 1 37  ? 108.470 134.768 89.851  1.00 48.82 ?  37  PHE A CB    1 
ATOM   270   C  CG    . PHE A 1 37  ? 109.716 135.497 90.254  1.00 49.00 ?  37  PHE A CG    1 
ATOM   271   C  CD1   . PHE A 1 37  ? 109.651 136.804 90.705  1.00 48.77 ?  37  PHE A CD1   1 
ATOM   272   C  CD2   . PHE A 1 37  ? 110.946 134.871 90.208  1.00 46.41 ?  37  PHE A CD2   1 
ATOM   273   C  CE1   . PHE A 1 37  ? 110.793 137.475 91.088  1.00 47.40 ?  37  PHE A CE1   1 
ATOM   274   C  CE2   . PHE A 1 37  ? 112.090 135.538 90.589  1.00 48.12 ?  37  PHE A CE2   1 
ATOM   275   C  CZ    . PHE A 1 37  ? 112.013 136.840 91.030  1.00 47.73 ?  37  PHE A CZ    1 
ATOM   276   N  N     . VAL A 1 38  ? 105.724 133.561 89.782  1.00 52.14 ?  38  VAL A N     1 
ATOM   277   C  CA    . VAL A 1 38  ? 104.331 133.743 89.386  1.00 52.73 ?  38  VAL A CA    1 
ATOM   278   C  C     . VAL A 1 38  ? 103.365 133.323 90.485  1.00 52.09 ?  38  VAL A C     1 
ATOM   279   O  O     . VAL A 1 38  ? 102.231 133.817 90.541  1.00 54.14 ?  38  VAL A O     1 
ATOM   280   C  CB    . VAL A 1 38  ? 104.056 132.977 88.077  1.00 50.57 ?  38  VAL A CB    1 
ATOM   281   C  CG1   . VAL A 1 38  ? 102.571 132.713 87.919  1.00 51.77 ?  38  VAL A CG1   1 
ATOM   282   C  CG2   . VAL A 1 38  ? 104.594 133.752 86.887  1.00 50.15 ?  38  VAL A CG2   1 
ATOM   283   N  N     . ASP A 1 39  ? 103.776 132.418 91.375  1.00 48.30 ?  39  ASP A N     1 
ATOM   284   C  CA    . ASP A 1 39  ? 102.846 131.895 92.367  1.00 49.72 ?  39  ASP A CA    1 
ATOM   285   C  C     . ASP A 1 39  ? 103.084 132.408 93.780  1.00 52.34 ?  39  ASP A C     1 
ATOM   286   O  O     . ASP A 1 39  ? 102.183 132.291 94.616  1.00 56.20 ?  39  ASP A O     1 
ATOM   287   C  CB    . ASP A 1 39  ? 102.893 130.363 92.381  1.00 51.59 ?  39  ASP A CB    1 
ATOM   288   C  CG    . ASP A 1 39  ? 102.721 129.762 90.999  1.00 55.57 ?  39  ASP A CG    1 
ATOM   289   O  OD1   . ASP A 1 39  ? 102.066 130.400 90.149  1.00 55.11 ?  39  ASP A OD1   1 
ATOM   290   O  OD2   . ASP A 1 39  ? 103.239 128.651 90.763  1.00 56.65 -1 39  ASP A OD2   1 
ATOM   291   N  N     . TYR A 1 40  ? 104.257 132.966 94.081  1.00 48.49 ?  40  TYR A N     1 
ATOM   292   C  CA    . TYR A 1 40  ? 104.521 133.485 95.416  1.00 48.52 ?  40  TYR A CA    1 
ATOM   293   C  C     . TYR A 1 40  ? 104.863 134.966 95.411  1.00 53.38 ?  40  TYR A C     1 
ATOM   294   O  O     . TYR A 1 40  ? 104.287 135.732 96.192  1.00 55.01 ?  40  TYR A O     1 
ATOM   295   C  CB    . TYR A 1 40  ? 105.660 132.680 96.067  1.00 50.02 ?  40  TYR A CB    1 
ATOM   296   C  CG    . TYR A 1 40  ? 105.762 132.843 97.567  1.00 51.00 ?  40  TYR A CG    1 
ATOM   297   C  CD1   . TYR A 1 40  ? 106.232 134.023 98.128  1.00 51.01 ?  40  TYR A CD1   1 
ATOM   298   C  CD2   . TYR A 1 40  ? 105.388 131.815 98.421  1.00 52.07 ?  40  TYR A CD2   1 
ATOM   299   C  CE1   . TYR A 1 40  ? 106.327 134.173 99.497  1.00 51.12 ?  40  TYR A CE1   1 
ATOM   300   C  CE2   . TYR A 1 40  ? 105.480 131.956 99.789  1.00 52.58 ?  40  TYR A CE2   1 
ATOM   301   C  CZ    . TYR A 1 40  ? 105.949 133.137 100.323 1.00 52.64 ?  40  TYR A CZ    1 
ATOM   302   O  OH    . TYR A 1 40  ? 106.041 133.280 101.687 1.00 53.27 ?  40  TYR A OH    1 
ATOM   303   N  N     . ILE A 1 41  ? 105.770 135.398 94.535  1.00 50.58 ?  41  ILE A N     1 
ATOM   304   C  CA    . ILE A 1 41  ? 106.330 136.739 94.650  1.00 48.64 ?  41  ILE A CA    1 
ATOM   305   C  C     . ILE A 1 41  ? 105.366 137.776 94.091  1.00 47.09 ?  41  ILE A C     1 
ATOM   306   O  O     . ILE A 1 41  ? 105.102 138.804 94.724  1.00 50.90 ?  41  ILE A O     1 
ATOM   307   C  CB    . ILE A 1 41  ? 107.701 136.805 93.949  1.00 50.18 ?  41  ILE A CB    1 
ATOM   308   C  CG1   . ILE A 1 41  ? 108.656 135.769 94.547  1.00 48.40 ?  41  ILE A CG1   1 
ATOM   309   C  CG2   . ILE A 1 41  ? 108.292 138.199 94.064  1.00 47.77 ?  41  ILE A CG2   1 
ATOM   310   C  CD1   . ILE A 1 41  ? 108.845 135.902 96.037  1.00 45.19 ?  41  ILE A CD1   1 
ATOM   311   N  N     . ASN A 1 42  ? 104.823 137.524 92.899  1.00 49.10 ?  42  ASN A N     1 
ATOM   312   C  CA    . ASN A 1 42  ? 103.846 138.446 92.336  1.00 51.69 ?  42  ASN A CA    1 
ATOM   313   C  C     . ASN A 1 42  ? 102.603 138.539 93.211  1.00 53.22 ?  42  ASN A C     1 
ATOM   314   O  O     . ASN A 1 42  ? 101.967 139.597 93.272  1.00 54.19 ?  42  ASN A O     1 
ATOM   315   C  CB    . ASN A 1 42  ? 103.471 138.016 90.920  1.00 51.53 ?  42  ASN A CB    1 
ATOM   316   C  CG    . ASN A 1 42  ? 104.667 137.971 89.989  1.00 51.51 ?  42  ASN A CG    1 
ATOM   317   O  OD1   . ASN A 1 42  ? 105.753 138.431 90.336  1.00 53.29 ?  42  ASN A OD1   1 
ATOM   318   N  ND2   . ASN A 1 42  ? 104.471 137.415 88.799  1.00 53.15 ?  42  ASN A ND2   1 
ATOM   319   N  N     . GLN A 1 43  ? 102.243 137.448 93.889  1.00 57.15 ?  43  GLN A N     1 
ATOM   320   C  CA    . GLN A 1 43  ? 101.089 137.477 94.781  1.00 55.18 ?  43  GLN A CA    1 
ATOM   321   C  C     . GLN A 1 43  ? 101.392 138.248 96.059  1.00 54.33 ?  43  GLN A C     1 
ATOM   322   O  O     . GLN A 1 43  ? 100.573 139.057 96.510  1.00 56.82 ?  43  GLN A O     1 
ATOM   323   C  CB    . GLN A 1 43  ? 100.651 136.050 95.111  1.00 54.33 ?  43  GLN A CB    1 
ATOM   324   C  CG    . GLN A 1 43  ? 100.715 135.091 93.934  1.00 55.66 ?  43  GLN A CG    1 
ATOM   325   C  CD    . GLN A 1 43  ? 99.781  135.486 92.806  1.00 57.37 ?  43  GLN A CD    1 
ATOM   326   O  OE1   . GLN A 1 43  ? 99.952  136.531 92.179  1.00 56.74 ?  43  GLN A OE1   1 
ATOM   327   N  NE2   . GLN A 1 43  ? 98.790  134.645 92.540  1.00 55.86 ?  43  GLN A NE2   1 
ATOM   328   N  N     . ASN A 1 44  ? 102.564 138.019 96.654  1.00 47.34 ?  44  ASN A N     1 
ATOM   329   C  CA    . ASN A 1 44  ? 102.905 138.561 97.961  1.00 50.29 ?  44  ASN A CA    1 
ATOM   330   C  C     . ASN A 1 44  ? 103.668 139.879 97.874  1.00 51.03 ?  44  ASN A C     1 
ATOM   331   O  O     . ASN A 1 44  ? 104.348 140.257 98.834  1.00 50.25 ?  44  ASN A O     1 
ATOM   332   C  CB    . ASN A 1 44  ? 103.713 137.536 98.756  1.00 50.19 ?  44  ASN A CB    1 
ATOM   333   C  CG    . ASN A 1 44  ? 102.886 136.336 99.169  1.00 50.75 ?  44  ASN A CG    1 
ATOM   334   O  OD1   . ASN A 1 44  ? 102.430 135.563 98.328  1.00 52.81 ?  44  ASN A OD1   1 
ATOM   335   N  ND2   . ASN A 1 44  ? 102.692 136.171 100.472 1.00 50.51 ?  44  ASN A ND2   1 
ATOM   336   N  N     . THR A 1 45  ? 103.569 140.584 96.752  1.00 51.03 ?  45  THR A N     1 
ATOM   337   C  CA    . THR A 1 45  ? 104.237 141.866 96.572  1.00 53.63 ?  45  THR A CA    1 
ATOM   338   C  C     . THR A 1 45  ? 103.233 142.984 96.818  1.00 54.11 ?  45  THR A C     1 
ATOM   339   O  O     . THR A 1 45  ? 102.199 143.055 96.145  1.00 54.84 ?  45  THR A O     1 
ATOM   340   C  CB    . THR A 1 45  ? 104.838 141.982 95.171  1.00 55.43 ?  45  THR A CB    1 
ATOM   341   O  OG1   . THR A 1 45  ? 105.695 140.862 94.922  1.00 57.72 ?  45  THR A OG1   1 
ATOM   342   C  CG2   . THR A 1 45  ? 105.644 143.265 95.043  1.00 51.71 ?  45  THR A CG2   1 
ATOM   343   N  N     . VAL A 1 46  ? 103.539 143.856 97.783  1.00 52.94 ?  46  VAL A N     1 
ATOM   344   C  CA    . VAL A 1 46  ? 102.653 144.974 98.077  1.00 51.69 ?  46  VAL A CA    1 
ATOM   345   C  C     . VAL A 1 46  ? 102.496 145.827 96.829  1.00 53.87 ?  46  VAL A C     1 
ATOM   346   O  O     . VAL A 1 46  ? 103.481 146.185 96.171  1.00 52.85 ?  46  VAL A O     1 
ATOM   347   C  CB    . VAL A 1 46  ? 103.197 145.795 99.255  1.00 51.04 ?  46  VAL A CB    1 
ATOM   348   C  CG1   . VAL A 1 46  ? 102.295 146.987 99.529  1.00 49.80 ?  46  VAL A CG1   1 
ATOM   349   C  CG2   . VAL A 1 46  ? 103.326 144.922 100.491 1.00 49.66 ?  46  VAL A CG2   1 
ATOM   350   N  N     . PHE A 1 47  ? 101.252 146.157 96.496  1.00 60.05 ?  47  PHE A N     1 
ATOM   351   C  CA    . PHE A 1 47  ? 100.949 146.866 95.262  1.00 57.43 ?  47  PHE A CA    1 
ATOM   352   C  C     . PHE A 1 47  ? 100.866 148.364 95.521  1.00 59.22 ?  47  PHE A C     1 
ATOM   353   O  O     . PHE A 1 47  ? 100.207 148.803 96.469  1.00 60.06 ?  47  PHE A O     1 
ATOM   354   C  CB    . PHE A 1 47  ? 99.640  146.356 94.657  1.00 57.28 ?  47  PHE A CB    1 
ATOM   355   C  CG    . PHE A 1 47  ? 99.201  147.110 93.432  1.00 59.79 ?  47  PHE A CG    1 
ATOM   356   C  CD1   . PHE A 1 47  ? 98.438  148.261 93.542  1.00 58.17 ?  47  PHE A CD1   1 
ATOM   357   C  CD2   . PHE A 1 47  ? 99.558  146.670 92.169  1.00 60.27 ?  47  PHE A CD2   1 
ATOM   358   C  CE1   . PHE A 1 47  ? 98.038  148.954 92.417  1.00 60.79 ?  47  PHE A CE1   1 
ATOM   359   C  CE2   . PHE A 1 47  ? 99.161  147.360 91.040  1.00 59.21 ?  47  PHE A CE2   1 
ATOM   360   C  CZ    . PHE A 1 47  ? 98.399  148.503 91.164  1.00 59.06 ?  47  PHE A CZ    1 
ATOM   361   N  N     . PHE A 1 48  ? 101.541 149.138 94.677  1.00 60.22 ?  48  PHE A N     1 
ATOM   362   C  CA    . PHE A 1 48  ? 101.477 150.591 94.703  1.00 57.93 ?  48  PHE A CA    1 
ATOM   363   C  C     . PHE A 1 48  ? 101.131 151.085 93.308  1.00 56.29 ?  48  PHE A C     1 
ATOM   364   O  O     . PHE A 1 48  ? 101.615 150.542 92.311  1.00 57.19 ?  48  PHE A O     1 
ATOM   365   C  CB    . PHE A 1 48  ? 102.800 151.204 95.172  1.00 56.80 ?  48  PHE A CB    1 
ATOM   366   C  CG    . PHE A 1 48  ? 103.165 150.849 96.583  1.00 54.31 ?  48  PHE A CG    1 
ATOM   367   C  CD1   . PHE A 1 48  ? 102.592 151.518 97.650  1.00 56.43 ?  48  PHE A CD1   1 
ATOM   368   C  CD2   . PHE A 1 48  ? 104.080 149.844 96.843  1.00 53.85 ?  48  PHE A CD2   1 
ATOM   369   C  CE1   . PHE A 1 48  ? 102.925 151.191 98.949  1.00 57.20 ?  48  PHE A CE1   1 
ATOM   370   C  CE2   . PHE A 1 48  ? 104.418 149.514 98.139  1.00 55.99 ?  48  PHE A CE2   1 
ATOM   371   C  CZ    . PHE A 1 48  ? 103.839 150.189 99.194  1.00 55.96 ?  48  PHE A CZ    1 
ATOM   372   N  N     . HIS A 1 49  ? 100.287 152.117 93.240  1.00 59.22 ?  49  HIS A N     1 
ATOM   373   C  CA    . HIS A 1 49  ? 99.847  152.616 91.943  1.00 61.42 ?  49  HIS A CA    1 
ATOM   374   C  C     . HIS A 1 49  ? 101.023 153.112 91.114  1.00 61.66 ?  49  HIS A C     1 
ATOM   375   O  O     . HIS A 1 49  ? 101.121 152.814 89.918  1.00 62.30 ?  49  HIS A O     1 
ATOM   376   C  CB    . HIS A 1 49  ? 98.815  153.729 92.131  1.00 63.34 ?  49  HIS A CB    1 
ATOM   377   C  CG    . HIS A 1 49  ? 97.614  153.312 92.919  1.00 64.55 ?  49  HIS A CG    1 
ATOM   378   N  ND1   . HIS A 1 49  ? 97.446  153.633 94.248  1.00 64.53 ?  49  HIS A ND1   1 
ATOM   379   C  CD2   . HIS A 1 49  ? 96.519  152.595 92.566  1.00 63.21 ?  49  HIS A CD2   1 
ATOM   380   C  CE1   . HIS A 1 49  ? 96.301  153.135 94.680  1.00 64.24 ?  49  HIS A CE1   1 
ATOM   381   N  NE2   . HIS A 1 49  ? 95.719  152.500 93.679  1.00 64.21 ?  49  HIS A NE2   1 
ATOM   382   N  N     . ASN A 1 50  ? 101.931 153.862 91.732  1.00 62.57 ?  50  ASN A N     1 
ATOM   383   C  CA    . ASN A 1 50  ? 103.073 154.423 91.028  1.00 60.54 ?  50  ASN A CA    1 
ATOM   384   C  C     . ASN A 1 50  ? 104.249 154.517 91.989  1.00 60.31 ?  50  ASN A C     1 
ATOM   385   O  O     . ASN A 1 50  ? 104.116 154.285 93.193  1.00 61.06 ?  50  ASN A O     1 
ATOM   386   C  CB    . ASN A 1 50  ? 102.739 155.793 90.430  1.00 58.89 ?  50  ASN A CB    1 
ATOM   387   C  CG    . ASN A 1 50  ? 102.148 156.745 91.448  1.00 61.20 ?  50  ASN A CG    1 
ATOM   388   O  OD1   . ASN A 1 50  ? 102.822 157.162 92.390  1.00 61.62 ?  50  ASN A OD1   1 
ATOM   389   N  ND2   . ASN A 1 50  ? 100.881 157.095 91.264  1.00 60.72 ?  50  ASN A ND2   1 
ATOM   390   N  N     . LEU A 1 51  ? 105.413 154.862 91.436  1.00 54.62 ?  51  LEU A N     1 
ATOM   391   C  CA    . LEU A 1 51  ? 106.622 154.942 92.249  1.00 54.23 ?  51  LEU A CA    1 
ATOM   392   C  C     . LEU A 1 51  ? 106.492 156.004 93.333  1.00 54.39 ?  51  LEU A C     1 
ATOM   393   O  O     . LEU A 1 51  ? 107.029 155.844 94.434  1.00 56.36 ?  51  LEU A O     1 
ATOM   394   C  CB    . LEU A 1 51  ? 107.834 155.224 91.363  1.00 54.04 ?  51  LEU A CB    1 
ATOM   395   C  CG    . LEU A 1 51  ? 109.184 155.338 92.075  1.00 52.67 ?  51  LEU A CG    1 
ATOM   396   C  CD1   . LEU A 1 51  ? 109.568 154.015 92.719  1.00 49.93 ?  51  LEU A CD1   1 
ATOM   397   C  CD2   . LEU A 1 51  ? 110.261 155.803 91.109  1.00 52.24 ?  51  LEU A CD2   1 
ATOM   398   N  N     . LYS A 1 52  ? 105.793 157.102 93.040  1.00 57.84 ?  52  LYS A N     1 
ATOM   399   C  CA    . LYS A 1 52  ? 105.643 158.165 94.028  1.00 55.42 ?  52  LYS A CA    1 
ATOM   400   C  C     . LYS A 1 52  ? 104.917 157.663 95.268  1.00 56.26 ?  52  LYS A C     1 
ATOM   401   O  O     . LYS A 1 52  ? 105.356 157.900 96.400  1.00 55.50 ?  52  LYS A O     1 
ATOM   402   C  CB    . LYS A 1 52  ? 104.902 159.352 93.412  1.00 52.67 ?  52  LYS A CB    1 
ATOM   403   C  CG    . LYS A 1 52  ? 104.804 160.562 94.326  1.00 54.53 ?  52  LYS A CG    1 
ATOM   404   C  CD    . LYS A 1 52  ? 105.489 161.772 93.711  1.00 57.10 ?  52  LYS A CD    1 
ATOM   405   C  CE    . LYS A 1 52  ? 105.611 162.908 94.713  1.00 57.34 ?  52  LYS A CE    1 
ATOM   406   N  NZ    . LYS A 1 52  ? 106.789 162.736 95.607  1.00 57.53 1  52  LYS A NZ    1 
ATOM   407   N  N     . GLU A 1 53  ? 103.801 156.959 95.073  1.00 59.05 ?  53  GLU A N     1 
ATOM   408   C  CA    . GLU A 1 53  ? 103.046 156.441 96.207  1.00 59.68 ?  53  GLU A CA    1 
ATOM   409   C  C     . GLU A 1 53  ? 103.865 155.431 96.998  1.00 57.99 ?  53  GLU A C     1 
ATOM   410   O  O     . GLU A 1 53  ? 103.857 155.444 98.235  1.00 59.66 ?  53  GLU A O     1 
ATOM   411   C  CB    . GLU A 1 53  ? 101.739 155.816 95.721  1.00 58.03 ?  53  GLU A CB    1 
ATOM   412   C  CG    . GLU A 1 53  ? 101.007 155.001 96.772  1.00 58.63 ?  53  GLU A CG    1 
ATOM   413   C  CD    . GLU A 1 53  ? 99.954  154.093 96.171  1.00 62.49 ?  53  GLU A CD    1 
ATOM   414   O  OE1   . GLU A 1 53  ? 99.333  154.487 95.162  1.00 64.11 ?  53  GLU A OE1   1 
ATOM   415   O  OE2   . GLU A 1 53  ? 99.747  152.982 96.706  1.00 61.28 -1 53  GLU A OE2   1 
ATOM   416   N  N     . LYS A 1 54  ? 104.583 154.546 96.302  1.00 57.02 ?  54  LYS A N     1 
ATOM   417   C  CA    . LYS A 1 54  ? 105.399 153.547 96.986  1.00 54.41 ?  54  LYS A CA    1 
ATOM   418   C  C     . LYS A 1 54  ? 106.494 154.205 97.816  1.00 49.51 ?  54  LYS A C     1 
ATOM   419   O  O     . LYS A 1 54  ? 106.731 153.825 98.968  1.00 51.78 ?  54  LYS A O     1 
ATOM   420   C  CB    . LYS A 1 54  ? 106.004 152.581 95.968  1.00 54.31 ?  54  LYS A CB    1 
ATOM   421   C  CG    . LYS A 1 54  ? 106.958 151.565 96.574  1.00 52.88 ?  54  LYS A CG    1 
ATOM   422   C  CD    . LYS A 1 54  ? 107.457 150.586 95.526  1.00 52.56 ?  54  LYS A CD    1 
ATOM   423   C  CE    . LYS A 1 54  ? 108.330 149.510 96.146  1.00 54.60 ?  54  LYS A CE    1 
ATOM   424   N  NZ    . LYS A 1 54  ? 108.585 148.396 95.195  1.00 53.54 1  54  LYS A NZ    1 
ATOM   425   N  N     . LEU A 1 55  ? 107.179 155.195 97.239  1.00 50.55 ?  55  LEU A N     1 
ATOM   426   C  CA    . LEU A 1 55  ? 108.247 155.873 97.965  1.00 51.94 ?  55  LEU A CA    1 
ATOM   427   C  C     . LEU A 1 55  ? 107.699 156.643 99.159  1.00 53.70 ?  55  LEU A C     1 
ATOM   428   O  O     . LEU A 1 55  ? 108.305 156.639 100.237 1.00 56.98 ?  55  LEU A O     1 
ATOM   429   C  CB    . LEU A 1 55  ? 109.011 156.804 97.025  1.00 53.82 ?  55  LEU A CB    1 
ATOM   430   C  CG    . LEU A 1 55  ? 109.906 156.117 95.993  1.00 54.01 ?  55  LEU A CG    1 
ATOM   431   C  CD1   . LEU A 1 55  ? 110.782 157.132 95.279  1.00 54.11 ?  55  LEU A CD1   1 
ATOM   432   C  CD2   . LEU A 1 55  ? 110.753 155.039 96.651  1.00 52.34 ?  55  LEU A CD2   1 
ATOM   433   N  N     . ASP A 1 56  ? 106.557 157.312 98.988  1.00 58.44 ?  56  ASP A N     1 
ATOM   434   C  CA    . ASP A 1 56  ? 105.952 158.025 100.106 1.00 58.34 ?  56  ASP A CA    1 
ATOM   435   C  C     . ASP A 1 56  ? 105.562 157.063 101.220 1.00 58.00 ?  56  ASP A C     1 
ATOM   436   O  O     . ASP A 1 56  ? 105.786 157.347 102.401 1.00 59.76 ?  56  ASP A O     1 
ATOM   437   C  CB    . ASP A 1 56  ? 104.737 158.818 99.626  1.00 57.76 ?  56  ASP A CB    1 
ATOM   438   C  CG    . ASP A 1 56  ? 105.125 160.081 98.880  1.00 60.79 ?  56  ASP A CG    1 
ATOM   439   O  OD1   . ASP A 1 56  ? 105.967 160.844 99.399  1.00 60.29 ?  56  ASP A OD1   1 
ATOM   440   O  OD2   . ASP A 1 56  ? 104.589 160.309 97.776  1.00 60.54 -1 56  ASP A OD2   1 
ATOM   441   N  N     . TYR A 1 57  ? 104.983 155.914 100.864 1.00 53.74 ?  57  TYR A N     1 
ATOM   442   C  CA    . TYR A 1 57  ? 104.625 154.926 101.875 1.00 54.05 ?  57  TYR A CA    1 
ATOM   443   C  C     . TYR A 1 57  ? 105.862 154.409 102.596 1.00 54.65 ?  57  TYR A C     1 
ATOM   444   O  O     . TYR A 1 57  ? 105.865 154.280 103.826 1.00 55.10 ?  57  TYR A O     1 
ATOM   445   C  CB    . TYR A 1 57  ? 103.846 153.779 101.223 1.00 53.65 ?  57  TYR A CB    1 
ATOM   446   C  CG    . TYR A 1 57  ? 103.642 152.555 102.095 1.00 55.16 ?  57  TYR A CG    1 
ATOM   447   C  CD1   . TYR A 1 57  ? 104.675 151.656 102.330 1.00 54.92 ?  57  TYR A CD1   1 
ATOM   448   C  CD2   . TYR A 1 57  ? 102.410 152.300 102.681 1.00 55.05 ?  57  TYR A CD2   1 
ATOM   449   C  CE1   . TYR A 1 57  ? 104.488 150.543 103.124 1.00 58.46 ?  57  TYR A CE1   1 
ATOM   450   C  CE2   . TYR A 1 57  ? 102.213 151.189 103.475 1.00 56.42 ?  57  TYR A CE2   1 
ATOM   451   C  CZ    . TYR A 1 57  ? 103.254 150.314 103.693 1.00 57.76 ?  57  TYR A CZ    1 
ATOM   452   O  OH    . TYR A 1 57  ? 103.061 149.206 104.485 1.00 55.65 ?  57  TYR A OH    1 
ATOM   453   N  N     . LEU A 1 58  ? 106.924 154.106 101.848 1.00 51.68 ?  58  LEU A N     1 
ATOM   454   C  CA    . LEU A 1 58  ? 108.127 153.550 102.458 1.00 49.39 ?  58  LEU A CA    1 
ATOM   455   C  C     . LEU A 1 58  ? 108.796 154.557 103.385 1.00 49.36 ?  58  LEU A C     1 
ATOM   456   O  O     . LEU A 1 58  ? 109.267 154.193 104.468 1.00 48.16 ?  58  LEU A O     1 
ATOM   457   C  CB    . LEU A 1 58  ? 109.094 153.085 101.371 1.00 48.40 ?  58  LEU A CB    1 
ATOM   458   C  CG    . LEU A 1 58  ? 108.676 151.820 100.619 1.00 48.42 ?  58  LEU A CG    1 
ATOM   459   C  CD1   . LEU A 1 58  ? 109.484 151.652 99.346  1.00 49.02 ?  58  LEU A CD1   1 
ATOM   460   C  CD2   . LEU A 1 58  ? 108.816 150.595 101.510 1.00 48.06 ?  58  LEU A CD2   1 
ATOM   461   N  N     . VAL A 1 59  ? 108.854 155.826 102.976 1.00 52.24 ?  59  VAL A N     1 
ATOM   462   C  CA    . VAL A 1 59  ? 109.477 156.844 103.818 1.00 53.97 ?  59  VAL A CA    1 
ATOM   463   C  C     . VAL A 1 59  ? 108.620 157.127 105.045 1.00 55.71 ?  59  VAL A C     1 
ATOM   464   O  O     . VAL A 1 59  ? 109.135 157.262 106.162 1.00 53.73 ?  59  VAL A O     1 
ATOM   465   C  CB    . VAL A 1 59  ? 109.741 158.121 103.002 1.00 52.20 ?  59  VAL A CB    1 
ATOM   466   C  CG1   . VAL A 1 59  ? 110.079 159.276 103.928 1.00 53.79 ?  59  VAL A CG1   1 
ATOM   467   C  CG2   . VAL A 1 59  ? 110.861 157.889 102.001 1.00 52.68 ?  59  VAL A CG2   1 
ATOM   468   N  N     . GLU A 1 60  ? 107.301 157.225 104.860 1.00 58.72 ?  60  GLU A N     1 
ATOM   469   C  CA    . GLU A 1 60  ? 106.416 157.552 105.974 1.00 57.37 ?  60  GLU A CA    1 
ATOM   470   C  C     . GLU A 1 60  ? 106.444 156.470 107.047 1.00 56.97 ?  60  GLU A C     1 
ATOM   471   O  O     . GLU A 1 60  ? 106.437 156.775 108.246 1.00 59.67 ?  60  GLU A O     1 
ATOM   472   C  CB    . GLU A 1 60  ? 104.991 157.767 105.459 1.00 56.25 ?  60  GLU A CB    1 
ATOM   473   C  CG    . GLU A 1 60  ? 104.086 156.550 105.585 1.00 58.58 ?  60  GLU A CG    1 
ATOM   474   C  CD    . GLU A 1 60  ? 102.847 156.646 104.715 1.00 60.27 ?  60  GLU A CD    1 
ATOM   475   O  OE1   . GLU A 1 60  ? 102.694 157.658 103.999 1.00 59.44 ?  60  GLU A OE1   1 
ATOM   476   O  OE2   . GLU A 1 60  ? 102.026 155.706 104.747 1.00 58.16 -1 60  GLU A OE2   1 
ATOM   477   N  N     . ASN A 1 61  ? 106.476 155.202 106.640 1.00 52.26 ?  61  ASN A N     1 
ATOM   478   C  CA    . ASN A 1 61  ? 106.394 154.082 107.566 1.00 53.93 ?  61  ASN A CA    1 
ATOM   479   C  C     . ASN A 1 61  ? 107.749 153.695 108.148 1.00 54.74 ?  61  ASN A C     1 
ATOM   480   O  O     . ASN A 1 61  ? 107.900 152.577 108.654 1.00 55.20 ?  61  ASN A O     1 
ATOM   481   C  CB    . ASN A 1 61  ? 105.750 152.878 106.878 1.00 56.03 ?  61  ASN A CB    1 
ATOM   482   C  CG    . ASN A 1 61  ? 104.246 153.013 106.764 1.00 58.58 ?  61  ASN A CG    1 
ATOM   483   O  OD1   . ASN A 1 61  ? 103.723 153.396 105.718 1.00 57.79 ?  61  ASN A OD1   1 
ATOM   484   N  ND2   . ASN A 1 61  ? 103.540 152.698 107.843 1.00 57.00 ?  61  ASN A ND2   1 
ATOM   485   N  N     . GLN A 1 62  ? 108.733 154.592 108.091 1.00 53.30 ?  62  GLN A N     1 
ATOM   486   C  CA    . GLN A 1 62  ? 110.041 154.356 108.698 1.00 53.93 ?  62  GLN A CA    1 
ATOM   487   C  C     . GLN A 1 62  ? 110.762 153.182 108.041 1.00 53.54 ?  62  GLN A C     1 
ATOM   488   O  O     . GLN A 1 62  ? 111.475 152.422 108.698 1.00 53.09 ?  62  GLN A O     1 
ATOM   489   C  CB    . GLN A 1 62  ? 109.914 154.137 110.207 1.00 54.39 ?  62  GLN A CB    1 
ATOM   490   C  CG    . GLN A 1 62  ? 109.072 155.183 110.921 1.00 52.62 ?  62  GLN A CG    1 
ATOM   491   C  CD    . GLN A 1 62  ? 109.536 156.597 110.636 1.00 54.90 ?  62  GLN A CD    1 
ATOM   492   O  OE1   . GLN A 1 62  ? 110.533 157.058 111.192 1.00 57.28 ?  62  GLN A OE1   1 
ATOM   493   N  NE2   . GLN A 1 62  ? 108.813 157.294 109.769 1.00 52.77 ?  62  GLN A NE2   1 
ATOM   494   N  N     . TYR A 1 63  ? 110.574 153.028 106.730 1.00 49.69 ?  63  TYR A N     1 
ATOM   495   C  CA    . TYR A 1 63  ? 111.292 152.025 105.952 1.00 47.31 ?  63  TYR A CA    1 
ATOM   496   C  C     . TYR A 1 63  ? 112.549 152.607 105.314 1.00 49.70 ?  63  TYR A C     1 
ATOM   497   O  O     . TYR A 1 63  ? 113.653 152.098 105.526 1.00 46.66 ?  63  TYR A O     1 
ATOM   498   C  CB    . TYR A 1 63  ? 110.379 151.431 104.870 1.00 48.86 ?  63  TYR A CB    1 
ATOM   499   C  CG    . TYR A 1 63  ? 109.339 150.469 105.389 1.00 50.12 ?  63  TYR A CG    1 
ATOM   500   C  CD1   . TYR A 1 63  ? 109.704 149.357 106.135 1.00 48.82 ?  63  TYR A CD1   1 
ATOM   501   C  CD2   . TYR A 1 63  ? 107.991 150.665 105.124 1.00 50.82 ?  63  TYR A CD2   1 
ATOM   502   C  CE1   . TYR A 1 63  ? 108.757 148.473 106.607 1.00 48.46 ?  63  TYR A CE1   1 
ATOM   503   C  CE2   . TYR A 1 63  ? 107.036 149.786 105.592 1.00 48.80 ?  63  TYR A CE2   1 
ATOM   504   C  CZ    . TYR A 1 63  ? 107.425 148.692 106.331 1.00 52.11 ?  63  TYR A CZ    1 
ATOM   505   O  OH    . TYR A 1 63  ? 106.477 147.813 106.800 1.00 53.81 ?  63  TYR A OH    1 
ATOM   506   N  N     . TYR A 1 64  ? 112.396 153.672 104.536 1.00 47.09 ?  64  TYR A N     1 
ATOM   507   C  CA    . TYR A 1 64  ? 113.505 154.320 103.854 1.00 42.55 ?  64  TYR A CA    1 
ATOM   508   C  C     . TYR A 1 64  ? 113.880 155.610 104.568 1.00 46.64 ?  64  TYR A C     1 
ATOM   509   O  O     . TYR A 1 64  ? 113.011 156.413 104.919 1.00 49.04 ?  64  TYR A O     1 
ATOM   510   C  CB    . TYR A 1 64  ? 113.147 154.636 102.401 1.00 42.06 ?  64  TYR A CB    1 
ATOM   511   C  CG    . TYR A 1 64  ? 113.119 153.440 101.486 1.00 44.45 ?  64  TYR A CG    1 
ATOM   512   C  CD1   . TYR A 1 64  ? 113.537 152.192 101.924 1.00 43.06 ?  64  TYR A CD1   1 
ATOM   513   C  CD2   . TYR A 1 64  ? 112.676 153.560 100.177 1.00 44.58 ?  64  TYR A CD2   1 
ATOM   514   C  CE1   . TYR A 1 64  ? 113.510 151.099 101.085 1.00 39.71 ?  64  TYR A CE1   1 
ATOM   515   C  CE2   . TYR A 1 64  ? 112.646 152.475 99.333  1.00 42.68 ?  64  TYR A CE2   1 
ATOM   516   C  CZ    . TYR A 1 64  ? 113.062 151.247 99.790  1.00 41.13 ?  64  TYR A CZ    1 
ATOM   517   O  OH    . TYR A 1 64  ? 113.031 150.165 98.943  1.00 44.46 ?  64  TYR A OH    1 
ATOM   518   N  N     . GLU A 1 65  ? 115.177 155.806 104.778 1.00 51.56 ?  65  GLU A N     1 
ATOM   519   C  CA    . GLU A 1 65  ? 115.662 157.091 105.261 1.00 47.56 ?  65  GLU A CA    1 
ATOM   520   C  C     . GLU A 1 65  ? 115.367 158.167 104.224 1.00 50.10 ?  65  GLU A C     1 
ATOM   521   O  O     . GLU A 1 65  ? 115.585 157.965 103.026 1.00 51.87 ?  65  GLU A O     1 
ATOM   522   C  CB    . GLU A 1 65  ? 117.161 157.019 105.549 1.00 44.92 ?  65  GLU A CB    1 
ATOM   523   C  CG    . GLU A 1 65  ? 117.515 156.314 106.851 1.00 48.31 ?  65  GLU A CG    1 
ATOM   524   C  CD    . GLU A 1 65  ? 118.939 155.787 106.865 1.00 52.51 ?  65  GLU A CD    1 
ATOM   525   O  OE1   . GLU A 1 65  ? 119.734 156.193 105.992 1.00 52.91 ?  65  GLU A OE1   1 
ATOM   526   O  OE2   . GLU A 1 65  ? 119.264 154.969 107.750 1.00 52.38 -1 65  GLU A OE2   1 
ATOM   527   N  N     . GLU A 1 66  ? 114.863 159.313 104.682 1.00 49.85 ?  66  GLU A N     1 
ATOM   528   C  CA    . GLU A 1 66  ? 114.535 160.405 103.774 1.00 49.11 ?  66  GLU A CA    1 
ATOM   529   C  C     . GLU A 1 66  ? 115.738 161.298 103.495 1.00 49.64 ?  66  GLU A C     1 
ATOM   530   O  O     . GLU A 1 66  ? 115.650 162.196 102.653 1.00 51.18 ?  66  GLU A O     1 
ATOM   531   C  CB    . GLU A 1 66  ? 113.398 161.248 104.362 1.00 50.03 ?  66  GLU A CB    1 
ATOM   532   C  CG    . GLU A 1 66  ? 112.782 162.306 103.439 1.00 51.19 ?  66  GLU A CG    1 
ATOM   533   C  CD    . GLU A 1 66  ? 112.757 161.901 101.967 1.00 55.13 ?  66  GLU A CD    1 
ATOM   534   O  OE1   . GLU A 1 66  ? 113.817 161.783 101.328 1.00 53.06 ?  66  GLU A OE1   1 
ATOM   535   O  OE2   . GLU A 1 66  ? 111.642 161.699 101.442 1.00 54.23 -1 66  GLU A OE2   1 
ATOM   536   N  N     . GLU A 1 67  ? 116.851 161.093 104.198 1.00 50.01 ?  67  GLU A N     1 
ATOM   537   C  CA    . GLU A 1 67  ? 118.017 161.948 104.001 1.00 50.68 ?  67  GLU A CA    1 
ATOM   538   C  C     . GLU A 1 67  ? 118.608 161.761 102.608 1.00 54.08 ?  67  GLU A C     1 
ATOM   539   O  O     . GLU A 1 67  ? 118.880 162.735 101.899 1.00 53.40 ?  67  GLU A O     1 
ATOM   540   C  CB    . GLU A 1 67  ? 119.064 161.654 105.077 1.00 53.18 ?  67  GLU A CB    1 
ATOM   541   C  CG    . GLU A 1 67  ? 118.639 162.047 106.486 1.00 51.07 ?  67  GLU A CG    1 
ATOM   542   C  CD    . GLU A 1 67  ? 117.635 161.081 107.086 1.00 53.44 ?  67  GLU A CD    1 
ATOM   543   O  OE1   . GLU A 1 67  ? 116.886 160.445 106.315 1.00 56.49 ?  67  GLU A OE1   1 
ATOM   544   O  OE2   . GLU A 1 67  ? 117.596 160.954 108.328 1.00 54.46 -1 67  GLU A OE2   1 
ATOM   545   N  N     . PHE A 1 68  ? 118.810 160.506 102.198 1.00 46.95 ?  68  PHE A N     1 
ATOM   546   C  CA    . PHE A 1 68  ? 119.417 160.242 100.899 1.00 45.50 ?  68  PHE A CA    1 
ATOM   547   C  C     . PHE A 1 68  ? 118.435 160.447 99.754  1.00 43.44 ?  68  PHE A C     1 
ATOM   548   O  O     . PHE A 1 68  ? 118.842 160.862 98.664  1.00 47.42 ?  68  PHE A O     1 
ATOM   549   C  CB    . PHE A 1 68  ? 119.991 158.823 100.865 1.00 45.65 ?  68  PHE A CB    1 
ATOM   550   C  CG    . PHE A 1 68  ? 118.996 157.769 100.473 1.00 43.74 ?  68  PHE A CG    1 
ATOM   551   C  CD1   . PHE A 1 68  ? 118.125 157.238 101.407 1.00 44.00 ?  68  PHE A CD1   1 
ATOM   552   C  CD2   . PHE A 1 68  ? 118.948 157.294 99.173  1.00 40.40 ?  68  PHE A CD2   1 
ATOM   553   C  CE1   . PHE A 1 68  ? 117.213 156.265 101.049 1.00 44.80 ?  68  PHE A CE1   1 
ATOM   554   C  CE2   . PHE A 1 68  ? 118.040 156.322 98.809  1.00 40.10 ?  68  PHE A CE2   1 
ATOM   555   C  CZ    . PHE A 1 68  ? 117.173 155.806 99.749  1.00 42.76 ?  68  PHE A CZ    1 
ATOM   556   N  N     . LEU A 1 69  ? 117.149 160.168 99.974  1.00 41.54 ?  69  LEU A N     1 
ATOM   557   C  CA    . LEU A 1 69  ? 116.164 160.352 98.914  1.00 46.16 ?  69  LEU A CA    1 
ATOM   558   C  C     . LEU A 1 69  ? 115.905 161.826 98.634  1.00 45.30 ?  69  LEU A C     1 
ATOM   559   O  O     . LEU A 1 69  ? 115.592 162.194 97.496  1.00 43.43 ?  69  LEU A O     1 
ATOM   560   C  CB    . LEU A 1 69  ? 114.860 159.644 99.281  1.00 45.60 ?  69  LEU A CB    1 
ATOM   561   C  CG    . LEU A 1 69  ? 114.860 158.124 99.131  1.00 43.57 ?  69  LEU A CG    1 
ATOM   562   C  CD1   . LEU A 1 69  ? 113.625 157.518 99.778  1.00 44.02 ?  69  LEU A CD1   1 
ATOM   563   C  CD2   . LEU A 1 69  ? 114.951 157.734 97.667  1.00 41.68 ?  69  LEU A CD2   1 
ATOM   564   N  N     . SER A 1 70  ? 116.032 162.682 99.650  1.00 47.73 ?  70  SER A N     1 
ATOM   565   C  CA    . SER A 1 70  ? 115.760 164.103 99.477  1.00 46.02 ?  70  SER A CA    1 
ATOM   566   C  C     . SER A 1 70  ? 116.788 164.794 98.592  1.00 49.29 ?  70  SER A C     1 
ATOM   567   O  O     . SER A 1 70  ? 116.517 165.889 98.090  1.00 46.15 ?  70  SER A O     1 
ATOM   568   C  CB    . SER A 1 70  ? 115.706 164.793 100.840 1.00 45.91 ?  70  SER A CB    1 
ATOM   569   O  OG    . SER A 1 70  ? 116.964 164.729 101.487 1.00 46.73 ?  70  SER A OG    1 
ATOM   570   N  N     . LEU A 1 71  ? 117.960 164.186 98.391  1.00 47.60 ?  71  LEU A N     1 
ATOM   571   C  CA    . LEU A 1 71  ? 118.985 164.791 97.550  1.00 40.40 ?  71  LEU A CA    1 
ATOM   572   C  C     . LEU A 1 71  ? 118.619 164.778 96.074  1.00 43.87 ?  71  LEU A C     1 
ATOM   573   O  O     . LEU A 1 71  ? 119.254 165.491 95.290  1.00 43.42 ?  71  LEU A O     1 
ATOM   574   C  CB    . LEU A 1 71  ? 120.322 164.076 97.752  1.00 42.06 ?  71  LEU A CB    1 
ATOM   575   C  CG    . LEU A 1 71  ? 120.772 163.867 99.197  1.00 43.09 ?  71  LEU A CG    1 
ATOM   576   C  CD1   . LEU A 1 71  ? 121.981 162.953 99.253  1.00 43.85 ?  71  LEU A CD1   1 
ATOM   577   C  CD2   . LEU A 1 71  ? 121.077 165.201 99.855  1.00 43.57 ?  71  LEU A CD2   1 
ATOM   578   N  N     . TYR A 1 72  ? 117.621 163.994 95.679  1.00 40.21 ?  72  TYR A N     1 
ATOM   579   C  CA    . TYR A 1 72  ? 117.213 163.874 94.288  1.00 43.18 ?  72  TYR A CA    1 
ATOM   580   C  C     . TYR A 1 72  ? 115.816 164.446 94.103  1.00 44.27 ?  72  TYR A C     1 
ATOM   581   O  O     . TYR A 1 72  ? 114.927 164.216 94.929  1.00 46.32 ?  72  TYR A O     1 
ATOM   582   C  CB    . TYR A 1 72  ? 117.214 162.412 93.833  1.00 41.20 ?  72  TYR A CB    1 
ATOM   583   C  CG    . TYR A 1 72  ? 118.511 161.675 94.055  1.00 37.84 ?  72  TYR A CG    1 
ATOM   584   C  CD1   . TYR A 1 72  ? 119.475 161.610 93.059  1.00 39.85 ?  72  TYR A CD1   1 
ATOM   585   C  CD2   . TYR A 1 72  ? 118.764 161.029 95.256  1.00 36.73 ?  72  TYR A CD2   1 
ATOM   586   C  CE1   . TYR A 1 72  ? 120.657 160.929 93.258  1.00 36.98 ?  72  TYR A CE1   1 
ATOM   587   C  CE2   . TYR A 1 72  ? 119.941 160.349 95.464  1.00 38.23 ?  72  TYR A CE2   1 
ATOM   588   C  CZ    . TYR A 1 72  ? 120.884 160.300 94.462  1.00 37.38 ?  72  TYR A CZ    1 
ATOM   589   O  OH    . TYR A 1 72  ? 122.059 159.621 94.669  1.00 38.78 ?  72  TYR A OH    1 
ATOM   590   N  N     . SER A 1 73  ? 115.625 165.188 93.019  1.00 45.32 ?  73  SER A N     1 
ATOM   591   C  CA    . SER A 1 73  ? 114.277 165.514 92.588  1.00 47.20 ?  73  SER A CA    1 
ATOM   592   C  C     . SER A 1 73  ? 113.561 164.234 92.179  1.00 45.93 ?  73  SER A C     1 
ATOM   593   O  O     . SER A 1 73  ? 114.175 163.290 91.677  1.00 48.65 ?  73  SER A O     1 
ATOM   594   C  CB    . SER A 1 73  ? 114.305 166.506 91.426  1.00 48.08 ?  73  SER A CB    1 
ATOM   595   O  OG    . SER A 1 73  ? 114.603 165.853 90.206  1.00 47.44 ?  73  SER A OG    1 
ATOM   596   N  N     . PHE A 1 74  ? 112.246 164.197 92.407  1.00 52.60 ?  74  PHE A N     1 
ATOM   597   C  CA    . PHE A 1 74  ? 111.519 162.960 92.146  1.00 50.35 ?  74  PHE A CA    1 
ATOM   598   C  C     . PHE A 1 74  ? 111.664 162.510 90.701  1.00 49.64 ?  74  PHE A C     1 
ATOM   599   O  O     . PHE A 1 74  ? 111.583 161.311 90.417  1.00 51.10 ?  74  PHE A O     1 
ATOM   600   C  CB    . PHE A 1 74  ? 110.043 163.102 92.499  1.00 49.96 ?  74  PHE A CB    1 
ATOM   601   C  CG    . PHE A 1 74  ? 109.311 161.798 92.485  1.00 52.81 ?  74  PHE A CG    1 
ATOM   602   C  CD1   . PHE A 1 74  ? 109.392 160.931 93.560  1.00 51.35 ?  74  PHE A CD1   1 
ATOM   603   C  CD2   . PHE A 1 74  ? 108.575 161.419 91.377  1.00 51.23 ?  74  PHE A CD2   1 
ATOM   604   C  CE1   . PHE A 1 74  ? 108.733 159.721 93.537  1.00 50.59 ?  74  PHE A CE1   1 
ATOM   605   C  CE2   . PHE A 1 74  ? 107.916 160.210 91.349  1.00 51.41 ?  74  PHE A CE2   1 
ATOM   606   C  CZ    . PHE A 1 74  ? 107.998 159.360 92.428  1.00 53.24 ?  74  PHE A CZ    1 
ATOM   607   N  N     . GLU A 1 75  ? 111.871 163.444 89.773  1.00 50.26 ?  75  GLU A N     1 
ATOM   608   C  CA    . GLU A 1 75  ? 112.135 163.050 88.394  1.00 48.78 ?  75  GLU A CA    1 
ATOM   609   C  C     . GLU A 1 75  ? 113.406 162.216 88.303  1.00 52.58 ?  75  GLU A C     1 
ATOM   610   O  O     . GLU A 1 75  ? 113.453 161.218 87.576  1.00 52.01 ?  75  GLU A O     1 
ATOM   611   C  CB    . GLU A 1 75  ? 112.234 164.287 87.502  1.00 50.87 ?  75  GLU A CB    1 
ATOM   612   C  CG    . GLU A 1 75  ? 110.896 164.936 87.189  1.00 51.09 ?  75  GLU A CG    1 
ATOM   613   C  CD    . GLU A 1 75  ? 109.979 164.027 86.394  1.00 55.71 ?  75  GLU A CD    1 
ATOM   614   O  OE1   . GLU A 1 75  ? 110.431 163.475 85.369  1.00 53.25 ?  75  GLU A OE1   1 
ATOM   615   O  OE2   . GLU A 1 75  ? 108.806 163.865 86.792  1.00 56.26 -1 75  GLU A OE2   1 
ATOM   616   N  N     . ASP A 1 76  ? 114.446 162.607 89.043  1.00 46.87 ?  76  ASP A N     1 
ATOM   617   C  CA    . ASP A 1 76  ? 115.690 161.844 89.038  1.00 43.10 ?  76  ASP A CA    1 
ATOM   618   C  C     . ASP A 1 76  ? 115.488 160.447 89.612  1.00 42.41 ?  76  ASP A C     1 
ATOM   619   O  O     . ASP A 1 76  ? 116.001 159.463 89.067  1.00 49.64 ?  76  ASP A O     1 
ATOM   620   C  CB    . ASP A 1 76  ? 116.763 162.598 89.824  1.00 46.78 ?  76  ASP A CB    1 
ATOM   621   C  CG    . ASP A 1 76  ? 117.197 163.876 89.134  1.00 49.09 ?  76  ASP A CG    1 
ATOM   622   O  OD1   . ASP A 1 76  ? 116.951 164.011 87.918  1.00 47.03 ?  76  ASP A OD1   1 
ATOM   623   O  OD2   . ASP A 1 76  ? 117.782 164.748 89.812  1.00 48.32 -1 76  ASP A OD2   1 
ATOM   624   N  N     . ILE A 1 77  ? 114.748 160.342 90.718  1.00 42.08 ?  77  ILE A N     1 
ATOM   625   C  CA    . ILE A 1 77  ? 114.487 159.035 91.316  1.00 40.41 ?  77  ILE A CA    1 
ATOM   626   C  C     . ILE A 1 77  ? 113.692 158.161 90.356  1.00 42.85 ?  77  ILE A C     1 
ATOM   627   O  O     . ILE A 1 77  ? 113.968 156.964 90.206  1.00 44.94 ?  77  ILE A O     1 
ATOM   628   C  CB    . ILE A 1 77  ? 113.764 159.200 92.664  1.00 44.68 ?  77  ILE A CB    1 
ATOM   629   C  CG1   . ILE A 1 77  ? 114.683 159.876 93.681  1.00 44.62 ?  77  ILE A CG1   1 
ATOM   630   C  CG2   . ILE A 1 77  ? 113.286 157.852 93.181  1.00 42.39 ?  77  ILE A CG2   1 
ATOM   631   C  CD1   . ILE A 1 77  ? 113.981 160.301 94.950  1.00 45.67 ?  77  ILE A CD1   1 
ATOM   632   N  N     . LYS A 1 78  ? 112.686 158.743 89.701  1.00 45.88 ?  78  LYS A N     1 
ATOM   633   C  CA    . LYS A 1 78  ? 111.897 157.990 88.734  1.00 43.84 ?  78  LYS A CA    1 
ATOM   634   C  C     . LYS A 1 78  ? 112.762 157.518 87.574  1.00 44.16 ?  78  LYS A C     1 
ATOM   635   O  O     . LYS A 1 78  ? 112.616 156.385 87.104  1.00 47.73 ?  78  LYS A O     1 
ATOM   636   C  CB    . LYS A 1 78  ? 110.736 158.847 88.227  1.00 46.03 ?  78  LYS A CB    1 
ATOM   637   C  CG    . LYS A 1 78  ? 109.653 158.067 87.505  1.00 46.22 ?  78  LYS A CG    1 
ATOM   638   C  CD    . LYS A 1 78  ? 108.437 158.937 87.236  1.00 49.77 ?  78  LYS A CD    1 
ATOM   639   C  CE    . LYS A 1 78  ? 107.457 158.891 88.396  1.00 50.88 ?  78  LYS A CE    1 
ATOM   640   N  NZ    . LYS A 1 78  ? 106.044 158.899 87.930  1.00 46.64 1  78  LYS A NZ    1 
ATOM   641   N  N     . GLU A 1 79  ? 113.666 158.375 87.095  1.00 46.14 ?  79  GLU A N     1 
ATOM   642   C  CA    . GLU A 1 79  ? 114.551 157.981 86.007  1.00 46.20 ?  79  GLU A CA    1 
ATOM   643   C  C     . GLU A 1 79  ? 115.470 156.843 86.431  1.00 43.46 ?  79  GLU A C     1 
ATOM   644   O  O     . GLU A 1 79  ? 115.702 155.903 85.662  1.00 46.42 ?  79  GLU A O     1 
ATOM   645   C  CB    . GLU A 1 79  ? 115.367 159.184 85.532  1.00 44.45 ?  79  GLU A CB    1 
ATOM   646   C  CG    . GLU A 1 79  ? 115.641 159.198 84.038  1.00 45.99 ?  79  GLU A CG    1 
ATOM   647   C  CD    . GLU A 1 79  ? 114.436 158.776 83.220  1.00 49.45 ?  79  GLU A CD    1 
ATOM   648   O  OE1   . GLU A 1 79  ? 113.295 159.058 83.647  1.00 47.31 ?  79  GLU A OE1   1 
ATOM   649   O  OE2   . GLU A 1 79  ? 114.627 158.164 82.148  1.00 51.71 -1 79  GLU A OE2   1 
ATOM   650   N  N     . VAL A 1 80  ? 115.999 156.906 87.653  1.00 34.57 ?  80  VAL A N     1 
ATOM   651   C  CA    . VAL A 1 80  ? 116.867 155.836 88.139  1.00 34.97 ?  80  VAL A CA    1 
ATOM   652   C  C     . VAL A 1 80  ? 116.091 154.528 88.244  1.00 40.30 ?  80  VAL A C     1 
ATOM   653   O  O     . VAL A 1 80  ? 116.580 153.460 87.847  1.00 41.55 ?  80  VAL A O     1 
ATOM   654   C  CB    . VAL A 1 80  ? 117.501 156.232 89.484  1.00 35.63 ?  80  VAL A CB    1 
ATOM   655   C  CG1   . VAL A 1 80  ? 118.162 155.030 90.137  1.00 37.11 ?  80  VAL A CG1   1 
ATOM   656   C  CG2   . VAL A 1 80  ? 118.506 157.354 89.284  1.00 34.56 ?  80  VAL A CG2   1 
ATOM   657   N  N     . PHE A 1 81  ? 114.870 154.588 88.779  1.00 39.64 ?  81  PHE A N     1 
ATOM   658   C  CA    . PHE A 1 81  ? 114.064 153.378 88.909  1.00 36.51 ?  81  PHE A CA    1 
ATOM   659   C  C     . PHE A 1 81  ? 113.707 152.804 87.544  1.00 39.64 ?  81  PHE A C     1 
ATOM   660   O  O     . PHE A 1 81  ? 113.700 151.582 87.358  1.00 40.42 ?  81  PHE A O     1 
ATOM   661   C  CB    . PHE A 1 81  ? 112.805 153.671 89.723  1.00 35.84 ?  81  PHE A CB    1 
ATOM   662   C  CG    . PHE A 1 81  ? 112.992 153.499 91.203  1.00 34.75 ?  81  PHE A CG    1 
ATOM   663   C  CD1   . PHE A 1 81  ? 113.593 154.490 91.958  1.00 38.47 ?  81  PHE A CD1   1 
ATOM   664   C  CD2   . PHE A 1 81  ? 112.574 152.343 91.836  1.00 35.09 ?  81  PHE A CD2   1 
ATOM   665   C  CE1   . PHE A 1 81  ? 113.769 154.333 93.318  1.00 39.49 ?  81  PHE A CE1   1 
ATOM   666   C  CE2   . PHE A 1 81  ? 112.746 152.182 93.197  1.00 37.04 ?  81  PHE A CE2   1 
ATOM   667   C  CZ    . PHE A 1 81  ? 113.345 153.177 93.938  1.00 36.38 ?  81  PHE A CZ    1 
ATOM   668   N  N     . LYS A 1 82  ? 113.403 153.670 86.575  1.00 38.74 ?  82  LYS A N     1 
ATOM   669   C  CA    . LYS A 1 82  ? 113.147 153.203 85.217  1.00 37.68 ?  82  LYS A CA    1 
ATOM   670   C  C     . LYS A 1 82  ? 114.389 152.558 84.618  1.00 39.14 ?  82  LYS A C     1 
ATOM   671   O  O     . LYS A 1 82  ? 114.294 151.556 83.900  1.00 41.98 ?  82  LYS A O     1 
ATOM   672   C  CB    . LYS A 1 82  ? 112.669 154.365 84.346  1.00 40.82 ?  82  LYS A CB    1 
ATOM   673   C  CG    . LYS A 1 82  ? 112.548 154.030 82.870  1.00 43.26 ?  82  LYS A CG    1 
ATOM   674   C  CD    . LYS A 1 82  ? 113.295 155.039 82.014  1.00 43.55 ?  82  LYS A CD    1 
ATOM   675   C  CE    . LYS A 1 82  ? 114.798 154.833 82.099  1.00 44.55 ?  82  LYS A CE    1 
ATOM   676   N  NZ    . LYS A 1 82  ? 115.271 153.775 81.163  1.00 42.89 1  82  LYS A NZ    1 
ATOM   677   N  N     . THR A 1 83  ? 115.564 153.124 84.897  1.00 38.75 ?  83  THR A N     1 
ATOM   678   C  CA    . THR A 1 83  ? 116.806 152.514 84.438  1.00 38.79 ?  83  THR A CA    1 
ATOM   679   C  C     . THR A 1 83  ? 116.980 151.120 85.025  1.00 38.81 ?  83  THR A C     1 
ATOM   680   O  O     . THR A 1 83  ? 117.406 150.193 84.327  1.00 38.66 ?  83  THR A O     1 
ATOM   681   C  CB    . THR A 1 83  ? 117.994 153.402 84.805  1.00 37.57 ?  83  THR A CB    1 
ATOM   682   O  OG1   . THR A 1 83  ? 117.910 154.639 84.085  1.00 42.51 ?  83  THR A OG1   1 
ATOM   683   C  CG2   . THR A 1 83  ? 119.302 152.712 84.461  1.00 37.00 ?  83  THR A CG2   1 
ATOM   684   N  N     . ALA A 1 84  ? 116.660 150.954 86.309  1.00 34.23 ?  84  ALA A N     1 
ATOM   685   C  CA    . ALA A 1 84  ? 116.771 149.637 86.925  1.00 34.01 ?  84  ALA A CA    1 
ATOM   686   C  C     . ALA A 1 84  ? 115.835 148.633 86.260  1.00 31.30 ?  84  ALA A C     1 
ATOM   687   O  O     . ALA A 1 84  ? 116.219 147.483 86.017  1.00 35.96 ?  84  ALA A O     1 
ATOM   688   C  CB    . ALA A 1 84  ? 116.483 149.728 88.422  1.00 37.65 ?  84  ALA A CB    1 
ATOM   689   N  N     . TYR A 1 85  ? 114.603 149.048 85.962  1.00 43.37 ?  85  TYR A N     1 
ATOM   690   C  CA    . TYR A 1 85  ? 113.620 148.157 85.359  1.00 39.12 ?  85  TYR A CA    1 
ATOM   691   C  C     . TYR A 1 85  ? 113.790 148.005 83.854  1.00 39.81 ?  85  TYR A C     1 
ATOM   692   O  O     . TYR A 1 85  ? 113.203 147.085 83.273  1.00 43.97 ?  85  TYR A O     1 
ATOM   693   C  CB    . TYR A 1 85  ? 112.206 148.653 85.666  1.00 34.41 ?  85  TYR A CB    1 
ATOM   694   C  CG    . TYR A 1 85  ? 111.739 148.342 87.069  1.00 37.78 ?  85  TYR A CG    1 
ATOM   695   C  CD1   . TYR A 1 85  ? 111.095 147.148 87.358  1.00 35.98 ?  85  TYR A CD1   1 
ATOM   696   C  CD2   . TYR A 1 85  ? 111.948 149.241 88.105  1.00 41.78 ?  85  TYR A CD2   1 
ATOM   697   C  CE1   . TYR A 1 85  ? 110.668 146.859 88.639  1.00 38.93 ?  85  TYR A CE1   1 
ATOM   698   C  CE2   . TYR A 1 85  ? 111.526 148.963 89.387  1.00 40.65 ?  85  TYR A CE2   1 
ATOM   699   C  CZ    . TYR A 1 85  ? 110.887 147.769 89.650  1.00 40.90 ?  85  TYR A CZ    1 
ATOM   700   O  OH    . TYR A 1 85  ? 110.466 147.490 90.928  1.00 39.07 ?  85  TYR A OH    1 
ATOM   701   N  N     . ALA A 1 86  ? 114.569 148.873 83.208  1.00 41.18 ?  86  ALA A N     1 
ATOM   702   C  CA    . ALA A 1 86  ? 114.749 148.782 81.764  1.00 37.49 ?  86  ALA A CA    1 
ATOM   703   C  C     . ALA A 1 86  ? 115.461 147.503 81.346  1.00 41.22 ?  86  ALA A C     1 
ATOM   704   O  O     . ALA A 1 86  ? 115.278 147.052 80.210  1.00 40.95 ?  86  ALA A O     1 
ATOM   705   C  CB    . ALA A 1 86  ? 115.523 149.996 81.250  1.00 38.40 ?  86  ALA A CB    1 
ATOM   706   N  N     . LYS A 1 87  ? 116.266 146.913 82.230  1.00 42.93 ?  87  LYS A N     1 
ATOM   707   C  CA    . LYS A 1 87  ? 117.008 145.711 81.875  1.00 40.77 ?  87  LYS A CA    1 
ATOM   708   C  C     . LYS A 1 87  ? 116.121 144.478 81.781  1.00 40.22 ?  87  LYS A C     1 
ATOM   709   O  O     . LYS A 1 87  ? 116.506 143.505 81.124  1.00 41.69 ?  87  LYS A O     1 
ATOM   710   C  CB    . LYS A 1 87  ? 118.127 145.467 82.890  1.00 38.11 ?  87  LYS A CB    1 
ATOM   711   C  CG    . LYS A 1 87  ? 118.666 144.046 82.882  1.00 39.12 ?  87  LYS A CG    1 
ATOM   712   C  CD    . LYS A 1 87  ? 119.977 143.941 83.631  1.00 40.10 ?  87  LYS A CD    1 
ATOM   713   C  CE    . LYS A 1 87  ? 120.991 143.136 82.839  1.00 42.23 ?  87  LYS A CE    1 
ATOM   714   N  NZ    . LYS A 1 87  ? 121.326 143.785 81.543  1.00 35.91 1  87  LYS A NZ    1 
ATOM   715   N  N     . LYS A 1 88  ? 114.945 144.497 82.405  1.00 39.98 ?  88  LYS A N     1 
ATOM   716   C  CA    . LYS A 1 88  ? 114.088 143.315 82.470  1.00 41.24 ?  88  LYS A CA    1 
ATOM   717   C  C     . LYS A 1 88  ? 114.839 142.139 83.087  1.00 40.43 ?  88  LYS A C     1 
ATOM   718   O  O     . LYS A 1 88  ? 114.768 141.008 82.605  1.00 44.88 ?  88  LYS A O     1 
ATOM   719   C  CB    . LYS A 1 88  ? 113.542 142.949 81.089  1.00 40.78 ?  88  LYS A CB    1 
ATOM   720   C  CG    . LYS A 1 88  ? 112.221 143.616 80.744  1.00 42.80 ?  88  LYS A CG    1 
ATOM   721   C  CD    . LYS A 1 88  ? 112.438 144.909 79.979  1.00 43.97 ?  88  LYS A CD    1 
ATOM   722   C  CE    . LYS A 1 88  ? 113.469 144.730 78.877  1.00 45.87 ?  88  LYS A CE    1 
ATOM   723   N  NZ    . LYS A 1 88  ? 113.409 145.830 77.875  1.00 44.82 1  88  LYS A NZ    1 
ATOM   724   N  N     . PHE A 1 89  ? 115.574 142.416 84.162  1.00 35.31 ?  89  PHE A N     1 
ATOM   725   C  CA    . PHE A 1 89  ? 116.397 141.397 84.795  1.00 33.90 ?  89  PHE A CA    1 
ATOM   726   C  C     . PHE A 1 89  ? 115.549 140.211 85.230  1.00 36.85 ?  89  PHE A C     1 
ATOM   727   O  O     . PHE A 1 89  ? 114.475 140.377 85.817  1.00 38.49 ?  89  PHE A O     1 
ATOM   728   C  CB    . PHE A 1 89  ? 117.133 141.989 85.998  1.00 32.94 ?  89  PHE A CB    1 
ATOM   729   C  CG    . PHE A 1 89  ? 117.752 140.958 86.896  1.00 32.95 ?  89  PHE A CG    1 
ATOM   730   C  CD1   . PHE A 1 89  ? 119.028 140.486 86.652  1.00 31.02 ?  89  PHE A CD1   1 
ATOM   731   C  CD2   . PHE A 1 89  ? 117.055 140.457 87.980  1.00 34.33 ?  89  PHE A CD2   1 
ATOM   732   C  CE1   . PHE A 1 89  ? 119.598 139.536 87.474  1.00 33.46 ?  89  PHE A CE1   1 
ATOM   733   C  CE2   . PHE A 1 89  ? 117.618 139.506 88.804  1.00 32.16 ?  89  PHE A CE2   1 
ATOM   734   C  CZ    . PHE A 1 89  ? 118.892 139.046 88.551  1.00 31.03 ?  89  PHE A CZ    1 
ATOM   735   N  N     . ARG A 1 90  ? 116.039 139.007 84.945  1.00 40.85 ?  90  ARG A N     1 
ATOM   736   C  CA    . ARG A 1 90  ? 115.380 137.773 85.344  1.00 36.91 ?  90  ARG A CA    1 
ATOM   737   C  C     . ARG A 1 90  ? 116.366 136.914 86.119  1.00 34.22 ?  90  ARG A C     1 
ATOM   738   O  O     . ARG A 1 90  ? 117.497 136.706 85.669  1.00 41.57 ?  90  ARG A O     1 
ATOM   739   C  CB    . ARG A 1 90  ? 114.855 137.002 84.128  1.00 41.18 ?  90  ARG A CB    1 
ATOM   740   C  CG    . ARG A 1 90  ? 113.803 137.741 83.326  1.00 38.80 ?  90  ARG A CG    1 
ATOM   741   C  CD    . ARG A 1 90  ? 112.516 137.905 84.111  1.00 42.42 ?  90  ARG A CD    1 
ATOM   742   N  NE    . ARG A 1 90  ? 111.557 138.737 83.396  1.00 45.45 ?  90  ARG A NE    1 
ATOM   743   C  CZ    . ARG A 1 90  ? 111.302 140.005 83.687  1.00 46.11 ?  90  ARG A CZ    1 
ATOM   744   N  NH1   . ARG A 1 90  ? 111.908 140.619 84.690  1.00 44.01 1  90  ARG A NH1   1 
ATOM   745   N  NH2   . ARG A 1 90  ? 110.415 140.673 82.956  1.00 43.91 ?  90  ARG A NH2   1 
ATOM   746   N  N     . PHE A 1 91  ? 115.941 136.423 87.272  1.00 35.83 ?  91  PHE A N     1 
ATOM   747   C  CA    . PHE A 1 91  ? 116.763 135.485 88.020  1.00 36.78 ?  91  PHE A CA    1 
ATOM   748   C  C     . PHE A 1 91  ? 116.869 134.179 87.241  1.00 40.06 ?  91  PHE A C     1 
ATOM   749   O  O     . PHE A 1 91  ? 115.841 133.596 86.876  1.00 39.46 ?  91  PHE A O     1 
ATOM   750   C  CB    . PHE A 1 91  ? 116.168 135.239 89.404  1.00 34.19 ?  91  PHE A CB    1 
ATOM   751   C  CG    . PHE A 1 91  ? 116.437 136.346 90.384  1.00 39.21 ?  91  PHE A CG    1 
ATOM   752   C  CD1   . PHE A 1 91  ? 117.655 136.432 91.035  1.00 38.81 ?  91  PHE A CD1   1 
ATOM   753   C  CD2   . PHE A 1 91  ? 115.474 137.303 90.649  1.00 39.41 ?  91  PHE A CD2   1 
ATOM   754   C  CE1   . PHE A 1 91  ? 117.904 137.448 91.936  1.00 34.55 ?  91  PHE A CE1   1 
ATOM   755   C  CE2   . PHE A 1 91  ? 115.718 138.321 91.548  1.00 36.78 ?  91  PHE A CE2   1 
ATOM   756   C  CZ    . PHE A 1 91  ? 116.935 138.394 92.193  1.00 35.61 ?  91  PHE A CZ    1 
ATOM   757   N  N     . PRO A 1 92  ? 118.081 133.687 86.963  1.00 41.81 ?  92  PRO A N     1 
ATOM   758   C  CA    . PRO A 1 92  ? 118.208 132.496 86.114  1.00 38.91 ?  92  PRO A CA    1 
ATOM   759   C  C     . PRO A 1 92  ? 117.904 131.193 86.827  1.00 38.07 ?  92  PRO A C     1 
ATOM   760   O  O     . PRO A 1 92  ? 117.659 130.185 86.153  1.00 41.26 ?  92  PRO A O     1 
ATOM   761   C  CB    . PRO A 1 92  ? 119.673 132.548 85.667  1.00 39.48 ?  92  PRO A CB    1 
ATOM   762   C  CG    . PRO A 1 92  ? 120.368 133.186 86.825  1.00 38.34 ?  92  PRO A CG    1 
ATOM   763   C  CD    . PRO A 1 92  ? 119.392 134.178 87.424  1.00 38.09 ?  92  PRO A CD    1 
ATOM   764   N  N     . SER A 1 93  ? 117.911 131.178 88.156  1.00 36.08 ?  93  SER A N     1 
ATOM   765   C  CA    . SER A 1 93  ? 117.678 129.963 88.918  1.00 38.07 ?  93  SER A CA    1 
ATOM   766   C  C     . SER A 1 93  ? 116.806 130.287 90.121  1.00 37.43 ?  93  SER A C     1 
ATOM   767   O  O     . SER A 1 93  ? 116.726 131.433 90.566  1.00 37.95 ?  93  SER A O     1 
ATOM   768   C  CB    . SER A 1 93  ? 118.995 129.317 89.371  1.00 39.54 ?  93  SER A CB    1 
ATOM   769   O  OG    . SER A 1 93  ? 119.501 129.949 90.535  1.00 43.18 ?  93  SER A OG    1 
ATOM   770   N  N     . PHE A 1 94  ? 116.148 129.251 90.644  1.00 36.79 ?  94  PHE A N     1 
ATOM   771   C  CA    . PHE A 1 94  ? 115.249 129.446 91.776  1.00 37.11 ?  94  PHE A CA    1 
ATOM   772   C  C     . PHE A 1 94  ? 115.999 129.950 93.002  1.00 38.67 ?  94  PHE A C     1 
ATOM   773   O  O     . PHE A 1 94  ? 115.486 130.794 93.746  1.00 39.59 ?  94  PHE A O     1 
ATOM   774   C  CB    . PHE A 1 94  ? 114.521 128.142 92.098  1.00 37.19 ?  94  PHE A CB    1 
ATOM   775   C  CG    . PHE A 1 94  ? 113.910 128.117 93.468  1.00 38.80 ?  94  PHE A CG    1 
ATOM   776   C  CD1   . PHE A 1 94  ? 112.813 128.906 93.766  1.00 38.16 ?  94  PHE A CD1   1 
ATOM   777   C  CD2   . PHE A 1 94  ? 114.443 127.316 94.463  1.00 38.53 ?  94  PHE A CD2   1 
ATOM   778   C  CE1   . PHE A 1 94  ? 112.255 128.888 95.028  1.00 37.33 ?  94  PHE A CE1   1 
ATOM   779   C  CE2   . PHE A 1 94  ? 113.889 127.296 95.724  1.00 41.01 ?  94  PHE A CE2   1 
ATOM   780   C  CZ    . PHE A 1 94  ? 112.794 128.083 96.008  1.00 36.13 ?  94  PHE A CZ    1 
ATOM   781   N  N     . MET A 1 95  ? 117.209 129.440 93.235  1.00 36.84 ?  95  MET A N     1 
ATOM   782   C  CA    . MET A 1 95  ? 117.918 129.758 94.470  1.00 34.89 ?  95  MET A CA    1 
ATOM   783   C  C     . MET A 1 95  ? 118.255 131.241 94.562  1.00 40.41 ?  95  MET A C     1 
ATOM   784   O  O     . MET A 1 95  ? 118.188 131.827 95.646  1.00 40.24 ?  95  MET A O     1 
ATOM   785   C  CB    . MET A 1 95  ? 119.185 128.914 94.582  1.00 40.42 ?  95  MET A CB    1 
ATOM   786   C  CG    . MET A 1 95  ? 119.534 128.520 96.005  1.00 40.61 ?  95  MET A CG    1 
ATOM   787   S  SD    . MET A 1 95  ? 118.078 128.097 96.981  1.00 55.80 ?  95  MET A SD    1 
ATOM   788   C  CE    . MET A 1 95  ? 118.057 126.317 96.795  1.00 43.92 ?  95  MET A CE    1 
ATOM   789   N  N     . SER A 1 96  ? 118.630 131.865 93.446  1.00 32.85 ?  96  SER A N     1 
ATOM   790   C  CA    . SER A 1 96  ? 118.980 133.282 93.481  1.00 27.12 ?  96  SER A CA    1 
ATOM   791   C  C     . SER A 1 96  ? 117.795 134.132 93.931  1.00 31.10 ?  96  SER A C     1 
ATOM   792   O  O     . SER A 1 96  ? 117.911 134.945 94.860  1.00 35.60 ?  96  SER A O     1 
ATOM   793   C  CB    . SER A 1 96  ? 119.477 133.726 92.106  1.00 31.75 ?  96  SER A CB    1 
ATOM   794   O  OG    . SER A 1 96  ? 118.571 133.342 91.089  1.00 37.38 ?  96  SER A OG    1 
ATOM   795   N  N     . ALA A 1 97  ? 116.644 133.954 93.280  1.00 35.08 ?  97  ALA A N     1 
ATOM   796   C  CA    . ALA A 1 97  ? 115.457 134.719 93.644  1.00 30.29 ?  97  ALA A CA    1 
ATOM   797   C  C     . ALA A 1 97  ? 114.995 134.385 95.055  1.00 31.64 ?  97  ALA A C     1 
ATOM   798   O  O     . ALA A 1 97  ? 114.573 135.273 95.804  1.00 36.51 ?  97  ALA A O     1 
ATOM   799   C  CB    . ALA A 1 97  ? 114.340 134.460 92.637  1.00 32.63 ?  97  ALA A CB    1 
ATOM   800   N  N     . PHE A 1 98  ? 115.052 133.106 95.428  1.00 33.15 ?  98  PHE A N     1 
ATOM   801   C  CA    . PHE A 1 98  ? 114.675 132.712 96.779  1.00 33.97 ?  98  PHE A CA    1 
ATOM   802   C  C     . PHE A 1 98  ? 115.542 133.418 97.812  1.00 35.30 ?  98  PHE A C     1 
ATOM   803   O  O     . PHE A 1 98  ? 115.036 133.974 98.791  1.00 42.81 ?  98  PHE A O     1 
ATOM   804   C  CB    . PHE A 1 98  ? 114.786 131.194 96.922  1.00 37.73 ?  98  PHE A CB    1 
ATOM   805   C  CG    . PHE A 1 98  ? 114.586 130.702 98.323  1.00 39.23 ?  98  PHE A CG    1 
ATOM   806   C  CD1   . PHE A 1 98  ? 113.313 130.493 98.823  1.00 37.42 ?  98  PHE A CD1   1 
ATOM   807   C  CD2   . PHE A 1 98  ? 115.673 130.446 99.142  1.00 39.26 ?  98  PHE A CD2   1 
ATOM   808   C  CE1   . PHE A 1 98  ? 113.128 130.039 100.111 1.00 39.97 ?  98  PHE A CE1   1 
ATOM   809   C  CE2   . PHE A 1 98  ? 115.493 129.994 100.433 1.00 40.02 ?  98  PHE A CE2   1 
ATOM   810   C  CZ    . PHE A 1 98  ? 114.219 129.790 100.917 1.00 38.19 ?  98  PHE A CZ    1 
ATOM   811   N  N     . LYS A 1 99  ? 116.859 133.416 97.597  1.00 36.81 ?  99  LYS A N     1 
ATOM   812   C  CA    . LYS A 1 99  ? 117.768 134.077 98.523  1.00 31.95 ?  99  LYS A CA    1 
ATOM   813   C  C     . LYS A 1 99  ? 117.465 135.564 98.609  1.00 36.41 ?  99  LYS A C     1 
ATOM   814   O  O     . LYS A 1 99  ? 117.380 136.129 99.705  1.00 39.69 ?  99  LYS A O     1 
ATOM   815   C  CB    . LYS A 1 99  ? 119.215 133.847 98.088  1.00 35.08 ?  99  LYS A CB    1 
ATOM   816   C  CG    . LYS A 1 99  ? 119.724 132.437 98.318  1.00 36.81 ?  99  LYS A CG    1 
ATOM   817   C  CD    . LYS A 1 99  ? 119.262 131.896 99.655  1.00 40.26 ?  99  LYS A CD    1 
ATOM   818   C  CE    . LYS A 1 99  ? 120.405 131.240 100.403 1.00 36.36 ?  99  LYS A CE    1 
ATOM   819   N  NZ    . LYS A 1 99  ? 120.319 131.486 101.866 1.00 38.62 1  99  LYS A NZ    1 
ATOM   820   N  N     . PHE A 1 100 ? 117.286 136.218 97.458  1.00 31.30 ?  100 PHE A N     1 
ATOM   821   C  CA    . PHE A 1 100 ? 117.019 137.650 97.491  1.00 31.04 ?  100 PHE A CA    1 
ATOM   822   C  C     . PHE A 1 100 ? 115.740 137.953 98.257  1.00 34.51 ?  100 PHE A C     1 
ATOM   823   O  O     . PHE A 1 100 ? 115.736 138.775 99.180  1.00 38.12 ?  100 PHE A O     1 
ATOM   824   C  CB    . PHE A 1 100 ? 116.932 138.228 96.082  1.00 30.06 ?  100 PHE A CB    1 
ATOM   825   C  CG    . PHE A 1 100 ? 116.534 139.674 96.065  1.00 32.94 ?  100 PHE A CG    1 
ATOM   826   C  CD1   . PHE A 1 100 ? 117.425 140.655 96.468  1.00 32.65 ?  100 PHE A CD1   1 
ATOM   827   C  CD2   . PHE A 1 100 ? 115.257 140.051 95.692  1.00 29.07 ?  100 PHE A CD2   1 
ATOM   828   C  CE1   . PHE A 1 100 ? 117.058 141.984 96.472  1.00 32.22 ?  100 PHE A CE1   1 
ATOM   829   C  CE2   . PHE A 1 100 ? 114.883 141.379 95.695  1.00 32.10 ?  100 PHE A CE2   1 
ATOM   830   C  CZ    . PHE A 1 100 ? 115.785 142.347 96.086  1.00 35.82 ?  100 PHE A CZ    1 
ATOM   831   N  N     . TYR A 1 101 ? 114.647 137.282 97.908  1.00 37.41 ?  101 TYR A N     1 
ATOM   832   C  CA    . TYR A 1 101 ? 113.350 137.615 98.479  1.00 36.25 ?  101 TYR A CA    1 
ATOM   833   C  C     . TYR A 1 101 ? 113.130 137.013 99.859  1.00 37.30 ?  101 TYR A C     1 
ATOM   834   O  O     . TYR A 1 101 ? 112.090 137.280 100.470 1.00 45.50 ?  101 TYR A O     1 
ATOM   835   C  CB    . TYR A 1 101 ? 112.236 137.183 97.525  1.00 36.15 ?  101 TYR A CB    1 
ATOM   836   C  CG    . TYR A 1 101 ? 112.176 138.030 96.277  1.00 33.19 ?  101 TYR A CG    1 
ATOM   837   C  CD1   . TYR A 1 101 ? 111.712 139.336 96.325  1.00 35.00 ?  101 TYR A CD1   1 
ATOM   838   C  CD2   . TYR A 1 101 ? 112.602 137.531 95.055  1.00 36.37 ?  101 TYR A CD2   1 
ATOM   839   C  CE1   . TYR A 1 101 ? 111.661 140.119 95.192  1.00 32.75 ?  101 TYR A CE1   1 
ATOM   840   C  CE2   . TYR A 1 101 ? 112.555 138.307 93.915  1.00 38.45 ?  101 TYR A CE2   1 
ATOM   841   C  CZ    . TYR A 1 101 ? 112.083 139.601 93.990  1.00 37.51 ?  101 TYR A CZ    1 
ATOM   842   O  OH    . TYR A 1 101 ? 112.035 140.378 92.856  1.00 35.01 ?  101 TYR A OH    1 
ATOM   843   N  N     . ASN A 1 102 ? 114.067 136.212 100.366 1.00 36.84 ?  102 ASN A N     1 
ATOM   844   C  CA    . ASN A 1 102 ? 113.997 135.751 101.743 1.00 39.77 ?  102 ASN A CA    1 
ATOM   845   C  C     . ASN A 1 102 ? 115.024 136.393 102.663 1.00 41.82 ?  102 ASN A C     1 
ATOM   846   O  O     . ASN A 1 102 ? 114.884 136.277 103.883 1.00 47.87 ?  102 ASN A O     1 
ATOM   847   C  CB    . ASN A 1 102 ? 114.165 134.225 101.804 1.00 42.05 ?  102 ASN A CB    1 
ATOM   848   C  CG    . ASN A 1 102 ? 112.870 133.509 102.129 1.00 44.84 ?  102 ASN A CG    1 
ATOM   849   O  OD1   . ASN A 1 102 ? 111.817 134.133 102.258 1.00 46.50 ?  102 ASN A OD1   1 
ATOM   850   N  ND2   . ASN A 1 102 ? 112.943 132.194 102.272 1.00 40.40 ?  102 ASN A ND2   1 
ATOM   851   N  N     . ASP A 1 103 ? 116.043 137.061 102.124 1.00 41.33 ?  103 ASP A N     1 
ATOM   852   C  CA    . ASP A 1 103 ? 117.050 137.693 102.966 1.00 40.20 ?  103 ASP A CA    1 
ATOM   853   C  C     . ASP A 1 103 ? 117.150 139.197 102.782 1.00 39.91 ?  103 ASP A C     1 
ATOM   854   O  O     . ASP A 1 103 ? 117.267 139.923 103.771 1.00 42.50 ?  103 ASP A O     1 
ATOM   855   C  CB    . ASP A 1 103 ? 118.429 137.066 102.702 1.00 43.32 ?  103 ASP A CB    1 
ATOM   856   C  CG    . ASP A 1 103 ? 118.476 135.588 103.039 1.00 45.08 ?  103 ASP A CG    1 
ATOM   857   O  OD1   . ASP A 1 103 ? 117.414 135.012 103.353 1.00 42.76 ?  103 ASP A OD1   1 
ATOM   858   O  OD2   . ASP A 1 103 ? 119.577 135.002 102.991 1.00 45.74 -1 103 ASP A OD2   1 
ATOM   859   N  N     . TYR A 1 104 ? 117.105 139.692 101.545 1.00 31.73 ?  104 TYR A N     1 
ATOM   860   C  CA    . TYR A 1 104 ? 117.396 141.092 101.265 1.00 35.21 ?  104 TYR A CA    1 
ATOM   861   C  C     . TYR A 1 104 ? 116.182 141.907 100.856 1.00 37.40 ?  104 TYR A C     1 
ATOM   862   O  O     . TYR A 1 104 ? 116.156 143.112 101.112 1.00 46.96 ?  104 TYR A O     1 
ATOM   863   C  CB    . TYR A 1 104 ? 118.457 141.196 100.162 1.00 36.58 ?  104 TYR A CB    1 
ATOM   864   C  CG    . TYR A 1 104 ? 119.710 140.405 100.458 1.00 38.85 ?  104 TYR A CG    1 
ATOM   865   C  CD1   . TYR A 1 104 ? 119.805 139.066 100.106 1.00 34.70 ?  104 TYR A CD1   1 
ATOM   866   C  CD2   . TYR A 1 104 ? 120.793 140.992 101.098 1.00 36.22 ?  104 TYR A CD2   1 
ATOM   867   C  CE1   . TYR A 1 104 ? 120.943 138.334 100.377 1.00 34.04 ?  104 TYR A CE1   1 
ATOM   868   C  CE2   . TYR A 1 104 ? 121.936 140.267 101.373 1.00 36.35 ?  104 TYR A CE2   1 
ATOM   869   C  CZ    . TYR A 1 104 ? 122.005 138.939 101.012 1.00 37.61 ?  104 TYR A CZ    1 
ATOM   870   O  OH    . TYR A 1 104 ? 123.139 138.211 101.282 1.00 40.33 ?  104 TYR A OH    1 
ATOM   871   N  N     . ALA A 1 105 ? 115.181 141.295 100.231 1.00 37.29 ?  105 ALA A N     1 
ATOM   872   C  CA    . ALA A 1 105 ? 113.997 142.039 99.828  1.00 38.83 ?  105 ALA A CA    1 
ATOM   873   C  C     . ALA A 1 105 ? 113.310 142.636 101.050 1.00 41.44 ?  105 ALA A C     1 
ATOM   874   O  O     . ALA A 1 105 ? 113.105 141.954 102.058 1.00 42.36 ?  105 ALA A O     1 
ATOM   875   C  CB    . ALA A 1 105 ? 113.031 141.131 99.067  1.00 33.28 ?  105 ALA A CB    1 
ATOM   876   N  N     . LEU A 1 106 ? 112.959 143.915 100.958 1.00 40.97 ?  106 LEU A N     1 
ATOM   877   C  CA    . LEU A 1 106 ? 112.300 144.586 102.070 1.00 40.39 ?  106 LEU A CA    1 
ATOM   878   C  C     . LEU A 1 106 ? 110.899 144.023 102.266 1.00 45.20 ?  106 LEU A C     1 
ATOM   879   O  O     . LEU A 1 106 ? 110.105 143.960 101.323 1.00 40.09 ?  106 LEU A O     1 
ATOM   880   C  CB    . LEU A 1 106 ? 112.241 146.092 101.823 1.00 43.14 ?  106 LEU A CB    1 
ATOM   881   C  CG    . LEU A 1 106 ? 111.628 146.938 102.942 1.00 41.18 ?  106 LEU A CG    1 
ATOM   882   C  CD1   . LEU A 1 106 ? 112.567 147.017 104.135 1.00 40.23 ?  106 LEU A CD1   1 
ATOM   883   C  CD2   . LEU A 1 106 ? 111.283 148.328 102.434 1.00 39.44 ?  106 LEU A CD2   1 
ATOM   884   N  N     . LYS A 1 107 ? 110.599 143.618 103.494 1.00 51.51 ?  107 LYS A N     1 
ATOM   885   C  CA    . LYS A 1 107 ? 109.304 143.065 103.851 1.00 47.35 ?  107 LYS A CA    1 
ATOM   886   C  C     . LYS A 1 107 ? 108.666 143.914 104.941 1.00 51.88 ?  107 LYS A C     1 
ATOM   887   O  O     . LYS A 1 107 ? 109.358 144.546 105.744 1.00 53.15 ?  107 LYS A O     1 
ATOM   888   C  CB    . LYS A 1 107 ? 109.429 141.612 104.322 1.00 47.37 ?  107 LYS A CB    1 
ATOM   889   C  CG    . LYS A 1 107 ? 109.765 140.626 103.217 1.00 48.02 ?  107 LYS A CG    1 
ATOM   890   C  CD    . LYS A 1 107 ? 109.816 139.202 103.747 1.00 51.38 ?  107 LYS A CD    1 
ATOM   891   C  CE    . LYS A 1 107 ? 110.147 138.211 102.644 1.00 50.36 ?  107 LYS A CE    1 
ATOM   892   N  NZ    . LYS A 1 107 ? 110.406 136.847 103.183 1.00 47.47 1  107 LYS A NZ    1 
ATOM   893   N  N     . THR A 1 108 ? 107.336 143.920 104.962 1.00 56.50 ?  108 THR A N     1 
ATOM   894   C  CA    . THR A 1 108 ? 106.606 144.680 105.964 1.00 54.17 ?  108 THR A CA    1 
ATOM   895   C  C     . THR A 1 108 ? 107.036 144.263 107.369 1.00 54.39 ?  108 THR A C     1 
ATOM   896   O  O     . THR A 1 108 ? 107.654 143.214 107.575 1.00 54.60 ?  108 THR A O     1 
ATOM   897   C  CB    . THR A 1 108 ? 105.100 144.484 105.793 1.00 55.05 ?  108 THR A CB    1 
ATOM   898   O  OG1   . THR A 1 108 ? 104.796 143.084 105.800 1.00 54.87 ?  108 THR A OG1   1 
ATOM   899   C  CG2   . THR A 1 108 ? 104.634 145.089 104.478 1.00 52.43 ?  108 THR A CG2   1 
ATOM   900   N  N     . ASN A 1 109 ? 106.701 145.108 108.348 1.00 57.51 ?  109 ASN A N     1 
ATOM   901   C  CA    . ASN A 1 109 ? 107.123 144.849 109.721 1.00 58.26 ?  109 ASN A CA    1 
ATOM   902   C  C     . ASN A 1 109 ? 106.626 143.499 110.218 1.00 57.97 ?  109 ASN A C     1 
ATOM   903   O  O     . ASN A 1 109 ? 107.271 142.878 111.071 1.00 58.16 ?  109 ASN A O     1 
ATOM   904   C  CB    . ASN A 1 109 ? 106.632 145.963 110.644 1.00 57.94 ?  109 ASN A CB    1 
ATOM   905   C  CG    . ASN A 1 109 ? 106.996 147.341 110.136 1.00 57.80 ?  109 ASN A CG    1 
ATOM   906   O  OD1   . ASN A 1 109 ? 106.859 147.632 108.949 1.00 60.60 ?  109 ASN A OD1   1 
ATOM   907   N  ND2   . ASN A 1 109 ? 107.470 148.197 111.032 1.00 58.36 ?  109 ASN A ND2   1 
ATOM   908   N  N     . ASP A 1 110 ? 105.494 143.030 109.703 1.00 60.40 ?  110 ASP A N     1 
ATOM   909   C  CA    . ASP A 1 110 ? 104.973 141.714 110.042 1.00 60.89 ?  110 ASP A CA    1 
ATOM   910   C  C     . ASP A 1 110 ? 105.601 140.604 109.210 1.00 61.85 ?  110 ASP A C     1 
ATOM   911   O  O     . ASP A 1 110 ? 105.265 139.432 109.411 1.00 62.03 ?  110 ASP A O     1 
ATOM   912   C  CB    . ASP A 1 110 ? 103.449 141.695 109.882 1.00 61.32 ?  110 ASP A CB    1 
ATOM   913   C  CG    . ASP A 1 110 ? 102.995 142.260 108.552 1.00 63.42 ?  110 ASP A CG    1 
ATOM   914   O  OD1   . ASP A 1 110 ? 103.816 142.905 107.867 1.00 62.74 ?  110 ASP A OD1   1 
ATOM   915   O  OD2   . ASP A 1 110 ? 101.814 142.070 108.197 1.00 63.00 -1 110 ASP A OD2   1 
ATOM   916   N  N     . LYS A 1 111 ? 106.501 140.944 108.287 1.00 60.15 ?  111 LYS A N     1 
ATOM   917   C  CA    . LYS A 1 111 ? 107.242 139.959 107.497 1.00 59.76 ?  111 LYS A CA    1 
ATOM   918   C  C     . LYS A 1 111 ? 106.313 139.065 106.682 1.00 60.20 ?  111 LYS A C     1 
ATOM   919   O  O     . LYS A 1 111 ? 106.604 137.888 106.462 1.00 61.30 ?  111 LYS A O     1 
ATOM   920   C  CB    . LYS A 1 111 ? 108.153 139.107 108.386 1.00 57.94 ?  111 LYS A CB    1 
ATOM   921   C  CG    . LYS A 1 111 ? 108.614 139.788 109.668 1.00 58.81 ?  111 LYS A CG    1 
ATOM   922   C  CD    . LYS A 1 111 ? 109.278 141.127 109.390 1.00 60.97 ?  111 LYS A CD    1 
ATOM   923   C  CE    . LYS A 1 111 ? 110.791 141.019 109.473 1.00 60.02 ?  111 LYS A CE    1 
ATOM   924   N  NZ    . LYS A 1 111 ? 111.453 142.345 109.330 1.00 59.34 1  111 LYS A NZ    1 
ATOM   925   N  N     . LYS A 1 112 ? 105.187 139.615 106.224 1.00 58.23 ?  112 LYS A N     1 
ATOM   926   C  CA    . LYS A 1 112 ? 104.224 138.855 105.439 1.00 58.33 ?  112 LYS A CA    1 
ATOM   927   C  C     . LYS A 1 112 ? 104.156 139.269 103.978 1.00 58.77 ?  112 LYS A C     1 
ATOM   928   O  O     . LYS A 1 112 ? 103.665 138.489 103.157 1.00 58.01 ?  112 LYS A O     1 
ATOM   929   C  CB    . LYS A 1 112 ? 102.821 138.980 106.049 1.00 58.50 ?  112 LYS A CB    1 
ATOM   930   C  CG    . LYS A 1 112 ? 102.218 140.368 105.917 1.00 60.56 ?  112 LYS A CG    1 
ATOM   931   C  CD    . LYS A 1 112 ? 100.710 140.338 106.103 1.00 59.20 ?  112 LYS A CD    1 
ATOM   932   C  CE    . LYS A 1 112 ? 100.095 141.700 105.824 1.00 60.12 ?  112 LYS A CE    1 
ATOM   933   N  NZ    . LYS A 1 112 ? 101.097 142.796 105.939 1.00 59.02 1  112 LYS A NZ    1 
ATOM   934   N  N     . LYS A 1 113 ? 104.629 140.463 103.635 1.00 54.52 ?  113 LYS A N     1 
ATOM   935   C  CA    . LYS A 1 113 ? 104.541 140.978 102.278 1.00 52.89 ?  113 LYS A CA    1 
ATOM   936   C  C     . LYS A 1 113 ? 105.902 141.500 101.838 1.00 51.97 ?  113 LYS A C     1 
ATOM   937   O  O     . LYS A 1 113 ? 106.764 141.826 102.658 1.00 52.72 ?  113 LYS A O     1 
ATOM   938   C  CB    . LYS A 1 113 ? 103.488 142.089 102.167 1.00 54.23 ?  113 LYS A CB    1 
ATOM   939   C  CG    . LYS A 1 113 ? 102.060 141.582 102.067 1.00 52.37 ?  113 LYS A CG    1 
ATOM   940   C  CD    . LYS A 1 113 ? 101.792 140.946 100.715 1.00 53.52 ?  113 LYS A CD    1 
ATOM   941   C  CE    . LYS A 1 113 ? 100.323 140.601 100.546 1.00 54.02 ?  113 LYS A CE    1 
ATOM   942   N  NZ    . LYS A 1 113 ? 100.064 139.894 99.263  1.00 53.32 1  113 LYS A NZ    1 
ATOM   943   N  N     . ILE A 1 114 ? 106.084 141.574 100.524 1.00 49.95 ?  114 ILE A N     1 
ATOM   944   C  CA    . ILE A 1 114 ? 107.338 142.010 99.923  1.00 49.11 ?  114 ILE A CA    1 
ATOM   945   C  C     . ILE A 1 114 ? 107.157 143.433 99.414  1.00 46.53 ?  114 ILE A C     1 
ATOM   946   O  O     . ILE A 1 114 ? 106.388 143.675 98.477  1.00 46.02 ?  114 ILE A O     1 
ATOM   947   C  CB    . ILE A 1 114 ? 107.774 141.071 98.788  1.00 48.91 ?  114 ILE A CB    1 
ATOM   948   C  CG1   . ILE A 1 114 ? 108.166 139.703 99.348  1.00 47.86 ?  114 ILE A CG1   1 
ATOM   949   C  CG2   . ILE A 1 114 ? 108.925 141.680 98.003  1.00 46.56 ?  114 ILE A CG2   1 
ATOM   950   C  CD1   . ILE A 1 114 ? 108.241 138.616 98.301  1.00 45.94 ?  114 ILE A CD1   1 
ATOM   951   N  N     . LEU A 1 115 ? 107.870 144.374 100.030 1.00 44.44 ?  115 LEU A N     1 
ATOM   952   C  CA    . LEU A 1 115 ? 107.818 145.768 99.614  1.00 44.73 ?  115 LEU A CA    1 
ATOM   953   C  C     . LEU A 1 115 ? 108.813 146.089 98.508  1.00 45.33 ?  115 LEU A C     1 
ATOM   954   O  O     . LEU A 1 115 ? 108.563 146.994 97.705  1.00 46.89 ?  115 LEU A O     1 
ATOM   955   C  CB    . LEU A 1 115 ? 108.083 146.685 100.811 1.00 45.97 ?  115 LEU A CB    1 
ATOM   956   C  CG    . LEU A 1 115 ? 106.994 146.756 101.882 1.00 43.44 ?  115 LEU A CG    1 
ATOM   957   C  CD1   . LEU A 1 115 ? 107.549 147.367 103.154 1.00 41.79 ?  115 LEU A CD1   1 
ATOM   958   C  CD2   . LEU A 1 115 ? 105.804 147.552 101.378 1.00 43.57 ?  115 LEU A CD2   1 
ATOM   959   N  N     . GLU A 1 116 ? 109.928 145.370 98.447  1.00 43.16 ?  116 GLU A N     1 
ATOM   960   C  CA    . GLU A 1 116 ? 111.003 145.650 97.507  1.00 39.91 ?  116 GLU A CA    1 
ATOM   961   C  C     . GLU A 1 116 ? 111.160 144.503 96.521  1.00 39.29 ?  116 GLU A C     1 
ATOM   962   O  O     . GLU A 1 116 ? 111.211 143.336 96.922  1.00 43.71 ?  116 GLU A O     1 
ATOM   963   C  CB    . GLU A 1 116 ? 112.326 145.874 98.241  1.00 39.97 ?  116 GLU A CB    1 
ATOM   964   C  CG    . GLU A 1 116 ? 112.698 147.325 98.448  1.00 39.88 ?  116 GLU A CG    1 
ATOM   965   C  CD    . GLU A 1 116 ? 113.934 147.478 99.308  1.00 42.48 ?  116 GLU A CD    1 
ATOM   966   O  OE1   . GLU A 1 116 ? 114.457 146.450 99.785  1.00 42.74 ?  116 GLU A OE1   1 
ATOM   967   O  OE2   . GLU A 1 116 ? 114.385 148.624 99.506  1.00 41.82 -1 116 GLU A OE2   1 
ATOM   968   N  N     . ARG A 1 117 ? 111.239 144.840 95.239  1.00 39.85 ?  117 ARG A N     1 
ATOM   969   C  CA    . ARG A 1 117 ? 111.712 143.912 94.227  1.00 38.83 ?  117 ARG A CA    1 
ATOM   970   C  C     . ARG A 1 117 ? 113.232 144.016 94.131  1.00 41.84 ?  117 ARG A C     1 
ATOM   971   O  O     . ARG A 1 117 ? 113.870 144.818 94.815  1.00 45.88 ?  117 ARG A O     1 
ATOM   972   C  CB    . ARG A 1 117 ? 111.049 144.197 92.880  1.00 39.03 ?  117 ARG A CB    1 
ATOM   973   C  CG    . ARG A 1 117 ? 109.532 144.166 92.908  1.00 42.97 ?  117 ARG A CG    1 
ATOM   974   C  CD    . ARG A 1 117 ? 109.022 142.789 93.297  1.00 45.73 ?  117 ARG A CD    1 
ATOM   975   N  NE    . ARG A 1 117 ? 109.059 141.860 92.175  1.00 42.39 ?  117 ARG A NE    1 
ATOM   976   C  CZ    . ARG A 1 117 ? 107.997 141.243 91.676  1.00 45.30 ?  117 ARG A CZ    1 
ATOM   977   N  NH1   . ARG A 1 117 ? 106.789 141.432 92.179  1.00 43.06 1  117 ARG A NH1   1 
ATOM   978   N  NH2   . ARG A 1 117 ? 108.152 140.415 90.648  1.00 45.39 ?  117 ARG A NH2   1 
ATOM   979   N  N     . TYR A 1 118 ? 113.829 143.189 93.271  1.00 35.54 ?  118 TYR A N     1 
ATOM   980   C  CA    . TYR A 1 118 ? 115.263 143.302 93.034  1.00 29.20 ?  118 TYR A CA    1 
ATOM   981   C  C     . TYR A 1 118 ? 115.610 144.665 92.447  1.00 32.30 ?  118 TYR A C     1 
ATOM   982   O  O     . TYR A 1 118 ? 116.583 145.305 92.865  1.00 34.04 ?  118 TYR A O     1 
ATOM   983   C  CB    . TYR A 1 118 ? 115.727 142.177 92.110  1.00 32.77 ?  118 TYR A CB    1 
ATOM   984   C  CG    . TYR A 1 118 ? 117.225 141.998 92.050  1.00 31.94 ?  118 TYR A CG    1 
ATOM   985   C  CD1   . TYR A 1 118 ? 117.960 141.749 93.200  1.00 29.32 ?  118 TYR A CD1   1 
ATOM   986   C  CD2   . TYR A 1 118 ? 117.903 142.073 90.843  1.00 30.79 ?  118 TYR A CD2   1 
ATOM   987   C  CE1   . TYR A 1 118 ? 119.327 141.583 93.148  1.00 30.43 ?  118 TYR A CE1   1 
ATOM   988   C  CE2   . TYR A 1 118 ? 119.270 141.905 90.781  1.00 27.06 ?  118 TYR A CE2   1 
ATOM   989   C  CZ    . TYR A 1 118 ? 119.977 141.662 91.936  1.00 32.55 ?  118 TYR A CZ    1 
ATOM   990   O  OH    . TYR A 1 118 ? 121.340 141.497 91.878  1.00 40.53 ?  118 TYR A OH    1 
ATOM   991   N  N     . GLU A 1 119 ? 114.808 145.131 91.487  1.00 39.97 ?  119 GLU A N     1 
ATOM   992   C  CA    . GLU A 1 119 ? 115.058 146.431 90.876  1.00 34.12 ?  119 GLU A CA    1 
ATOM   993   C  C     . GLU A 1 119 ? 114.911 147.560 91.888  1.00 34.96 ?  119 GLU A C     1 
ATOM   994   O  O     . GLU A 1 119 ? 115.689 148.517 91.868  1.00 41.43 ?  119 GLU A O     1 
ATOM   995   C  CB    . GLU A 1 119 ? 114.115 146.643 89.692  1.00 33.17 ?  119 GLU A CB    1 
ATOM   996   C  CG    . GLU A 1 119 ? 114.477 145.828 88.464  1.00 32.54 ?  119 GLU A CG    1 
ATOM   997   C  CD    . GLU A 1 119 ? 113.829 144.460 88.459  1.00 38.69 ?  119 GLU A CD    1 
ATOM   998   O  OE1   . GLU A 1 119 ? 113.584 143.911 89.554  1.00 41.82 ?  119 GLU A OE1   1 
ATOM   999   O  OE2   . GLU A 1 119 ? 113.569 143.928 87.360  1.00 40.34 -1 119 GLU A OE2   1 
ATOM   1000  N  N     . ASP A 1 120 ? 113.916 147.475 92.774  1.00 36.99 ?  120 ASP A N     1 
ATOM   1001  C  CA    . ASP A 1 120 ? 113.745 148.518 93.781  1.00 36.79 ?  120 ASP A CA    1 
ATOM   1002  C  C     . ASP A 1 120 ? 114.937 148.574 94.727  1.00 36.14 ?  120 ASP A C     1 
ATOM   1003  O  O     . ASP A 1 120 ? 115.440 149.658 95.044  1.00 36.96 ?  120 ASP A O     1 
ATOM   1004  C  CB    . ASP A 1 120 ? 112.452 148.290 94.562  1.00 37.13 ?  120 ASP A CB    1 
ATOM   1005  C  CG    . ASP A 1 120 ? 111.247 148.138 93.660  1.00 39.88 ?  120 ASP A CG    1 
ATOM   1006  O  OD1   . ASP A 1 120 ? 110.988 149.052 92.852  1.00 41.40 ?  120 ASP A OD1   1 
ATOM   1007  O  OD2   . ASP A 1 120 ? 110.558 147.101 93.759  1.00 43.96 -1 120 ASP A OD2   1 
ATOM   1008  N  N     . ARG A 1 121 ? 115.403 147.412 95.190  1.00 31.02 ?  121 ARG A N     1 
ATOM   1009  C  CA    . ARG A 1 121 ? 116.569 147.376 96.064  1.00 28.88 ?  121 ARG A CA    1 
ATOM   1010  C  C     . ARG A 1 121 ? 117.800 147.933 95.362  1.00 31.20 ?  121 ARG A C     1 
ATOM   1011  O  O     . ARG A 1 121 ? 118.564 148.709 95.949  1.00 36.18 ?  121 ARG A O     1 
ATOM   1012  C  CB    . ARG A 1 121 ? 116.819 145.942 96.535  1.00 31.12 ?  121 ARG A CB    1 
ATOM   1013  C  CG    . ARG A 1 121 ? 118.104 145.741 97.314  1.00 25.99 ?  121 ARG A CG    1 
ATOM   1014  C  CD    . ARG A 1 121 ? 117.888 145.985 98.793  1.00 28.01 ?  121 ARG A CD    1 
ATOM   1015  N  NE    . ARG A 1 121 ? 118.435 147.267 99.220  1.00 36.89 ?  121 ARG A NE    1 
ATOM   1016  C  CZ    . ARG A 1 121 ? 117.873 148.058 100.122 1.00 31.79 ?  121 ARG A CZ    1 
ATOM   1017  N  NH1   . ARG A 1 121 ? 116.724 147.744 100.695 1.00 39.02 1  121 ARG A NH1   1 
ATOM   1018  N  NH2   . ARG A 1 121 ? 118.476 149.195 100.453 1.00 25.87 ?  121 ARG A NH2   1 
ATOM   1019  N  N     . ILE A 1 122 ? 118.001 147.557 94.097  1.00 29.83 ?  122 ILE A N     1 
ATOM   1020  C  CA    . ILE A 1 122 ? 119.162 148.044 93.360  1.00 27.00 ?  122 ILE A CA    1 
ATOM   1021  C  C     . ILE A 1 122 ? 119.078 149.553 93.162  1.00 25.91 ?  122 ILE A C     1 
ATOM   1022  O  O     . ILE A 1 122 ? 120.080 150.262 93.288  1.00 33.48 ?  122 ILE A O     1 
ATOM   1023  C  CB    . ILE A 1 122 ? 119.297 147.300 92.021  1.00 29.29 ?  122 ILE A CB    1 
ATOM   1024  C  CG1   . ILE A 1 122 ? 119.913 145.918 92.243  1.00 24.59 ?  122 ILE A CG1   1 
ATOM   1025  C  CG2   . ILE A 1 122 ? 120.138 148.106 91.046  1.00 26.32 ?  122 ILE A CG2   1 
ATOM   1026  C  CD1   . ILE A 1 122 ? 119.939 145.063 91.008  1.00 28.71 ?  122 ILE A CD1   1 
ATOM   1027  N  N     . SER A 1 123 ? 117.889 150.067 92.838  1.00 30.25 ?  123 SER A N     1 
ATOM   1028  C  CA    . SER A 1 123 ? 117.727 151.505 92.655  1.00 28.76 ?  123 SER A CA    1 
ATOM   1029  C  C     . SER A 1 123 ? 117.968 152.260 93.954  1.00 30.67 ?  123 SER A C     1 
ATOM   1030  O  O     . SER A 1 123 ? 118.588 153.329 93.951  1.00 35.69 ?  123 SER A O     1 
ATOM   1031  C  CB    . SER A 1 123 ? 116.332 151.813 92.112  1.00 29.06 ?  123 SER A CB    1 
ATOM   1032  O  OG    . SER A 1 123 ? 116.103 151.147 90.884  1.00 32.21 ?  123 SER A OG    1 
ATOM   1033  N  N     . ILE A 1 124 ? 117.483 151.725 95.075  1.00 25.89 ?  124 ILE A N     1 
ATOM   1034  C  CA    . ILE A 1 124 ? 117.714 152.378 96.360  1.00 30.38 ?  124 ILE A CA    1 
ATOM   1035  C  C     . ILE A 1 124 ? 119.200 152.398 96.685  1.00 29.18 ?  124 ILE A C     1 
ATOM   1036  O  O     . ILE A 1 124 ? 119.738 153.414 97.146  1.00 30.48 ?  124 ILE A O     1 
ATOM   1037  C  CB    . ILE A 1 124 ? 116.895 151.689 97.465  1.00 37.25 ?  124 ILE A CB    1 
ATOM   1038  C  CG1   . ILE A 1 124 ? 115.416 152.055 97.332  1.00 34.62 ?  124 ILE A CG1   1 
ATOM   1039  C  CG2   . ILE A 1 124 ? 117.421 152.070 98.839  1.00 32.25 ?  124 ILE A CG2   1 
ATOM   1040  C  CD1   . ILE A 1 124 ? 115.149 153.540 97.416  1.00 31.86 ?  124 ILE A CD1   1 
ATOM   1041  N  N     . VAL A 1 125 ? 119.891 151.281 96.448  1.00 24.45 ?  125 VAL A N     1 
ATOM   1042  C  CA    . VAL A 1 125 ? 121.325 151.227 96.718  1.00 23.87 ?  125 VAL A CA    1 
ATOM   1043  C  C     . VAL A 1 125 ? 122.075 152.202 95.819  1.00 22.33 ?  125 VAL A C     1 
ATOM   1044  O  O     . VAL A 1 125 ? 123.016 152.875 96.255  1.00 28.15 ?  125 VAL A O     1 
ATOM   1045  C  CB    . VAL A 1 125 ? 121.845 149.788 96.559  1.00 32.37 ?  125 VAL A CB    1 
ATOM   1046  C  CG1   . VAL A 1 125 ? 123.353 149.744 96.739  1.00 31.27 ?  125 VAL A CG1   1 
ATOM   1047  C  CG2   . VAL A 1 125 ? 121.161 148.866 97.554  1.00 22.03 ?  125 VAL A CG2   1 
ATOM   1048  N  N     . ALA A 1 126 ? 121.676 152.291 94.549  1.00 24.26 ?  126 ALA A N     1 
ATOM   1049  C  CA    . ALA A 1 126 ? 122.329 153.213 93.626  1.00 21.60 ?  126 ALA A CA    1 
ATOM   1050  C  C     . ALA A 1 126 ? 122.105 154.662 94.035  1.00 26.03 ?  126 ALA A C     1 
ATOM   1051  O  O     . ALA A 1 126 ? 123.025 155.482 93.958  1.00 34.23 ?  126 ALA A O     1 
ATOM   1052  C  CB    . ALA A 1 126 ? 121.825 152.972 92.203  1.00 26.68 ?  126 ALA A CB    1 
ATOM   1053  N  N     . LEU A 1 127 ? 120.886 155.001 94.460  1.00 29.34 ?  127 LEU A N     1 
ATOM   1054  C  CA    . LEU A 1 127 ? 120.619 156.357 94.930  1.00 27.49 ?  127 LEU A CA    1 
ATOM   1055  C  C     . LEU A 1 127 ? 121.429 156.670 96.180  1.00 22.93 ?  127 LEU A C     1 
ATOM   1056  O  O     . LEU A 1 127 ? 121.957 157.778 96.328  1.00 25.67 ?  127 LEU A O     1 
ATOM   1057  C  CB    . LEU A 1 127 ? 119.125 156.536 95.194  1.00 26.33 ?  127 LEU A CB    1 
ATOM   1058  C  CG    . LEU A 1 127 ? 118.229 156.579 93.955  1.00 26.66 ?  127 LEU A CG    1 
ATOM   1059  C  CD1   . LEU A 1 127 ? 116.765 156.473 94.343  1.00 32.31 ?  127 LEU A CD1   1 
ATOM   1060  C  CD2   . LEU A 1 127 ? 118.483 157.843 93.155  1.00 26.91 ?  127 LEU A CD2   1 
ATOM   1061  N  N     . PHE A 1 128 ? 121.538 155.703 97.093  1.00 23.26 ?  128 PHE A N     1 
ATOM   1062  C  CA    . PHE A 1 128 ? 122.369 155.892 98.276  1.00 25.09 ?  128 PHE A CA    1 
ATOM   1063  C  C     . PHE A 1 128 ? 123.824 156.129 97.890  1.00 23.34 ?  128 PHE A C     1 
ATOM   1064  O  O     . PHE A 1 128 ? 124.492 157.000 98.460  1.00 32.48 ?  128 PHE A O     1 
ATOM   1065  C  CB    . PHE A 1 128 ? 122.238 154.677 99.195  1.00 25.42 ?  128 PHE A CB    1 
ATOM   1066  C  CG    . PHE A 1 128 ? 123.193 154.680 100.351 1.00 29.14 ?  128 PHE A CG    1 
ATOM   1067  C  CD1   . PHE A 1 128 ? 122.902 155.385 101.506 1.00 29.76 ?  128 PHE A CD1   1 
ATOM   1068  C  CD2   . PHE A 1 128 ? 124.379 153.969 100.290 1.00 30.16 ?  128 PHE A CD2   1 
ATOM   1069  C  CE1   . PHE A 1 128 ? 123.778 155.386 102.572 1.00 28.79 ?  128 PHE A CE1   1 
ATOM   1070  C  CE2   . PHE A 1 128 ? 125.258 153.968 101.353 1.00 28.97 ?  128 PHE A CE2   1 
ATOM   1071  C  CZ    . PHE A 1 128 ? 124.957 154.676 102.495 1.00 28.30 ?  128 PHE A CZ    1 
ATOM   1072  N  N     . PHE A 1 129 ? 124.330 155.367 96.920  1.00 25.63 ?  129 PHE A N     1 
ATOM   1073  C  CA    . PHE A 1 129 ? 125.719 155.514 96.496  1.00 20.47 ?  129 PHE A CA    1 
ATOM   1074  C  C     . PHE A 1 129 ? 125.962 156.866 95.834  1.00 23.13 ?  129 PHE A C     1 
ATOM   1075  O  O     . PHE A 1 129 ? 126.954 157.541 96.127  1.00 28.77 ?  129 PHE A O     1 
ATOM   1076  C  CB    . PHE A 1 129 ? 126.096 154.380 95.543  1.00 24.00 ?  129 PHE A CB    1 
ATOM   1077  C  CG    . PHE A 1 129 ? 126.380 153.076 96.228  1.00 22.07 ?  129 PHE A CG    1 
ATOM   1078  C  CD1   . PHE A 1 129 ? 126.793 153.046 97.549  1.00 22.86 ?  129 PHE A CD1   1 
ATOM   1079  C  CD2   . PHE A 1 129 ? 126.238 151.878 95.547  1.00 22.34 ?  129 PHE A CD2   1 
ATOM   1080  C  CE1   . PHE A 1 129 ? 127.055 151.847 98.179  1.00 26.57 ?  129 PHE A CE1   1 
ATOM   1081  C  CE2   . PHE A 1 129 ? 126.501 150.675 96.174  1.00 22.49 ?  129 PHE A CE2   1 
ATOM   1082  C  CZ    . PHE A 1 129 ? 126.909 150.660 97.491  1.00 25.99 ?  129 PHE A CZ    1 
ATOM   1083  N  N     . ALA A 1 130 ? 125.063 157.277 94.936  1.00 29.37 ?  130 ALA A N     1 
ATOM   1084  C  CA    . ALA A 1 130 ? 125.312 158.461 94.122  1.00 27.31 ?  130 ALA A CA    1 
ATOM   1085  C  C     . ALA A 1 130 ? 125.395 159.728 94.963  1.00 34.83 ?  130 ALA A C     1 
ATOM   1086  O  O     . ALA A 1 130 ? 126.073 160.685 94.573  1.00 40.53 ?  130 ALA A O     1 
ATOM   1087  C  CB    . ALA A 1 130 ? 124.228 158.602 93.056  1.00 28.89 ?  130 ALA A CB    1 
ATOM   1088  N  N     . ASN A 1 131 ? 124.718 159.758 96.109  1.00 33.49 ?  131 ASN A N     1 
ATOM   1089  C  CA    . ASN A 1 131 ? 124.751 160.916 96.999  1.00 34.89 ?  131 ASN A CA    1 
ATOM   1090  C  C     . ASN A 1 131 ? 124.309 162.188 96.276  1.00 34.70 ?  131 ASN A C     1 
ATOM   1091  O  O     . ASN A 1 131 ? 124.913 163.252 96.424  1.00 39.75 ?  131 ASN A O     1 
ATOM   1092  C  CB    . ASN A 1 131 ? 126.141 161.095 97.612  1.00 37.35 ?  131 ASN A CB    1 
ATOM   1093  C  CG    . ASN A 1 131 ? 126.141 162.037 98.796  1.00 39.60 ?  131 ASN A CG    1 
ATOM   1094  O  OD1   . ASN A 1 131 ? 125.298 161.934 99.686  1.00 36.96 ?  131 ASN A OD1   1 
ATOM   1095  N  ND2   . ASN A 1 131 ? 127.091 162.963 98.814  1.00 34.51 ?  131 ASN A ND2   1 
ATOM   1096  N  N     . GLY A 1 132 ? 123.243 162.078 95.485  1.00 34.98 ?  132 GLY A N     1 
ATOM   1097  C  CA    . GLY A 1 132 ? 122.687 163.207 94.771  1.00 35.21 ?  132 GLY A CA    1 
ATOM   1098  C  C     . GLY A 1 132 ? 123.007 163.259 93.292  1.00 39.57 ?  132 GLY A C     1 
ATOM   1099  O  O     . GLY A 1 132 ? 122.372 164.037 92.569  1.00 41.56 ?  132 GLY A O     1 
ATOM   1100  N  N     . ASP A 1 133 ? 123.962 162.463 92.820  1.00 40.04 ?  133 ASP A N     1 
ATOM   1101  C  CA    . ASP A 1 133 ? 124.345 162.455 91.411  1.00 38.58 ?  133 ASP A CA    1 
ATOM   1102  C  C     . ASP A 1 133 ? 123.422 161.504 90.658  1.00 39.99 ?  133 ASP A C     1 
ATOM   1103  O  O     . ASP A 1 133 ? 123.524 160.283 90.806  1.00 45.57 ?  133 ASP A O     1 
ATOM   1104  C  CB    . ASP A 1 133 ? 125.807 162.045 91.254  1.00 40.60 ?  133 ASP A CB    1 
ATOM   1105  C  CG    . ASP A 1 133 ? 126.396 162.482 89.929  1.00 44.02 ?  133 ASP A CG    1 
ATOM   1106  O  OD1   . ASP A 1 133 ? 125.617 162.779 88.999  1.00 43.13 ?  133 ASP A OD1   1 
ATOM   1107  O  OD2   . ASP A 1 133 ? 127.638 162.525 89.817  1.00 43.39 -1 133 ASP A OD2   1 
ATOM   1108  N  N     . THR A 1 134 ? 122.522 162.064 89.848  1.00 39.22 ?  134 THR A N     1 
ATOM   1109  C  CA    . THR A 1 134 ? 121.560 161.232 89.132  1.00 39.54 ?  134 THR A CA    1 
ATOM   1110  C  C     . THR A 1 134 ? 122.244 160.363 88.084  1.00 38.53 ?  134 THR A C     1 
ATOM   1111  O  O     . THR A 1 134 ? 121.909 159.183 87.937  1.00 41.70 ?  134 THR A O     1 
ATOM   1112  C  CB    . THR A 1 134 ? 120.488 162.108 88.484  1.00 42.17 ?  134 THR A CB    1 
ATOM   1113  O  OG1   . THR A 1 134 ? 119.858 162.909 89.490  1.00 45.64 ?  134 THR A OG1   1 
ATOM   1114  C  CG2   . THR A 1 134 ? 119.439 161.245 87.803  1.00 40.52 ?  134 THR A CG2   1 
ATOM   1115  N  N     . GLU A 1 135 ? 123.195 160.928 87.338  1.00 42.00 ?  135 GLU A N     1 
ATOM   1116  C  CA    . GLU A 1 135 ? 123.936 160.131 86.365  1.00 41.30 ?  135 GLU A CA    1 
ATOM   1117  C  C     . GLU A 1 135 ? 124.801 159.086 87.056  1.00 41.99 ?  135 GLU A C     1 
ATOM   1118  O  O     . GLU A 1 135 ? 124.906 157.946 86.587  1.00 46.40 ?  135 GLU A O     1 
ATOM   1119  C  CB    . GLU A 1 135 ? 124.785 161.039 85.478  1.00 40.30 ?  135 GLU A CB    1 
ATOM   1120  C  CG    . GLU A 1 135 ? 124.013 162.204 84.886  1.00 41.05 ?  135 GLU A CG    1 
ATOM   1121  C  CD    . GLU A 1 135 ? 122.922 161.751 83.937  1.00 48.39 ?  135 GLU A CD    1 
ATOM   1122  O  OE1   . GLU A 1 135 ? 123.235 161.015 82.978  1.00 48.59 ?  135 GLU A OE1   1 
ATOM   1123  O  OE2   . GLU A 1 135 ? 121.750 162.126 84.152  1.00 49.65 -1 135 GLU A OE2   1 
ATOM   1124  N  N     . LYS A 1 136 ? 125.436 159.455 88.170  1.00 30.68 ?  136 LYS A N     1 
ATOM   1125  C  CA    . LYS A 1 136 ? 126.163 158.471 88.963  1.00 30.77 ?  136 LYS A CA    1 
ATOM   1126  C  C     . LYS A 1 136 ? 125.227 157.375 89.456  1.00 33.25 ?  136 LYS A C     1 
ATOM   1127  O  O     . LYS A 1 136 ? 125.590 156.193 89.468  1.00 35.39 ?  136 LYS A O     1 
ATOM   1128  C  CB    . LYS A 1 136 ? 126.859 159.159 90.138  1.00 34.75 ?  136 LYS A CB    1 
ATOM   1129  C  CG    . LYS A 1 136 ? 127.874 158.294 90.862  1.00 30.74 ?  136 LYS A CG    1 
ATOM   1130  C  CD    . LYS A 1 136 ? 129.216 158.309 90.155  1.00 34.15 ?  136 LYS A CD    1 
ATOM   1131  C  CE    . LYS A 1 136 ? 130.317 157.782 91.059  1.00 38.76 ?  136 LYS A CE    1 
ATOM   1132  N  NZ    . LYS A 1 136 ? 131.667 158.001 90.475  1.00 37.35 1  136 LYS A NZ    1 
ATOM   1133  N  N     . ALA A 1 137 ? 124.015 157.752 89.873  1.00 31.32 ?  137 ALA A N     1 
ATOM   1134  C  CA    . ALA A 1 137 ? 123.047 156.759 90.324  1.00 26.86 ?  137 ALA A CA    1 
ATOM   1135  C  C     . ALA A 1 137 ? 122.654 155.818 89.193  1.00 25.22 ?  137 ALA A C     1 
ATOM   1136  O  O     . ALA A 1 137 ? 122.507 154.611 89.405  1.00 28.27 ?  137 ALA A O     1 
ATOM   1137  C  CB    . ALA A 1 137 ? 121.816 157.451 90.904  1.00 30.14 ?  137 ALA A CB    1 
ATOM   1138  N  N     . LYS A 1 138 ? 122.473 156.353 87.985  1.00 28.96 ?  138 LYS A N     1 
ATOM   1139  C  CA    . LYS A 1 138 ? 122.145 155.500 86.846  1.00 32.28 ?  138 LYS A CA    1 
ATOM   1140  C  C     . LYS A 1 138 ? 123.301 154.568 86.506  1.00 32.08 ?  138 LYS A C     1 
ATOM   1141  O  O     . LYS A 1 138 ? 123.086 153.404 86.145  1.00 36.44 ?  138 LYS A O     1 
ATOM   1142  C  CB    . LYS A 1 138 ? 121.765 156.356 85.639  1.00 35.73 ?  138 LYS A CB    1 
ATOM   1143  C  CG    . LYS A 1 138 ? 120.358 156.923 85.708  1.00 32.89 ?  138 LYS A CG    1 
ATOM   1144  C  CD    . LYS A 1 138 ? 120.020 157.725 84.466  1.00 32.21 ?  138 LYS A CD    1 
ATOM   1145  C  CE    . LYS A 1 138 ? 119.764 159.182 84.808  1.00 37.66 ?  138 LYS A CE    1 
ATOM   1146  N  NZ    . LYS A 1 138 ? 119.829 160.058 83.606  1.00 37.28 1  138 LYS A NZ    1 
ATOM   1147  N  N     . GLU A 1 139 ? 124.537 155.061 86.611  1.00 33.92 ?  139 GLU A N     1 
ATOM   1148  C  CA    . GLU A 1 139 ? 125.694 154.200 86.394  1.00 28.27 ?  139 GLU A CA    1 
ATOM   1149  C  C     . GLU A 1 139 ? 125.746 153.081 87.425  1.00 26.37 ?  139 GLU A C     1 
ATOM   1150  O  O     . GLU A 1 139 ? 126.041 151.929 87.089  1.00 33.53 ?  139 GLU A O     1 
ATOM   1151  C  CB    . GLU A 1 139 ? 126.979 155.026 86.428  1.00 29.26 ?  139 GLU A CB    1 
ATOM   1152  C  CG    . GLU A 1 139 ? 127.444 155.500 85.063  1.00 32.42 ?  139 GLU A CG    1 
ATOM   1153  C  CD    . GLU A 1 139 ? 128.164 156.831 85.120  1.00 42.41 ?  139 GLU A CD    1 
ATOM   1154  O  OE1   . GLU A 1 139 ? 128.947 157.045 86.069  1.00 41.78 ?  139 GLU A OE1   1 
ATOM   1155  O  OE2   . GLU A 1 139 ? 127.950 157.664 84.214  1.00 42.28 -1 139 GLU A OE2   1 
ATOM   1156  N  N     . TYR A 1 140 ? 125.457 153.397 88.688  1.00 22.17 ?  140 TYR A N     1 
ATOM   1157  C  CA    . TYR A 1 140 ? 125.415 152.365 89.720  1.00 22.02 ?  140 TYR A CA    1 
ATOM   1158  C  C     . TYR A 1 140 ? 124.300 151.362 89.450  1.00 22.73 ?  140 TYR A C     1 
ATOM   1159  O  O     . TYR A 1 140 ? 124.466 150.156 89.674  1.00 29.88 ?  140 TYR A O     1 
ATOM   1160  C  CB    . TYR A 1 140 ? 125.235 153.001 91.097  1.00 22.18 ?  140 TYR A CB    1 
ATOM   1161  C  CG    . TYR A 1 140 ? 126.494 153.613 91.661  1.00 28.54 ?  140 TYR A CG    1 
ATOM   1162  C  CD1   . TYR A 1 140 ? 127.659 152.868 91.785  1.00 29.45 ?  140 TYR A CD1   1 
ATOM   1163  C  CD2   . TYR A 1 140 ? 126.516 154.937 92.076  1.00 27.65 ?  140 TYR A CD2   1 
ATOM   1164  C  CE1   . TYR A 1 140 ? 128.810 153.425 92.301  1.00 25.69 ?  140 TYR A CE1   1 
ATOM   1165  C  CE2   . TYR A 1 140 ? 127.662 155.502 92.593  1.00 24.73 ?  140 TYR A CE2   1 
ATOM   1166  C  CZ    . TYR A 1 140 ? 128.805 154.743 92.704  1.00 23.36 ?  140 TYR A CZ    1 
ATOM   1167  O  OH    . TYR A 1 140 ? 129.947 155.308 93.219  1.00 37.72 ?  140 TYR A OH    1 
ATOM   1168  N  N     . VAL A 1 141 ? 123.149 151.847 88.984  1.00 31.82 ?  141 VAL A N     1 
ATOM   1169  C  CA    . VAL A 1 141 ? 122.037 150.958 88.666  1.00 31.16 ?  141 VAL A CA    1 
ATOM   1170  C  C     . VAL A 1 141 ? 122.428 150.003 87.550  1.00 22.39 ?  141 VAL A C     1 
ATOM   1171  O  O     . VAL A 1 141 ? 122.131 148.806 87.607  1.00 28.49 ?  141 VAL A O     1 
ATOM   1172  C  CB    . VAL A 1 141 ? 120.783 151.775 88.299  1.00 28.73 ?  141 VAL A CB    1 
ATOM   1173  C  CG1   . VAL A 1 141 ? 119.854 150.953 87.422  1.00 30.63 ?  141 VAL A CG1   1 
ATOM   1174  C  CG2   . VAL A 1 141 ? 120.065 152.230 89.552  1.00 24.45 ?  141 VAL A CG2   1 
ATOM   1175  N  N     . ASN A 1 142 ? 123.088 150.516 86.512  1.00 26.21 ?  142 ASN A N     1 
ATOM   1176  C  CA    . ASN A 1 142 ? 123.548 149.647 85.434  1.00 26.02 ?  142 ASN A CA    1 
ATOM   1177  C  C     . ASN A 1 142 ? 124.595 148.658 85.931  1.00 28.81 ?  142 ASN A C     1 
ATOM   1178  O  O     . ASN A 1 142 ? 124.593 147.487 85.535  1.00 31.34 ?  142 ASN A O     1 
ATOM   1179  C  CB    . ASN A 1 142 ? 124.100 150.484 84.282  1.00 25.33 ?  142 ASN A CB    1 
ATOM   1180  C  CG    . ASN A 1 142 ? 123.007 151.074 83.419  1.00 32.33 ?  142 ASN A CG    1 
ATOM   1181  O  OD1   . ASN A 1 142 ? 121.979 150.441 83.182  1.00 31.96 ?  142 ASN A OD1   1 
ATOM   1182  N  ND2   . ASN A 1 142 ? 123.222 152.294 82.941  1.00 32.46 ?  142 ASN A ND2   1 
ATOM   1183  N  N     . LEU A 1 143 ? 125.498 149.112 86.802  1.00 26.78 ?  143 LEU A N     1 
ATOM   1184  C  CA    . LEU A 1 143 ? 126.540 148.234 87.322  1.00 22.41 ?  143 LEU A CA    1 
ATOM   1185  C  C     . LEU A 1 143 ? 125.949 147.081 88.123  1.00 26.41 ?  143 LEU A C     1 
ATOM   1186  O  O     . LEU A 1 143 ? 126.384 145.933 87.984  1.00 28.39 ?  143 LEU A O     1 
ATOM   1187  C  CB    . LEU A 1 143 ? 127.513 149.043 88.181  1.00 24.64 ?  143 LEU A CB    1 
ATOM   1188  C  CG    . LEU A 1 143 ? 128.810 148.379 88.647  1.00 25.69 ?  143 LEU A CG    1 
ATOM   1189  C  CD1   . LEU A 1 143 ? 129.806 148.295 87.509  1.00 24.50 ?  143 LEU A CD1   1 
ATOM   1190  C  CD2   . LEU A 1 143 ? 129.404 149.136 89.823  1.00 24.92 ?  143 LEU A CD2   1 
ATOM   1191  N  N     . MET A 1 144 ? 124.956 147.365 88.967  1.00 28.04 ?  144 MET A N     1 
ATOM   1192  C  CA    . MET A 1 144 ? 124.408 146.326 89.833  1.00 21.95 ?  144 MET A CA    1 
ATOM   1193  C  C     . MET A 1 144 ? 123.373 145.465 89.114  1.00 22.60 ?  144 MET A C     1 
ATOM   1194  O  O     . MET A 1 144 ? 123.285 144.259 89.368  1.00 27.35 ?  144 MET A O     1 
ATOM   1195  C  CB    . MET A 1 144 ? 123.804 146.950 91.090  1.00 21.82 ?  144 MET A CB    1 
ATOM   1196  C  CG    . MET A 1 144 ? 124.839 147.369 92.124  1.00 24.14 ?  144 MET A CG    1 
ATOM   1197  S  SD    . MET A 1 144 ? 124.137 148.246 93.535  1.00 40.23 ?  144 MET A SD    1 
ATOM   1198  C  CE    . MET A 1 144 ? 123.422 149.675 92.733  1.00 25.78 ?  144 MET A CE    1 
ATOM   1199  N  N     . ILE A 1 145 ? 122.579 146.060 88.221  1.00 22.04 ?  145 ILE A N     1 
ATOM   1200  C  CA    . ILE A 1 145 ? 121.587 145.292 87.477  1.00 26.08 ?  145 ILE A CA    1 
ATOM   1201  C  C     . ILE A 1 145 ? 122.272 144.368 86.478  1.00 29.52 ?  145 ILE A C     1 
ATOM   1202  O  O     . ILE A 1 145 ? 121.817 143.244 86.238  1.00 31.11 ?  145 ILE A O     1 
ATOM   1203  C  CB    . ILE A 1 145 ? 120.581 146.238 86.795  1.00 28.33 ?  145 ILE A CB    1 
ATOM   1204  C  CG1   . ILE A 1 145 ? 119.213 145.565 86.670  1.00 25.36 ?  145 ILE A CG1   1 
ATOM   1205  C  CG2   . ILE A 1 145 ? 121.086 146.688 85.434  1.00 27.22 ?  145 ILE A CG2   1 
ATOM   1206  C  CD1   . ILE A 1 145 ? 118.539 145.300 87.993  1.00 24.83 ?  145 ILE A CD1   1 
ATOM   1207  N  N     . ASN A 1 146 ? 123.374 144.825 85.880  1.00 26.32 ?  146 ASN A N     1 
ATOM   1208  C  CA    . ASN A 1 146 ? 124.223 143.933 85.102  1.00 22.53 ?  146 ASN A CA    1 
ATOM   1209  C  C     . ASN A 1 146 ? 124.933 142.915 85.980  1.00 20.02 ?  146 ASN A C     1 
ATOM   1210  O  O     . ASN A 1 146 ? 125.499 141.952 85.454  1.00 31.41 ?  146 ASN A O     1 
ATOM   1211  C  CB    . ASN A 1 146 ? 125.251 144.740 84.308  1.00 23.96 ?  146 ASN A CB    1 
ATOM   1212  C  CG    . ASN A 1 146 ? 124.618 145.584 83.222  1.00 27.08 ?  146 ASN A CG    1 
ATOM   1213  O  OD1   . ASN A 1 146 ? 123.484 145.340 82.813  1.00 30.83 ?  146 ASN A OD1   1 
ATOM   1214  N  ND2   . ASN A 1 146 ? 125.349 146.584 82.747  1.00 29.05 ?  146 ASN A ND2   1 
ATOM   1215  N  N     . GLN A 1 147 ? 124.908 143.107 87.297  1.00 26.01 ?  147 GLN A N     1 
ATOM   1216  C  CA    . GLN A 1 147 ? 125.540 142.199 88.247  1.00 18.84 ?  147 GLN A CA    1 
ATOM   1217  C  C     . GLN A 1 147 ? 127.045 142.115 88.024  1.00 21.99 ?  147 GLN A C     1 
ATOM   1218  O  O     . GLN A 1 147 ? 127.665 141.078 88.265  1.00 33.70 ?  147 GLN A O     1 
ATOM   1219  C  CB    . GLN A 1 147 ? 124.899 140.811 88.195  1.00 22.15 ?  147 GLN A CB    1 
ATOM   1220  C  CG    . GLN A 1 147 ? 123.467 140.794 88.707  1.00 20.62 ?  147 GLN A CG    1 
ATOM   1221  C  CD    . GLN A 1 147 ? 122.991 139.408 89.074  1.00 23.70 ?  147 GLN A CD    1 
ATOM   1222  O  OE1   . GLN A 1 147 ? 123.285 138.435 88.383  1.00 34.92 ?  147 GLN A OE1   1 
ATOM   1223  N  NE2   . GLN A 1 147 ? 122.252 139.310 90.171  1.00 22.81 ?  147 GLN A NE2   1 
ATOM   1224  N  N     . GLU A 1 148 ? 127.640 143.212 87.555  1.00 23.14 ?  148 GLU A N     1 
ATOM   1225  C  CA    . GLU A 1 148 ? 129.092 143.307 87.484  1.00 19.09 ?  148 GLU A CA    1 
ATOM   1226  C  C     . GLU A 1 148 ? 129.701 143.561 88.855  1.00 17.50 ?  148 GLU A C     1 
ATOM   1227  O  O     . GLU A 1 148 ? 130.790 143.056 89.152  1.00 20.52 ?  148 GLU A O     1 
ATOM   1228  C  CB    . GLU A 1 148 ? 129.497 144.417 86.514  1.00 15.83 ?  148 GLU A CB    1 
ATOM   1229  C  CG    . GLU A 1 148 ? 129.047 144.187 85.084  1.00 16.21 ?  148 GLU A CG    1 
ATOM   1230  C  CD    . GLU A 1 148 ? 129.141 145.440 84.236  1.00 29.63 ?  148 GLU A CD    1 
ATOM   1231  O  OE1   . GLU A 1 148 ? 128.216 146.276 84.302  1.00 32.15 ?  148 GLU A OE1   1 
ATOM   1232  O  OE2   . GLU A 1 148 ? 130.140 145.591 83.503  1.00 34.07 -1 148 GLU A OE2   1 
ATOM   1233  N  N     . TYR A 1 149 ? 129.017 144.330 89.696  1.00 22.08 ?  149 TYR A N     1 
ATOM   1234  C  CA    . TYR A 1 149 ? 129.473 144.639 91.043  1.00 17.98 ?  149 TYR A CA    1 
ATOM   1235  C  C     . TYR A 1 149 ? 128.360 144.311 92.024  1.00 19.06 ?  149 TYR A C     1 
ATOM   1236  O  O     . TYR A 1 149 ? 127.196 144.648 91.783  1.00 25.42 ?  149 TYR A O     1 
ATOM   1237  C  CB    . TYR A 1 149 ? 129.876 146.111 91.166  1.00 16.38 ?  149 TYR A CB    1 
ATOM   1238  C  CG    . TYR A 1 149 ? 130.140 146.559 92.585  1.00 18.83 ?  149 TYR A CG    1 
ATOM   1239  C  CD1   . TYR A 1 149 ? 131.233 146.079 93.292  1.00 14.37 ?  149 TYR A CD1   1 
ATOM   1240  C  CD2   . TYR A 1 149 ? 129.296 147.462 93.216  1.00 16.89 ?  149 TYR A CD2   1 
ATOM   1241  C  CE1   . TYR A 1 149 ? 131.478 146.485 94.586  1.00 13.85 ?  149 TYR A CE1   1 
ATOM   1242  C  CE2   . TYR A 1 149 ? 129.535 147.873 94.509  1.00 20.78 ?  149 TYR A CE2   1 
ATOM   1243  C  CZ    . TYR A 1 149 ? 130.627 147.382 95.190  1.00 17.58 ?  149 TYR A CZ    1 
ATOM   1244  O  OH    . TYR A 1 149 ? 130.870 147.788 96.480  1.00 18.36 ?  149 TYR A OH    1 
ATOM   1245  N  N     . GLN A 1 150 ? 128.714 143.647 93.115  1.00 13.82 ?  150 GLN A N     1 
ATOM   1246  C  CA    . GLN A 1 150 ? 127.761 143.312 94.171  1.00 2.91  ?  150 GLN A CA    1 
ATOM   1247  C  C     . GLN A 1 150 ? 128.212 143.930 95.484  1.00 10.80 ?  150 GLN A C     1 
ATOM   1248  O  O     . GLN A 1 150 ? 129.245 143.511 96.038  1.00 17.70 ?  150 GLN A O     1 
ATOM   1249  C  CB    . GLN A 1 150 ? 127.625 141.796 94.312  1.00 8.60  ?  150 GLN A CB    1 
ATOM   1250  C  CG    . GLN A 1 150 ? 126.798 141.340 95.505  1.00 17.32 ?  150 GLN A CG    1 
ATOM   1251  C  CD    . GLN A 1 150 ? 125.390 141.903 95.503  1.00 17.02 ?  150 GLN A CD    1 
ATOM   1252  O  OE1   . GLN A 1 150 ? 124.571 141.554 94.656  1.00 29.99 ?  150 GLN A OE1   1 
ATOM   1253  N  NE2   . GLN A 1 150 ? 125.102 142.776 96.458  1.00 4.33  ?  150 GLN A NE2   1 
ATOM   1254  N  N     . PRO A 1 151 ? 127.496 144.916 96.020  1.00 21.61 ?  151 PRO A N     1 
ATOM   1255  C  CA    . PRO A 1 151 ? 127.835 145.422 97.353  1.00 10.77 ?  151 PRO A CA    1 
ATOM   1256  C  C     . PRO A 1 151 ? 127.692 144.321 98.391  1.00 12.20 ?  151 PRO A C     1 
ATOM   1257  O  O     . PRO A 1 151 ? 126.890 143.397 98.243  1.00 18.95 ?  151 PRO A O     1 
ATOM   1258  C  CB    . PRO A 1 151 ? 126.819 146.546 97.582  1.00 9.11  ?  151 PRO A CB    1 
ATOM   1259  C  CG    . PRO A 1 151 ? 126.303 146.895 96.226  1.00 16.40 ?  151 PRO A CG    1 
ATOM   1260  C  CD    . PRO A 1 151 ? 126.359 145.635 95.423  1.00 19.25 ?  151 PRO A CD    1 
ATOM   1261  N  N     . SER A 1 152 ? 128.490 144.423 99.450  1.00 18.27 ?  152 SER A N     1 
ATOM   1262  C  CA    . SER A 1 152 ? 128.477 143.395 100.476 1.00 13.17 ?  152 SER A CA    1 
ATOM   1263  C  C     . SER A 1 152 ? 127.098 143.305 101.124 1.00 25.07 ?  152 SER A C     1 
ATOM   1264  O  O     . SER A 1 152 ? 126.270 144.214 101.020 1.00 25.53 ?  152 SER A O     1 
ATOM   1265  C  CB    . SER A 1 152 ? 129.544 143.676 101.533 1.00 18.64 ?  152 SER A CB    1 
ATOM   1266  O  OG    . SER A 1 152 ? 129.171 144.761 102.362 1.00 25.88 ?  152 SER A OG    1 
ATOM   1267  N  N     . THR A 1 153 ? 126.856 142.182 101.796 1.00 21.66 ?  153 THR A N     1 
ATOM   1268  C  CA    . THR A 1 153 ? 125.558 141.951 102.426 1.00 18.45 ?  153 THR A CA    1 
ATOM   1269  C  C     . THR A 1 153 ? 125.133 143.092 103.339 1.00 23.18 ?  153 THR A C     1 
ATOM   1270  O  O     . THR A 1 153 ? 123.972 143.521 103.249 1.00 22.84 ?  153 THR A O     1 
ATOM   1271  C  CB    . THR A 1 153 ? 125.595 140.620 103.189 1.00 25.04 ?  153 THR A CB    1 
ATOM   1272  O  OG1   . THR A 1 153 ? 125.677 139.535 102.256 1.00 28.17 ?  153 THR A OG1   1 
ATOM   1273  C  CG2   . THR A 1 153 ? 124.346 140.453 104.038 1.00 23.83 ?  153 THR A CG2   1 
ATOM   1274  N  N     . PRO A 1 154 ? 125.989 143.627 104.213 1.00 28.94 ?  154 PRO A N     1 
ATOM   1275  C  CA    . PRO A 1 154 ? 125.564 144.786 105.018 1.00 23.17 ?  154 PRO A CA    1 
ATOM   1276  C  C     . PRO A 1 154 ? 125.160 145.984 104.177 1.00 21.05 ?  154 PRO A C     1 
ATOM   1277  O  O     . PRO A 1 154 ? 124.057 146.515 104.351 1.00 28.46 ?  154 PRO A O     1 
ATOM   1278  C  CB    . PRO A 1 154 ? 126.799 145.073 105.883 1.00 18.15 ?  154 PRO A CB    1 
ATOM   1279  C  CG    . PRO A 1 154 ? 127.524 143.781 105.942 1.00 18.10 ?  154 PRO A CG    1 
ATOM   1280  C  CD    . PRO A 1 154 ? 127.321 143.141 104.607 1.00 20.40 ?  154 PRO A CD    1 
ATOM   1281  N  N     . THR A 1 155 ? 126.024 146.428 103.262 1.00 20.27 ?  155 THR A N     1 
ATOM   1282  C  CA    . THR A 1 155 ? 125.695 147.582 102.434 1.00 17.95 ?  155 THR A CA    1 
ATOM   1283  C  C     . THR A 1 155 ? 124.458 147.318 101.585 1.00 21.86 ?  155 THR A C     1 
ATOM   1284  O  O     . THR A 1 155 ? 123.557 148.159 101.500 1.00 21.76 ?  155 THR A O     1 
ATOM   1285  C  CB    . THR A 1 155 ? 126.883 147.948 101.542 1.00 18.71 ?  155 THR A CB    1 
ATOM   1286  O  OG1   . THR A 1 155 ? 128.046 148.158 102.352 1.00 24.76 ?  155 THR A OG1   1 
ATOM   1287  C  CG2   . THR A 1 155 ? 126.584 149.210 100.750 1.00 14.02 ?  155 THR A CG2   1 
ATOM   1288  N  N     . PHE A 1 156 ? 124.397 146.148 100.948 1.00 24.71 ?  156 PHE A N     1 
ATOM   1289  C  CA    . PHE A 1 156 ? 123.285 145.856 100.052 1.00 21.16 ?  156 PHE A CA    1 
ATOM   1290  C  C     . PHE A 1 156 ? 121.963 145.793 100.806 1.00 25.46 ?  156 PHE A C     1 
ATOM   1291  O  O     . PHE A 1 156 ? 120.950 146.329 100.343 1.00 31.98 ?  156 PHE A O     1 
ATOM   1292  C  CB    . PHE A 1 156 ? 123.544 144.546 99.309  1.00 22.97 ?  156 PHE A CB    1 
ATOM   1293  C  CG    . PHE A 1 156 ? 122.652 144.340 98.120  1.00 25.02 ?  156 PHE A CG    1 
ATOM   1294  C  CD1   . PHE A 1 156 ? 122.636 145.255 97.084  1.00 21.50 ?  156 PHE A CD1   1 
ATOM   1295  C  CD2   . PHE A 1 156 ? 121.827 143.231 98.042  1.00 24.32 ?  156 PHE A CD2   1 
ATOM   1296  C  CE1   . PHE A 1 156 ? 121.816 145.068 95.990  1.00 22.52 ?  156 PHE A CE1   1 
ATOM   1297  C  CE2   . PHE A 1 156 ? 121.006 143.040 96.951  1.00 19.36 ?  156 PHE A CE2   1 
ATOM   1298  C  CZ    . PHE A 1 156 ? 120.999 143.959 95.924  1.00 19.98 ?  156 PHE A CZ    1 
ATOM   1299  N  N     . LEU A 1 157 ? 121.952 145.141 101.969 1.00 27.84 ?  157 LEU A N     1 
ATOM   1300  C  CA    . LEU A 1 157 ? 120.710 144.965 102.713 1.00 25.53 ?  157 LEU A CA    1 
ATOM   1301  C  C     . LEU A 1 157 ? 120.274 146.252 103.402 1.00 28.18 ?  157 LEU A C     1 
ATOM   1302  O  O     . LEU A 1 157 ? 119.089 146.602 103.378 1.00 36.58 ?  157 LEU A O     1 
ATOM   1303  C  CB    . LEU A 1 157 ? 120.877 143.839 103.734 1.00 30.08 ?  157 LEU A CB    1 
ATOM   1304  C  CG    . LEU A 1 157 ? 119.673 143.497 104.611 1.00 31.40 ?  157 LEU A CG    1 
ATOM   1305  C  CD1   . LEU A 1 157 ? 118.939 142.291 104.059 1.00 32.28 ?  157 LEU A CD1   1 
ATOM   1306  C  CD2   . LEU A 1 157 ? 120.113 143.245 106.043 1.00 28.67 ?  157 LEU A CD2   1 
ATOM   1307  N  N     . ASN A 1 158 ? 121.213 146.973 104.015 1.00 30.35 ?  158 ASN A N     1 
ATOM   1308  C  CA    . ASN A 1 158 ? 120.868 148.086 104.888 1.00 27.14 ?  158 ASN A CA    1 
ATOM   1309  C  C     . ASN A 1 158 ? 120.845 149.437 104.186 1.00 26.55 ?  158 ASN A C     1 
ATOM   1310  O  O     . ASN A 1 158 ? 120.260 150.382 104.723 1.00 34.14 ?  158 ASN A O     1 
ATOM   1311  C  CB    . ASN A 1 158 ? 121.849 148.151 106.062 1.00 27.54 ?  158 ASN A CB    1 
ATOM   1312  C  CG    . ASN A 1 158 ? 121.757 146.939 106.964 1.00 32.01 ?  158 ASN A CG    1 
ATOM   1313  O  OD1   . ASN A 1 158 ? 120.666 146.466 107.277 1.00 34.73 ?  158 ASN A OD1   1 
ATOM   1314  N  ND2   . ASN A 1 158 ? 122.906 146.423 107.381 1.00 34.25 ?  158 ASN A ND2   1 
ATOM   1315  N  N     . ALA A 1 159 ? 121.449 149.554 103.006 1.00 33.54 ?  159 ALA A N     1 
ATOM   1316  C  CA    . ALA A 1 159 ? 121.552 150.856 102.359 1.00 28.33 ?  159 ALA A CA    1 
ATOM   1317  C  C     . ALA A 1 159 ? 120.173 151.469 102.156 1.00 33.48 ?  159 ALA A C     1 
ATOM   1318  O  O     . ALA A 1 159 ? 119.266 150.827 101.621 1.00 38.30 ?  159 ALA A O     1 
ATOM   1319  C  CB    . ALA A 1 159 ? 122.276 150.724 101.020 1.00 30.01 ?  159 ALA A CB    1 
ATOM   1320  N  N     . GLY A 1 160 ? 120.020 152.719 102.588 1.00 41.52 ?  160 GLY A N     1 
ATOM   1321  C  CA    . GLY A 1 160 ? 118.774 153.437 102.425 1.00 37.03 ?  160 GLY A CA    1 
ATOM   1322  C  C     . GLY A 1 160 ? 117.661 153.047 103.369 1.00 37.91 ?  160 GLY A C     1 
ATOM   1323  O  O     . GLY A 1 160 ? 116.523 153.481 103.164 1.00 40.86 ?  160 GLY A O     1 
ATOM   1324  N  N     . ARG A 1 161 ? 117.943 152.251 104.395 1.00 40.22 ?  161 ARG A N     1 
ATOM   1325  C  CA    . ARG A 1 161 ? 116.927 151.769 105.322 1.00 41.75 ?  161 ARG A CA    1 
ATOM   1326  C  C     . ARG A 1 161 ? 117.066 152.479 106.661 1.00 41.16 ?  161 ARG A C     1 
ATOM   1327  O  O     . ARG A 1 161 ? 118.176 152.605 107.189 1.00 44.06 ?  161 ARG A O     1 
ATOM   1328  C  CB    . ARG A 1 161 ? 117.034 150.254 105.516 1.00 35.72 ?  161 ARG A CB    1 
ATOM   1329  C  CG    . ARG A 1 161 ? 116.666 149.444 104.289 1.00 33.73 ?  161 ARG A CG    1 
ATOM   1330  C  CD    . ARG A 1 161 ? 116.385 147.997 104.652 1.00 37.32 ?  161 ARG A CD    1 
ATOM   1331  N  NE    . ARG A 1 161 ? 116.208 147.163 103.470 1.00 42.28 ?  161 ARG A NE    1 
ATOM   1332  C  CZ    . ARG A 1 161 ? 116.047 145.848 103.497 1.00 43.35 ?  161 ARG A CZ    1 
ATOM   1333  N  NH1   . ARG A 1 161 ? 116.012 145.179 104.638 1.00 42.61 1  161 ARG A NH1   1 
ATOM   1334  N  NH2   . ARG A 1 161 ? 115.920 145.186 102.350 1.00 40.13 ?  161 ARG A NH2   1 
ATOM   1335  N  N     . LYS A 1 162 ? 115.938 152.938 107.206 1.00 48.78 ?  162 LYS A N     1 
ATOM   1336  C  CA    . LYS A 1 162 ? 115.964 153.613 108.500 1.00 50.61 ?  162 LYS A CA    1 
ATOM   1337  C  C     . LYS A 1 162 ? 116.385 152.661 109.613 1.00 48.94 ?  162 LYS A C     1 
ATOM   1338  O  O     . LYS A 1 162 ? 117.232 153.002 110.446 1.00 50.65 ?  162 LYS A O     1 
ATOM   1339  C  CB    . LYS A 1 162 ? 114.593 154.220 108.797 1.00 48.62 ?  162 LYS A CB    1 
ATOM   1340  C  CG    . LYS A 1 162 ? 114.624 155.396 109.756 1.00 48.84 ?  162 LYS A CG    1 
ATOM   1341  C  CD    . LYS A 1 162 ? 113.305 156.149 109.734 1.00 50.73 ?  162 LYS A CD    1 
ATOM   1342  C  CE    . LYS A 1 162 ? 113.383 157.370 108.832 1.00 49.89 ?  162 LYS A CE    1 
ATOM   1343  N  NZ    . LYS A 1 162 ? 112.113 157.593 108.087 1.00 51.21 1  162 LYS A NZ    1 
ATOM   1344  N  N     . ARG A 1 163 ? 115.807 151.461 109.640 1.00 47.82 ?  163 ARG A N     1 
ATOM   1345  C  CA    . ARG A 1 163 ? 116.179 150.444 110.615 1.00 48.14 ?  163 ARG A CA    1 
ATOM   1346  C  C     . ARG A 1 163 ? 117.558 149.856 110.348 1.00 52.78 ?  163 ARG A C     1 
ATOM   1347  O  O     . ARG A 1 163 ? 118.083 149.130 111.199 1.00 52.32 ?  163 ARG A O     1 
ATOM   1348  C  CB    . ARG A 1 163 ? 115.127 149.330 110.626 1.00 50.01 ?  163 ARG A CB    1 
ATOM   1349  C  CG    . ARG A 1 163 ? 115.034 148.537 111.924 1.00 52.31 ?  163 ARG A CG    1 
ATOM   1350  C  CD    . ARG A 1 163 ? 116.065 147.420 111.985 1.00 52.82 ?  163 ARG A CD    1 
ATOM   1351  N  NE    . ARG A 1 163 ? 116.301 146.821 110.678 1.00 52.65 ?  163 ARG A NE    1 
ATOM   1352  C  CZ    . ARG A 1 163 ? 117.495 146.482 110.213 1.00 54.50 ?  163 ARG A CZ    1 
ATOM   1353  N  NH1   . ARG A 1 163 ? 118.593 146.668 110.930 1.00 52.21 1  163 ARG A NH1   1 
ATOM   1354  N  NH2   . ARG A 1 163 ? 117.593 145.946 109.000 1.00 52.96 ?  163 ARG A NH2   1 
ATOM   1355  N  N     . ARG A 1 164 ? 118.155 150.169 109.199 1.00 52.20 ?  164 ARG A N     1 
ATOM   1356  C  CA    . ARG A 1 164 ? 119.421 149.572 108.795 1.00 45.55 ?  164 ARG A CA    1 
ATOM   1357  C  C     . ARG A 1 164 ? 120.456 149.635 109.909 1.00 46.04 ?  164 ARG A C     1 
ATOM   1358  O  O     . ARG A 1 164 ? 120.509 150.596 110.681 1.00 49.82 ?  164 ARG A O     1 
ATOM   1359  C  CB    . ARG A 1 164 ? 119.956 150.291 107.556 1.00 46.78 ?  164 ARG A CB    1 
ATOM   1360  C  CG    . ARG A 1 164 ? 120.771 151.540 107.870 1.00 40.97 ?  164 ARG A CG    1 
ATOM   1361  C  CD    . ARG A 1 164 ? 121.538 152.022 106.648 1.00 47.97 ?  164 ARG A CD    1 
ATOM   1362  N  NE    . ARG A 1 164 ? 122.465 153.105 106.955 1.00 48.06 ?  164 ARG A NE    1 
ATOM   1363  C  CZ    . ARG A 1 164 ? 123.467 153.018 107.820 1.00 48.66 ?  164 ARG A CZ    1 
ATOM   1364  N  NH1   . ARG A 1 164 ? 123.697 151.909 108.502 1.00 46.43 1  164 ARG A NH1   1 
ATOM   1365  N  NH2   . ARG A 1 164 ? 124.259 154.070 108.003 1.00 46.01 ?  164 ARG A NH2   1 
ATOM   1366  N  N     . GLY A 1 165 ? 121.279 148.594 109.985 1.00 43.15 ?  165 GLY A N     1 
ATOM   1367  C  CA    . GLY A 1 165 ? 122.467 148.610 110.807 1.00 40.03 ?  165 GLY A CA    1 
ATOM   1368  C  C     . GLY A 1 165 ? 123.629 149.242 110.063 1.00 41.98 ?  165 GLY A C     1 
ATOM   1369  O  O     . GLY A 1 165 ? 123.471 149.892 109.029 1.00 41.83 ?  165 GLY A O     1 
ATOM   1370  N  N     . GLU A 1 166 ? 124.825 149.036 110.607 1.00 38.08 ?  166 GLU A N     1 
ATOM   1371  C  CA    . GLU A 1 166 ? 126.019 149.581 109.980 1.00 34.16 ?  166 GLU A CA    1 
ATOM   1372  C  C     . GLU A 1 166 ? 126.272 148.913 108.633 1.00 34.67 ?  166 GLU A C     1 
ATOM   1373  O  O     . GLU A 1 166 ? 126.100 147.701 108.478 1.00 36.22 ?  166 GLU A O     1 
ATOM   1374  C  CB    . GLU A 1 166 ? 127.232 149.401 110.889 1.00 31.63 ?  166 GLU A CB    1 
ATOM   1375  C  CG    . GLU A 1 166 ? 127.264 150.349 112.074 1.00 37.16 ?  166 GLU A CG    1 
ATOM   1376  C  CD    . GLU A 1 166 ? 127.104 151.800 111.665 1.00 41.47 ?  166 GLU A CD    1 
ATOM   1377  O  OE1   . GLU A 1 166 ? 127.436 152.135 110.509 1.00 44.48 ?  166 GLU A OE1   1 
ATOM   1378  O  OE2   . GLU A 1 166 ? 126.646 152.606 112.501 1.00 36.82 -1 166 GLU A OE2   1 
ATOM   1379  N  N     . LEU A 1 167 ? 126.676 149.719 107.650 1.00 26.17 ?  167 LEU A N     1 
ATOM   1380  C  CA    . LEU A 1 167 ? 127.025 149.188 106.340 1.00 21.40 ?  167 LEU A CA    1 
ATOM   1381  C  C     . LEU A 1 167 ? 128.367 148.469 106.347 1.00 28.61 ?  167 LEU A C     1 
ATOM   1382  O  O     . LEU A 1 167 ? 128.632 147.668 105.444 1.00 26.45 ?  167 LEU A O     1 
ATOM   1383  C  CB    . LEU A 1 167 ? 127.041 150.313 105.305 1.00 22.39 ?  167 LEU A CB    1 
ATOM   1384  C  CG    . LEU A 1 167 ? 125.706 151.020 105.065 1.00 25.66 ?  167 LEU A CG    1 
ATOM   1385  C  CD1   . LEU A 1 167 ? 125.624 151.541 103.642 1.00 25.14 ?  167 LEU A CD1   1 
ATOM   1386  C  CD2   . LEU A 1 167 ? 124.543 150.091 105.366 1.00 24.98 ?  167 LEU A CD2   1 
ATOM   1387  N  N     . VAL A 1 168 ? 129.210 148.737 107.338 1.00 28.00 ?  168 VAL A N     1 
ATOM   1388  C  CA    . VAL A 1 168 ? 130.460 148.017 107.546 1.00 21.08 ?  168 VAL A CA    1 
ATOM   1389  C  C     . VAL A 1 168 ? 130.193 146.878 108.516 1.00 24.86 ?  168 VAL A C     1 
ATOM   1390  O  O     . VAL A 1 168 ? 129.440 147.037 109.485 1.00 30.29 ?  168 VAL A O     1 
ATOM   1391  C  CB    . VAL A 1 168 ? 131.562 148.954 108.076 1.00 24.72 ?  168 VAL A CB    1 
ATOM   1392  C  CG1   . VAL A 1 168 ? 132.857 148.189 108.288 1.00 24.42 ?  168 VAL A CG1   1 
ATOM   1393  C  CG2   . VAL A 1 168 ? 131.773 150.117 107.119 1.00 30.28 ?  168 VAL A CG2   1 
ATOM   1394  N  N     . SER A 1 169 ? 130.803 145.724 108.260 1.00 25.77 ?  169 SER A N     1 
ATOM   1395  C  CA    . SER A 1 169 ? 130.563 144.538 109.069 1.00 21.85 ?  169 SER A CA    1 
ATOM   1396  C  C     . SER A 1 169 ? 131.834 143.879 109.584 1.00 16.36 ?  169 SER A C     1 
ATOM   1397  O  O     . SER A 1 169 ? 131.743 142.949 110.392 1.00 23.91 ?  169 SER A O     1 
ATOM   1398  C  CB    . SER A 1 169 ? 129.745 143.512 108.272 1.00 25.12 ?  169 SER A CB    1 
ATOM   1399  O  OG    . SER A 1 169 ? 129.538 142.331 109.025 1.00 32.55 ?  169 SER A OG    1 
ATOM   1400  N  N     . CYS A 1 170 ? 133.009 144.324 109.148 1.00 20.89 ?  170 CYS A N     1 
ATOM   1401  C  CA    . CYS A 1 170 ? 134.279 143.748 109.572 1.00 15.50 ?  170 CYS A CA    1 
ATOM   1402  C  C     . CYS A 1 170 ? 134.988 144.740 110.483 1.00 15.65 ?  170 CYS A C     1 
ATOM   1403  O  O     . CYS A 1 170 ? 135.215 145.890 110.095 1.00 19.52 ?  170 CYS A O     1 
ATOM   1404  C  CB    . CYS A 1 170 ? 135.155 143.401 108.367 1.00 21.76 ?  170 CYS A CB    1 
ATOM   1405  S  SG    . CYS A 1 170 ? 134.580 141.983 107.404 1.00 51.87 ?  170 CYS A SG    1 
ATOM   1406  N  N     . PHE A 1 171 ? 135.333 144.294 111.688 1.00 18.48 ?  171 PHE A N     1 
ATOM   1407  C  CA    . PHE A 1 171 ? 136.003 145.145 112.663 1.00 13.00 ?  171 PHE A CA    1 
ATOM   1408  C  C     . PHE A 1 171 ? 137.171 144.393 113.277 1.00 1.67  ?  171 PHE A C     1 
ATOM   1409  O  O     . PHE A 1 171 ? 137.038 143.222 113.642 1.00 18.41 ?  171 PHE A O     1 
ATOM   1410  C  CB    . PHE A 1 171 ? 135.036 145.601 113.760 1.00 16.80 ?  171 PHE A CB    1 
ATOM   1411  C  CG    . PHE A 1 171 ? 133.829 146.321 113.241 1.00 13.33 ?  171 PHE A CG    1 
ATOM   1412  C  CD1   . PHE A 1 171 ? 133.933 147.612 112.753 1.00 8.43  ?  171 PHE A CD1   1 
ATOM   1413  C  CD2   . PHE A 1 171 ? 132.589 145.707 113.237 1.00 11.33 ?  171 PHE A CD2   1 
ATOM   1414  C  CE1   . PHE A 1 171 ? 132.825 148.276 112.274 1.00 9.30  ?  171 PHE A CE1   1 
ATOM   1415  C  CE2   . PHE A 1 171 ? 131.477 146.366 112.757 1.00 9.30  ?  171 PHE A CE2   1 
ATOM   1416  C  CZ    . PHE A 1 171 ? 131.595 147.653 112.276 1.00 9.33  ?  171 PHE A CZ    1 
ATOM   1417  N  N     . LEU A 1 172 ? 138.309 145.070 113.391 1.00 15.02 ?  172 LEU A N     1 
ATOM   1418  C  CA    . LEU A 1 172 ? 139.487 144.543 114.065 1.00 8.01  ?  172 LEU A CA    1 
ATOM   1419  C  C     . LEU A 1 172 ? 139.855 145.483 115.201 1.00 5.20  ?  172 LEU A C     1 
ATOM   1420  O  O     . LEU A 1 172 ? 139.970 146.694 114.994 1.00 14.37 ?  172 LEU A O     1 
ATOM   1421  C  CB    . LEU A 1 172 ? 140.663 144.387 113.098 1.00 10.01 ?  172 LEU A CB    1 
ATOM   1422  C  CG    . LEU A 1 172 ? 140.562 143.271 112.057 1.00 2.63  ?  172 LEU A CG    1 
ATOM   1423  C  CD1   . LEU A 1 172 ? 139.559 143.630 110.976 1.00 8.28  ?  172 LEU A CD1   1 
ATOM   1424  C  CD2   . LEU A 1 172 ? 141.923 142.986 111.454 1.00 7.58  ?  172 LEU A CD2   1 
ATOM   1425  N  N     . LEU A 1 173 ? 140.036 144.929 116.396 1.00 20.17 ?  173 LEU A N     1 
ATOM   1426  C  CA    . LEU A 1 173 ? 140.337 145.712 117.586 1.00 7.81  ?  173 LEU A CA    1 
ATOM   1427  C  C     . LEU A 1 173 ? 141.664 145.266 118.178 1.00 0.13  ?  173 LEU A C     1 
ATOM   1428  O  O     . LEU A 1 173 ? 141.912 144.065 118.326 1.00 17.25 ?  173 LEU A O     1 
ATOM   1429  C  CB    . LEU A 1 173 ? 139.226 145.577 118.632 1.00 14.81 ?  173 LEU A CB    1 
ATOM   1430  C  CG    . LEU A 1 173 ? 137.790 145.837 118.175 1.00 19.18 ?  173 LEU A CG    1 
ATOM   1431  C  CD1   . LEU A 1 173 ? 136.820 145.605 119.325 1.00 21.83 ?  173 LEU A CD1   1 
ATOM   1432  C  CD2   . LEU A 1 173 ? 137.648 147.243 117.618 1.00 7.96  ?  173 LEU A CD2   1 
ATOM   1433  N  N     . GLU A 1 174 ? 142.514 146.233 118.505 1.00 19.13 ?  174 GLU A N     1 
ATOM   1434  C  CA    . GLU A 1 174 ? 143.724 145.981 119.272 1.00 19.22 ?  174 GLU A CA    1 
ATOM   1435  C  C     . GLU A 1 174 ? 143.405 146.124 120.755 1.00 13.79 ?  174 GLU A C     1 
ATOM   1436  O  O     . GLU A 1 174 ? 142.764 147.095 121.166 1.00 22.95 ?  174 GLU A O     1 
ATOM   1437  C  CB    . GLU A 1 174 ? 144.835 146.951 118.874 1.00 19.12 ?  174 GLU A CB    1 
ATOM   1438  C  CG    . GLU A 1 174 ? 145.327 146.796 117.447 1.00 12.28 ?  174 GLU A CG    1 
ATOM   1439  C  CD    . GLU A 1 174 ? 146.715 146.195 117.373 1.00 21.52 ?  174 GLU A CD    1 
ATOM   1440  O  OE1   . GLU A 1 174 ? 146.830 144.955 117.441 1.00 31.40 ?  174 GLU A OE1   1 
ATOM   1441  O  OE2   . GLU A 1 174 ? 147.692 146.963 117.250 1.00 24.80 -1 174 GLU A OE2   1 
ATOM   1442  N  N     . VAL A 1 175 ? 143.848 145.157 121.552 1.00 15.11 ?  175 VAL A N     1 
ATOM   1443  C  CA    . VAL A 1 175 ? 143.605 145.148 122.989 1.00 16.57 ?  175 VAL A CA    1 
ATOM   1444  C  C     . VAL A 1 175 ? 144.932 145.380 123.695 1.00 15.15 ?  175 VAL A C     1 
ATOM   1445  O  O     . VAL A 1 175 ? 145.892 144.625 123.494 1.00 22.59 ?  175 VAL A O     1 
ATOM   1446  C  CB    . VAL A 1 175 ? 142.958 143.834 123.449 1.00 17.30 ?  175 VAL A CB    1 
ATOM   1447  C  CG1   . VAL A 1 175 ? 142.476 143.957 124.888 1.00 8.95  ?  175 VAL A CG1   1 
ATOM   1448  C  CG2   . VAL A 1 175 ? 141.813 143.455 122.525 1.00 14.40 ?  175 VAL A CG2   1 
ATOM   1449  N  N     . ASN A 1 176 ? 144.987 146.421 124.518 1.00 16.81 ?  176 ASN A N     1 
ATOM   1450  C  CA    . ASN A 1 176 ? 146.179 146.709 125.296 1.00 17.31 ?  176 ASN A CA    1 
ATOM   1451  C  C     . ASN A 1 176 ? 146.171 145.903 126.593 1.00 24.13 ?  176 ASN A C     1 
ATOM   1452  O  O     . ASN A 1 176 ? 145.127 145.456 127.075 1.00 19.69 ?  176 ASN A O     1 
ATOM   1453  C  CB    . ASN A 1 176 ? 146.277 148.204 125.593 1.00 13.84 ?  176 ASN A CB    1 
ATOM   1454  C  CG    . ASN A 1 176 ? 147.688 148.731 125.466 1.00 16.03 ?  176 ASN A CG    1 
ATOM   1455  O  OD1   . ASN A 1 176 ? 148.648 147.964 125.424 1.00 25.03 ?  176 ASN A OD1   1 
ATOM   1456  N  ND2   . ASN A 1 176 ? 147.823 150.048 125.403 1.00 14.07 ?  176 ASN A ND2   1 
ATOM   1457  N  N     . ASP A 1 177 ? 147.364 145.724 127.162 1.00 26.03 ?  177 ASP A N     1 
ATOM   1458  C  CA    . ASP A 1 177 ? 147.556 144.843 128.314 1.00 21.59 ?  177 ASP A CA    1 
ATOM   1459  C  C     . ASP A 1 177 ? 147.226 145.602 129.598 1.00 20.79 ?  177 ASP A C     1 
ATOM   1460  O  O     . ASP A 1 177 ? 148.099 146.040 130.351 1.00 28.07 ?  177 ASP A O     1 
ATOM   1461  C  CB    . ASP A 1 177 ? 148.978 144.298 128.333 1.00 12.52 ?  177 ASP A CB    1 
ATOM   1462  C  CG    . ASP A 1 177 ? 149.185 143.249 129.406 1.00 22.16 ?  177 ASP A CG    1 
ATOM   1463  O  OD1   . ASP A 1 177 ? 148.272 142.426 129.619 1.00 23.72 ?  177 ASP A OD1   1 
ATOM   1464  O  OD2   . ASP A 1 177 ? 150.266 143.246 130.028 1.00 26.54 -1 177 ASP A OD2   1 
ATOM   1465  N  N     . SER A 1 178 ? 145.929 145.750 129.852 1.00 22.22 ?  178 SER A N     1 
ATOM   1466  C  CA    . SER A 1 178 ? 145.468 146.397 131.071 1.00 16.63 ?  178 SER A CA    1 
ATOM   1467  C  C     . SER A 1 178 ? 143.991 146.091 131.262 1.00 17.50 ?  178 SER A C     1 
ATOM   1468  O  O     . SER A 1 178 ? 143.267 145.811 130.304 1.00 27.24 ?  178 SER A O     1 
ATOM   1469  C  CB    . SER A 1 178 ? 145.712 147.908 131.032 1.00 15.95 ?  178 SER A CB    1 
ATOM   1470  O  OG    . SER A 1 178 ? 144.614 148.593 130.461 1.00 20.77 ?  178 SER A OG    1 
ATOM   1471  N  N     . LEU A 1 179 ? 143.554 146.148 132.522 1.00 22.15 ?  179 LEU A N     1 
ATOM   1472  C  CA    . LEU A 1 179 ? 142.149 145.894 132.827 1.00 14.10 ?  179 LEU A CA    1 
ATOM   1473  C  C     . LEU A 1 179 ? 141.248 146.930 132.170 1.00 16.79 ?  179 LEU A C     1 
ATOM   1474  O  O     . LEU A 1 179 ? 140.170 146.595 131.668 1.00 21.89 ?  179 LEU A O     1 
ATOM   1475  C  CB    . LEU A 1 179 ? 141.930 145.876 134.338 1.00 21.44 ?  179 LEU A CB    1 
ATOM   1476  C  CG    . LEU A 1 179 ? 140.511 145.522 134.791 1.00 21.18 ?  179 LEU A CG    1 
ATOM   1477  C  CD1   . LEU A 1 179 ? 140.191 144.069 134.477 1.00 16.78 ?  179 LEU A CD1   1 
ATOM   1478  C  CD2   . LEU A 1 179 ? 140.327 145.811 136.272 1.00 18.66 ?  179 LEU A CD2   1 
ATOM   1479  N  N     . ASN A 1 180 ? 141.665 148.196 132.175 1.00 21.01 ?  180 ASN A N     1 
ATOM   1480  C  CA    . ASN A 1 180 ? 140.885 149.230 131.504 1.00 16.97 ?  180 ASN A CA    1 
ATOM   1481  C  C     . ASN A 1 180 ? 140.731 148.912 130.024 1.00 16.44 ?  180 ASN A C     1 
ATOM   1482  O  O     . ASN A 1 180 ? 139.632 149.006 129.463 1.00 29.16 ?  180 ASN A O     1 
ATOM   1483  C  CB    . ASN A 1 180 ? 141.552 150.593 131.690 1.00 19.64 ?  180 ASN A CB    1 
ATOM   1484  C  CG    . ASN A 1 180 ? 141.333 151.167 133.072 1.00 18.06 ?  180 ASN A CG    1 
ATOM   1485  O  OD1   . ASN A 1 180 ? 140.427 150.750 133.794 1.00 29.57 ?  180 ASN A OD1   1 
ATOM   1486  N  ND2   . ASN A 1 180 ? 142.168 152.123 133.453 1.00 17.19 ?  180 ASN A ND2   1 
ATOM   1487  N  N     . ASP A 1 181 ? 141.828 148.516 129.379 1.00 19.89 ?  181 ASP A N     1 
ATOM   1488  C  CA    . ASP A 1 181 ? 141.783 148.199 127.957 1.00 9.81  ?  181 ASP A CA    1 
ATOM   1489  C  C     . ASP A 1 181 ? 140.956 146.948 127.691 1.00 15.38 ?  181 ASP A C     1 
ATOM   1490  O  O     . ASP A 1 181 ? 140.244 146.877 126.687 1.00 23.66 ?  181 ASP A O     1 
ATOM   1491  C  CB    . ASP A 1 181 ? 143.202 148.045 127.417 1.00 14.61 ?  181 ASP A CB    1 
ATOM   1492  C  CG    . ASP A 1 181 ? 143.926 149.373 127.311 1.00 28.54 ?  181 ASP A CG    1 
ATOM   1493  O  OD1   . ASP A 1 181 ? 143.470 150.238 126.536 1.00 23.68 ?  181 ASP A OD1   1 
ATOM   1494  O  OD2   . ASP A 1 181 ? 144.950 149.554 128.001 1.00 29.30 -1 181 ASP A OD2   1 
ATOM   1495  N  N     . ILE A 1 182 ? 141.026 145.953 128.577 1.00 16.53 ?  182 ILE A N     1 
ATOM   1496  C  CA    . ILE A 1 182 ? 140.236 144.740 128.390 1.00 15.50 ?  182 ILE A CA    1 
ATOM   1497  C  C     . ILE A 1 182 ? 138.748 145.038 128.532 1.00 16.91 ?  182 ILE A C     1 
ATOM   1498  O  O     . ILE A 1 182 ? 137.922 144.542 127.754 1.00 26.13 ?  182 ILE A O     1 
ATOM   1499  C  CB    . ILE A 1 182 ? 140.695 143.649 129.374 1.00 21.71 ?  182 ILE A CB    1 
ATOM   1500  C  CG1   . ILE A 1 182 ? 141.990 143.002 128.881 1.00 14.32 ?  182 ILE A CG1   1 
ATOM   1501  C  CG2   . ILE A 1 182 ? 139.605 142.604 129.561 1.00 18.95 ?  182 ILE A CG2   1 
ATOM   1502  C  CD1   . ILE A 1 182 ? 142.737 142.245 129.949 1.00 16.86 ?  182 ILE A CD1   1 
ATOM   1503  N  N     . SER A 1 183 ? 138.380 145.846 129.528 1.00 21.80 ?  183 SER A N     1 
ATOM   1504  C  CA    . SER A 1 183 ? 136.983 146.238 129.687 1.00 12.50 ?  183 SER A CA    1 
ATOM   1505  C  C     . SER A 1 183 ? 136.500 147.037 128.485 1.00 17.20 ?  183 SER A C     1 
ATOM   1506  O  O     . SER A 1 183 ? 135.388 146.819 127.988 1.00 21.49 ?  183 SER A O     1 
ATOM   1507  C  CB    . SER A 1 183 ? 136.810 147.042 130.975 1.00 14.47 ?  183 SER A CB    1 
ATOM   1508  O  OG    . SER A 1 183 ? 136.869 146.202 132.112 1.00 29.38 ?  183 SER A OG    1 
ATOM   1509  N  N     . ARG A 1 184 ? 137.322 147.973 128.005 1.00 19.90 ?  184 ARG A N     1 
ATOM   1510  C  CA    . ARG A 1 184 ? 136.945 148.741 126.825 1.00 17.12 ?  184 ARG A CA    1 
ATOM   1511  C  C     . ARG A 1 184 ? 136.802 147.839 125.607 1.00 16.10 ?  184 ARG A C     1 
ATOM   1512  O  O     . ARG A 1 184 ? 135.917 148.047 124.774 1.00 25.00 ?  184 ARG A O     1 
ATOM   1513  C  CB    . ARG A 1 184 ? 137.969 149.843 126.564 1.00 14.11 ?  184 ARG A CB    1 
ATOM   1514  C  CG    . ARG A 1 184 ? 137.571 150.789 125.451 1.00 22.46 ?  184 ARG A CG    1 
ATOM   1515  C  CD    . ARG A 1 184 ? 136.173 151.329 125.674 1.00 18.83 ?  184 ARG A CD    1 
ATOM   1516  N  NE    . ARG A 1 184 ? 136.118 152.230 126.817 1.00 27.26 ?  184 ARG A NE    1 
ATOM   1517  C  CZ    . ARG A 1 184 ? 135.084 153.007 127.110 1.00 30.15 ?  184 ARG A CZ    1 
ATOM   1518  N  NH1   . ARG A 1 184 ? 133.981 152.993 126.382 1.00 21.33 1  184 ARG A NH1   1 
ATOM   1519  N  NH2   . ARG A 1 184 ? 135.160 153.816 128.162 1.00 24.47 ?  184 ARG A NH2   1 
ATOM   1520  N  N     . ALA A 1 185 ? 137.673 146.837 125.481 1.00 20.72 ?  185 ALA A N     1 
ATOM   1521  C  CA    . ALA A 1 185 ? 137.574 145.902 124.366 1.00 17.33 ?  185 ALA A CA    1 
ATOM   1522  C  C     . ALA A 1 185 ? 136.283 145.102 124.434 1.00 22.17 ?  185 ALA A C     1 
ATOM   1523  O  O     . ALA A 1 185 ? 135.620 144.900 123.414 1.00 25.69 ?  185 ALA A O     1 
ATOM   1524  C  CB    . ALA A 1 185 ? 138.782 144.969 124.355 1.00 10.98 ?  185 ALA A CB    1 
ATOM   1525  N  N     . ILE A 1 186 ? 135.914 144.634 125.627 1.00 16.78 ?  186 ILE A N     1 
ATOM   1526  C  CA    . ILE A 1 186 ? 134.652 143.912 125.781 1.00 13.99 ?  186 ILE A CA    1 
ATOM   1527  C  C     . ILE A 1 186 ? 133.483 144.811 125.396 1.00 14.20 ?  186 ILE A C     1 
ATOM   1528  O  O     . ILE A 1 186 ? 132.571 144.403 124.662 1.00 20.87 ?  186 ILE A O     1 
ATOM   1529  C  CB    . ILE A 1 186 ? 134.506 143.384 127.219 1.00 22.90 ?  186 ILE A CB    1 
ATOM   1530  C  CG1   . ILE A 1 186 ? 135.458 142.213 127.464 1.00 21.76 ?  186 ILE A CG1   1 
ATOM   1531  C  CG2   . ILE A 1 186 ? 133.069 142.969 127.495 1.00 17.35 ?  186 ILE A CG2   1 
ATOM   1532  C  CD1   . ILE A 1 186 ? 135.706 141.931 128.926 1.00 18.47 ?  186 ILE A CD1   1 
ATOM   1533  N  N     . ASP A 1 187 ? 133.501 146.054 125.879 1.00 21.72 ?  187 ASP A N     1 
ATOM   1534  C  CA    . ASP A 1 187 ? 132.422 146.987 125.576 1.00 12.41 ?  187 ASP A CA    1 
ATOM   1535  C  C     . ASP A 1 187 ? 132.324 147.250 124.079 1.00 22.18 ?  187 ASP A C     1 
ATOM   1536  O  O     . ASP A 1 187 ? 131.230 147.248 123.506 1.00 22.42 ?  187 ASP A O     1 
ATOM   1537  C  CB    . ASP A 1 187 ? 132.632 148.294 126.340 1.00 14.31 ?  187 ASP A CB    1 
ATOM   1538  C  CG    . ASP A 1 187 ? 131.749 149.417 125.829 1.00 28.20 ?  187 ASP A CG    1 
ATOM   1539  O  OD1   . ASP A 1 187 ? 130.528 149.199 125.685 1.00 33.73 ?  187 ASP A OD1   1 
ATOM   1540  O  OD2   . ASP A 1 187 ? 132.277 150.519 125.574 1.00 31.72 -1 187 ASP A OD2   1 
ATOM   1541  N  N     . ILE A 1 188 ? 133.465 147.480 123.427 1.00 19.20 ?  188 ILE A N     1 
ATOM   1542  C  CA    . ILE A 1 188 ? 133.465 147.791 122.002 1.00 14.95 ?  188 ILE A CA    1 
ATOM   1543  C  C     . ILE A 1 188 ? 133.041 146.577 121.188 1.00 17.40 ?  188 ILE A C     1 
ATOM   1544  O  O     . ILE A 1 188 ? 132.342 146.705 120.179 1.00 24.57 ?  188 ILE A O     1 
ATOM   1545  C  CB    . ILE A 1 188 ? 134.848 148.309 121.567 1.00 20.96 ?  188 ILE A CB    1 
ATOM   1546  C  CG1   . ILE A 1 188 ? 135.175 149.619 122.285 1.00 19.72 ?  188 ILE A CG1   1 
ATOM   1547  C  CG2   . ILE A 1 188 ? 134.896 148.496 120.061 1.00 16.78 ?  188 ILE A CG2   1 
ATOM   1548  C  CD1   . ILE A 1 188 ? 136.587 150.104 122.060 1.00 14.56 ?  188 ILE A CD1   1 
ATOM   1549  N  N     . SER A 1 189 ? 133.463 145.382 121.604 1.00 16.77 ?  189 SER A N     1 
ATOM   1550  C  CA    . SER A 1 189 ? 133.032 144.170 120.921 1.00 11.88 ?  189 SER A CA    1 
ATOM   1551  C  C     . SER A 1 189 ? 131.523 144.007 121.009 1.00 18.36 ?  189 SER A C     1 
ATOM   1552  O  O     . SER A 1 189 ? 130.869 143.682 120.013 1.00 23.10 ?  189 SER A O     1 
ATOM   1553  C  CB    . SER A 1 189 ? 133.738 142.953 121.514 1.00 14.70 ?  189 SER A CB    1 
ATOM   1554  O  OG    . SER A 1 189 ? 135.144 143.096 121.454 1.00 26.80 ?  189 SER A OG    1 
ATOM   1555  N  N     . MET A 1 190 ? 130.951 144.230 122.195 1.00 23.28 ?  190 MET A N     1 
ATOM   1556  C  CA    . MET A 1 190 ? 129.500 144.142 122.329 1.00 15.47 ?  190 MET A CA    1 
ATOM   1557  C  C     . MET A 1 190 ? 128.804 145.213 121.497 1.00 14.64 ?  190 MET A C     1 
ATOM   1558  O  O     . MET A 1 190 ? 127.775 144.948 120.867 1.00 24.52 ?  190 MET A O     1 
ATOM   1559  C  CB    . MET A 1 190 ? 129.102 144.251 123.801 1.00 18.04 ?  190 MET A CB    1 
ATOM   1560  C  CG    . MET A 1 190 ? 129.427 143.011 124.618 1.00 21.51 ?  190 MET A CG    1 
ATOM   1561  S  SD    . MET A 1 190 ? 128.586 142.976 126.210 1.00 31.52 ?  190 MET A SD    1 
ATOM   1562  C  CE    . MET A 1 190 ? 129.102 144.548 126.894 1.00 23.05 ?  190 MET A CE    1 
ATOM   1563  N  N     . GLN A 1 191 ? 129.360 146.425 121.472 1.00 19.73 ?  191 GLN A N     1 
ATOM   1564  C  CA    . GLN A 1 191 ? 128.758 147.505 120.697 1.00 14.63 ?  191 GLN A CA    1 
ATOM   1565  C  C     . GLN A 1 191 ? 128.765 147.190 119.206 1.00 19.24 ?  191 GLN A C     1 
ATOM   1566  O  O     . GLN A 1 191 ? 127.782 147.453 118.503 1.00 24.70 ?  191 GLN A O     1 
ATOM   1567  C  CB    . GLN A 1 191 ? 129.499 148.815 120.966 1.00 17.25 ?  191 GLN A CB    1 
ATOM   1568  C  CG    . GLN A 1 191 ? 129.374 149.334 122.387 1.00 18.81 ?  191 GLN A CG    1 
ATOM   1569  C  CD    . GLN A 1 191 ? 127.989 149.862 122.699 1.00 21.53 ?  191 GLN A CD    1 
ATOM   1570  O  OE1   . GLN A 1 191 ? 127.209 150.161 121.796 1.00 24.01 ?  191 GLN A OE1   1 
ATOM   1571  N  NE2   . GLN A 1 191 ? 127.677 149.984 123.982 1.00 17.88 ?  191 GLN A NE2   1 
ATOM   1572  N  N     . LEU A 1 192 ? 129.868 146.635 118.703 1.00 22.40 ?  192 LEU A N     1 
ATOM   1573  C  CA    . LEU A 1 192 ? 129.981 146.348 117.278 1.00 12.07 ?  192 LEU A CA    1 
ATOM   1574  C  C     . LEU A 1 192 ? 129.171 145.119 116.888 1.00 20.22 ?  192 LEU A C     1 
ATOM   1575  O  O     . LEU A 1 192 ? 128.588 145.081 115.799 1.00 27.28 ?  192 LEU A O     1 
ATOM   1576  C  CB    . LEU A 1 192 ? 131.449 146.171 116.894 1.00 17.80 ?  192 LEU A CB    1 
ATOM   1577  C  CG    . LEU A 1 192 ? 132.304 147.439 116.950 1.00 16.27 ?  192 LEU A CG    1 
ATOM   1578  C  CD1   . LEU A 1 192 ? 133.779 147.103 116.827 1.00 16.26 ?  192 LEU A CD1   1 
ATOM   1579  C  CD2   . LEU A 1 192 ? 131.882 148.424 115.872 1.00 12.37 ?  192 LEU A CD2   1 
ATOM   1580  N  N     . SER A 1 193 ? 129.123 144.104 117.754 1.00 14.29 ?  193 SER A N     1 
ATOM   1581  C  CA    . SER A 1 193 ? 128.249 142.965 117.501 1.00 17.27 ?  193 SER A CA    1 
ATOM   1582  C  C     . SER A 1 193 ? 126.791 143.396 117.486 1.00 27.53 ?  193 SER A C     1 
ATOM   1583  O  O     . SER A 1 193 ? 126.001 142.919 116.665 1.00 34.38 ?  193 SER A O     1 
ATOM   1584  C  CB    . SER A 1 193 ? 128.478 141.881 118.552 1.00 21.56 ?  193 SER A CB    1 
ATOM   1585  O  OG    . SER A 1 193 ? 129.776 141.327 118.438 1.00 35.11 ?  193 SER A OG    1 
ATOM   1586  N  N     . LYS A 1 194 ? 126.417 144.305 118.390 1.00 24.70 ?  194 LYS A N     1 
ATOM   1587  C  CA    . LYS A 1 194 ? 125.069 144.861 118.377 1.00 23.74 ?  194 LYS A CA    1 
ATOM   1588  C  C     . LYS A 1 194 ? 124.729 145.432 117.007 1.00 24.84 ?  194 LYS A C     1 
ATOM   1589  O  O     . LYS A 1 194 ? 123.582 145.347 116.556 1.00 30.70 ?  194 LYS A O     1 
ATOM   1590  C  CB    . LYS A 1 194 ? 124.948 145.933 119.463 1.00 22.38 ?  194 LYS A CB    1 
ATOM   1591  C  CG    . LYS A 1 194 ? 123.669 146.739 119.424 1.00 22.18 ?  194 LYS A CG    1 
ATOM   1592  C  CD    . LYS A 1 194 ? 123.706 147.850 120.459 1.00 27.87 ?  194 LYS A CD    1 
ATOM   1593  C  CE    . LYS A 1 194 ? 122.379 148.587 120.540 1.00 29.10 ?  194 LYS A CE    1 
ATOM   1594  N  NZ    . LYS A 1 194 ? 122.400 149.636 121.595 1.00 27.13 1  194 LYS A NZ    1 
ATOM   1595  N  N     . LEU A 1 195 ? 125.717 146.013 116.329 1.00 26.31 ?  195 LEU A N     1 
ATOM   1596  C  CA    . LEU A 1 195 ? 125.534 146.514 114.974 1.00 24.51 ?  195 LEU A CA    1 
ATOM   1597  C  C     . LEU A 1 195 ? 125.544 145.409 113.928 1.00 21.78 ?  195 LEU A C     1 
ATOM   1598  O  O     . LEU A 1 195 ? 125.292 145.691 112.753 1.00 29.53 ?  195 LEU A O     1 
ATOM   1599  C  CB    . LEU A 1 195 ? 126.620 147.542 114.648 1.00 26.92 ?  195 LEU A CB    1 
ATOM   1600  C  CG    . LEU A 1 195 ? 126.641 148.783 115.541 1.00 31.21 ?  195 LEU A CG    1 
ATOM   1601  C  CD1   . LEU A 1 195 ? 127.839 149.661 115.216 1.00 22.94 ?  195 LEU A CD1   1 
ATOM   1602  C  CD2   . LEU A 1 195 ? 125.343 149.561 115.400 1.00 24.81 ?  195 LEU A CD2   1 
ATOM   1603  N  N     . GLY A 1 196 ? 125.832 144.170 114.320 1.00 24.13 ?  196 GLY A N     1 
ATOM   1604  C  CA    . GLY A 1 196 ? 125.826 143.049 113.407 1.00 20.02 ?  196 GLY A CA    1 
ATOM   1605  C  C     . GLY A 1 196 ? 127.140 142.757 112.719 1.00 26.63 ?  196 GLY A C     1 
ATOM   1606  O  O     . GLY A 1 196 ? 127.200 141.825 111.906 1.00 30.27 ?  196 GLY A O     1 
ATOM   1607  N  N     . GLY A 1 197 ? 128.194 143.513 113.013 1.00 23.62 ?  197 GLY A N     1 
ATOM   1608  C  CA    . GLY A 1 197 ? 129.483 143.298 112.381 1.00 17.26 ?  197 GLY A CA    1 
ATOM   1609  C  C     . GLY A 1 197 ? 130.338 142.301 113.147 1.00 17.42 ?  197 GLY A C     1 
ATOM   1610  O  O     . GLY A 1 197 ? 130.309 142.247 114.374 1.00 22.64 ?  197 GLY A O     1 
ATOM   1611  N  N     . GLY A 1 198 ? 131.094 141.504 112.397 1.00 12.64 ?  198 GLY A N     1 
ATOM   1612  C  CA    . GLY A 1 198 ? 132.043 140.598 113.018 1.00 6.08  ?  198 GLY A CA    1 
ATOM   1613  C  C     . GLY A 1 198 ? 133.225 141.360 113.590 1.00 9.69  ?  198 GLY A C     1 
ATOM   1614  O  O     . GLY A 1 198 ? 133.754 142.286 112.972 1.00 18.78 ?  198 GLY A O     1 
ATOM   1615  N  N     . VAL A 1 199 ? 133.636 140.968 114.791 1.00 12.61 ?  199 VAL A N     1 
ATOM   1616  C  CA    . VAL A 1 199 ? 134.684 141.659 115.530 1.00 8.78  ?  199 VAL A CA    1 
ATOM   1617  C  C     . VAL A 1 199 ? 135.841 140.700 115.754 1.00 5.93  ?  199 VAL A C     1 
ATOM   1618  O  O     . VAL A 1 199 ? 135.649 139.596 116.274 1.00 19.57 ?  199 VAL A O     1 
ATOM   1619  C  CB    . VAL A 1 199 ? 134.166 142.211 116.870 1.00 11.11 ?  199 VAL A CB    1 
ATOM   1620  C  CG1   . VAL A 1 199 ? 135.275 142.945 117.604 1.00 15.89 ?  199 VAL A CG1   1 
ATOM   1621  C  CG2   . VAL A 1 199 ? 132.973 143.126 116.639 1.00 6.05  ?  199 VAL A CG2   1 
ATOM   1622  N  N     . SER A 1 200 ? 137.039 141.126 115.366 1.00 5.43  ?  200 SER A N     1 
ATOM   1623  C  CA    . SER A 1 200 ? 138.263 140.366 115.571 1.00 0.79  ?  200 SER A CA    1 
ATOM   1624  C  C     . SER A 1 200 ? 139.169 141.141 116.515 1.00 11.34 ?  200 SER A C     1 
ATOM   1625  O  O     . SER A 1 200 ? 139.367 142.349 116.340 1.00 21.76 ?  200 SER A O     1 
ATOM   1626  C  CB    . SER A 1 200 ? 138.977 140.100 114.244 1.00 6.10  ?  200 SER A CB    1 
ATOM   1627  O  OG    . SER A 1 200 ? 139.953 139.086 114.389 1.00 12.10 ?  200 SER A OG    1 
ATOM   1628  N  N     . LEU A 1 201 ? 139.714 140.453 117.513 1.00 4.10  ?  201 LEU A N     1 
ATOM   1629  C  CA    . LEU A 1 201 ? 140.555 141.069 118.526 1.00 8.50  ?  201 LEU A CA    1 
ATOM   1630  C  C     . LEU A 1 201 ? 141.946 140.453 118.495 1.00 6.58  ?  201 LEU A C     1 
ATOM   1631  O  O     . LEU A 1 201 ? 142.100 139.251 118.258 1.00 10.13 ?  201 LEU A O     1 
ATOM   1632  C  CB    . LEU A 1 201 ? 139.947 140.907 119.925 1.00 13.43 ?  201 LEU A CB    1 
ATOM   1633  C  CG    . LEU A 1 201 ? 138.635 141.645 120.196 1.00 16.60 ?  201 LEU A CG    1 
ATOM   1634  C  CD1   . LEU A 1 201 ? 137.452 140.701 120.069 1.00 10.05 ?  201 LEU A CD1   1 
ATOM   1635  C  CD2   . LEU A 1 201 ? 138.660 142.298 121.564 1.00 17.75 ?  201 LEU A CD2   1 
ATOM   1636  N  N     . ASN A 1 202 ? 142.954 141.286 118.727 1.00 10.22 ?  202 ASN A N     1 
ATOM   1637  C  CA    . ASN A 1 202 ? 144.333 140.840 118.866 1.00 5.13  ?  202 ASN A CA    1 
ATOM   1638  C  C     . ASN A 1 202 ? 144.656 140.707 120.348 1.00 14.00 ?  202 ASN A C     1 
ATOM   1639  O  O     . ASN A 1 202 ? 144.643 141.701 121.081 1.00 22.10 ?  202 ASN A O     1 
ATOM   1640  C  CB    . ASN A 1 202 ? 145.295 141.816 118.191 1.00 2.65  ?  202 ASN A CB    1 
ATOM   1641  C  CG    . ASN A 1 202 ? 146.699 141.265 118.078 1.00 7.30  ?  202 ASN A CG    1 
ATOM   1642  O  OD1   . ASN A 1 202 ? 146.904 140.053 118.098 1.00 17.32 ?  202 ASN A OD1   1 
ATOM   1643  N  ND2   . ASN A 1 202 ? 147.674 142.153 117.953 1.00 12.80 ?  202 ASN A ND2   1 
ATOM   1644  N  N     . LEU A 1 203 ? 144.941 139.483 120.786 1.00 10.42 ?  203 LEU A N     1 
ATOM   1645  C  CA    . LEU A 1 203 ? 145.249 139.205 122.181 1.00 8.77  ?  203 LEU A CA    1 
ATOM   1646  C  C     . LEU A 1 203 ? 146.742 139.039 122.434 1.00 9.89  ?  203 LEU A C     1 
ATOM   1647  O  O     . LEU A 1 203 ? 147.132 138.662 123.542 1.00 19.62 ?  203 LEU A O     1 
ATOM   1648  C  CB    . LEU A 1 203 ? 144.498 137.958 122.645 1.00 15.72 ?  203 LEU A CB    1 
ATOM   1649  C  CG    . LEU A 1 203 ? 142.978 137.982 122.474 1.00 17.57 ?  203 LEU A CG    1 
ATOM   1650  C  CD1   . LEU A 1 203 ? 142.336 136.872 123.289 1.00 16.21 ?  203 LEU A CD1   1 
ATOM   1651  C  CD2   . LEU A 1 203 ? 142.410 139.336 122.866 1.00 15.11 ?  203 LEU A CD2   1 
ATOM   1652  N  N     . SER A 1 204 ? 147.584 139.319 121.437 1.00 14.40 ?  204 SER A N     1 
ATOM   1653  C  CA    . SER A 1 204 ? 149.016 139.085 121.579 1.00 11.50 ?  204 SER A CA    1 
ATOM   1654  C  C     . SER A 1 204 ? 149.679 140.050 122.554 1.00 11.38 ?  204 SER A C     1 
ATOM   1655  O  O     . SER A 1 204 ? 150.759 139.743 123.068 1.00 19.83 ?  204 SER A O     1 
ATOM   1656  C  CB    . SER A 1 204 ? 149.698 139.174 120.216 1.00 5.83  ?  204 SER A CB    1 
ATOM   1657  O  OG    . SER A 1 204 ? 149.082 138.307 119.282 1.00 20.47 ?  204 SER A OG    1 
ATOM   1658  N  N     . LYS A 1 205 ? 149.066 141.204 122.824 1.00 15.38 ?  205 LYS A N     1 
ATOM   1659  C  CA    . LYS A 1 205 ? 149.640 142.146 123.776 1.00 14.55 ?  205 LYS A CA    1 
ATOM   1660  C  C     . LYS A 1 205 ? 149.329 141.788 125.222 1.00 13.03 ?  205 LYS A C     1 
ATOM   1661  O  O     . LYS A 1 205 ? 150.083 142.182 126.116 1.00 20.87 ?  205 LYS A O     1 
ATOM   1662  C  CB    . LYS A 1 205 ? 149.154 143.566 123.485 1.00 14.44 ?  205 LYS A CB    1 
ATOM   1663  C  CG    . LYS A 1 205 ? 149.808 144.199 122.277 1.00 11.13 ?  205 LYS A CG    1 
ATOM   1664  C  CD    . LYS A 1 205 ? 149.320 145.617 122.075 1.00 17.98 ?  205 LYS A CD    1 
ATOM   1665  C  CE    . LYS A 1 205 ? 150.129 146.327 121.008 1.00 25.05 ?  205 LYS A CE    1 
ATOM   1666  N  NZ    . LYS A 1 205 ? 149.938 145.714 119.667 1.00 22.20 1  205 LYS A NZ    1 
ATOM   1667  N  N     . LEU A 1 206 ? 148.245 141.058 125.471 1.00 17.42 ?  206 LEU A N     1 
ATOM   1668  C  CA    . LEU A 1 206 ? 147.944 140.624 126.826 1.00 7.53  ?  206 LEU A CA    1 
ATOM   1669  C  C     . LEU A 1 206 ? 149.059 139.730 127.349 1.00 11.02 ?  206 LEU A C     1 
ATOM   1670  O  O     . LEU A 1 206 ? 149.574 138.868 126.632 1.00 24.19 ?  206 LEU A O     1 
ATOM   1671  C  CB    . LEU A 1 206 ? 146.611 139.877 126.861 1.00 17.65 ?  206 LEU A CB    1 
ATOM   1672  C  CG    . LEU A 1 206 ? 145.397 140.610 126.289 1.00 21.51 ?  206 LEU A CG    1 
ATOM   1673  C  CD1   . LEU A 1 206 ? 144.156 139.739 126.385 1.00 19.69 ?  206 LEU A CD1   1 
ATOM   1674  C  CD2   . LEU A 1 206 ? 145.184 141.934 126.999 1.00 22.98 ?  206 LEU A CD2   1 
ATOM   1675  N  N     . ARG A 1 207 ? 149.438 139.941 128.604 1.00 23.36 ?  207 ARG A N     1 
ATOM   1676  C  CA    . ARG A 1 207 ? 150.479 139.121 129.202 1.00 18.86 ?  207 ARG A CA    1 
ATOM   1677  C  C     . ARG A 1 207 ? 149.975 137.698 129.417 1.00 21.81 ?  207 ARG A C     1 
ATOM   1678  O  O     . ARG A 1 207 ? 148.776 137.453 129.572 1.00 23.25 ?  207 ARG A O     1 
ATOM   1679  C  CB    . ARG A 1 207 ? 150.953 139.726 130.524 1.00 17.60 ?  207 ARG A CB    1 
ATOM   1680  C  CG    . ARG A 1 207 ? 149.851 140.008 131.523 1.00 19.45 ?  207 ARG A CG    1 
ATOM   1681  C  CD    . ARG A 1 207 ? 150.355 140.895 132.646 1.00 17.01 ?  207 ARG A CD    1 
ATOM   1682  N  NE    . ARG A 1 207 ? 150.467 142.287 132.229 1.00 21.57 ?  207 ARG A NE    1 
ATOM   1683  C  CZ    . ARG A 1 207 ? 150.863 143.276 133.017 1.00 20.67 ?  207 ARG A CZ    1 
ATOM   1684  N  NH1   . ARG A 1 207 ? 151.185 143.065 134.282 1.00 24.08 1  207 ARG A NH1   1 
ATOM   1685  N  NH2   . ARG A 1 207 ? 150.932 144.509 132.526 1.00 14.54 ?  207 ARG A NH2   1 
ATOM   1686  N  N     . ALA A 1 208 ? 150.911 136.754 129.417 1.00 25.28 ?  208 ALA A N     1 
ATOM   1687  C  CA    . ALA A 1 208 ? 150.567 135.347 129.501 1.00 19.75 ?  208 ALA A CA    1 
ATOM   1688  C  C     . ALA A 1 208 ? 150.106 134.987 130.912 1.00 26.37 ?  208 ALA A C     1 
ATOM   1689  O  O     . ALA A 1 208 ? 150.291 135.736 131.874 1.00 24.88 ?  208 ALA A O     1 
ATOM   1690  C  CB    . ALA A 1 208 ? 151.758 134.483 129.091 1.00 19.28 ?  208 ALA A CB    1 
ATOM   1691  N  N     . LYS A 1 209 ? 149.485 133.815 131.022 1.00 22.92 ?  209 LYS A N     1 
ATOM   1692  C  CA    . LYS A 1 209 ? 149.067 133.311 132.321 1.00 17.48 ?  209 LYS A CA    1 
ATOM   1693  C  C     . LYS A 1 209 ? 150.280 133.083 133.214 1.00 27.23 ?  209 LYS A C     1 
ATOM   1694  O  O     . LYS A 1 209 ? 151.312 132.570 132.773 1.00 26.90 ?  209 LYS A O     1 
ATOM   1695  C  CB    . LYS A 1 209 ? 148.279 132.011 132.155 1.00 18.78 ?  209 LYS A CB    1 
ATOM   1696  C  CG    . LYS A 1 209 ? 147.837 131.377 133.459 1.00 27.88 ?  209 LYS A CG    1 
ATOM   1697  C  CD    . LYS A 1 209 ? 147.608 129.884 133.290 1.00 26.54 ?  209 LYS A CD    1 
ATOM   1698  C  CE    . LYS A 1 209 ? 148.654 129.266 132.375 1.00 29.48 ?  209 LYS A CE    1 
ATOM   1699  N  NZ    . LYS A 1 209 ? 148.564 127.779 132.347 1.00 29.60 1  209 LYS A NZ    1 
ATOM   1700  N  N     . GLY A 1 210 ? 150.151 133.471 134.479 1.00 31.73 ?  210 GLY A N     1 
ATOM   1701  C  CA    . GLY A 1 210 ? 151.245 133.374 135.419 1.00 27.72 ?  210 GLY A CA    1 
ATOM   1702  C  C     . GLY A 1 210 ? 152.174 134.565 135.457 1.00 30.06 ?  210 GLY A C     1 
ATOM   1703  O  O     . GLY A 1 210 ? 153.289 134.441 135.975 1.00 39.04 ?  210 GLY A O     1 
ATOM   1704  N  N     . GLU A 1 211 ? 151.759 135.708 134.925 1.00 29.71 ?  211 GLU A N     1 
ATOM   1705  C  CA    . GLU A 1 211 ? 152.555 136.923 134.991 1.00 26.63 ?  211 GLU A CA    1 
ATOM   1706  C  C     . GLU A 1 211 ? 152.059 137.816 136.124 1.00 28.52 ?  211 GLU A C     1 
ATOM   1707  O  O     . GLU A 1 211 ? 150.932 137.687 136.605 1.00 32.35 ?  211 GLU A O     1 
ATOM   1708  C  CB    . GLU A 1 211 ? 152.513 137.669 133.656 1.00 24.91 ?  211 GLU A CB    1 
ATOM   1709  C  CG    . GLU A 1 211 ? 153.221 136.932 132.530 1.00 21.97 ?  211 GLU A CG    1 
ATOM   1710  C  CD    . GLU A 1 211 ? 153.781 137.863 131.474 1.00 26.54 ?  211 GLU A CD    1 
ATOM   1711  O  OE1   . GLU A 1 211 ? 154.818 138.504 131.736 1.00 29.34 ?  211 GLU A OE1   1 
ATOM   1712  O  OE2   . GLU A 1 211 ? 153.193 137.941 130.377 1.00 28.56 -1 211 GLU A OE2   1 
ATOM   1713  N  N     . ALA A 1 212 ? 152.925 138.733 136.548 1.00 31.84 ?  212 ALA A N     1 
ATOM   1714  C  CA    . ALA A 1 212 ? 152.677 139.532 137.738 1.00 30.36 ?  212 ALA A CA    1 
ATOM   1715  C  C     . ALA A 1 212 ? 151.854 140.772 137.414 1.00 31.54 ?  212 ALA A C     1 
ATOM   1716  O  O     . ALA A 1 212 ? 152.036 141.400 136.368 1.00 30.03 ?  212 ALA A O     1 
ATOM   1717  C  CB    . ALA A 1 212 ? 153.999 139.942 138.388 1.00 33.43 ?  212 ALA A CB    1 
ATOM   1718  N  N     . ILE A 1 213 ? 150.942 141.114 138.321 1.00 31.45 ?  213 ILE A N     1 
ATOM   1719  C  CA    . ILE A 1 213 ? 150.176 142.354 138.262 1.00 30.07 ?  213 ILE A CA    1 
ATOM   1720  C  C     . ILE A 1 213 ? 150.582 143.186 139.469 1.00 32.96 ?  213 ILE A C     1 
ATOM   1721  O  O     . ILE A 1 213 ? 150.316 142.799 140.614 1.00 38.37 ?  213 ILE A O     1 
ATOM   1722  C  CB    . ILE A 1 213 ? 148.663 142.106 138.255 1.00 32.59 ?  213 ILE A CB    1 
ATOM   1723  C  CG1   . ILE A 1 213 ? 148.305 140.971 137.296 1.00 31.87 ?  213 ILE A CG1   1 
ATOM   1724  C  CG2   . ILE A 1 213 ? 147.919 143.379 137.882 1.00 27.26 ?  213 ILE A CG2   1 
ATOM   1725  C  CD1   . ILE A 1 213 ? 146.899 140.450 137.480 1.00 23.86 ?  213 ILE A CD1   1 
ATOM   1726  N  N     . LYS A 1 214 ? 151.216 144.331 139.221 1.00 33.00 ?  214 LYS A N     1 
ATOM   1727  C  CA    . LYS A 1 214 ? 151.676 145.216 140.288 1.00 34.11 ?  214 LYS A CA    1 
ATOM   1728  C  C     . LYS A 1 214 ? 152.593 144.463 141.254 1.00 38.50 ?  214 LYS A C     1 
ATOM   1729  O  O     . LYS A 1 214 ? 152.295 144.293 142.438 1.00 38.12 ?  214 LYS A O     1 
ATOM   1730  C  CB    . LYS A 1 214 ? 150.489 145.843 141.028 1.00 31.05 ?  214 LYS A CB    1 
ATOM   1731  C  CG    . LYS A 1 214 ? 149.549 146.642 140.144 1.00 31.09 ?  214 LYS A CG    1 
ATOM   1732  C  CD    . LYS A 1 214 ? 150.022 148.077 139.976 1.00 33.13 ?  214 LYS A CD    1 
ATOM   1733  C  CE    . LYS A 1 214 ? 151.236 148.156 139.066 1.00 36.61 ?  214 LYS A CE    1 
ATOM   1734  N  NZ    . LYS A 1 214 ? 151.459 149.538 138.562 1.00 38.60 1  214 LYS A NZ    1 
ATOM   1735  N  N     . ASP A 1 215 ? 153.719 143.994 140.710 1.00 39.12 ?  215 ASP A N     1 
ATOM   1736  C  CA    . ASP A 1 215 ? 154.735 143.258 141.469 1.00 41.55 ?  215 ASP A CA    1 
ATOM   1737  C  C     . ASP A 1 215 ? 154.126 142.150 142.327 1.00 42.07 ?  215 ASP A C     1 
ATOM   1738  O  O     . ASP A 1 215 ? 154.648 141.809 143.391 1.00 44.51 ?  215 ASP A O     1 
ATOM   1739  C  CB    . ASP A 1 215 ? 155.592 144.207 142.317 1.00 41.84 ?  215 ASP A CB    1 
ATOM   1740  C  CG    . ASP A 1 215 ? 154.808 144.888 143.428 1.00 43.77 ?  215 ASP A CG    1 
ATOM   1741  O  OD1   . ASP A 1 215 ? 154.131 144.190 144.212 1.00 40.93 ?  215 ASP A OD1   1 
ATOM   1742  O  OD2   . ASP A 1 215 ? 154.872 146.133 143.513 1.00 44.01 -1 215 ASP A OD2   1 
ATOM   1743  N  N     . VAL A 1 216 ? 153.018 141.575 141.866 1.00 38.63 ?  216 VAL A N     1 
ATOM   1744  C  CA    . VAL A 1 216 ? 152.412 140.403 142.489 1.00 39.53 ?  216 VAL A CA    1 
ATOM   1745  C  C     . VAL A 1 216 ? 152.457 139.274 141.469 1.00 39.96 ?  216 VAL A C     1 
ATOM   1746  O  O     . VAL A 1 216 ? 151.768 139.330 140.444 1.00 44.58 ?  216 VAL A O     1 
ATOM   1747  C  CB    . VAL A 1 216 ? 150.975 140.674 142.955 1.00 35.85 ?  216 VAL A CB    1 
ATOM   1748  C  CG1   . VAL A 1 216 ? 150.177 139.382 142.989 1.00 37.26 ?  216 VAL A CG1   1 
ATOM   1749  C  CG2   . VAL A 1 216 ? 150.982 141.333 144.322 1.00 41.63 ?  216 VAL A CG2   1 
ATOM   1750  N  N     . GLU A 1 217 ? 153.258 138.253 141.752 1.00 35.17 ?  217 GLU A N     1 
ATOM   1751  C  CA    . GLU A 1 217 ? 153.559 137.214 140.780 1.00 37.98 ?  217 GLU A CA    1 
ATOM   1752  C  C     . GLU A 1 217 ? 152.424 136.200 140.677 1.00 41.03 ?  217 GLU A C     1 
ATOM   1753  O  O     . GLU A 1 217 ? 151.627 136.019 141.600 1.00 42.61 ?  217 GLU A O     1 
ATOM   1754  C  CB    . GLU A 1 217 ? 154.864 136.503 141.146 1.00 39.61 ?  217 GLU A CB    1 
ATOM   1755  C  CG    . GLU A 1 217 ? 156.122 137.227 140.686 1.00 41.55 ?  217 GLU A CG    1 
ATOM   1756  C  CD    . GLU A 1 217 ? 156.147 138.686 141.102 1.00 42.46 ?  217 GLU A CD    1 
ATOM   1757  O  OE1   . GLU A 1 217 ? 155.466 139.037 142.087 1.00 45.18 ?  217 GLU A OE1   1 
ATOM   1758  O  OE2   . GLU A 1 217 ? 156.843 139.482 140.439 1.00 41.34 -1 217 GLU A OE2   1 
ATOM   1759  N  N     . ASN A 1 218 ? 152.366 135.533 139.523 1.00 37.75 ?  218 ASN A N     1 
ATOM   1760  C  CA    . ASN A 1 218 ? 151.398 134.467 139.272 1.00 36.17 ?  218 ASN A CA    1 
ATOM   1761  C  C     . ASN A 1 218 ? 149.968 134.949 139.505 1.00 40.00 ?  218 ASN A C     1 
ATOM   1762  O  O     . ASN A 1 218 ? 149.123 134.228 140.040 1.00 44.48 ?  218 ASN A O     1 
ATOM   1763  C  CB    . ASN A 1 218 ? 151.706 133.239 140.129 1.00 39.01 ?  218 ASN A CB    1 
ATOM   1764  C  CG    . ASN A 1 218 ? 151.504 131.938 139.378 1.00 44.31 ?  218 ASN A CG    1 
ATOM   1765  O  OD1   . ASN A 1 218 ? 152.273 131.603 138.477 1.00 44.80 ?  218 ASN A OD1   1 
ATOM   1766  N  ND2   . ASN A 1 218 ? 150.468 131.196 139.749 1.00 42.91 ?  218 ASN A ND2   1 
ATOM   1767  N  N     . ALA A 1 219 ? 149.691 136.183 139.089 1.00 31.28 ?  219 ALA A N     1 
ATOM   1768  C  CA    . ALA A 1 219 ? 148.375 136.787 139.257 1.00 28.79 ?  219 ALA A CA    1 
ATOM   1769  C  C     . ALA A 1 219 ? 147.568 136.833 137.968 1.00 29.32 ?  219 ALA A C     1 
ATOM   1770  O  O     . ALA A 1 219 ? 146.342 136.684 138.006 1.00 29.01 ?  219 ALA A O     1 
ATOM   1771  C  CB    . ALA A 1 219 ? 148.514 138.204 139.820 1.00 29.12 ?  219 ALA A CB    1 
ATOM   1772  N  N     . THR A 1 220 ? 148.223 137.036 136.829 1.00 30.29 ?  220 THR A N     1 
ATOM   1773  C  CA    . THR A 1 220 ? 147.513 137.158 135.564 1.00 24.99 ?  220 THR A CA    1 
ATOM   1774  C  C     . THR A 1 220 ? 146.884 135.826 135.169 1.00 28.23 ?  220 THR A C     1 
ATOM   1775  O  O     . THR A 1 220 ? 147.453 134.757 135.403 1.00 27.57 ?  220 THR A O     1 
ATOM   1776  C  CB    . THR A 1 220 ? 148.467 137.640 134.470 1.00 24.77 ?  220 THR A CB    1 
ATOM   1777  O  OG1   . THR A 1 220 ? 148.986 138.929 134.822 1.00 30.16 ?  220 THR A OG1   1 
ATOM   1778  C  CG2   . THR A 1 220 ? 147.752 137.736 133.136 1.00 24.85 ?  220 THR A CG2   1 
ATOM   1779  N  N     . LYS A 1 221 ? 145.697 135.899 134.571 1.00 29.43 ?  221 LYS A N     1 
ATOM   1780  C  CA    . LYS A 1 221 ? 144.976 134.716 134.124 1.00 20.76 ?  221 LYS A CA    1 
ATOM   1781  C  C     . LYS A 1 221 ? 145.282 134.340 132.681 1.00 24.22 ?  221 LYS A C     1 
ATOM   1782  O  O     . LYS A 1 221 ? 144.811 133.298 132.215 1.00 29.08 ?  221 LYS A O     1 
ATOM   1783  C  CB    . LYS A 1 221 ? 143.467 134.922 134.290 1.00 24.24 ?  221 LYS A CB    1 
ATOM   1784  C  CG    . LYS A 1 221 ? 142.984 134.739 135.713 1.00 29.99 ?  221 LYS A CG    1 
ATOM   1785  C  CD    . LYS A 1 221 ? 141.501 134.427 135.762 1.00 28.99 ?  221 LYS A CD    1 
ATOM   1786  C  CE    . LYS A 1 221 ? 140.935 134.737 137.133 1.00 30.70 ?  221 LYS A CE    1 
ATOM   1787  N  NZ    . LYS A 1 221 ? 141.687 135.847 137.776 1.00 27.58 1  221 LYS A NZ    1 
ATOM   1788  N  N     . GLY A 1 222 ? 146.057 135.150 131.970 1.00 24.00 ?  222 GLY A N     1 
ATOM   1789  C  CA    . GLY A 1 222 ? 146.400 134.850 130.602 1.00 23.11 ?  222 GLY A CA    1 
ATOM   1790  C  C     . GLY A 1 222 ? 145.329 135.285 129.620 1.00 26.71 ?  222 GLY A C     1 
ATOM   1791  O  O     . GLY A 1 222 ? 144.333 135.928 129.963 1.00 27.18 ?  222 GLY A O     1 
ATOM   1792  N  N     . VAL A 1 223 ? 145.554 134.913 128.358 1.00 21.20 ?  223 VAL A N     1 
ATOM   1793  C  CA    . VAL A 1 223 ? 144.629 135.291 127.299 1.00 22.03 ?  223 VAL A CA    1 
ATOM   1794  C  C     . VAL A 1 223 ? 143.354 134.464 127.333 1.00 18.61 ?  223 VAL A C     1 
ATOM   1795  O  O     . VAL A 1 223 ? 142.362 134.845 126.708 1.00 25.80 ?  223 VAL A O     1 
ATOM   1796  C  CB    . VAL A 1 223 ? 145.308 135.172 125.921 1.00 23.94 ?  223 VAL A CB    1 
ATOM   1797  C  CG1   . VAL A 1 223 ? 146.610 135.956 125.899 1.00 17.78 ?  223 VAL A CG1   1 
ATOM   1798  C  CG2   . VAL A 1 223 ? 145.545 133.712 125.567 1.00 24.94 ?  223 VAL A CG2   1 
ATOM   1799  N  N     . VAL A 1 224 ? 143.344 133.341 128.053 1.00 22.77 ?  224 VAL A N     1 
ATOM   1800  C  CA    . VAL A 1 224 ? 142.161 132.487 128.047 1.00 24.41 ?  224 VAL A CA    1 
ATOM   1801  C  C     . VAL A 1 224 ? 141.045 133.066 128.915 1.00 23.56 ?  224 VAL A C     1 
ATOM   1802  O  O     . VAL A 1 224 ? 139.864 132.902 128.595 1.00 25.09 ?  224 VAL A O     1 
ATOM   1803  C  CB    . VAL A 1 224 ? 142.529 131.059 128.482 1.00 27.50 ?  224 VAL A CB    1 
ATOM   1804  C  CG1   . VAL A 1 224 ? 141.280 130.212 128.626 1.00 22.48 ?  224 VAL A CG1   1 
ATOM   1805  C  CG2   . VAL A 1 224 ? 143.481 130.439 127.473 1.00 23.60 ?  224 VAL A CG2   1 
ATOM   1806  N  N     . GLY A 1 225 ? 141.380 133.756 130.005 1.00 19.62 ?  225 GLY A N     1 
ATOM   1807  C  CA    . GLY A 1 225 ? 140.348 134.440 130.769 1.00 19.68 ?  225 GLY A CA    1 
ATOM   1808  C  C     . GLY A 1 225 ? 139.716 135.579 129.989 1.00 16.24 ?  225 GLY A C     1 
ATOM   1809  O  O     . GLY A 1 225 ? 138.491 135.750 129.993 1.00 24.88 ?  225 GLY A O     1 
ATOM   1810  N  N     . VAL A 1 226 ? 140.543 136.367 129.301 1.00 16.42 ?  226 VAL A N     1 
ATOM   1811  C  CA    . VAL A 1 226 ? 140.017 137.409 128.427 1.00 21.37 ?  226 VAL A CA    1 
ATOM   1812  C  C     . VAL A 1 226 ? 139.182 136.791 127.315 1.00 17.81 ?  226 VAL A C     1 
ATOM   1813  O  O     . VAL A 1 226 ? 138.170 137.358 126.892 1.00 17.93 ?  226 VAL A O     1 
ATOM   1814  C  CB    . VAL A 1 226 ? 141.167 138.266 127.865 1.00 20.17 ?  226 VAL A CB    1 
ATOM   1815  C  CG1   . VAL A 1 226 ? 140.627 139.318 126.913 1.00 16.86 ?  226 VAL A CG1   1 
ATOM   1816  C  CG2   . VAL A 1 226 ? 141.943 138.912 128.998 1.00 15.53 ?  226 VAL A CG2   1 
ATOM   1817  N  N     . MET A 1 227 ? 139.598 135.625 126.816 1.00 22.50 ?  227 MET A N     1 
ATOM   1818  C  CA    . MET A 1 227 ? 138.823 134.946 125.784 1.00 16.48 ?  227 MET A CA    1 
ATOM   1819  C  C     . MET A 1 227 ? 137.470 134.492 126.314 1.00 17.01 ?  227 MET A C     1 
ATOM   1820  O  O     . MET A 1 227 ? 136.472 134.553 125.595 1.00 22.93 ?  227 MET A O     1 
ATOM   1821  C  CB    . MET A 1 227 ? 139.602 133.758 125.225 1.00 18.98 ?  227 MET A CB    1 
ATOM   1822  C  CG    . MET A 1 227 ? 140.766 134.138 124.334 1.00 18.34 ?  227 MET A CG    1 
ATOM   1823  S  SD    . MET A 1 227 ? 141.921 132.776 124.128 1.00 40.30 ?  227 MET A SD    1 
ATOM   1824  C  CE    . MET A 1 227 ? 140.928 131.653 123.153 1.00 20.81 ?  227 MET A CE    1 
ATOM   1825  N  N     . LYS A 1 228 ? 137.419 134.012 127.557 1.00 19.66 ?  228 LYS A N     1 
ATOM   1826  C  CA    . LYS A 1 228 ? 136.134 133.665 128.155 1.00 19.79 ?  228 LYS A CA    1 
ATOM   1827  C  C     . LYS A 1 228 ? 135.245 134.894 128.285 1.00 21.88 ?  228 LYS A C     1 
ATOM   1828  O  O     . LYS A 1 228 ? 134.041 134.838 127.997 1.00 21.96 ?  228 LYS A O     1 
ATOM   1829  C  CB    . LYS A 1 228 ? 136.346 133.013 129.521 1.00 22.37 ?  228 LYS A CB    1 
ATOM   1830  C  CG    . LYS A 1 228 ? 136.350 131.497 129.495 1.00 26.01 ?  228 LYS A CG    1 
ATOM   1831  C  CD    . LYS A 1 228 ? 137.727 130.953 129.832 1.00 28.98 ?  228 LYS A CD    1 
ATOM   1832  C  CE    . LYS A 1 228 ? 138.043 131.144 131.308 1.00 28.91 ?  228 LYS A CE    1 
ATOM   1833  N  NZ    . LYS A 1 228 ? 139.431 130.718 131.641 1.00 32.43 1  228 LYS A NZ    1 
ATOM   1834  N  N     . LEU A 1 229 ? 135.824 136.018 128.710 1.00 20.01 ?  229 LEU A N     1 
ATOM   1835  C  CA    . LEU A 1 229 ? 135.058 137.259 128.784 1.00 13.31 ?  229 LEU A CA    1 
ATOM   1836  C  C     . LEU A 1 229 ? 134.511 137.645 127.415 1.00 17.92 ?  229 LEU A C     1 
ATOM   1837  O  O     . LEU A 1 229 ? 133.338 138.011 127.280 1.00 19.84 ?  229 LEU A O     1 
ATOM   1838  C  CB    . LEU A 1 229 ? 135.930 138.383 129.345 1.00 21.01 ?  229 LEU A CB    1 
ATOM   1839  C  CG    . LEU A 1 229 ? 136.496 138.213 130.753 1.00 17.69 ?  229 LEU A CG    1 
ATOM   1840  C  CD1   . LEU A 1 229 ? 137.671 139.150 130.956 1.00 20.51 ?  229 LEU A CD1   1 
ATOM   1841  C  CD2   . LEU A 1 229 ? 135.418 138.475 131.787 1.00 15.64 ?  229 LEU A CD2   1 
ATOM   1842  N  N     . LEU A 1 230 ? 135.356 137.570 126.385 1.00 23.65 ?  230 LEU A N     1 
ATOM   1843  C  CA    . LEU A 1 230 ? 134.936 137.928 125.034 1.00 16.70 ?  230 LEU A CA    1 
ATOM   1844  C  C     . LEU A 1 230 ? 133.870 136.975 124.511 1.00 14.44 ?  230 LEU A C     1 
ATOM   1845  O  O     . LEU A 1 230 ? 132.933 137.397 123.830 1.00 21.19 ?  230 LEU A O     1 
ATOM   1846  C  CB    . LEU A 1 230 ? 136.145 137.943 124.099 1.00 18.26 ?  230 LEU A CB    1 
ATOM   1847  C  CG    . LEU A 1 230 ? 137.204 139.014 124.370 1.00 21.80 ?  230 LEU A CG    1 
ATOM   1848  C  CD1   . LEU A 1 230 ? 138.472 138.727 123.582 1.00 21.36 ?  230 LEU A CD1   1 
ATOM   1849  C  CD2   . LEU A 1 230 ? 136.664 140.395 124.040 1.00 20.80 ?  230 LEU A CD2   1 
ATOM   1850  N  N     . ASP A 1 231 ? 134.015 135.681 124.798 1.00 24.38 ?  231 ASP A N     1 
ATOM   1851  C  CA    . ASP A 1 231 ? 133.020 134.703 124.377 1.00 21.03 ?  231 ASP A CA    1 
ATOM   1852  C  C     . ASP A 1 231 ? 131.670 134.993 125.013 1.00 23.72 ?  231 ASP A C     1 
ATOM   1853  O  O     . ASP A 1 231 ? 130.635 134.946 124.340 1.00 26.17 ?  231 ASP A O     1 
ATOM   1854  C  CB    . ASP A 1 231 ? 133.498 133.296 124.731 1.00 23.79 ?  231 ASP A CB    1 
ATOM   1855  C  CG    . ASP A 1 231 ? 132.558 132.217 124.235 1.00 34.16 ?  231 ASP A CG    1 
ATOM   1856  O  OD1   . ASP A 1 231 ? 132.651 131.850 123.046 1.00 36.46 ?  231 ASP A OD1   1 
ATOM   1857  O  OD2   . ASP A 1 231 ? 131.731 131.733 125.033 1.00 33.98 -1 231 ASP A OD2   1 
ATOM   1858  N  N     . ASN A 1 232 ? 131.661 135.309 126.309 1.00 28.14 ?  232 ASN A N     1 
ATOM   1859  C  CA    . ASN A 1 232 ? 130.408 135.666 126.965 1.00 25.56 ?  232 ASN A CA    1 
ATOM   1860  C  C     . ASN A 1 232 ? 129.828 136.955 126.396 1.00 18.76 ?  232 ASN A C     1 
ATOM   1861  O  O     . ASN A 1 232 ? 128.610 137.069 126.214 1.00 25.01 ?  232 ASN A O     1 
ATOM   1862  C  CB    . ASN A 1 232 ? 130.618 135.784 128.472 1.00 27.90 ?  232 ASN A CB    1 
ATOM   1863  C  CG    . ASN A 1 232 ? 130.023 134.620 129.229 1.00 30.52 ?  232 ASN A CG    1 
ATOM   1864  O  OD1   . ASN A 1 232 ? 130.708 133.644 129.529 1.00 39.33 ?  232 ASN A OD1   1 
ATOM   1865  N  ND2   . ASN A 1 232 ? 128.747 134.730 129.570 1.00 28.37 ?  232 ASN A ND2   1 
ATOM   1866  N  N     . ALA A 1 233 ? 130.682 137.941 126.114 1.00 22.71 ?  233 ALA A N     1 
ATOM   1867  C  CA    . ALA A 1 233 ? 130.201 139.196 125.546 1.00 13.56 ?  233 ALA A CA    1 
ATOM   1868  C  C     . ALA A 1 233 ? 129.583 138.984 124.169 1.00 22.65 ?  233 ALA A C     1 
ATOM   1869  O  O     . ALA A 1 233 ? 128.537 139.563 123.853 1.00 26.82 ?  233 ALA A O     1 
ATOM   1870  C  CB    . ALA A 1 233 ? 131.342 140.209 125.475 1.00 17.00 ?  233 ALA A CB    1 
ATOM   1871  N  N     . PHE A 1 234 ? 130.220 138.163 123.333 1.00 25.06 ?  234 PHE A N     1 
ATOM   1872  C  CA    . PHE A 1 234 ? 129.687 137.896 122.001 1.00 18.95 ?  234 PHE A CA    1 
ATOM   1873  C  C     . PHE A 1 234 ? 128.418 137.059 122.075 1.00 21.86 ?  234 PHE A C     1 
ATOM   1874  O  O     . PHE A 1 234 ? 127.509 137.225 121.254 1.00 27.40 ?  234 PHE A O     1 
ATOM   1875  C  CB    . PHE A 1 234 ? 130.745 137.201 121.144 1.00 19.45 ?  234 PHE A CB    1 
ATOM   1876  C  CG    . PHE A 1 234 ? 131.782 138.134 120.590 1.00 17.62 ?  234 PHE A CG    1 
ATOM   1877  C  CD1   . PHE A 1 234 ? 131.416 139.186 119.771 1.00 21.11 ?  234 PHE A CD1   1 
ATOM   1878  C  CD2   . PHE A 1 234 ? 133.121 137.965 120.894 1.00 21.98 ?  234 PHE A CD2   1 
ATOM   1879  C  CE1   . PHE A 1 234 ? 132.365 140.049 119.261 1.00 14.86 ?  234 PHE A CE1   1 
ATOM   1880  C  CE2   . PHE A 1 234 ? 134.074 138.825 120.386 1.00 23.66 ?  234 PHE A CE2   1 
ATOM   1881  C  CZ    . PHE A 1 234 ? 133.695 139.868 119.569 1.00 19.45 ?  234 PHE A CZ    1 
ATOM   1882  N  N     . ARG A 1 235 ? 128.341 136.150 123.048 1.00 29.93 ?  235 ARG A N     1 
ATOM   1883  C  CA    . ARG A 1 235 ? 127.117 135.391 123.261 1.00 21.52 ?  235 ARG A CA    1 
ATOM   1884  C  C     . ARG A 1 235 ? 125.969 136.293 123.688 1.00 26.13 ?  235 ARG A C     1 
ATOM   1885  O  O     . ARG A 1 235 ? 124.830 136.095 123.252 1.00 36.77 ?  235 ARG A O     1 
ATOM   1886  C  CB    . ARG A 1 235 ? 127.366 134.305 124.305 1.00 26.29 ?  235 ARG A CB    1 
ATOM   1887  C  CG    . ARG A 1 235 ? 126.376 133.161 124.290 1.00 33.68 ?  235 ARG A CG    1 
ATOM   1888  C  CD    . ARG A 1 235 ? 126.241 132.548 125.676 1.00 34.66 ?  235 ARG A CD    1 
ATOM   1889  N  NE    . ARG A 1 235 ? 127.530 132.373 126.341 1.00 38.36 ?  235 ARG A NE    1 
ATOM   1890  C  CZ    . ARG A 1 235 ? 128.594 131.794 125.801 1.00 37.30 ?  235 ARG A CZ    1 
ATOM   1891  N  NH1   . ARG A 1 235 ? 128.563 131.289 124.580 1.00 32.83 1  235 ARG A NH1   1 
ATOM   1892  N  NH2   . ARG A 1 235 ? 129.719 131.719 126.507 1.00 29.60 ?  235 ARG A NH2   1 
ATOM   1893  N  N     . TYR A 1 236 ? 126.246 137.284 124.537 1.00 23.31 ?  236 TYR A N     1 
ATOM   1894  C  CA    . TYR A 1 236 ? 125.193 138.182 124.996 1.00 23.28 ?  236 TYR A CA    1 
ATOM   1895  C  C     . TYR A 1 236 ? 124.696 139.080 123.868 1.00 26.10 ?  236 TYR A C     1 
ATOM   1896  O  O     . TYR A 1 236 ? 123.485 139.251 123.692 1.00 28.46 ?  236 TYR A O     1 
ATOM   1897  C  CB    . TYR A 1 236 ? 125.700 139.016 126.172 1.00 21.62 ?  236 TYR A CB    1 
ATOM   1898  C  CG    . TYR A 1 236 ? 124.725 140.067 126.643 1.00 27.39 ?  236 TYR A CG    1 
ATOM   1899  C  CD1   . TYR A 1 236 ? 123.647 139.729 127.448 1.00 21.08 ?  236 TYR A CD1   1 
ATOM   1900  C  CD2   . TYR A 1 236 ? 124.883 141.398 126.284 1.00 27.32 ?  236 TYR A CD2   1 
ATOM   1901  C  CE1   . TYR A 1 236 ? 122.755 140.685 127.879 1.00 17.22 ?  236 TYR A CE1   1 
ATOM   1902  C  CE2   . TYR A 1 236 ? 123.996 142.359 126.711 1.00 20.26 ?  236 TYR A CE2   1 
ATOM   1903  C  CZ    . TYR A 1 236 ? 122.935 141.998 127.510 1.00 20.03 ?  236 TYR A CZ    1 
ATOM   1904  O  OH    . TYR A 1 236 ? 122.050 142.955 127.938 1.00 29.04 ?  236 TYR A OH    1 
ATOM   1905  N  N     . ALA A 1 237 ? 125.613 139.659 123.092 1.00 32.91 ?  237 ALA A N     1 
ATOM   1906  C  CA    . ALA A 1 237 ? 125.251 140.501 121.952 1.00 31.61 ?  237 ALA A CA    1 
ATOM   1907  C  C     . ALA A 1 237 ? 125.073 139.604 120.730 1.00 37.73 ?  237 ALA A C     1 
ATOM   1908  O  O     . ALA A 1 237 ? 125.900 139.562 119.817 1.00 44.18 ?  237 ALA A O     1 
ATOM   1909  C  CB    . ALA A 1 237 ? 126.303 141.577 121.722 1.00 30.27 ?  237 ALA A CB    1 
ATOM   1910  N  N     . ASP A 1 238 ? 123.960 138.873 120.723 1.00 48.38 ?  238 ASP A N     1 
ATOM   1911  C  CA    . ASP A 1 238 ? 123.675 137.882 119.695 1.00 49.78 ?  238 ASP A CA    1 
ATOM   1912  C  C     . ASP A 1 238 ? 122.911 138.455 118.509 1.00 54.33 ?  238 ASP A C     1 
ATOM   1913  O  O     . ASP A 1 238 ? 122.549 137.703 117.600 1.00 59.77 ?  238 ASP A O     1 
ATOM   1914  C  CB    . ASP A 1 238 ? 122.896 136.711 120.296 1.00 53.03 ?  238 ASP A CB    1 
ATOM   1915  C  CG    . ASP A 1 238 ? 123.784 135.527 120.619 1.00 53.55 ?  238 ASP A CG    1 
ATOM   1916  O  OD1   . ASP A 1 238 ? 125.011 135.635 120.419 1.00 51.83 ?  238 ASP A OD1   1 
ATOM   1917  O  OD2   . ASP A 1 238 ? 123.257 134.492 121.076 1.00 53.86 -1 238 ASP A OD2   1 
ATOM   1918  N  N     . GLN A 1 239 ? 122.653 139.759 118.497 1.00 55.66 ?  239 GLN A N     1 
ATOM   1919  C  CA    . GLN A 1 239 ? 121.996 140.419 117.370 1.00 58.32 ?  239 GLN A CA    1 
ATOM   1920  C  C     . GLN A 1 239 ? 120.607 139.822 117.123 1.00 60.26 ?  239 GLN A C     1 
ATOM   1921  O  O     . GLN A 1 239 ? 120.276 139.361 116.032 1.00 61.25 ?  239 GLN A O     1 
ATOM   1922  C  CB    . GLN A 1 239 ? 122.862 140.313 116.113 1.00 55.81 ?  239 GLN A CB    1 
ATOM   1923  C  CG    . GLN A 1 239 ? 124.319 140.670 116.327 1.00 55.86 ?  239 GLN A CG    1 
ATOM   1924  C  CD    . GLN A 1 239 ? 125.205 140.193 115.191 1.00 59.30 ?  239 GLN A CD    1 
ATOM   1925  O  OE1   . GLN A 1 239 ? 124.785 140.157 114.035 1.00 59.97 ?  239 GLN A OE1   1 
ATOM   1926  N  NE2   . GLN A 1 239 ? 126.439 139.826 115.518 1.00 56.61 ?  239 GLN A NE2   1 
ATOM   1927  N  N     . MET A 1 240 ? 119.800 139.841 118.181 1.00 69.07 ?  240 MET A N     1 
ATOM   1928  C  CA    . MET A 1 240 ? 118.440 139.321 118.220 1.00 72.61 ?  240 MET A CA    1 
ATOM   1929  C  C     . MET A 1 240 ? 118.453 137.791 118.262 1.00 72.93 ?  240 MET A C     1 
ATOM   1930  O  O     . MET A 1 240 ? 117.395 137.183 118.417 1.00 72.00 ?  240 MET A O     1 
ATOM   1931  C  CB    . MET A 1 240 ? 117.585 139.791 117.024 1.00 72.86 ?  240 MET A CB    1 
ATOM   1932  C  CG    . MET A 1 240 ? 116.150 139.273 116.952 1.00 73.56 ?  240 MET A CG    1 
ATOM   1933  S  SD    . MET A 1 240 ? 115.336 138.952 118.531 1.00 77.56 ?  240 MET A SD    1 
ATOM   1934  C  CE    . MET A 1 240 ? 113.623 138.975 118.016 1.00 71.23 ?  240 MET A CE    1 
ATOM   1935  N  N     . GLY A 1 241 ? 119.613 137.146 118.143 1.00 72.42 ?  241 GLY A N     1 
ATOM   1936  C  CA    . GLY A 1 241 ? 119.687 135.702 118.129 1.00 72.66 ?  241 GLY A CA    1 
ATOM   1937  C  C     . GLY A 1 241 ? 119.526 135.061 116.770 1.00 75.72 ?  241 GLY A C     1 
ATOM   1938  O  O     . GLY A 1 241 ? 119.865 133.880 116.621 1.00 74.49 ?  241 GLY A O     1 
ATOM   1939  N  N     . GLN A 1 242 ? 119.023 135.791 115.771 1.00 81.30 ?  242 GLN A N     1 
ATOM   1940  C  CA    . GLN A 1 242 ? 118.909 135.223 114.431 1.00 81.24 ?  242 GLN A CA    1 
ATOM   1941  C  C     . GLN A 1 242 ? 120.280 134.849 113.884 1.00 81.16 ?  242 GLN A C     1 
ATOM   1942  O  O     . GLN A 1 242 ? 120.449 133.782 113.283 1.00 78.78 ?  242 GLN A O     1 
ATOM   1943  C  CB    . GLN A 1 242 ? 118.208 136.212 113.500 1.00 78.99 ?  242 GLN A CB    1 
ATOM   1944  C  CG    . GLN A 1 242 ? 116.740 136.438 113.825 1.00 80.38 ?  242 GLN A CG    1 
ATOM   1945  C  CD    . GLN A 1 242 ? 116.044 137.311 112.799 1.00 81.42 ?  242 GLN A CD    1 
ATOM   1946  O  OE1   . GLN A 1 242 ? 116.639 137.702 111.794 1.00 81.05 ?  242 GLN A OE1   1 
ATOM   1947  N  NE2   . GLN A 1 242 ? 114.777 137.621 113.048 1.00 81.09 ?  242 GLN A NE2   1 
ATOM   1948  N  N     . ARG A 1 243 ? 121.270 135.716 114.086 1.00 74.37 ?  243 ARG A N     1 
ATOM   1949  C  CA    . ARG A 1 243 ? 122.659 135.423 113.761 1.00 71.72 ?  243 ARG A CA    1 
ATOM   1950  C  C     . ARG A 1 243 ? 123.478 135.585 115.030 1.00 71.12 ?  243 ARG A C     1 
ATOM   1951  O  O     . ARG A 1 243 ? 123.669 136.709 115.507 1.00 70.24 ?  243 ARG A O     1 
ATOM   1952  C  CB    . ARG A 1 243 ? 123.181 136.343 112.654 1.00 71.85 ?  243 ARG A CB    1 
ATOM   1953  C  CG    . ARG A 1 243 ? 124.693 136.316 112.489 1.00 72.58 ?  243 ARG A CG    1 
ATOM   1954  C  CD    . ARG A 1 243 ? 125.086 136.211 111.023 1.00 72.09 ?  243 ARG A CD    1 
ATOM   1955  N  NE    . ARG A 1 243 ? 126.528 136.093 110.847 1.00 72.54 ?  243 ARG A NE    1 
ATOM   1956  C  CZ    . ARG A 1 243 ? 127.155 136.233 109.688 1.00 71.99 ?  243 ARG A CZ    1 
ATOM   1957  N  NH1   . ARG A 1 243 ? 126.496 136.496 108.572 1.00 71.48 1  243 ARG A NH1   1 
ATOM   1958  N  NH2   . ARG A 1 243 ? 128.479 136.105 109.646 1.00 71.10 ?  243 ARG A NH2   1 
ATOM   1959  N  N     . GLN A 1 244 ? 123.961 134.469 115.572 1.00 64.26 ?  244 GLN A N     1 
ATOM   1960  C  CA    . GLN A 1 244 ? 124.679 134.508 116.837 1.00 63.95 ?  244 GLN A CA    1 
ATOM   1961  C  C     . GLN A 1 244 ? 125.919 135.386 116.719 1.00 62.50 ?  244 GLN A C     1 
ATOM   1962  O  O     . GLN A 1 244 ? 126.569 135.448 115.671 1.00 62.12 ?  244 GLN A O     1 
ATOM   1963  C  CB    . GLN A 1 244 ? 125.073 133.096 117.271 1.00 62.31 ?  244 GLN A CB    1 
ATOM   1964  C  CG    . GLN A 1 244 ? 123.896 132.220 117.676 1.00 62.90 ?  244 GLN A CG    1 
ATOM   1965  C  CD    . GLN A 1 244 ? 124.331 130.910 118.305 1.00 63.70 ?  244 GLN A CD    1 
ATOM   1966  O  OE1   . GLN A 1 244 ? 125.224 130.231 117.798 1.00 61.66 ?  244 GLN A OE1   1 
ATOM   1967  N  NE2   . GLN A 1 244 ? 123.702 130.551 119.417 1.00 62.88 ?  244 GLN A NE2   1 
ATOM   1968  N  N     . GLY A 1 245 ? 126.240 136.078 117.809 1.00 48.01 ?  245 GLY A N     1 
ATOM   1969  C  CA    . GLY A 1 245 ? 127.396 136.952 117.829 1.00 45.96 ?  245 GLY A CA    1 
ATOM   1970  C  C     . GLY A 1 245 ? 128.672 136.220 117.474 1.00 42.66 ?  245 GLY A C     1 
ATOM   1971  O  O     . GLY A 1 245 ? 128.985 135.182 118.064 1.00 38.57 ?  245 GLY A O     1 
ATOM   1972  N  N     . SER A 1 246 ? 129.418 136.754 116.512 1.00 36.22 ?  246 SER A N     1 
ATOM   1973  C  CA    . SER A 1 246 ? 130.623 136.114 115.999 1.00 30.55 ?  246 SER A CA    1 
ATOM   1974  C  C     . SER A 1 246 ? 131.830 136.983 116.318 1.00 28.98 ?  246 SER A C     1 
ATOM   1975  O  O     . SER A 1 246 ? 131.866 138.164 115.955 1.00 25.27 ?  246 SER A O     1 
ATOM   1976  C  CB    . SER A 1 246 ? 130.516 135.875 114.493 1.00 22.13 ?  246 SER A CB    1 
ATOM   1977  O  OG    . SER A 1 246 ? 129.620 134.816 114.210 1.00 38.58 ?  246 SER A OG    1 
ATOM   1978  N  N     . GLY A 1 247 ? 132.809 136.397 116.990 1.00 20.26 ?  247 GLY A N     1 
ATOM   1979  C  CA    . GLY A 1 247 ? 134.052 137.085 117.275 1.00 3.36  ?  247 GLY A CA    1 
ATOM   1980  C  C     . GLY A 1 247 ? 135.227 136.159 117.057 1.00 11.84 ?  247 GLY A C     1 
ATOM   1981  O  O     . GLY A 1 247 ? 135.125 134.941 117.223 1.00 20.16 ?  247 GLY A O     1 
ATOM   1982  N  N     . ALA A 1 248 ? 136.349 136.751 116.670 1.00 22.65 ?  248 ALA A N     1 
ATOM   1983  C  CA    . ALA A 1 248 ? 137.593 136.025 116.471 1.00 11.23 ?  248 ALA A CA    1 
ATOM   1984  C  C     . ALA A 1 248 ? 138.673 136.625 117.356 1.00 9.84  ?  248 ALA A C     1 
ATOM   1985  O  O     . ALA A 1 248 ? 138.748 137.847 117.519 1.00 18.09 ?  248 ALA A O     1 
ATOM   1986  C  CB    . ALA A 1 248 ? 138.033 136.061 115.004 1.00 2.83  ?  248 ALA A CB    1 
ATOM   1987  N  N     . ALA A 1 249 ? 139.495 135.761 117.940 1.00 15.25 ?  249 ALA A N     1 
ATOM   1988  C  CA    . ALA A 1 249 ? 140.655 136.172 118.715 1.00 9.82  ?  249 ALA A CA    1 
ATOM   1989  C  C     . ALA A 1 249 ? 141.906 135.668 118.018 1.00 5.01  ?  249 ALA A C     1 
ATOM   1990  O  O     . ALA A 1 249 ? 141.967 134.505 117.607 1.00 14.33 ?  249 ALA A O     1 
ATOM   1991  C  CB    . ALA A 1 249 ? 140.588 135.638 120.148 1.00 11.29 ?  249 ALA A CB    1 
ATOM   1992  N  N     . TYR A 1 250 ? 142.893 136.542 117.873 1.00 8.60  ?  250 TYR A N     1 
ATOM   1993  C  CA    . TYR A 1 250 ? 144.155 136.200 117.240 1.00 2.74  ?  250 TYR A CA    1 
ATOM   1994  C  C     . TYR A 1 250 ? 145.272 136.259 118.271 1.00 11.07 ?  250 TYR A C     1 
ATOM   1995  O  O     . TYR A 1 250 ? 145.322 137.176 119.094 1.00 9.95  ?  250 TYR A O     1 
ATOM   1996  C  CB    . TYR A 1 250 ? 144.468 137.144 116.077 1.00 6.02  ?  250 TYR A CB    1 
ATOM   1997  C  CG    . TYR A 1 250 ? 143.765 136.782 114.789 1.00 9.07  ?  250 TYR A CG    1 
ATOM   1998  C  CD1   . TYR A 1 250 ? 142.420 137.071 114.609 1.00 4.27  ?  250 TYR A CD1   1 
ATOM   1999  C  CD2   . TYR A 1 250 ? 144.443 136.149 113.757 1.00 4.71  ?  250 TYR A CD2   1 
ATOM   2000  C  CE1   . TYR A 1 250 ? 141.771 136.744 113.439 1.00 0.00  ?  250 TYR A CE1   1 
ATOM   2001  C  CE2   . TYR A 1 250 ? 143.801 135.818 112.580 1.00 6.93  ?  250 TYR A CE2   1 
ATOM   2002  C  CZ    . TYR A 1 250 ? 142.465 136.116 112.429 1.00 0.00  ?  250 TYR A CZ    1 
ATOM   2003  O  OH    . TYR A 1 250 ? 141.816 135.794 111.260 1.00 7.84  ?  250 TYR A OH    1 
ATOM   2004  N  N     . LEU A 1 251 ? 146.157 135.272 118.226 1.00 14.47 ?  251 LEU A N     1 
ATOM   2005  C  CA    . LEU A 1 251 ? 147.303 135.222 119.117 1.00 9.53  ?  251 LEU A CA    1 
ATOM   2006  C  C     . LEU A 1 251 ? 148.546 134.871 118.319 1.00 7.55  ?  251 LEU A C     1 
ATOM   2007  O  O     . LEU A 1 251 ? 148.509 134.004 117.442 1.00 20.94 ?  251 LEU A O     1 
ATOM   2008  C  CB    . LEU A 1 251 ? 147.099 134.204 120.242 1.00 18.23 ?  251 LEU A CB    1 
ATOM   2009  C  CG    . LEU A 1 251 ? 148.067 134.344 121.416 1.00 13.66 ?  251 LEU A CG    1 
ATOM   2010  C  CD1   . LEU A 1 251 ? 147.796 135.634 122.175 1.00 5.11  ?  251 LEU A CD1   1 
ATOM   2011  C  CD2   . LEU A 1 251 ? 147.991 133.140 122.340 1.00 8.21  ?  251 LEU A CD2   1 
ATOM   2012  N  N     . ASN A 1 252 ? 149.645 135.551 118.626 1.00 17.45 ?  252 ASN A N     1 
ATOM   2013  C  CA    . ASN A 1 252 ? 150.918 135.221 118.006 1.00 11.76 ?  252 ASN A CA    1 
ATOM   2014  C  C     . ASN A 1 252 ? 151.385 133.850 118.471 1.00 14.62 ?  252 ASN A C     1 
ATOM   2015  O  O     . ASN A 1 252 ? 151.168 133.456 119.620 1.00 17.57 ?  252 ASN A O     1 
ATOM   2016  C  CB    . ASN A 1 252 ? 151.964 136.281 118.341 1.00 12.75 ?  252 ASN A CB    1 
ATOM   2017  C  CG    . ASN A 1 252 ? 153.097 136.316 117.337 1.00 17.84 ?  252 ASN A CG    1 
ATOM   2018  O  OD1   . ASN A 1 252 ? 154.009 135.493 117.383 1.00 24.68 ?  252 ASN A OD1   1 
ATOM   2019  N  ND2   . ASN A 1 252 ? 153.043 137.271 116.418 1.00 15.90 ?  252 ASN A ND2   1 
ATOM   2020  N  N     . ILE A 1 253 ? 152.025 133.112 117.560 1.00 14.64 ?  253 ILE A N     1 
ATOM   2021  C  CA    . ILE A 1 253 ? 152.505 131.778 117.892 1.00 13.94 ?  253 ILE A CA    1 
ATOM   2022  C  C     . ILE A 1 253 ? 153.596 131.819 118.952 1.00 17.54 ?  253 ILE A C     1 
ATOM   2023  O  O     . ILE A 1 253 ? 153.792 130.834 119.672 1.00 21.09 ?  253 ILE A O     1 
ATOM   2024  C  CB    . ILE A 1 253 ? 152.999 131.059 116.623 1.00 18.72 ?  253 ILE A CB    1 
ATOM   2025  C  CG1   . ILE A 1 253 ? 153.003 129.546 116.839 1.00 11.73 ?  253 ILE A CG1   1 
ATOM   2026  C  CG2   . ILE A 1 253 ? 154.379 131.562 116.223 1.00 10.80 ?  253 ILE A CG2   1 
ATOM   2027  C  CD1   . ILE A 1 253 ? 152.788 128.754 115.576 1.00 15.33 ?  253 ILE A CD1   1 
ATOM   2028  N  N     . PHE A 1 254 ? 154.307 132.935 119.072 1.00 19.66 ?  254 PHE A N     1 
ATOM   2029  C  CA    . PHE A 1 254 ? 155.367 133.075 120.060 1.00 14.59 ?  254 PHE A CA    1 
ATOM   2030  C  C     . PHE A 1 254 ? 154.857 133.571 121.405 1.00 19.65 ?  254 PHE A C     1 
ATOM   2031  O  O     . PHE A 1 254 ? 155.660 133.769 122.322 1.00 25.26 ?  254 PHE A O     1 
ATOM   2032  C  CB    . PHE A 1 254 ? 156.452 134.017 119.532 1.00 16.72 ?  254 PHE A CB    1 
ATOM   2033  C  CG    . PHE A 1 254 ? 157.392 133.365 118.562 1.00 20.70 ?  254 PHE A CG    1 
ATOM   2034  C  CD1   . PHE A 1 254 ? 158.290 132.405 118.990 1.00 19.29 ?  254 PHE A CD1   1 
ATOM   2035  C  CD2   . PHE A 1 254 ? 157.367 133.702 117.220 1.00 24.20 ?  254 PHE A CD2   1 
ATOM   2036  C  CE1   . PHE A 1 254 ? 159.155 131.799 118.100 1.00 22.11 ?  254 PHE A CE1   1 
ATOM   2037  C  CE2   . PHE A 1 254 ? 158.229 133.099 116.326 1.00 26.72 ?  254 PHE A CE2   1 
ATOM   2038  C  CZ    . PHE A 1 254 ? 159.125 132.146 116.768 1.00 21.56 ?  254 PHE A CZ    1 
ATOM   2039  N  N     . HIS A 1 255 ? 153.552 133.782 121.539 1.00 21.33 ?  255 HIS A N     1 
ATOM   2040  C  CA    . HIS A 1 255 ? 152.969 134.093 122.832 1.00 15.28 ?  255 HIS A CA    1 
ATOM   2041  C  C     . HIS A 1 255 ? 153.040 132.875 123.745 1.00 13.42 ?  255 HIS A C     1 
ATOM   2042  O  O     . HIS A 1 255 ? 152.940 131.729 123.301 1.00 26.25 ?  255 HIS A O     1 
ATOM   2043  C  CB    . HIS A 1 255 ? 151.519 134.543 122.665 1.00 14.01 ?  255 HIS A CB    1 
ATOM   2044  C  CG    . HIS A 1 255 ? 150.982 135.315 123.830 1.00 12.50 ?  255 HIS A CG    1 
ATOM   2045  N  ND1   . HIS A 1 255 ? 150.486 134.708 124.962 1.00 11.93 ?  255 HIS A ND1   1 
ATOM   2046  C  CD2   . HIS A 1 255 ? 150.845 136.648 124.027 1.00 16.09 ?  255 HIS A CD2   1 
ATOM   2047  C  CE1   . HIS A 1 255 ? 150.073 135.632 125.810 1.00 13.60 ?  255 HIS A CE1   1 
ATOM   2048  N  NE2   . HIS A 1 255 ? 150.280 136.818 125.268 1.00 10.35 ?  255 HIS A NE2   1 
ATOM   2049  N  N     . ARG A 1 256 ? 153.219 133.135 125.039 1.00 22.23 ?  256 ARG A N     1 
ATOM   2050  C  CA    . ARG A 1 256 ? 153.321 132.044 126.002 1.00 15.94 ?  256 ARG A CA    1 
ATOM   2051  C  C     . ARG A 1 256 ? 152.030 131.236 126.061 1.00 17.88 ?  256 ARG A C     1 
ATOM   2052  O  O     . ARG A 1 256 ? 152.061 130.002 126.114 1.00 21.73 ?  256 ARG A O     1 
ATOM   2053  C  CB    . ARG A 1 256 ? 153.670 132.605 127.380 1.00 20.69 ?  256 ARG A CB    1 
ATOM   2054  C  CG    . ARG A 1 256 ? 154.707 131.808 128.131 1.00 22.00 ?  256 ARG A CG    1 
ATOM   2055  C  CD    . ARG A 1 256 ? 154.130 130.494 128.593 1.00 27.03 ?  256 ARG A CD    1 
ATOM   2056  N  NE    . ARG A 1 256 ? 152.851 130.665 129.270 1.00 27.03 ?  256 ARG A NE    1 
ATOM   2057  C  CZ    . ARG A 1 256 ? 152.216 129.698 129.917 1.00 28.37 ?  256 ARG A CZ    1 
ATOM   2058  N  NH1   . ARG A 1 256 ? 152.722 128.480 130.008 1.00 25.73 1  256 ARG A NH1   1 
ATOM   2059  N  NH2   . ARG A 1 256 ? 151.044 129.960 130.485 1.00 28.04 ?  256 ARG A NH2   1 
ATOM   2060  N  N     . ASP A 1 257 ? 150.886 131.915 126.039 1.00 18.26 ?  257 ASP A N     1 
ATOM   2061  C  CA    . ASP A 1 257 ? 149.579 131.282 126.157 1.00 16.32 ?  257 ASP A CA    1 
ATOM   2062  C  C     . ASP A 1 257 ? 149.128 130.584 124.880 1.00 16.93 ?  257 ASP A C     1 
ATOM   2063  O  O     . ASP A 1 257 ? 147.949 130.236 124.773 1.00 19.11 ?  257 ASP A O     1 
ATOM   2064  C  CB    . ASP A 1 257 ? 148.532 132.321 126.566 1.00 20.18 ?  257 ASP A CB    1 
ATOM   2065  C  CG    . ASP A 1 257 ? 148.653 132.729 128.019 1.00 25.04 ?  257 ASP A CG    1 
ATOM   2066  O  OD1   . ASP A 1 257 ? 149.333 132.015 128.785 1.00 28.63 ?  257 ASP A OD1   1 
ATOM   2067  O  OD2   . ASP A 1 257 ? 148.068 133.765 128.396 1.00 29.07 -1 257 ASP A OD2   1 
ATOM   2068  N  N     . ILE A 1 258 ? 150.028 130.369 123.917 1.00 22.17 ?  258 ILE A N     1 
ATOM   2069  C  CA    . ILE A 1 258 ? 149.612 129.832 122.624 1.00 22.87 ?  258 ILE A CA    1 
ATOM   2070  C  C     . ILE A 1 258 ? 149.009 128.441 122.783 1.00 16.21 ?  258 ILE A C     1 
ATOM   2071  O  O     . ILE A 1 258 ? 148.000 128.112 122.147 1.00 23.27 ?  258 ILE A O     1 
ATOM   2072  C  CB    . ILE A 1 258 ? 150.793 129.832 121.635 1.00 24.80 ?  258 ILE A CB    1 
ATOM   2073  C  CG1   . ILE A 1 258 ? 150.315 129.430 120.237 1.00 18.01 ?  258 ILE A CG1   1 
ATOM   2074  C  CG2   . ILE A 1 258 ? 151.902 128.909 122.116 1.00 16.80 ?  258 ILE A CG2   1 
ATOM   2075  C  CD1   . ILE A 1 258 ? 149.128 130.228 119.746 1.00 4.53  ?  258 ILE A CD1   1 
ATOM   2076  N  N     . ASN A 1 259 ? 149.614 127.601 123.623 1.00 23.69 ?  259 ASN A N     1 
ATOM   2077  C  CA    . ASN A 1 259 ? 149.089 126.251 123.810 1.00 19.77 ?  259 ASN A CA    1 
ATOM   2078  C  C     . ASN A 1 259 ? 147.722 126.279 124.480 1.00 20.98 ?  259 ASN A C     1 
ATOM   2079  O  O     . ASN A 1 259 ? 146.795 125.581 124.053 1.00 26.48 ?  259 ASN A O     1 
ATOM   2080  C  CB    . ASN A 1 259 ? 150.077 125.411 124.619 1.00 23.49 ?  259 ASN A CB    1 
ATOM   2081  C  CG    . ASN A 1 259 ? 151.144 124.778 123.751 1.00 26.06 ?  259 ASN A CG    1 
ATOM   2082  O  OD1   . ASN A 1 259 ? 150.841 124.028 122.825 1.00 27.00 ?  259 ASN A OD1   1 
ATOM   2083  N  ND2   . ASN A 1 259 ? 152.402 125.077 124.046 1.00 27.46 ?  259 ASN A ND2   1 
ATOM   2084  N  N     . ASP A 1 260 ? 147.573 127.084 125.534 1.00 22.71 ?  260 ASP A N     1 
ATOM   2085  C  CA    . ASP A 1 260 ? 146.262 127.255 126.150 1.00 19.55 ?  260 ASP A CA    1 
ATOM   2086  C  C     . ASP A 1 260 ? 145.289 127.920 125.187 1.00 22.32 ?  260 ASP A C     1 
ATOM   2087  O  O     . ASP A 1 260 ? 144.094 127.604 125.177 1.00 26.23 ?  260 ASP A O     1 
ATOM   2088  C  CB    . ASP A 1 260 ? 146.387 128.067 127.438 1.00 21.77 ?  260 ASP A CB    1 
ATOM   2089  C  CG    . ASP A 1 260 ? 147.602 127.679 128.258 1.00 34.95 ?  260 ASP A CG    1 
ATOM   2090  O  OD1   . ASP A 1 260 ? 147.998 126.496 128.215 1.00 35.74 ?  260 ASP A OD1   1 
ATOM   2091  O  OD2   . ASP A 1 260 ? 148.163 128.558 128.946 1.00 35.96 -1 260 ASP A OD2   1 
ATOM   2092  N  N     . PHE A 1 261 ? 145.787 128.853 124.372 1.00 29.37 ?  261 PHE A N     1 
ATOM   2093  C  CA    . PHE A 1 261 ? 144.944 129.506 123.377 1.00 19.65 ?  261 PHE A CA    1 
ATOM   2094  C  C     . PHE A 1 261 ? 144.356 128.490 122.406 1.00 17.09 ?  261 PHE A C     1 
ATOM   2095  O  O     . PHE A 1 261 ? 143.177 128.571 122.047 1.00 20.94 ?  261 PHE A O     1 
ATOM   2096  C  CB    . PHE A 1 261 ? 145.764 130.567 122.637 1.00 9.26  ?  261 PHE A CB    1 
ATOM   2097  C  CG    . PHE A 1 261 ? 145.051 131.205 121.479 1.00 19.56 ?  261 PHE A CG    1 
ATOM   2098  C  CD1   . PHE A 1 261 ? 144.148 132.233 121.685 1.00 16.56 ?  261 PHE A CD1   1 
ATOM   2099  C  CD2   . PHE A 1 261 ? 145.309 130.798 120.181 1.00 22.12 ?  261 PHE A CD2   1 
ATOM   2100  C  CE1   . PHE A 1 261 ? 143.503 132.830 120.620 1.00 13.63 ?  261 PHE A CE1   1 
ATOM   2101  C  CE2   . PHE A 1 261 ? 144.667 131.392 119.114 1.00 13.12 ?  261 PHE A CE2   1 
ATOM   2102  C  CZ    . PHE A 1 261 ? 143.764 132.409 119.335 1.00 16.89 ?  261 PHE A CZ    1 
ATOM   2103  N  N     . LEU A 1 262 ? 145.164 127.520 121.978 1.00 22.31 ?  262 LEU A N     1 
ATOM   2104  C  CA    . LEU A 1 262 ? 144.686 126.480 121.075 1.00 18.92 ?  262 LEU A CA    1 
ATOM   2105  C  C     . LEU A 1 262 ? 143.818 125.451 121.788 1.00 27.00 ?  262 LEU A C     1 
ATOM   2106  O  O     . LEU A 1 262 ? 142.912 124.879 121.171 1.00 25.80 ?  262 LEU A O     1 
ATOM   2107  C  CB    . LEU A 1 262 ? 145.869 125.782 120.404 1.00 25.66 ?  262 LEU A CB    1 
ATOM   2108  C  CG    . LEU A 1 262 ? 146.791 126.660 119.558 1.00 22.95 ?  262 LEU A CG    1 
ATOM   2109  C  CD1   . LEU A 1 262 ? 147.959 125.846 119.032 1.00 22.20 ?  262 LEU A CD1   1 
ATOM   2110  C  CD2   . LEU A 1 262 ? 146.022 127.307 118.417 1.00 18.08 ?  262 LEU A CD2   1 
ATOM   2111  N  N     . ASP A 1 263 ? 144.075 125.199 123.073 1.00 36.79 ?  263 ASP A N     1 
ATOM   2112  C  CA    . ASP A 1 263 ? 143.321 124.188 123.804 1.00 26.23 ?  263 ASP A CA    1 
ATOM   2113  C  C     . ASP A 1 263 ? 141.864 124.580 124.006 1.00 29.36 ?  263 ASP A C     1 
ATOM   2114  O  O     . ASP A 1 263 ? 141.038 123.710 124.304 1.00 39.48 ?  263 ASP A O     1 
ATOM   2115  C  CB    . ASP A 1 263 ? 143.976 123.919 125.159 1.00 27.46 ?  263 ASP A CB    1 
ATOM   2116  C  CG    . ASP A 1 263 ? 145.311 123.222 125.028 1.00 36.58 ?  263 ASP A CG    1 
ATOM   2117  O  OD1   . ASP A 1 263 ? 145.517 122.518 124.018 1.00 36.42 ?  263 ASP A OD1   1 
ATOM   2118  O  OD2   . ASP A 1 263 ? 146.157 123.380 125.934 1.00 37.70 -1 263 ASP A OD2   1 
ATOM   2119  N  N     . THR A 1 264 ? 141.529 125.862 123.854 1.00 31.07 ?  264 THR A N     1 
ATOM   2120  C  CA    . THR A 1 264 ? 140.140 126.285 123.983 1.00 30.28 ?  264 THR A CA    1 
ATOM   2121  C  C     . THR A 1 264 ? 139.256 125.697 122.893 1.00 32.41 ?  264 THR A C     1 
ATOM   2122  O  O     . THR A 1 264 ? 138.033 125.648 123.061 1.00 34.42 ?  264 THR A O     1 
ATOM   2123  C  CB    . THR A 1 264 ? 140.046 127.812 123.953 1.00 30.49 ?  264 THR A CB    1 
ATOM   2124  O  OG1   . THR A 1 264 ? 140.486 128.293 122.676 1.00 28.79 ?  264 THR A OG1   1 
ATOM   2125  C  CG2   . THR A 1 264 ? 140.908 128.423 125.043 1.00 29.12 ?  264 THR A CG2   1 
ATOM   2126  N  N     . LYS A 1 265 ? 139.842 125.260 121.781 1.00 32.31 ?  265 LYS A N     1 
ATOM   2127  C  CA    . LYS A 1 265 ? 139.089 124.714 120.660 1.00 34.53 ?  265 LYS A CA    1 
ATOM   2128  C  C     . LYS A 1 265 ? 139.096 123.194 120.618 1.00 34.64 ?  265 LYS A C     1 
ATOM   2129  O  O     . LYS A 1 265 ? 138.505 122.611 119.703 1.00 38.78 ?  265 LYS A O     1 
ATOM   2130  C  CB    . LYS A 1 265 ? 139.636 125.269 119.341 1.00 33.44 ?  265 LYS A CB    1 
ATOM   2131  C  CG    . LYS A 1 265 ? 139.173 126.677 119.040 1.00 33.83 ?  265 LYS A CG    1 
ATOM   2132  C  CD    . LYS A 1 265 ? 137.661 126.763 119.094 1.00 34.15 ?  265 LYS A CD    1 
ATOM   2133  C  CE    . LYS A 1 265 ? 137.185 128.192 118.980 1.00 34.53 ?  265 LYS A CE    1 
ATOM   2134  N  NZ    . LYS A 1 265 ? 135.739 128.311 119.307 1.00 37.67 1  265 LYS A NZ    1 
ATOM   2135  N  N     . LYS A 1 266 ? 139.745 122.537 121.575 1.00 39.80 ?  266 LYS A N     1 
ATOM   2136  C  CA    . LYS A 1 266 ? 139.701 121.084 121.638 1.00 43.62 ?  266 LYS A CA    1 
ATOM   2137  C  C     . LYS A 1 266 ? 138.349 120.618 122.161 1.00 46.69 ?  266 LYS A C     1 
ATOM   2138  O  O     . LYS A 1 266 ? 137.798 121.193 123.104 1.00 47.18 ?  266 LYS A O     1 
ATOM   2139  C  CB    . LYS A 1 266 ? 140.821 120.554 122.532 1.00 40.50 ?  266 LYS A CB    1 
ATOM   2140  C  CG    . LYS A 1 266 ? 142.185 120.511 121.871 1.00 42.26 ?  266 LYS A CG    1 
ATOM   2141  C  CD    . LYS A 1 266 ? 143.213 119.863 122.781 1.00 46.15 ?  266 LYS A CD    1 
ATOM   2142  C  CE    . LYS A 1 266 ? 144.494 119.542 122.028 1.00 45.54 ?  266 LYS A CE    1 
ATOM   2143  N  NZ    . LYS A 1 266 ? 145.606 119.178 122.949 1.00 45.99 1  266 LYS A NZ    1 
ATOM   2144  N  N     . ILE A 1 267 ? 137.811 119.567 121.540 1.00 51.59 ?  267 ILE A N     1 
ATOM   2145  C  CA    . ILE A 1 267 ? 136.545 119.013 122.008 1.00 55.10 ?  267 ILE A CA    1 
ATOM   2146  C  C     . ILE A 1 267 ? 136.702 118.421 123.402 1.00 54.32 ?  267 ILE A C     1 
ATOM   2147  O  O     . ILE A 1 267 ? 135.784 118.505 124.227 1.00 52.67 ?  267 ILE A O     1 
ATOM   2148  C  CB    . ILE A 1 267 ? 136.012 117.971 121.007 1.00 55.25 ?  267 ILE A CB    1 
ATOM   2149  C  CG1   . ILE A 1 267 ? 137.066 116.895 120.745 1.00 53.82 ?  267 ILE A CG1   1 
ATOM   2150  C  CG2   . ILE A 1 267 ? 135.597 118.645 119.708 1.00 54.86 ?  267 ILE A CG2   1 
ATOM   2151  C  CD1   . ILE A 1 267 ? 136.814 116.090 119.491 1.00 52.95 ?  267 ILE A CD1   1 
ATOM   2152  N  N     . SER A 1 268 ? 137.856 117.817 123.689 1.00 54.54 ?  268 SER A N     1 
ATOM   2153  C  CA    . SER A 1 268 ? 138.121 117.257 125.007 1.00 56.26 ?  268 SER A CA    1 
ATOM   2154  C  C     . SER A 1 268 ? 138.351 118.325 126.068 1.00 58.15 ?  268 SER A C     1 
ATOM   2155  O  O     . SER A 1 268 ? 138.436 117.987 127.253 1.00 58.96 ?  268 SER A O     1 
ATOM   2156  C  CB    . SER A 1 268 ? 139.333 116.328 124.945 1.00 59.71 ?  268 SER A CB    1 
ATOM   2157  O  OG    . SER A 1 268 ? 140.479 117.018 124.478 1.00 58.15 ?  268 SER A OG    1 
ATOM   2158  N  N     . ALA A 1 269 ? 138.454 119.593 125.677 1.00 60.24 ?  269 ALA A N     1 
ATOM   2159  C  CA    . ALA A 1 269 ? 138.737 120.653 126.634 1.00 58.79 ?  269 ALA A CA    1 
ATOM   2160  C  C     . ALA A 1 269 ? 137.620 120.767 127.665 1.00 60.81 ?  269 ALA A C     1 
ATOM   2161  O  O     . ALA A 1 269 ? 136.445 120.528 127.376 1.00 57.94 ?  269 ALA A O     1 
ATOM   2162  C  CB    . ALA A 1 269 ? 138.922 121.988 125.912 1.00 56.63 ?  269 ALA A CB    1 
ATOM   2163  N  N     . ASP A 1 270 ? 138.003 121.134 128.886 1.00 65.87 ?  270 ASP A N     1 
ATOM   2164  C  CA    . ASP A 1 270 ? 137.035 121.325 129.955 1.00 66.22 ?  270 ASP A CA    1 
ATOM   2165  C  C     . ASP A 1 270 ? 136.113 122.495 129.630 1.00 67.58 ?  270 ASP A C     1 
ATOM   2166  O  O     . ASP A 1 270 ? 136.506 123.465 128.976 1.00 68.60 ?  270 ASP A O     1 
ATOM   2167  C  CB    . ASP A 1 270 ? 137.754 121.564 131.283 1.00 66.37 ?  270 ASP A CB    1 
ATOM   2168  C  CG    . ASP A 1 270 ? 136.843 122.143 132.349 1.00 69.72 ?  270 ASP A CG    1 
ATOM   2169  O  OD1   . ASP A 1 270 ? 135.659 121.750 132.401 1.00 69.96 ?  270 ASP A OD1   1 
ATOM   2170  O  OD2   . ASP A 1 270 ? 137.313 122.993 133.134 1.00 69.74 -1 270 ASP A OD2   1 
ATOM   2171  N  N     . GLU A 1 271 ? 134.865 122.394 130.095 1.00 67.22 ?  271 GLU A N     1 
ATOM   2172  C  CA    . GLU A 1 271 ? 133.869 123.403 129.761 1.00 68.55 ?  271 GLU A CA    1 
ATOM   2173  C  C     . GLU A 1 271 ? 134.212 124.773 130.331 1.00 67.53 ?  271 GLU A C     1 
ATOM   2174  O  O     . GLU A 1 271 ? 133.843 125.788 129.732 1.00 65.95 ?  271 GLU A O     1 
ATOM   2175  C  CB    . GLU A 1 271 ? 132.489 122.961 130.251 1.00 65.80 ?  271 GLU A CB    1 
ATOM   2176  C  CG    . GLU A 1 271 ? 131.790 122.004 129.305 1.00 66.11 ?  271 GLU A CG    1 
ATOM   2177  C  CD    . GLU A 1 271 ? 131.396 122.665 128.000 1.00 68.50 ?  271 GLU A CD    1 
ATOM   2178  O  OE1   . GLU A 1 271 ? 130.906 123.813 128.039 1.00 69.16 ?  271 GLU A OE1   1 
ATOM   2179  O  OE2   . GLU A 1 271 ? 131.582 122.041 126.934 1.00 67.17 -1 271 GLU A OE2   1 
ATOM   2180  N  N     . ASP A 1 272 ? 134.906 124.828 131.466 1.00 65.15 ?  272 ASP A N     1 
ATOM   2181  C  CA    . ASP A 1 272 ? 135.334 126.107 132.018 1.00 67.04 ?  272 ASP A CA    1 
ATOM   2182  C  C     . ASP A 1 272 ? 136.429 126.766 131.189 1.00 63.93 ?  272 ASP A C     1 
ATOM   2183  O  O     . ASP A 1 272 ? 136.701 127.955 131.385 1.00 64.01 ?  272 ASP A O     1 
ATOM   2184  C  CB    . ASP A 1 272 ? 135.815 125.926 133.460 1.00 67.11 ?  272 ASP A CB    1 
ATOM   2185  C  CG    . ASP A 1 272 ? 134.668 125.846 134.450 1.00 68.90 ?  272 ASP A CG    1 
ATOM   2186  O  OD1   . ASP A 1 272 ? 133.550 126.284 134.106 1.00 67.26 ?  272 ASP A OD1   1 
ATOM   2187  O  OD2   . ASP A 1 272 ? 134.883 125.342 135.574 1.00 66.57 -1 272 ASP A OD2   1 
ATOM   2188  N  N     . VAL A 1 273 ? 137.056 126.026 130.276 1.00 53.34 ?  273 VAL A N     1 
ATOM   2189  C  CA    . VAL A 1 273 ? 138.047 126.588 129.376 1.00 53.29 ?  273 VAL A CA    1 
ATOM   2190  C  C     . VAL A 1 273 ? 137.529 126.711 127.946 1.00 52.72 ?  273 VAL A C     1 
ATOM   2191  O  O     . VAL A 1 273 ? 138.048 127.534 127.182 1.00 53.88 ?  273 VAL A O     1 
ATOM   2192  C  CB    . VAL A 1 273 ? 139.347 125.758 129.415 1.00 55.72 ?  273 VAL A CB    1 
ATOM   2193  C  CG1   . VAL A 1 273 ? 139.951 125.637 128.024 1.00 53.38 ?  273 VAL A CG1   1 
ATOM   2194  C  CG2   . VAL A 1 273 ? 140.342 126.378 130.384 1.00 53.25 ?  273 VAL A CG2   1 
ATOM   2195  N  N     . ARG A 1 274 ? 136.520 125.931 127.567 1.00 49.54 ?  274 ARG A N     1 
ATOM   2196  C  CA    . ARG A 1 274 ? 136.009 125.969 126.205 1.00 48.60 ?  274 ARG A CA    1 
ATOM   2197  C  C     . ARG A 1 274 ? 135.430 127.340 125.882 1.00 48.89 ?  274 ARG A C     1 
ATOM   2198  O  O     . ARG A 1 274 ? 134.755 127.960 126.708 1.00 50.39 ?  274 ARG A O     1 
ATOM   2199  C  CB    . ARG A 1 274 ? 134.943 124.889 126.017 1.00 49.61 ?  274 ARG A CB    1 
ATOM   2200  C  CG    . ARG A 1 274 ? 134.547 124.640 124.573 1.00 48.02 ?  274 ARG A CG    1 
ATOM   2201  C  CD    . ARG A 1 274 ? 135.461 123.612 123.925 1.00 48.62 ?  274 ARG A CD    1 
ATOM   2202  N  NE    . ARG A 1 274 ? 135.296 123.555 122.477 1.00 51.37 ?  274 ARG A NE    1 
ATOM   2203  C  CZ    . ARG A 1 274 ? 135.435 124.591 121.660 1.00 49.76 ?  274 ARG A CZ    1 
ATOM   2204  N  NH1   . ARG A 1 274 ? 135.752 125.792 122.114 1.00 45.00 1  274 ARG A NH1   1 
ATOM   2205  N  NH2   . ARG A 1 274 ? 135.255 124.416 120.355 1.00 48.59 ?  274 ARG A NH2   1 
ATOM   2206  N  N     . VAL A 1 275 ? 135.699 127.813 124.667 1.00 37.65 ?  275 VAL A N     1 
ATOM   2207  C  CA    . VAL A 1 275 ? 135.168 129.076 124.167 1.00 36.21 ?  275 VAL A CA    1 
ATOM   2208  C  C     . VAL A 1 275 ? 134.340 128.739 122.934 1.00 42.73 ?  275 VAL A C     1 
ATOM   2209  O  O     . VAL A 1 275 ? 134.887 128.499 121.851 1.00 44.48 ?  275 VAL A O     1 
ATOM   2210  C  CB    . VAL A 1 275 ? 136.274 130.086 123.843 1.00 36.09 ?  275 VAL A CB    1 
ATOM   2211  C  CG1   . VAL A 1 275 ? 135.675 131.349 123.268 1.00 37.12 ?  275 VAL A CG1   1 
ATOM   2212  C  CG2   . VAL A 1 275 ? 137.086 130.400 125.089 1.00 34.21 ?  275 VAL A CG2   1 
ATOM   2213  N  N     . LYS A 1 276 ? 133.015 128.721 123.092 1.00 41.83 ?  276 LYS A N     1 
ATOM   2214  C  CA    . LYS A 1 276 ? 132.149 128.186 122.045 1.00 41.06 ?  276 LYS A CA    1 
ATOM   2215  C  C     . LYS A 1 276 ? 132.015 129.143 120.866 1.00 37.01 ?  276 LYS A C     1 
ATOM   2216  O  O     . LYS A 1 276 ? 132.074 128.716 119.707 1.00 45.04 ?  276 LYS A O     1 
ATOM   2217  C  CB    . LYS A 1 276 ? 130.774 127.864 122.627 1.00 41.69 ?  276 LYS A CB    1 
ATOM   2218  C  CG    . LYS A 1 276 ? 130.719 126.560 123.406 1.00 41.65 ?  276 LYS A CG    1 
ATOM   2219  C  CD    . LYS A 1 276 ? 129.502 126.510 124.316 1.00 41.95 ?  276 LYS A CD    1 
ATOM   2220  C  CE    . LYS A 1 276 ? 129.470 127.695 125.268 1.00 43.02 ?  276 LYS A CE    1 
ATOM   2221  N  NZ    . LYS A 1 276 ? 130.836 128.191 125.600 1.00 41.03 1  276 LYS A NZ    1 
ATOM   2222  N  N     . THR A 1 277 ? 131.831 130.433 121.132 1.00 33.19 ?  277 THR A N     1 
ATOM   2223  C  CA    . THR A 1 277 ? 131.431 131.388 120.106 1.00 31.91 ?  277 THR A CA    1 
ATOM   2224  C  C     . THR A 1 277 ? 132.579 132.235 119.574 1.00 34.60 ?  277 THR A C     1 
ATOM   2225  O  O     . THR A 1 277 ? 132.326 133.201 118.847 1.00 36.13 ?  277 THR A O     1 
ATOM   2226  C  CB    . THR A 1 277 ? 130.332 132.311 120.645 1.00 35.16 ?  277 THR A CB    1 
ATOM   2227  O  OG1   . THR A 1 277 ? 130.930 133.449 121.281 1.00 35.11 ?  277 THR A OG1   1 
ATOM   2228  C  CG2   . THR A 1 277 ? 129.464 131.574 121.651 1.00 35.02 ?  277 THR A CG2   1 
ATOM   2229  N  N     . LEU A 1 278 ? 133.822 131.911 119.907 1.00 29.37 ?  278 LEU A N     1 
ATOM   2230  C  CA    . LEU A 1 278 ? 134.963 132.736 119.534 1.00 22.84 ?  278 LEU A CA    1 
ATOM   2231  C  C     . LEU A 1 278 ? 135.871 131.956 118.594 1.00 24.15 ?  278 LEU A C     1 
ATOM   2232  O  O     . LEU A 1 278 ? 136.458 130.944 118.991 1.00 33.76 ?  278 LEU A O     1 
ATOM   2233  C  CB    . LEU A 1 278 ? 135.732 133.190 120.774 1.00 28.15 ?  278 LEU A CB    1 
ATOM   2234  C  CG    . LEU A 1 278 ? 136.599 134.441 120.638 1.00 28.27 ?  278 LEU A CG    1 
ATOM   2235  C  CD1   . LEU A 1 278 ? 135.730 135.677 120.478 1.00 19.40 ?  278 LEU A CD1   1 
ATOM   2236  C  CD2   . LEU A 1 278 ? 137.517 134.579 121.842 1.00 23.94 ?  278 LEU A CD2   1 
ATOM   2237  N  N     . SER A 1 279 ? 135.984 132.426 117.357 1.00 22.79 ?  279 SER A N     1 
ATOM   2238  C  CA    . SER A 1 279 ? 136.968 131.880 116.436 1.00 9.91  ?  279 SER A CA    1 
ATOM   2239  C  C     . SER A 1 279 ? 138.364 132.336 116.839 1.00 13.74 ?  279 SER A C     1 
ATOM   2240  O  O     . SER A 1 279 ? 138.550 133.417 117.402 1.00 24.52 ?  279 SER A O     1 
ATOM   2241  C  CB    . SER A 1 279 ? 136.664 132.315 115.004 1.00 15.14 ?  279 SER A CB    1 
ATOM   2242  O  OG    . SER A 1 279 ? 135.419 131.800 114.569 1.00 25.34 ?  279 SER A OG    1 
ATOM   2243  N  N     . ILE A 1 280 ? 139.355 131.499 116.552 1.00 18.08 ?  280 ILE A N     1 
ATOM   2244  C  CA    . ILE A 1 280 ? 140.731 131.757 116.955 1.00 17.25 ?  280 ILE A CA    1 
ATOM   2245  C  C     . ILE A 1 280 ? 141.624 131.709 115.725 1.00 13.23 ?  280 ILE A C     1 
ATOM   2246  O  O     . ILE A 1 280 ? 141.519 130.788 114.910 1.00 19.17 ?  280 ILE A O     1 
ATOM   2247  C  CB    . ILE A 1 280 ? 141.216 130.750 118.014 1.00 14.16 ?  280 ILE A CB    1 
ATOM   2248  C  CG1   . ILE A 1 280 ? 141.168 129.325 117.461 1.00 20.90 ?  280 ILE A CG1   1 
ATOM   2249  C  CG2   . ILE A 1 280 ? 140.389 130.873 119.280 1.00 15.09 ?  280 ILE A CG2   1 
ATOM   2250  C  CD1   . ILE A 1 280 ? 142.093 128.367 118.167 1.00 17.14 ?  280 ILE A CD1   1 
ATOM   2251  N  N     . GLY A 1 281 ? 142.489 132.707 115.591 1.00 11.70 ?  281 GLY A N     1 
ATOM   2252  C  CA    . GLY A 1 281 ? 143.513 132.709 114.568 1.00 2.98  ?  281 GLY A CA    1 
ATOM   2253  C  C     . GLY A 1 281 ? 144.882 132.832 115.205 1.00 1.52  ?  281 GLY A C     1 
ATOM   2254  O  O     . GLY A 1 281 ? 145.037 133.432 116.269 1.00 15.42 ?  281 GLY A O     1 
ATOM   2255  N  N     . VAL A 1 282 ? 145.879 132.250 114.548 1.00 20.67 ?  282 VAL A N     1 
ATOM   2256  C  CA    . VAL A 1 282 ? 147.258 132.280 115.017 1.00 10.29 ?  282 VAL A CA    1 
ATOM   2257  C  C     . VAL A 1 282 ? 148.098 133.046 114.007 1.00 4.73  ?  282 VAL A C     1 
ATOM   2258  O  O     . VAL A 1 282 ? 147.947 132.866 112.794 1.00 4.67  ?  282 VAL A O     1 
ATOM   2259  C  CB    . VAL A 1 282 ? 147.823 130.861 115.235 1.00 11.77 ?  282 VAL A CB    1 
ATOM   2260  C  CG1   . VAL A 1 282 ? 149.264 130.932 115.710 1.00 16.14 ?  282 VAL A CG1   1 
ATOM   2261  C  CG2   . VAL A 1 282 ? 146.969 130.101 116.235 1.00 18.28 ?  282 VAL A CG2   1 
ATOM   2262  N  N     . VAL A 1 283 ? 148.978 133.905 114.511 1.00 8.24  ?  283 VAL A N     1 
ATOM   2263  C  CA    . VAL A 1 283 ? 149.888 134.684 113.682 1.00 7.30  ?  283 VAL A CA    1 
ATOM   2264  C  C     . VAL A 1 283 ? 151.259 134.032 113.764 1.00 8.77  ?  283 VAL A C     1 
ATOM   2265  O  O     . VAL A 1 283 ? 151.851 133.942 114.846 1.00 17.43 ?  283 VAL A O     1 
ATOM   2266  C  CB    . VAL A 1 283 ? 149.940 136.153 114.129 1.00 9.04  ?  283 VAL A CB    1 
ATOM   2267  C  CG1   . VAL A 1 283 ? 150.732 136.983 113.134 1.00 7.42  ?  283 VAL A CG1   1 
ATOM   2268  C  CG2   . VAL A 1 283 ? 148.533 136.702 114.295 1.00 6.05  ?  283 VAL A CG2   1 
ATOM   2269  N  N     . ILE A 1 284 ? 151.765 133.578 112.623 1.00 18.40 ?  284 ILE A N     1 
ATOM   2270  C  CA    . ILE A 1 284 ? 152.977 132.771 112.551 1.00 13.48 ?  284 ILE A CA    1 
ATOM   2271  C  C     . ILE A 1 284 ? 154.041 133.581 111.811 1.00 19.53 ?  284 ILE A C     1 
ATOM   2272  O  O     . ILE A 1 284 ? 153.955 133.740 110.584 1.00 17.56 ?  284 ILE A O     1 
ATOM   2273  C  CB    . ILE A 1 284 ? 152.720 131.427 111.858 1.00 10.81 ?  284 ILE A CB    1 
ATOM   2274  C  CG1   . ILE A 1 284 ? 151.623 130.655 112.593 1.00 18.08 ?  284 ILE A CG1   1 
ATOM   2275  C  CG2   . ILE A 1 284 ? 153.998 130.611 111.786 1.00 13.41 ?  284 ILE A CG2   1 
ATOM   2276  C  CD1   . ILE A 1 284 ? 151.344 129.289 112.015 1.00 17.46 ?  284 ILE A CD1   1 
ATOM   2277  N  N     . PRO A 1 285 ? 155.046 134.110 112.501 1.00 22.61 ?  285 PRO A N     1 
ATOM   2278  C  CA    . PRO A 1 285 ? 156.163 134.754 111.804 1.00 24.25 ?  285 PRO A CA    1 
ATOM   2279  C  C     . PRO A 1 285 ? 157.051 133.727 111.117 1.00 23.30 ?  285 PRO A C     1 
ATOM   2280  O  O     . PRO A 1 285 ? 157.014 132.530 111.410 1.00 25.92 ?  285 PRO A O     1 
ATOM   2281  C  CB    . PRO A 1 285 ? 156.921 135.476 112.924 1.00 13.02 ?  285 PRO A CB    1 
ATOM   2282  C  CG    . PRO A 1 285 ? 155.989 135.476 114.100 1.00 19.84 ?  285 PRO A CG    1 
ATOM   2283  C  CD    . PRO A 1 285 ? 155.156 134.250 113.959 1.00 17.57 ?  285 PRO A CD    1 
ATOM   2284  N  N     . ASP A 1 286 ? 157.866 134.221 110.183 1.00 24.52 ?  286 ASP A N     1 
ATOM   2285  C  CA    . ASP A 1 286 ? 158.797 133.347 109.479 1.00 18.59 ?  286 ASP A CA    1 
ATOM   2286  C  C     . ASP A 1 286 ? 159.754 132.656 110.441 1.00 27.79 ?  286 ASP A C     1 
ATOM   2287  O  O     . ASP A 1 286 ? 160.253 131.566 110.142 1.00 31.34 ?  286 ASP A O     1 
ATOM   2288  C  CB    . ASP A 1 286 ? 159.583 134.144 108.437 1.00 21.56 ?  286 ASP A CB    1 
ATOM   2289  C  CG    . ASP A 1 286 ? 158.960 134.074 107.059 1.00 33.70 ?  286 ASP A CG    1 
ATOM   2290  O  OD1   . ASP A 1 286 ? 157.779 133.681 106.956 1.00 33.00 ?  286 ASP A OD1   1 
ATOM   2291  O  OD2   . ASP A 1 286 ? 159.652 134.411 106.077 1.00 38.28 -1 286 ASP A OD2   1 
ATOM   2292  N  N     . LYS A 1 287 ? 160.024 133.273 111.594 1.00 27.82 ?  287 LYS A N     1 
ATOM   2293  C  CA    . LYS A 1 287 ? 160.945 132.679 112.557 1.00 21.83 ?  287 LYS A CA    1 
ATOM   2294  C  C     . LYS A 1 287 ? 160.446 131.325 113.042 1.00 20.83 ?  287 LYS A C     1 
ATOM   2295  O  O     . LYS A 1 287 ? 161.232 130.384 113.190 1.00 27.76 ?  287 LYS A O     1 
ATOM   2296  C  CB    . LYS A 1 287 ? 161.155 133.626 113.737 1.00 23.47 ?  287 LYS A CB    1 
ATOM   2297  C  CG    . LYS A 1 287 ? 162.299 133.222 114.648 1.00 24.04 ?  287 LYS A CG    1 
ATOM   2298  C  CD    . LYS A 1 287 ? 163.572 133.008 113.851 1.00 29.40 ?  287 LYS A CD    1 
ATOM   2299  C  CE    . LYS A 1 287 ? 164.760 132.764 114.759 1.00 28.82 ?  287 LYS A CE    1 
ATOM   2300  N  NZ    . LYS A 1 287 ? 166.037 132.732 113.997 1.00 29.89 1  287 LYS A NZ    1 
ATOM   2301  N  N     . PHE A 1 288 ? 159.145 131.208 113.310 1.00 21.04 ?  288 PHE A N     1 
ATOM   2302  C  CA    . PHE A 1 288 ? 158.605 129.936 113.777 1.00 19.62 ?  288 PHE A CA    1 
ATOM   2303  C  C     . PHE A 1 288 ? 158.744 128.852 112.716 1.00 25.33 ?  288 PHE A C     1 
ATOM   2304  O  O     . PHE A 1 288 ? 159.103 127.710 113.025 1.00 30.75 ?  288 PHE A O     1 
ATOM   2305  C  CB    . PHE A 1 288 ? 157.144 130.105 114.185 1.00 21.23 ?  288 PHE A CB    1 
ATOM   2306  C  CG    . PHE A 1 288 ? 156.578 128.917 114.901 1.00 21.23 ?  288 PHE A CG    1 
ATOM   2307  C  CD1   . PHE A 1 288 ? 156.688 128.804 116.276 1.00 22.02 ?  288 PHE A CD1   1 
ATOM   2308  C  CD2   . PHE A 1 288 ? 155.938 127.911 114.200 1.00 19.94 ?  288 PHE A CD2   1 
ATOM   2309  C  CE1   . PHE A 1 288 ? 156.169 127.710 116.936 1.00 24.99 ?  288 PHE A CE1   1 
ATOM   2310  C  CE2   . PHE A 1 288 ? 155.417 126.816 114.856 1.00 20.56 ?  288 PHE A CE2   1 
ATOM   2311  C  CZ    . PHE A 1 288 ? 155.533 126.716 116.226 1.00 23.16 ?  288 PHE A CZ    1 
ATOM   2312  N  N     . VAL A 1 289 ? 158.452 129.188 111.459 1.00 24.09 ?  289 VAL A N     1 
ATOM   2313  C  CA    . VAL A 1 289 ? 158.591 128.213 110.383 1.00 24.98 ?  289 VAL A CA    1 
ATOM   2314  C  C     . VAL A 1 289 ? 160.048 127.801 110.230 1.00 27.24 ?  289 VAL A C     1 
ATOM   2315  O  O     . VAL A 1 289 ? 160.356 126.629 109.988 1.00 29.43 ?  289 VAL A O     1 
ATOM   2316  C  CB    . VAL A 1 289 ? 158.017 128.776 109.071 1.00 29.12 ?  289 VAL A CB    1 
ATOM   2317  C  CG1   . VAL A 1 289 ? 158.069 127.724 107.976 1.00 23.61 ?  289 VAL A CG1   1 
ATOM   2318  C  CG2   . VAL A 1 289 ? 156.595 129.265 109.284 1.00 17.98 ?  289 VAL A CG2   1 
ATOM   2319  N  N     . GLU A 1 290 ? 160.967 128.758 110.368 1.00 31.13 ?  290 GLU A N     1 
ATOM   2320  C  CA    . GLU A 1 290 ? 162.389 128.435 110.306 1.00 26.58 ?  290 GLU A CA    1 
ATOM   2321  C  C     . GLU A 1 290 ? 162.793 127.503 111.441 1.00 32.07 ?  290 GLU A C     1 
ATOM   2322  O  O     . GLU A 1 290 ? 163.572 126.566 111.238 1.00 39.10 ?  290 GLU A O     1 
ATOM   2323  C  CB    . GLU A 1 290 ? 163.215 129.720 110.344 1.00 29.39 ?  290 GLU A CB    1 
ATOM   2324  C  CG    . GLU A 1 290 ? 164.711 129.493 110.460 1.00 38.87 ?  290 GLU A CG    1 
ATOM   2325  C  CD    . GLU A 1 290 ? 165.451 130.725 110.937 1.00 43.21 ?  290 GLU A CD    1 
ATOM   2326  O  OE1   . GLU A 1 290 ? 165.207 131.819 110.385 1.00 43.15 ?  290 GLU A OE1   1 
ATOM   2327  O  OE2   . GLU A 1 290 ? 166.277 130.601 111.864 1.00 36.98 -1 290 GLU A OE2   1 
ATOM   2328  N  N     . LEU A 1 291 ? 162.278 127.753 112.647 1.00 25.93 ?  291 LEU A N     1 
ATOM   2329  C  CA    . LEU A 1 291 ? 162.607 126.903 113.785 1.00 25.67 ?  291 LEU A CA    1 
ATOM   2330  C  C     . LEU A 1 291 ? 162.068 125.491 113.596 1.00 29.23 ?  291 LEU A C     1 
ATOM   2331  O  O     . LEU A 1 291 ? 162.748 124.512 113.923 1.00 37.20 ?  291 LEU A O     1 
ATOM   2332  C  CB    . LEU A 1 291 ? 162.059 127.516 115.074 1.00 30.21 ?  291 LEU A CB    1 
ATOM   2333  C  CG    . LEU A 1 291 ? 162.633 128.869 115.500 1.00 30.90 ?  291 LEU A CG    1 
ATOM   2334  C  CD1   . LEU A 1 291 ? 161.821 129.459 116.641 1.00 24.81 ?  291 LEU A CD1   1 
ATOM   2335  C  CD2   . LEU A 1 291 ? 164.094 128.736 115.887 1.00 27.65 ?  291 LEU A CD2   1 
ATOM   2336  N  N     . ALA A 1 292 ? 160.846 125.367 113.076 1.00 30.57 ?  292 ALA A N     1 
ATOM   2337  C  CA    . ALA A 1 292 ? 160.272 124.043 112.852 1.00 22.63 ?  292 ALA A CA    1 
ATOM   2338  C  C     . ALA A 1 292 ? 160.992 123.311 111.725 1.00 23.61 ?  292 ALA A C     1 
ATOM   2339  O  O     . ALA A 1 292 ? 161.163 122.088 111.781 1.00 27.40 ?  292 ALA A O     1 
ATOM   2340  C  CB    . ALA A 1 292 ? 158.780 124.161 112.552 1.00 25.00 ?  292 ALA A CB    1 
ATOM   2341  N  N     . ARG A 1 293 ? 161.419 124.042 110.694 1.00 32.85 ?  293 ARG A N     1 
ATOM   2342  C  CA    . ARG A 1 293 ? 162.108 123.412 109.573 1.00 33.50 ?  293 ARG A CA    1 
ATOM   2343  C  C     . ARG A 1 293 ? 163.432 122.801 110.010 1.00 36.87 ?  293 ARG A C     1 
ATOM   2344  O  O     . ARG A 1 293 ? 163.803 121.711 109.557 1.00 41.04 ?  293 ARG A O     1 
ATOM   2345  C  CB    . ARG A 1 293 ? 162.328 124.434 108.458 1.00 31.28 ?  293 ARG A CB    1 
ATOM   2346  C  CG    . ARG A 1 293 ? 163.323 123.998 107.402 1.00 33.73 ?  293 ARG A CG    1 
ATOM   2347  C  CD    . ARG A 1 293 ? 163.220 124.869 106.165 1.00 38.14 ?  293 ARG A CD    1 
ATOM   2348  N  NE    . ARG A 1 293 ? 163.603 126.250 106.433 1.00 39.04 ?  293 ARG A NE    1 
ATOM   2349  C  CZ    . ARG A 1 293 ? 162.757 127.270 106.460 1.00 37.39 ?  293 ARG A CZ    1 
ATOM   2350  N  NH1   . ARG A 1 293 ? 161.463 127.100 106.246 1.00 31.67 1  293 ARG A NH1   1 
ATOM   2351  N  NH2   . ARG A 1 293 ? 163.221 128.491 106.705 1.00 35.16 ?  293 ARG A NH2   1 
ATOM   2352  N  N     . GLU A 1 294 ? 164.159 123.486 110.886 1.00 37.78 ?  294 GLU A N     1 
ATOM   2353  C  CA    . GLU A 1 294 ? 165.427 122.990 111.403 1.00 37.00 ?  294 GLU A CA    1 
ATOM   2354  C  C     . GLU A 1 294 ? 165.256 122.095 112.622 1.00 37.33 ?  294 GLU A C     1 
ATOM   2355  O  O     . GLU A 1 294 ? 166.257 121.636 113.179 1.00 43.13 ?  294 GLU A O     1 
ATOM   2356  C  CB    . GLU A 1 294 ? 166.349 124.161 111.750 1.00 34.88 ?  294 GLU A CB    1 
ATOM   2357  C  CG    . GLU A 1 294 ? 166.476 125.198 110.649 1.00 35.88 ?  294 GLU A CG    1 
ATOM   2358  C  CD    . GLU A 1 294 ? 166.619 126.606 111.193 1.00 46.62 ?  294 GLU A CD    1 
ATOM   2359  O  OE1   . GLU A 1 294 ? 166.432 126.794 112.414 1.00 46.88 ?  294 GLU A OE1   1 
ATOM   2360  O  OE2   . GLU A 1 294 ? 166.919 127.523 110.401 1.00 46.27 -1 294 GLU A OE2   1 
ATOM   2361  N  N     . ASP A 1 295 ? 164.020 121.844 113.051 1.00 34.26 ?  295 ASP A N     1 
ATOM   2362  C  CA    . ASP A 1 295 ? 163.731 121.006 114.210 1.00 35.24 ?  295 ASP A CA    1 
ATOM   2363  C  C     . ASP A 1 295 ? 164.338 121.564 115.491 1.00 39.67 ?  295 ASP A C     1 
ATOM   2364  O  O     . ASP A 1 295 ? 164.427 120.858 116.501 1.00 39.11 ?  295 ASP A O     1 
ATOM   2365  C  CB    . ASP A 1 295 ? 164.208 119.567 113.983 1.00 37.98 ?  295 ASP A CB    1 
ATOM   2366  C  CG    . ASP A 1 295 ? 163.282 118.540 114.602 1.00 43.02 ?  295 ASP A CG    1 
ATOM   2367  O  OD1   . ASP A 1 295 ? 162.363 118.938 115.349 1.00 40.66 ?  295 ASP A OD1   1 
ATOM   2368  O  OD2   . ASP A 1 295 ? 163.472 117.335 114.340 1.00 40.33 -1 295 ASP A OD2   1 
ATOM   2369  N  N     . LYS A 1 296 ? 164.757 122.825 115.465 1.00 39.92 ?  296 LYS A N     1 
ATOM   2370  C  CA    . LYS A 1 296 ? 165.347 123.452 116.639 1.00 39.25 ?  296 LYS A CA    1 
ATOM   2371  C  C     . LYS A 1 296 ? 164.298 123.660 117.723 1.00 39.31 ?  296 LYS A C     1 
ATOM   2372  O  O     . LYS A 1 296 ? 163.114 123.868 117.445 1.00 41.50 ?  296 LYS A O     1 
ATOM   2373  C  CB    . LYS A 1 296 ? 165.978 124.793 116.265 1.00 37.45 ?  296 LYS A CB    1 
ATOM   2374  C  CG    . LYS A 1 296 ? 167.206 124.683 115.382 1.00 37.85 ?  296 LYS A CG    1 
ATOM   2375  C  CD    . LYS A 1 296 ? 167.756 126.057 115.035 1.00 39.42 ?  296 LYS A CD    1 
ATOM   2376  C  CE    . LYS A 1 296 ? 168.996 125.954 114.162 1.00 38.50 ?  296 LYS A CE    1 
ATOM   2377  N  NZ    . LYS A 1 296 ? 169.379 127.272 113.586 1.00 40.21 1  296 LYS A NZ    1 
ATOM   2378  N  N     . ALA A 1 297 ? 164.744 123.594 118.974 1.00 35.70 ?  297 ALA A N     1 
ATOM   2379  C  CA    . ALA A 1 297 ? 163.863 123.902 120.091 1.00 36.32 ?  297 ALA A CA    1 
ATOM   2380  C  C     . ALA A 1 297 ? 163.546 125.392 120.100 1.00 36.78 ?  297 ALA A C     1 
ATOM   2381  O  O     . ALA A 1 297 ? 164.444 126.230 119.979 1.00 42.72 ?  297 ALA A O     1 
ATOM   2382  C  CB    . ALA A 1 297 ? 164.509 123.486 121.411 1.00 37.50 ?  297 ALA A CB    1 
ATOM   2383  N  N     . ALA A 1 298 ? 162.269 125.722 120.240 1.00 29.21 ?  298 ALA A N     1 
ATOM   2384  C  CA    . ALA A 1 298 ? 161.812 127.102 120.237 1.00 29.37 ?  298 ALA A CA    1 
ATOM   2385  C  C     . ALA A 1 298 ? 161.335 127.498 121.627 1.00 28.51 ?  298 ALA A C     1 
ATOM   2386  O  O     . ALA A 1 298 ? 161.145 126.663 122.512 1.00 32.57 ?  298 ALA A O     1 
ATOM   2387  C  CB    . ALA A 1 298 ? 160.696 127.306 119.207 1.00 29.64 ?  298 ALA A CB    1 
ATOM   2388  N  N     . TYR A 1 299 ? 161.148 128.801 121.809 1.00 26.72 ?  299 TYR A N     1 
ATOM   2389  C  CA    . TYR A 1 299 ? 160.688 129.353 123.071 1.00 27.93 ?  299 TYR A CA    1 
ATOM   2390  C  C     . TYR A 1 299 ? 159.472 130.231 122.835 1.00 28.57 ?  299 TYR A C     1 
ATOM   2391  O  O     . TYR A 1 299 ? 159.400 130.955 121.837 1.00 34.09 ?  299 TYR A O     1 
ATOM   2392  C  CB    . TYR A 1 299 ? 161.790 130.169 123.760 1.00 26.43 ?  299 TYR A CB    1 
ATOM   2393  C  CG    . TYR A 1 299 ? 162.973 129.344 124.203 1.00 29.08 ?  299 TYR A CG    1 
ATOM   2394  C  CD1   . TYR A 1 299 ? 164.050 129.131 123.356 1.00 27.39 ?  299 TYR A CD1   1 
ATOM   2395  C  CD2   . TYR A 1 299 ? 163.011 128.777 125.469 1.00 29.78 ?  299 TYR A CD2   1 
ATOM   2396  C  CE1   . TYR A 1 299 ? 165.134 128.377 123.756 1.00 29.88 ?  299 TYR A CE1   1 
ATOM   2397  C  CE2   . TYR A 1 299 ? 164.090 128.020 125.878 1.00 33.58 ?  299 TYR A CE2   1 
ATOM   2398  C  CZ    . TYR A 1 299 ? 165.149 127.824 125.020 1.00 36.69 ?  299 TYR A CZ    1 
ATOM   2399  O  OH    . TYR A 1 299 ? 166.228 127.072 125.424 1.00 39.80 ?  299 TYR A OH    1 
ATOM   2400  N  N     . VAL A 1 300 ? 158.517 130.155 123.750 1.00 31.06 ?  300 VAL A N     1 
ATOM   2401  C  CA    . VAL A 1 300 ? 157.397 131.083 123.803 1.00 24.84 ?  300 VAL A CA    1 
ATOM   2402  C  C     . VAL A 1 300 ? 157.648 132.036 124.959 1.00 22.95 ?  300 VAL A C     1 
ATOM   2403  O  O     . VAL A 1 300 ? 158.032 131.616 126.057 1.00 28.79 ?  300 VAL A O     1 
ATOM   2404  C  CB    . VAL A 1 300 ? 156.055 130.346 123.959 1.00 23.88 ?  300 VAL A CB    1 
ATOM   2405  C  CG1   . VAL A 1 300 ? 155.657 129.697 122.646 1.00 23.03 ?  300 VAL A CG1   1 
ATOM   2406  C  CG2   . VAL A 1 300 ? 156.142 129.311 125.066 1.00 24.43 ?  300 VAL A CG2   1 
ATOM   2407  N  N     . PHE A 1 301 ? 157.440 133.322 124.716 1.00 22.94 ?  301 PHE A N     1 
ATOM   2408  C  CA    . PHE A 1 301 ? 157.859 134.357 125.644 1.00 19.43 ?  301 PHE A CA    1 
ATOM   2409  C  C     . PHE A 1 301 ? 156.670 134.911 126.412 1.00 23.22 ?  301 PHE A C     1 
ATOM   2410  O  O     . PHE A 1 301 ? 155.536 134.913 125.927 1.00 26.83 ?  301 PHE A O     1 
ATOM   2411  C  CB    . PHE A 1 301 ? 158.573 135.487 124.902 1.00 18.45 ?  301 PHE A CB    1 
ATOM   2412  C  CG    . PHE A 1 301 ? 159.615 135.005 123.937 1.00 17.87 ?  301 PHE A CG    1 
ATOM   2413  C  CD1   . PHE A 1 301 ? 160.913 134.781 124.358 1.00 19.99 ?  301 PHE A CD1   1 
ATOM   2414  C  CD2   . PHE A 1 301 ? 159.293 134.763 122.614 1.00 16.92 ?  301 PHE A CD2   1 
ATOM   2415  C  CE1   . PHE A 1 301 ? 161.872 134.331 123.476 1.00 27.38 ?  301 PHE A CE1   1 
ATOM   2416  C  CE2   . PHE A 1 301 ? 160.248 134.313 121.728 1.00 18.48 ?  301 PHE A CE2   1 
ATOM   2417  C  CZ    . PHE A 1 301 ? 161.540 134.097 122.160 1.00 26.27 ?  301 PHE A CZ    1 
ATOM   2418  N  N     . TYR A 1 302 ? 156.943 135.367 127.629 1.00 26.31 ?  302 TYR A N     1 
ATOM   2419  C  CA    . TYR A 1 302 ? 155.951 136.071 128.425 1.00 20.27 ?  302 TYR A CA    1 
ATOM   2420  C  C     . TYR A 1 302 ? 155.943 137.527 127.982 1.00 22.18 ?  302 TYR A C     1 
ATOM   2421  O  O     . TYR A 1 302 ? 156.938 138.240 128.165 1.00 24.02 ?  302 TYR A O     1 
ATOM   2422  C  CB    . TYR A 1 302 ? 156.262 135.941 129.916 1.00 22.45 ?  302 TYR A CB    1 
ATOM   2423  C  CG    . TYR A 1 302 ? 156.037 134.548 130.459 1.00 18.56 ?  302 TYR A CG    1 
ATOM   2424  C  CD1   . TYR A 1 302 ? 156.932 133.523 130.186 1.00 21.59 ?  302 TYR A CD1   1 
ATOM   2425  C  CD2   . TYR A 1 302 ? 154.928 134.258 131.239 1.00 20.28 ?  302 TYR A CD2   1 
ATOM   2426  C  CE1   . TYR A 1 302 ? 156.730 132.250 130.677 1.00 20.62 ?  302 TYR A CE1   1 
ATOM   2427  C  CE2   . TYR A 1 302 ? 154.718 132.987 131.736 1.00 24.17 ?  302 TYR A CE2   1 
ATOM   2428  C  CZ    . TYR A 1 302 ? 155.621 131.986 131.451 1.00 27.85 ?  302 TYR A CZ    1 
ATOM   2429  O  OH    . TYR A 1 302 ? 155.415 130.718 131.944 1.00 32.06 ?  302 TYR A OH    1 
ATOM   2430  N  N     . PRO A 1 303 ? 154.843 138.002 127.392 1.00 21.76 ?  303 PRO A N     1 
ATOM   2431  C  CA    . PRO A 1 303 ? 154.877 139.327 126.747 1.00 20.00 ?  303 PRO A CA    1 
ATOM   2432  C  C     . PRO A 1 303 ? 155.241 140.462 127.686 1.00 21.87 ?  303 PRO A C     1 
ATOM   2433  O  O     . PRO A 1 303 ? 155.929 141.402 127.269 1.00 29.71 ?  303 PRO A O     1 
ATOM   2434  C  CB    . PRO A 1 303 ? 153.450 139.479 126.199 1.00 19.58 ?  303 PRO A CB    1 
ATOM   2435  C  CG    . PRO A 1 303 ? 152.926 138.091 126.104 1.00 21.86 ?  303 PRO A CG    1 
ATOM   2436  C  CD    . PRO A 1 303 ? 153.535 137.345 127.240 1.00 15.00 ?  303 PRO A CD    1 
ATOM   2437  N  N     . HIS A 1 304 ? 154.799 140.408 128.944 1.00 21.32 ?  304 HIS A N     1 
ATOM   2438  C  CA    . HIS A 1 304 ? 155.056 141.526 129.843 1.00 21.76 ?  304 HIS A CA    1 
ATOM   2439  C  C     . HIS A 1 304 ? 156.531 141.643 130.198 1.00 23.88 ?  304 HIS A C     1 
ATOM   2440  O  O     . HIS A 1 304 ? 157.031 142.756 130.382 1.00 30.71 ?  304 HIS A O     1 
ATOM   2441  C  CB    . HIS A 1 304 ? 154.216 141.398 131.112 1.00 24.40 ?  304 HIS A CB    1 
ATOM   2442  C  CG    . HIS A 1 304 ? 154.209 142.638 131.950 1.00 23.67 ?  304 HIS A CG    1 
ATOM   2443  N  ND1   . HIS A 1 304 ? 154.255 142.608 133.326 1.00 29.90 ?  304 HIS A ND1   1 
ATOM   2444  C  CD2   . HIS A 1 304 ? 154.172 143.946 131.602 1.00 23.54 ?  304 HIS A CD2   1 
ATOM   2445  C  CE1   . HIS A 1 304 ? 154.241 143.844 133.791 1.00 27.67 ?  304 HIS A CE1   1 
ATOM   2446  N  NE2   . HIS A 1 304 ? 154.191 144.675 132.765 1.00 29.14 ?  304 HIS A NE2   1 
ATOM   2447  N  N     . THR A 1 305 ? 157.245 140.521 130.297 1.00 20.70 ?  305 THR A N     1 
ATOM   2448  C  CA    . THR A 1 305 ? 158.682 140.601 130.533 1.00 21.11 ?  305 THR A CA    1 
ATOM   2449  C  C     . THR A 1 305 ? 159.384 141.307 129.379 1.00 22.04 ?  305 THR A C     1 
ATOM   2450  O  O     . THR A 1 305 ? 160.262 142.148 129.598 1.00 31.28 ?  305 THR A O     1 
ATOM   2451  C  CB    . THR A 1 305 ? 159.266 139.203 130.742 1.00 22.84 ?  305 THR A CB    1 
ATOM   2452  O  OG1   . THR A 1 305 ? 159.238 138.479 129.507 1.00 30.92 ?  305 THR A OG1   1 
ATOM   2453  C  CG2   . THR A 1 305 ? 158.463 138.446 131.786 1.00 23.35 ?  305 THR A CG2   1 
ATOM   2454  N  N     . ILE A 1 306 ? 158.992 140.992 128.143 1.00 26.16 ?  306 ILE A N     1 
ATOM   2455  C  CA    . ILE A 1 306 ? 159.563 141.672 126.984 1.00 25.10 ?  306 ILE A CA    1 
ATOM   2456  C  C     . ILE A 1 306 ? 159.219 143.155 127.012 1.00 22.56 ?  306 ILE A C     1 
ATOM   2457  O  O     . ILE A 1 306 ? 160.070 144.011 126.742 1.00 27.10 ?  306 ILE A O     1 
ATOM   2458  C  CB    . ILE A 1 306 ? 159.083 141.003 125.683 1.00 21.72 ?  306 ILE A CB    1 
ATOM   2459  C  CG1   . ILE A 1 306 ? 159.770 139.650 125.493 1.00 21.27 ?  306 ILE A CG1   1 
ATOM   2460  C  CG2   . ILE A 1 306 ? 159.337 141.911 124.490 1.00 21.73 ?  306 ILE A CG2   1 
ATOM   2461  C  CD1   . ILE A 1 306 ? 159.237 138.857 124.327 1.00 24.02 ?  306 ILE A CD1   1 
ATOM   2462  N  N     . TYR A 1 307 ? 157.965 143.481 127.328 1.00 28.01 ?  307 TYR A N     1 
ATOM   2463  C  CA    . TYR A 1 307 ? 157.551 144.881 127.360 1.00 26.26 ?  307 TYR A CA    1 
ATOM   2464  C  C     . TYR A 1 307 ? 158.326 145.664 128.412 1.00 27.25 ?  307 TYR A C     1 
ATOM   2465  O  O     . TYR A 1 307 ? 158.722 146.812 128.178 1.00 30.25 ?  307 TYR A O     1 
ATOM   2466  C  CB    . TYR A 1 307 ? 156.047 144.977 127.617 1.00 21.38 ?  307 TYR A CB    1 
ATOM   2467  C  CG    . TYR A 1 307 ? 155.537 146.393 127.731 1.00 26.74 ?  307 TYR A CG    1 
ATOM   2468  C  CD1   . TYR A 1 307 ? 155.284 147.154 126.599 1.00 24.71 ?  307 TYR A CD1   1 
ATOM   2469  C  CD2   . TYR A 1 307 ? 155.313 146.971 128.972 1.00 28.34 ?  307 TYR A CD2   1 
ATOM   2470  C  CE1   . TYR A 1 307 ? 154.822 148.449 126.699 1.00 26.43 ?  307 TYR A CE1   1 
ATOM   2471  C  CE2   . TYR A 1 307 ? 154.853 148.266 129.083 1.00 27.16 ?  307 TYR A CE2   1 
ATOM   2472  C  CZ    . TYR A 1 307 ? 154.608 149.000 127.943 1.00 31.59 ?  307 TYR A CZ    1 
ATOM   2473  O  OH    . TYR A 1 307 ? 154.145 150.291 128.048 1.00 34.08 ?  307 TYR A OH    1 
ATOM   2474  N  N     . LYS A 1 308 ? 158.544 145.064 129.582 1.00 27.54 ?  308 LYS A N     1 
ATOM   2475  C  CA    . LYS A 1 308 ? 159.316 145.727 130.625 1.00 27.50 ?  308 LYS A CA    1 
ATOM   2476  C  C     . LYS A 1 308 ? 160.778 145.875 130.225 1.00 27.38 ?  308 LYS A C     1 
ATOM   2477  O  O     . LYS A 1 308 ? 161.394 146.916 130.477 1.00 33.42 ?  308 LYS A O     1 
ATOM   2478  C  CB    . LYS A 1 308 ? 159.190 144.956 131.937 1.00 27.28 ?  308 LYS A CB    1 
ATOM   2479  C  CG    . LYS A 1 308 ? 157.881 145.198 132.669 1.00 26.79 ?  308 LYS A CG    1 
ATOM   2480  C  CD    . LYS A 1 308 ? 157.872 144.528 134.031 1.00 32.68 ?  308 LYS A CD    1 
ATOM   2481  C  CE    . LYS A 1 308 ? 158.419 143.113 133.951 1.00 35.77 ?  308 LYS A CE    1 
ATOM   2482  N  NZ    . LYS A 1 308 ? 157.329 142.098 133.930 1.00 31.06 1  308 LYS A NZ    1 
ATOM   2483  N  N     . GLU A 1 309 ? 161.350 144.845 129.597 1.00 28.15 ?  309 GLU A N     1 
ATOM   2484  C  CA    . GLU A 1 309 ? 162.760 144.897 129.228 1.00 29.71 ?  309 GLU A CA    1 
ATOM   2485  C  C     . GLU A 1 309 ? 163.017 145.921 128.130 1.00 34.09 ?  309 GLU A C     1 
ATOM   2486  O  O     . GLU A 1 309 ? 164.043 146.612 128.148 1.00 36.59 ?  309 GLU A O     1 
ATOM   2487  C  CB    . GLU A 1 309 ? 163.234 143.512 128.789 1.00 26.11 ?  309 GLU A CB    1 
ATOM   2488  C  CG    . GLU A 1 309 ? 164.639 143.492 128.222 1.00 35.09 ?  309 GLU A CG    1 
ATOM   2489  C  CD    . GLU A 1 309 ? 165.689 143.831 129.259 1.00 39.96 ?  309 GLU A CD    1 
ATOM   2490  O  OE1   . GLU A 1 309 ? 165.362 143.810 130.464 1.00 37.09 ?  309 GLU A OE1   1 
ATOM   2491  O  OE2   . GLU A 1 309 ? 166.840 144.117 128.871 1.00 41.57 -1 309 GLU A OE2   1 
ATOM   2492  N  N     . TYR A 1 310 ? 162.101 146.039 127.169 1.00 32.87 ?  310 TYR A N     1 
ATOM   2493  C  CA    . TYR A 1 310 ? 162.328 146.862 125.991 1.00 25.52 ?  310 TYR A CA    1 
ATOM   2494  C  C     . TYR A 1 310 ? 161.379 148.042 125.860 1.00 29.46 ?  310 TYR A C     1 
ATOM   2495  O  O     . TYR A 1 310 ? 161.564 148.858 124.950 1.00 34.95 ?  310 TYR A O     1 
ATOM   2496  C  CB    . TYR A 1 310 ? 162.231 146.004 124.721 1.00 27.02 ?  310 TYR A CB    1 
ATOM   2497  C  CG    . TYR A 1 310 ? 163.238 144.879 124.672 1.00 29.74 ?  310 TYR A CG    1 
ATOM   2498  C  CD1   . TYR A 1 310 ? 164.504 145.077 124.141 1.00 27.44 ?  310 TYR A CD1   1 
ATOM   2499  C  CD2   . TYR A 1 310 ? 162.923 143.619 125.163 1.00 26.49 ?  310 TYR A CD2   1 
ATOM   2500  C  CE1   . TYR A 1 310 ? 165.426 144.053 124.099 1.00 28.34 ?  310 TYR A CE1   1 
ATOM   2501  C  CE2   . TYR A 1 310 ? 163.839 142.590 125.126 1.00 27.42 ?  310 TYR A CE2   1 
ATOM   2502  C  CZ    . TYR A 1 310 ? 165.089 142.812 124.591 1.00 29.82 ?  310 TYR A CZ    1 
ATOM   2503  O  OH    . TYR A 1 310 ? 166.007 141.790 124.549 1.00 33.31 ?  310 TYR A OH    1 
ATOM   2504  N  N     . GLY A 1 311 ? 160.377 148.164 126.727 1.00 24.55 ?  311 GLY A N     1 
ATOM   2505  C  CA    . GLY A 1 311 ? 159.437 149.258 126.609 1.00 29.06 ?  311 GLY A CA    1 
ATOM   2506  C  C     . GLY A 1 311 ? 158.523 149.185 125.411 1.00 28.29 ?  311 GLY A C     1 
ATOM   2507  O  O     . GLY A 1 311 ? 157.806 150.152 125.138 1.00 35.81 ?  311 GLY A O     1 
ATOM   2508  N  N     . GLN A 1 312 ? 158.530 148.073 124.681 1.00 27.39 ?  312 GLN A N     1 
ATOM   2509  C  CA    . GLN A 1 312 ? 157.634 147.863 123.555 1.00 26.24 ?  312 GLN A CA    1 
ATOM   2510  C  C     . GLN A 1 312 ? 157.056 146.459 123.631 1.00 29.53 ?  312 GLN A C     1 
ATOM   2511  O  O     . GLN A 1 312 ? 157.650 145.555 124.223 1.00 30.24 ?  312 GLN A O     1 
ATOM   2512  C  CB    . GLN A 1 312 ? 158.346 148.069 122.213 1.00 26.60 ?  312 GLN A CB    1 
ATOM   2513  C  CG    . GLN A 1 312 ? 159.847 147.875 122.264 1.00 33.29 ?  312 GLN A CG    1 
ATOM   2514  C  CD    . GLN A 1 312 ? 160.530 148.293 120.978 1.00 36.07 ?  312 GLN A CD    1 
ATOM   2515  O  OE1   . GLN A 1 312 ? 159.890 148.415 119.934 1.00 35.30 ?  312 GLN A OE1   1 
ATOM   2516  N  NE2   . GLN A 1 312 ? 161.838 148.510 121.046 1.00 32.34 ?  312 GLN A NE2   1 
ATOM   2517  N  N     . HIS A 1 313 ? 155.885 146.289 123.027 1.00 27.72 ?  313 HIS A N     1 
ATOM   2518  C  CA    . HIS A 1 313 ? 155.200 145.007 123.062 1.00 21.37 ?  313 HIS A CA    1 
ATOM   2519  C  C     . HIS A 1 313 ? 155.925 143.978 122.203 1.00 25.03 ?  313 HIS A C     1 
ATOM   2520  O  O     . HIS A 1 313 ? 156.610 144.312 121.234 1.00 30.70 ?  313 HIS A O     1 
ATOM   2521  C  CB    . HIS A 1 313 ? 153.758 145.167 122.587 1.00 23.52 ?  313 HIS A CB    1 
ATOM   2522  C  CG    . HIS A 1 313 ? 152.943 146.085 123.442 1.00 25.52 ?  313 HIS A CG    1 
ATOM   2523  N  ND1   . HIS A 1 313 ? 152.328 145.669 124.603 1.00 25.05 ?  313 HIS A ND1   1 
ATOM   2524  C  CD2   . HIS A 1 313 ? 152.644 147.399 123.307 1.00 26.44 ?  313 HIS A CD2   1 
ATOM   2525  C  CE1   . HIS A 1 313 ? 151.683 146.687 125.145 1.00 24.26 ?  313 HIS A CE1   1 
ATOM   2526  N  NE2   . HIS A 1 313 ? 151.859 147.748 124.378 1.00 25.04 ?  313 HIS A NE2   1 
ATOM   2527  N  N     . MET A 1 314 ? 155.763 142.704 122.573 1.00 32.55 ?  314 MET A N     1 
ATOM   2528  C  CA    . MET A 1 314 ? 156.388 141.629 121.811 1.00 24.31 ?  314 MET A CA    1 
ATOM   2529  C  C     . MET A 1 314 ? 155.876 141.600 120.378 1.00 31.07 ?  314 MET A C     1 
ATOM   2530  O  O     . MET A 1 314 ? 156.655 141.421 119.435 1.00 35.42 ?  314 MET A O     1 
ATOM   2531  C  CB    . MET A 1 314 ? 156.139 140.285 122.494 1.00 17.50 ?  314 MET A CB    1 
ATOM   2532  C  CG    . MET A 1 314 ? 156.955 139.141 121.916 1.00 25.56 ?  314 MET A CG    1 
ATOM   2533  S  SD    . MET A 1 314 ? 156.167 137.529 122.109 1.00 39.70 ?  314 MET A SD    1 
ATOM   2534  C  CE    . MET A 1 314 ? 155.135 137.826 123.538 1.00 22.66 ?  314 MET A CE    1 
ATOM   2535  N  N     . ASP A 1 315 ? 154.569 141.776 120.189 1.00 23.27 ?  315 ASP A N     1 
ATOM   2536  C  CA    . ASP A 1 315 ? 153.992 141.757 118.852 1.00 28.91 ?  315 ASP A CA    1 
ATOM   2537  C  C     . ASP A 1 315 ? 154.200 143.060 118.093 1.00 23.59 ?  315 ASP A C     1 
ATOM   2538  O  O     . ASP A 1 315 ? 153.811 143.146 116.923 1.00 29.14 ?  315 ASP A O     1 
ATOM   2539  C  CB    . ASP A 1 315 ? 152.502 141.380 118.929 1.00 25.26 ?  315 ASP A CB    1 
ATOM   2540  C  CG    . ASP A 1 315 ? 151.577 142.571 119.172 1.00 30.96 ?  315 ASP A CG    1 
ATOM   2541  O  OD1   . ASP A 1 315 ? 152.042 143.723 119.297 1.00 39.91 ?  315 ASP A OD1   1 
ATOM   2542  O  OD2   . ASP A 1 315 ? 150.351 142.345 119.226 1.00 21.49 -1 315 ASP A OD2   1 
ATOM   2543  N  N     . GLU A 1 316 ? 154.797 144.066 118.721 1.00 25.98 ?  316 GLU A N     1 
ATOM   2544  C  CA    . GLU A 1 316 ? 155.203 145.287 118.040 1.00 21.42 ?  316 GLU A CA    1 
ATOM   2545  C  C     . GLU A 1 316 ? 156.634 145.222 117.527 1.00 26.71 ?  316 GLU A C     1 
ATOM   2546  O  O     . GLU A 1 316 ? 157.097 146.176 116.895 1.00 30.21 ?  316 GLU A O     1 
ATOM   2547  C  CB    . GLU A 1 316 ? 155.051 146.491 118.974 1.00 26.82 ?  316 GLU A CB    1 
ATOM   2548  C  CG    . GLU A 1 316 ? 154.307 147.663 118.362 1.00 24.65 ?  316 GLU A CG    1 
ATOM   2549  C  CD    . GLU A 1 316 ? 152.918 147.291 117.896 1.00 34.40 ?  316 GLU A CD    1 
ATOM   2550  O  OE1   . GLU A 1 316 ? 152.265 146.473 118.575 1.00 39.85 ?  316 GLU A OE1   1 
ATOM   2551  O  OE2   . GLU A 1 316 ? 152.481 147.813 116.850 1.00 32.45 -1 316 GLU A OE2   1 
ATOM   2552  N  N     . MET A 1 317 ? 157.340 144.125 117.784 1.00 34.07 ?  317 MET A N     1 
ATOM   2553  C  CA    . MET A 1 317 ? 158.734 143.958 117.407 1.00 32.63 ?  317 MET A CA    1 
ATOM   2554  C  C     . MET A 1 317 ? 158.862 142.936 116.286 1.00 32.10 ?  317 MET A C     1 
ATOM   2555  O  O     . MET A 1 317 ? 157.945 142.158 116.013 1.00 35.92 ?  317 MET A O     1 
ATOM   2556  C  CB    . MET A 1 317 ? 159.573 143.515 118.611 1.00 31.06 ?  317 MET A CB    1 
ATOM   2557  C  CG    . MET A 1 317 ? 160.086 144.655 119.468 1.00 31.36 ?  317 MET A CG    1 
ATOM   2558  S  SD    . MET A 1 317 ? 160.213 144.205 121.207 1.00 42.35 ?  317 MET A SD    1 
ATOM   2559  C  CE    . MET A 1 317 ? 161.627 145.187 121.693 1.00 32.40 ?  317 MET A CE    1 
ATOM   2560  N  N     . ASP A 1 318 ? 160.022 142.948 115.635 1.00 34.35 ?  318 ASP A N     1 
ATOM   2561  C  CA    . ASP A 1 318 ? 160.328 141.979 114.589 1.00 32.66 ?  318 ASP A CA    1 
ATOM   2562  C  C     . ASP A 1 318 ? 160.889 140.721 115.240 1.00 31.89 ?  318 ASP A C     1 
ATOM   2563  O  O     . ASP A 1 318 ? 162.012 140.727 115.754 1.00 30.17 ?  318 ASP A O     1 
ATOM   2564  C  CB    . ASP A 1 318 ? 161.316 142.566 113.585 1.00 34.08 ?  318 ASP A CB    1 
ATOM   2565  C  CG    . ASP A 1 318 ? 161.456 141.714 112.339 1.00 38.56 ?  318 ASP A CG    1 
ATOM   2566  O  OD1   . ASP A 1 318 ? 160.428 141.200 111.849 1.00 37.65 ?  318 ASP A OD1   1 
ATOM   2567  O  OD2   . ASP A 1 318 ? 162.593 141.559 111.846 1.00 40.46 -1 318 ASP A OD2   1 
ATOM   2568  N  N     . MET A 1 319 ? 160.108 139.639 115.223 1.00 31.18 ?  319 MET A N     1 
ATOM   2569  C  CA    . MET A 1 319 ? 160.562 138.404 115.851 1.00 29.53 ?  319 MET A CA    1 
ATOM   2570  C  C     . MET A 1 319 ? 161.761 137.812 115.124 1.00 25.58 ?  319 MET A C     1 
ATOM   2571  O  O     . MET A 1 319 ? 162.621 137.195 115.760 1.00 31.73 ?  319 MET A O     1 
ATOM   2572  C  CB    . MET A 1 319 ? 159.420 137.390 115.912 1.00 25.73 ?  319 MET A CB    1 
ATOM   2573  C  CG    . MET A 1 319 ? 159.823 136.036 116.471 1.00 34.42 ?  319 MET A CG    1 
ATOM   2574  S  SD    . MET A 1 319 ? 160.291 136.080 118.212 1.00 38.25 ?  319 MET A SD    1 
ATOM   2575  C  CE    . MET A 1 319 ? 158.960 137.052 118.911 1.00 28.62 ?  319 MET A CE    1 
ATOM   2576  N  N     . ASN A 1 320 ? 161.850 138.004 113.807 1.00 34.53 ?  320 ASN A N     1 
ATOM   2577  C  CA    . ASN A 1 320 ? 162.989 137.477 113.066 1.00 32.41 ?  320 ASN A CA    1 
ATOM   2578  C  C     . ASN A 1 320 ? 164.285 138.167 113.469 1.00 36.54 ?  320 ASN A C     1 
ATOM   2579  O  O     . ASN A 1 320 ? 165.371 137.620 113.250 1.00 35.83 ?  320 ASN A O     1 
ATOM   2580  C  CB    . ASN A 1 320 ? 162.748 137.622 111.564 1.00 32.63 ?  320 ASN A CB    1 
ATOM   2581  C  CG    . ASN A 1 320 ? 161.368 137.152 111.149 1.00 35.05 ?  320 ASN A CG    1 
ATOM   2582  O  OD1   . ASN A 1 320 ? 161.003 135.997 111.364 1.00 33.69 ?  320 ASN A OD1   1 
ATOM   2583  N  ND2   . ASN A 1 320 ? 160.594 138.049 110.552 1.00 36.81 ?  320 ASN A ND2   1 
ATOM   2584  N  N     . GLU A 1 321 ? 164.192 139.359 114.053 1.00 36.14 ?  321 GLU A N     1 
ATOM   2585  C  CA    . GLU A 1 321 ? 165.359 140.075 114.552 1.00 33.78 ?  321 GLU A CA    1 
ATOM   2586  C  C     . GLU A 1 321 ? 165.487 140.035 116.066 1.00 34.37 ?  321 GLU A C     1 
ATOM   2587  O  O     . GLU A 1 321 ? 166.592 140.215 116.587 1.00 38.65 ?  321 GLU A O     1 
ATOM   2588  C  CB    . GLU A 1 321 ? 165.318 141.538 114.098 1.00 34.83 ?  321 GLU A CB    1 
ATOM   2589  C  CG    . GLU A 1 321 ? 166.481 142.373 114.607 1.00 38.53 ?  321 GLU A CG    1 
ATOM   2590  C  CD    . GLU A 1 321 ? 166.046 143.737 115.112 1.00 45.02 ?  321 GLU A CD    1 
ATOM   2591  O  OE1   . GLU A 1 321 ? 164.959 144.204 114.712 1.00 41.40 ?  321 GLU A OE1   1 
ATOM   2592  O  OE2   . GLU A 1 321 ? 166.793 144.339 115.910 1.00 42.94 -1 321 GLU A OE2   1 
ATOM   2593  N  N     . MET A 1 322 ? 164.389 139.800 116.783 1.00 30.41 ?  322 MET A N     1 
ATOM   2594  C  CA    . MET A 1 322 ? 164.377 139.902 118.234 1.00 29.22 ?  322 MET A CA    1 
ATOM   2595  C  C     . MET A 1 322 ? 164.304 138.558 118.945 1.00 30.27 ?  322 MET A C     1 
ATOM   2596  O  O     . MET A 1 322 ? 164.412 138.526 120.173 1.00 37.10 ?  322 MET A O     1 
ATOM   2597  C  CB    . MET A 1 322 ? 163.198 140.771 118.690 1.00 30.12 ?  322 MET A CB    1 
ATOM   2598  C  CG    . MET A 1 322 ? 163.481 142.264 118.683 1.00 31.21 ?  322 MET A CG    1 
ATOM   2599  S  SD    . MET A 1 322 ? 165.213 142.659 118.980 1.00 44.25 ?  322 MET A SD    1 
ATOM   2600  C  CE    . MET A 1 322 ? 165.153 143.165 120.697 1.00 32.76 ?  322 MET A CE    1 
ATOM   2601  N  N     . TYR A 1 323 ? 164.121 137.453 118.219 1.00 27.14 ?  323 TYR A N     1 
ATOM   2602  C  CA    . TYR A 1 323 ? 163.966 136.160 118.878 1.00 27.14 ?  323 TYR A CA    1 
ATOM   2603  C  C     . TYR A 1 323 ? 165.237 135.762 119.618 1.00 31.08 ?  323 TYR A C     1 
ATOM   2604  O  O     . TYR A 1 323 ? 165.184 135.317 120.772 1.00 28.39 ?  323 TYR A O     1 
ATOM   2605  C  CB    . TYR A 1 323 ? 163.577 135.095 117.853 1.00 29.95 ?  323 TYR A CB    1 
ATOM   2606  C  CG    . TYR A 1 323 ? 163.502 133.696 118.419 1.00 25.55 ?  323 TYR A CG    1 
ATOM   2607  C  CD1   . TYR A 1 323 ? 162.350 133.242 119.044 1.00 21.39 ?  323 TYR A CD1   1 
ATOM   2608  C  CD2   . TYR A 1 323 ? 164.581 132.830 118.324 1.00 22.93 ?  323 TYR A CD2   1 
ATOM   2609  C  CE1   . TYR A 1 323 ? 162.278 131.966 119.563 1.00 21.37 ?  323 TYR A CE1   1 
ATOM   2610  C  CE2   . TYR A 1 323 ? 164.517 131.554 118.838 1.00 24.34 ?  323 TYR A CE2   1 
ATOM   2611  C  CZ    . TYR A 1 323 ? 163.364 131.127 119.457 1.00 24.93 ?  323 TYR A CZ    1 
ATOM   2612  O  OH    . TYR A 1 323 ? 163.301 129.853 119.969 1.00 28.14 ?  323 TYR A OH    1 
ATOM   2613  N  N     . ASP A 1 324 ? 166.392 135.914 118.970 1.00 33.24 ?  324 ASP A N     1 
ATOM   2614  C  CA    . ASP A 1 324 ? 167.648 135.547 119.613 1.00 29.56 ?  324 ASP A CA    1 
ATOM   2615  C  C     . ASP A 1 324 ? 167.938 136.446 120.808 1.00 33.54 ?  324 ASP A C     1 
ATOM   2616  O  O     . ASP A 1 324 ? 168.427 135.976 121.841 1.00 37.17 ?  324 ASP A O     1 
ATOM   2617  C  CB    . ASP A 1 324 ? 168.790 135.599 118.600 1.00 34.78 ?  324 ASP A CB    1 
ATOM   2618  C  CG    . ASP A 1 324 ? 168.867 134.347 117.749 1.00 40.95 ?  324 ASP A CG    1 
ATOM   2619  O  OD1   . ASP A 1 324 ? 168.380 133.290 118.200 1.00 38.13 ?  324 ASP A OD1   1 
ATOM   2620  O  OD2   . ASP A 1 324 ? 169.414 134.418 116.628 1.00 43.01 -1 324 ASP A OD2   1 
ATOM   2621  N  N     . LYS A 1 325 ? 167.647 137.742 120.685 1.00 34.44 ?  325 LYS A N     1 
ATOM   2622  C  CA    . LYS A 1 325 ? 167.839 138.649 121.811 1.00 30.60 ?  325 LYS A CA    1 
ATOM   2623  C  C     . LYS A 1 325 ? 166.935 138.275 122.979 1.00 31.45 ?  325 LYS A C     1 
ATOM   2624  O  O     . LYS A 1 325 ? 167.364 138.303 124.138 1.00 35.11 ?  325 LYS A O     1 
ATOM   2625  C  CB    . LYS A 1 325 ? 167.589 140.090 121.370 1.00 33.36 ?  325 LYS A CB    1 
ATOM   2626  C  CG    . LYS A 1 325 ? 168.402 140.510 120.158 1.00 30.85 ?  325 LYS A CG    1 
ATOM   2627  C  CD    . LYS A 1 325 ? 168.359 142.012 119.950 1.00 33.53 ?  325 LYS A CD    1 
ATOM   2628  C  CE    . LYS A 1 325 ? 169.088 142.414 118.679 1.00 35.25 ?  325 LYS A CE    1 
ATOM   2629  N  NZ    . LYS A 1 325 ? 170.270 143.273 118.963 1.00 33.33 1  325 LYS A NZ    1 
ATOM   2630  N  N     . PHE A 1 326 ? 165.679 137.926 122.696 1.00 30.52 ?  326 PHE A N     1 
ATOM   2631  C  CA    . PHE A 1 326 ? 164.778 137.489 123.757 1.00 28.34 ?  326 PHE A CA    1 
ATOM   2632  C  C     . PHE A 1 326 ? 165.297 136.226 124.428 1.00 28.20 ?  326 PHE A C     1 
ATOM   2633  O  O     . PHE A 1 326 ? 165.267 136.108 125.658 1.00 35.69 ?  326 PHE A O     1 
ATOM   2634  C  CB    . PHE A 1 326 ? 163.376 137.250 123.196 1.00 26.88 ?  326 PHE A CB    1 
ATOM   2635  C  CG    . PHE A 1 326 ? 162.718 138.482 122.649 1.00 30.62 ?  326 PHE A CG    1 
ATOM   2636  C  CD1   . PHE A 1 326 ? 163.118 139.743 123.057 1.00 31.76 ?  326 PHE A CD1   1 
ATOM   2637  C  CD2   . PHE A 1 326 ? 161.694 138.379 121.724 1.00 30.28 ?  326 PHE A CD2   1 
ATOM   2638  C  CE1   . PHE A 1 326 ? 162.511 140.874 122.552 1.00 27.25 ?  326 PHE A CE1   1 
ATOM   2639  C  CE2   . PHE A 1 326 ? 161.083 139.507 121.217 1.00 31.62 ?  326 PHE A CE2   1 
ATOM   2640  C  CZ    . PHE A 1 326 ? 161.492 140.756 121.631 1.00 29.38 ?  326 PHE A CZ    1 
ATOM   2641  N  N     . VAL A 1 327 ? 165.774 135.267 123.632 1.00 35.53 ?  327 VAL A N     1 
ATOM   2642  C  CA    . VAL A 1 327 ? 166.268 134.013 124.194 1.00 32.17 ?  327 VAL A CA    1 
ATOM   2643  C  C     . VAL A 1 327 ? 167.495 134.261 125.060 1.00 34.08 ?  327 VAL A C     1 
ATOM   2644  O  O     . VAL A 1 327 ? 167.648 133.667 126.134 1.00 42.68 ?  327 VAL A O     1 
ATOM   2645  C  CB    . VAL A 1 327 ? 166.560 133.003 123.070 1.00 33.81 ?  327 VAL A CB    1 
ATOM   2646  C  CG1   . VAL A 1 327 ? 167.100 131.706 123.649 1.00 38.30 ?  327 VAL A CG1   1 
ATOM   2647  C  CG2   . VAL A 1 327 ? 165.308 132.746 122.250 1.00 27.14 ?  327 VAL A CG2   1 
ATOM   2648  N  N     . ASP A 1 328 ? 168.390 135.141 124.610 1.00 32.69 ?  328 ASP A N     1 
ATOM   2649  C  CA    . ASP A 1 328 ? 169.629 135.417 125.327 1.00 31.55 ?  328 ASP A CA    1 
ATOM   2650  C  C     . ASP A 1 328 ? 169.454 136.403 126.474 1.00 37.68 ?  328 ASP A C     1 
ATOM   2651  O  O     . ASP A 1 328 ? 170.402 136.607 127.239 1.00 43.72 ?  328 ASP A O     1 
ATOM   2652  C  CB    . ASP A 1 328 ? 170.685 135.952 124.357 1.00 33.69 ?  328 ASP A CB    1 
ATOM   2653  C  CG    . ASP A 1 328 ? 171.121 134.915 123.343 1.00 42.39 ?  328 ASP A CG    1 
ATOM   2654  O  OD1   . ASP A 1 328 ? 171.040 133.708 123.652 1.00 42.93 ?  328 ASP A OD1   1 
ATOM   2655  O  OD2   . ASP A 1 328 ? 171.544 135.308 122.236 1.00 44.94 -1 328 ASP A OD2   1 
ATOM   2656  N  N     . ASN A 1 329 ? 168.280 137.015 126.614 1.00 35.58 ?  329 ASN A N     1 
ATOM   2657  C  CA    . ASN A 1 329 ? 168.065 138.022 127.643 1.00 29.66 ?  329 ASN A CA    1 
ATOM   2658  C  C     . ASN A 1 329 ? 167.517 137.357 128.898 1.00 38.47 ?  329 ASN A C     1 
ATOM   2659  O  O     . ASN A 1 329 ? 166.388 136.843 128.870 1.00 39.45 ?  329 ASN A O     1 
ATOM   2660  C  CB    . ASN A 1 329 ? 167.106 139.095 127.147 1.00 32.94 ?  329 ASN A CB    1 
ATOM   2661  C  CG    . ASN A 1 329 ? 167.138 140.344 128.001 1.00 36.06 ?  329 ASN A CG    1 
ATOM   2662  O  OD1   . ASN A 1 329 ? 167.389 140.282 129.202 1.00 43.25 ?  329 ASN A OD1   1 
ATOM   2663  N  ND2   . ASN A 1 329 ? 166.881 141.489 127.381 1.00 33.20 ?  329 ASN A ND2   1 
ATOM   2664  N  N     . PRO A 1 330 ? 168.260 137.336 130.007 1.00 40.94 ?  330 PRO A N     1 
ATOM   2665  C  CA    . PRO A 1 330 ? 167.733 136.701 131.226 1.00 34.05 ?  330 PRO A CA    1 
ATOM   2666  C  C     . PRO A 1 330 ? 166.475 137.360 131.757 1.00 32.70 ?  330 PRO A C     1 
ATOM   2667  O  O     . PRO A 1 330 ? 165.619 136.670 132.323 1.00 39.56 ?  330 PRO A O     1 
ATOM   2668  C  CB    . PRO A 1 330 ? 168.901 136.826 132.214 1.00 35.18 ?  330 PRO A CB    1 
ATOM   2669  C  CG    . PRO A 1 330 ? 169.689 137.988 131.720 1.00 33.93 ?  330 PRO A CG    1 
ATOM   2670  C  CD    . PRO A 1 330 ? 169.582 137.946 130.225 1.00 34.65 ?  330 PRO A CD    1 
ATOM   2671  N  N     . ARG A 1 331 ? 166.335 138.677 131.596 1.00 32.52 ?  331 ARG A N     1 
ATOM   2672  C  CA    . ARG A 1 331 ? 165.161 139.379 132.101 1.00 34.98 ?  331 ARG A CA    1 
ATOM   2673  C  C     . ARG A 1 331 ? 163.895 139.048 131.323 1.00 36.66 ?  331 ARG A C     1 
ATOM   2674  O  O     . ARG A 1 331 ? 162.801 139.400 131.776 1.00 35.04 ?  331 ARG A O     1 
ATOM   2675  C  CB    . ARG A 1 331 ? 165.406 140.886 132.077 1.00 38.38 ?  331 ARG A CB    1 
ATOM   2676  C  CG    . ARG A 1 331 ? 166.194 141.399 133.267 1.00 34.08 ?  331 ARG A CG    1 
ATOM   2677  C  CD    . ARG A 1 331 ? 166.674 142.823 133.036 1.00 36.76 ?  331 ARG A CD    1 
ATOM   2678  N  NE    . ARG A 1 331 ? 167.699 142.930 132.003 1.00 40.37 ?  331 ARG A NE    1 
ATOM   2679  C  CZ    . ARG A 1 331 ? 168.719 142.096 131.843 1.00 41.02 ?  331 ARG A CZ    1 
ATOM   2680  N  NH1   . ARG A 1 331 ? 168.924 141.081 132.667 1.00 42.66 1  331 ARG A NH1   1 
ATOM   2681  N  NH2   . ARG A 1 331 ? 169.564 142.292 130.835 1.00 37.79 ?  331 ARG A NH2   1 
ATOM   2682  N  N     . VAL A 1 332 ? 164.015 138.393 130.174 1.00 30.98 ?  332 VAL A N     1 
ATOM   2683  C  CA    . VAL A 1 332 ? 162.861 137.945 129.405 1.00 25.80 ?  332 VAL A CA    1 
ATOM   2684  C  C     . VAL A 1 332 ? 162.531 136.520 129.823 1.00 31.94 ?  332 VAL A C     1 
ATOM   2685  O  O     . VAL A 1 332 ? 163.405 135.646 129.829 1.00 31.83 ?  332 VAL A O     1 
ATOM   2686  C  CB    . VAL A 1 332 ? 163.139 138.031 127.895 1.00 28.75 ?  332 VAL A CB    1 
ATOM   2687  C  CG1   . VAL A 1 332 ? 162.052 137.309 127.112 1.00 23.70 ?  332 VAL A CG1   1 
ATOM   2688  C  CG2   . VAL A 1 332 ? 163.246 139.481 127.457 1.00 29.02 ?  332 VAL A CG2   1 
ATOM   2689  N  N     . LYS A 1 333 ? 161.273 136.284 130.179 1.00 31.11 ?  333 LYS A N     1 
ATOM   2690  C  CA    . LYS A 1 333 ? 160.829 134.964 130.596 1.00 24.27 ?  333 LYS A CA    1 
ATOM   2691  C  C     . LYS A 1 333 ? 160.276 134.196 129.404 1.00 26.16 ?  333 LYS A C     1 
ATOM   2692  O  O     . LYS A 1 333 ? 159.444 134.707 128.650 1.00 29.65 ?  333 LYS A O     1 
ATOM   2693  C  CB    . LYS A 1 333 ? 159.769 135.066 131.692 1.00 24.08 ?  333 LYS A CB    1 
ATOM   2694  C  CG    . LYS A 1 333 ? 159.531 133.766 132.439 1.00 27.87 ?  333 LYS A CG    1 
ATOM   2695  C  CD    . LYS A 1 333 ? 158.404 133.900 133.446 1.00 28.76 ?  333 LYS A CD    1 
ATOM   2696  C  CE    . LYS A 1 333 ? 158.157 132.588 134.172 1.00 28.51 ?  333 LYS A CE    1 
ATOM   2697  N  NZ    . LYS A 1 333 ? 157.053 132.702 135.164 1.00 36.63 1  333 LYS A NZ    1 
ATOM   2698  N  N     . LYS A 1 334 ? 160.745 132.962 129.244 1.00 29.21 ?  334 LYS A N     1 
ATOM   2699  C  CA    . LYS A 1 334 ? 160.346 132.126 128.123 1.00 26.28 ?  334 LYS A CA    1 
ATOM   2700  C  C     . LYS A 1 334 ? 160.312 130.676 128.578 1.00 31.26 ?  334 LYS A C     1 
ATOM   2701  O  O     . LYS A 1 334 ? 161.014 130.290 129.516 1.00 39.37 ?  334 LYS A O     1 
ATOM   2702  C  CB    . LYS A 1 334 ? 161.305 132.286 126.938 1.00 30.47 ?  334 LYS A CB    1 
ATOM   2703  C  CG    . LYS A 1 334 ? 162.680 131.684 127.174 1.00 28.31 ?  334 LYS A CG    1 
ATOM   2704  C  CD    . LYS A 1 334 ? 163.787 132.654 126.810 1.00 26.17 ?  334 LYS A CD    1 
ATOM   2705  C  CE    . LYS A 1 334 ? 164.068 133.620 127.946 1.00 28.70 ?  334 LYS A CE    1 
ATOM   2706  N  NZ    . LYS A 1 334 ? 165.394 134.281 127.811 1.00 29.22 1  334 LYS A NZ    1 
ATOM   2707  N  N     . GLU A 1 335 ? 159.483 129.878 127.911 1.00 29.82 ?  335 GLU A N     1 
ATOM   2708  C  CA    . GLU A 1 335 ? 159.455 128.440 128.130 1.00 28.27 ?  335 GLU A CA    1 
ATOM   2709  C  C     . GLU A 1 335 ? 159.624 127.726 126.798 1.00 27.29 ?  335 GLU A C     1 
ATOM   2710  O  O     . GLU A 1 335 ? 159.172 128.206 125.755 1.00 31.61 ?  335 GLU A O     1 
ATOM   2711  C  CB    . GLU A 1 335 ? 158.160 127.982 128.820 1.00 33.09 ?  335 GLU A CB    1 
ATOM   2712  C  CG    . GLU A 1 335 ? 156.889 128.207 128.028 1.00 32.84 ?  335 GLU A CG    1 
ATOM   2713  C  CD    . GLU A 1 335 ? 155.651 127.815 128.814 1.00 38.85 ?  335 GLU A CD    1 
ATOM   2714  O  OE1   . GLU A 1 335 ? 155.750 127.688 130.051 1.00 35.82 ?  335 GLU A OE1   1 
ATOM   2715  O  OE2   . GLU A 1 335 ? 154.580 127.635 128.196 1.00 36.99 -1 335 GLU A OE2   1 
ATOM   2716  N  N     . LYS A 1 336 ? 160.291 126.579 126.846 1.00 31.33 ?  336 LYS A N     1 
ATOM   2717  C  CA    . LYS A 1 336 ? 160.637 125.848 125.636 1.00 25.70 ?  336 LYS A CA    1 
ATOM   2718  C  C     . LYS A 1 336 ? 159.420 125.136 125.062 1.00 30.06 ?  336 LYS A C     1 
ATOM   2719  O  O     . LYS A 1 336 ? 158.547 124.671 125.798 1.00 36.10 ?  336 LYS A O     1 
ATOM   2720  C  CB    . LYS A 1 336 ? 161.746 124.838 125.926 1.00 33.64 ?  336 LYS A CB    1 
ATOM   2721  C  CG    . LYS A 1 336 ? 162.713 124.631 124.777 1.00 37.70 ?  336 LYS A CG    1 
ATOM   2722  C  CD    . LYS A 1 336 ? 163.533 123.368 124.972 1.00 36.04 ?  336 LYS A CD    1 
ATOM   2723  C  CE    . LYS A 1 336 ? 164.844 123.668 125.678 1.00 36.55 ?  336 LYS A CE    1 
ATOM   2724  N  NZ    . LYS A 1 336 ? 165.982 123.756 124.722 1.00 36.80 1  336 LYS A NZ    1 
ATOM   2725  N  N     . ILE A 1 337 ? 159.368 125.060 123.732 1.00 32.75 ?  337 ILE A N     1 
ATOM   2726  C  CA    . ILE A 1 337 ? 158.326 124.342 123.012 1.00 28.79 ?  337 ILE A CA    1 
ATOM   2727  C  C     . ILE A 1 337 ? 158.968 123.609 121.843 1.00 30.88 ?  337 ILE A C     1 
ATOM   2728  O  O     . ILE A 1 337 ? 160.122 123.849 121.486 1.00 32.89 ?  337 ILE A O     1 
ATOM   2729  C  CB    . ILE A 1 337 ? 157.206 125.275 122.505 1.00 27.88 ?  337 ILE A CB    1 
ATOM   2730  C  CG1   . ILE A 1 337 ? 157.774 126.300 121.521 1.00 26.31 ?  337 ILE A CG1   1 
ATOM   2731  C  CG2   . ILE A 1 337 ? 156.516 125.964 123.671 1.00 27.97 ?  337 ILE A CG2   1 
ATOM   2732  C  CD1   . ILE A 1 337 ? 156.789 126.742 120.467 1.00 28.92 ?  337 ILE A CD1   1 
ATOM   2733  N  N     . ASN A 1 338 ? 158.202 122.698 121.248 1.00 32.84 ?  338 ASN A N     1 
ATOM   2734  C  CA    . ASN A 1 338 ? 158.628 122.025 120.032 1.00 30.64 ?  338 ASN A CA    1 
ATOM   2735  C  C     . ASN A 1 338 ? 157.901 122.651 118.854 1.00 33.74 ?  338 ASN A C     1 
ATOM   2736  O  O     . ASN A 1 338 ? 156.682 122.466 118.725 1.00 37.29 ?  338 ASN A O     1 
ATOM   2737  C  CB    . ASN A 1 338 ? 158.334 120.528 120.108 1.00 31.47 ?  338 ASN A CB    1 
ATOM   2738  C  CG    . ASN A 1 338 ? 159.275 119.708 119.253 1.00 31.89 ?  338 ASN A CG    1 
ATOM   2739  O  OD1   . ASN A 1 338 ? 159.185 119.715 118.027 1.00 33.11 ?  338 ASN A OD1   1 
ATOM   2740  N  ND2   . ASN A 1 338 ? 160.190 118.994 119.898 1.00 33.53 ?  338 ASN A ND2   1 
ATOM   2741  N  N     . PRO A 1 339 ? 158.582 123.403 117.986 1.00 31.04 ?  339 PRO A N     1 
ATOM   2742  C  CA    . PRO A 1 339 ? 157.866 124.029 116.862 1.00 27.31 ?  339 PRO A CA    1 
ATOM   2743  C  C     . PRO A 1 339 ? 157.171 123.027 115.959 1.00 25.07 ?  339 PRO A C     1 
ATOM   2744  O  O     . PRO A 1 339 ? 156.061 123.296 115.484 1.00 29.82 ?  339 PRO A O     1 
ATOM   2745  C  CB    . PRO A 1 339 ? 158.975 124.797 116.127 1.00 31.40 ?  339 PRO A CB    1 
ATOM   2746  C  CG    . PRO A 1 339 ? 160.254 124.188 116.595 1.00 31.31 ?  339 PRO A CG    1 
ATOM   2747  C  CD    . PRO A 1 339 ? 160.011 123.748 117.998 1.00 29.87 ?  339 PRO A CD    1 
ATOM   2748  N  N     . ARG A 1 340 ? 157.786 121.869 115.712 1.00 30.49 ?  340 ARG A N     1 
ATOM   2749  C  CA    . ARG A 1 340 ? 157.135 120.857 114.886 1.00 25.29 ?  340 ARG A CA    1 
ATOM   2750  C  C     . ARG A 1 340 ? 155.952 120.233 115.613 1.00 27.61 ?  340 ARG A C     1 
ATOM   2751  O  O     . ARG A 1 340 ? 154.920 119.944 114.997 1.00 36.56 ?  340 ARG A O     1 
ATOM   2752  C  CB    . ARG A 1 340 ? 158.143 119.788 114.469 1.00 25.28 ?  340 ARG A CB    1 
ATOM   2753  C  CG    . ARG A 1 340 ? 159.142 120.271 113.439 1.00 25.03 ?  340 ARG A CG    1 
ATOM   2754  C  CD    . ARG A 1 340 ? 159.866 119.120 112.771 1.00 26.84 ?  340 ARG A CD    1 
ATOM   2755  N  NE    . ARG A 1 340 ? 160.812 119.602 111.774 1.00 29.83 ?  340 ARG A NE    1 
ATOM   2756  C  CZ    . ARG A 1 340 ? 161.603 118.821 111.052 1.00 33.07 ?  340 ARG A CZ    1 
ATOM   2757  N  NH1   . ARG A 1 340 ? 161.587 117.506 111.188 1.00 31.52 1  340 ARG A NH1   1 
ATOM   2758  N  NH2   . ARG A 1 340 ? 162.430 119.375 110.171 1.00 28.94 ?  340 ARG A NH2   1 
ATOM   2759  N  N     . LYS A 1 341 ? 156.078 120.023 116.924 1.00 27.14 ?  341 LYS A N     1 
ATOM   2760  C  CA    . LYS A 1 341 ? 154.938 119.552 117.702 1.00 27.99 ?  341 LYS A CA    1 
ATOM   2761  C  C     . LYS A 1 341 ? 153.808 120.573 117.683 1.00 28.35 ?  341 LYS A C     1 
ATOM   2762  O  O     . LYS A 1 341 ? 152.631 120.206 117.605 1.00 32.19 ?  341 LYS A O     1 
ATOM   2763  C  CB    . LYS A 1 341 ? 155.366 119.248 119.137 1.00 35.76 ?  341 LYS A CB    1 
ATOM   2764  C  CG    . LYS A 1 341 ? 155.266 117.781 119.516 1.00 30.81 ?  341 LYS A CG    1 
ATOM   2765  C  CD    . LYS A 1 341 ? 156.194 116.928 118.667 1.00 33.67 ?  341 LYS A CD    1 
ATOM   2766  C  CE    . LYS A 1 341 ? 156.097 115.460 119.048 1.00 38.82 ?  341 LYS A CE    1 
ATOM   2767  N  NZ    . LYS A 1 341 ? 156.180 114.571 117.857 1.00 37.99 1  341 LYS A NZ    1 
ATOM   2768  N  N     . LEU A 1 342 ? 154.146 121.862 117.747 1.00 27.46 ?  342 LEU A N     1 
ATOM   2769  C  CA    . LEU A 1 342 ? 153.121 122.897 117.679 1.00 25.54 ?  342 LEU A CA    1 
ATOM   2770  C  C     . LEU A 1 342 ? 152.451 122.923 116.310 1.00 28.62 ?  342 LEU A C     1 
ATOM   2771  O  O     . LEU A 1 342 ? 151.232 123.103 116.214 1.00 29.44 ?  342 LEU A O     1 
ATOM   2772  C  CB    . LEU A 1 342 ? 153.730 124.259 118.012 1.00 26.79 ?  342 LEU A CB    1 
ATOM   2773  C  CG    . LEU A 1 342 ? 152.750 125.405 118.273 1.00 26.83 ?  342 LEU A CG    1 
ATOM   2774  C  CD1   . LEU A 1 342 ? 151.627 124.955 119.191 1.00 24.03 ?  342 LEU A CD1   1 
ATOM   2775  C  CD2   . LEU A 1 342 ? 153.479 126.600 118.861 1.00 21.82 ?  342 LEU A CD2   1 
ATOM   2776  N  N     . LEU A 1 343 ? 153.227 122.752 115.239 1.00 29.94 ?  343 LEU A N     1 
ATOM   2777  C  CA    . LEU A 1 343 ? 152.639 122.690 113.904 1.00 25.86 ?  343 LEU A CA    1 
ATOM   2778  C  C     . LEU A 1 343 ? 151.712 121.489 113.765 1.00 26.47 ?  343 LEU A C     1 
ATOM   2779  O  O     . LEU A 1 343 ? 150.627 121.593 113.179 1.00 31.89 ?  343 LEU A O     1 
ATOM   2780  C  CB    . LEU A 1 343 ? 153.742 122.641 112.848 1.00 26.95 ?  343 LEU A CB    1 
ATOM   2781  C  CG    . LEU A 1 343 ? 154.210 123.986 112.298 1.00 31.94 ?  343 LEU A CG    1 
ATOM   2782  C  CD1   . LEU A 1 343 ? 155.309 123.785 111.270 1.00 28.55 ?  343 LEU A CD1   1 
ATOM   2783  C  CD2   . LEU A 1 343 ? 153.043 124.755 111.700 1.00 26.90 ?  343 LEU A CD2   1 
ATOM   2784  N  N     . GLU A 1 344 ? 152.128 120.334 114.287 1.00 30.13 ?  344 GLU A N     1 
ATOM   2785  C  CA    . GLU A 1 344 ? 151.273 119.154 114.246 1.00 27.34 ?  344 GLU A CA    1 
ATOM   2786  C  C     . GLU A 1 344 ? 150.002 119.369 115.056 1.00 24.90 ?  344 GLU A C     1 
ATOM   2787  O  O     . GLU A 1 344 ? 148.919 118.935 114.650 1.00 32.61 ?  344 GLU A O     1 
ATOM   2788  C  CB    . GLU A 1 344 ? 152.041 117.934 114.752 1.00 28.63 ?  344 GLU A CB    1 
ATOM   2789  C  CG    . GLU A 1 344 ? 153.259 117.586 113.913 1.00 30.54 ?  344 GLU A CG    1 
ATOM   2790  C  CD    . GLU A 1 344 ? 154.233 116.690 114.648 1.00 37.92 ?  344 GLU A CD    1 
ATOM   2791  O  OE1   . GLU A 1 344 ? 153.892 116.229 115.758 1.00 38.38 ?  344 GLU A OE1   1 
ATOM   2792  O  OE2   . GLU A 1 344 ? 155.339 116.450 114.120 1.00 34.64 -1 344 GLU A OE2   1 
ATOM   2793  N  N     . LYS A 1 345 ? 150.115 120.027 116.210 1.00 21.93 ?  345 LYS A N     1 
ATOM   2794  C  CA    . LYS A 1 345 ? 148.932 120.347 117.000 1.00 23.10 ?  345 LYS A CA    1 
ATOM   2795  C  C     . LYS A 1 345 ? 147.999 121.279 116.240 1.00 26.68 ?  345 LYS A C     1 
ATOM   2796  O  O     . LYS A 1 345 ? 146.775 121.116 116.286 1.00 28.15 ?  345 LYS A O     1 
ATOM   2797  C  CB    . LYS A 1 345 ? 149.349 120.972 118.331 1.00 26.73 ?  345 LYS A CB    1 
ATOM   2798  C  CG    . LYS A 1 345 ? 148.188 121.374 119.223 1.00 24.29 ?  345 LYS A CG    1 
ATOM   2799  C  CD    . LYS A 1 345 ? 148.681 121.943 120.541 1.00 28.34 ?  345 LYS A CD    1 
ATOM   2800  C  CE    . LYS A 1 345 ? 147.522 122.351 121.434 1.00 32.65 ?  345 LYS A CE    1 
ATOM   2801  N  NZ    . LYS A 1 345 ? 147.987 122.839 122.759 1.00 30.46 1  345 LYS A NZ    1 
ATOM   2802  N  N     . LEU A 1 346 ? 148.559 122.264 115.537 1.00 33.70 ?  346 LEU A N     1 
ATOM   2803  C  CA    . LEU A 1 346 ? 147.737 123.151 114.721 1.00 26.20 ?  346 LEU A CA    1 
ATOM   2804  C  C     . LEU A 1 346 ? 147.007 122.374 113.636 1.00 24.08 ?  346 LEU A C     1 
ATOM   2805  O  O     . LEU A 1 346 ? 145.814 122.596 113.398 1.00 26.62 ?  346 LEU A O     1 
ATOM   2806  C  CB    . LEU A 1 346 ? 148.601 124.247 114.097 1.00 24.08 ?  346 LEU A CB    1 
ATOM   2807  C  CG    . LEU A 1 346 ? 149.112 125.352 115.021 1.00 24.04 ?  346 LEU A CG    1 
ATOM   2808  C  CD1   . LEU A 1 346 ? 150.001 126.311 114.249 1.00 25.20 ?  346 LEU A CD1   1 
ATOM   2809  C  CD2   . LEU A 1 346 ? 147.957 126.088 115.668 1.00 28.47 ?  346 LEU A CD2   1 
ATOM   2810  N  N     . ALA A 1 347 ? 147.710 121.464 112.959 1.00 23.10 ?  347 ALA A N     1 
ATOM   2811  C  CA    . ALA A 1 347 ? 147.073 120.665 111.916 1.00 22.59 ?  347 ALA A CA    1 
ATOM   2812  C  C     . ALA A 1 347 ? 145.967 119.787 112.489 1.00 29.04 ?  347 ALA A C     1 
ATOM   2813  O  O     . ALA A 1 347 ? 144.885 119.675 111.902 1.00 34.39 ?  347 ALA A O     1 
ATOM   2814  C  CB    . ALA A 1 347 ? 148.115 119.813 111.193 1.00 24.23 ?  347 ALA A CB    1 
ATOM   2815  N  N     . MET A 1 348 ? 146.223 119.157 113.636 1.00 31.23 ?  348 MET A N     1 
ATOM   2816  C  CA    . MET A 1 348 ? 145.208 118.321 114.268 1.00 28.43 ?  348 MET A CA    1 
ATOM   2817  C  C     . MET A 1 348 ? 143.986 119.138 114.668 1.00 24.75 ?  348 MET A C     1 
ATOM   2818  O  O     . MET A 1 348 ? 142.846 118.704 114.471 1.00 33.07 ?  348 MET A O     1 
ATOM   2819  C  CB    . MET A 1 348 ? 145.806 117.609 115.482 1.00 32.04 ?  348 MET A CB    1 
ATOM   2820  C  CG    . MET A 1 348 ? 144.783 117.143 116.503 1.00 37.47 ?  348 MET A CG    1 
ATOM   2821  S  SD    . MET A 1 348 ? 145.351 117.378 118.199 1.00 56.11 ?  348 MET A SD    1 
ATOM   2822  C  CE    . MET A 1 348 ? 144.528 118.908 118.635 1.00 33.90 ?  348 MET A CE    1 
ATOM   2823  N  N     . LEU A 1 349 ? 144.206 120.327 115.233 1.00 21.09 ?  349 LEU A N     1 
ATOM   2824  C  CA    . LEU A 1 349 ? 143.089 121.175 115.632 1.00 17.55 ?  349 LEU A CA    1 
ATOM   2825  C  C     . LEU A 1 349 ? 142.298 121.652 114.420 1.00 19.53 ?  349 LEU A C     1 
ATOM   2826  O  O     . LEU A 1 349 ? 141.067 121.742 114.472 1.00 22.80 ?  349 LEU A O     1 
ATOM   2827  C  CB    . LEU A 1 349 ? 143.601 122.364 116.443 1.00 23.66 ?  349 LEU A CB    1 
ATOM   2828  C  CG    . LEU A 1 349 ? 142.618 122.979 117.439 1.00 29.22 ?  349 LEU A CG    1 
ATOM   2829  C  CD1   . LEU A 1 349 ? 142.441 122.069 118.645 1.00 31.70 ?  349 LEU A CD1   1 
ATOM   2830  C  CD2   . LEU A 1 349 ? 143.077 124.364 117.864 1.00 25.30 ?  349 LEU A CD2   1 
ATOM   2831  N  N     . ARG A 1 350 ? 142.987 121.966 113.321 1.00 25.18 ?  350 ARG A N     1 
ATOM   2832  C  CA    . ARG A 1 350 ? 142.292 122.406 112.117 1.00 21.90 ?  350 ARG A CA    1 
ATOM   2833  C  C     . ARG A 1 350 ? 141.502 121.264 111.491 1.00 25.50 ?  350 ARG A C     1 
ATOM   2834  O  O     . ARG A 1 350 ? 140.428 121.483 110.920 1.00 30.93 ?  350 ARG A O     1 
ATOM   2835  C  CB    . ARG A 1 350 ? 143.290 122.989 111.118 1.00 21.04 ?  350 ARG A CB    1 
ATOM   2836  C  CG    . ARG A 1 350 ? 143.792 124.376 111.493 1.00 19.63 ?  350 ARG A CG    1 
ATOM   2837  C  CD    . ARG A 1 350 ? 144.893 124.851 110.561 1.00 24.23 ?  350 ARG A CD    1 
ATOM   2838  N  NE    . ARG A 1 350 ? 144.444 124.938 109.178 1.00 32.56 ?  350 ARG A NE    1 
ATOM   2839  C  CZ    . ARG A 1 350 ? 143.737 125.943 108.680 1.00 31.40 ?  350 ARG A CZ    1 
ATOM   2840  N  NH1   . ARG A 1 350 ? 143.376 126.972 109.429 1.00 19.20 1  350 ARG A NH1   1 
ATOM   2841  N  NH2   . ARG A 1 350 ? 143.380 125.913 107.401 1.00 24.43 ?  350 ARG A NH2   1 
ATOM   2842  N  N     . SER A 1 351 ? 142.021 120.039 111.579 1.00 30.43 ?  351 SER A N     1 
ATOM   2843  C  CA    . SER A 1 351 ? 141.264 118.886 111.102 1.00 26.14 ?  351 SER A CA    1 
ATOM   2844  C  C     . SER A 1 351 ? 140.030 118.644 111.963 1.00 31.13 ?  351 SER A C     1 
ATOM   2845  O  O     . SER A 1 351 ? 138.939 118.391 111.437 1.00 38.89 ?  351 SER A O     1 
ATOM   2846  C  CB    . SER A 1 351 ? 142.153 117.644 111.078 1.00 26.47 ?  351 SER A CB    1 
ATOM   2847  O  OG    . SER A 1 351 ? 143.468 117.960 110.657 1.00 37.52 ?  351 SER A OG    1 
ATOM   2848  N  N     . GLU A 1 352 ? 140.180 118.715 113.287 1.00 28.97 ?  352 GLU A N     1 
ATOM   2849  C  CA    . GLU A 1 352 ? 139.056 118.432 114.173 1.00 28.01 ?  352 GLU A CA    1 
ATOM   2850  C  C     . GLU A 1 352 ? 137.975 119.502 114.066 1.00 28.74 ?  352 GLU A C     1 
ATOM   2851  O  O     . GLU A 1 352 ? 136.790 119.186 113.910 1.00 35.53 ?  352 GLU A O     1 
ATOM   2852  C  CB    . GLU A 1 352 ? 139.543 118.302 115.617 1.00 32.36 ?  352 GLU A CB    1 
ATOM   2853  C  CG    . GLU A 1 352 ? 140.714 117.348 115.795 1.00 33.22 ?  352 GLU A CG    1 
ATOM   2854  C  CD    . GLU A 1 352 ? 141.301 117.395 117.193 1.00 39.75 ?  352 GLU A CD    1 
ATOM   2855  O  OE1   . GLU A 1 352 ? 141.405 118.502 117.762 1.00 39.07 ?  352 GLU A OE1   1 
ATOM   2856  O  OE2   . GLU A 1 352 ? 141.664 116.323 117.722 1.00 42.88 -1 352 GLU A OE2   1 
ATOM   2857  N  N     . SER A 1 353 ? 138.360 120.776 114.144 1.00 34.78 ?  353 SER A N     1 
ATOM   2858  C  CA    . SER A 1 353 ? 137.401 121.869 114.209 1.00 26.15 ?  353 SER A CA    1 
ATOM   2859  C  C     . SER A 1 353 ? 137.565 122.905 113.107 1.00 27.16 ?  353 SER A C     1 
ATOM   2860  O  O     . SER A 1 353 ? 136.739 123.820 113.016 1.00 33.29 ?  353 SER A O     1 
ATOM   2861  C  CB    . SER A 1 353 ? 137.490 122.566 115.574 1.00 27.76 ?  353 SER A CB    1 
ATOM   2862  O  OG    . SER A 1 353 ? 138.763 123.155 115.761 1.00 28.71 ?  353 SER A OG    1 
ATOM   2863  N  N     . GLY A 1 354 ? 138.594 122.797 112.272 1.00 20.25 ?  354 GLY A N     1 
ATOM   2864  C  CA    . GLY A 1 354 ? 138.853 123.803 111.266 1.00 19.20 ?  354 GLY A CA    1 
ATOM   2865  C  C     . GLY A 1 354 ? 139.589 125.026 111.765 1.00 21.42 ?  354 GLY A C     1 
ATOM   2866  O  O     . GLY A 1 354 ? 139.894 125.914 110.961 1.00 24.99 ?  354 GLY A O     1 
ATOM   2867  N  N     . TYR A 1 355 ? 139.882 125.099 113.055 1.00 16.98 ?  355 TYR A N     1 
ATOM   2868  C  CA    . TYR A 1 355 ? 140.603 126.199 113.667 1.00 11.96 ?  355 TYR A CA    1 
ATOM   2869  C  C     . TYR A 1 355 ? 142.033 125.790 113.987 1.00 16.82 ?  355 TYR A C     1 
ATOM   2870  O  O     . TYR A 1 355 ? 142.355 124.599 114.040 1.00 27.20 ?  355 TYR A O     1 
ATOM   2871  C  CB    . TYR A 1 355 ? 139.908 126.663 114.953 1.00 22.11 ?  355 TYR A CB    1 
ATOM   2872  C  CG    . TYR A 1 355 ? 138.591 127.361 114.720 1.00 25.86 ?  355 TYR A CG    1 
ATOM   2873  C  CD1   . TYR A 1 355 ? 138.528 128.533 113.980 1.00 17.32 ?  355 TYR A CD1   1 
ATOM   2874  C  CD2   . TYR A 1 355 ? 137.410 126.849 115.238 1.00 27.95 ?  355 TYR A CD2   1 
ATOM   2875  C  CE1   . TYR A 1 355 ? 137.329 129.174 113.763 1.00 20.44 ?  355 TYR A CE1   1 
ATOM   2876  C  CE2   . TYR A 1 355 ? 136.206 127.486 115.027 1.00 23.54 ?  355 TYR A CE2   1 
ATOM   2877  C  CZ    . TYR A 1 355 ? 136.171 128.647 114.288 1.00 23.46 ?  355 TYR A CZ    1 
ATOM   2878  O  OH    . TYR A 1 355 ? 134.972 129.285 114.073 1.00 30.57 ?  355 TYR A OH    1 
ATOM   2879  N  N     . PRO A 1 356 ? 142.925 126.758 114.206 1.00 19.69 ?  356 PRO A N     1 
ATOM   2880  C  CA    . PRO A 1 356 ? 142.715 128.206 114.102 1.00 14.43 ?  356 PRO A CA    1 
ATOM   2881  C  C     . PRO A 1 356 ? 142.928 128.719 112.686 1.00 11.89 ?  356 PRO A C     1 
ATOM   2882  O  O     . PRO A 1 356 ? 143.467 128.010 111.843 1.00 17.30 ?  356 PRO A O     1 
ATOM   2883  C  CB    . PRO A 1 356 ? 143.768 128.765 115.064 1.00 10.89 ?  356 PRO A CB    1 
ATOM   2884  C  CG    . PRO A 1 356 ? 144.905 127.794 114.937 1.00 11.24 ?  356 PRO A CG    1 
ATOM   2885  C  CD    . PRO A 1 356 ? 144.262 126.440 114.738 1.00 14.30 ?  356 PRO A CD    1 
ATOM   2886  N  N     . TYR A 1 357 ? 142.514 129.947 112.390 1.00 21.77 ?  357 TYR A N     1 
ATOM   2887  C  CA    . TYR A 1 357 ? 142.984 130.599 111.179 1.00 13.74 ?  357 TYR A CA    1 
ATOM   2888  C  C     . TYR A 1 357 ? 144.491 130.802 111.272 1.00 7.83  ?  357 TYR A C     1 
ATOM   2889  O  O     . TYR A 1 357 ? 145.039 131.054 112.348 1.00 14.53 ?  357 TYR A O     1 
ATOM   2890  C  CB    . TYR A 1 357 ? 142.289 131.947 110.975 1.00 8.72  ?  357 TYR A CB    1 
ATOM   2891  C  CG    . TYR A 1 357 ? 140.800 131.945 111.234 1.00 7.28  ?  357 TYR A CG    1 
ATOM   2892  C  CD1   . TYR A 1 357 ? 140.018 130.843 110.920 1.00 13.76 ?  357 TYR A CD1   1 
ATOM   2893  C  CD2   . TYR A 1 357 ? 140.177 133.052 111.790 1.00 13.63 ?  357 TYR A CD2   1 
ATOM   2894  C  CE1   . TYR A 1 357 ? 138.658 130.843 111.151 1.00 12.91 ?  357 TYR A CE1   1 
ATOM   2895  C  CE2   . TYR A 1 357 ? 138.818 133.060 112.028 1.00 14.19 ?  357 TYR A CE2   1 
ATOM   2896  C  CZ    . TYR A 1 357 ? 138.064 131.953 111.707 1.00 17.35 ?  357 TYR A CZ    1 
ATOM   2897  O  OH    . TYR A 1 357 ? 136.710 131.960 111.941 1.00 26.80 ?  357 TYR A OH    1 
ATOM   2898  N  N     . ILE A 1 358 ? 145.169 130.677 110.138 1.00 13.94 ?  358 ILE A N     1 
ATOM   2899  C  CA    . ILE A 1 358 ? 146.615 130.839 110.071 1.00 13.42 ?  358 ILE A CA    1 
ATOM   2900  C  C     . ILE A 1 358 ? 146.913 132.128 109.321 1.00 15.14 ?  358 ILE A C     1 
ATOM   2901  O  O     . ILE A 1 358 ? 146.495 132.298 108.170 1.00 19.31 ?  358 ILE A O     1 
ATOM   2902  C  CB    . ILE A 1 358 ? 147.296 129.641 109.393 1.00 24.00 ?  358 ILE A CB    1 
ATOM   2903  C  CG1   . ILE A 1 358 ? 146.852 128.326 110.038 1.00 15.08 ?  358 ILE A CG1   1 
ATOM   2904  C  CG2   . ILE A 1 358 ? 148.809 129.790 109.456 1.00 17.35 ?  358 ILE A CG2   1 
ATOM   2905  C  CD1   . ILE A 1 358 ? 147.316 128.155 111.462 1.00 15.92 ?  358 ILE A CD1   1 
ATOM   2906  N  N     . MET A 1 359 ? 147.632 133.033 109.973 1.00 14.53 ?  359 MET A N     1 
ATOM   2907  C  CA    . MET A 1 359 ? 148.158 134.234 109.341 1.00 3.56  ?  359 MET A CA    1 
ATOM   2908  C  C     . MET A 1 359 ? 149.675 134.124 109.288 1.00 13.17 ?  359 MET A C     1 
ATOM   2909  O  O     . MET A 1 359 ? 150.325 133.991 110.330 1.00 13.36 ?  359 MET A O     1 
ATOM   2910  C  CB    . MET A 1 359 ? 147.739 135.491 110.100 1.00 9.22  ?  359 MET A CB    1 
ATOM   2911  C  CG    . MET A 1 359 ? 148.691 136.655 109.903 1.00 18.45 ?  359 MET A CG    1 
ATOM   2912  S  SD    . MET A 1 359 ? 147.899 138.269 109.948 1.00 32.53 ?  359 MET A SD    1 
ATOM   2913  C  CE    . MET A 1 359 ? 149.341 139.325 109.984 1.00 2.39  ?  359 MET A CE    1 
ATOM   2914  N  N     . PHE A 1 360 ? 150.231 134.178 108.084 1.00 10.75 ?  360 PHE A N     1 
ATOM   2915  C  CA    . PHE A 1 360 ? 151.680 134.176 107.903 1.00 1.81  ?  360 PHE A CA    1 
ATOM   2916  C  C     . PHE A 1 360 ? 152.137 135.629 107.928 1.00 13.50 ?  360 PHE A C     1 
ATOM   2917  O  O     . PHE A 1 360 ? 152.015 136.351 106.937 1.00 23.47 ?  360 PHE A O     1 
ATOM   2918  C  CB    . PHE A 1 360 ? 152.061 133.466 106.610 1.00 8.17  ?  360 PHE A CB    1 
ATOM   2919  C  CG    . PHE A 1 360 ? 151.725 132.003 106.611 1.00 15.69 ?  360 PHE A CG    1 
ATOM   2920  C  CD1   . PHE A 1 360 ? 152.228 131.165 107.593 1.00 13.48 ?  360 PHE A CD1   1 
ATOM   2921  C  CD2   . PHE A 1 360 ? 150.892 131.468 105.645 1.00 8.72  ?  360 PHE A CD2   1 
ATOM   2922  C  CE1   . PHE A 1 360 ? 151.914 129.821 107.603 1.00 14.08 ?  360 PHE A CE1   1 
ATOM   2923  C  CE2   . PHE A 1 360 ? 150.575 130.123 105.651 1.00 15.48 ?  360 PHE A CE2   1 
ATOM   2924  C  CZ    . PHE A 1 360 ? 151.087 129.300 106.633 1.00 17.40 ?  360 PHE A CZ    1 
ATOM   2925  N  N     . GLN A 1 361 ? 152.666 136.054 109.077 1.00 14.29 ?  361 GLN A N     1 
ATOM   2926  C  CA    . GLN A 1 361 ? 152.938 137.470 109.300 1.00 5.00  ?  361 GLN A CA    1 
ATOM   2927  C  C     . GLN A 1 361 ? 153.958 138.013 108.306 1.00 4.06  ?  361 GLN A C     1 
ATOM   2928  O  O     . GLN A 1 361 ? 153.796 139.121 107.786 1.00 11.39 ?  361 GLN A O     1 
ATOM   2929  C  CB    . GLN A 1 361 ? 153.420 137.682 110.735 1.00 14.61 ?  361 GLN A CB    1 
ATOM   2930  C  CG    . GLN A 1 361 ? 153.759 139.119 111.075 1.00 17.65 ?  361 GLN A CG    1 
ATOM   2931  C  CD    . GLN A 1 361 ? 153.504 139.447 112.529 1.00 22.82 ?  361 GLN A CD    1 
ATOM   2932  O  OE1   . GLN A 1 361 ? 154.010 138.774 113.425 1.00 25.87 ?  361 GLN A OE1   1 
ATOM   2933  N  NE2   . GLN A 1 361 ? 152.712 140.484 112.772 1.00 18.69 ?  361 GLN A NE2   1 
ATOM   2934  N  N     . ASP A 1 362 ? 155.018 137.251 108.033 1.00 20.62 ?  362 ASP A N     1 
ATOM   2935  C  CA    . ASP A 1 362 ? 156.055 137.738 107.130 1.00 10.72 ?  362 ASP A CA    1 
ATOM   2936  C  C     . ASP A 1 362 ? 155.576 137.765 105.685 1.00 11.20 ?  362 ASP A C     1 
ATOM   2937  O  O     . ASP A 1 362 ? 155.978 138.647 104.918 1.00 18.14 ?  362 ASP A O     1 
ATOM   2938  C  CB    . ASP A 1 362 ? 157.314 136.887 107.266 1.00 18.62 ?  362 ASP A CB    1 
ATOM   2939  C  CG    . ASP A 1 362 ? 158.087 137.194 108.535 1.00 26.98 ?  362 ASP A CG    1 
ATOM   2940  O  OD1   . ASP A 1 362 ? 157.639 136.776 109.621 1.00 26.50 ?  362 ASP A OD1   1 
ATOM   2941  O  OD2   . ASP A 1 362 ? 159.143 137.854 108.444 1.00 29.52 -1 362 ASP A OD2   1 
ATOM   2942  N  N     . ASN A 1 363 ? 154.725 136.817 105.293 1.00 10.83 ?  363 ASN A N     1 
ATOM   2943  C  CA    . ASN A 1 363 ? 154.116 136.884 103.969 1.00 12.56 ?  363 ASN A CA    1 
ATOM   2944  C  C     . ASN A 1 363 ? 153.269 138.140 103.827 1.00 15.55 ?  363 ASN A C     1 
ATOM   2945  O  O     . ASN A 1 363 ? 153.246 138.769 102.763 1.00 21.41 ?  363 ASN A O     1 
ATOM   2946  C  CB    . ASN A 1 363 ? 153.271 135.636 103.712 1.00 12.06 ?  363 ASN A CB    1 
ATOM   2947  C  CG    . ASN A 1 363 ? 154.108 134.422 103.375 1.00 8.91  ?  363 ASN A CG    1 
ATOM   2948  O  OD1   . ASN A 1 363 ? 155.229 134.542 102.883 1.00 19.44 ?  363 ASN A OD1   1 
ATOM   2949  N  ND2   . ASN A 1 363 ? 153.568 133.242 103.641 1.00 12.12 ?  363 ASN A ND2   1 
ATOM   2950  N  N     . VAL A 1 364 ? 152.560 138.515 104.892 1.00 13.53 ?  364 VAL A N     1 
ATOM   2951  C  CA    . VAL A 1 364 ? 151.719 139.705 104.849 1.00 9.34  ?  364 VAL A CA    1 
ATOM   2952  C  C     . VAL A 1 364 ? 152.571 140.968 104.813 1.00 11.03 ?  364 VAL A C     1 
ATOM   2953  O  O     . VAL A 1 364 ? 152.307 141.887 104.030 1.00 20.71 ?  364 VAL A O     1 
ATOM   2954  C  CB    . VAL A 1 364 ? 150.751 139.713 106.045 1.00 4.20  ?  364 VAL A CB    1 
ATOM   2955  C  CG1   . VAL A 1 364 ? 149.874 140.955 106.009 1.00 4.29  ?  364 VAL A CG1   1 
ATOM   2956  C  CG2   . VAL A 1 364 ? 149.904 138.452 106.055 1.00 0.00  ?  364 VAL A CG2   1 
ATOM   2957  N  N     . ASN A 1 365 ? 153.604 141.036 105.651 1.00 16.63 ?  365 ASN A N     1 
ATOM   2958  C  CA    . ASN A 1 365 ? 154.334 142.278 105.860 1.00 7.00  ?  365 ASN A CA    1 
ATOM   2959  C  C     . ASN A 1 365 ? 155.474 142.500 104.877 1.00 11.08 ?  365 ASN A C     1 
ATOM   2960  O  O     . ASN A 1 365 ? 155.995 143.618 104.811 1.00 17.79 ?  365 ASN A O     1 
ATOM   2961  C  CB    . ASN A 1 365 ? 154.880 142.332 107.288 1.00 5.65  ?  365 ASN A CB    1 
ATOM   2962  C  CG    . ASN A 1 365 ? 153.788 142.528 108.316 1.00 6.23  ?  365 ASN A CG    1 
ATOM   2963  O  OD1   . ASN A 1 365 ? 152.962 143.430 108.191 1.00 8.00  ?  365 ASN A OD1   1 
ATOM   2964  N  ND2   . ASN A 1 365 ? 153.776 141.683 109.335 1.00 11.93 ?  365 ASN A ND2   1 
ATOM   2965  N  N     . LYS A 1 366 ? 155.879 141.485 104.115 1.00 17.03 ?  366 LYS A N     1 
ATOM   2966  C  CA    . LYS A 1 366 ? 156.912 141.707 103.111 1.00 11.52 ?  366 LYS A CA    1 
ATOM   2967  C  C     . LYS A 1 366 ? 156.379 142.446 101.892 1.00 15.40 ?  366 LYS A C     1 
ATOM   2968  O  O     . LYS A 1 366 ? 157.170 142.993 101.116 1.00 23.08 ?  366 LYS A O     1 
ATOM   2969  C  CB    . LYS A 1 366 ? 157.543 140.380 102.683 1.00 17.58 ?  366 LYS A CB    1 
ATOM   2970  C  CG    . LYS A 1 366 ? 156.721 139.566 101.699 1.00 18.19 ?  366 LYS A CG    1 
ATOM   2971  C  CD    . LYS A 1 366 ? 157.301 138.171 101.537 1.00 20.44 ?  366 LYS A CD    1 
ATOM   2972  C  CE    . LYS A 1 366 ? 156.217 137.106 101.542 1.00 23.00 ?  366 LYS A CE    1 
ATOM   2973  N  NZ    . LYS A 1 366 ? 155.148 137.390 100.544 1.00 25.28 1  366 LYS A NZ    1 
ATOM   2974  N  N     . VAL A 1 367 ? 155.060 142.477 101.712 1.00 23.51 ?  367 VAL A N     1 
ATOM   2975  C  CA    . VAL A 1 367 ? 154.415 143.240 100.652 1.00 9.42  ?  367 VAL A CA    1 
ATOM   2976  C  C     . VAL A 1 367 ? 153.511 144.332 101.197 1.00 9.83  ?  367 VAL A C     1 
ATOM   2977  O  O     . VAL A 1 367 ? 152.853 145.022 100.412 1.00 20.43 ?  367 VAL A O     1 
ATOM   2978  C  CB    . VAL A 1 367 ? 153.624 142.320 99.700  1.00 14.14 ?  367 VAL A CB    1 
ATOM   2979  C  CG1   . VAL A 1 367 ? 154.572 141.438 98.907  1.00 12.11 ?  367 VAL A CG1   1 
ATOM   2980  C  CG2   . VAL A 1 367 ? 152.636 141.475 100.482 1.00 6.53  ?  367 VAL A CG2   1 
ATOM   2981  N  N     . HIS A 1 368 ? 153.459 144.510 102.513 1.00 16.31 ?  368 HIS A N     1 
ATOM   2982  C  CA    . HIS A 1 368 ? 152.605 145.527 103.109 1.00 2.49  ?  368 HIS A CA    1 
ATOM   2983  C  C     . HIS A 1 368 ? 153.111 146.917 102.743 1.00 15.02 ?  368 HIS A C     1 
ATOM   2984  O  O     . HIS A 1 368 ? 154.300 147.216 102.887 1.00 23.85 ?  368 HIS A O     1 
ATOM   2985  C  CB    . HIS A 1 368 ? 152.568 145.349 104.625 1.00 6.65  ?  368 HIS A CB    1 
ATOM   2986  C  CG    . HIS A 1 368 ? 151.592 146.244 105.319 1.00 1.87  ?  368 HIS A CG    1 
ATOM   2987  N  ND1   . HIS A 1 368 ? 151.806 146.732 106.590 1.00 13.82 ?  368 HIS A ND1   1 
ATOM   2988  C  CD2   . HIS A 1 368 ? 150.394 146.735 104.926 1.00 1.23  ?  368 HIS A CD2   1 
ATOM   2989  C  CE1   . HIS A 1 368 ? 150.783 147.486 106.947 1.00 12.06 ?  368 HIS A CE1   1 
ATOM   2990  N  NE2   . HIS A 1 368 ? 149.912 147.505 105.956 1.00 7.17  ?  368 HIS A NE2   1 
ATOM   2991  N  N     . ALA A 1 369 ? 152.202 147.767 102.263 1.00 12.15 ?  369 ALA A N     1 
ATOM   2992  C  CA    . ALA A 1 369 ? 152.578 149.104 101.820 1.00 9.24  ?  369 ALA A CA    1 
ATOM   2993  C  C     . ALA A 1 369 ? 152.645 150.114 102.956 1.00 12.23 ?  369 ALA A C     1 
ATOM   2994  O  O     . ALA A 1 369 ? 153.216 151.193 102.771 1.00 12.21 ?  369 ALA A O     1 
ATOM   2995  C  CB    . ALA A 1 369 ? 151.596 149.600 100.758 1.00 1.40  ?  369 ALA A CB    1 
ATOM   2996  N  N     . ASN A 1 370 ? 152.087 149.794 104.119 1.00 20.76 ?  370 ASN A N     1 
ATOM   2997  C  CA    . ASN A 1 370 ? 151.966 150.740 105.220 1.00 11.71 ?  370 ASN A CA    1 
ATOM   2998  C  C     . ASN A 1 370 ? 152.687 150.240 106.465 1.00 2.28  ?  370 ASN A C     1 
ATOM   2999  O  O     . ASN A 1 370 ? 152.218 150.418 107.589 1.00 12.93 ?  370 ASN A O     1 
ATOM   3000  C  CB    . ASN A 1 370 ? 150.498 151.028 105.524 1.00 5.58  ?  370 ASN A CB    1 
ATOM   3001  C  CG    . ASN A 1 370 ? 149.783 151.682 104.363 1.00 7.70  ?  370 ASN A CG    1 
ATOM   3002  O  OD1   . ASN A 1 370 ? 150.258 152.669 103.806 1.00 23.31 ?  370 ASN A OD1   1 
ATOM   3003  N  ND2   . ASN A 1 370 ? 148.638 151.131 103.987 1.00 9.87  ?  370 ASN A ND2   1 
ATOM   3004  N  N     . ASN A 1 371 ? 153.846 149.604 106.277 1.00 9.68  ?  371 ASN A N     1 
ATOM   3005  C  CA    . ASN A 1 371 ? 154.631 149.166 107.424 1.00 11.08 ?  371 ASN A CA    1 
ATOM   3006  C  C     . ASN A 1 371 ? 155.064 150.341 108.288 1.00 10.85 ?  371 ASN A C     1 
ATOM   3007  O  O     . ASN A 1 371 ? 155.294 150.176 109.491 1.00 21.21 ?  371 ASN A O     1 
ATOM   3008  C  CB    . ASN A 1 371 ? 155.850 148.371 106.957 1.00 9.10  ?  371 ASN A CB    1 
ATOM   3009  C  CG    . ASN A 1 371 ? 155.541 146.908 106.738 1.00 9.16  ?  371 ASN A CG    1 
ATOM   3010  O  OD1   . ASN A 1 371 ? 154.627 146.358 107.349 1.00 10.93 ?  371 ASN A OD1   1 
ATOM   3011  N  ND2   . ASN A 1 371 ? 156.303 146.267 105.865 1.00 16.42 ?  371 ASN A ND2   1 
ATOM   3012  N  N     . HIS A 1 372 ? 155.188 151.531 107.697 1.00 14.48 ?  372 HIS A N     1 
ATOM   3013  C  CA    . HIS A 1 372 ? 155.563 152.707 108.474 1.00 9.89  ?  372 HIS A CA    1 
ATOM   3014  C  C     . HIS A 1 372 ? 154.498 153.042 109.511 1.00 13.87 ?  372 HIS A C     1 
ATOM   3015  O  O     . HIS A 1 372 ? 154.819 153.437 110.636 1.00 26.28 ?  372 HIS A O     1 
ATOM   3016  C  CB    . HIS A 1 372 ? 155.807 153.896 107.546 1.00 14.30 ?  372 HIS A CB    1 
ATOM   3017  C  CG    . HIS A 1 372 ? 154.569 154.396 106.868 1.00 21.90 ?  372 HIS A CG    1 
ATOM   3018  N  ND1   . HIS A 1 372 ? 153.811 153.608 106.031 1.00 8.45  ?  372 HIS A ND1   1 
ATOM   3019  C  CD2   . HIS A 1 372 ? 153.957 155.603 106.907 1.00 18.03 ?  372 HIS A CD2   1 
ATOM   3020  C  CE1   . HIS A 1 372 ? 152.783 154.308 105.582 1.00 10.91 ?  372 HIS A CE1   1 
ATOM   3021  N  NE2   . HIS A 1 372 ? 152.851 155.522 106.097 1.00 21.38 ?  372 HIS A NE2   1 
ATOM   3022  N  N     . ILE A 1 373 ? 153.222 152.904 109.145 1.00 15.79 ?  373 ILE A N     1 
ATOM   3023  C  CA    . ILE A 1 373 ? 152.151 153.112 110.113 1.00 14.88 ?  373 ILE A CA    1 
ATOM   3024  C  C     . ILE A 1 373 ? 152.182 152.019 111.173 1.00 10.11 ?  373 ILE A C     1 
ATOM   3025  O  O     . ILE A 1 373 ? 152.132 152.292 112.377 1.00 25.47 ?  373 ILE A O     1 
ATOM   3026  C  CB    . ILE A 1 373 ? 150.789 153.167 109.400 1.00 16.28 ?  373 ILE A CB    1 
ATOM   3027  C  CG1   . ILE A 1 373 ? 150.775 154.292 108.364 1.00 13.05 ?  373 ILE A CG1   1 
ATOM   3028  C  CG2   . ILE A 1 373 ? 149.665 153.341 110.406 1.00 13.26 ?  373 ILE A CG2   1 
ATOM   3029  C  CD1   . ILE A 1 373 ? 149.579 154.260 107.445 1.00 9.33  ?  373 ILE A CD1   1 
ATOM   3030  N  N     . SER A 1 374 ? 152.262 150.767 110.737 1.00 14.43 ?  374 SER A N     1 
ATOM   3031  C  CA    . SER A 1 374 ? 152.401 149.619 111.619 1.00 6.43  ?  374 SER A CA    1 
ATOM   3032  C  C     . SER A 1 374 ? 152.461 148.375 110.748 1.00 11.38 ?  374 SER A C     1 
ATOM   3033  O  O     . SER A 1 374 ? 152.042 148.391 109.588 1.00 19.25 ?  374 SER A O     1 
ATOM   3034  C  CB    . SER A 1 374 ? 151.245 149.520 112.619 1.00 12.86 ?  374 SER A CB    1 
ATOM   3035  O  OG    . SER A 1 374 ? 151.374 148.373 113.438 1.00 17.11 ?  374 SER A OG    1 
ATOM   3036  N  N     . LYS A 1 375 ? 152.991 147.300 111.318 1.00 21.62 ?  375 LYS A N     1 
ATOM   3037  C  CA    . LYS A 1 375 ? 152.913 146.008 110.662 1.00 7.63  ?  375 LYS A CA    1 
ATOM   3038  C  C     . LYS A 1 375 ? 151.549 145.376 110.916 1.00 10.67 ?  375 LYS A C     1 
ATOM   3039  O  O     . LYS A 1 375 ? 150.855 145.700 111.882 1.00 18.59 ?  375 LYS A O     1 
ATOM   3040  C  CB    . LYS A 1 375 ? 154.023 145.079 111.151 1.00 4.80  ?  375 LYS A CB    1 
ATOM   3041  C  CG    . LYS A 1 375 ? 155.420 145.637 110.983 1.00 7.54  ?  375 LYS A CG    1 
ATOM   3042  C  CD    . LYS A 1 375 ? 156.214 144.830 109.975 1.00 14.83 ?  375 LYS A CD    1 
ATOM   3043  C  CE    . LYS A 1 375 ? 157.653 145.303 109.902 1.00 17.19 ?  375 LYS A CE    1 
ATOM   3044  N  NZ    . LYS A 1 375 ? 157.757 146.779 110.063 1.00 17.81 1  375 LYS A NZ    1 
ATOM   3045  N  N     . VAL A 1 376 ? 151.162 144.470 110.023 1.00 4.07  ?  376 VAL A N     1 
ATOM   3046  C  CA    . VAL A 1 376 ? 149.914 143.732 110.180 1.00 14.83 ?  376 VAL A CA    1 
ATOM   3047  C  C     . VAL A 1 376 ? 150.152 142.642 111.220 1.00 7.14  ?  376 VAL A C     1 
ATOM   3048  O  O     . VAL A 1 376 ? 150.942 141.722 110.999 1.00 22.02 ?  376 VAL A O     1 
ATOM   3049  C  CB    . VAL A 1 376 ? 149.436 143.143 108.848 1.00 7.92  ?  376 VAL A CB    1 
ATOM   3050  C  CG1   . VAL A 1 376 ? 148.117 142.408 109.028 1.00 0.00  ?  376 VAL A CG1   1 
ATOM   3051  C  CG2   . VAL A 1 376 ? 149.304 144.245 107.808 1.00 0.00  ?  376 VAL A CG2   1 
ATOM   3052  N  N     . LYS A 1 377 ? 149.474 142.749 112.361 1.00 5.16  ?  377 LYS A N     1 
ATOM   3053  C  CA    . LYS A 1 377 ? 149.693 141.835 113.472 1.00 9.42  ?  377 LYS A CA    1 
ATOM   3054  C  C     . LYS A 1 377 ? 148.651 140.733 113.569 1.00 7.95  ?  377 LYS A C     1 
ATOM   3055  O  O     . LYS A 1 377 ? 148.921 139.704 114.197 1.00 18.96 ?  377 LYS A O     1 
ATOM   3056  C  CB    . LYS A 1 377 ? 149.718 142.604 114.800 1.00 10.68 ?  377 LYS A CB    1 
ATOM   3057  C  CG    . LYS A 1 377 ? 150.705 143.753 114.848 1.00 9.38  ?  377 LYS A CG    1 
ATOM   3058  C  CD    . LYS A 1 377 ? 150.096 144.942 115.567 1.00 21.66 ?  377 LYS A CD    1 
ATOM   3059  C  CE    . LYS A 1 377 ? 150.713 146.248 115.110 1.00 20.05 ?  377 LYS A CE    1 
ATOM   3060  N  NZ    . LYS A 1 377 ? 149.910 147.410 115.570 1.00 20.67 1  377 LYS A NZ    1 
ATOM   3061  N  N     . PHE A 1 378 ? 147.476 140.916 112.977 1.00 7.13  ?  378 PHE A N     1 
ATOM   3062  C  CA    . PHE A 1 378 ? 146.420 139.915 113.046 1.00 7.24  ?  378 PHE A CA    1 
ATOM   3063  C  C     . PHE A 1 378 ? 145.439 140.174 111.910 1.00 9.38  ?  378 PHE A C     1 
ATOM   3064  O  O     . PHE A 1 378 ? 145.586 141.128 111.141 1.00 13.84 ?  378 PHE A O     1 
ATOM   3065  C  CB    . PHE A 1 378 ? 145.732 139.924 114.416 1.00 0.79  ?  378 PHE A CB    1 
ATOM   3066  C  CG    . PHE A 1 378 ? 144.877 141.135 114.669 1.00 6.65  ?  378 PHE A CG    1 
ATOM   3067  C  CD1   . PHE A 1 378 ? 145.420 142.407 114.638 1.00 7.64  ?  378 PHE A CD1   1 
ATOM   3068  C  CD2   . PHE A 1 378 ? 143.531 140.997 114.959 1.00 1.31  ?  378 PHE A CD2   1 
ATOM   3069  C  CE1   . PHE A 1 378 ? 144.636 143.516 114.877 1.00 3.48  ?  378 PHE A CE1   1 
ATOM   3070  C  CE2   . PHE A 1 378 ? 142.743 142.102 115.194 1.00 3.99  ?  378 PHE A CE2   1 
ATOM   3071  C  CZ    . PHE A 1 378 ? 143.296 143.362 115.159 1.00 10.30 ?  378 PHE A CZ    1 
ATOM   3072  N  N     . SER A 1 379 ? 144.441 139.307 111.805 1.00 0.00  ?  379 SER A N     1 
ATOM   3073  C  CA    . SER A 1 379 ? 143.445 139.366 110.747 1.00 4.78  ?  379 SER A CA    1 
ATOM   3074  C  C     . SER A 1 379 ? 142.051 139.465 111.366 1.00 5.09  ?  379 SER A C     1 
ATOM   3075  O  O     . SER A 1 379 ? 141.896 139.614 112.580 1.00 10.25 ?  379 SER A O     1 
ATOM   3076  C  CB    . SER A 1 379 ? 143.576 138.156 109.822 1.00 6.43  ?  379 SER A CB    1 
ATOM   3077  O  OG    . SER A 1 379 ? 142.925 138.389 108.589 1.00 10.12 ?  379 SER A OG    1 
ATOM   3078  N  N     . ASN A 1 380 ? 141.032 139.386 110.518 1.00 0.00  ?  380 ASN A N     1 
ATOM   3079  C  CA    . ASN A 1 380 ? 139.653 139.556 110.940 1.00 0.00  ?  380 ASN A CA    1 
ATOM   3080  C  C     . ASN A 1 380 ? 138.979 138.194 111.091 1.00 3.32  ?  380 ASN A C     1 
ATOM   3081  O  O     . ASN A 1 380 ? 139.619 137.142 111.026 1.00 12.17 ?  380 ASN A O     1 
ATOM   3082  C  CB    . ASN A 1 380 ? 138.905 140.450 109.950 1.00 2.88  ?  380 ASN A CB    1 
ATOM   3083  C  CG    . ASN A 1 380 ? 138.728 139.800 108.597 1.00 6.84  ?  380 ASN A CG    1 
ATOM   3084  O  OD1   . ASN A 1 380 ? 139.670 139.249 108.032 1.00 17.39 ?  380 ASN A OD1   1 
ATOM   3085  N  ND2   . ASN A 1 380 ? 137.514 139.858 108.072 1.00 7.76  ?  380 ASN A ND2   1 
ATOM   3086  N  N     . LEU A 1 381 ? 137.664 138.215 111.308 1.00 15.33 ?  381 LEU A N     1 
ATOM   3087  C  CA    . LEU A 1 381 ? 136.904 136.985 111.485 1.00 8.00  ?  381 LEU A CA    1 
ATOM   3088  C  C     . LEU A 1 381 ? 136.837 136.153 110.211 1.00 7.12  ?  381 LEU A C     1 
ATOM   3089  O  O     . LEU A 1 381 ? 136.576 134.948 110.286 1.00 16.05 ?  381 LEU A O     1 
ATOM   3090  C  CB    . LEU A 1 381 ? 135.492 137.315 111.974 1.00 14.89 ?  381 LEU A CB    1 
ATOM   3091  C  CG    . LEU A 1 381 ? 134.492 136.168 112.123 1.00 13.05 ?  381 LEU A CG    1 
ATOM   3092  C  CD1   . LEU A 1 381 ? 134.940 135.189 113.194 1.00 17.61 ?  381 LEU A CD1   1 
ATOM   3093  C  CD2   . LEU A 1 381 ? 133.114 136.713 112.436 1.00 12.16 ?  381 LEU A CD2   1 
ATOM   3094  N  N     . CYS A 1 382 ? 137.067 136.760 109.049 1.00 12.12 ?  382 CYS A N     1 
ATOM   3095  C  CA    . CYS A 1 382 ? 137.064 136.048 107.779 1.00 0.00  ?  382 CYS A CA    1 
ATOM   3096  C  C     . CYS A 1 382 ? 138.464 135.833 107.217 1.00 5.60  ?  382 CYS A C     1 
ATOM   3097  O  O     . CYS A 1 382 ? 138.603 135.186 106.177 1.00 12.94 ?  382 CYS A O     1 
ATOM   3098  C  CB    . CYS A 1 382 ? 136.202 136.796 106.758 1.00 17.28 ?  382 CYS A CB    1 
ATOM   3099  S  SG    . CYS A 1 382 ? 134.467 136.972 107.236 1.00 30.70 ?  382 CYS A SG    1 
ATOM   3100  N  N     . SER A 1 383 ? 139.494 136.361 107.874 1.00 3.93  ?  383 SER A N     1 
ATOM   3101  C  CA    . SER A 1 383 ? 140.907 136.112 107.589 1.00 6.81  ?  383 SER A CA    1 
ATOM   3102  C  C     . SER A 1 383 ? 141.429 136.799 106.332 1.00 17.81 ?  383 SER A C     1 
ATOM   3103  O  O     . SER A 1 383 ? 142.519 136.439 105.867 1.00 21.39 ?  383 SER A O     1 
ATOM   3104  C  CB    . SER A 1 383 ? 141.205 134.614 107.471 1.00 7.53  ?  383 SER A CB    1 
ATOM   3105  O  OG    . SER A 1 383 ? 140.910 133.941 108.680 1.00 32.06 ?  383 SER A OG    1 
ATOM   3106  N  N     . GLU A 1 384 ? 140.714 137.766 105.762 1.00 7.03  ?  384 GLU A N     1 
ATOM   3107  C  CA    . GLU A 1 384 ? 141.194 138.437 104.563 1.00 9.42  ?  384 GLU A CA    1 
ATOM   3108  C  C     . GLU A 1 384 ? 141.553 139.902 104.778 1.00 6.00  ?  384 GLU A C     1 
ATOM   3109  O  O     . GLU A 1 384 ? 142.115 140.520 103.870 1.00 21.79 ?  384 GLU A O     1 
ATOM   3110  C  CB    . GLU A 1 384 ? 140.161 138.321 103.428 1.00 0.00  ?  384 GLU A CB    1 
ATOM   3111  C  CG    . GLU A 1 384 ? 139.328 139.564 103.170 1.00 7.53  ?  384 GLU A CG    1 
ATOM   3112  C  CD    . GLU A 1 384 ? 138.276 139.804 104.231 1.00 19.90 ?  384 GLU A CD    1 
ATOM   3113  O  OE1   . GLU A 1 384 ? 137.656 140.888 104.222 1.00 17.81 ?  384 GLU A OE1   1 
ATOM   3114  O  OE2   . GLU A 1 384 ? 138.054 138.902 105.064 1.00 8.34  -1 384 GLU A OE2   1 
ATOM   3115  N  N     . VAL A 1 385 ? 141.262 140.468 105.943 1.00 1.82  ?  385 VAL A N     1 
ATOM   3116  C  CA    . VAL A 1 385 ? 141.592 141.859 106.231 1.00 2.90  ?  385 VAL A CA    1 
ATOM   3117  C  C     . VAL A 1 385 ? 142.992 141.909 106.831 1.00 16.10 ?  385 VAL A C     1 
ATOM   3118  O  O     . VAL A 1 385 ? 143.245 141.322 107.887 1.00 16.66 ?  385 VAL A O     1 
ATOM   3119  C  CB    . VAL A 1 385 ? 140.562 142.493 107.176 1.00 4.72  ?  385 VAL A CB    1 
ATOM   3120  C  CG1   . VAL A 1 385 ? 140.972 143.912 107.529 1.00 10.24 ?  385 VAL A CG1   1 
ATOM   3121  C  CG2   . VAL A 1 385 ? 139.189 142.478 106.540 1.00 0.00  ?  385 VAL A CG2   1 
ATOM   3122  N  N     . LEU A 1 386 ? 143.901 142.613 106.153 1.00 7.97  ?  386 LEU A N     1 
ATOM   3123  C  CA    . LEU A 1 386 ? 145.302 142.715 106.572 1.00 0.00  ?  386 LEU A CA    1 
ATOM   3124  C  C     . LEU A 1 386 ? 145.708 144.184 106.475 1.00 5.13  ?  386 LEU A C     1 
ATOM   3125  O  O     . LEU A 1 386 ? 146.098 144.662 105.408 1.00 15.28 ?  386 LEU A O     1 
ATOM   3126  C  CB    . LEU A 1 386 ? 146.197 141.824 105.722 1.00 3.36  ?  386 LEU A CB    1 
ATOM   3127  C  CG    . LEU A 1 386 ? 145.818 140.344 105.666 1.00 8.27  ?  386 LEU A CG    1 
ATOM   3128  C  CD1   . LEU A 1 386 ? 146.695 139.615 104.669 1.00 8.33  ?  386 LEU A CD1   1 
ATOM   3129  C  CD2   . LEU A 1 386 ? 145.926 139.711 107.043 1.00 0.00  ?  386 LEU A CD2   1 
ATOM   3130  N  N     . GLN A 1 387 ? 145.622 144.891 107.600 1.00 14.48 ?  387 GLN A N     1 
ATOM   3131  C  CA    . GLN A 1 387 ? 145.904 146.316 107.641 1.00 2.49  ?  387 GLN A CA    1 
ATOM   3132  C  C     . GLN A 1 387 ? 146.724 146.645 108.878 1.00 9.61  ?  387 GLN A C     1 
ATOM   3133  O  O     . GLN A 1 387 ? 146.721 145.911 109.868 1.00 14.33 ?  387 GLN A O     1 
ATOM   3134  C  CB    . GLN A 1 387 ? 144.615 147.146 107.632 1.00 0.00  ?  387 GLN A CB    1 
ATOM   3135  C  CG    . GLN A 1 387 ? 143.674 146.814 106.495 1.00 0.00  ?  387 GLN A CG    1 
ATOM   3136  C  CD    . GLN A 1 387 ? 142.461 147.713 106.471 1.00 7.72  ?  387 GLN A CD    1 
ATOM   3137  O  OE1   . GLN A 1 387 ? 142.459 148.786 107.070 1.00 19.89 ?  387 GLN A OE1   1 
ATOM   3138  N  NE2   . GLN A 1 387 ? 141.418 147.279 105.778 1.00 9.75  ?  387 GLN A NE2   1 
ATOM   3139  N  N     . ALA A 1 388 ? 147.438 147.764 108.801 1.00 8.13  ?  388 ALA A N     1 
ATOM   3140  C  CA    . ALA A 1 388 ? 148.173 148.270 109.950 1.00 6.05  ?  388 ALA A CA    1 
ATOM   3141  C  C     . ALA A 1 388 ? 147.210 148.750 111.028 1.00 10.83 ?  388 ALA A C     1 
ATOM   3142  O  O     . ALA A 1 388 ? 146.217 149.424 110.743 1.00 23.06 ?  388 ALA A O     1 
ATOM   3143  C  CB    . ALA A 1 388 ? 149.097 149.412 109.527 1.00 4.01  ?  388 ALA A CB    1 
ATOM   3144  N  N     . SER A 1 389 ? 147.512 148.403 112.275 1.00 15.63 ?  389 SER A N     1 
ATOM   3145  C  CA    . SER A 1 389 ? 146.707 148.811 113.414 1.00 0.00  ?  389 SER A CA    1 
ATOM   3146  C  C     . SER A 1 389 ? 147.610 149.395 114.490 1.00 13.98 ?  389 SER A C     1 
ATOM   3147  O  O     . SER A 1 389 ? 148.769 148.998 114.634 1.00 21.13 ?  389 SER A O     1 
ATOM   3148  C  CB    . SER A 1 389 ? 145.902 147.638 113.995 1.00 13.55 ?  389 SER A CB    1 
ATOM   3149  O  OG    . SER A 1 389 ? 146.713 146.487 114.156 1.00 17.08 ?  389 SER A OG    1 
ATOM   3150  N  N     . GLN A 1 390 ? 147.068 150.350 115.238 1.00 19.32 ?  390 GLN A N     1 
ATOM   3151  C  CA    . GLN A 1 390 ? 147.754 150.948 116.376 1.00 12.56 ?  390 GLN A CA    1 
ATOM   3152  C  C     . GLN A 1 390 ? 146.880 150.766 117.606 1.00 11.21 ?  390 GLN A C     1 
ATOM   3153  O  O     . GLN A 1 390 ? 145.713 151.170 117.608 1.00 24.29 ?  390 GLN A O     1 
ATOM   3154  C  CB    . GLN A 1 390 ? 148.049 152.428 116.127 1.00 11.58 ?  390 GLN A CB    1 
ATOM   3155  C  CG    . GLN A 1 390 ? 149.110 152.667 115.066 1.00 10.90 ?  390 GLN A CG    1 
ATOM   3156  C  CD    . GLN A 1 390 ? 149.351 154.137 114.796 1.00 17.06 ?  390 GLN A CD    1 
ATOM   3157  O  OE1   . GLN A 1 390 ? 148.641 154.999 115.310 1.00 31.36 ?  390 GLN A OE1   1 
ATOM   3158  N  NE2   . GLN A 1 390 ? 150.357 154.429 113.982 1.00 17.47 ?  390 GLN A NE2   1 
ATOM   3159  N  N     . VAL A 1 391 ? 147.445 150.158 118.650 1.00 15.83 ?  391 VAL A N     1 
ATOM   3160  C  CA    . VAL A 1 391 ? 146.676 149.877 119.854 1.00 16.86 ?  391 VAL A CA    1 
ATOM   3161  C  C     . VAL A 1 391 ? 146.297 151.183 120.541 1.00 16.06 ?  391 VAL A C     1 
ATOM   3162  O  O     . VAL A 1 391 ? 147.004 152.195 120.449 1.00 19.15 ?  391 VAL A O     1 
ATOM   3163  C  CB    . VAL A 1 391 ? 147.467 148.957 120.801 1.00 19.54 ?  391 VAL A CB    1 
ATOM   3164  C  CG1   . VAL A 1 391 ? 148.529 149.748 121.548 1.00 15.01 ?  391 VAL A CG1   1 
ATOM   3165  C  CG2   . VAL A 1 391 ? 146.528 148.255 121.768 1.00 7.30  ?  391 VAL A CG2   1 
ATOM   3166  N  N     . SER A 1 392 ? 145.164 151.163 121.234 1.00 21.95 ?  392 SER A N     1 
ATOM   3167  C  CA    . SER A 1 392 ? 144.682 152.309 121.987 1.00 14.67 ?  392 SER A CA    1 
ATOM   3168  C  C     . SER A 1 392 ? 145.070 152.171 123.453 1.00 22.52 ?  392 SER A C     1 
ATOM   3169  O  O     . SER A 1 392 ? 145.301 151.068 123.953 1.00 28.47 ?  392 SER A O     1 
ATOM   3170  C  CB    . SER A 1 392 ? 143.164 152.448 121.863 1.00 16.16 ?  392 SER A CB    1 
ATOM   3171  O  OG    . SER A 1 392 ? 142.777 152.629 120.514 1.00 23.92 ?  392 SER A OG    1 
ATOM   3172  N  N     . SER A 1 393 ? 145.143 153.305 124.137 1.00 22.99 ?  393 SER A N     1 
ATOM   3173  C  CA    . SER A 1 393 ? 145.454 153.354 125.562 1.00 20.74 ?  393 SER A CA    1 
ATOM   3174  C  C     . SER A 1 393 ? 144.227 153.895 126.284 1.00 21.33 ?  393 SER A C     1 
ATOM   3175  O  O     . SER A 1 393 ? 144.070 155.109 126.442 1.00 23.79 ?  393 SER A O     1 
ATOM   3176  C  CB    . SER A 1 393 ? 146.685 154.215 125.827 1.00 26.23 ?  393 SER A CB    1 
ATOM   3177  O  OG    . SER A 1 393 ? 146.956 154.298 127.214 1.00 29.03 ?  393 SER A OG    1 
ATOM   3178  N  N     . TYR A 1 394 ? 143.359 152.989 126.722 1.00 24.40 ?  394 TYR A N     1 
ATOM   3179  C  CA    . TYR A 1 394 ? 142.161 153.356 127.467 1.00 23.04 ?  394 TYR A CA    1 
ATOM   3180  C  C     . TYR A 1 394 ? 142.536 153.469 128.940 1.00 23.25 ?  394 TYR A C     1 
ATOM   3181  O  O     . TYR A 1 394 ? 142.863 152.468 129.586 1.00 26.60 ?  394 TYR A O     1 
ATOM   3182  C  CB    . TYR A 1 394 ? 141.053 152.334 127.237 1.00 19.37 ?  394 TYR A CB    1 
ATOM   3183  C  CG    . TYR A 1 394 ? 140.588 152.293 125.802 1.00 24.16 ?  394 TYR A CG    1 
ATOM   3184  C  CD1   . TYR A 1 394 ? 139.814 153.315 125.273 1.00 17.87 ?  394 TYR A CD1   1 
ATOM   3185  C  CD2   . TYR A 1 394 ? 140.940 151.240 124.968 1.00 20.10 ?  394 TYR A CD2   1 
ATOM   3186  C  CE1   . TYR A 1 394 ? 139.393 153.284 123.961 1.00 20.32 ?  394 TYR A CE1   1 
ATOM   3187  C  CE2   . TYR A 1 394 ? 140.524 151.202 123.655 1.00 18.67 ?  394 TYR A CE2   1 
ATOM   3188  C  CZ    . TYR A 1 394 ? 139.751 152.226 123.156 1.00 26.76 ?  394 TYR A CZ    1 
ATOM   3189  O  OH    . TYR A 1 394 ? 139.336 152.190 121.846 1.00 32.78 ?  394 TYR A OH    1 
ATOM   3190  N  N     . THR A 1 395 ? 142.497 154.688 129.462 1.00 25.83 ?  395 THR A N     1 
ATOM   3191  C  CA    . THR A 1 395 ? 142.953 154.994 130.805 1.00 29.00 ?  395 THR A CA    1 
ATOM   3192  C  C     . THR A 1 395 ? 141.777 154.994 131.779 1.00 26.44 ?  395 THR A C     1 
ATOM   3193  O  O     . THR A 1 395 ? 140.659 154.586 131.447 1.00 26.81 ?  395 THR A O     1 
ATOM   3194  C  CB    . THR A 1 395 ? 143.694 156.332 130.800 1.00 30.37 ?  395 THR A CB    1 
ATOM   3195  O  OG1   . THR A 1 395 ? 142.795 157.374 130.404 1.00 32.71 ?  395 THR A OG1   1 
ATOM   3196  C  CG2   . THR A 1 395 ? 144.857 156.286 129.826 1.00 28.05 ?  395 THR A CG2   1 
ATOM   3197  N  N     . ASP A 1 396 ? 142.029 155.449 133.002 1.00 31.54 ?  396 ASP A N     1 
ATOM   3198  C  CA    . ASP A 1 396 ? 140.998 155.492 134.025 1.00 31.54 ?  396 ASP A CA    1 
ATOM   3199  C  C     . ASP A 1 396 ? 139.929 156.520 133.668 1.00 28.16 ?  396 ASP A C     1 
ATOM   3200  O  O     . ASP A 1 396 ? 140.134 157.413 132.844 1.00 35.50 ?  396 ASP A O     1 
ATOM   3201  C  CB    . ASP A 1 396 ? 141.605 155.833 135.386 1.00 27.95 ?  396 ASP A CB    1 
ATOM   3202  C  CG    . ASP A 1 396 ? 142.567 154.774 135.876 1.00 34.85 ?  396 ASP A CG    1 
ATOM   3203  O  OD1   . ASP A 1 396 ? 142.218 153.578 135.820 1.00 36.98 ?  396 ASP A OD1   1 
ATOM   3204  O  OD2   . ASP A 1 396 ? 143.674 155.140 136.324 1.00 40.08 -1 396 ASP A OD2   1 
ATOM   3205  N  N     . TYR A 1 397 ? 138.768 156.377 134.302 1.00 28.45 ?  397 TYR A N     1 
ATOM   3206  C  CA    . TYR A 1 397 ? 137.717 157.372 134.153 1.00 27.80 ?  397 TYR A CA    1 
ATOM   3207  C  C     . TYR A 1 397 ? 138.237 158.743 134.568 1.00 32.55 ?  397 TYR A C     1 
ATOM   3208  O  O     . TYR A 1 397 ? 138.987 158.874 135.539 1.00 38.66 ?  397 TYR A O     1 
ATOM   3209  C  CB    . TYR A 1 397 ? 136.499 156.992 134.997 1.00 31.38 ?  397 TYR A CB    1 
ATOM   3210  C  CG    . TYR A 1 397 ? 135.211 157.637 134.541 1.00 30.56 ?  397 TYR A CG    1 
ATOM   3211  C  CD1   . TYR A 1 397 ? 134.384 157.008 133.622 1.00 30.51 ?  397 TYR A CD1   1 
ATOM   3212  C  CD2   . TYR A 1 397 ? 134.826 158.880 135.027 1.00 26.46 ?  397 TYR A CD2   1 
ATOM   3213  C  CE1   . TYR A 1 397 ? 133.208 157.594 133.204 1.00 24.97 ?  397 TYR A CE1   1 
ATOM   3214  C  CE2   . TYR A 1 397 ? 133.653 159.474 134.613 1.00 28.75 ?  397 TYR A CE2   1 
ATOM   3215  C  CZ    . TYR A 1 397 ? 132.848 158.826 133.703 1.00 27.24 ?  397 TYR A CZ    1 
ATOM   3216  O  OH    . TYR A 1 397 ? 131.677 159.415 133.286 1.00 36.56 ?  397 TYR A OH    1 
ATOM   3217  N  N     . ASP A 1 398 ? 137.834 159.768 133.824 1.00 35.84 ?  398 ASP A N     1 
ATOM   3218  C  CA    . ASP A 1 398 ? 138.273 161.152 133.980 1.00 40.14 ?  398 ASP A CA    1 
ATOM   3219  C  C     . ASP A 1 398 ? 139.665 161.364 133.399 1.00 42.08 ?  398 ASP A C     1 
ATOM   3220  O  O     . ASP A 1 398 ? 140.142 162.506 133.385 1.00 44.94 ?  398 ASP A O     1 
ATOM   3221  C  CB    . ASP A 1 398 ? 138.267 161.621 135.444 1.00 38.45 ?  398 ASP A CB    1 
ATOM   3222  C  CG    . ASP A 1 398 ? 136.877 161.628 136.049 1.00 45.01 ?  398 ASP A CG    1 
ATOM   3223  O  OD1   . ASP A 1 398 ? 135.958 162.195 135.422 1.00 44.45 ?  398 ASP A OD1   1 
ATOM   3224  O  OD2   . ASP A 1 398 ? 136.705 161.068 137.152 1.00 47.36 -1 398 ASP A OD2   1 
ATOM   3225  N  N     . GLU A 1 399 ? 140.333 160.317 132.925 1.00 40.94 ?  399 GLU A N     1 
ATOM   3226  C  CA    . GLU A 1 399 ? 141.616 160.437 132.248 1.00 34.67 ?  399 GLU A CA    1 
ATOM   3227  C  C     . GLU A 1 399 ? 141.395 160.348 130.744 1.00 38.63 ?  399 GLU A C     1 
ATOM   3228  O  O     . GLU A 1 399 ? 140.618 159.508 130.276 1.00 41.58 ?  399 GLU A O     1 
ATOM   3229  C  CB    . GLU A 1 399 ? 142.583 159.345 132.705 1.00 34.73 ?  399 GLU A CB    1 
ATOM   3230  C  CG    . GLU A 1 399 ? 143.649 159.819 133.675 1.00 38.74 ?  399 GLU A CG    1 
ATOM   3231  C  CD    . GLU A 1 399 ? 144.811 158.849 133.777 1.00 45.84 ?  399 GLU A CD    1 
ATOM   3232  O  OE1   . GLU A 1 399 ? 144.782 157.972 134.665 1.00 44.50 ?  399 GLU A OE1   1 
ATOM   3233  O  OE2   . GLU A 1 399 ? 145.754 158.963 132.966 1.00 46.70 -1 399 GLU A OE2   1 
ATOM   3234  N  N     . GLU A 1 400 ? 142.068 161.217 129.995 1.00 39.04 ?  400 GLU A N     1 
ATOM   3235  C  CA    . GLU A 1 400 ? 141.952 161.190 128.544 1.00 34.05 ?  400 GLU A CA    1 
ATOM   3236  C  C     . GLU A 1 400 ? 142.493 159.878 127.989 1.00 34.81 ?  400 GLU A C     1 
ATOM   3237  O  O     . GLU A 1 400 ? 143.533 159.380 128.426 1.00 31.67 ?  400 GLU A O     1 
ATOM   3238  C  CB    . GLU A 1 400 ? 142.703 162.369 127.925 1.00 33.64 ?  400 GLU A CB    1 
ATOM   3239  C  CG    . GLU A 1 400 ? 141.916 163.669 127.897 1.00 38.20 ?  400 GLU A CG    1 
ATOM   3240  C  CD    . GLU A 1 400 ? 140.420 163.442 127.819 1.00 44.87 ?  400 GLU A CD    1 
ATOM   3241  O  OE1   . GLU A 1 400 ? 139.902 163.246 126.700 1.00 43.14 ?  400 GLU A OE1   1 
ATOM   3242  O  OE2   . GLU A 1 400 ? 139.759 163.463 128.879 1.00 45.42 -1 400 GLU A OE2   1 
ATOM   3243  N  N     . ASP A 1 401 ? 141.778 159.320 127.019 1.00 31.72 ?  401 ASP A N     1 
ATOM   3244  C  CA    . ASP A 1 401 ? 142.202 158.100 126.351 1.00 25.80 ?  401 ASP A CA    1 
ATOM   3245  C  C     . ASP A 1 401 ? 143.119 158.426 125.180 1.00 25.58 ?  401 ASP A C     1 
ATOM   3246  O  O     . ASP A 1 401 ? 143.009 159.483 124.553 1.00 28.01 ?  401 ASP A O     1 
ATOM   3247  C  CB    . ASP A 1 401 ? 140.995 157.303 125.854 1.00 22.94 ?  401 ASP A CB    1 
ATOM   3248  C  CG    . ASP A 1 401 ? 140.205 156.674 126.982 1.00 29.01 ?  401 ASP A CG    1 
ATOM   3249  O  OD1   . ASP A 1 401 ? 140.815 156.315 128.009 1.00 28.66 ?  401 ASP A OD1   1 
ATOM   3250  O  OD2   . ASP A 1 401 ? 138.974 156.534 126.838 1.00 30.86 -1 401 ASP A OD2   1 
ATOM   3251  N  N     . GLU A 1 402 ? 144.034 157.505 124.893 1.00 30.01 ?  402 GLU A N     1 
ATOM   3252  C  CA    . GLU A 1 402 ? 144.934 157.612 123.747 1.00 24.91 ?  402 GLU A CA    1 
ATOM   3253  C  C     . GLU A 1 402 ? 144.375 156.718 122.647 1.00 22.14 ?  402 GLU A C     1 
ATOM   3254  O  O     . GLU A 1 402 ? 144.693 155.529 122.575 1.00 28.63 ?  402 GLU A O     1 
ATOM   3255  C  CB    . GLU A 1 402 ? 146.356 157.217 124.128 1.00 26.08 ?  402 GLU A CB    1 
ATOM   3256  C  CG    . GLU A 1 402 ? 147.064 158.227 125.011 1.00 27.99 ?  402 GLU A CG    1 
ATOM   3257  C  CD    . GLU A 1 402 ? 147.769 157.578 126.187 1.00 39.47 ?  402 GLU A CD    1 
ATOM   3258  O  OE1   . GLU A 1 402 ? 147.112 157.351 127.224 1.00 38.05 ?  402 GLU A OE1   1 
ATOM   3259  O  OE2   . GLU A 1 402 ? 148.982 157.299 126.073 1.00 40.37 -1 402 GLU A OE2   1 
ATOM   3260  N  N     . ILE A 1 403 ? 143.542 157.294 121.790 1.00 22.07 ?  403 ILE A N     1 
ATOM   3261  C  CA    . ILE A 1 403 ? 142.854 156.524 120.761 1.00 22.67 ?  403 ILE A CA    1 
ATOM   3262  C  C     . ILE A 1 403 ? 143.840 156.165 119.660 1.00 23.60 ?  403 ILE A C     1 
ATOM   3263  O  O     . ILE A 1 403 ? 144.514 157.038 119.101 1.00 26.02 ?  403 ILE A O     1 
ATOM   3264  C  CB    . ILE A 1 403 ? 141.659 157.311 120.202 1.00 18.54 ?  403 ILE A CB    1 
ATOM   3265  C  CG1   . ILE A 1 403 ? 140.711 157.713 121.336 1.00 21.77 ?  403 ILE A CG1   1 
ATOM   3266  C  CG2   . ILE A 1 403 ? 140.926 156.490 119.155 1.00 13.00 ?  403 ILE A CG2   1 
ATOM   3267  C  CD1   . ILE A 1 403 ? 140.335 156.574 122.255 1.00 21.95 ?  403 ILE A CD1   1 
ATOM   3268  N  N     . GLY A 1 404 ? 143.930 154.881 119.352 1.00 21.16 ?  404 GLY A N     1 
ATOM   3269  C  CA    . GLY A 1 404 ? 144.782 154.378 118.292 1.00 3.41  ?  404 GLY A CA    1 
ATOM   3270  C  C     . GLY A 1 404 ? 144.022 154.202 116.995 1.00 14.72 ?  404 GLY A C     1 
ATOM   3271  O  O     . GLY A 1 404 ? 143.095 154.958 116.686 1.00 28.63 ?  404 GLY A O     1 
ATOM   3272  N  N     . LEU A 1 405 ? 144.421 153.196 116.223 1.00 22.00 ?  405 LEU A N     1 
ATOM   3273  C  CA    . LEU A 1 405 ? 143.786 152.877 114.952 1.00 5.36  ?  405 LEU A CA    1 
ATOM   3274  C  C     . LEU A 1 405 ? 143.268 151.449 115.007 1.00 7.03  ?  405 LEU A C     1 
ATOM   3275  O  O     . LEU A 1 405 ? 144.048 150.509 115.188 1.00 10.10 ?  405 LEU A O     1 
ATOM   3276  C  CB    . LEU A 1 405 ? 144.766 153.051 113.789 1.00 12.69 ?  405 LEU A CB    1 
ATOM   3277  C  CG    . LEU A 1 405 ? 145.301 154.464 113.544 1.00 15.33 ?  405 LEU A CG    1 
ATOM   3278  C  CD1   . LEU A 1 405 ? 146.356 154.456 112.452 1.00 16.24 ?  405 LEU A CD1   1 
ATOM   3279  C  CD2   . LEU A 1 405 ? 144.172 155.421 113.197 1.00 13.02 ?  405 LEU A CD2   1 
ATOM   3280  N  N     . ASP A 1 406 ? 141.957 151.291 114.857 1.00 16.96 ?  406 ASP A N     1 
ATOM   3281  C  CA    . ASP A 1 406 ? 141.332 149.985 114.736 1.00 15.39 ?  406 ASP A CA    1 
ATOM   3282  C  C     . ASP A 1 406 ? 140.855 149.786 113.305 1.00 15.17 ?  406 ASP A C     1 
ATOM   3283  O  O     . ASP A 1 406 ? 140.339 150.709 112.671 1.00 26.28 ?  406 ASP A O     1 
ATOM   3284  C  CB    . ASP A 1 406 ? 140.161 149.834 115.711 1.00 6.55  ?  406 ASP A CB    1 
ATOM   3285  C  CG    . ASP A 1 406 ? 140.605 149.384 117.088 1.00 23.91 ?  406 ASP A CG    1 
ATOM   3286  O  OD1   . ASP A 1 406 ? 141.812 149.120 117.270 1.00 26.78 ?  406 ASP A OD1   1 
ATOM   3287  O  OD2   . ASP A 1 406 ? 139.747 149.293 117.990 1.00 28.59 -1 406 ASP A OD2   1 
ATOM   3288  N  N     . ILE A 1 407 ? 141.027 148.574 112.802 1.00 12.78 ?  407 ILE A N     1 
ATOM   3289  C  CA    . ILE A 1 407 ? 140.822 148.280 111.389 1.00 15.53 ?  407 ILE A CA    1 
ATOM   3290  C  C     . ILE A 1 407 ? 139.350 148.013 111.128 1.00 10.41 ?  407 ILE A C     1 
ATOM   3291  O  O     . ILE A 1 407 ? 138.661 147.369 111.930 1.00 17.18 ?  407 ILE A O     1 
ATOM   3292  C  CB    . ILE A 1 407 ? 141.687 147.089 110.938 1.00 7.27  ?  407 ILE A CB    1 
ATOM   3293  C  CG1   . ILE A 1 407 ? 143.166 147.381 111.191 1.00 2.93  ?  407 ILE A CG1   1 
ATOM   3294  C  CG2   . ILE A 1 407 ? 141.445 146.783 109.473 1.00 13.04 ?  407 ILE A CG2   1 
ATOM   3295  C  CD1   . ILE A 1 407 ? 143.951 146.180 111.651 1.00 5.97  ?  407 ILE A CD1   1 
ATOM   3296  N  N     . SER A 1 408 ? 138.865 148.525 110.002 1.00 18.24 ?  408 SER A N     1 
ATOM   3297  C  CA    . SER A 1 408 ? 137.537 148.232 109.488 1.00 11.26 ?  408 SER A CA    1 
ATOM   3298  C  C     . SER A 1 408 ? 137.537 148.519 107.997 1.00 14.79 ?  408 SER A C     1 
ATOM   3299  O  O     . SER A 1 408 ? 138.243 149.420 107.534 1.00 27.92 ?  408 SER A O     1 
ATOM   3300  C  CB    . SER A 1 408 ? 136.458 149.064 110.190 1.00 19.43 ?  408 SER A CB    1 
ATOM   3301  O  OG    . SER A 1 408 ? 136.320 150.335 109.583 1.00 26.85 ?  408 SER A OG    1 
ATOM   3302  N  N     . CYS A 1 409 ? 136.762 147.747 107.245 1.00 17.50 ?  409 CYS A N     1 
ATOM   3303  C  CA    . CYS A 1 409 ? 136.612 147.976 105.817 1.00 25.81 ?  409 CYS A CA    1 
ATOM   3304  C  C     . CYS A 1 409 ? 135.234 147.517 105.368 1.00 15.78 ?  409 CYS A C     1 
ATOM   3305  O  O     . CYS A 1 409 ? 134.724 146.497 105.840 1.00 18.36 ?  409 CYS A O     1 
ATOM   3306  C  CB    . CYS A 1 409 ? 137.704 147.253 105.013 1.00 13.30 ?  409 CYS A CB    1 
ATOM   3307  S  SG    . CYS A 1 409 ? 137.558 145.453 104.976 1.00 41.51 ?  409 CYS A SG    1 
ATOM   3308  N  N     . ASN A 1 410 ? 134.636 148.281 104.462 1.00 16.54 ?  410 ASN A N     1 
ATOM   3309  C  CA    . ASN A 1 410 ? 133.379 147.910 103.836 1.00 19.49 ?  410 ASN A CA    1 
ATOM   3310  C  C     . ASN A 1 410 ? 133.672 147.170 102.538 1.00 19.75 ?  410 ASN A C     1 
ATOM   3311  O  O     . ASN A 1 410 ? 134.580 147.540 101.789 1.00 13.93 ?  410 ASN A O     1 
ATOM   3312  C  CB    . ASN A 1 410 ? 132.502 149.138 103.579 1.00 20.33 ?  410 ASN A CB    1 
ATOM   3313  C  CG    . ASN A 1 410 ? 133.116 150.098 102.582 1.00 25.86 ?  410 ASN A CG    1 
ATOM   3314  O  OD1   . ASN A 1 410 ? 134.241 150.563 102.760 1.00 24.82 ?  410 ASN A OD1   1 
ATOM   3315  N  ND2   . ASN A 1 410 ? 132.374 150.403 101.526 1.00 26.94 ?  410 ASN A ND2   1 
ATOM   3316  N  N     . LEU A 1 411 ? 132.902 146.119 102.282 1.00 20.42 ?  411 LEU A N     1 
ATOM   3317  C  CA    . LEU A 1 411 ? 133.249 145.120 101.286 1.00 6.35  ?  411 LEU A CA    1 
ATOM   3318  C  C     . LEU A 1 411 ? 132.403 145.273 100.032 1.00 16.52 ?  411 LEU A C     1 
ATOM   3319  O  O     . LEU A 1 411 ? 131.248 145.706 100.092 1.00 20.82 ?  411 LEU A O     1 
ATOM   3320  C  CB    . LEU A 1 411 ? 133.074 143.711 101.856 1.00 13.72 ?  411 LEU A CB    1 
ATOM   3321  C  CG    . LEU A 1 411 ? 133.908 143.400 103.096 1.00 14.19 ?  411 LEU A CG    1 
ATOM   3322  C  CD1   . LEU A 1 411 ? 134.214 141.921 103.171 1.00 21.72 ?  411 LEU A CD1   1 
ATOM   3323  C  CD2   . LEU A 1 411 ? 135.190 144.211 103.084 1.00 15.31 ?  411 LEU A CD2   1 
ATOM   3324  N  N     . GLY A 1 412 ? 132.996 144.916 98.901  1.00 18.57 ?  412 GLY A N     1 
ATOM   3325  C  CA    . GLY A 1 412 ? 132.270 144.794 97.654  1.00 12.82 ?  412 GLY A CA    1 
ATOM   3326  C  C     . GLY A 1 412 ? 132.951 143.763 96.791  1.00 6.96  ?  412 GLY A C     1 
ATOM   3327  O  O     . GLY A 1 412 ? 134.156 143.526 96.916  1.00 13.66 ?  412 GLY A O     1 
ATOM   3328  N  N     . SER A 1 413 ? 132.175 143.134 95.913  1.00 9.16  ?  413 SER A N     1 
ATOM   3329  C  CA    . SER A 1 413 ? 132.684 142.051 95.086  1.00 11.11 ?  413 SER A CA    1 
ATOM   3330  C  C     . SER A 1 413 ? 132.376 142.320 93.623  1.00 10.69 ?  413 SER A C     1 
ATOM   3331  O  O     . SER A 1 413 ? 131.226 142.587 93.264  1.00 19.31 ?  413 SER A O     1 
ATOM   3332  C  CB    . SER A 1 413 ? 132.085 140.704 95.502  1.00 6.34  ?  413 SER A CB    1 
ATOM   3333  O  OG    . SER A 1 413 ? 132.587 140.291 96.758  1.00 28.09 ?  413 SER A OG    1 
ATOM   3334  N  N     . LEU A 1 414 ? 133.407 142.248 92.790  1.00 14.37 ?  414 LEU A N     1 
ATOM   3335  C  CA    . LEU A 1 414 ? 133.217 142.197 91.351  1.00 6.86  ?  414 LEU A CA    1 
ATOM   3336  C  C     . LEU A 1 414 ? 132.750 140.807 90.949  1.00 10.61 ?  414 LEU A C     1 
ATOM   3337  O  O     . LEU A 1 414 ? 133.219 139.800 91.485  1.00 10.15 ?  414 LEU A O     1 
ATOM   3338  C  CB    . LEU A 1 414 ? 134.517 142.536 90.623  1.00 10.43 ?  414 LEU A CB    1 
ATOM   3339  C  CG    . LEU A 1 414 ? 135.192 143.863 90.962  1.00 16.75 ?  414 LEU A CG    1 
ATOM   3340  C  CD1   . LEU A 1 414 ? 136.494 143.992 90.197  1.00 14.53 ?  414 LEU A CD1   1 
ATOM   3341  C  CD2   . LEU A 1 414 ? 134.268 145.024 90.652  1.00 21.36 ?  414 LEU A CD2   1 
ATOM   3342  N  N     . ASN A 1 415 ? 131.813 140.754 90.009  1.00 18.74 ?  415 ASN A N     1 
ATOM   3343  C  CA    . ASN A 1 415 ? 131.406 139.494 89.401  1.00 15.27 ?  415 ASN A CA    1 
ATOM   3344  C  C     . ASN A 1 415 ? 132.305 139.256 88.195  1.00 20.01 ?  415 ASN A C     1 
ATOM   3345  O  O     . ASN A 1 415 ? 132.147 139.905 87.156  1.00 26.49 ?  415 ASN A O     1 
ATOM   3346  C  CB    . ASN A 1 415 ? 129.932 139.526 89.007  1.00 19.59 ?  415 ASN A CB    1 
ATOM   3347  C  CG    . ASN A 1 415 ? 129.375 138.145 88.726  1.00 21.07 ?  415 ASN A CG    1 
ATOM   3348  O  OD1   . ASN A 1 415 ? 130.014 137.330 88.063  1.00 27.82 ?  415 ASN A OD1   1 
ATOM   3349  N  ND2   . ASN A 1 415 ? 128.180 137.874 89.234  1.00 20.68 ?  415 ASN A ND2   1 
ATOM   3350  N  N     . ILE A 1 416 ? 133.252 138.326 88.334  1.00 8.34  ?  416 ILE A N     1 
ATOM   3351  C  CA    . ILE A 1 416 ? 134.272 138.143 87.306  1.00 19.57 ?  416 ILE A CA    1 
ATOM   3352  C  C     . ILE A 1 416 ? 133.634 137.756 85.979  1.00 21.69 ?  416 ILE A C     1 
ATOM   3353  O  O     . ILE A 1 416 ? 134.005 138.276 84.922  1.00 26.04 ?  416 ILE A O     1 
ATOM   3354  C  CB    . ILE A 1 416 ? 135.312 137.102 87.760  1.00 23.15 ?  416 ILE A CB    1 
ATOM   3355  C  CG1   . ILE A 1 416 ? 136.131 137.645 88.933  1.00 14.39 ?  416 ILE A CG1   1 
ATOM   3356  C  CG2   . ILE A 1 416 ? 136.227 136.722 86.607  1.00 6.35  ?  416 ILE A CG2   1 
ATOM   3357  C  CD1   . ILE A 1 416 ? 136.894 136.584 89.690  1.00 19.08 ?  416 ILE A CD1   1 
ATOM   3358  N  N     . LEU A 1 417 ? 132.665 136.839 86.011  1.00 14.60 ?  417 LEU A N     1 
ATOM   3359  C  CA    . LEU A 1 417 ? 132.022 136.403 84.777  1.00 20.86 ?  417 LEU A CA    1 
ATOM   3360  C  C     . LEU A 1 417 ? 131.334 137.566 84.076  1.00 15.50 ?  417 LEU A C     1 
ATOM   3361  O  O     . LEU A 1 417 ? 131.488 137.758 82.865  1.00 29.35 ?  417 LEU A O     1 
ATOM   3362  C  CB    . LEU A 1 417 ? 131.021 135.287 85.075  1.00 23.56 ?  417 LEU A CB    1 
ATOM   3363  C  CG    . LEU A 1 417 ? 130.261 134.723 83.872  1.00 23.99 ?  417 LEU A CG    1 
ATOM   3364  C  CD1   . LEU A 1 417 ? 130.390 133.211 83.821  1.00 20.66 ?  417 LEU A CD1   1 
ATOM   3365  C  CD2   . LEU A 1 417 ? 128.800 135.139 83.913  1.00 25.86 ?  417 LEU A CD2   1 
ATOM   3366  N  N     . ASN A 1 418 ? 130.574 138.362 84.828  1.00 21.99 ?  418 ASN A N     1 
ATOM   3367  C  CA    . ASN A 1 418 ? 129.842 139.475 84.236  1.00 22.88 ?  418 ASN A CA    1 
ATOM   3368  C  C     . ASN A 1 418 ? 130.758 140.638 83.879  1.00 17.70 ?  418 ASN A C     1 
ATOM   3369  O  O     . ASN A 1 418 ? 130.489 141.357 82.912  1.00 21.99 ?  418 ASN A O     1 
ATOM   3370  C  CB    . ASN A 1 418 ? 128.741 139.937 85.190  1.00 22.90 ?  418 ASN A CB    1 
ATOM   3371  C  CG    . ASN A 1 418 ? 127.536 139.021 85.171  1.00 21.88 ?  418 ASN A CG    1 
ATOM   3372  O  OD1   . ASN A 1 418 ? 127.079 138.603 84.109  1.00 33.50 ?  418 ASN A OD1   1 
ATOM   3373  N  ND2   . ASN A 1 418 ? 127.020 138.697 86.349  1.00 20.65 ?  418 ASN A ND2   1 
ATOM   3374  N  N     . VAL A 1 419 ? 131.833 140.839 84.643  1.00 21.16 ?  419 VAL A N     1 
ATOM   3375  C  CA    . VAL A 1 419 ? 132.788 141.890 84.312  1.00 23.41 ?  419 VAL A CA    1 
ATOM   3376  C  C     . VAL A 1 419 ? 133.533 141.548 83.028  1.00 25.12 ?  419 VAL A C     1 
ATOM   3377  O  O     . VAL A 1 419 ? 133.836 142.430 82.216  1.00 27.83 ?  419 VAL A O     1 
ATOM   3378  C  CB    . VAL A 1 419 ? 133.757 142.119 85.486  1.00 23.02 ?  419 VAL A CB    1 
ATOM   3379  C  CG1   . VAL A 1 419 ? 134.885 143.040 85.068  1.00 25.65 ?  419 VAL A CG1   1 
ATOM   3380  C  CG2   . VAL A 1 419 ? 133.014 142.690 86.679  1.00 13.81 ?  419 VAL A CG2   1 
ATOM   3381  N  N     . MET A 1 420 ? 133.847 140.268 82.828  1.00 26.00 ?  420 MET A N     1 
ATOM   3382  C  CA    . MET A 1 420 ? 134.535 139.845 81.613  1.00 22.39 ?  420 MET A CA    1 
ATOM   3383  C  C     . MET A 1 420 ? 133.593 139.804 80.417  1.00 24.13 ?  420 MET A C     1 
ATOM   3384  O  O     . MET A 1 420 ? 133.999 140.130 79.296  1.00 28.60 ?  420 MET A O     1 
ATOM   3385  C  CB    . MET A 1 420 ? 135.181 138.477 81.830  1.00 24.55 ?  420 MET A CB    1 
ATOM   3386  C  CG    . MET A 1 420 ? 136.267 138.470 82.888  1.00 15.53 ?  420 MET A CG    1 
ATOM   3387  S  SD    . MET A 1 420 ? 137.652 139.530 82.439  1.00 32.02 ?  420 MET A SD    1 
ATOM   3388  C  CE    . MET A 1 420 ? 138.235 138.704 80.962  1.00 25.36 ?  420 MET A CE    1 
ATOM   3389  N  N     . GLU A 1 421 ? 132.337 139.408 80.633  1.00 27.73 ?  421 GLU A N     1 
ATOM   3390  C  CA    . GLU A 1 421 ? 131.370 139.403 79.541  1.00 27.36 ?  421 GLU A CA    1 
ATOM   3391  C  C     . GLU A 1 421 ? 131.106 140.815 79.037  1.00 28.43 ?  421 GLU A C     1 
ATOM   3392  O  O     . GLU A 1 421 ? 130.979 141.036 77.827  1.00 32.52 ?  421 GLU A O     1 
ATOM   3393  C  CB    . GLU A 1 421 ? 130.070 138.739 79.995  1.00 29.60 ?  421 GLU A CB    1 
ATOM   3394  C  CG    . GLU A 1 421 ? 130.092 137.220 79.911  1.00 33.80 ?  421 GLU A CG    1 
ATOM   3395  C  CD    . GLU A 1 421 ? 128.790 136.590 80.369  1.00 39.35 ?  421 GLU A CD    1 
ATOM   3396  O  OE1   . GLU A 1 421 ? 127.905 137.332 80.844  1.00 38.38 ?  421 GLU A OE1   1 
ATOM   3397  O  OE2   . GLU A 1 421 ? 128.654 135.354 80.253  1.00 35.89 -1 421 GLU A OE2   1 
ATOM   3398  N  N     . HIS A 1 422 ? 131.023 141.783 79.948  1.00 25.57 ?  422 HIS A N     1 
ATOM   3399  C  CA    . HIS A 1 422 ? 130.814 143.174 79.572  1.00 27.46 ?  422 HIS A CA    1 
ATOM   3400  C  C     . HIS A 1 422 ? 132.105 143.895 79.216  1.00 32.28 ?  422 HIS A C     1 
ATOM   3401  O  O     . HIS A 1 422 ? 132.045 145.032 78.736  1.00 32.89 ?  422 HIS A O     1 
ATOM   3402  C  CB    . HIS A 1 422 ? 130.108 143.922 80.704  1.00 26.44 ?  422 HIS A CB    1 
ATOM   3403  C  CG    . HIS A 1 422 ? 128.669 143.550 80.872  1.00 25.99 ?  422 HIS A CG    1 
ATOM   3404  N  ND1   . HIS A 1 422 ? 128.256 142.540 81.713  1.00 29.10 ?  422 HIS A ND1   1 
ATOM   3405  C  CD2   . HIS A 1 422 ? 127.546 144.053 80.307  1.00 29.83 ?  422 HIS A CD2   1 
ATOM   3406  C  CE1   . HIS A 1 422 ? 126.939 142.436 81.660  1.00 31.93 ?  422 HIS A CE1   1 
ATOM   3407  N  NE2   . HIS A 1 422 ? 126.485 143.343 80.813  1.00 35.30 ?  422 HIS A NE2   1 
ATOM   3408  N  N     . LYS A 1 423 ? 133.261 143.270 79.432  1.00 36.06 ?  423 LYS A N     1 
ATOM   3409  C  CA    . LYS A 1 423 ? 134.550 143.892 79.134  1.00 31.84 ?  423 LYS A CA    1 
ATOM   3410  C  C     . LYS A 1 423 ? 134.673 145.244 79.831  1.00 32.52 ?  423 LYS A C     1 
ATOM   3411  O  O     . LYS A 1 423 ? 135.156 146.224 79.259  1.00 32.08 ?  423 LYS A O     1 
ATOM   3412  C  CB    . LYS A 1 423 ? 134.751 144.036 77.625  1.00 28.99 ?  423 LYS A CB    1 
ATOM   3413  C  CG    . LYS A 1 423 ? 135.068 142.732 76.918  1.00 36.29 ?  423 LYS A CG    1 
ATOM   3414  C  CD    . LYS A 1 423 ? 134.166 142.524 75.714  1.00 36.89 ?  423 LYS A CD    1 
ATOM   3415  C  CE    . LYS A 1 423 ? 134.926 141.906 74.554  1.00 33.64 ?  423 LYS A CE    1 
ATOM   3416  N  NZ    . LYS A 1 423 ? 135.888 140.867 75.013  1.00 37.61 1  423 LYS A NZ    1 
ATOM   3417  N  N     . SER A 1 424 ? 134.236 145.294 81.085  1.00 25.49 ?  424 SER A N     1 
ATOM   3418  C  CA    . SER A 1 424 ? 134.150 146.532 81.847  1.00 23.26 ?  424 SER A CA    1 
ATOM   3419  C  C     . SER A 1 424 ? 134.917 146.423 83.154  1.00 24.11 ?  424 SER A C     1 
ATOM   3420  O  O     . SER A 1 424 ? 134.431 146.822 84.215  1.00 28.59 ?  424 SER A O     1 
ATOM   3421  C  CB    . SER A 1 424 ? 132.694 146.903 82.110  1.00 27.76 ?  424 SER A CB    1 
ATOM   3422  O  OG    . SER A 1 424 ? 132.059 145.922 82.911  1.00 29.90 ?  424 SER A OG    1 
ATOM   3423  N  N     . ILE A 1 425 ? 136.133 145.875 83.105  1.00 23.36 ?  425 ILE A N     1 
ATOM   3424  C  CA    . ILE A 1 425 ? 136.941 145.770 84.317  1.00 16.21 ?  425 ILE A CA    1 
ATOM   3425  C  C     . ILE A 1 425 ? 137.232 147.154 84.883  1.00 22.37 ?  425 ILE A C     1 
ATOM   3426  O  O     . ILE A 1 425 ? 137.036 147.411 86.076  1.00 29.85 ?  425 ILE A O     1 
ATOM   3427  C  CB    . ILE A 1 425 ? 138.241 144.994 84.038  1.00 26.18 ?  425 ILE A CB    1 
ATOM   3428  C  CG1   . ILE A 1 425 ? 137.949 143.506 83.836  1.00 24.20 ?  425 ILE A CG1   1 
ATOM   3429  C  CG2   . ILE A 1 425 ? 139.233 145.197 85.173  1.00 18.95 ?  425 ILE A CG2   1 
ATOM   3430  C  CD1   . ILE A 1 425 ? 139.180 142.685 83.524  1.00 23.95 ?  425 ILE A CD1   1 
ATOM   3431  N  N     . GLU A 1 426 ? 137.699 148.069 84.032  1.00 22.18 ?  426 GLU A N     1 
ATOM   3432  C  CA    . GLU A 1 426 ? 138.088 149.392 84.509  1.00 19.52 ?  426 GLU A CA    1 
ATOM   3433  C  C     . GLU A 1 426 ? 136.896 150.150 85.084  1.00 23.80 ?  426 GLU A C     1 
ATOM   3434  O  O     . GLU A 1 426 ? 136.947 150.650 86.214  1.00 28.49 ?  426 GLU A O     1 
ATOM   3435  C  CB    . GLU A 1 426 ? 138.727 150.186 83.370  1.00 19.84 ?  426 GLU A CB    1 
ATOM   3436  C  CG    . GLU A 1 426 ? 138.865 151.670 83.652  1.00 19.42 ?  426 GLU A CG    1 
ATOM   3437  C  CD    . GLU A 1 426 ? 139.271 152.461 82.426  1.00 31.56 ?  426 GLU A CD    1 
ATOM   3438  O  OE1   . GLU A 1 426 ? 139.235 151.895 81.314  1.00 31.42 ?  426 GLU A OE1   1 
ATOM   3439  O  OE2   . GLU A 1 426 ? 139.626 153.649 82.573  1.00 37.46 -1 426 GLU A OE2   1 
ATOM   3440  N  N     . LYS A 1 427 ? 135.813 150.247 84.311  1.00 31.50 ?  427 LYS A N     1 
ATOM   3441  C  CA    . LYS A 1 427 ? 134.655 151.016 84.754  1.00 22.49 ?  427 LYS A CA    1 
ATOM   3442  C  C     . LYS A 1 427 ? 134.022 150.394 85.989  1.00 27.63 ?  427 LYS A C     1 
ATOM   3443  O  O     . LYS A 1 427 ? 133.654 151.103 86.934  1.00 32.13 ?  427 LYS A O     1 
ATOM   3444  C  CB    . LYS A 1 427 ? 133.637 151.127 83.620  1.00 25.19 ?  427 LYS A CB    1 
ATOM   3445  C  CG    . LYS A 1 427 ? 132.213 151.380 84.078  1.00 25.08 ?  427 LYS A CG    1 
ATOM   3446  C  CD    . LYS A 1 427 ? 131.208 150.715 83.153  1.00 29.56 ?  427 LYS A CD    1 
ATOM   3447  C  CE    . LYS A 1 427 ? 131.021 149.250 83.500  1.00 29.78 ?  427 LYS A CE    1 
ATOM   3448  N  NZ    . LYS A 1 427 ? 130.056 149.061 84.616  1.00 33.25 1  427 LYS A NZ    1 
ATOM   3449  N  N     . THR A 1 428 ? 133.883 149.067 85.999  1.00 20.47 ?  428 THR A N     1 
ATOM   3450  C  CA    . THR A 1 428 ? 133.305 148.399 87.158  1.00 20.89 ?  428 THR A CA    1 
ATOM   3451  C  C     . THR A 1 428 ? 134.162 148.615 88.397  1.00 21.84 ?  428 THR A C     1 
ATOM   3452  O  O     . THR A 1 428 ? 133.639 148.899 89.480  1.00 26.14 ?  428 THR A O     1 
ATOM   3453  C  CB    . THR A 1 428 ? 133.137 146.906 86.878  1.00 18.66 ?  428 THR A CB    1 
ATOM   3454  O  OG1   . THR A 1 428 ? 132.324 146.727 85.711  1.00 24.95 ?  428 THR A OG1   1 
ATOM   3455  C  CG2   . THR A 1 428 ? 132.479 146.216 88.059  1.00 17.49 ?  428 THR A CG2   1 
ATOM   3456  N  N     . VAL A 1 429 ? 135.483 148.491 88.256  1.00 21.06 ?  429 VAL A N     1 
ATOM   3457  C  CA    . VAL A 1 429 ? 136.375 148.670 89.397  1.00 19.50 ?  429 VAL A CA    1 
ATOM   3458  C  C     . VAL A 1 429 ? 136.280 150.092 89.929  1.00 21.08 ?  429 VAL A C     1 
ATOM   3459  O  O     . VAL A 1 429 ? 136.239 150.315 91.142  1.00 24.10 ?  429 VAL A O     1 
ATOM   3460  C  CB    . VAL A 1 429 ? 137.820 148.304 89.011  1.00 16.05 ?  429 VAL A CB    1 
ATOM   3461  C  CG1   . VAL A 1 429 ? 138.785 148.752 90.094  1.00 14.45 ?  429 VAL A CG1   1 
ATOM   3462  C  CG2   . VAL A 1 429 ? 137.942 146.811 88.772  1.00 19.28 ?  429 VAL A CG2   1 
ATOM   3463  N  N     . LYS A 1 430 ? 136.254 151.079 89.031  1.00 20.46 ?  430 LYS A N     1 
ATOM   3464  C  CA    . LYS A 1 430 ? 136.214 152.468 89.479  1.00 18.36 ?  430 LYS A CA    1 
ATOM   3465  C  C     . LYS A 1 430 ? 134.885 152.801 90.149  1.00 18.17 ?  430 LYS A C     1 
ATOM   3466  O  O     . LYS A 1 430 ? 134.858 153.484 91.181  1.00 27.94 ?  430 LYS A O     1 
ATOM   3467  C  CB    . LYS A 1 430 ? 136.490 153.399 88.301  1.00 20.04 ?  430 LYS A CB    1 
ATOM   3468  C  CG    . LYS A 1 430 ? 137.877 153.201 87.714  1.00 20.12 ?  430 LYS A CG    1 
ATOM   3469  C  CD    . LYS A 1 430 ? 138.298 154.365 86.843  1.00 25.89 ?  430 LYS A CD    1 
ATOM   3470  C  CE    . LYS A 1 430 ? 139.768 154.260 86.476  1.00 26.96 ?  430 LYS A CE    1 
ATOM   3471  N  NZ    . LYS A 1 430 ? 140.209 155.391 85.618  1.00 32.66 1  430 LYS A NZ    1 
ATOM   3472  N  N     . LEU A 1 431 ? 133.773 152.319 89.592  1.00 26.53 ?  431 LEU A N     1 
ATOM   3473  C  CA    . LEU A 1 431 ? 132.478 152.549 90.226  1.00 14.85 ?  431 LEU A CA    1 
ATOM   3474  C  C     . LEU A 1 431 ? 132.392 151.852 91.579  1.00 18.65 ?  431 LEU A C     1 
ATOM   3475  O  O     . LEU A 1 431 ? 131.842 152.410 92.537  1.00 23.37 ?  431 LEU A O     1 
ATOM   3476  C  CB    . LEU A 1 431 ? 131.353 152.084 89.304  1.00 23.13 ?  431 LEU A CB    1 
ATOM   3477  C  CG    . LEU A 1 431 ? 130.897 153.109 88.267  1.00 27.06 ?  431 LEU A CG    1 
ATOM   3478  C  CD1   . LEU A 1 431 ? 129.910 152.485 87.297  1.00 27.61 ?  431 LEU A CD1   1 
ATOM   3479  C  CD2   . LEU A 1 431 ? 130.287 154.320 88.953  1.00 29.96 ?  431 LEU A CD2   1 
ATOM   3480  N  N     . ALA A 1 432 ? 132.926 150.633 91.678  1.00 22.81 ?  432 ALA A N     1 
ATOM   3481  C  CA    . ALA A 1 432 ? 132.935 149.934 92.958  1.00 11.62 ?  432 ALA A CA    1 
ATOM   3482  C  C     . ALA A 1 432 ? 133.791 150.672 93.977  1.00 21.04 ?  432 ALA A C     1 
ATOM   3483  O  O     . ALA A 1 432 ? 133.431 150.753 95.157  1.00 27.23 ?  432 ALA A O     1 
ATOM   3484  C  CB    . ALA A 1 432 ? 133.432 148.502 92.769  1.00 14.37 ?  432 ALA A CB    1 
ATOM   3485  N  N     . THR A 1 433 ? 134.932 151.210 93.541  1.00 26.21 ?  433 THR A N     1 
ATOM   3486  C  CA    . THR A 1 433 ? 135.772 151.993 94.440  1.00 18.84 ?  433 THR A CA    1 
ATOM   3487  C  C     . THR A 1 433 ? 135.042 153.236 94.925  1.00 20.68 ?  433 THR A C     1 
ATOM   3488  O  O     . THR A 1 433 ? 135.126 153.592 96.104  1.00 31.14 ?  433 THR A O     1 
ATOM   3489  C  CB    . THR A 1 433 ? 137.076 152.377 93.739  1.00 24.87 ?  433 THR A CB    1 
ATOM   3490  O  OG1   . THR A 1 433 ? 137.775 151.192 93.340  1.00 26.67 ?  433 THR A OG1   1 
ATOM   3491  C  CG2   . THR A 1 433 ? 137.960 153.192 94.669  1.00 20.10 ?  433 THR A CG2   1 
ATOM   3492  N  N     . ASP A 1 434 ? 134.318 153.908 94.029  1.00 20.99 ?  434 ASP A N     1 
ATOM   3493  C  CA    . ASP A 1 434 ? 133.558 155.086 94.433  1.00 16.86 ?  434 ASP A CA    1 
ATOM   3494  C  C     . ASP A 1 434 ? 132.468 154.728 95.437  1.00 20.98 ?  434 ASP A C     1 
ATOM   3495  O  O     . ASP A 1 434 ? 132.265 155.439 96.427  1.00 25.19 ?  434 ASP A O     1 
ATOM   3496  C  CB    . ASP A 1 434 ? 132.957 155.768 93.206  1.00 20.99 ?  434 ASP A CB    1 
ATOM   3497  C  CG    . ASP A 1 434 ? 134.012 156.340 92.285  1.00 29.52 ?  434 ASP A CG    1 
ATOM   3498  O  OD1   . ASP A 1 434 ? 135.061 156.787 92.789  1.00 33.51 ?  434 ASP A OD1   1 
ATOM   3499  O  OD2   . ASP A 1 434 ? 133.792 156.345 91.055  1.00 36.09 -1 434 ASP A OD2   1 
ATOM   3500  N  N     . SER A 1 435 ? 131.753 153.626 95.199  1.00 21.46 ?  435 SER A N     1 
ATOM   3501  C  CA    . SER A 1 435 ? 130.705 153.218 96.131  1.00 15.53 ?  435 SER A CA    1 
ATOM   3502  C  C     . SER A 1 435 ? 131.287 152.836 97.488  1.00 17.52 ?  435 SER A C     1 
ATOM   3503  O  O     . SER A 1 435 ? 130.727 153.190 98.535  1.00 21.78 ?  435 SER A O     1 
ATOM   3504  C  CB    . SER A 1 435 ? 129.900 152.060 95.543  1.00 14.71 ?  435 SER A CB    1 
ATOM   3505  O  OG    . SER A 1 435 ? 130.664 150.870 95.500  1.00 18.74 ?  435 SER A OG    1 
ATOM   3506  N  N     . LEU A 1 436 ? 132.408 152.112 97.492  1.00 16.89 ?  436 LEU A N     1 
ATOM   3507  C  CA    . LEU A 1 436 ? 133.052 151.748 98.749  1.00 9.65  ?  436 LEU A CA    1 
ATOM   3508  C  C     . LEU A 1 436 ? 133.538 152.984 99.491  1.00 12.75 ?  436 LEU A C     1 
ATOM   3509  O  O     . LEU A 1 436 ? 133.430 153.063 100.719 1.00 19.25 ?  436 LEU A O     1 
ATOM   3510  C  CB    . LEU A 1 436 ? 134.209 150.783 98.482  1.00 16.82 ?  436 LEU A CB    1 
ATOM   3511  C  CG    . LEU A 1 436 ? 133.827 149.377 98.010  1.00 17.77 ?  436 LEU A CG    1 
ATOM   3512  C  CD1   . LEU A 1 436 ? 135.049 148.622 97.510  1.00 12.55 ?  436 LEU A CD1   1 
ATOM   3513  C  CD2   . LEU A 1 436 ? 133.126 148.599 99.107  1.00 11.14 ?  436 LEU A CD2   1 
ATOM   3514  N  N     . THR A 1 437 ? 134.083 153.960 98.760  1.00 20.18 ?  437 THR A N     1 
ATOM   3515  C  CA    . THR A 1 437 ? 134.507 155.208 99.384  1.00 13.38 ?  437 THR A CA    1 
ATOM   3516  C  C     . THR A 1 437 ? 133.324 155.947 99.993  1.00 16.99 ?  437 THR A C     1 
ATOM   3517  O  O     . THR A 1 437 ? 133.432 156.506 101.090 1.00 26.34 ?  437 THR A O     1 
ATOM   3518  C  CB    . THR A 1 437 ? 135.219 156.092 98.362  1.00 15.89 ?  437 THR A CB    1 
ATOM   3519  O  OG1   . THR A 1 437 ? 136.299 155.362 97.768  1.00 21.46 ?  437 THR A OG1   1 
ATOM   3520  C  CG2   . THR A 1 437 ? 135.766 157.340 99.030  1.00 16.60 ?  437 THR A CG2   1 
ATOM   3521  N  N     . HIS A 1 438 ? 132.190 155.974 99.292  1.00 17.40 ?  438 HIS A N     1 
ATOM   3522  C  CA    . HIS A 1 438 ? 131.006 156.616 99.852  1.00 15.58 ?  438 HIS A CA    1 
ATOM   3523  C  C     . HIS A 1 438 ? 130.557 155.917 101.129 1.00 14.53 ?  438 HIS A C     1 
ATOM   3524  O  O     . HIS A 1 438 ? 130.237 156.574 102.128 1.00 22.90 ?  438 HIS A O     1 
ATOM   3525  C  CB    . HIS A 1 438 ? 129.873 156.633 98.827  1.00 19.81 ?  438 HIS A CB    1 
ATOM   3526  C  CG    . HIS A 1 438 ? 128.587 157.177 99.365  1.00 23.82 ?  438 HIS A CG    1 
ATOM   3527  N  ND1   . HIS A 1 438 ? 128.308 158.527 99.404  1.00 21.59 ?  438 HIS A ND1   1 
ATOM   3528  C  CD2   . HIS A 1 438 ? 127.513 156.556 99.907  1.00 22.15 ?  438 HIS A CD2   1 
ATOM   3529  C  CE1   . HIS A 1 438 ? 127.115 158.712 99.938  1.00 27.71 ?  438 HIS A CE1   1 
ATOM   3530  N  NE2   . HIS A 1 438 ? 126.611 157.532 100.252 1.00 26.99 ?  438 HIS A NE2   1 
ATOM   3531  N  N     . VAL A 1 439 ? 130.537 154.584 101.118 1.00 16.47 ?  439 VAL A N     1 
ATOM   3532  C  CA    . VAL A 1 439 ? 130.140 153.846 102.314 1.00 10.97 ?  439 VAL A CA    1 
ATOM   3533  C  C     . VAL A 1 439 ? 131.093 154.146 103.464 1.00 24.06 ?  439 VAL A C     1 
ATOM   3534  O  O     . VAL A 1 439 ? 130.667 154.336 104.610 1.00 32.08 ?  439 VAL A O     1 
ATOM   3535  C  CB    . VAL A 1 439 ? 130.067 152.337 102.016 1.00 19.33 ?  439 VAL A CB    1 
ATOM   3536  C  CG1   . VAL A 1 439 ? 129.768 151.563 103.287 1.00 16.76 ?  439 VAL A CG1   1 
ATOM   3537  C  CG2   . VAL A 1 439 ? 129.015 152.058 100.960 1.00 15.44 ?  439 VAL A CG2   1 
ATOM   3538  N  N     . SER A 1 440 ? 132.396 154.196 103.177 1.00 20.67 ?  440 SER A N     1 
ATOM   3539  C  CA    . SER A 1 440 ? 133.374 154.513 104.212 1.00 14.42 ?  440 SER A CA    1 
ATOM   3540  C  C     . SER A 1 440 ? 133.162 155.919 104.763 1.00 18.64 ?  440 SER A C     1 
ATOM   3541  O  O     . SER A 1 440 ? 133.276 156.143 105.974 1.00 28.14 ?  440 SER A O     1 
ATOM   3542  C  CB    . SER A 1 440 ? 134.789 154.362 103.653 1.00 23.39 ?  440 SER A CB    1 
ATOM   3543  O  OG    . SER A 1 440 ? 135.767 154.598 104.650 1.00 24.99 ?  440 SER A OG    1 
ATOM   3544  N  N     . GLU A 1 441 ? 132.858 156.880 103.889 1.00 20.39 ?  441 GLU A N     1 
ATOM   3545  C  CA    . GLU A 1 441 ? 132.694 158.260 104.330 1.00 15.51 ?  441 GLU A CA    1 
ATOM   3546  C  C     . GLU A 1 441 ? 131.396 158.460 105.099 1.00 26.37 ?  441 GLU A C     1 
ATOM   3547  O  O     . GLU A 1 441 ? 131.294 159.394 105.902 1.00 37.16 ?  441 GLU A O     1 
ATOM   3548  C  CB    . GLU A 1 441 ? 132.741 159.204 103.130 1.00 17.29 ?  441 GLU A CB    1 
ATOM   3549  C  CG    . GLU A 1 441 ? 134.139 159.548 102.654 1.00 21.07 ?  441 GLU A CG    1 
ATOM   3550  C  CD    . GLU A 1 441 ? 134.188 159.847 101.170 1.00 31.75 ?  441 GLU A CD    1 
ATOM   3551  O  OE1   . GLU A 1 441 ? 133.126 159.791 100.514 1.00 32.05 ?  441 GLU A OE1   1 
ATOM   3552  O  OE2   . GLU A 1 441 ? 135.286 160.145 100.659 1.00 29.99 -1 441 GLU A OE2   1 
ATOM   3553  N  N     . THR A 1 442 ? 130.400 157.610 104.868 1.00 27.62 ?  442 THR A N     1 
ATOM   3554  C  CA    . THR A 1 442 ? 129.122 157.726 105.558 1.00 20.78 ?  442 THR A CA    1 
ATOM   3555  C  C     . THR A 1 442 ? 129.057 156.903 106.837 1.00 23.71 ?  442 THR A C     1 
ATOM   3556  O  O     . THR A 1 442 ? 128.002 156.865 107.478 1.00 31.25 ?  442 THR A O     1 
ATOM   3557  C  CB    . THR A 1 442 ? 127.976 157.315 104.626 1.00 25.87 ?  442 THR A CB    1 
ATOM   3558  O  OG1   . THR A 1 442 ? 128.129 155.941 104.250 1.00 27.27 ?  442 THR A OG1   1 
ATOM   3559  C  CG2   . THR A 1 442 ? 127.973 158.180 103.378 1.00 24.09 ?  442 THR A CG2   1 
ATOM   3560  N  N     . THR A 1 443 ? 130.147 156.250 107.225 1.00 26.43 ?  443 THR A N     1 
ATOM   3561  C  CA    . THR A 1 443 ? 130.176 155.439 108.435 1.00 26.74 ?  443 THR A CA    1 
ATOM   3562  C  C     . THR A 1 443 ? 130.714 156.258 109.600 1.00 30.28 ?  443 THR A C     1 
ATOM   3563  O  O     . THR A 1 443 ? 131.720 156.961 109.461 1.00 36.96 ?  443 THR A O     1 
ATOM   3564  C  CB    . THR A 1 443 ? 131.034 154.190 108.230 1.00 29.68 ?  443 THR A CB    1 
ATOM   3565  O  OG1   . THR A 1 443 ? 130.347 153.274 107.368 1.00 35.30 ?  443 THR A OG1   1 
ATOM   3566  C  CG2   . THR A 1 443 ? 131.317 153.514 109.560 1.00 25.72 ?  443 THR A CG2   1 
ATOM   3567  N  N     . ASP A 1 444 ? 130.038 156.168 110.746 1.00 34.48 ?  444 ASP A N     1 
ATOM   3568  C  CA    . ASP A 1 444 ? 130.479 156.862 111.956 1.00 35.10 ?  444 ASP A CA    1 
ATOM   3569  C  C     . ASP A 1 444 ? 130.087 155.992 113.148 1.00 34.53 ?  444 ASP A C     1 
ATOM   3570  O  O     . ASP A 1 444 ? 128.910 155.930 113.513 1.00 36.05 ?  444 ASP A O     1 
ATOM   3571  C  CB    . ASP A 1 444 ? 129.866 158.252 112.049 1.00 39.53 ?  444 ASP A CB    1 
ATOM   3572  C  CG    . ASP A 1 444 ? 130.739 159.222 112.819 1.00 39.50 ?  444 ASP A CG    1 
ATOM   3573  O  OD1   . ASP A 1 444 ? 131.883 159.466 112.383 1.00 37.61 ?  444 ASP A OD1   1 
ATOM   3574  O  OD2   . ASP A 1 444 ? 130.283 159.739 113.859 1.00 36.08 -1 444 ASP A OD2   1 
ATOM   3575  N  N     . ILE A 1 445 ? 131.074 155.331 113.745 1.00 31.43 ?  445 ILE A N     1 
ATOM   3576  C  CA    . ILE A 1 445 ? 130.844 154.429 114.868 1.00 34.20 ?  445 ILE A CA    1 
ATOM   3577  C  C     . ILE A 1 445 ? 130.963 155.232 116.157 1.00 33.28 ?  445 ILE A C     1 
ATOM   3578  O  O     . ILE A 1 445 ? 132.008 155.831 116.432 1.00 30.07 ?  445 ILE A O     1 
ATOM   3579  C  CB    . ILE A 1 445 ? 131.834 153.256 114.850 1.00 32.94 ?  445 ILE A CB    1 
ATOM   3580  C  CG1   . ILE A 1 445 ? 131.662 152.440 113.566 1.00 24.82 ?  445 ILE A CG1   1 
ATOM   3581  C  CG2   . ILE A 1 445 ? 131.639 152.374 116.073 1.00 30.86 ?  445 ILE A CG2   1 
ATOM   3582  C  CD1   . ILE A 1 445 ? 130.466 151.517 113.582 1.00 26.05 ?  445 ILE A CD1   1 
ATOM   3583  N  N     . ARG A 1 446 ? 129.895 155.237 116.953 1.00 36.64 ?  446 ARG A N     1 
ATOM   3584  C  CA    . ARG A 1 446 ? 129.801 156.109 118.115 1.00 35.05 ?  446 ARG A CA    1 
ATOM   3585  C  C     . ARG A 1 446 ? 130.359 155.495 119.392 1.00 37.34 ?  446 ARG A C     1 
ATOM   3586  O  O     . ARG A 1 446 ? 130.487 156.207 120.394 1.00 31.04 ?  446 ARG A O     1 
ATOM   3587  C  CB    . ARG A 1 446 ? 128.341 156.516 118.344 1.00 31.59 ?  446 ARG A CB    1 
ATOM   3588  C  CG    . ARG A 1 446 ? 127.759 157.364 117.226 1.00 34.69 ?  446 ARG A CG    1 
ATOM   3589  C  CD    . ARG A 1 446 ? 128.390 158.746 117.201 1.00 33.44 ?  446 ARG A CD    1 
ATOM   3590  N  NE    . ARG A 1 446 ? 127.870 159.564 116.110 1.00 38.23 ?  446 ARG A NE    1 
ATOM   3591  C  CZ    . ARG A 1 446 ? 128.273 160.798 115.843 1.00 37.24 ?  446 ARG A CZ    1 
ATOM   3592  N  NH1   . ARG A 1 446 ? 129.198 161.398 116.575 1.00 36.49 1  446 ARG A NH1   1 
ATOM   3593  N  NH2   . ARG A 1 446 ? 127.734 161.448 114.815 1.00 36.37 ?  446 ARG A NH2   1 
ATOM   3594  N  N     . ASN A 1 447 ? 130.700 154.203 119.390 1.00 25.31 ?  447 ASN A N     1 
ATOM   3595  C  CA    . ASN A 1 447 ? 131.217 153.548 120.586 1.00 18.99 ?  447 ASN A CA    1 
ATOM   3596  C  C     . ASN A 1 447 ? 132.523 152.810 120.319 1.00 26.39 ?  447 ASN A C     1 
ATOM   3597  O  O     . ASN A 1 447 ? 132.958 152.012 121.155 1.00 33.83 ?  447 ASN A O     1 
ATOM   3598  C  CB    . ASN A 1 447 ? 130.178 152.587 121.171 1.00 27.77 ?  447 ASN A CB    1 
ATOM   3599  C  CG    . ASN A 1 447 ? 129.050 153.309 121.877 1.00 23.83 ?  447 ASN A CG    1 
ATOM   3600  O  OD1   . ASN A 1 447 ? 129.241 153.882 122.948 1.00 24.53 ?  447 ASN A OD1   1 
ATOM   3601  N  ND2   . ASN A 1 447 ? 127.864 153.281 121.282 1.00 26.65 ?  447 ASN A ND2   1 
ATOM   3602  N  N     . ALA A 1 448 ? 133.155 153.056 119.175 1.00 29.78 ?  448 ALA A N     1 
ATOM   3603  C  CA    . ALA A 1 448 ? 134.449 152.470 118.832 1.00 17.54 ?  448 ALA A CA    1 
ATOM   3604  C  C     . ALA A 1 448 ? 135.366 153.605 118.403 1.00 24.71 ?  448 ALA A C     1 
ATOM   3605  O  O     . ALA A 1 448 ? 135.570 153.837 117.204 1.00 28.00 ?  448 ALA A O     1 
ATOM   3606  C  CB    . ALA A 1 448 ? 134.312 151.411 117.738 1.00 22.68 ?  448 ALA A CB    1 
ATOM   3607  N  N     . PRO A 1 449 ? 135.931 154.343 119.361 1.00 27.79 ?  449 PRO A N     1 
ATOM   3608  C  CA    . PRO A 1 449 ? 136.728 155.525 118.991 1.00 16.37 ?  449 PRO A CA    1 
ATOM   3609  C  C     . PRO A 1 449 ? 137.875 155.207 118.050 1.00 13.05 ?  449 PRO A C     1 
ATOM   3610  O  O     . PRO A 1 449 ? 138.121 155.964 117.103 1.00 17.71 ?  449 PRO A O     1 
ATOM   3611  C  CB    . PRO A 1 449 ? 137.234 156.046 120.345 1.00 13.11 ?  449 PRO A CB    1 
ATOM   3612  C  CG    . PRO A 1 449 ? 136.365 155.407 121.367 1.00 19.65 ?  449 PRO A CG    1 
ATOM   3613  C  CD    . PRO A 1 449 ? 135.938 154.096 120.811 1.00 16.60 ?  449 PRO A CD    1 
ATOM   3614  N  N     . ALA A 1 450 ? 138.575 154.093 118.273 1.00 24.37 ?  450 ALA A N     1 
ATOM   3615  C  CA    . ALA A 1 450 ? 139.693 153.745 117.404 1.00 14.74 ?  450 ALA A CA    1 
ATOM   3616  C  C     . ALA A 1 450 ? 139.206 153.313 116.029 1.00 19.69 ?  450 ALA A C     1 
ATOM   3617  O  O     . ALA A 1 450 ? 139.825 153.646 115.015 1.00 24.71 ?  450 ALA A O     1 
ATOM   3618  C  CB    . ALA A 1 450 ? 140.542 152.649 118.048 1.00 10.02 ?  450 ALA A CB    1 
ATOM   3619  N  N     . VAL A 1 451 ? 138.088 152.588 115.973 1.00 19.65 ?  451 VAL A N     1 
ATOM   3620  C  CA    . VAL A 1 451 ? 137.517 152.205 114.685 1.00 18.15 ?  451 VAL A CA    1 
ATOM   3621  C  C     . VAL A 1 451 ? 137.160 153.444 113.877 1.00 14.55 ?  451 VAL A C     1 
ATOM   3622  O  O     . VAL A 1 451 ? 137.487 153.549 112.690 1.00 21.64 ?  451 VAL A O     1 
ATOM   3623  C  CB    . VAL A 1 451 ? 136.292 151.294 114.888 1.00 19.34 ?  451 VAL A CB    1 
ATOM   3624  C  CG1   . VAL A 1 451 ? 135.529 151.139 113.585 1.00 18.65 ?  451 VAL A CG1   1 
ATOM   3625  C  CG2   . VAL A 1 451 ? 136.721 149.942 115.420 1.00 14.36 ?  451 VAL A CG2   1 
ATOM   3626  N  N     . ARG A 1 452 ? 136.480 154.400 114.509 1.00 17.21 ?  452 ARG A N     1 
ATOM   3627  C  CA    . ARG A 1 452 ? 136.064 155.609 113.805 1.00 17.62 ?  452 ARG A CA    1 
ATOM   3628  C  C     . ARG A 1 452 ? 137.265 156.446 113.378 1.00 16.63 ?  452 ARG A C     1 
ATOM   3629  O  O     . ARG A 1 452 ? 137.305 156.961 112.252 1.00 25.20 ?  452 ARG A O     1 
ATOM   3630  C  CB    . ARG A 1 452 ? 135.116 156.413 114.696 1.00 11.88 ?  452 ARG A CB    1 
ATOM   3631  C  CG    . ARG A 1 452 ? 134.581 157.690 114.087 1.00 20.24 ?  452 ARG A CG    1 
ATOM   3632  C  CD    . ARG A 1 452 ? 133.637 158.379 115.058 1.00 18.64 ?  452 ARG A CD    1 
ATOM   3633  N  NE    . ARG A 1 452 ? 133.095 159.616 114.513 1.00 31.56 ?  452 ARG A NE    1 
ATOM   3634  C  CZ    . ARG A 1 452 ? 133.694 160.797 114.590 1.00 36.94 ?  452 ARG A CZ    1 
ATOM   3635  N  NH1   . ARG A 1 452 ? 134.860 160.941 115.200 1.00 29.02 1  452 ARG A NH1   1 
ATOM   3636  N  NH2   . ARG A 1 452 ? 133.108 161.857 114.043 1.00 27.74 ?  452 ARG A NH2   1 
ATOM   3637  N  N     . ARG A 1 453 ? 138.261 156.578 114.255 1.00 17.85 ?  453 ARG A N     1 
ATOM   3638  C  CA    . ARG A 1 453 ? 139.448 157.346 113.903 1.00 13.61 ?  453 ARG A CA    1 
ATOM   3639  C  C     . ARG A 1 453 ? 140.200 156.702 112.746 1.00 21.96 ?  453 ARG A C     1 
ATOM   3640  O  O     . ARG A 1 453 ? 140.651 157.395 111.827 1.00 23.36 ?  453 ARG A O     1 
ATOM   3641  C  CB    . ARG A 1 453 ? 140.355 157.498 115.124 1.00 13.96 ?  453 ARG A CB    1 
ATOM   3642  C  CG    . ARG A 1 453 ? 141.828 157.565 114.794 1.00 19.66 ?  453 ARG A CG    1 
ATOM   3643  C  CD    . ARG A 1 453 ? 142.555 158.545 115.691 1.00 18.23 ?  453 ARG A CD    1 
ATOM   3644  N  NE    . ARG A 1 453 ? 143.871 158.877 115.162 1.00 22.47 ?  453 ARG A NE    1 
ATOM   3645  C  CZ    . ARG A 1 453 ? 144.981 158.213 115.450 1.00 22.02 ?  453 ARG A CZ    1 
ATOM   3646  N  NH1   . ARG A 1 453 ? 144.973 157.177 116.272 1.00 19.20 1  453 ARG A NH1   1 
ATOM   3647  N  NH2   . ARG A 1 453 ? 146.128 158.596 114.897 1.00 23.17 ?  453 ARG A NH2   1 
ATOM   3648  N  N     . ALA A 1 454 ? 140.338 155.373 112.765 1.00 21.35 ?  454 ALA A N     1 
ATOM   3649  C  CA    . ALA A 1 454 ? 141.032 154.687 111.683 1.00 11.94 ?  454 ALA A CA    1 
ATOM   3650  C  C     . ALA A 1 454 ? 140.238 154.733 110.388 1.00 13.76 ?  454 ALA A C     1 
ATOM   3651  O  O     . ALA A 1 454 ? 140.829 154.798 109.309 1.00 22.39 ?  454 ALA A O     1 
ATOM   3652  C  CB    . ALA A 1 454 ? 141.325 153.242 112.077 1.00 18.86 ?  454 ALA A CB    1 
ATOM   3653  N  N     . ASN A 1 455 ? 138.908 154.695 110.467 1.00 18.74 ?  455 ASN A N     1 
ATOM   3654  C  CA    . ASN A 1 455 ? 138.103 154.862 109.264 1.00 12.28 ?  455 ASN A CA    1 
ATOM   3655  C  C     . ASN A 1 455 ? 138.313 156.244 108.660 1.00 14.93 ?  455 ASN A C     1 
ATOM   3656  O  O     . ASN A 1 455 ? 138.437 156.383 107.438 1.00 21.59 ?  455 ASN A O     1 
ATOM   3657  C  CB    . ASN A 1 455 ? 136.627 154.626 109.583 1.00 14.03 ?  455 ASN A CB    1 
ATOM   3658  C  CG    . ASN A 1 455 ? 135.736 154.764 108.364 1.00 22.05 ?  455 ASN A CG    1 
ATOM   3659  O  OD1   . ASN A 1 455 ? 135.837 153.988 107.415 1.00 28.74 ?  455 ASN A OD1   1 
ATOM   3660  N  ND2   . ASN A 1 455 ? 134.857 155.756 108.384 1.00 22.92 ?  455 ASN A ND2   1 
ATOM   3661  N  N     . LYS A 1 456 ? 138.357 157.279 109.501 1.00 17.53 ?  456 LYS A N     1 
ATOM   3662  C  CA    . LYS A 1 456 ? 138.586 158.626 108.985 1.00 16.85 ?  456 LYS A CA    1 
ATOM   3663  C  C     . LYS A 1 456 ? 139.987 158.772 108.399 1.00 15.81 ?  456 LYS A C     1 
ATOM   3664  O  O     . LYS A 1 456 ? 140.165 159.410 107.356 1.00 25.71 ?  456 LYS A O     1 
ATOM   3665  C  CB    . LYS A 1 456 ? 138.356 159.661 110.085 1.00 20.81 ?  456 LYS A CB    1 
ATOM   3666  C  CG    . LYS A 1 456 ? 136.931 159.718 110.603 1.00 23.57 ?  456 LYS A CG    1 
ATOM   3667  C  CD    . LYS A 1 456 ? 136.802 160.691 111.767 1.00 29.88 ?  456 LYS A CD    1 
ATOM   3668  C  CE    . LYS A 1 456 ? 137.991 160.598 112.713 1.00 26.26 ?  456 LYS A CE    1 
ATOM   3669  N  NZ    . LYS A 1 456 ? 137.571 160.573 114.143 1.00 24.39 1  456 LYS A NZ    1 
ATOM   3670  N  N     . ALA A 1 457 ? 140.996 158.193 109.054 1.00 16.00 ?  457 ALA A N     1 
ATOM   3671  C  CA    . ALA A 1 457 ? 142.379 158.452 108.670 1.00 14.82 ?  457 ALA A CA    1 
ATOM   3672  C  C     . ALA A 1 457 ? 142.825 157.581 107.499 1.00 25.27 ?  457 ALA A C     1 
ATOM   3673  O  O     . ALA A 1 457 ? 143.481 158.066 106.570 1.00 27.24 ?  457 ALA A O     1 
ATOM   3674  C  CB    . ALA A 1 457 ? 143.302 158.238 109.871 1.00 12.93 ?  457 ALA A CB    1 
ATOM   3675  N  N     . MET A 1 458 ? 142.485 156.295 107.526 1.00 21.70 ?  458 MET A N     1 
ATOM   3676  C  CA    . MET A 1 458 ? 142.984 155.345 106.542 1.00 14.20 ?  458 MET A CA    1 
ATOM   3677  C  C     . MET A 1 458 ? 142.108 155.253 105.303 1.00 17.26 ?  458 MET A C     1 
ATOM   3678  O  O     . MET A 1 458 ? 142.629 155.041 104.204 1.00 27.24 ?  458 MET A O     1 
ATOM   3679  C  CB    . MET A 1 458 ? 143.110 153.956 107.174 1.00 14.00 ?  458 MET A CB    1 
ATOM   3680  C  CG    . MET A 1 458 ? 143.922 153.929 108.456 1.00 14.93 ?  458 MET A CG    1 
ATOM   3681  S  SD    . MET A 1 458 ? 145.668 154.278 108.187 1.00 31.01 ?  458 MET A SD    1 
ATOM   3682  C  CE    . MET A 1 458 ? 146.337 152.619 108.083 1.00 10.74 ?  458 MET A CE    1 
ATOM   3683  N  N     . LYS A 1 459 ? 140.794 155.412 105.451 1.00 14.29 ?  459 LYS A N     1 
ATOM   3684  C  CA    . LYS A 1 459 ? 139.870 155.297 104.326 1.00 18.18 ?  459 LYS A CA    1 
ATOM   3685  C  C     . LYS A 1 459 ? 140.024 153.948 103.629 1.00 17.29 ?  459 LYS A C     1 
ATOM   3686  O  O     . LYS A 1 459 ? 139.959 153.847 102.403 1.00 19.20 ?  459 LYS A O     1 
ATOM   3687  C  CB    . LYS A 1 459 ? 140.065 156.447 103.335 1.00 14.82 ?  459 LYS A CB    1 
ATOM   3688  C  CG    . LYS A 1 459 ? 140.146 157.816 103.984 1.00 15.46 ?  459 LYS A CG    1 
ATOM   3689  C  CD    . LYS A 1 459 ? 141.105 158.720 103.230 1.00 21.93 ?  459 LYS A CD    1 
ATOM   3690  C  CE    . LYS A 1 459 ? 141.290 160.048 103.938 1.00 25.50 ?  459 LYS A CE    1 
ATOM   3691  N  NZ    . LYS A 1 459 ? 139.990 160.667 104.317 1.00 31.64 1  459 LYS A NZ    1 
ATOM   3692  N  N     . SER A 1 460 ? 140.232 152.902 104.422 1.00 23.68 ?  460 SER A N     1 
ATOM   3693  C  CA    . SER A 1 460 ? 140.442 151.570 103.874 1.00 10.27 ?  460 SER A CA    1 
ATOM   3694  C  C     . SER A 1 460 ? 139.140 151.007 103.319 1.00 16.14 ?  460 SER A C     1 
ATOM   3695  O  O     . SER A 1 460 ? 138.087 151.101 103.956 1.00 19.66 ?  460 SER A O     1 
ATOM   3696  C  CB    . SER A 1 460 ? 141.005 150.642 104.947 1.00 4.46  ?  460 SER A CB    1 
ATOM   3697  O  OG    . SER A 1 460 ? 140.551 149.315 104.762 1.00 25.58 ?  460 SER A OG    1 
ATOM   3698  N  N     . ILE A 1 461 ? 139.216 150.420 102.125 1.00 12.17 ?  461 ILE A N     1 
ATOM   3699  C  CA    . ILE A 1 461 ? 138.084 149.753 101.500 1.00 7.67  ?  461 ILE A CA    1 
ATOM   3700  C  C     . ILE A 1 461 ? 138.526 148.359 101.082 1.00 15.24 ?  461 ILE A C     1 
ATOM   3701  O  O     . ILE A 1 461 ? 139.712 148.091 100.884 1.00 26.01 ?  461 ILE A O     1 
ATOM   3702  C  CB    . ILE A 1 461 ? 137.540 150.528 100.282 1.00 13.43 ?  461 ILE A CB    1 
ATOM   3703  C  CG1   . ILE A 1 461 ? 138.621 150.650 99.207  1.00 6.10  ?  461 ILE A CG1   1 
ATOM   3704  C  CG2   . ILE A 1 461 ? 137.042 151.899 100.704 1.00 8.84  ?  461 ILE A CG2   1 
ATOM   3705  C  CD1   . ILE A 1 461 ? 138.154 151.322 97.942  1.00 1.21  ?  461 ILE A CD1   1 
ATOM   3706  N  N     . GLY A 1 462 ? 137.556 147.461 100.965 1.00 17.83 ?  462 GLY A N     1 
ATOM   3707  C  CA    . GLY A 1 462 ? 137.847 146.137 100.456 1.00 5.86  ?  462 GLY A CA    1 
ATOM   3708  C  C     . GLY A 1 462 ? 137.031 145.787 99.232  1.00 1.98  ?  462 GLY A C     1 
ATOM   3709  O  O     . GLY A 1 462 ? 135.819 145.580 99.325  1.00 18.87 ?  462 GLY A O     1 
ATOM   3710  N  N     . LEU A 1 463 ? 137.686 145.703 98.081  1.00 6.37  ?  463 LEU A N     1 
ATOM   3711  C  CA    . LEU A 1 463 ? 137.041 145.329 96.829  1.00 10.33 ?  463 LEU A CA    1 
ATOM   3712  C  C     . LEU A 1 463 ? 137.459 143.904 96.494  1.00 4.94  ?  463 LEU A C     1 
ATOM   3713  O  O     . LEU A 1 463 ? 138.599 143.667 96.084  1.00 26.27 ?  463 LEU A O     1 
ATOM   3714  C  CB    . LEU A 1 463 ? 137.412 146.296 95.706  1.00 14.77 ?  463 LEU A CB    1 
ATOM   3715  C  CG    . LEU A 1 463 ? 136.949 145.917 94.297  1.00 11.15 ?  463 LEU A CG    1 
ATOM   3716  C  CD1   . LEU A 1 463 ? 135.456 145.644 94.275  1.00 6.23  ?  463 LEU A CD1   1 
ATOM   3717  C  CD2   . LEU A 1 463 ? 137.310 147.009 93.304  1.00 6.43  ?  463 LEU A CD2   1 
ATOM   3718  N  N     . GLY A 1 464 ? 136.538 142.962 96.673  1.00 6.62  ?  464 GLY A N     1 
ATOM   3719  C  CA    . GLY A 1 464 ? 136.795 141.572 96.375  1.00 0.13  ?  464 GLY A CA    1 
ATOM   3720  C  C     . GLY A 1 464 ? 136.330 141.188 94.987  1.00 2.23  ?  464 GLY A C     1 
ATOM   3721  O  O     . GLY A 1 464 ? 135.986 142.024 94.151  1.00 11.59 ?  464 GLY A O     1 
ATOM   3722  N  N     . ALA A 1 465 ? 136.332 139.882 94.743  1.00 14.24 ?  465 ALA A N     1 
ATOM   3723  C  CA    . ALA A 1 465 ? 135.848 139.330 93.488  1.00 7.11  ?  465 ALA A CA    1 
ATOM   3724  C  C     . ALA A 1 465 ? 135.186 137.992 93.774  1.00 8.22  ?  465 ALA A C     1 
ATOM   3725  O  O     . ALA A 1 465 ? 135.475 137.337 94.778  1.00 16.85 ?  465 ALA A O     1 
ATOM   3726  C  CB    . ALA A 1 465 ? 136.977 139.176 92.464  1.00 7.62  ?  465 ALA A CB    1 
ATOM   3727  N  N     . MET A 1 466 ? 134.281 137.600 92.883  1.00 14.80 ?  466 MET A N     1 
ATOM   3728  C  CA    . MET A 1 466 ? 133.573 136.336 93.006  1.00 16.83 ?  466 MET A CA    1 
ATOM   3729  C  C     . MET A 1 466 ? 133.306 135.785 91.613  1.00 14.14 ?  466 MET A C     1 
ATOM   3730  O  O     . MET A 1 466 ? 133.407 136.496 90.611  1.00 19.76 ?  466 MET A O     1 
ATOM   3731  C  CB    . MET A 1 466 ? 132.265 136.495 93.788  1.00 17.61 ?  466 MET A CB    1 
ATOM   3732  C  CG    . MET A 1 466 ? 131.266 137.431 93.139  1.00 13.78 ?  466 MET A CG    1 
ATOM   3733  S  SD    . MET A 1 466 ? 129.675 137.423 93.977  1.00 30.65 ?  466 MET A SD    1 
ATOM   3734  C  CE    . MET A 1 466 ? 129.171 139.115 93.713  1.00 26.32 ?  466 MET A CE    1 
ATOM   3735  N  N     . ASN A 1 467 ? 132.964 134.500 91.560  1.00 10.76 ?  467 ASN A N     1 
ATOM   3736  C  CA    . ASN A 1 467 ? 132.662 133.800 90.317  1.00 12.46 ?  467 ASN A CA    1 
ATOM   3737  C  C     . ASN A 1 467 ? 133.908 133.473 89.505  1.00 16.95 ?  467 ASN A C     1 
ATOM   3738  O  O     . ASN A 1 467 ? 133.830 133.341 88.281  1.00 25.18 ?  467 ASN A O     1 
ATOM   3739  C  CB    . ASN A 1 467 ? 131.678 134.600 89.457  1.00 16.76 ?  467 ASN A CB    1 
ATOM   3740  C  CG    . ASN A 1 467 ? 130.618 133.730 88.819  1.00 17.05 ?  467 ASN A CG    1 
ATOM   3741  O  OD1   . ASN A 1 467 ? 130.371 132.609 89.261  1.00 30.53 ?  467 ASN A OD1   1 
ATOM   3742  N  ND2   . ASN A 1 467 ? 129.979 134.244 87.778  1.00 18.67 ?  467 ASN A ND2   1 
ATOM   3743  N  N     . LEU A 1 468 ? 135.069 133.359 90.152  1.00 15.20 ?  468 LEU A N     1 
ATOM   3744  C  CA    . LEU A 1 468 ? 136.267 132.938 89.435  1.00 12.59 ?  468 LEU A CA    1 
ATOM   3745  C  C     . LEU A 1 468 ? 136.105 131.525 88.892  1.00 19.47 ?  468 LEU A C     1 
ATOM   3746  O  O     . LEU A 1 468 ? 136.312 131.277 87.698  1.00 23.75 ?  468 LEU A O     1 
ATOM   3747  C  CB    . LEU A 1 468 ? 137.490 133.026 90.347  1.00 20.28 ?  468 LEU A CB    1 
ATOM   3748  C  CG    . LEU A 1 468 ? 138.803 132.548 89.719  1.00 14.18 ?  468 LEU A CG    1 
ATOM   3749  C  CD1   . LEU A 1 468 ? 139.220 133.460 88.578  1.00 13.09 ?  468 LEU A CD1   1 
ATOM   3750  C  CD2   . LEU A 1 468 ? 139.901 132.446 90.763  1.00 12.22 ?  468 LEU A CD2   1 
ATOM   3751  N  N     . HIS A 1 469 ? 135.722 130.583 89.757  1.00 19.12 ?  469 HIS A N     1 
ATOM   3752  C  CA    . HIS A 1 469 ? 135.532 129.210 89.304  1.00 10.32 ?  469 HIS A CA    1 
ATOM   3753  C  C     . HIS A 1 469 ? 134.369 129.103 88.329  1.00 24.18 ?  469 HIS A C     1 
ATOM   3754  O  O     . HIS A 1 469 ? 134.447 128.360 87.348  1.00 33.67 ?  469 HIS A O     1 
ATOM   3755  C  CB    . HIS A 1 469 ? 135.314 128.274 90.490  1.00 17.08 ?  469 HIS A CB    1 
ATOM   3756  C  CG    . HIS A 1 469 ? 135.446 126.826 90.134  1.00 20.75 ?  469 HIS A CG    1 
ATOM   3757  N  ND1   . HIS A 1 469 ? 135.122 125.810 91.006  1.00 25.77 ?  469 HIS A ND1   1 
ATOM   3758  C  CD2   . HIS A 1 469 ? 135.866 126.225 88.997  1.00 18.02 ?  469 HIS A CD2   1 
ATOM   3759  C  CE1   . HIS A 1 469 ? 135.336 124.645 90.421  1.00 23.75 ?  469 HIS A CE1   1 
ATOM   3760  N  NE2   . HIS A 1 469 ? 135.788 124.869 89.201  1.00 15.87 ?  469 HIS A NE2   1 
ATOM   3761  N  N     . GLY A 1 470 ? 133.273 129.816 88.592  1.00 22.60 ?  470 GLY A N     1 
ATOM   3762  C  CA    . GLY A 1 470 ? 132.160 129.795 87.659  1.00 14.30 ?  470 GLY A CA    1 
ATOM   3763  C  C     . GLY A 1 470 ? 132.557 130.303 86.288  1.00 16.51 ?  470 GLY A C     1 
ATOM   3764  O  O     . GLY A 1 470 ? 132.234 129.694 85.265  1.00 31.02 ?  470 GLY A O     1 
ATOM   3765  N  N     . TYR A 1 471 ? 133.283 131.421 86.251  1.00 10.33 ?  471 TYR A N     1 
ATOM   3766  C  CA    . TYR A 1 471 ? 133.739 131.969 84.980  1.00 17.29 ?  471 TYR A CA    1 
ATOM   3767  C  C     . TYR A 1 471 ? 134.670 130.995 84.267  1.00 20.73 ?  471 TYR A C     1 
ATOM   3768  O  O     . TYR A 1 471 ? 134.545 130.770 83.059  1.00 22.81 ?  471 TYR A O     1 
ATOM   3769  C  CB    . TYR A 1 471 ? 134.437 133.310 85.212  1.00 17.21 ?  471 TYR A CB    1 
ATOM   3770  C  CG    . TYR A 1 471 ? 135.145 133.848 83.991  1.00 17.22 ?  471 TYR A CG    1 
ATOM   3771  C  CD1   . TYR A 1 471 ? 134.451 134.556 83.021  1.00 14.36 ?  471 TYR A CD1   1 
ATOM   3772  C  CD2   . TYR A 1 471 ? 136.503 133.637 83.802  1.00 9.73  ?  471 TYR A CD2   1 
ATOM   3773  C  CE1   . TYR A 1 471 ? 135.090 135.048 81.904  1.00 15.30 ?  471 TYR A CE1   1 
ATOM   3774  C  CE2   . TYR A 1 471 ? 137.150 134.122 82.685  1.00 12.50 ?  471 TYR A CE2   1 
ATOM   3775  C  CZ    . TYR A 1 471 ? 136.438 134.828 81.740  1.00 19.26 ?  471 TYR A CZ    1 
ATOM   3776  O  OH    . TYR A 1 471 ? 137.077 135.316 80.626  1.00 25.49 ?  471 TYR A OH    1 
ATOM   3777  N  N     . LEU A 1 472 ? 135.616 130.408 85.003  1.00 20.58 ?  472 LEU A N     1 
ATOM   3778  C  CA    . LEU A 1 472 ? 136.575 129.497 84.385  1.00 21.54 ?  472 LEU A CA    1 
ATOM   3779  C  C     . LEU A 1 472 ? 135.882 128.255 83.836  1.00 22.65 ?  472 LEU A C     1 
ATOM   3780  O  O     . LEU A 1 472 ? 136.162 127.819 82.714  1.00 25.03 ?  472 LEU A O     1 
ATOM   3781  C  CB    . LEU A 1 472 ? 137.653 129.109 85.397  1.00 20.17 ?  472 LEU A CB    1 
ATOM   3782  C  CG    . LEU A 1 472 ? 138.574 130.230 85.883  1.00 21.47 ?  472 LEU A CG    1 
ATOM   3783  C  CD1   . LEU A 1 472 ? 139.442 129.744 87.031  1.00 16.96 ?  472 LEU A CD1   1 
ATOM   3784  C  CD2   . LEU A 1 472 ? 139.426 130.765 84.743  1.00 18.15 ?  472 LEU A CD2   1 
ATOM   3785  N  N     . ALA A 1 473 ? 134.974 127.668 84.618  1.00 25.02 ?  473 ALA A N     1 
ATOM   3786  C  CA    . ALA A 1 473 ? 134.263 126.476 84.171  1.00 20.45 ?  473 ALA A CA    1 
ATOM   3787  C  C     . ALA A 1 473 ? 133.374 126.781 82.975  1.00 26.10 ?  473 ALA A C     1 
ATOM   3788  O  O     . ALA A 1 473 ? 133.277 125.974 82.043  1.00 38.80 ?  473 ALA A O     1 
ATOM   3789  C  CB    . ALA A 1 473 ? 133.442 125.895 85.321  1.00 22.16 ?  473 ALA A CB    1 
ATOM   3790  N  N     . GLN A 1 474 ? 132.715 127.939 82.982  1.00 19.22 ?  474 GLN A N     1 
ATOM   3791  C  CA    . GLN A 1 474 ? 131.883 128.328 81.851  1.00 18.94 ?  474 GLN A CA    1 
ATOM   3792  C  C     . GLN A 1 474 ? 132.698 128.763 80.644  1.00 24.02 ?  474 GLN A C     1 
ATOM   3793  O  O     . GLN A 1 474 ? 132.119 129.260 79.673  1.00 33.67 ?  474 GLN A O     1 
ATOM   3794  C  CB    . GLN A 1 474 ? 130.927 129.443 82.271  1.00 27.07 ?  474 GLN A CB    1 
ATOM   3795  C  CG    . GLN A 1 474 ? 129.816 128.976 83.194  1.00 25.38 ?  474 GLN A CG    1 
ATOM   3796  C  CD    . GLN A 1 474 ? 128.992 130.119 83.741  1.00 26.67 ?  474 GLN A CD    1 
ATOM   3797  O  OE1   . GLN A 1 474 ? 129.045 130.421 84.933  1.00 28.88 ?  474 GLN A OE1   1 
ATOM   3798  N  NE2   . GLN A 1 474 ? 128.224 130.763 82.873  1.00 31.20 ?  474 GLN A NE2   1 
ATOM   3799  N  N     . ASN A 1 475 ? 134.020 128.593 80.680  1.00 26.99 ?  475 ASN A N     1 
ATOM   3800  C  CA    . ASN A 1 475 ? 134.893 128.943 79.567  1.00 27.26 ?  475 ASN A CA    1 
ATOM   3801  C  C     . ASN A 1 475 ? 135.847 127.813 79.204  1.00 28.16 ?  475 ASN A C     1 
ATOM   3802  O  O     . ASN A 1 475 ? 136.814 128.045 78.470  1.00 28.62 ?  475 ASN A O     1 
ATOM   3803  C  CB    . ASN A 1 475 ? 135.684 130.214 79.892  1.00 28.63 ?  475 ASN A CB    1 
ATOM   3804  C  CG    . ASN A 1 475 ? 134.837 131.466 79.793  1.00 27.91 ?  475 ASN A CG    1 
ATOM   3805  O  OD1   . ASN A 1 475 ? 134.731 132.075 78.730  1.00 31.54 ?  475 ASN A OD1   1 
ATOM   3806  N  ND2   . ASN A 1 475 ? 134.224 131.853 80.904  1.00 21.63 ?  475 ASN A ND2   1 
ATOM   3807  N  N     . GLY A 1 476 ? 135.603 126.603 79.697  1.00 26.26 ?  476 GLY A N     1 
ATOM   3808  C  CA    . GLY A 1 476 ? 136.455 125.470 79.384  1.00 28.05 ?  476 GLY A CA    1 
ATOM   3809  C  C     . GLY A 1 476 ? 137.861 125.573 79.934  1.00 29.16 ?  476 GLY A C     1 
ATOM   3810  O  O     . GLY A 1 476 ? 138.822 125.247 79.227  1.00 36.23 ?  476 GLY A O     1 
ATOM   3811  N  N     . ILE A 1 477 ? 138.007 126.024 81.177  1.00 24.03 ?  477 ILE A N     1 
ATOM   3812  C  CA    . ILE A 1 477 ? 139.309 126.160 81.817  1.00 26.32 ?  477 ILE A CA    1 
ATOM   3813  C  C     . ILE A 1 477 ? 139.262 125.459 83.166  1.00 26.19 ?  477 ILE A C     1 
ATOM   3814  O  O     . ILE A 1 477 ? 138.376 125.734 83.982  1.00 28.05 ?  477 ILE A O     1 
ATOM   3815  C  CB    . ILE A 1 477 ? 139.712 127.637 81.990  1.00 23.27 ?  477 ILE A CB    1 
ATOM   3816  C  CG1   . ILE A 1 477 ? 139.805 128.330 80.630  1.00 22.06 ?  477 ILE A CG1   1 
ATOM   3817  C  CG2   . ILE A 1 477 ? 141.030 127.745 82.736  1.00 26.14 ?  477 ILE A CG2   1 
ATOM   3818  C  CD1   . ILE A 1 477 ? 139.811 129.835 80.715  1.00 30.51 ?  477 ILE A CD1   1 
ATOM   3819  N  N     . ALA A 1 478 ? 140.208 124.555 83.394  1.00 25.33 ?  478 ALA A N     1 
ATOM   3820  C  CA    . ALA A 1 478 ? 140.310 123.894 84.688  1.00 23.87 ?  478 ALA A CA    1 
ATOM   3821  C  C     . ALA A 1 478 ? 140.817 124.871 85.740  1.00 25.48 ?  478 ALA A C     1 
ATOM   3822  O  O     . ALA A 1 478 ? 141.690 125.699 85.472  1.00 30.55 ?  478 ALA A O     1 
ATOM   3823  C  CB    . ALA A 1 478 ? 141.240 122.684 84.597  1.00 24.77 ?  478 ALA A CB    1 
ATOM   3824  N  N     . TYR A 1 479 ? 140.260 124.771 86.947  1.00 24.48 ?  479 TYR A N     1 
ATOM   3825  C  CA    . TYR A 1 479 ? 140.670 125.665 88.024  1.00 17.19 ?  479 TYR A CA    1 
ATOM   3826  C  C     . TYR A 1 479 ? 142.151 125.501 88.339  1.00 25.60 ?  479 TYR A C     1 
ATOM   3827  O  O     . TYR A 1 479 ? 142.865 126.491 88.537  1.00 34.72 ?  479 TYR A O     1 
ATOM   3828  C  CB    . TYR A 1 479 ? 139.823 125.409 89.269  1.00 15.66 ?  479 TYR A CB    1 
ATOM   3829  C  CG    . TYR A 1 479 ? 140.023 126.419 90.377  1.00 23.73 ?  479 TYR A CG    1 
ATOM   3830  C  CD1   . TYR A 1 479 ? 141.038 126.264 91.313  1.00 27.17 ?  479 TYR A CD1   1 
ATOM   3831  C  CD2   . TYR A 1 479 ? 139.196 127.528 90.489  1.00 20.86 ?  479 TYR A CD2   1 
ATOM   3832  C  CE1   . TYR A 1 479 ? 141.224 127.183 92.327  1.00 23.55 ?  479 TYR A CE1   1 
ATOM   3833  C  CE2   . TYR A 1 479 ? 139.373 128.451 91.498  1.00 17.58 ?  479 TYR A CE2   1 
ATOM   3834  C  CZ    . TYR A 1 479 ? 140.388 128.276 92.414  1.00 24.53 ?  479 TYR A CZ    1 
ATOM   3835  O  OH    . TYR A 1 479 ? 140.564 129.196 93.421  1.00 22.94 ?  479 TYR A OH    1 
ATOM   3836  N  N     . GLU A 1 480 ? 142.633 124.259 88.385  1.00 22.29 ?  480 GLU A N     1 
ATOM   3837  C  CA    . GLU A 1 480 ? 144.026 123.984 88.711  1.00 21.55 ?  480 GLU A CA    1 
ATOM   3838  C  C     . GLU A 1 480 ? 144.966 124.154 87.525  1.00 27.60 ?  480 GLU A C     1 
ATOM   3839  O  O     . GLU A 1 480 ? 146.185 124.083 87.711  1.00 35.43 ?  480 GLU A O     1 
ATOM   3840  C  CB    . GLU A 1 480 ? 144.166 122.564 89.260  1.00 29.48 ?  480 GLU A CB    1 
ATOM   3841  C  CG    . GLU A 1 480 ? 143.375 122.294 90.524  1.00 27.89 ?  480 GLU A CG    1 
ATOM   3842  C  CD    . GLU A 1 480 ? 143.122 120.816 90.739  1.00 33.63 ?  480 GLU A CD    1 
ATOM   3843  O  OE1   . GLU A 1 480 ? 142.215 120.266 90.080  1.00 36.90 ?  480 GLU A OE1   1 
ATOM   3844  O  OE2   . GLU A 1 480 ? 143.835 120.201 91.558  1.00 35.90 -1 480 GLU A OE2   1 
ATOM   3845  N  N     . SER A 1 481 ? 144.439 124.372 86.324  1.00 27.27 ?  481 SER A N     1 
ATOM   3846  C  CA    . SER A 1 481 ? 145.275 124.432 85.140  1.00 25.58 ?  481 SER A CA    1 
ATOM   3847  C  C     . SER A 1 481 ? 146.113 125.709 85.124  1.00 28.50 ?  481 SER A C     1 
ATOM   3848  O  O     . SER A 1 481 ? 145.761 126.708 85.756  1.00 28.04 ?  481 SER A O     1 
ATOM   3849  C  CB    . SER A 1 481 ? 144.416 124.353 83.882  1.00 26.82 ?  481 SER A CB    1 
ATOM   3850  O  OG    . SER A 1 481 ? 144.048 125.644 83.433  1.00 25.94 ?  481 SER A OG    1 
ATOM   3851  N  N     . PRO A 1 482 ? 147.238 125.694 84.406  1.00 36.55 ?  482 PRO A N     1 
ATOM   3852  C  CA    . PRO A 1 482 ? 148.037 126.922 84.275  1.00 29.40 ?  482 PRO A CA    1 
ATOM   3853  C  C     . PRO A 1 482 ? 147.274 128.071 83.642  1.00 29.26 ?  482 PRO A C     1 
ATOM   3854  O  O     . PRO A 1 482 ? 147.530 129.233 83.980  1.00 37.32 ?  482 PRO A O     1 
ATOM   3855  C  CB    . PRO A 1 482 ? 149.219 126.480 83.400  1.00 25.33 ?  482 PRO A CB    1 
ATOM   3856  C  CG    . PRO A 1 482 ? 149.292 125.004 83.575  1.00 31.14 ?  482 PRO A CG    1 
ATOM   3857  C  CD    . PRO A 1 482 ? 147.882 124.538 83.761  1.00 31.54 ?  482 PRO A CD    1 
ATOM   3858  N  N     . GLU A 1 483 ? 146.347 127.783 82.726  1.00 33.59 ?  483 GLU A N     1 
ATOM   3859  C  CA    . GLU A 1 483 ? 145.586 128.846 82.080  1.00 29.87 ?  483 GLU A CA    1 
ATOM   3860  C  C     . GLU A 1 483 ? 144.693 129.574 83.078  1.00 27.33 ?  483 GLU A C     1 
ATOM   3861  O  O     . GLU A 1 483 ? 144.493 130.790 82.969  1.00 30.12 ?  483 GLU A O     1 
ATOM   3862  C  CB    . GLU A 1 483 ? 144.755 128.273 80.932  1.00 31.54 ?  483 GLU A CB    1 
ATOM   3863  C  CG    . GLU A 1 483 ? 145.583 127.653 79.821  1.00 30.89 ?  483 GLU A CG    1 
ATOM   3864  C  CD    . GLU A 1 483 ? 145.892 126.190 80.071  1.00 36.68 ?  483 GLU A CD    1 
ATOM   3865  O  OE1   . GLU A 1 483 ? 145.774 125.745 81.232  1.00 36.17 ?  483 GLU A OE1   1 
ATOM   3866  O  OE2   . GLU A 1 483 ? 146.255 125.485 79.106  1.00 38.37 -1 483 GLU A OE2   1 
ATOM   3867  N  N     . ALA A 1 484 ? 144.136 128.848 84.049  1.00 27.11 ?  484 ALA A N     1 
ATOM   3868  C  CA    . ALA A 1 484 ? 143.333 129.498 85.077  1.00 23.82 ?  484 ALA A CA    1 
ATOM   3869  C  C     . ALA A 1 484 ? 144.167 130.489 85.875  1.00 22.48 ?  484 ALA A C     1 
ATOM   3870  O  O     . ALA A 1 484 ? 143.727 131.615 86.138  1.00 25.38 ?  484 ALA A O     1 
ATOM   3871  C  CB    . ALA A 1 484 ? 142.710 128.449 85.997  1.00 19.89 ?  484 ALA A CB    1 
ATOM   3872  N  N     . ARG A 1 485 ? 145.381 130.093 86.261  1.00 26.99 ?  485 ARG A N     1 
ATOM   3873  C  CA    . ARG A 1 485 ? 146.257 131.004 86.988  1.00 19.10 ?  485 ARG A CA    1 
ATOM   3874  C  C     . ARG A 1 485 ? 146.685 132.173 86.113  1.00 15.83 ?  485 ARG A C     1 
ATOM   3875  O  O     . ARG A 1 485 ? 146.831 133.296 86.602  1.00 28.41 ?  485 ARG A O     1 
ATOM   3876  C  CB    . ARG A 1 485 ? 147.475 130.253 87.523  1.00 22.03 ?  485 ARG A CB    1 
ATOM   3877  C  CG    . ARG A 1 485 ? 147.171 129.376 88.724  1.00 18.81 ?  485 ARG A CG    1 
ATOM   3878  C  CD    . ARG A 1 485 ? 148.439 128.794 89.321  1.00 25.87 ?  485 ARG A CD    1 
ATOM   3879  N  NE    . ARG A 1 485 ? 149.161 127.958 88.369  1.00 27.92 ?  485 ARG A NE    1 
ATOM   3880  C  CZ    . ARG A 1 485 ? 148.850 126.698 88.093  1.00 25.00 ?  485 ARG A CZ    1 
ATOM   3881  N  NH1   . ARG A 1 485 ? 147.827 126.096 88.675  1.00 24.54 1  485 ARG A NH1   1 
ATOM   3882  N  NH2   . ARG A 1 485 ? 149.585 126.029 87.212  1.00 22.93 ?  485 ARG A NH2   1 
ATOM   3883  N  N     . ASP A 1 486 ? 146.892 131.933 84.818  1.00 24.59 ?  486 ASP A N     1 
ATOM   3884  C  CA    . ASP A 1 486 ? 147.232 133.024 83.908  1.00 21.28 ?  486 ASP A CA    1 
ATOM   3885  C  C     . ASP A 1 486 ? 146.109 134.052 83.843  1.00 24.18 ?  486 ASP A C     1 
ATOM   3886  O  O     . ASP A 1 486 ? 146.349 135.266 83.935  1.00 31.44 ?  486 ASP A O     1 
ATOM   3887  C  CB    . ASP A 1 486 ? 147.532 132.461 82.518  1.00 27.44 ?  486 ASP A CB    1 
ATOM   3888  C  CG    . ASP A 1 486 ? 148.040 133.514 81.560  1.00 36.45 ?  486 ASP A CG    1 
ATOM   3889  O  OD1   . ASP A 1 486 ? 149.058 134.165 81.872  1.00 37.53 ?  486 ASP A OD1   1 
ATOM   3890  O  OD2   . ASP A 1 486 ? 147.419 133.691 80.491  1.00 35.40 -1 486 ASP A OD2   1 
ATOM   3891  N  N     . PHE A 1 487 ? 144.869 133.582 83.686  1.00 24.13 ?  487 PHE A N     1 
ATOM   3892  C  CA    . PHE A 1 487 ? 143.742 134.506 83.663  1.00 18.44 ?  487 PHE A CA    1 
ATOM   3893  C  C     . PHE A 1 487 ? 143.616 135.248 84.985  1.00 25.00 ?  487 PHE A C     1 
ATOM   3894  O  O     . PHE A 1 487 ? 143.365 136.455 84.999  1.00 27.50 ?  487 PHE A O     1 
ATOM   3895  C  CB    . PHE A 1 487 ? 142.432 133.783 83.363  1.00 17.37 ?  487 PHE A CB    1 
ATOM   3896  C  CG    . PHE A 1 487 ? 141.220 134.588 83.739  1.00 17.64 ?  487 PHE A CG    1 
ATOM   3897  C  CD1   . PHE A 1 487 ? 140.739 135.575 82.894  1.00 17.12 ?  487 PHE A CD1   1 
ATOM   3898  C  CD2   . PHE A 1 487 ? 140.590 134.395 84.957  1.00 18.38 ?  487 PHE A CD2   1 
ATOM   3899  C  CE1   . PHE A 1 487 ? 139.642 136.333 83.246  1.00 21.94 ?  487 PHE A CE1   1 
ATOM   3900  C  CE2   . PHE A 1 487 ? 139.493 135.152 85.313  1.00 16.04 ?  487 PHE A CE2   1 
ATOM   3901  C  CZ    . PHE A 1 487 ? 139.018 136.121 84.457  1.00 20.75 ?  487 PHE A CZ    1 
ATOM   3902  N  N     . ALA A 1 488 ? 143.750 134.536 86.105  1.00 18.69 ?  488 ALA A N     1 
ATOM   3903  C  CA    . ALA A 1 488 ? 143.638 135.199 87.398  1.00 14.01 ?  488 ALA A CA    1 
ATOM   3904  C  C     . ALA A 1 488 ? 144.709 136.267 87.550  1.00 22.50 ?  488 ALA A C     1 
ATOM   3905  O  O     . ALA A 1 488 ? 144.428 137.381 88.007  1.00 33.94 ?  488 ALA A O     1 
ATOM   3906  C  CB    . ALA A 1 488 ? 143.732 134.173 88.526  1.00 16.39 ?  488 ALA A CB    1 
ATOM   3907  N  N     . ASN A 1 489 ? 145.941 135.950 87.152  1.00 20.62 ?  489 ASN A N     1 
ATOM   3908  C  CA    . ASN A 1 489 ? 147.024 136.921 87.210  1.00 19.04 ?  489 ASN A CA    1 
ATOM   3909  C  C     . ASN A 1 489 ? 146.674 138.170 86.416  1.00 15.55 ?  489 ASN A C     1 
ATOM   3910  O  O     . ASN A 1 489 ? 146.722 139.286 86.945  1.00 31.24 ?  489 ASN A O     1 
ATOM   3911  C  CB    . ASN A 1 489 ? 148.310 136.284 86.682  1.00 20.07 ?  489 ASN A CB    1 
ATOM   3912  C  CG    . ASN A 1 489 ? 149.526 137.154 86.901  1.00 25.70 ?  489 ASN A CG    1 
ATOM   3913  O  OD1   . ASN A 1 489 ? 149.669 137.792 87.943  1.00 31.84 ?  489 ASN A OD1   1 
ATOM   3914  N  ND2   . ASN A 1 489 ? 150.418 137.179 85.919  1.00 29.94 ?  489 ASN A ND2   1 
ATOM   3915  N  N     . THR A 1 490 ? 146.294 138.001 85.148  1.00 20.42 ?  490 THR A N     1 
ATOM   3916  C  CA    . THR A 1 490 ? 146.004 139.169 84.321  1.00 20.52 ?  490 THR A CA    1 
ATOM   3917  C  C     . THR A 1 490 ? 144.821 139.962 84.868  1.00 18.82 ?  490 THR A C     1 
ATOM   3918  O  O     . THR A 1 490 ? 144.882 141.195 84.972  1.00 22.42 ?  490 THR A O     1 
ATOM   3919  C  CB    . THR A 1 490 ? 145.736 138.742 82.878  1.00 25.70 ?  490 THR A CB    1 
ATOM   3920  O  OG1   . THR A 1 490 ? 146.906 138.112 82.344  1.00 32.93 ?  490 THR A OG1   1 
ATOM   3921  C  CG2   . THR A 1 490 ? 145.381 139.949 82.024  1.00 18.48 ?  490 THR A CG2   1 
ATOM   3922  N  N     . PHE A 1 491 ? 143.743 139.271 85.242  1.00 17.56 ?  491 PHE A N     1 
ATOM   3923  C  CA    . PHE A 1 491 ? 142.528 139.951 85.672  1.00 18.90 ?  491 PHE A CA    1 
ATOM   3924  C  C     . PHE A 1 491 ? 142.758 140.728 86.960  1.00 17.13 ?  491 PHE A C     1 
ATOM   3925  O  O     . PHE A 1 491 ? 142.348 141.888 87.078  1.00 21.08 ?  491 PHE A O     1 
ATOM   3926  C  CB    . PHE A 1 491 ? 141.397 138.937 85.849  1.00 19.50 ?  491 PHE A CB    1 
ATOM   3927  C  CG    . PHE A 1 491 ? 140.142 139.523 86.428  1.00 17.98 ?  491 PHE A CG    1 
ATOM   3928  C  CD1   . PHE A 1 491 ? 139.173 140.068 85.605  1.00 13.46 ?  491 PHE A CD1   1 
ATOM   3929  C  CD2   . PHE A 1 491 ? 139.927 139.525 87.797  1.00 15.09 ?  491 PHE A CD2   1 
ATOM   3930  C  CE1   . PHE A 1 491 ? 138.020 140.609 86.134  1.00 16.01 ?  491 PHE A CE1   1 
ATOM   3931  C  CE2   . PHE A 1 491 ? 138.777 140.063 88.330  1.00 11.00 ?  491 PHE A CE2   1 
ATOM   3932  C  CZ    . PHE A 1 491 ? 137.821 140.607 87.497  1.00 16.39 ?  491 PHE A CZ    1 
ATOM   3933  N  N     . PHE A 1 492 ? 143.411 140.109 87.942  1.00 17.22 ?  492 PHE A N     1 
ATOM   3934  C  CA    . PHE A 1 492 ? 143.613 140.794 89.210  1.00 13.10 ?  492 PHE A CA    1 
ATOM   3935  C  C     . PHE A 1 492 ? 144.710 141.843 89.121  1.00 12.68 ?  492 PHE A C     1 
ATOM   3936  O  O     . PHE A 1 492 ? 144.663 142.836 89.852  1.00 19.88 ?  492 PHE A O     1 
ATOM   3937  C  CB    . PHE A 1 492 ? 143.890 139.772 90.311  1.00 15.05 ?  492 PHE A CB    1 
ATOM   3938  C  CG    . PHE A 1 492 ? 142.671 138.996 90.718  1.00 14.18 ?  492 PHE A CG    1 
ATOM   3939  C  CD1   . PHE A 1 492 ? 141.714 139.568 91.539  1.00 11.90 ?  492 PHE A CD1   1 
ATOM   3940  C  CD2   . PHE A 1 492 ? 142.460 137.712 90.250  1.00 18.32 ?  492 PHE A CD2   1 
ATOM   3941  C  CE1   . PHE A 1 492 ? 140.584 138.863 91.903  1.00 10.68 ?  492 PHE A CE1   1 
ATOM   3942  C  CE2   . PHE A 1 492 ? 141.332 137.004 90.609  1.00 13.34 ?  492 PHE A CE2   1 
ATOM   3943  C  CZ    . PHE A 1 492 ? 140.393 137.580 91.439  1.00 13.29 ?  492 PHE A CZ    1 
ATOM   3944  N  N     . MET A 1 493 ? 145.673 141.684 88.208  1.00 6.28  ?  493 MET A N     1 
ATOM   3945  C  CA    . MET A 1 493 ? 146.590 142.782 87.926  1.00 9.65  ?  493 MET A CA    1 
ATOM   3946  C  C     . MET A 1 493 ? 145.842 143.984 87.369  1.00 11.75 ?  493 MET A C     1 
ATOM   3947  O  O     . MET A 1 493 ? 146.091 145.123 87.779  1.00 20.85 ?  493 MET A O     1 
ATOM   3948  C  CB    . MET A 1 493 ? 147.677 142.323 86.955  1.00 17.64 ?  493 MET A CB    1 
ATOM   3949  C  CG    . MET A 1 493 ? 148.795 143.329 86.749  1.00 13.36 ?  493 MET A CG    1 
ATOM   3950  S  SD    . MET A 1 493 ? 148.448 144.538 85.457  1.00 35.30 ?  493 MET A SD    1 
ATOM   3951  C  CE    . MET A 1 493 ? 147.562 143.528 84.274  1.00 18.31 ?  493 MET A CE    1 
ATOM   3952  N  N     . MET A 1 494 ? 144.919 143.752 86.433  1.00 15.16 ?  494 MET A N     1 
ATOM   3953  C  CA    . MET A 1 494 ? 144.129 144.856 85.895  1.00 14.63 ?  494 MET A CA    1 
ATOM   3954  C  C     . MET A 1 494 ? 143.261 145.486 86.977  1.00 15.89 ?  494 MET A C     1 
ATOM   3955  O  O     . MET A 1 494 ? 143.108 146.713 87.030  1.00 23.64 ?  494 MET A O     1 
ATOM   3956  C  CB    . MET A 1 494 ? 143.268 144.367 84.732  1.00 12.54 ?  494 MET A CB    1 
ATOM   3957  C  CG    . MET A 1 494 ? 144.059 143.785 83.574  1.00 16.88 ?  494 MET A CG    1 
ATOM   3958  S  SD    . MET A 1 494 ? 143.152 143.811 82.019  1.00 30.82 ?  494 MET A SD    1 
ATOM   3959  C  CE    . MET A 1 494 ? 141.755 144.841 82.452  1.00 24.74 ?  494 MET A CE    1 
ATOM   3960  N  N     . VAL A 1 495 ? 142.676 144.657 87.844  1.00 16.52 ?  495 VAL A N     1 
ATOM   3961  C  CA    . VAL A 1 495 ? 141.845 145.172 88.928  1.00 8.67  ?  495 VAL A CA    1 
ATOM   3962  C  C     . VAL A 1 495 ? 142.672 146.054 89.854  1.00 13.82 ?  495 VAL A C     1 
ATOM   3963  O  O     . VAL A 1 495 ? 142.245 147.146 90.242  1.00 21.27 ?  495 VAL A O     1 
ATOM   3964  C  CB    . VAL A 1 495 ? 141.185 144.015 89.697  1.00 16.31 ?  495 VAL A CB    1 
ATOM   3965  C  CG1   . VAL A 1 495 ? 140.455 144.542 90.924  1.00 12.57 ?  495 VAL A CG1   1 
ATOM   3966  C  CG2   . VAL A 1 495 ? 140.236 143.252 88.793  1.00 13.81 ?  495 VAL A CG2   1 
ATOM   3967  N  N     . ASN A 1 496 ? 143.867 145.590 90.226  1.00 21.62 ?  496 ASN A N     1 
ATOM   3968  C  CA    . ASN A 1 496 ? 144.739 146.393 91.076  1.00 9.43  ?  496 ASN A CA    1 
ATOM   3969  C  C     . ASN A 1 496 ? 145.133 147.690 90.386  1.00 6.68  ?  496 ASN A C     1 
ATOM   3970  O  O     . ASN A 1 496 ? 145.137 148.758 91.008  1.00 19.01 ?  496 ASN A O     1 
ATOM   3971  C  CB    . ASN A 1 496 ? 145.982 145.588 91.458  1.00 11.85 ?  496 ASN A CB    1 
ATOM   3972  C  CG    . ASN A 1 496 ? 146.740 146.204 92.613  1.00 10.57 ?  496 ASN A CG    1 
ATOM   3973  O  OD1   . ASN A 1 496 ? 146.149 146.782 93.522  1.00 21.83 ?  496 ASN A OD1   1 
ATOM   3974  N  ND2   . ASN A 1 496 ? 148.060 146.081 92.584  1.00 11.35 ?  496 ASN A ND2   1 
ATOM   3975  N  N     . PHE A 1 497 ? 145.463 147.619 89.097  1.00 8.85  ?  497 PHE A N     1 
ATOM   3976  C  CA    . PHE A 1 497 ? 145.844 148.818 88.363  1.00 9.34  ?  497 PHE A CA    1 
ATOM   3977  C  C     . PHE A 1 497 ? 144.726 149.848 88.387  1.00 19.93 ?  497 PHE A C     1 
ATOM   3978  O  O     . PHE A 1 497 ? 144.950 151.021 88.702  1.00 22.70 ?  497 PHE A O     1 
ATOM   3979  C  CB    . PHE A 1 497 ? 146.209 148.450 86.924  1.00 14.60 ?  497 PHE A CB    1 
ATOM   3980  C  CG    . PHE A 1 497 ? 146.554 149.629 86.063  1.00 17.98 ?  497 PHE A CG    1 
ATOM   3981  C  CD1   . PHE A 1 497 ? 145.567 150.308 85.369  1.00 16.90 ?  497 PHE A CD1   1 
ATOM   3982  C  CD2   . PHE A 1 497 ? 147.865 150.054 85.941  1.00 17.85 ?  497 PHE A CD2   1 
ATOM   3983  C  CE1   . PHE A 1 497 ? 145.880 151.391 84.577  1.00 16.93 ?  497 PHE A CE1   1 
ATOM   3984  C  CE2   . PHE A 1 497 ? 148.184 151.136 85.148  1.00 17.69 ?  497 PHE A CE2   1 
ATOM   3985  C  CZ    . PHE A 1 497 ? 147.190 151.806 84.465  1.00 20.30 ?  497 PHE A CZ    1 
ATOM   3986  N  N     . TYR A 1 498 ? 143.502 149.423 88.072  1.00 17.48 ?  498 TYR A N     1 
ATOM   3987  C  CA    . TYR A 1 498 ? 142.408 150.382 87.979  1.00 12.66 ?  498 TYR A CA    1 
ATOM   3988  C  C     . TYR A 1 498 ? 141.946 150.854 89.350  1.00 18.78 ?  498 TYR A C     1 
ATOM   3989  O  O     . TYR A 1 498 ? 141.507 152.000 89.485  1.00 23.45 ?  498 TYR A O     1 
ATOM   3990  C  CB    . TYR A 1 498 ? 141.254 149.786 87.176  1.00 20.13 ?  498 TYR A CB    1 
ATOM   3991  C  CG    . TYR A 1 498 ? 141.565 149.726 85.701  1.00 19.29 ?  498 TYR A CG    1 
ATOM   3992  C  CD1   . TYR A 1 498 ? 141.932 150.872 85.008  1.00 19.47 ?  498 TYR A CD1   1 
ATOM   3993  C  CD2   . TYR A 1 498 ? 141.518 148.526 85.006  1.00 17.54 ?  498 TYR A CD2   1 
ATOM   3994  C  CE1   . TYR A 1 498 ? 142.231 150.829 83.665  1.00 19.64 ?  498 TYR A CE1   1 
ATOM   3995  C  CE2   . TYR A 1 498 ? 141.815 148.473 83.659  1.00 21.16 ?  498 TYR A CE2   1 
ATOM   3996  C  CZ    . TYR A 1 498 ? 142.170 149.628 82.994  1.00 22.67 ?  498 TYR A CZ    1 
ATOM   3997  O  OH    . TYR A 1 498 ? 142.466 149.584 81.652  1.00 27.43 ?  498 TYR A OH    1 
ATOM   3998  N  N     . SER A 1 499 ? 142.070 150.020 90.384  1.00 17.80 ?  499 SER A N     1 
ATOM   3999  C  CA    . SER A 1 499 ? 141.734 150.487 91.723  1.00 10.72 ?  499 SER A CA    1 
ATOM   4000  C  C     . SER A 1 499 ? 142.755 151.503 92.216  1.00 8.85  ?  499 SER A C     1 
ATOM   4001  O  O     . SER A 1 499 ? 142.391 152.494 92.856  1.00 14.04 ?  499 SER A O     1 
ATOM   4002  C  CB    . SER A 1 499 ? 141.630 149.307 92.691  1.00 10.23 ?  499 SER A CB    1 
ATOM   4003  O  OG    . SER A 1 499 ? 142.908 148.840 93.077  1.00 21.33 ?  499 SER A OG    1 
ATOM   4004  N  N     . ILE A 1 500 ? 144.036 151.287 91.909  1.00 13.24 ?  500 ILE A N     1 
ATOM   4005  C  CA    . ILE A 1 500 ? 145.055 152.272 92.257  1.00 12.65 ?  500 ILE A CA    1 
ATOM   4006  C  C     . ILE A 1 500 ? 144.824 153.565 91.490  1.00 14.95 ?  500 ILE A C     1 
ATOM   4007  O  O     . ILE A 1 500 ? 144.969 154.664 92.036  1.00 22.37 ?  500 ILE A O     1 
ATOM   4008  C  CB    . ILE A 1 500 ? 146.461 151.704 91.995  1.00 21.08 ?  500 ILE A CB    1 
ATOM   4009  C  CG1   . ILE A 1 500 ? 146.825 150.672 93.062  1.00 15.11 ?  500 ILE A CG1   1 
ATOM   4010  C  CG2   . ILE A 1 500 ? 147.486 152.825 91.953  1.00 12.81 ?  500 ILE A CG2   1 
ATOM   4011  C  CD1   . ILE A 1 500 ? 148.046 149.856 92.727  1.00 10.87 ?  500 ILE A CD1   1 
ATOM   4012  N  N     . GLN A 1 501 ? 144.472 153.455 90.207  1.00 18.63 ?  501 GLN A N     1 
ATOM   4013  C  CA    . GLN A 1 501 ? 144.207 154.649 89.414  1.00 14.56 ?  501 GLN A CA    1 
ATOM   4014  C  C     . GLN A 1 501 ? 143.020 155.423 89.969  1.00 18.79 ?  501 GLN A C     1 
ATOM   4015  O  O     . GLN A 1 501 ? 143.062 156.654 90.061  1.00 29.77 ?  501 GLN A O     1 
ATOM   4016  C  CB    . GLN A 1 501 ? 143.967 154.262 87.954  1.00 20.35 ?  501 GLN A CB    1 
ATOM   4017  C  CG    . GLN A 1 501 ? 144.327 155.352 86.962  1.00 19.80 ?  501 GLN A CG    1 
ATOM   4018  C  CD    . GLN A 1 501 ? 144.025 154.958 85.531  1.00 25.12 ?  501 GLN A CD    1 
ATOM   4019  O  OE1   . GLN A 1 501 ? 142.899 154.589 85.201  1.00 28.02 ?  501 GLN A OE1   1 
ATOM   4020  N  NE2   . GLN A 1 501 ? 145.034 155.029 84.674  1.00 26.48 ?  501 GLN A NE2   1 
ATOM   4021  N  N     . ARG A 1 502 ? 141.952 154.720 90.353  1.00 20.30 ?  502 ARG A N     1 
ATOM   4022  C  CA    . ARG A 1 502 ? 140.796 155.390 90.938  1.00 15.38 ?  502 ARG A CA    1 
ATOM   4023  C  C     . ARG A 1 502 ? 141.136 156.016 92.285  1.00 12.78 ?  502 ARG A C     1 
ATOM   4024  O  O     . ARG A 1 502 ? 140.669 157.114 92.596  1.00 28.68 ?  502 ARG A O     1 
ATOM   4025  C  CB    . ARG A 1 502 ? 139.632 154.413 91.079  1.00 19.73 ?  502 ARG A CB    1 
ATOM   4026  C  CG    . ARG A 1 502 ? 138.320 155.082 91.450  1.00 18.36 ?  502 ARG A CG    1 
ATOM   4027  C  CD    . ARG A 1 502 ? 137.966 156.180 90.466  1.00 16.95 ?  502 ARG A CD    1 
ATOM   4028  N  NE    . ARG A 1 502 ? 136.893 157.033 90.961  1.00 22.83 ?  502 ARG A NE    1 
ATOM   4029  C  CZ    . ARG A 1 502 ? 136.784 158.327 90.699  1.00 22.42 ?  502 ARG A CZ    1 
ATOM   4030  N  NH1   . ARG A 1 502 ? 137.670 158.958 89.946  1.00 26.12 1  502 ARG A NH1   1 
ATOM   4031  N  NH2   . ARG A 1 502 ? 135.761 159.007 91.207  1.00 20.31 ?  502 ARG A NH2   1 
ATOM   4032  N  N     . SER A 1 503 ? 141.935 155.331 93.104  1.00 14.56 ?  503 SER A N     1 
ATOM   4033  C  CA    . SER A 1 503 ? 142.337 155.901 94.385  1.00 15.09 ?  503 SER A CA    1 
ATOM   4034  C  C     . SER A 1 503 ? 143.153 157.172 94.187  1.00 20.29 ?  503 SER A C     1 
ATOM   4035  O  O     . SER A 1 503 ? 142.935 158.177 94.876  1.00 19.19 ?  503 SER A O     1 
ATOM   4036  C  CB    . SER A 1 503 ? 143.125 154.866 95.188  1.00 12.70 ?  503 SER A CB    1 
ATOM   4037  O  OG    . SER A 1 503 ? 143.257 155.252 96.542  1.00 12.35 ?  503 SER A OG    1 
ATOM   4038  N  N     . ALA A 1 504 ? 144.092 157.152 93.239  1.00 22.69 ?  504 ALA A N     1 
ATOM   4039  C  CA    . ALA A 1 504 ? 144.883 158.343 92.951  1.00 16.87 ?  504 ALA A CA    1 
ATOM   4040  C  C     . ALA A 1 504 ? 144.012 159.466 92.401  1.00 21.25 ?  504 ALA A C     1 
ATOM   4041  O  O     . ALA A 1 504 ? 144.201 160.636 92.751  1.00 30.28 ?  504 ALA A O     1 
ATOM   4042  C  CB    . ALA A 1 504 ? 146.005 158.001 91.971  1.00 20.07 ?  504 ALA A CB    1 
ATOM   4043  N  N     . GLU A 1 505 ? 143.053 159.131 91.534  1.00 21.39 ?  505 GLU A N     1 
ATOM   4044  C  CA    . GLU A 1 505 ? 142.158 160.146 90.990  1.00 22.88 ?  505 GLU A CA    1 
ATOM   4045  C  C     . GLU A 1 505 ? 141.294 160.763 92.082  1.00 22.16 ?  505 GLU A C     1 
ATOM   4046  O  O     . GLU A 1 505 ? 141.046 161.973 92.079  1.00 28.83 ?  505 GLU A O     1 
ATOM   4047  C  CB    . GLU A 1 505 ? 141.285 159.538 89.893  1.00 23.46 ?  505 GLU A CB    1 
ATOM   4048  C  CG    . GLU A 1 505 ? 142.037 159.198 88.618  1.00 23.03 ?  505 GLU A CG    1 
ATOM   4049  C  CD    . GLU A 1 505 ? 141.265 158.251 87.722  1.00 31.96 ?  505 GLU A CD    1 
ATOM   4050  O  OE1   . GLU A 1 505 ? 140.125 157.888 88.080  1.00 37.45 ?  505 GLU A OE1   1 
ATOM   4051  O  OE2   . GLU A 1 505 ? 141.796 157.873 86.657  1.00 33.24 -1 505 GLU A OE2   1 
ATOM   4052  N  N     . ILE A 1 506 ? 140.815 159.942 93.017  1.00 22.41 ?  506 ILE A N     1 
ATOM   4053  C  CA    . ILE A 1 506 ? 140.034 160.457 94.135  1.00 20.23 ?  506 ILE A CA    1 
ATOM   4054  C  C     . ILE A 1 506 ? 140.891 161.359 95.012  1.00 25.70 ?  506 ILE A C     1 
ATOM   4055  O  O     . ILE A 1 506 ? 140.437 162.410 95.475  1.00 30.60 ?  506 ILE A O     1 
ATOM   4056  C  CB    . ILE A 1 506 ? 139.425 159.298 94.942  1.00 21.42 ?  506 ILE A CB    1 
ATOM   4057  C  CG1   . ILE A 1 506 ? 138.423 158.519 94.087  1.00 22.59 ?  506 ILE A CG1   1 
ATOM   4058  C  CG2   . ILE A 1 506 ? 138.765 159.819 96.206  1.00 23.20 ?  506 ILE A CG2   1 
ATOM   4059  C  CD1   . ILE A 1 506 ? 138.037 157.180 94.671  1.00 18.03 ?  506 ILE A CD1   1 
ATOM   4060  N  N     . ALA A 1 507 ? 142.140 160.960 95.259  1.00 25.82 ?  507 ALA A N     1 
ATOM   4061  C  CA    . ALA A 1 507 ? 143.040 161.807 96.034  1.00 21.00 ?  507 ALA A CA    1 
ATOM   4062  C  C     . ALA A 1 507 ? 143.274 163.141 95.334  1.00 26.01 ?  507 ALA A C     1 
ATOM   4063  O  O     . ALA A 1 507 ? 143.346 164.188 95.984  1.00 29.46 ?  507 ALA A O     1 
ATOM   4064  C  CB    . ALA A 1 507 ? 144.364 161.084 96.273  1.00 17.37 ?  507 ALA A CB    1 
ATOM   4065  N  N     . LYS A 1 508 ? 143.400 163.118 94.007  1.00 26.95 ?  508 LYS A N     1 
ATOM   4066  C  CA    . LYS A 1 508 ? 143.591 164.354 93.255  1.00 26.34 ?  508 LYS A CA    1 
ATOM   4067  C  C     . LYS A 1 508 ? 142.348 165.235 93.301  1.00 33.38 ?  508 LYS A C     1 
ATOM   4068  O  O     . LYS A 1 508 ? 142.452 166.459 93.436  1.00 38.44 ?  508 LYS A O     1 
ATOM   4069  C  CB    . LYS A 1 508 ? 143.963 164.032 91.809  1.00 32.58 ?  508 LYS A CB    1 
ATOM   4070  C  CG    . LYS A 1 508 ? 144.091 165.249 90.912  1.00 29.57 ?  508 LYS A CG    1 
ATOM   4071  C  CD    . LYS A 1 508 ? 144.334 164.844 89.469  1.00 31.00 ?  508 LYS A CD    1 
ATOM   4072  C  CE    . LYS A 1 508 ? 144.541 166.058 88.582  1.00 36.32 ?  508 LYS A CE    1 
ATOM   4073  N  NZ    . LYS A 1 508 ? 145.452 165.765 87.441  1.00 37.35 1  508 LYS A NZ    1 
ATOM   4074  N  N     . GLU A 1 509 ? 141.163 164.631 93.187  1.00 30.65 ?  509 GLU A N     1 
ATOM   4075  C  CA    . GLU A 1 509 ? 139.934 165.416 93.163  1.00 29.65 ?  509 GLU A CA    1 
ATOM   4076  C  C     . GLU A 1 509 ? 139.626 166.011 94.531  1.00 35.83 ?  509 GLU A C     1 
ATOM   4077  O  O     . GLU A 1 509 ? 139.216 167.173 94.630  1.00 43.17 ?  509 GLU A O     1 
ATOM   4078  C  CB    . GLU A 1 509 ? 138.772 164.551 92.668  1.00 28.18 ?  509 GLU A CB    1 
ATOM   4079  C  CG    . GLU A 1 509 ? 137.911 163.958 93.769  1.00 32.33 ?  509 GLU A CG    1 
ATOM   4080  C  CD    . GLU A 1 509 ? 137.158 162.722 93.319  1.00 41.95 ?  509 GLU A CD    1 
ATOM   4081  O  OE1   . GLU A 1 509 ? 137.240 162.376 92.121  1.00 39.51 ?  509 GLU A OE1   1 
ATOM   4082  O  OE2   . GLU A 1 509 ? 136.487 162.093 94.164  1.00 38.40 -1 509 GLU A OE2   1 
ATOM   4083  N  N     . LYS A 1 510 ? 139.814 165.234 95.596  1.00 32.55 ?  510 LYS A N     1 
ATOM   4084  C  CA    . LYS A 1 510 ? 139.575 165.710 96.950  1.00 26.51 ?  510 LYS A CA    1 
ATOM   4085  C  C     . LYS A 1 510 ? 140.771 166.440 97.544  1.00 35.32 ?  510 LYS A C     1 
ATOM   4086  O  O     . LYS A 1 510 ? 140.621 167.097 98.579  1.00 42.94 ?  510 LYS A O     1 
ATOM   4087  C  CB    . LYS A 1 510 ? 139.191 164.538 97.858  1.00 27.97 ?  510 LYS A CB    1 
ATOM   4088  C  CG    . LYS A 1 510 ? 137.961 163.783 97.398  1.00 31.90 ?  510 LYS A CG    1 
ATOM   4089  C  CD    . LYS A 1 510 ? 137.444 162.853 98.480  1.00 30.01 ?  510 LYS A CD    1 
ATOM   4090  C  CE    . LYS A 1 510 ? 136.105 162.252 98.093  1.00 30.76 ?  510 LYS A CE    1 
ATOM   4091  N  NZ    . LYS A 1 510 ? 135.254 161.985 99.283  1.00 33.43 1  510 LYS A NZ    1 
ATOM   4092  N  N     . GLY A 1 511 ? 141.943 166.341 96.923  1.00 30.22 ?  511 GLY A N     1 
ATOM   4093  C  CA    . GLY A 1 511 ? 143.115 167.029 97.419  1.00 28.44 ?  511 GLY A CA    1 
ATOM   4094  C  C     . GLY A 1 511 ? 143.739 166.430 98.657  1.00 34.08 ?  511 GLY A C     1 
ATOM   4095  O  O     . GLY A 1 511 ? 144.632 167.049 99.241  1.00 35.87 ?  511 GLY A O     1 
ATOM   4096  N  N     . GLU A 1 512 ? 143.303 165.244 99.079  1.00 32.26 ?  512 GLU A N     1 
ATOM   4097  C  CA    . GLU A 1 512 ? 143.815 164.626 100.291 1.00 26.54 ?  512 GLU A CA    1 
ATOM   4098  C  C     . GLU A 1 512 ? 144.131 163.160 100.037 1.00 25.73 ?  512 GLU A C     1 
ATOM   4099  O  O     . GLU A 1 512 ? 143.462 162.489 99.249  1.00 28.97 ?  512 GLU A O     1 
ATOM   4100  C  CB    . GLU A 1 512 ? 142.815 164.741 101.449 1.00 29.37 ?  512 GLU A CB    1 
ATOM   4101  C  CG    . GLU A 1 512 ? 141.470 164.097 101.172 1.00 24.48 ?  512 GLU A CG    1 
ATOM   4102  C  CD    . GLU A 1 512 ? 140.647 163.906 102.429 1.00 33.51 ?  512 GLU A CD    1 
ATOM   4103  O  OE1   . GLU A 1 512 ? 141.246 163.756 103.514 1.00 36.74 ?  512 GLU A OE1   1 
ATOM   4104  O  OE2   . GLU A 1 512 ? 139.401 163.909 102.335 1.00 34.30 -1 512 GLU A OE2   1 
ATOM   4105  N  N     . THR A 1 513 ? 145.162 162.677 100.718 1.00 28.69 ?  513 THR A N     1 
ATOM   4106  C  CA    . THR A 1 513 ? 145.535 161.273 100.747 1.00 22.47 ?  513 THR A CA    1 
ATOM   4107  C  C     . THR A 1 513 ? 145.167 160.687 102.105 1.00 22.48 ?  513 THR A C     1 
ATOM   4108  O  O     . THR A 1 513 ? 144.654 161.380 102.988 1.00 37.27 ?  513 THR A O     1 
ATOM   4109  C  CB    . THR A 1 513 ? 147.029 161.105 100.459 1.00 23.85 ?  513 THR A CB    1 
ATOM   4110  O  OG1   . THR A 1 513 ? 147.788 161.833 101.433 1.00 25.68 ?  513 THR A OG1   1 
ATOM   4111  C  CG2   . THR A 1 513 ? 147.368 161.628 99.074  1.00 22.37 ?  513 THR A CG2   1 
ATOM   4112  N  N     . PHE A 1 514 ? 145.425 159.394 102.274 1.00 20.66 ?  514 PHE A N     1 
ATOM   4113  C  CA    . PHE A 1 514 ? 145.195 158.787 103.575 1.00 19.63 ?  514 PHE A CA    1 
ATOM   4114  C  C     . PHE A 1 514 ? 146.315 159.170 104.538 1.00 17.72 ?  514 PHE A C     1 
ATOM   4115  O  O     . PHE A 1 514 ? 147.432 159.508 104.137 1.00 23.22 ?  514 PHE A O     1 
ATOM   4116  C  CB    . PHE A 1 514 ? 145.066 157.266 103.455 1.00 7.37  ?  514 PHE A CB    1 
ATOM   4117  C  CG    . PHE A 1 514 ? 146.319 156.573 103.007 1.00 14.08 ?  514 PHE A CG    1 
ATOM   4118  C  CD1   . PHE A 1 514 ? 146.585 156.399 101.662 1.00 10.96 ?  514 PHE A CD1   1 
ATOM   4119  C  CD2   . PHE A 1 514 ? 147.221 156.075 103.933 1.00 14.22 ?  514 PHE A CD2   1 
ATOM   4120  C  CE1   . PHE A 1 514 ? 147.731 155.753 101.247 1.00 15.00 ?  514 PHE A CE1   1 
ATOM   4121  C  CE2   . PHE A 1 514 ? 148.370 155.430 103.523 1.00 8.99  ?  514 PHE A CE2   1 
ATOM   4122  C  CZ    . PHE A 1 514 ? 148.624 155.268 102.179 1.00 10.67 ?  514 PHE A CZ    1 
ATOM   4123  N  N     . ASP A 1 515 ? 145.995 159.129 105.829 1.00 26.78 ?  515 ASP A N     1 
ATOM   4124  C  CA    . ASP A 1 515 ? 146.932 159.590 106.844 1.00 17.30 ?  515 ASP A CA    1 
ATOM   4125  C  C     . ASP A 1 515 ? 148.210 158.765 106.815 1.00 21.11 ?  515 ASP A C     1 
ATOM   4126  O  O     . ASP A 1 515 ? 148.169 157.532 106.780 1.00 34.00 ?  515 ASP A O     1 
ATOM   4127  C  CB    . ASP A 1 515 ? 146.287 159.521 108.227 1.00 23.24 ?  515 ASP A CB    1 
ATOM   4128  C  CG    . ASP A 1 515 ? 145.539 160.788 108.584 1.00 30.03 ?  515 ASP A CG    1 
ATOM   4129  O  OD1   . ASP A 1 515 ? 145.058 161.475 107.659 1.00 28.63 ?  515 ASP A OD1   1 
ATOM   4130  O  OD2   . ASP A 1 515 ? 145.432 161.096 109.789 1.00 35.73 -1 515 ASP A OD2   1 
ATOM   4131  N  N     . GLN A 1 516 ? 149.349 159.453 106.838 1.00 22.04 ?  516 GLN A N     1 
ATOM   4132  C  CA    . GLN A 1 516 ? 150.660 158.812 106.773 1.00 20.91 ?  516 GLN A CA    1 
ATOM   4133  C  C     . GLN A 1 516 ? 150.890 158.133 105.427 1.00 22.78 ?  516 GLN A C     1 
ATOM   4134  O  O     . GLN A 1 516 ? 151.557 157.100 105.346 1.00 27.50 ?  516 GLN A O     1 
ATOM   4135  C  CB    . GLN A 1 516 ? 150.847 157.813 107.917 1.00 23.68 ?  516 GLN A CB    1 
ATOM   4136  C  CG    . GLN A 1 516 ? 150.856 158.452 109.294 1.00 18.67 ?  516 GLN A CG    1 
ATOM   4137  C  CD    . GLN A 1 516 ? 151.063 157.443 110.402 1.00 25.84 ?  516 GLN A CD    1 
ATOM   4138  O  OE1   . GLN A 1 516 ? 152.184 157.002 110.652 1.00 30.70 ?  516 GLN A OE1   1 
ATOM   4139  N  NE2   . GLN A 1 516 ? 149.980 157.070 111.074 1.00 25.68 ?  516 GLN A NE2   1 
ATOM   4140  N  N     . TYR A 1 517 ? 150.331 158.708 104.361 1.00 20.85 ?  517 TYR A N     1 
ATOM   4141  C  CA    . TYR A 1 517 ? 150.579 158.179 103.026 1.00 17.93 ?  517 TYR A CA    1 
ATOM   4142  C  C     . TYR A 1 517 ? 152.018 158.416 102.586 1.00 22.42 ?  517 TYR A C     1 
ATOM   4143  O  O     . TYR A 1 517 ? 152.571 157.618 101.822 1.00 28.71 ?  517 TYR A O     1 
ATOM   4144  C  CB    . TYR A 1 517 ? 149.613 158.807 102.020 1.00 12.73 ?  517 TYR A CB    1 
ATOM   4145  C  CG    . TYR A 1 517 ? 150.158 158.836 100.612 1.00 21.03 ?  517 TYR A CG    1 
ATOM   4146  C  CD1   . TYR A 1 517 ? 150.105 157.710 99.802  1.00 21.02 ?  517 TYR A CD1   1 
ATOM   4147  C  CD2   . TYR A 1 517 ? 150.742 159.984 100.098 1.00 20.49 ?  517 TYR A CD2   1 
ATOM   4148  C  CE1   . TYR A 1 517 ? 150.611 157.730 98.519  1.00 24.00 ?  517 TYR A CE1   1 
ATOM   4149  C  CE2   . TYR A 1 517 ? 151.250 160.014 98.818  1.00 17.91 ?  517 TYR A CE2   1 
ATOM   4150  C  CZ    . TYR A 1 517 ? 151.182 158.884 98.033  1.00 22.04 ?  517 TYR A CZ    1 
ATOM   4151  O  OH    . TYR A 1 517 ? 151.686 158.910 96.755  1.00 34.56 ?  517 TYR A OH    1 
ATOM   4152  N  N     . GLU A 1 518 ? 152.640 159.499 103.060 1.00 24.24 ?  518 GLU A N     1 
ATOM   4153  C  CA    . GLU A 1 518 ? 153.965 159.867 102.576 1.00 24.89 ?  518 GLU A CA    1 
ATOM   4154  C  C     . GLU A 1 518 ? 154.998 158.788 102.868 1.00 30.90 ?  518 GLU A C     1 
ATOM   4155  O  O     . GLU A 1 518 ? 155.929 158.591 102.079 1.00 34.36 ?  518 GLU A O     1 
ATOM   4156  C  CB    . GLU A 1 518 ? 154.396 161.196 103.198 1.00 25.13 ?  518 GLU A CB    1 
ATOM   4157  C  CG    . GLU A 1 518 ? 153.595 162.391 102.713 1.00 26.54 ?  518 GLU A CG    1 
ATOM   4158  C  CD    . GLU A 1 518 ? 153.660 162.564 101.210 1.00 37.43 ?  518 GLU A CD    1 
ATOM   4159  O  OE1   . GLU A 1 518 ? 154.677 162.161 100.606 1.00 38.33 ?  518 GLU A OE1   1 
ATOM   4160  O  OE2   . GLU A 1 518 ? 152.693 163.103 100.631 1.00 37.31 -1 518 GLU A OE2   1 
ATOM   4161  N  N     . GLY A 1 519 ? 154.862 158.087 103.989 1.00 16.61 ?  519 GLY A N     1 
ATOM   4162  C  CA    . GLY A 1 519 ? 155.775 157.018 104.326 1.00 12.28 ?  519 GLY A CA    1 
ATOM   4163  C  C     . GLY A 1 519 ? 155.444 155.669 103.732 1.00 19.56 ?  519 GLY A C     1 
ATOM   4164  O  O     . GLY A 1 519 ? 156.177 154.705 103.970 1.00 28.97 ?  519 GLY A O     1 
ATOM   4165  N  N     . SER A 1 520 ? 154.367 155.569 102.960 1.00 14.92 ?  520 SER A N     1 
ATOM   4166  C  CA    . SER A 1 520 ? 153.953 154.298 102.389 1.00 13.56 ?  520 SER A CA    1 
ATOM   4167  C  C     . SER A 1 520 ? 154.783 153.962 101.153 1.00 19.92 ?  520 SER A C     1 
ATOM   4168  O  O     . SER A 1 520 ? 155.468 154.811 100.579 1.00 26.87 ?  520 SER A O     1 
ATOM   4169  C  CB    . SER A 1 520 ? 152.467 154.330 102.027 1.00 13.57 ?  520 SER A CB    1 
ATOM   4170  O  OG    . SER A 1 520 ? 152.211 155.265 100.995 1.00 24.51 ?  520 SER A OG    1 
ATOM   4171  N  N     . THR A 1 521 ? 154.714 152.692 100.749 1.00 17.69 ?  521 THR A N     1 
ATOM   4172  C  CA    . THR A 1 521 ? 155.429 152.253 99.557  1.00 12.98 ?  521 THR A CA    1 
ATOM   4173  C  C     . THR A 1 521 ? 154.809 152.799 98.279  1.00 20.20 ?  521 THR A C     1 
ATOM   4174  O  O     . THR A 1 521 ? 155.476 152.816 97.241  1.00 18.42 ?  521 THR A O     1 
ATOM   4175  C  CB    . THR A 1 521 ? 155.481 150.725 99.504  1.00 19.62 ?  521 THR A CB    1 
ATOM   4176  O  OG1   . THR A 1 521 ? 154.178 150.209 99.209  1.00 27.93 ?  521 THR A OG1   1 
ATOM   4177  C  CG2   . THR A 1 521 ? 155.955 150.166 100.834 1.00 9.54  ?  521 THR A CG2   1 
ATOM   4178  N  N     . TYR A 1 522 ? 153.548 153.234 98.327  1.00 26.92 ?  522 TYR A N     1 
ATOM   4179  C  CA    . TYR A 1 522 ? 152.969 153.940 97.189  1.00 15.59 ?  522 TYR A CA    1 
ATOM   4180  C  C     . TYR A 1 522 ? 153.686 155.261 96.943  1.00 22.05 ?  522 TYR A C     1 
ATOM   4181  O  O     . TYR A 1 522 ? 153.971 155.619 95.794  1.00 22.74 ?  522 TYR A O     1 
ATOM   4182  C  CB    . TYR A 1 522 ? 151.478 154.185 97.417  1.00 11.46 ?  522 TYR A CB    1 
ATOM   4183  C  CG    . TYR A 1 522 ? 150.654 152.940 97.642  1.00 18.10 ?  522 TYR A CG    1 
ATOM   4184  C  CD1   . TYR A 1 522 ? 150.453 152.022 96.620  1.00 15.84 ?  522 TYR A CD1   1 
ATOM   4185  C  CD2   . TYR A 1 522 ? 150.065 152.689 98.873  1.00 22.57 ?  522 TYR A CD2   1 
ATOM   4186  C  CE1   . TYR A 1 522 ? 149.694 150.889 96.821  1.00 11.58 ?  522 TYR A CE1   1 
ATOM   4187  C  CE2   . TYR A 1 522 ? 149.308 151.558 99.083  1.00 12.10 ?  522 TYR A CE2   1 
ATOM   4188  C  CZ    . TYR A 1 522 ? 149.126 150.661 98.053  1.00 14.40 ?  522 TYR A CZ    1 
ATOM   4189  O  OH    . TYR A 1 522 ? 148.371 149.532 98.261  1.00 30.15 ?  522 TYR A OH    1 
ATOM   4190  N  N     . ALA A 1 523 ? 153.983 156.000 98.014  1.00 23.29 ?  523 ALA A N     1 
ATOM   4191  C  CA    . ALA A 1 523 ? 154.610 157.310 97.865  1.00 21.38 ?  523 ALA A CA    1 
ATOM   4192  C  C     . ALA A 1 523 ? 156.044 157.188 97.367  1.00 20.91 ?  523 ALA A C     1 
ATOM   4193  O  O     . ALA A 1 523 ? 156.473 157.957 96.499  1.00 25.20 ?  523 ALA A O     1 
ATOM   4194  C  CB    . ALA A 1 523 ? 154.566 158.065 99.193  1.00 18.74 ?  523 ALA A CB    1 
ATOM   4195  N  N     . THR A 1 524 ? 156.801 156.232 97.902  1.00 22.63 ?  524 THR A N     1 
ATOM   4196  C  CA    . THR A 1 524 ? 158.191 156.053 97.505  1.00 22.13 ?  524 THR A CA    1 
ATOM   4197  C  C     . THR A 1 524 ? 158.340 155.329 96.174  1.00 28.46 ?  524 THR A C     1 
ATOM   4198  O  O     . THR A 1 524 ? 159.446 155.301 95.626  1.00 37.22 ?  524 THR A O     1 
ATOM   4199  C  CB    . THR A 1 524 ? 158.957 155.287 98.588  1.00 21.56 ?  524 THR A CB    1 
ATOM   4200  O  OG1   . THR A 1 524 ? 158.548 153.915 98.589  1.00 29.78 ?  524 THR A OG1   1 
ATOM   4201  C  CG2   . THR A 1 524 ? 158.691 155.892 99.956  1.00 19.56 ?  524 THR A CG2   1 
ATOM   4202  N  N     . GLY A 1 525 ? 157.265 154.748 95.647  1.00 23.38 ?  525 GLY A N     1 
ATOM   4203  C  CA    . GLY A 1 525 ? 157.321 154.014 94.403  1.00 20.79 ?  525 GLY A CA    1 
ATOM   4204  C  C     . GLY A 1 525 ? 157.766 152.576 94.528  1.00 25.00 ?  525 GLY A C     1 
ATOM   4205  O  O     . GLY A 1 525 ? 157.749 151.850 93.527  1.00 25.58 ?  525 GLY A O     1 
ATOM   4206  N  N     . GLU A 1 526 ? 158.160 152.136 95.725  1.00 26.64 ?  526 GLU A N     1 
ATOM   4207  C  CA    . GLU A 1 526 ? 158.573 150.752 95.917  1.00 27.54 ?  526 GLU A CA    1 
ATOM   4208  C  C     . GLU A 1 526 ? 157.438 149.772 95.655  1.00 27.46 ?  526 GLU A C     1 
ATOM   4209  O  O     . GLU A 1 526 ? 157.697 148.592 95.398  1.00 32.80 ?  526 GLU A O     1 
ATOM   4210  C  CB    . GLU A 1 526 ? 159.116 150.567 97.335  1.00 27.09 ?  526 GLU A CB    1 
ATOM   4211  C  CG    . GLU A 1 526 ? 159.368 149.125 97.732  1.00 29.67 ?  526 GLU A CG    1 
ATOM   4212  C  CD    . GLU A 1 526 ? 159.592 148.966 99.221  1.00 33.09 ?  526 GLU A CD    1 
ATOM   4213  O  OE1   . GLU A 1 526 ? 159.872 149.983 99.891  1.00 36.03 ?  526 GLU A OE1   1 
ATOM   4214  O  OE2   . GLU A 1 526 ? 159.480 147.830 99.725  1.00 36.37 -1 526 GLU A OE2   1 
ATOM   4215  N  N     . TYR A 1 527 ? 156.188 150.235 95.714  1.00 26.45 ?  527 TYR A N     1 
ATOM   4216  C  CA    . TYR A 1 527 ? 155.054 149.358 95.445  1.00 20.57 ?  527 TYR A CA    1 
ATOM   4217  C  C     . TYR A 1 527 ? 155.023 148.914 93.987  1.00 23.44 ?  527 TYR A C     1 
ATOM   4218  O  O     . TYR A 1 527 ? 154.683 147.764 93.690  1.00 26.02 ?  527 TYR A O     1 
ATOM   4219  C  CB    . TYR A 1 527 ? 153.752 150.067 95.817  1.00 15.63 ?  527 TYR A CB    1 
ATOM   4220  C  CG    . TYR A 1 527 ? 152.512 149.244 95.575  1.00 24.05 ?  527 TYR A CG    1 
ATOM   4221  C  CD1   . TYR A 1 527 ? 152.022 148.391 96.553  1.00 21.38 ?  527 TYR A CD1   1 
ATOM   4222  C  CD2   . TYR A 1 527 ? 151.827 149.320 94.369  1.00 17.80 ?  527 TYR A CD2   1 
ATOM   4223  C  CE1   . TYR A 1 527 ? 150.889 147.637 96.338  1.00 17.90 ?  527 TYR A CE1   1 
ATOM   4224  C  CE2   . TYR A 1 527 ? 150.694 148.568 94.144  1.00 14.73 ?  527 TYR A CE2   1 
ATOM   4225  C  CZ    . TYR A 1 527 ? 150.229 147.728 95.132  1.00 14.13 ?  527 TYR A CZ    1 
ATOM   4226  O  OH    . TYR A 1 527 ? 149.099 146.978 94.915  1.00 25.61 ?  527 TYR A OH    1 
ATOM   4227  N  N     . PHE A 1 528 ? 155.378 149.808 93.069  1.00 25.91 ?  528 PHE A N     1 
ATOM   4228  C  CA    . PHE A 1 528 ? 155.220 149.580 91.640  1.00 23.96 ?  528 PHE A CA    1 
ATOM   4229  C  C     . PHE A 1 528 ? 156.427 148.909 90.998  1.00 31.53 ?  528 PHE A C     1 
ATOM   4230  O  O     . PHE A 1 528 ? 156.493 148.837 89.767  1.00 34.81 ?  528 PHE A O     1 
ATOM   4231  C  CB    . PHE A 1 528 ? 154.938 150.906 90.928  1.00 23.86 ?  528 PHE A CB    1 
ATOM   4232  C  CG    . PHE A 1 528 ? 153.742 151.636 91.459  1.00 26.63 ?  528 PHE A CG    1 
ATOM   4233  C  CD1   . PHE A 1 528 ? 152.488 151.421 90.916  1.00 25.04 ?  528 PHE A CD1   1 
ATOM   4234  C  CD2   . PHE A 1 528 ? 153.869 152.537 92.502  1.00 21.56 ?  528 PHE A CD2   1 
ATOM   4235  C  CE1   . PHE A 1 528 ? 151.385 152.090 91.401  1.00 21.86 ?  528 PHE A CE1   1 
ATOM   4236  C  CE2   . PHE A 1 528 ? 152.769 153.207 92.992  1.00 20.61 ?  528 PHE A CE2   1 
ATOM   4237  C  CZ    . PHE A 1 528 ? 151.526 152.985 92.441  1.00 22.71 ?  528 PHE A CZ    1 
ATOM   4238  N  N     . ASP A 1 529 ? 157.381 148.421 91.793  1.00 30.67 ?  529 ASP A N     1 
ATOM   4239  C  CA    . ASP A 1 529 ? 158.599 147.853 91.220  1.00 29.59 ?  529 ASP A CA    1 
ATOM   4240  C  C     . ASP A 1 529 ? 158.282 146.685 90.294  1.00 28.10 ?  529 ASP A C     1 
ATOM   4241  O  O     . ASP A 1 529 ? 158.715 146.660 89.135  1.00 35.43 ?  529 ASP A O     1 
ATOM   4242  C  CB    . ASP A 1 529 ? 159.542 147.413 92.340  1.00 30.14 ?  529 ASP A CB    1 
ATOM   4243  C  CG    . ASP A 1 529 ? 160.313 148.569 92.940  1.00 36.33 ?  529 ASP A CG    1 
ATOM   4244  O  OD1   . ASP A 1 529 ? 160.303 149.668 92.346  1.00 33.74 ?  529 ASP A OD1   1 
ATOM   4245  O  OD2   . ASP A 1 529 ? 160.930 148.381 94.010  1.00 41.24 -1 529 ASP A OD2   1 
ATOM   4246  N  N     . LYS A 1 530 ? 157.516 145.711 90.786  1.00 27.94 ?  530 LYS A N     1 
ATOM   4247  C  CA    . LYS A 1 530 ? 157.211 144.535 89.978  1.00 30.02 ?  530 LYS A CA    1 
ATOM   4248  C  C     . LYS A 1 530 ? 156.317 144.877 88.795  1.00 28.41 ?  530 LYS A C     1 
ATOM   4249  O  O     . LYS A 1 530 ? 156.424 144.249 87.738  1.00 32.28 ?  530 LYS A O     1 
ATOM   4250  C  CB    . LYS A 1 530 ? 156.560 143.458 90.843  1.00 27.67 ?  530 LYS A CB    1 
ATOM   4251  C  CG    . LYS A 1 530 ? 155.044 143.439 90.781  1.00 26.86 ?  530 LYS A CG    1 
ATOM   4252  C  CD    . LYS A 1 530 ? 154.474 142.431 91.760  1.00 29.21 ?  530 LYS A CD    1 
ATOM   4253  C  CE    . LYS A 1 530 ? 152.991 142.223 91.537  1.00 29.78 ?  530 LYS A CE    1 
ATOM   4254  N  NZ    . LYS A 1 530 ? 152.272 142.037 92.823  1.00 29.23 1  530 LYS A NZ    1 
ATOM   4255  N  N     . TYR A 1 531 ? 155.433 145.863 88.951  1.00 26.17 ?  531 TYR A N     1 
ATOM   4256  C  CA    . TYR A 1 531 ? 154.535 146.221 87.860  1.00 23.07 ?  531 TYR A CA    1 
ATOM   4257  C  C     . TYR A 1 531 ? 155.259 146.992 86.766  1.00 26.31 ?  531 TYR A C     1 
ATOM   4258  O  O     . TYR A 1 531 ? 154.921 146.855 85.585  1.00 34.31 ?  531 TYR A O     1 
ATOM   4259  C  CB    . TYR A 1 531 ? 153.359 147.030 88.399  1.00 23.75 ?  531 TYR A CB    1 
ATOM   4260  C  CG    . TYR A 1 531 ? 152.404 146.221 89.241  1.00 22.52 ?  531 TYR A CG    1 
ATOM   4261  C  CD1   . TYR A 1 531 ? 151.743 145.122 88.711  1.00 17.27 ?  531 TYR A CD1   1 
ATOM   4262  C  CD2   . TYR A 1 531 ? 152.157 146.560 90.564  1.00 15.45 ?  531 TYR A CD2   1 
ATOM   4263  C  CE1   . TYR A 1 531 ? 150.867 144.381 89.475  1.00 23.31 ?  531 TYR A CE1   1 
ATOM   4264  C  CE2   . TYR A 1 531 ? 151.283 145.824 91.335  1.00 20.76 ?  531 TYR A CE2   1 
ATOM   4265  C  CZ    . TYR A 1 531 ? 150.639 144.735 90.785  1.00 23.27 ?  531 TYR A CZ    1 
ATOM   4266  O  OH    . TYR A 1 531 ? 149.767 143.999 91.550  1.00 23.99 ?  531 TYR A OH    1 
ATOM   4267  N  N     . VAL A 1 532 ? 156.249 147.808 87.133  1.00 31.86 ?  532 VAL A N     1 
ATOM   4268  C  CA    . VAL A 1 532 ? 157.035 148.515 86.130  1.00 30.66 ?  532 VAL A CA    1 
ATOM   4269  C  C     . VAL A 1 532 ? 158.136 147.638 85.548  1.00 31.43 ?  532 VAL A C     1 
ATOM   4270  O  O     . VAL A 1 532 ? 158.669 147.958 84.478  1.00 35.11 ?  532 VAL A O     1 
ATOM   4271  C  CB    . VAL A 1 532 ? 157.649 149.800 86.712  1.00 29.95 ?  532 VAL A CB    1 
ATOM   4272  C  CG1   . VAL A 1 532 ? 156.555 150.768 87.135  1.00 26.39 ?  532 VAL A CG1   1 
ATOM   4273  C  CG2   . VAL A 1 532 ? 158.565 149.473 87.880  1.00 29.26 ?  532 VAL A CG2   1 
ATOM   4274  N  N     . SER A 1 533 ? 158.492 146.540 86.215  1.00 32.66 ?  533 SER A N     1 
ATOM   4275  C  CA    . SER A 1 533 ? 159.534 145.652 85.718  1.00 31.21 ?  533 SER A CA    1 
ATOM   4276  C  C     . SER A 1 533 ? 158.999 144.397 85.042  1.00 38.10 ?  533 SER A C     1 
ATOM   4277  O  O     . SER A 1 533 ? 159.704 143.815 84.212  1.00 41.83 ?  533 SER A O     1 
ATOM   4278  C  CB    . SER A 1 533 ? 160.470 145.240 86.860  1.00 35.09 ?  533 SER A CB    1 
ATOM   4279  O  OG    . SER A 1 533 ? 159.871 144.251 87.678  1.00 40.68 ?  533 SER A OG    1 
ATOM   4280  N  N     . THR A 1 534 ? 157.784 143.965 85.370  1.00 34.86 ?  534 THR A N     1 
ATOM   4281  C  CA    . THR A 1 534 ? 157.231 142.716 84.867  1.00 33.04 ?  534 THR A CA    1 
ATOM   4282  C  C     . THR A 1 534 ? 155.958 142.977 84.075  1.00 37.50 ?  534 THR A C     1 
ATOM   4283  O  O     . THR A 1 534 ? 155.156 143.844 84.435  1.00 40.26 ?  534 THR A O     1 
ATOM   4284  C  CB    . THR A 1 534 ? 156.929 141.743 86.014  1.00 35.08 ?  534 THR A CB    1 
ATOM   4285  O  OG1   . THR A 1 534 ? 158.068 141.651 86.878  1.00 39.42 ?  534 THR A OG1   1 
ATOM   4286  C  CG2   . THR A 1 534 ? 156.601 140.364 85.467  1.00 34.43 ?  534 THR A CG2   1 
ATOM   4287  N  N     . ASP A 1 535 ? 155.779 142.219 82.996  1.00 38.18 ?  535 ASP A N     1 
ATOM   4288  C  CA    . ASP A 1 535 ? 154.567 142.283 82.191  1.00 36.03 ?  535 ASP A CA    1 
ATOM   4289  C  C     . ASP A 1 535 ? 153.602 141.197 82.645  1.00 39.82 ?  535 ASP A C     1 
ATOM   4290  O  O     . ASP A 1 535 ? 153.979 140.025 82.748  1.00 42.09 ?  535 ASP A O     1 
ATOM   4291  C  CB    . ASP A 1 535 ? 154.892 142.117 80.706  1.00 39.26 ?  535 ASP A CB    1 
ATOM   4292  C  CG    . ASP A 1 535 ? 153.774 142.602 79.807  1.00 44.38 ?  535 ASP A CG    1 
ATOM   4293  O  OD1   . ASP A 1 535 ? 152.856 143.282 80.311  1.00 42.50 ?  535 ASP A OD1   1 
ATOM   4294  O  OD2   . ASP A 1 535 ? 153.810 142.301 78.596  1.00 44.53 -1 535 ASP A OD2   1 
ATOM   4295  N  N     . PHE A 1 536 ? 152.357 141.589 82.917  1.00 29.72 ?  536 PHE A N     1 
ATOM   4296  C  CA    . PHE A 1 536 ? 151.348 140.673 83.433  1.00 26.55 ?  536 PHE A CA    1 
ATOM   4297  C  C     . PHE A 1 536 ? 150.274 140.347 82.400  1.00 28.65 ?  536 PHE A C     1 
ATOM   4298  O  O     . PHE A 1 536 ? 149.166 139.946 82.769  1.00 30.93 ?  536 PHE A O     1 
ATOM   4299  C  CB    . PHE A 1 536 ? 150.716 141.246 84.701  1.00 28.50 ?  536 PHE A CB    1 
ATOM   4300  C  CG    . PHE A 1 536 ? 151.629 141.224 85.891  1.00 23.38 ?  536 PHE A CG    1 
ATOM   4301  C  CD1   . PHE A 1 536 ? 151.732 140.092 86.680  1.00 24.91 ?  536 PHE A CD1   1 
ATOM   4302  C  CD2   . PHE A 1 536 ? 152.394 142.330 86.215  1.00 24.14 ?  536 PHE A CD2   1 
ATOM   4303  C  CE1   . PHE A 1 536 ? 152.575 140.067 87.773  1.00 26.23 ?  536 PHE A CE1   1 
ATOM   4304  C  CE2   . PHE A 1 536 ? 153.240 142.309 87.307  1.00 29.84 ?  536 PHE A CE2   1 
ATOM   4305  C  CZ    . PHE A 1 536 ? 153.329 141.176 88.086  1.00 26.93 ?  536 PHE A CZ    1 
ATOM   4306  N  N     . SER A 1 537 ? 150.580 140.514 81.117  1.00 31.01 ?  537 SER A N     1 
ATOM   4307  C  CA    . SER A 1 537 ? 149.648 140.115 80.078  1.00 30.52 ?  537 SER A CA    1 
ATOM   4308  C  C     . SER A 1 537 ? 149.551 138.591 80.018  1.00 32.02 ?  537 SER A C     1 
ATOM   4309  O  O     . SER A 1 537 ? 150.498 137.886 80.377  1.00 37.06 ?  537 SER A O     1 
ATOM   4310  C  CB    . SER A 1 537 ? 150.088 140.661 78.723  1.00 31.32 ?  537 SER A CB    1 
ATOM   4311  O  OG    . SER A 1 537 ? 149.450 141.894 78.440  1.00 43.54 ?  537 SER A OG    1 
ATOM   4312  N  N     . PRO A 1 538 ? 148.416 138.058 79.569  1.00 30.40 ?  538 PRO A N     1 
ATOM   4313  C  CA    . PRO A 1 538 ? 148.261 136.600 79.525  1.00 33.09 ?  538 PRO A CA    1 
ATOM   4314  C  C     . PRO A 1 538 ? 149.325 135.953 78.652  1.00 38.13 ?  538 PRO A C     1 
ATOM   4315  O  O     . PRO A 1 538 ? 149.665 136.452 77.578  1.00 36.40 ?  538 PRO A O     1 
ATOM   4316  C  CB    . PRO A 1 538 ? 146.857 136.411 78.939  1.00 32.09 ?  538 PRO A CB    1 
ATOM   4317  C  CG    . PRO A 1 538 ? 146.156 137.705 79.199  1.00 31.18 ?  538 PRO A CG    1 
ATOM   4318  C  CD    . PRO A 1 538 ? 147.211 138.758 79.096  1.00 32.34 ?  538 PRO A CD    1 
ATOM   4319  N  N     . LYS A 1 539 ? 149.850 134.825 79.128  1.00 41.73 ?  539 LYS A N     1 
ATOM   4320  C  CA    . LYS A 1 539 ? 150.858 134.070 78.397  1.00 39.47 ?  539 LYS A CA    1 
ATOM   4321  C  C     . LYS A 1 539 ? 150.265 132.974 77.522  1.00 41.95 ?  539 LYS A C     1 
ATOM   4322  O  O     . LYS A 1 539 ? 151.003 132.357 76.745  1.00 44.96 ?  539 LYS A O     1 
ATOM   4323  C  CB    . LYS A 1 539 ? 151.868 133.456 79.371  1.00 40.52 ?  539 LYS A CB    1 
ATOM   4324  C  CG    . LYS A 1 539 ? 153.088 134.326 79.610  1.00 41.16 ?  539 LYS A CG    1 
ATOM   4325  C  CD    . LYS A 1 539 ? 153.545 134.260 81.056  1.00 40.56 ?  539 LYS A CD    1 
ATOM   4326  C  CE    . LYS A 1 539 ? 154.432 135.444 81.397  1.00 43.89 ?  539 LYS A CE    1 
ATOM   4327  N  NZ    . LYS A 1 539 ? 153.702 136.737 81.276  1.00 43.08 1  539 LYS A NZ    1 
ATOM   4328  N  N     . TYR A 1 540 ? 148.965 132.718 77.626  1.00 39.62 ?  540 TYR A N     1 
ATOM   4329  C  CA    . TYR A 1 540 ? 148.283 131.735 76.799  1.00 37.96 ?  540 TYR A CA    1 
ATOM   4330  C  C     . TYR A 1 540 ? 147.353 132.445 75.827  1.00 42.02 ?  540 TYR A C     1 
ATOM   4331  O  O     . TYR A 1 540 ? 146.696 133.427 76.187  1.00 46.43 ?  540 TYR A O     1 
ATOM   4332  C  CB    . TYR A 1 540 ? 147.489 130.746 77.654  1.00 37.93 ?  540 TYR A CB    1 
ATOM   4333  C  CG    . TYR A 1 540 ? 148.345 129.898 78.565  1.00 41.62 ?  540 TYR A CG    1 
ATOM   4334  C  CD1   . TYR A 1 540 ? 148.679 130.334 79.840  1.00 41.00 ?  540 TYR A CD1   1 
ATOM   4335  C  CD2   . TYR A 1 540 ? 148.824 128.664 78.149  1.00 40.53 ?  540 TYR A CD2   1 
ATOM   4336  C  CE1   . TYR A 1 540 ? 149.463 129.563 80.675  1.00 40.30 ?  540 TYR A CE1   1 
ATOM   4337  C  CE2   . TYR A 1 540 ? 149.607 127.886 78.976  1.00 38.00 ?  540 TYR A CE2   1 
ATOM   4338  C  CZ    . TYR A 1 540 ? 149.924 128.340 80.239  1.00 41.90 ?  540 TYR A CZ    1 
ATOM   4339  O  OH    . TYR A 1 540 ? 150.705 127.568 81.067  1.00 44.18 ?  540 TYR A OH    1 
ATOM   4340  N  N     . GLU A 1 541 ? 147.304 131.948 74.590  1.00 44.74 ?  541 GLU A N     1 
ATOM   4341  C  CA    . GLU A 1 541 ? 146.428 132.550 73.592  1.00 41.66 ?  541 GLU A CA    1 
ATOM   4342  C  C     . GLU A 1 541 ? 144.968 132.455 74.015  1.00 41.02 ?  541 GLU A C     1 
ATOM   4343  O  O     . GLU A 1 541 ? 144.191 133.394 73.810  1.00 41.08 ?  541 GLU A O     1 
ATOM   4344  C  CB    . GLU A 1 541 ? 146.640 131.883 72.233  1.00 44.47 ?  541 GLU A CB    1 
ATOM   4345  C  CG    . GLU A 1 541 ? 146.239 132.750 71.053  1.00 43.34 ?  541 GLU A CG    1 
ATOM   4346  C  CD    . GLU A 1 541 ? 146.585 134.211 71.262  1.00 49.38 ?  541 GLU A CD    1 
ATOM   4347  O  OE1   . GLU A 1 541 ? 147.740 134.502 71.639  1.00 47.30 ?  541 GLU A OE1   1 
ATOM   4348  O  OE2   . GLU A 1 541 ? 145.702 135.069 71.050  1.00 52.24 -1 541 GLU A OE2   1 
ATOM   4349  N  N     . LYS A 1 542 ? 144.576 131.324 74.607  1.00 40.50 ?  542 LYS A N     1 
ATOM   4350  C  CA    . LYS A 1 542 ? 143.200 131.174 75.066  1.00 37.99 ?  542 LYS A CA    1 
ATOM   4351  C  C     . LYS A 1 542 ? 142.851 132.222 76.116  1.00 39.01 ?  542 LYS A C     1 
ATOM   4352  O  O     . LYS A 1 542 ? 141.768 132.816 76.074  1.00 39.17 ?  542 LYS A O     1 
ATOM   4353  C  CB    . LYS A 1 542 ? 142.982 129.767 75.622  1.00 38.81 ?  542 LYS A CB    1 
ATOM   4354  C  CG    . LYS A 1 542 ? 141.592 129.539 76.188  1.00 40.89 ?  542 LYS A CG    1 
ATOM   4355  C  CD    . LYS A 1 542 ? 141.378 128.085 76.571  1.00 37.30 ?  542 LYS A CD    1 
ATOM   4356  C  CE    . LYS A 1 542 ? 139.976 127.863 77.113  1.00 39.48 ?  542 LYS A CE    1 
ATOM   4357  N  NZ    . LYS A 1 542 ? 139.696 126.423 77.361  1.00 39.92 1  542 LYS A NZ    1 
ATOM   4358  N  N     . ILE A 1 543 ? 143.756 132.459 77.067  1.00 36.30 ?  543 ILE A N     1 
ATOM   4359  C  CA    . ILE A 1 543 ? 143.504 133.469 78.088  1.00 33.83 ?  543 ILE A CA    1 
ATOM   4360  C  C     . ILE A 1 543 ? 143.565 134.866 77.485  1.00 30.83 ?  543 ILE A C     1 
ATOM   4361  O  O     . ILE A 1 543 ? 142.732 135.726 77.792  1.00 34.63 ?  543 ILE A O     1 
ATOM   4362  C  CB    . ILE A 1 543 ? 144.495 133.309 79.254  1.00 31.87 ?  543 ILE A CB    1 
ATOM   4363  C  CG1   . ILE A 1 543 ? 144.338 131.932 79.898  1.00 35.39 ?  543 ILE A CG1   1 
ATOM   4364  C  CG2   . ILE A 1 543 ? 144.291 134.410 80.280  1.00 31.48 ?  543 ILE A CG2   1 
ATOM   4365  C  CD1   . ILE A 1 543 ? 142.909 131.578 80.243  1.00 31.57 ?  543 ILE A CD1   1 
ATOM   4366  N  N     . ALA A 1 544 ? 144.551 135.118 76.620  1.00 33.09 ?  544 ALA A N     1 
ATOM   4367  C  CA    . ALA A 1 544 ? 144.664 136.431 75.995  1.00 37.65 ?  544 ALA A CA    1 
ATOM   4368  C  C     . ALA A 1 544 ? 143.422 136.775 75.186  1.00 39.42 ?  544 ALA A C     1 
ATOM   4369  O  O     . ALA A 1 544 ? 143.075 137.953 75.052  1.00 40.99 ?  544 ALA A O     1 
ATOM   4370  C  CB    . ALA A 1 544 ? 145.909 136.487 75.109  1.00 35.91 ?  544 ALA A CB    1 
ATOM   4371  N  N     . ASN A 1 545 ? 142.743 135.765 74.638  1.00 43.05 ?  545 ASN A N     1 
ATOM   4372  C  CA    . ASN A 1 545 ? 141.526 136.020 73.878  1.00 41.41 ?  545 ASN A CA    1 
ATOM   4373  C  C     . ASN A 1 545 ? 140.374 136.434 74.783  1.00 40.66 ?  545 ASN A C     1 
ATOM   4374  O  O     . ASN A 1 545 ? 139.520 137.227 74.373  1.00 43.34 ?  545 ASN A O     1 
ATOM   4375  C  CB    . ASN A 1 545 ? 141.147 134.783 73.065  1.00 42.14 ?  545 ASN A CB    1 
ATOM   4376  C  CG    . ASN A 1 545 ? 141.862 134.724 71.732  1.00 45.30 ?  545 ASN A CG    1 
ATOM   4377  O  OD1   . ASN A 1 545 ? 142.151 135.755 71.125  1.00 45.27 ?  545 ASN A OD1   1 
ATOM   4378  N  ND2   . ASN A 1 545 ? 142.154 133.514 71.269  1.00 43.65 ?  545 ASN A ND2   1 
ATOM   4379  N  N     . LEU A 1 546 ? 140.330 135.910 76.010  1.00 36.33 ?  546 LEU A N     1 
ATOM   4380  C  CA    . LEU A 1 546 ? 139.278 136.299 76.942  1.00 35.08 ?  546 LEU A CA    1 
ATOM   4381  C  C     . LEU A 1 546 ? 139.322 137.790 77.243  1.00 36.30 ?  546 LEU A C     1 
ATOM   4382  O  O     . LEU A 1 546 ? 138.282 138.401 77.510  1.00 42.81 ?  546 LEU A O     1 
ATOM   4383  C  CB    . LEU A 1 546 ? 139.400 135.495 78.236  1.00 37.78 ?  546 LEU A CB    1 
ATOM   4384  C  CG    . LEU A 1 546 ? 139.230 133.981 78.115  1.00 35.08 ?  546 LEU A CG    1 
ATOM   4385  C  CD1   . LEU A 1 546 ? 139.450 133.315 79.462  1.00 32.85 ?  546 LEU A CD1   1 
ATOM   4386  C  CD2   . LEU A 1 546 ? 137.860 133.636 77.559  1.00 33.23 ?  546 LEU A CD2   1 
ATOM   4387  N  N     . PHE A 1 547 ? 140.508 138.391 77.203  1.00 35.63 ?  547 PHE A N     1 
ATOM   4388  C  CA    . PHE A 1 547 ? 140.678 139.812 77.462  1.00 34.26 ?  547 PHE A CA    1 
ATOM   4389  C  C     . PHE A 1 547 ? 140.582 140.656 76.199  1.00 34.34 ?  547 PHE A C     1 
ATOM   4390  O  O     . PHE A 1 547 ? 140.796 141.871 76.263  1.00 41.84 ?  547 PHE A O     1 
ATOM   4391  C  CB    . PHE A 1 547 ? 142.019 140.065 78.157  1.00 35.24 ?  547 PHE A CB    1 
ATOM   4392  C  CG    . PHE A 1 547 ? 142.077 139.545 79.565  1.00 36.31 ?  547 PHE A CG    1 
ATOM   4393  C  CD1   . PHE A 1 547 ? 141.593 140.302 80.617  1.00 33.10 ?  547 PHE A CD1   1 
ATOM   4394  C  CD2   . PHE A 1 547 ? 142.610 138.297 79.834  1.00 30.43 ?  547 PHE A CD2   1 
ATOM   4395  C  CE1   . PHE A 1 547 ? 141.643 139.826 81.912  1.00 30.24 ?  547 PHE A CE1   1 
ATOM   4396  C  CE2   . PHE A 1 547 ? 142.662 137.816 81.127  1.00 31.27 ?  547 PHE A CE2   1 
ATOM   4397  C  CZ    . PHE A 1 547 ? 142.179 138.582 82.167  1.00 32.67 ?  547 PHE A CZ    1 
ATOM   4398  N  N     . GLU A 1 548 ? 140.273 140.046 75.056  1.00 43.06 ?  548 GLU A N     1 
ATOM   4399  C  CA    . GLU A 1 548 ? 140.115 140.809 73.826  1.00 43.82 ?  548 GLU A CA    1 
ATOM   4400  C  C     . GLU A 1 548 ? 139.004 141.839 73.985  1.00 46.10 ?  548 GLU A C     1 
ATOM   4401  O  O     . GLU A 1 548 ? 137.955 141.561 74.572  1.00 49.14 ?  548 GLU A O     1 
ATOM   4402  C  CB    . GLU A 1 548 ? 139.807 139.876 72.654  1.00 45.60 ?  548 GLU A CB    1 
ATOM   4403  C  CG    . GLU A 1 548 ? 139.786 140.549 71.283  1.00 45.56 ?  548 GLU A CG    1 
ATOM   4404  C  CD    . GLU A 1 548 ? 141.003 141.423 71.009  1.00 48.72 ?  548 GLU A CD    1 
ATOM   4405  O  OE1   . GLU A 1 548 ? 141.861 141.577 71.903  1.00 46.81 ?  548 GLU A OE1   1 
ATOM   4406  O  OE2   . GLU A 1 548 ? 141.097 141.962 69.886  1.00 51.28 -1 548 GLU A OE2   1 
ATOM   4407  N  N     . GLY A 1 549 ? 139.242 143.037 73.456  1.00 42.07 ?  549 GLY A N     1 
ATOM   4408  C  CA    . GLY A 1 549 ? 138.349 144.156 73.654  1.00 37.87 ?  549 GLY A CA    1 
ATOM   4409  C  C     . GLY A 1 549 ? 138.614 144.952 74.911  1.00 40.82 ?  549 GLY A C     1 
ATOM   4410  O  O     . GLY A 1 549 ? 137.969 145.988 75.117  1.00 44.34 ?  549 GLY A O     1 
ATOM   4411  N  N     . MET A 1 550 ? 139.539 144.504 75.754  1.00 42.38 ?  550 MET A N     1 
ATOM   4412  C  CA    . MET A 1 550 ? 139.929 145.202 76.968  1.00 38.69 ?  550 MET A CA    1 
ATOM   4413  C  C     . MET A 1 550 ? 141.413 145.525 76.899  1.00 39.92 ?  550 MET A C     1 
ATOM   4414  O  O     . MET A 1 550 ? 142.216 144.700 76.449  1.00 42.16 ?  550 MET A O     1 
ATOM   4415  C  CB    . MET A 1 550 ? 139.634 144.357 78.214  1.00 34.47 ?  550 MET A CB    1 
ATOM   4416  C  CG    . MET A 1 550 ? 138.442 144.834 79.026  1.00 40.49 ?  550 MET A CG    1 
ATOM   4417  S  SD    . MET A 1 550 ? 138.145 143.823 80.489  1.00 49.34 ?  550 MET A SD    1 
ATOM   4418  C  CE    . MET A 1 550 ? 138.090 142.184 79.769  1.00 41.03 ?  550 MET A CE    1 
ATOM   4419  N  N     . HIS A 1 551 ? 141.776 146.724 77.339  1.00 37.35 ?  551 HIS A N     1 
ATOM   4420  C  CA    . HIS A 1 551 ? 143.174 147.133 77.346  1.00 32.69 ?  551 HIS A CA    1 
ATOM   4421  C  C     . HIS A 1 551 ? 143.852 146.597 78.601  1.00 36.52 ?  551 HIS A C     1 
ATOM   4422  O  O     . HIS A 1 551 ? 143.464 146.946 79.721  1.00 37.67 ?  551 HIS A O     1 
ATOM   4423  C  CB    . HIS A 1 551 ? 143.289 148.653 77.278  1.00 36.67 ?  551 HIS A CB    1 
ATOM   4424  C  CG    . HIS A 1 551 ? 144.683 149.160 77.471  1.00 39.24 ?  551 HIS A CG    1 
ATOM   4425  N  ND1   . HIS A 1 551 ? 145.686 148.948 76.550  1.00 37.67 ?  551 HIS A ND1   1 
ATOM   4426  C  CD2   . HIS A 1 551 ? 145.244 149.866 78.482  1.00 40.22 ?  551 HIS A CD2   1 
ATOM   4427  C  CE1   . HIS A 1 551 ? 146.804 149.503 76.983  1.00 40.74 ?  551 HIS A CE1   1 
ATOM   4428  N  NE2   . HIS A 1 551 ? 146.563 150.066 78.153  1.00 42.59 ?  551 HIS A NE2   1 
ATOM   4429  N  N     . ILE A 1 552 ? 144.858 145.750 78.415  1.00 33.92 ?  552 ILE A N     1 
ATOM   4430  C  CA    . ILE A 1 552 ? 145.618 145.180 79.523  1.00 30.56 ?  552 ILE A CA    1 
ATOM   4431  C  C     . ILE A 1 552 ? 146.788 146.116 79.816  1.00 30.98 ?  552 ILE A C     1 
ATOM   4432  O  O     . ILE A 1 552 ? 147.625 146.334 78.927  1.00 37.94 ?  552 ILE A O     1 
ATOM   4433  C  CB    . ILE A 1 552 ? 146.114 143.767 79.199  1.00 33.70 ?  552 ILE A CB    1 
ATOM   4434  C  CG1   . ILE A 1 552 ? 144.946 142.883 78.757  1.00 31.69 ?  552 ILE A CG1   1 
ATOM   4435  C  CG2   . ILE A 1 552 ? 146.821 143.162 80.403  1.00 30.72 ?  552 ILE A CG2   1 
ATOM   4436  C  CD1   . ILE A 1 552 ? 145.356 141.491 78.346  1.00 31.52 ?  552 ILE A CD1   1 
ATOM   4437  N  N     . PRO A 1 553 ? 146.880 146.683 81.017  1.00 36.41 ?  553 PRO A N     1 
ATOM   4438  C  CA    . PRO A 1 553 ? 147.973 147.618 81.304  1.00 32.19 ?  553 PRO A CA    1 
ATOM   4439  C  C     . PRO A 1 553 ? 149.332 146.966 81.103  1.00 31.07 ?  553 PRO A C     1 
ATOM   4440  O  O     . PRO A 1 553 ? 149.542 145.801 81.444  1.00 33.31 ?  553 PRO A O     1 
ATOM   4441  C  CB    . PRO A 1 553 ? 147.740 147.994 82.770  1.00 28.23 ?  553 PRO A CB    1 
ATOM   4442  C  CG    . PRO A 1 553 ? 146.284 147.767 82.987  1.00 25.80 ?  553 PRO A CG    1 
ATOM   4443  C  CD    . PRO A 1 553 ? 145.931 146.581 82.138  1.00 32.22 ?  553 PRO A CD    1 
ATOM   4444  N  N     . THR A 1 554 ? 150.258 147.736 80.543  1.00 37.00 ?  554 THR A N     1 
ATOM   4445  C  CA    . THR A 1 554 ? 151.620 147.287 80.317  1.00 34.57 ?  554 THR A CA    1 
ATOM   4446  C  C     . THR A 1 554 ? 152.550 147.918 81.348  1.00 27.83 ?  554 THR A C     1 
ATOM   4447  O  O     . THR A 1 554 ? 152.124 148.634 82.257  1.00 29.94 ?  554 THR A O     1 
ATOM   4448  C  CB    . THR A 1 554 ? 152.072 147.626 78.894  1.00 29.67 ?  554 THR A CB    1 
ATOM   4449  O  OG1   . THR A 1 554 ? 152.170 149.047 78.747  1.00 33.54 ?  554 THR A OG1   1 
ATOM   4450  C  CG2   . THR A 1 554 ? 151.082 147.083 77.878  1.00 29.42 ?  554 THR A CG2   1 
ATOM   4451  N  N     . THR A 1 555 ? 153.847 147.642 81.203  1.00 33.36 ?  555 THR A N     1 
ATOM   4452  C  CA    . THR A 1 555 ? 154.827 148.271 82.081  1.00 30.19 ?  555 THR A CA    1 
ATOM   4453  C  C     . THR A 1 555 ? 154.840 149.782 81.904  1.00 30.46 ?  555 THR A C     1 
ATOM   4454  O  O     . THR A 1 555 ? 155.070 150.516 82.870  1.00 30.85 ?  555 THR A O     1 
ATOM   4455  C  CB    . THR A 1 555 ? 156.219 147.692 81.827  1.00 33.15 ?  555 THR A CB    1 
ATOM   4456  O  OG1   . THR A 1 555 ? 156.508 147.731 80.424  1.00 38.14 ?  555 THR A OG1   1 
ATOM   4457  C  CG2   . THR A 1 555 ? 156.295 146.254 82.319  1.00 29.63 ?  555 THR A CG2   1 
ATOM   4458  N  N     . GLU A 1 556 ? 154.603 150.267 80.683  1.00 32.60 ?  556 GLU A N     1 
ATOM   4459  C  CA    . GLU A 1 556 ? 154.505 151.708 80.466  1.00 27.27 ?  556 GLU A CA    1 
ATOM   4460  C  C     . GLU A 1 556 ? 153.283 152.291 81.167  1.00 30.19 ?  556 GLU A C     1 
ATOM   4461  O  O     . GLU A 1 556 ? 153.359 153.372 81.763  1.00 33.86 ?  556 GLU A O     1 
ATOM   4462  C  CB    . GLU A 1 556 ? 154.463 152.009 78.968  1.00 32.88 ?  556 GLU A CB    1 
ATOM   4463  C  CG    . GLU A 1 556 ? 154.682 153.472 78.621  1.00 32.99 ?  556 GLU A CG    1 
ATOM   4464  C  CD    . GLU A 1 556 ? 155.772 154.114 79.459  1.00 40.00 ?  556 GLU A CD    1 
ATOM   4465  O  OE1   . GLU A 1 556 ? 155.477 155.107 80.156  1.00 37.66 ?  556 GLU A OE1   1 
ATOM   4466  O  OE2   . GLU A 1 556 ? 156.921 153.626 79.419  1.00 41.27 -1 556 GLU A OE2   1 
ATOM   4467  N  N     . ASP A 1 557 ? 152.149 151.590 81.105  1.00 32.95 ?  557 ASP A N     1 
ATOM   4468  C  CA    . ASP A 1 557 ? 150.960 152.051 81.813  1.00 27.38 ?  557 ASP A CA    1 
ATOM   4469  C  C     . ASP A 1 557 ? 151.197 152.080 83.316  1.00 28.61 ?  557 ASP A C     1 
ATOM   4470  O  O     . ASP A 1 557 ? 150.766 153.012 84.003  1.00 32.50 ?  557 ASP A O     1 
ATOM   4471  C  CB    . ASP A 1 557 ? 149.765 151.160 81.475  1.00 30.45 ?  557 ASP A CB    1 
ATOM   4472  C  CG    . ASP A 1 557 ? 149.403 151.204 80.006  1.00 36.09 ?  557 ASP A CG    1 
ATOM   4473  O  OD1   . ASP A 1 557 ? 149.382 152.312 79.431  1.00 37.91 ?  557 ASP A OD1   1 
ATOM   4474  O  OD2   . ASP A 1 557 ? 149.137 150.131 79.425  1.00 37.91 -1 557 ASP A OD2   1 
ATOM   4475  N  N     . TRP A 1 558 ? 151.881 151.066 83.846  1.00 24.42 ?  558 TRP A N     1 
ATOM   4476  C  CA    . TRP A 1 558 ? 152.188 151.059 85.270  1.00 21.42 ?  558 TRP A CA    1 
ATOM   4477  C  C     . TRP A 1 558 ? 153.176 152.158 85.638  1.00 29.67 ?  558 TRP A C     1 
ATOM   4478  O  O     . TRP A 1 558 ? 153.082 152.727 86.727  1.00 30.80 ?  558 TRP A O     1 
ATOM   4479  C  CB    . TRP A 1 558 ? 152.723 149.693 85.686  1.00 19.36 ?  558 TRP A CB    1 
ATOM   4480  C  CG    . TRP A 1 558 ? 151.648 148.683 85.941  1.00 21.76 ?  558 TRP A CG    1 
ATOM   4481  C  CD1   . TRP A 1 558 ? 151.253 147.682 85.105  1.00 21.95 ?  558 TRP A CD1   1 
ATOM   4482  C  CD2   . TRP A 1 558 ? 150.830 148.572 87.114  1.00 18.35 ?  558 TRP A CD2   1 
ATOM   4483  N  NE1   . TRP A 1 558 ? 150.243 146.954 85.682  1.00 25.03 ?  558 TRP A NE1   1 
ATOM   4484  C  CE2   . TRP A 1 558 ? 149.965 147.480 86.917  1.00 20.33 ?  558 TRP A CE2   1 
ATOM   4485  C  CE3   . TRP A 1 558 ? 150.749 149.288 88.311  1.00 23.54 ?  558 TRP A CE3   1 
ATOM   4486  C  CZ2   . TRP A 1 558 ? 149.029 147.087 87.870  1.00 16.43 ?  558 TRP A CZ2   1 
ATOM   4487  C  CZ3   . TRP A 1 558 ? 149.818 148.898 89.256  1.00 17.21 ?  558 TRP A CZ3   1 
ATOM   4488  C  CH2   . TRP A 1 558 ? 148.971 147.808 89.030  1.00 10.44 ?  558 TRP A CH2   1 
ATOM   4489  N  N     . LYS A 1 559 ? 154.123 152.474 84.753  1.00 31.65 ?  559 LYS A N     1 
ATOM   4490  C  CA    . LYS A 1 559 ? 155.015 153.603 85.001  1.00 27.07 ?  559 LYS A CA    1 
ATOM   4491  C  C     . LYS A 1 559 ? 154.235 154.910 85.057  1.00 27.97 ?  559 LYS A C     1 
ATOM   4492  O  O     . LYS A 1 559 ? 154.474 155.754 85.931  1.00 32.21 ?  559 LYS A O     1 
ATOM   4493  C  CB    . LYS A 1 559 ? 156.089 153.672 83.916  1.00 28.23 ?  559 LYS A CB    1 
ATOM   4494  C  CG    . LYS A 1 559 ? 157.320 152.832 84.197  1.00 28.41 ?  559 LYS A CG    1 
ATOM   4495  C  CD    . LYS A 1 559 ? 158.110 152.580 82.923  1.00 30.82 ?  559 LYS A CD    1 
ATOM   4496  C  CE    . LYS A 1 559 ? 158.522 151.122 82.801  1.00 30.92 ?  559 LYS A CE    1 
ATOM   4497  N  NZ    . LYS A 1 559 ? 159.807 150.847 83.501  1.00 34.07 1  559 LYS A NZ    1 
ATOM   4498  N  N     . LYS A 1 560 ? 153.296 155.092 84.127  1.00 28.19 ?  560 LYS A N     1 
ATOM   4499  C  CA    . LYS A 1 560 ? 152.463 156.290 84.142  1.00 23.26 ?  560 LYS A CA    1 
ATOM   4500  C  C     . LYS A 1 560 ? 151.634 156.364 85.418  1.00 30.49 ?  560 LYS A C     1 
ATOM   4501  O  O     . LYS A 1 560 ? 151.501 157.435 86.019  1.00 34.68 ?  560 LYS A O     1 
ATOM   4502  C  CB    . LYS A 1 560 ? 151.559 156.318 82.911  1.00 28.33 ?  560 LYS A CB    1 
ATOM   4503  C  CG    . LYS A 1 560 ? 152.286 156.082 81.600  1.00 34.39 ?  560 LYS A CG    1 
ATOM   4504  C  CD    . LYS A 1 560 ? 152.389 157.361 80.789  1.00 35.43 ?  560 LYS A CD    1 
ATOM   4505  C  CE    . LYS A 1 560 ? 152.455 157.059 79.303  1.00 34.68 ?  560 LYS A CE    1 
ATOM   4506  N  NZ    . LYS A 1 560 ? 151.497 155.990 78.912  1.00 34.77 1  560 LYS A NZ    1 
ATOM   4507  N  N     . LEU A 1 561 ? 151.060 155.236 85.842  1.00 32.14 ?  561 LEU A N     1 
ATOM   4508  C  CA    . LEU A 1 561 ? 150.277 155.223 87.072  1.00 25.21 ?  561 LEU A CA    1 
ATOM   4509  C  C     . LEU A 1 561 ? 151.150 155.513 88.286  1.00 26.06 ?  561 LEU A C     1 
ATOM   4510  O  O     . LEU A 1 561 ? 150.715 156.194 89.221  1.00 30.96 ?  561 LEU A O     1 
ATOM   4511  C  CB    . LEU A 1 561 ? 149.563 153.882 87.232  1.00 24.45 ?  561 LEU A CB    1 
ATOM   4512  C  CG    . LEU A 1 561 ? 148.770 153.711 88.531  1.00 24.63 ?  561 LEU A CG    1 
ATOM   4513  C  CD1   . LEU A 1 561 ? 147.674 154.761 88.630  1.00 25.61 ?  561 LEU A CD1   1 
ATOM   4514  C  CD2   . LEU A 1 561 ? 148.187 152.314 88.631  1.00 19.48 ?  561 LEU A CD2   1 
ATOM   4515  N  N     . LYS A 1 562 ? 152.376 154.991 88.298  1.00 24.34 ?  562 LYS A N     1 
ATOM   4516  C  CA    . LYS A 1 562 ? 153.304 155.275 89.386  1.00 29.12 ?  562 LYS A CA    1 
ATOM   4517  C  C     . LYS A 1 562 ? 153.616 156.763 89.462  1.00 29.38 ?  562 LYS A C     1 
ATOM   4518  O  O     . LYS A 1 562 ? 153.613 157.359 90.546  1.00 31.79 ?  562 LYS A O     1 
ATOM   4519  C  CB    . LYS A 1 562 ? 154.581 154.457 89.189  1.00 27.82 ?  562 LYS A CB    1 
ATOM   4520  C  CG    . LYS A 1 562 ? 155.713 154.786 90.139  1.00 24.32 ?  562 LYS A CG    1 
ATOM   4521  C  CD    . LYS A 1 562 ? 156.950 153.982 89.778  1.00 24.94 ?  562 LYS A CD    1 
ATOM   4522  C  CE    . LYS A 1 562 ? 158.093 154.246 90.737  1.00 28.29 ?  562 LYS A CE    1 
ATOM   4523  N  NZ    . LYS A 1 562 ? 159.118 153.172 90.670  1.00 33.18 1  562 LYS A NZ    1 
ATOM   4524  N  N     . ALA A 1 563 ? 153.882 157.385 88.311  1.00 29.64 ?  563 ALA A N     1 
ATOM   4525  C  CA    . ALA A 1 563 ? 154.129 158.824 88.293  1.00 27.02 ?  563 ALA A CA    1 
ATOM   4526  C  C     . ALA A 1 563 ? 152.900 159.599 88.754  1.00 23.40 ?  563 ALA A C     1 
ATOM   4527  O  O     . ALA A 1 563 ? 153.014 160.572 89.508  1.00 37.33 ?  563 ALA A O     1 
ATOM   4528  C  CB    . ALA A 1 563 ? 154.553 159.266 86.893  1.00 30.13 ?  563 ALA A CB    1 
ATOM   4529  N  N     . PHE A 1 564 ? 151.715 159.177 88.311  1.00 28.06 ?  564 PHE A N     1 
ATOM   4530  C  CA    . PHE A 1 564 ? 150.484 159.850 88.713  1.00 27.54 ?  564 PHE A CA    1 
ATOM   4531  C  C     . PHE A 1 564 ? 150.272 159.757 90.220  1.00 29.61 ?  564 PHE A C     1 
ATOM   4532  O  O     . PHE A 1 564 ? 149.877 160.738 90.861  1.00 30.43 ?  564 PHE A O     1 
ATOM   4533  C  CB    . PHE A 1 564 ? 149.302 159.246 87.957  1.00 25.25 ?  564 PHE A CB    1 
ATOM   4534  C  CG    . PHE A 1 564 ? 147.994 159.930 88.221  1.00 26.14 ?  564 PHE A CG    1 
ATOM   4535  C  CD1   . PHE A 1 564 ? 147.647 161.080 87.534  1.00 24.82 ?  564 PHE A CD1   1 
ATOM   4536  C  CD2   . PHE A 1 564 ? 147.106 159.417 89.148  1.00 28.58 ?  564 PHE A CD2   1 
ATOM   4537  C  CE1   . PHE A 1 564 ? 146.442 161.707 87.774  1.00 29.91 ?  564 PHE A CE1   1 
ATOM   4538  C  CE2   . PHE A 1 564 ? 145.901 160.040 89.391  1.00 30.30 ?  564 PHE A CE2   1 
ATOM   4539  C  CZ    . PHE A 1 564 ? 145.568 161.187 88.704  1.00 29.02 ?  564 PHE A CZ    1 
ATOM   4540  N  N     . VAL A 1 565 ? 150.524 158.584 90.801  1.00 26.58 ?  565 VAL A N     1 
ATOM   4541  C  CA    . VAL A 1 565 ? 150.396 158.422 92.244  1.00 25.02 ?  565 VAL A CA    1 
ATOM   4542  C  C     . VAL A 1 565 ? 151.412 159.293 92.970  1.00 30.31 ?  565 VAL A C     1 
ATOM   4543  O  O     . VAL A 1 565 ? 151.081 159.969 93.951  1.00 34.28 ?  565 VAL A O     1 
ATOM   4544  C  CB    . VAL A 1 565 ? 150.541 156.939 92.633  1.00 25.45 ?  565 VAL A CB    1 
ATOM   4545  C  CG1   . VAL A 1 565 ? 150.614 156.794 94.143  1.00 21.98 ?  565 VAL A CG1   1 
ATOM   4546  C  CG2   . VAL A 1 565 ? 149.386 156.129 92.070  1.00 24.32 ?  565 VAL A CG2   1 
ATOM   4547  N  N     . ALA A 1 566 ? 152.661 159.294 92.502  1.00 31.54 ?  566 ALA A N     1 
ATOM   4548  C  CA    . ALA A 1 566 ? 153.670 160.157 93.105  1.00 27.98 ?  566 ALA A CA    1 
ATOM   4549  C  C     . ALA A 1 566 ? 153.228 161.614 93.075  1.00 32.56 ?  566 ALA A C     1 
ATOM   4550  O  O     . ALA A 1 566 ? 153.489 162.371 94.017  1.00 38.96 ?  566 ALA A O     1 
ATOM   4551  C  CB    . ALA A 1 566 ? 155.007 159.986 92.385  1.00 26.75 ?  566 ALA A CB    1 
ATOM   4552  N  N     . GLU A 1 567 ? 152.559 162.024 91.998  1.00 35.03 ?  567 GLU A N     1 
ATOM   4553  C  CA    . GLU A 1 567 ? 152.094 163.403 91.896  1.00 31.84 ?  567 GLU A CA    1 
ATOM   4554  C  C     . GLU A 1 567 ? 150.948 163.680 92.863  1.00 34.60 ?  567 GLU A C     1 
ATOM   4555  O  O     . GLU A 1 567 ? 150.963 164.681 93.587  1.00 40.33 ?  567 GLU A O     1 
ATOM   4556  C  CB    . GLU A 1 567 ? 151.665 163.704 90.461  1.00 31.03 ?  567 GLU A CB    1 
ATOM   4557  C  CG    . GLU A 1 567 ? 151.543 165.183 90.152  1.00 37.45 ?  567 GLU A CG    1 
ATOM   4558  C  CD    . GLU A 1 567 ? 152.143 165.549 88.811  1.00 42.76 ?  567 GLU A CD    1 
ATOM   4559  O  OE1   . GLU A 1 567 ? 153.233 166.159 88.791  1.00 42.85 ?  567 GLU A OE1   1 
ATOM   4560  O  OE2   . GLU A 1 567 ? 151.523 165.228 87.774  1.00 41.56 -1 567 GLU A OE2   1 
ATOM   4561  N  N     . HIS A 1 568 ? 149.946 162.800 92.894  1.00 37.42 ?  568 HIS A N     1 
ATOM   4562  C  CA    . HIS A 1 568 ? 148.697 163.083 93.585  1.00 30.32 ?  568 HIS A CA    1 
ATOM   4563  C  C     . HIS A 1 568 ? 148.457 162.224 94.817  1.00 30.71 ?  568 HIS A C     1 
ATOM   4564  O  O     . HIS A 1 568 ? 147.542 162.530 95.590  1.00 37.74 ?  568 HIS A O     1 
ATOM   4565  C  CB    . HIS A 1 568 ? 147.516 162.914 92.618  1.00 27.15 ?  568 HIS A CB    1 
ATOM   4566  C  CG    . HIS A 1 568 ? 147.660 163.703 91.354  1.00 33.19 ?  568 HIS A CG    1 
ATOM   4567  N  ND1   . HIS A 1 568 ? 148.203 163.173 90.204  1.00 34.83 ?  568 HIS A ND1   1 
ATOM   4568  C  CD2   . HIS A 1 568 ? 147.350 164.989 91.066  1.00 31.93 ?  568 HIS A CD2   1 
ATOM   4569  C  CE1   . HIS A 1 568 ? 148.211 164.095 89.258  1.00 31.68 ?  568 HIS A CE1   1 
ATOM   4570  N  NE2   . HIS A 1 568 ? 147.698 165.206 89.755  1.00 35.00 ?  568 HIS A NE2   1 
ATOM   4571  N  N     . GLY A 1 569 ? 149.239 161.175 95.029  1.00 25.45 ?  569 GLY A N     1 
ATOM   4572  C  CA    . GLY A 1 569 ? 149.034 160.322 96.178  1.00 24.13 ?  569 GLY A CA    1 
ATOM   4573  C  C     . GLY A 1 569 ? 147.923 159.311 95.969  1.00 25.45 ?  569 GLY A C     1 
ATOM   4574  O  O     . GLY A 1 569 ? 147.448 159.068 94.857  1.00 31.68 ?  569 GLY A O     1 
ATOM   4575  N  N     . MET A 1 570 ? 147.507 158.708 97.079  1.00 20.61 ?  570 MET A N     1 
ATOM   4576  C  CA    . MET A 1 570 ? 146.495 157.660 97.059  1.00 20.61 ?  570 MET A CA    1 
ATOM   4577  C  C     . MET A 1 570 ? 145.489 157.918 98.171  1.00 24.28 ?  570 MET A C     1 
ATOM   4578  O  O     . MET A 1 570 ? 145.878 158.188 99.310  1.00 28.37 ?  570 MET A O     1 
ATOM   4579  C  CB    . MET A 1 570 ? 147.138 156.278 97.221  1.00 28.02 ?  570 MET A CB    1 
ATOM   4580  C  CG    . MET A 1 570 ? 147.579 155.650 95.907  1.00 13.66 ?  570 MET A CG    1 
ATOM   4581  S  SD    . MET A 1 570 ? 147.598 153.850 95.933  1.00 36.82 ?  570 MET A SD    1 
ATOM   4582  C  CE    . MET A 1 570 ? 145.849 153.490 95.940  1.00 22.63 ?  570 MET A CE    1 
ATOM   4583  N  N     . TYR A 1 571 ? 144.201 157.841 97.835  1.00 16.87 ?  571 TYR A N     1 
ATOM   4584  C  CA    . TYR A 1 571 ? 143.151 158.152 98.799  1.00 6.12  ?  571 TYR A CA    1 
ATOM   4585  C  C     . TYR A 1 571 ? 142.924 157.030 99.804  1.00 1.89  ?  571 TYR A C     1 
ATOM   4586  O  O     . TYR A 1 571 ? 142.493 157.296 100.931 1.00 15.95 ?  571 TYR A O     1 
ATOM   4587  C  CB    . TYR A 1 571 ? 141.843 158.463 98.070  1.00 19.17 ?  571 TYR A CB    1 
ATOM   4588  C  CG    . TYR A 1 571 ? 140.769 159.040 98.961  1.00 20.50 ?  571 TYR A CG    1 
ATOM   4589  C  CD1   . TYR A 1 571 ? 140.814 160.368 99.366  1.00 18.47 ?  571 TYR A CD1   1 
ATOM   4590  C  CD2   . TYR A 1 571 ? 139.710 158.258 99.400  1.00 10.97 ?  571 TYR A CD2   1 
ATOM   4591  C  CE1   . TYR A 1 571 ? 139.833 160.897 100.179 1.00 21.45 ?  571 TYR A CE1   1 
ATOM   4592  C  CE2   . TYR A 1 571 ? 138.725 158.779 100.213 1.00 14.54 ?  571 TYR A CE2   1 
ATOM   4593  C  CZ    . TYR A 1 571 ? 138.791 160.100 100.600 1.00 27.11 ?  571 TYR A CZ    1 
ATOM   4594  O  OH    . TYR A 1 571 ? 137.814 160.626 101.410 1.00 22.71 ?  571 TYR A OH    1 
ATOM   4595  N  N     . HIS A 1 572 ? 143.194 155.787 99.425  1.00 16.56 ?  572 HIS A N     1 
ATOM   4596  C  CA    . HIS A 1 572 ? 142.913 154.629 100.264 1.00 8.34  ?  572 HIS A CA    1 
ATOM   4597  C  C     . HIS A 1 572 ? 144.217 153.965 100.679 1.00 7.83  ?  572 HIS A C     1 
ATOM   4598  O  O     . HIS A 1 572 ? 145.086 153.715 99.839  1.00 24.05 ?  572 HIS A O     1 
ATOM   4599  C  CB    . HIS A 1 572 ? 142.026 153.619 99.531  1.00 7.09  ?  572 HIS A CB    1 
ATOM   4600  C  CG    . HIS A 1 572 ? 140.774 154.209 98.961  1.00 6.52  ?  572 HIS A CG    1 
ATOM   4601  N  ND1   . HIS A 1 572 ? 140.720 154.767 97.704  1.00 12.94 ?  572 HIS A ND1   1 
ATOM   4602  C  CD2   . HIS A 1 572 ? 139.526 154.319 99.475  1.00 8.49  ?  572 HIS A CD2   1 
ATOM   4603  C  CE1   . HIS A 1 572 ? 139.495 155.202 97.468  1.00 11.27 ?  572 HIS A CE1   1 
ATOM   4604  N  NE2   . HIS A 1 572 ? 138.750 154.940 98.528  1.00 11.83 ?  572 HIS A NE2   1 
ATOM   4605  N  N     . SER A 1 573 ? 144.349 153.685 101.976 1.00 8.36  ?  573 SER A N     1 
ATOM   4606  C  CA    . SER A 1 573 ? 145.490 152.909 102.449 1.00 3.50  ?  573 SER A CA    1 
ATOM   4607  C  C     . SER A 1 573 ? 145.373 151.451 102.030 1.00 7.58  ?  573 SER A C     1 
ATOM   4608  O  O     . SER A 1 573 ? 146.390 150.775 101.848 1.00 19.77 ?  573 SER A O     1 
ATOM   4609  C  CB    . SER A 1 573 ? 145.612 153.020 103.967 1.00 6.56  ?  573 SER A CB    1 
ATOM   4610  O  OG    . SER A 1 573 ? 144.387 152.704 104.603 1.00 21.83 ?  573 SER A OG    1 
ATOM   4611  N  N     . TYR A 1 574 ? 144.148 150.957 101.876 1.00 8.95  ?  574 TYR A N     1 
ATOM   4612  C  CA    . TYR A 1 574 ? 143.884 149.599 101.434 1.00 0.00  ?  574 TYR A CA    1 
ATOM   4613  C  C     . TYR A 1 574 ? 142.685 149.617 100.500 1.00 1.66  ?  574 TYR A C     1 
ATOM   4614  O  O     . TYR A 1 574 ? 141.714 150.337 100.743 1.00 11.30 ?  574 TYR A O     1 
ATOM   4615  C  CB    . TYR A 1 574 ? 143.632 148.669 102.624 1.00 4.56  ?  574 TYR A CB    1 
ATOM   4616  C  CG    . TYR A 1 574 ? 144.781 148.653 103.600 1.00 0.00  ?  574 TYR A CG    1 
ATOM   4617  C  CD1   . TYR A 1 574 ? 145.837 147.769 103.441 1.00 8.11  ?  574 TYR A CD1   1 
ATOM   4618  C  CD2   . TYR A 1 574 ? 144.824 149.542 104.666 1.00 0.00  ?  574 TYR A CD2   1 
ATOM   4619  C  CE1   . TYR A 1 574 ? 146.894 147.759 104.322 1.00 4.62  ?  574 TYR A CE1   1 
ATOM   4620  C  CE2   . TYR A 1 574 ? 145.879 149.539 105.552 1.00 0.00  ?  574 TYR A CE2   1 
ATOM   4621  C  CZ    . TYR A 1 574 ? 146.910 148.645 105.376 1.00 0.00  ?  574 TYR A CZ    1 
ATOM   4622  O  OH    . TYR A 1 574 ? 147.964 148.634 106.257 1.00 8.55  ?  574 TYR A OH    1 
ATOM   4623  N  N     . ARG A 1 575 ? 142.761 148.834 99.431  1.00 10.85 ?  575 ARG A N     1 
ATOM   4624  C  CA    . ARG A 1 575 ? 141.735 148.843 98.399  1.00 0.04  ?  575 ARG A CA    1 
ATOM   4625  C  C     . ARG A 1 575 ? 141.111 147.483 98.141  1.00 5.67  ?  575 ARG A C     1 
ATOM   4626  O  O     . ARG A 1 575 ? 139.896 147.398 97.952  1.00 16.34 ?  575 ARG A O     1 
ATOM   4627  C  CB    . ARG A 1 575 ? 142.317 149.380 97.085  1.00 9.59  ?  575 ARG A CB    1 
ATOM   4628  C  CG    . ARG A 1 575 ? 142.756 150.830 97.133  1.00 5.68  ?  575 ARG A CG    1 
ATOM   4629  C  CD    . ARG A 1 575 ? 143.769 151.116 96.039  1.00 9.26  ?  575 ARG A CD    1 
ATOM   4630  N  NE    . ARG A 1 575 ? 145.019 150.398 96.255  1.00 15.70 ?  575 ARG A NE    1 
ATOM   4631  C  CZ    . ARG A 1 575 ? 145.362 149.284 95.623  1.00 12.15 ?  575 ARG A CZ    1 
ATOM   4632  N  NH1   . ARG A 1 575 ? 144.569 148.728 94.723  1.00 11.04 1  575 ARG A NH1   1 
ATOM   4633  N  NH2   . ARG A 1 575 ? 146.531 148.714 95.901  1.00 6.02  ?  575 ARG A NH2   1 
ATOM   4634  N  N     . LEU A 1 576 ? 141.904 146.415 98.130  1.00 15.50 ?  576 LEU A N     1 
ATOM   4635  C  CA    . LEU A 1 576 ? 141.464 145.113 97.649  1.00 8.00  ?  576 LEU A CA    1 
ATOM   4636  C  C     . LEU A 1 576 ? 141.559 144.076 98.759  1.00 0.00  ?  576 LEU A C     1 
ATOM   4637  O  O     . LEU A 1 576 ? 142.612 143.922 99.384  1.00 17.06 ?  576 LEU A O     1 
ATOM   4638  C  CB    . LEU A 1 576 ? 142.303 144.668 96.448  1.00 6.19  ?  576 LEU A CB    1 
ATOM   4639  C  CG    . LEU A 1 576 ? 142.306 145.627 95.256  1.00 4.56  ?  576 LEU A CG    1 
ATOM   4640  C  CD1   . LEU A 1 576 ? 143.138 145.072 94.112  1.00 10.67 ?  576 LEU A CD1   1 
ATOM   4641  C  CD2   . LEU A 1 576 ? 140.886 145.919 94.805  1.00 2.13  ?  576 LEU A CD2   1 
ATOM   4642  N  N     . CYS A 1 577 ? 140.456 143.371 98.993  1.00 1.90  ?  577 CYS A N     1 
ATOM   4643  C  CA    . CYS A 1 577 ? 140.438 142.202 99.858  1.00 5.66  ?  577 CYS A CA    1 
ATOM   4644  C  C     . CYS A 1 577 ? 139.335 141.280 99.362  1.00 12.97 ?  577 CYS A C     1 
ATOM   4645  O  O     . CYS A 1 577 ? 138.246 141.741 99.012  1.00 19.66 ?  577 CYS A O     1 
ATOM   4646  C  CB    . CYS A 1 577 ? 140.220 142.576 101.329 1.00 6.49  ?  577 CYS A CB    1 
ATOM   4647  S  SG    . CYS A 1 577 ? 138.494 142.799 101.822 1.00 30.39 ?  577 CYS A SG    1 
ATOM   4648  N  N     . ILE A 1 578 ? 139.620 139.985 99.326  1.00 2.38  ?  578 ILE A N     1 
ATOM   4649  C  CA    . ILE A 1 578 ? 138.697 138.998 98.770  1.00 4.34  ?  578 ILE A CA    1 
ATOM   4650  C  C     . ILE A 1 578 ? 138.048 138.281 99.949  1.00 3.31  ?  578 ILE A C     1 
ATOM   4651  O  O     . ILE A 1 578 ? 138.592 137.330 100.510 1.00 10.58 ?  578 ILE A O     1 
ATOM   4652  C  CB    . ILE A 1 578 ? 139.400 138.036 97.815  1.00 12.38 ?  578 ILE A CB    1 
ATOM   4653  C  CG1   . ILE A 1 578 ? 140.026 138.815 96.655  1.00 4.83  ?  578 ILE A CG1   1 
ATOM   4654  C  CG2   . ILE A 1 578 ? 138.423 136.996 97.294  1.00 7.14  ?  578 ILE A CG2   1 
ATOM   4655  C  CD1   . ILE A 1 578 ? 140.714 137.951 95.635  1.00 6.94  ?  578 ILE A CD1   1 
ATOM   4656  N  N     . ALA A 1 579 ? 136.864 138.748 100.326 1.00 13.36 ?  579 ALA A N     1 
ATOM   4657  C  CA    . ALA A 1 579 ? 136.090 138.143 101.393 1.00 3.78  ?  579 ALA A CA    1 
ATOM   4658  C  C     . ALA A 1 579 ? 135.326 136.924 100.885 1.00 20.57 ?  579 ALA A C     1 
ATOM   4659  O  O     . ALA A 1 579 ? 135.178 136.727 99.678  1.00 23.45 ?  579 ALA A O     1 
ATOM   4660  C  CB    . ALA A 1 579 ? 135.125 139.161 101.986 1.00 4.12  ?  579 ALA A CB    1 
ATOM   4661  N  N     . PRO A 1 580 ? 134.841 136.078 101.797 1.00 25.65 ?  580 PRO A N     1 
ATOM   4662  C  CA    . PRO A 1 580 ? 134.136 134.858 101.366 1.00 16.82 ?  580 PRO A CA    1 
ATOM   4663  C  C     . PRO A 1 580 ? 132.917 135.112 100.490 1.00 20.33 ?  580 PRO A C     1 
ATOM   4664  O  O     . PRO A 1 580 ? 132.659 134.322 99.574  1.00 31.10 ?  580 PRO A O     1 
ATOM   4665  C  CB    . PRO A 1 580 ? 133.745 134.190 102.694 1.00 12.24 ?  580 PRO A CB    1 
ATOM   4666  C  CG    . PRO A 1 580 ? 134.000 135.213 103.761 1.00 13.13 ?  580 PRO A CG    1 
ATOM   4667  C  CD    . PRO A 1 580 ? 135.079 136.095 103.248 1.00 13.70 ?  580 PRO A CD    1 
ATOM   4668  N  N     . THR A 1 581 ? 132.155 136.182 100.732 1.00 19.82 ?  581 THR A N     1 
ATOM   4669  C  CA    . THR A 1 581 ? 130.939 136.469 99.966  1.00 30.23 ?  581 THR A CA    1 
ATOM   4670  C  C     . THR A 1 581 ? 129.967 135.286 100.037 1.00 28.59 ?  581 THR A C     1 
ATOM   4671  O  O     . THR A 1 581 ? 129.645 134.638 99.040  1.00 33.19 ?  581 THR A O     1 
ATOM   4672  C  CB    . THR A 1 581 ? 131.261 136.814 98.506  1.00 29.54 ?  581 THR A CB    1 
ATOM   4673  O  OG1   . THR A 1 581 ? 131.282 135.616 97.722  1.00 18.90 ?  581 THR A OG1   1 
ATOM   4674  C  CG2   . THR A 1 581 ? 132.598 137.521 98.397  1.00 23.55 ?  581 THR A CG2   1 
ATOM   4675  N  N     . GLY A 1 582 ? 129.512 135.019 101.257 1.00 31.94 ?  582 GLY A N     1 
ATOM   4676  C  CA    . GLY A 1 582 ? 128.778 133.801 101.525 1.00 27.15 ?  582 GLY A CA    1 
ATOM   4677  C  C     . GLY A 1 582 ? 127.409 133.695 100.886 1.00 32.97 ?  582 GLY A C     1 
ATOM   4678  O  O     . GLY A 1 582 ? 127.207 132.866 99.994  1.00 38.73 ?  582 GLY A O     1 
ATOM   4679  N  N     . SER A 1 583 ? 126.462 134.529 101.313 1.00 33.28 ?  583 SER A N     1 
ATOM   4680  C  CA    . SER A 1 583 ? 125.077 134.364 100.889 1.00 35.83 ?  583 SER A CA    1 
ATOM   4681  C  C     . SER A 1 583 ? 124.699 135.231 99.697  1.00 34.23 ?  583 SER A C     1 
ATOM   4682  O  O     . SER A 1 583 ? 123.725 134.921 99.003  1.00 35.35 ?  583 SER A O     1 
ATOM   4683  C  CB    . SER A 1 583 ? 124.129 134.667 102.053 1.00 39.63 ?  583 SER A CB    1 
ATOM   4684  O  OG    . SER A 1 583 ? 124.139 133.617 103.003 1.00 42.36 ?  583 SER A OG    1 
ATOM   4685  N  N     . ILE A 1 584 ? 125.442 136.309 99.435  1.00 33.40 ?  584 ILE A N     1 
ATOM   4686  C  CA    . ILE A 1 584 ? 125.115 137.178 98.313  1.00 29.00 ?  584 ILE A CA    1 
ATOM   4687  C  C     . ILE A 1 584 ? 125.518 136.583 96.975  1.00 26.22 ?  584 ILE A C     1 
ATOM   4688  O  O     . ILE A 1 584 ? 125.126 137.112 95.930  1.00 32.21 ?  584 ILE A O     1 
ATOM   4689  C  CB    . ILE A 1 584 ? 125.763 138.565 98.497  1.00 30.65 ?  584 ILE A CB    1 
ATOM   4690  C  CG1   . ILE A 1 584 ? 124.934 139.631 97.782  1.00 31.33 ?  584 ILE A CG1   1 
ATOM   4691  C  CG2   . ILE A 1 584 ? 127.191 138.560 97.986  1.00 28.54 ?  584 ILE A CG2   1 
ATOM   4692  C  CD1   . ILE A 1 584 ? 123.456 139.554 98.074  1.00 26.82 ?  584 ILE A CD1   1 
ATOM   4693  N  N     . SER A 1 585 ? 126.291 135.494 96.976  1.00 25.17 ?  585 SER A N     1 
ATOM   4694  C  CA    . SER A 1 585 ? 126.653 134.847 95.722  1.00 22.39 ?  585 SER A CA    1 
ATOM   4695  C  C     . SER A 1 585 ? 125.443 134.208 95.052  1.00 27.91 ?  585 SER A C     1 
ATOM   4696  O  O     . SER A 1 585 ? 125.382 134.147 93.820  1.00 23.29 ?  585 SER A O     1 
ATOM   4697  C  CB    . SER A 1 585 ? 127.739 133.800 95.964  1.00 21.47 ?  585 SER A CB    1 
ATOM   4698  O  OG    . SER A 1 585 ? 127.302 132.816 96.883  1.00 27.37 ?  585 SER A OG    1 
ATOM   4699  N  N     . TYR A 1 586 ? 124.480 133.726 95.841  1.00 29.33 ?  586 TYR A N     1 
ATOM   4700  C  CA    . TYR A 1 586 ? 123.268 133.154 95.259  1.00 29.17 ?  586 TYR A CA    1 
ATOM   4701  C  C     . TYR A 1 586 ? 122.508 134.191 94.446  1.00 26.67 ?  586 TYR A C     1 
ATOM   4702  O  O     . TYR A 1 586 ? 122.042 133.902 93.338  1.00 29.85 ?  586 TYR A O     1 
ATOM   4703  C  CB    . TYR A 1 586 ? 122.374 132.584 96.360  1.00 31.88 ?  586 TYR A CB    1 
ATOM   4704  C  CG    . TYR A 1 586 ? 122.948 131.378 97.062  1.00 34.69 ?  586 TYR A CG    1 
ATOM   4705  C  CD1   . TYR A 1 586 ? 122.990 130.142 96.433  1.00 34.84 ?  586 TYR A CD1   1 
ATOM   4706  C  CD2   . TYR A 1 586 ? 123.446 131.474 98.353  1.00 32.82 ?  586 TYR A CD2   1 
ATOM   4707  C  CE1   . TYR A 1 586 ? 123.511 129.036 97.070  1.00 34.44 ?  586 TYR A CE1   1 
ATOM   4708  C  CE2   . TYR A 1 586 ? 123.969 130.373 98.997  1.00 32.24 ?  586 TYR A CE2   1 
ATOM   4709  C  CZ    . TYR A 1 586 ? 124.000 129.157 98.351  1.00 34.20 ?  586 TYR A CZ    1 
ATOM   4710  O  OH    . TYR A 1 586 ? 124.521 128.056 98.990  1.00 36.60 ?  586 TYR A OH    1 
ATOM   4711  N  N     . VAL A 1 587 ? 122.377 135.406 94.977  1.00 26.92 ?  587 VAL A N     1 
ATOM   4712  C  CA    . VAL A 1 587 ? 121.656 136.457 94.265  1.00 24.89 ?  587 VAL A CA    1 
ATOM   4713  C  C     . VAL A 1 587 ? 122.331 136.753 92.934  1.00 27.85 ?  587 VAL A C     1 
ATOM   4714  O  O     . VAL A 1 587 ? 121.664 136.960 91.912  1.00 30.31 ?  587 VAL A O     1 
ATOM   4715  C  CB    . VAL A 1 587 ? 121.555 137.719 95.140  1.00 26.14 ?  587 VAL A CB    1 
ATOM   4716  C  CG1   . VAL A 1 587 ? 120.878 138.841 94.374  1.00 28.30 ?  587 VAL A CG1   1 
ATOM   4717  C  CG2   . VAL A 1 587 ? 120.813 137.410 96.428  1.00 27.68 ?  587 VAL A CG2   1 
ATOM   4718  N  N     . GLN A 1 588 ? 123.661 136.781 92.924  1.00 31.94 ?  588 GLN A N     1 
ATOM   4719  C  CA    . GLN A 1 588 ? 124.417 137.043 91.708  1.00 21.23 ?  588 GLN A CA    1 
ATOM   4720  C  C     . GLN A 1 588 ? 124.546 135.818 90.816  1.00 24.26 ?  588 GLN A C     1 
ATOM   4721  O  O     . GLN A 1 588 ? 125.078 135.936 89.707  1.00 28.76 ?  588 GLN A O     1 
ATOM   4722  C  CB    . GLN A 1 588 ? 125.811 137.568 92.065  1.00 21.98 ?  588 GLN A CB    1 
ATOM   4723  C  CG    . GLN A 1 588 ? 125.810 138.931 92.735  1.00 20.05 ?  588 GLN A CG    1 
ATOM   4724  C  CD    . GLN A 1 588 ? 126.027 140.061 91.753  1.00 18.65 ?  588 GLN A CD    1 
ATOM   4725  O  OE1   . GLN A 1 588 ? 126.865 139.967 90.858  1.00 23.61 ?  588 GLN A OE1   1 
ATOM   4726  N  NE2   . GLN A 1 588 ? 125.271 141.139 91.912  1.00 26.61 ?  588 GLN A NE2   1 
ATOM   4727  N  N     . SER A 1 589 ? 124.073 134.657 91.267  1.00 27.32 ?  589 SER A N     1 
ATOM   4728  C  CA    . SER A 1 589 ? 124.212 133.408 90.523  1.00 21.98 ?  589 SER A CA    1 
ATOM   4729  C  C     . SER A 1 589 ? 125.674 133.164 90.158  1.00 22.16 ?  589 SER A C     1 
ATOM   4730  O  O     . SER A 1 589 ? 126.017 132.819 89.026  1.00 23.53 ?  589 SER A O     1 
ATOM   4731  C  CB    . SER A 1 589 ? 123.319 133.406 89.282  1.00 22.22 ?  589 SER A CB    1 
ATOM   4732  O  OG    . SER A 1 589 ? 123.710 134.411 88.364  1.00 29.30 ?  589 SER A OG    1 
ATOM   4733  N  N     . SER A 1 590 ? 126.545 133.354 91.145  1.00 27.19 ?  590 SER A N     1 
ATOM   4734  C  CA    . SER A 1 590 ? 127.981 133.245 90.959  1.00 23.59 ?  590 SER A CA    1 
ATOM   4735  C  C     . SER A 1 590 ? 128.568 132.319 92.013  1.00 17.02 ?  590 SER A C     1 
ATOM   4736  O  O     . SER A 1 590 ? 127.995 132.138 93.090  1.00 26.80 ?  590 SER A O     1 
ATOM   4737  C  CB    . SER A 1 590 ? 128.659 134.620 91.040  1.00 19.75 ?  590 SER A CB    1 
ATOM   4738  O  OG    . SER A 1 590 ? 129.074 134.906 92.363  1.00 23.22 ?  590 SER A OG    1 
ATOM   4739  N  N     . THR A 1 591 ? 129.714 131.727 91.691  1.00 19.89 ?  591 THR A N     1 
ATOM   4740  C  CA    . THR A 1 591 ? 130.437 130.938 92.674  1.00 17.09 ?  591 THR A CA    1 
ATOM   4741  C  C     . THR A 1 591 ? 131.013 131.846 93.757  1.00 15.48 ?  591 THR A C     1 
ATOM   4742  O  O     . THR A 1 591 ? 131.236 133.042 93.551  1.00 19.01 ?  591 THR A O     1 
ATOM   4743  C  CB    . THR A 1 591 ? 131.553 130.130 92.010  1.00 16.11 ?  591 THR A CB    1 
ATOM   4744  O  OG1   . THR A 1 591 ? 132.603 131.009 91.594  1.00 25.14 ?  591 THR A OG1   1 
ATOM   4745  C  CG2   . THR A 1 591 ? 131.020 129.371 90.805  1.00 22.01 ?  591 THR A CG2   1 
ATOM   4746  N  N     . ALA A 1 592 ? 131.250 131.262 94.926  1.00 14.93 ?  592 ALA A N     1 
ATOM   4747  C  CA    . ALA A 1 592 ? 131.655 132.033 96.094  1.00 13.02 ?  592 ALA A CA    1 
ATOM   4748  C  C     . ALA A 1 592 ? 133.115 132.450 95.973  1.00 21.17 ?  592 ALA A C     1 
ATOM   4749  O  O     . ALA A 1 592 ? 134.003 131.598 95.857  1.00 23.38 ?  592 ALA A O     1 
ATOM   4750  C  CB    . ALA A 1 592 ? 131.430 131.223 97.369  1.00 17.41 ?  592 ALA A CB    1 
ATOM   4751  N  N     . SER A 1 593 ? 133.358 133.753 96.005  1.00 25.76 ?  593 SER A N     1 
ATOM   4752  C  CA    . SER A 1 593 ? 134.707 134.315 96.065  1.00 8.84  ?  593 SER A CA    1 
ATOM   4753  C  C     . SER A 1 593 ? 135.548 133.724 94.932  1.00 11.68 ?  593 SER A C     1 
ATOM   4754  O  O     . SER A 1 593 ? 135.035 133.415 93.853  1.00 23.67 ?  593 SER A O     1 
ATOM   4755  C  CB    . SER A 1 593 ? 135.273 134.095 97.457  1.00 20.48 ?  593 SER A CB    1 
ATOM   4756  O  OG    . SER A 1 593 ? 136.478 134.813 97.645  1.00 26.35 ?  593 SER A OG    1 
ATOM   4757  N  N     . VAL A 1 594 ? 136.850 133.565 95.170  1.00 16.17 ?  594 VAL A N     1 
ATOM   4758  C  CA    . VAL A 1 594 ? 137.759 132.979 94.194  1.00 14.92 ?  594 VAL A CA    1 
ATOM   4759  C  C     . VAL A 1 594 ? 138.050 131.514 94.505  1.00 12.07 ?  594 VAL A C     1 
ATOM   4760  O  O     . VAL A 1 594 ? 138.876 130.894 93.831  1.00 16.26 ?  594 VAL A O     1 
ATOM   4761  C  CB    . VAL A 1 594 ? 139.062 133.788 94.101  1.00 19.74 ?  594 VAL A CB    1 
ATOM   4762  C  CG1   . VAL A 1 594 ? 138.782 135.179 93.556  1.00 13.82 ?  594 VAL A CG1   1 
ATOM   4763  C  CG2   . VAL A 1 594 ? 139.737 133.870 95.462  1.00 15.47 ?  594 VAL A CG2   1 
ATOM   4764  N  N     . MET A 1 595 ? 137.389 130.949 95.511  1.00 11.93 ?  595 MET A N     1 
ATOM   4765  C  CA    . MET A 1 595 ? 137.561 129.548 95.840  1.00 11.57 ?  595 MET A CA    1 
ATOM   4766  C  C     . MET A 1 595 ? 136.891 128.668 94.790  1.00 20.67 ?  595 MET A C     1 
ATOM   4767  O  O     . MET A 1 595 ? 135.945 129.089 94.121  1.00 29.55 ?  595 MET A O     1 
ATOM   4768  C  CB    . MET A 1 595 ? 136.969 129.245 97.213  1.00 11.70 ?  595 MET A CB    1 
ATOM   4769  C  CG    . MET A 1 595 ? 137.686 129.903 98.382  1.00 24.50 ?  595 MET A CG    1 
ATOM   4770  S  SD    . MET A 1 595 ? 139.332 129.232 98.676  1.00 31.79 ?  595 MET A SD    1 
ATOM   4771  C  CE    . MET A 1 595 ? 140.304 130.239 97.567  1.00 15.77 ?  595 MET A CE    1 
ATOM   4772  N  N     . PRO A 1 596 ? 137.371 127.440 94.621  1.00 24.82 ?  596 PRO A N     1 
ATOM   4773  C  CA    . PRO A 1 596 ? 136.640 126.473 93.799  1.00 16.68 ?  596 PRO A CA    1 
ATOM   4774  C  C     . PRO A 1 596 ? 135.361 126.032 94.495  1.00 19.22 ?  596 PRO A C     1 
ATOM   4775  O  O     . PRO A 1 596 ? 135.237 126.068 95.720  1.00 22.79 ?  596 PRO A O     1 
ATOM   4776  C  CB    . PRO A 1 596 ? 137.626 125.312 93.649  1.00 15.41 ?  596 PRO A CB    1 
ATOM   4777  C  CG    . PRO A 1 596 ? 138.490 125.402 94.856  1.00 18.68 ?  596 PRO A CG    1 
ATOM   4778  C  CD    . PRO A 1 596 ? 138.598 126.864 95.200  1.00 26.44 ?  596 PRO A CD    1 
ATOM   4779  N  N     . ILE A 1 597 ? 134.393 125.612 93.680  1.00 22.75 ?  597 ILE A N     1 
ATOM   4780  C  CA    . ILE A 1 597 ? 133.097 125.208 94.205  1.00 27.22 ?  597 ILE A CA    1 
ATOM   4781  C  C     . ILE A 1 597 ? 133.254 123.976 95.086  1.00 25.80 ?  597 ILE A C     1 
ATOM   4782  O  O     . ILE A 1 597 ? 134.100 123.106 94.841  1.00 29.83 ?  597 ILE A O     1 
ATOM   4783  C  CB    . ILE A 1 597 ? 132.107 124.946 93.057  1.00 25.54 ?  597 ILE A CB    1 
ATOM   4784  C  CG1   . ILE A 1 597 ? 132.490 123.666 92.312  1.00 25.37 ?  597 ILE A CG1   1 
ATOM   4785  C  CG2   . ILE A 1 597 ? 132.067 126.131 92.109  1.00 23.49 ?  597 ILE A CG2   1 
ATOM   4786  C  CD1   . ILE A 1 597 ? 131.371 123.072 91.499  1.00 25.95 ?  597 ILE A CD1   1 
ATOM   4787  N  N     . MET A 1 598 ? 132.426 123.898 96.129  1.00 33.24 ?  598 MET A N     1 
ATOM   4788  C  CA    . MET A 1 598 ? 132.462 122.747 97.023  1.00 36.15 ?  598 MET A CA    1 
ATOM   4789  C  C     . MET A 1 598 ? 131.681 121.571 96.451  1.00 37.11 ?  598 MET A C     1 
ATOM   4790  O  O     . MET A 1 598 ? 132.133 120.424 96.531  1.00 39.74 ?  598 MET A O     1 
ATOM   4791  C  CB    . MET A 1 598 ? 131.913 123.130 98.396  1.00 35.42 ?  598 MET A CB    1 
ATOM   4792  C  CG    . MET A 1 598 ? 132.959 123.188 99.492  1.00 35.26 ?  598 MET A CG    1 
ATOM   4793  S  SD    . MET A 1 598 ? 132.391 124.113 100.927 1.00 55.84 ?  598 MET A SD    1 
ATOM   4794  C  CE    . MET A 1 598 ? 132.256 125.758 100.236 1.00 37.43 ?  598 MET A CE    1 
ATOM   4795  N  N     . GLU A 1 599 ? 130.509 121.837 95.877  1.00 37.84 ?  599 GLU A N     1 
ATOM   4796  C  CA    . GLU A 1 599 ? 129.673 120.812 95.276  1.00 33.20 ?  599 GLU A CA    1 
ATOM   4797  C  C     . GLU A 1 599 ? 129.196 121.284 93.912  1.00 35.94 ?  599 GLU A C     1 
ATOM   4798  O  O     . GLU A 1 599 ? 129.027 122.483 93.678  1.00 40.13 ?  599 GLU A O     1 
ATOM   4799  C  CB    . GLU A 1 599 ? 128.460 120.481 96.156  1.00 35.05 ?  599 GLU A CB    1 
ATOM   4800  C  CG    . GLU A 1 599 ? 128.638 120.830 97.623  1.00 39.30 ?  599 GLU A CG    1 
ATOM   4801  C  CD    . GLU A 1 599 ? 127.431 120.453 98.459  1.00 42.47 ?  599 GLU A CD    1 
ATOM   4802  O  OE1   . GLU A 1 599 ? 127.309 120.955 99.595  1.00 41.41 ?  599 GLU A OE1   1 
ATOM   4803  O  OE2   . GLU A 1 599 ? 126.602 119.650 97.979  1.00 44.46 -1 599 GLU A OE2   1 
ATOM   4804  N  N     . ARG A 1 600 ? 128.984 120.327 93.007  1.00 37.36 ?  600 ARG A N     1 
ATOM   4805  C  CA    . ARG A 1 600 ? 128.407 120.662 91.709  1.00 30.77 ?  600 ARG A CA    1 
ATOM   4806  C  C     . ARG A 1 600 ? 126.946 121.064 91.848  1.00 31.76 ?  600 ARG A C     1 
ATOM   4807  O  O     . ARG A 1 600 ? 126.498 122.034 91.225  1.00 34.02 ?  600 ARG A O     1 
ATOM   4808  C  CB    . ARG A 1 600 ? 128.550 119.483 90.749  1.00 31.74 ?  600 ARG A CB    1 
ATOM   4809  C  CG    . ARG A 1 600 ? 129.910 119.386 90.088  1.00 34.72 ?  600 ARG A CG    1 
ATOM   4810  C  CD    . ARG A 1 600 ? 129.912 118.324 89.009  1.00 32.25 ?  600 ARG A CD    1 
ATOM   4811  N  NE    . ARG A 1 600 ? 131.223 118.170 88.392  1.00 27.20 ?  600 ARG A NE    1 
ATOM   4812  C  CZ    . ARG A 1 600 ? 132.193 117.409 88.878  1.00 33.17 ?  600 ARG A CZ    1 
ATOM   4813  N  NH1   . ARG A 1 600 ? 132.037 116.724 89.998  1.00 34.45 1  600 ARG A NH1   1 
ATOM   4814  N  NH2   . ARG A 1 600 ? 133.348 117.335 88.225  1.00 32.94 ?  600 ARG A NH2   1 
ATOM   4815  N  N     . ILE A 1 601 ? 126.188 120.329 92.657  1.00 41.06 ?  601 ILE A N     1 
ATOM   4816  C  CA    . ILE A 1 601 ? 124.795 120.643 92.950  1.00 40.39 ?  601 ILE A CA    1 
ATOM   4817  C  C     . ILE A 1 601 ? 124.659 120.753 94.460  1.00 37.86 ?  601 ILE A C     1 
ATOM   4818  O  O     . ILE A 1 601 ? 125.034 119.828 95.190  1.00 41.19 ?  601 ILE A O     1 
ATOM   4819  C  CB    . ILE A 1 601 ? 123.832 119.585 92.389  1.00 38.37 ?  601 ILE A CB    1 
ATOM   4820  C  CG1   . ILE A 1 601 ? 124.067 119.401 90.889  1.00 36.86 ?  601 ILE A CG1   1 
ATOM   4821  C  CG2   . ILE A 1 601 ? 122.392 119.984 92.658  1.00 39.32 ?  601 ILE A CG2   1 
ATOM   4822  C  CD1   . ILE A 1 601 ? 123.168 118.372 90.249  1.00 40.47 ?  601 ILE A CD1   1 
ATOM   4823  N  N     . GLU A 1 602 ? 124.130 121.878 94.927  1.00 43.07 ?  602 GLU A N     1 
ATOM   4824  C  CA    . GLU A 1 602 ? 124.054 122.179 96.352  1.00 45.74 ?  602 GLU A CA    1 
ATOM   4825  C  C     . GLU A 1 602 ? 122.670 121.797 96.862  1.00 47.42 ?  602 GLU A C     1 
ATOM   4826  O  O     . GLU A 1 602 ? 121.669 122.413 96.484  1.00 49.18 ?  602 GLU A O     1 
ATOM   4827  C  CB    . GLU A 1 602 ? 124.349 123.658 96.590  1.00 44.85 ?  602 GLU A CB    1 
ATOM   4828  C  CG    . GLU A 1 602 ? 124.039 124.159 97.984  1.00 46.79 ?  602 GLU A CG    1 
ATOM   4829  C  CD    . GLU A 1 602 ? 125.134 125.055 98.526  1.00 49.55 ?  602 GLU A CD    1 
ATOM   4830  O  OE1   . GLU A 1 602 ? 125.804 125.729 97.714  1.00 50.93 ?  602 GLU A OE1   1 
ATOM   4831  O  OE2   . GLU A 1 602 ? 125.323 125.095 99.758  1.00 49.45 -1 602 GLU A OE2   1 
ATOM   4832  N  N     . GLU A 1 603 ? 122.613 120.779 97.716  1.00 53.21 ?  603 GLU A N     1 
ATOM   4833  C  CA    . GLU A 1 603 ? 121.364 120.311 98.300  1.00 52.63 ?  603 GLU A CA    1 
ATOM   4834  C  C     . GLU A 1 603 ? 121.206 120.921 99.686  1.00 52.59 ?  603 GLU A C     1 
ATOM   4835  O  O     . GLU A 1 603 ? 122.066 120.731 100.553 1.00 53.99 ?  603 GLU A O     1 
ATOM   4836  C  CB    . GLU A 1 603 ? 121.333 118.785 98.383  1.00 53.98 ?  603 GLU A CB    1 
ATOM   4837  C  CG    . GLU A 1 603 ? 120.063 118.230 99.008  1.00 54.68 ?  603 GLU A CG    1 
ATOM   4838  C  CD    . GLU A 1 603 ? 120.200 116.778 99.420  1.00 57.28 ?  603 GLU A CD    1 
ATOM   4839  O  OE1   . GLU A 1 603 ? 120.172 115.899 98.533  1.00 57.07 ?  603 GLU A OE1   1 
ATOM   4840  O  OE2   . GLU A 1 603 ? 120.336 116.513 100.634 1.00 56.37 -1 603 GLU A OE2   1 
ATOM   4841  N  N     . ARG A 1 604 ? 120.111 121.647 99.893  1.00 55.60 ?  604 ARG A N     1 
ATOM   4842  C  CA    . ARG A 1 604 ? 119.842 122.299 101.162 1.00 54.99 ?  604 ARG A CA    1 
ATOM   4843  C  C     . ARG A 1 604 ? 118.374 122.128 101.524 1.00 56.22 ?  604 ARG A C     1 
ATOM   4844  O  O     . ARG A 1 604 ? 117.512 122.001 100.651 1.00 55.39 ?  604 ARG A O     1 
ATOM   4845  C  CB    . ARG A 1 604 ? 120.203 123.789 101.113 1.00 57.47 ?  604 ARG A CB    1 
ATOM   4846  C  CG    . ARG A 1 604 ? 121.687 124.053 100.915 1.00 55.20 ?  604 ARG A CG    1 
ATOM   4847  C  CD    . ARG A 1 604 ? 122.448 123.909 102.222 1.00 54.94 ?  604 ARG A CD    1 
ATOM   4848  N  NE    . ARG A 1 604 ? 123.891 123.882 102.023 1.00 54.17 ?  604 ARG A NE    1 
ATOM   4849  C  CZ    . ARG A 1 604 ? 124.544 122.922 101.384 1.00 55.03 ?  604 ARG A CZ    1 
ATOM   4850  N  NH1   . ARG A 1 604 ? 123.912 121.883 100.864 1.00 56.51 1  604 ARG A NH1   1 
ATOM   4851  N  NH2   . ARG A 1 604 ? 125.866 123.005 101.263 1.00 55.14 ?  604 ARG A NH2   1 
ATOM   4852  N  N     . THR A 1 605 ? 118.101 122.123 102.824 1.00 62.18 ?  605 THR A N     1 
ATOM   4853  C  CA    . THR A 1 605 ? 116.747 121.995 103.348 1.00 65.27 ?  605 THR A CA    1 
ATOM   4854  C  C     . THR A 1 605 ? 116.325 123.325 103.958 1.00 63.58 ?  605 THR A C     1 
ATOM   4855  O  O     . THR A 1 605 ? 116.939 123.795 104.921 1.00 62.70 ?  605 THR A O     1 
ATOM   4856  C  CB    . THR A 1 605 ? 116.661 120.873 104.384 1.00 63.47 ?  605 THR A CB    1 
ATOM   4857  O  OG1   . THR A 1 605 ? 115.322 120.787 104.887 1.00 63.37 ?  605 THR A OG1   1 
ATOM   4858  C  CG2   . THR A 1 605 ? 117.621 121.129 105.538 1.00 63.16 ?  605 THR A CG2   1 
ATOM   4859  N  N     . TYR A 1 606 ? 115.284 123.927 103.391 1.00 62.34 ?  606 TYR A N     1 
ATOM   4860  C  CA    . TYR A 1 606 ? 114.697 125.153 103.913 1.00 64.18 ?  606 TYR A CA    1 
ATOM   4861  C  C     . TYR A 1 606 ? 113.281 124.844 104.372 1.00 65.17 ?  606 TYR A C     1 
ATOM   4862  O  O     . TYR A 1 606 ? 112.492 124.269 103.615 1.00 63.38 ?  606 TYR A O     1 
ATOM   4863  C  CB    . TYR A 1 606 ? 114.701 126.263 102.857 1.00 62.44 ?  606 TYR A CB    1 
ATOM   4864  C  CG    . TYR A 1 606 ? 116.091 126.751 102.508 1.00 61.54 ?  606 TYR A CG    1 
ATOM   4865  C  CD1   . TYR A 1 606 ? 116.820 127.523 103.402 1.00 61.67 ?  606 TYR A CD1   1 
ATOM   4866  C  CD2   . TYR A 1 606 ? 116.675 126.432 101.290 1.00 59.87 ?  606 TYR A CD2   1 
ATOM   4867  C  CE1   . TYR A 1 606 ? 118.090 127.968 103.091 1.00 62.27 ?  606 TYR A CE1   1 
ATOM   4868  C  CE2   . TYR A 1 606 ? 117.945 126.871 100.971 1.00 61.73 ?  606 TYR A CE2   1 
ATOM   4869  C  CZ    . TYR A 1 606 ? 118.648 127.639 101.875 1.00 64.14 ?  606 TYR A CZ    1 
ATOM   4870  O  OH    . TYR A 1 606 ? 119.913 128.080 101.561 1.00 63.86 ?  606 TYR A OH    1 
ATOM   4871  N  N     . GLY A 1 607 ? 112.963 125.222 105.605 1.00 68.83 ?  607 GLY A N     1 
ATOM   4872  C  CA    . GLY A 1 607 ? 111.713 124.765 106.187 1.00 68.01 ?  607 GLY A CA    1 
ATOM   4873  C  C     . GLY A 1 607 ? 111.718 123.252 106.271 1.00 69.32 ?  607 GLY A C     1 
ATOM   4874  O  O     . GLY A 1 607 ? 112.658 122.640 106.792 1.00 68.82 ?  607 GLY A O     1 
ATOM   4875  N  N     . ASN A 1 608 ? 110.660 122.630 105.754 1.00 70.48 ?  608 ASN A N     1 
ATOM   4876  C  CA    . ASN A 1 608 ? 110.581 121.177 105.672 1.00 71.30 ?  608 ASN A CA    1 
ATOM   4877  C  C     . ASN A 1 608 ? 110.697 120.669 104.241 1.00 72.99 ?  608 ASN A C     1 
ATOM   4878  O  O     . ASN A 1 608 ? 110.468 119.478 103.996 1.00 72.97 ?  608 ASN A O     1 
ATOM   4879  C  CB    . ASN A 1 608 ? 109.281 120.673 106.308 1.00 72.60 ?  608 ASN A CB    1 
ATOM   4880  C  CG    . ASN A 1 608 ? 109.255 120.870 107.813 1.00 73.19 ?  608 ASN A CG    1 
ATOM   4881  O  OD1   . ASN A 1 608 ? 110.269 121.206 108.425 1.00 72.23 ?  608 ASN A OD1   1 
ATOM   4882  N  ND2   . ASN A 1 608 ? 108.092 120.657 108.417 1.00 72.85 ?  608 ASN A ND2   1 
ATOM   4883  N  N     . SER A 1 609 ? 111.048 121.534 103.295 1.00 70.53 ?  609 SER A N     1 
ATOM   4884  C  CA    . SER A 1 609 ? 111.269 121.147 101.909 1.00 68.79 ?  609 SER A CA    1 
ATOM   4885  C  C     . SER A 1 609 ? 112.727 121.385 101.547 1.00 67.87 ?  609 SER A C     1 
ATOM   4886  O  O     . SER A 1 609 ? 113.299 122.427 101.883 1.00 67.63 ?  609 SER A O     1 
ATOM   4887  C  CB    . SER A 1 609 ? 110.356 121.931 100.959 1.00 67.60 ?  609 SER A CB    1 
ATOM   4888  O  OG    . SER A 1 609 ? 110.635 123.318 101.012 1.00 67.40 ?  609 SER A OG    1 
ATOM   4889  N  N     . LYS A 1 610 ? 113.325 120.416 100.862 1.00 60.37 ?  610 LYS A N     1 
ATOM   4890  C  CA    . LYS A 1 610 ? 114.719 120.493 100.456 1.00 60.85 ?  610 LYS A CA    1 
ATOM   4891  C  C     . LYS A 1 610 ? 114.821 121.056 99.045  1.00 59.67 ?  610 LYS A C     1 
ATOM   4892  O  O     . LYS A 1 610 ? 113.964 120.796 98.195  1.00 57.44 ?  610 LYS A O     1 
ATOM   4893  C  CB    . LYS A 1 610 ? 115.384 119.117 100.523 1.00 61.21 ?  610 LYS A CB    1 
ATOM   4894  C  CG    . LYS A 1 610 ? 115.335 118.334 99.225  1.00 59.06 ?  610 LYS A CG    1 
ATOM   4895  C  CD    . LYS A 1 610 ? 116.241 117.117 99.287  1.00 60.92 ?  610 LYS A CD    1 
ATOM   4896  C  CE    . LYS A 1 610 ? 116.080 116.378 100.606 1.00 60.42 ?  610 LYS A CE    1 
ATOM   4897  N  NZ    . LYS A 1 610 ? 114.695 115.863 100.785 1.00 59.93 1  610 LYS A NZ    1 
ATOM   4898  N  N     . THR A 1 611 ? 115.875 121.832 98.803  1.00 58.18 ?  611 THR A N     1 
ATOM   4899  C  CA    . THR A 1 611 ? 116.084 122.497 97.526  1.00 55.98 ?  611 THR A CA    1 
ATOM   4900  C  C     . THR A 1 611 ? 117.454 122.130 96.976  1.00 52.58 ?  611 THR A C     1 
ATOM   4901  O  O     . THR A 1 611 ? 118.390 121.849 97.730  1.00 54.63 ?  611 THR A O     1 
ATOM   4902  C  CB    . THR A 1 611 ? 115.973 124.019 97.660  1.00 55.57 ?  611 THR A CB    1 
ATOM   4903  O  OG1   . THR A 1 611 ? 116.685 124.451 98.825  1.00 58.06 ?  611 THR A OG1   1 
ATOM   4904  C  CG2   . THR A 1 611 ? 114.516 124.435 97.782  1.00 53.48 ?  611 THR A CG2   1 
ATOM   4905  N  N     . TYR A 1 612 ? 117.563 122.135 95.651  1.00 47.77 ?  612 TYR A N     1 
ATOM   4906  C  CA    . TYR A 1 612 ? 118.797 121.793 94.959  1.00 48.23 ?  612 TYR A CA    1 
ATOM   4907  C  C     . TYR A 1 612 ? 119.285 123.003 94.177  1.00 47.48 ?  612 TYR A C     1 
ATOM   4908  O  O     . TYR A 1 612 ? 118.523 123.601 93.411  1.00 48.33 ?  612 TYR A O     1 
ATOM   4909  C  CB    . TYR A 1 612 ? 118.589 120.603 94.020  1.00 49.47 ?  612 TYR A CB    1 
ATOM   4910  C  CG    . TYR A 1 612 ? 118.165 119.342 94.734  1.00 50.46 ?  612 TYR A CG    1 
ATOM   4911  C  CD1   . TYR A 1 612 ? 119.078 118.591 95.460  1.00 50.76 ?  612 TYR A CD1   1 
ATOM   4912  C  CD2   . TYR A 1 612 ? 116.849 118.902 94.684  1.00 51.82 ?  612 TYR A CD2   1 
ATOM   4913  C  CE1   . TYR A 1 612 ? 118.693 117.438 96.115  1.00 53.21 ?  612 TYR A CE1   1 
ATOM   4914  C  CE2   . TYR A 1 612 ? 116.454 117.751 95.335  1.00 52.82 ?  612 TYR A CE2   1 
ATOM   4915  C  CZ    . TYR A 1 612 ? 117.380 117.022 96.050  1.00 53.27 ?  612 TYR A CZ    1 
ATOM   4916  O  OH    . TYR A 1 612 ? 116.992 115.874 96.701  1.00 52.85 ?  612 TYR A OH    1 
ATOM   4917  N  N     . TYR A 1 613 ? 120.552 123.359 94.369  1.00 43.41 ?  613 TYR A N     1 
ATOM   4918  C  CA    . TYR A 1 613 ? 121.160 124.495 93.677  1.00 37.57 ?  613 TYR A CA    1 
ATOM   4919  C  C     . TYR A 1 613 ? 122.355 124.036 92.857  1.00 36.56 ?  613 TYR A C     1 
ATOM   4920  O  O     . TYR A 1 613 ? 123.461 123.872 93.404  1.00 39.27 ?  613 TYR A O     1 
ATOM   4921  C  CB    . TYR A 1 613 ? 121.583 125.577 94.668  1.00 34.69 ?  613 TYR A CB    1 
ATOM   4922  C  CG    . TYR A 1 613 ? 122.238 126.769 94.009  1.00 36.41 ?  613 TYR A CG    1 
ATOM   4923  C  CD1   . TYR A 1 613 ? 121.567 127.508 93.045  1.00 38.38 ?  613 TYR A CD1   1 
ATOM   4924  C  CD2   . TYR A 1 613 ? 123.528 127.150 94.346  1.00 35.25 ?  613 TYR A CD2   1 
ATOM   4925  C  CE1   . TYR A 1 613 ? 122.162 128.596 92.440  1.00 39.18 ?  613 TYR A CE1   1 
ATOM   4926  C  CE2   . TYR A 1 613 ? 124.131 128.235 93.746  1.00 38.00 ?  613 TYR A CE2   1 
ATOM   4927  C  CZ    . TYR A 1 613 ? 123.443 128.956 92.793  1.00 41.26 ?  613 TYR A CZ    1 
ATOM   4928  O  OH    . TYR A 1 613 ? 124.040 130.039 92.193  1.00 41.73 ?  613 TYR A OH    1 
ATOM   4929  N  N     . PRO A 1 614 ? 122.195 123.812 91.557  1.00 36.10 ?  614 PRO A N     1 
ATOM   4930  C  CA    . PRO A 1 614 ? 123.361 123.540 90.714  1.00 35.12 ?  614 PRO A CA    1 
ATOM   4931  C  C     . PRO A 1 614 ? 124.252 124.766 90.612  1.00 37.62 ?  614 PRO A C     1 
ATOM   4932  O  O     . PRO A 1 614 ? 123.791 125.907 90.676  1.00 37.53 ?  614 PRO A O     1 
ATOM   4933  C  CB    . PRO A 1 614 ? 122.749 123.181 89.352  1.00 30.57 ?  614 PRO A CB    1 
ATOM   4934  C  CG    . PRO A 1 614 ? 121.286 122.961 89.613  1.00 36.98 ?  614 PRO A CG    1 
ATOM   4935  C  CD    . PRO A 1 614 ? 120.946 123.821 90.782  1.00 35.02 ?  614 PRO A CD    1 
ATOM   4936  N  N     . MET A 1 615 ? 125.546 124.518 90.448  1.00 33.94 ?  615 MET A N     1 
ATOM   4937  C  CA    . MET A 1 615 ? 126.482 125.619 90.300  1.00 28.62 ?  615 MET A CA    1 
ATOM   4938  C  C     . MET A 1 615 ? 126.113 126.441 89.068  1.00 33.88 ?  615 MET A C     1 
ATOM   4939  O  O     . MET A 1 615 ? 125.715 125.878 88.042  1.00 31.44 ?  615 MET A O     1 
ATOM   4940  C  CB    . MET A 1 615 ? 127.914 125.099 90.182  1.00 27.87 ?  615 MET A CB    1 
ATOM   4941  C  CG    . MET A 1 615 ? 128.567 124.792 91.517  1.00 29.84 ?  615 MET A CG    1 
ATOM   4942  S  SD    . MET A 1 615 ? 128.192 126.028 92.773  1.00 46.79 ?  615 MET A SD    1 
ATOM   4943  C  CE    . MET A 1 615 ? 127.000 125.144 93.773  1.00 33.00 ?  615 MET A CE    1 
ATOM   4944  N  N     . PRO A 1 616 ? 126.223 127.767 89.134  1.00 38.73 ?  616 PRO A N     1 
ATOM   4945  C  CA    . PRO A 1 616 ? 125.762 128.600 88.016  1.00 31.32 ?  616 PRO A CA    1 
ATOM   4946  C  C     . PRO A 1 616 ? 126.426 128.197 86.709  1.00 26.96 ?  616 PRO A C     1 
ATOM   4947  O  O     . PRO A 1 616 ? 127.639 127.992 86.643  1.00 35.28 ?  616 PRO A O     1 
ATOM   4948  C  CB    . PRO A 1 616 ? 126.164 130.015 88.444  1.00 30.83 ?  616 PRO A CB    1 
ATOM   4949  C  CG    . PRO A 1 616 ? 126.247 129.946 89.932  1.00 30.91 ?  616 PRO A CG    1 
ATOM   4950  C  CD    . PRO A 1 616 ? 126.746 128.573 90.249  1.00 27.02 ?  616 PRO A CD    1 
ATOM   4951  N  N     . GLY A 1 617 ? 125.614 128.088 85.661  1.00 32.97 ?  617 GLY A N     1 
ATOM   4952  C  CA    . GLY A 1 617 ? 126.106 127.666 84.369  1.00 30.37 ?  617 GLY A CA    1 
ATOM   4953  C  C     . GLY A 1 617 ? 126.414 126.193 84.251  1.00 35.37 ?  617 GLY A C     1 
ATOM   4954  O  O     . GLY A 1 617 ? 126.961 125.770 83.229  1.00 38.06 ?  617 GLY A O     1 
ATOM   4955  N  N     . LEU A 1 618 ? 126.079 125.395 85.262  1.00 37.16 ?  618 LEU A N     1 
ATOM   4956  C  CA    . LEU A 1 618 ? 126.393 123.973 85.227  1.00 33.74 ?  618 LEU A CA    1 
ATOM   4957  C  C     . LEU A 1 618 ? 125.584 123.276 84.142  1.00 34.47 ?  618 LEU A C     1 
ATOM   4958  O  O     . LEU A 1 618 ? 124.371 123.475 84.030  1.00 34.67 ?  618 LEU A O     1 
ATOM   4959  C  CB    . LEU A 1 618 ? 126.118 123.336 86.587  1.00 34.16 ?  618 LEU A CB    1 
ATOM   4960  C  CG    . LEU A 1 618 ? 126.414 121.840 86.701  1.00 32.65 ?  618 LEU A CG    1 
ATOM   4961  C  CD1   . LEU A 1 618 ? 127.867 121.552 86.365  1.00 35.11 ?  618 LEU A CD1   1 
ATOM   4962  C  CD2   . LEU A 1 618 ? 126.074 121.329 88.090  1.00 31.33 ?  618 LEU A CD2   1 
ATOM   4963  N  N     . ALA A 1 619 ? 126.261 122.457 83.346  1.00 41.83 ?  619 ALA A N     1 
ATOM   4964  C  CA    . ALA A 1 619 ? 125.626 121.718 82.264  1.00 40.85 ?  619 ALA A CA    1 
ATOM   4965  C  C     . ALA A 1 619 ? 126.484 120.499 81.957  1.00 44.63 ?  619 ALA A C     1 
ATOM   4966  O  O     . ALA A 1 619 ? 127.561 120.313 82.530  1.00 48.82 ?  619 ALA A O     1 
ATOM   4967  C  CB    . ALA A 1 619 ? 125.433 122.601 81.028  1.00 38.79 ?  619 ALA A CB    1 
ATOM   4968  N  N     . SER A 1 620 ? 125.993 119.659 81.044  1.00 47.22 ?  620 SER A N     1 
ATOM   4969  C  CA    . SER A 1 620 ? 126.737 118.459 80.674  1.00 45.44 ?  620 SER A CA    1 
ATOM   4970  C  C     . SER A 1 620 ? 128.075 118.812 80.037  1.00 47.65 ?  620 SER A C     1 
ATOM   4971  O  O     . SER A 1 620 ? 129.092 118.165 80.314  1.00 51.51 ?  620 SER A O     1 
ATOM   4972  C  CB    . SER A 1 620 ? 125.902 117.597 79.729  1.00 50.13 ?  620 SER A CB    1 
ATOM   4973  O  OG    . SER A 1 620 ? 124.610 117.360 80.262  1.00 54.72 ?  620 SER A OG    1 
ATOM   4974  N  N     . ASN A 1 621 ? 128.096 119.835 79.180  1.00 45.36 ?  621 ASN A N     1 
ATOM   4975  C  CA    . ASN A 1 621 ? 129.327 120.184 78.479  1.00 45.40 ?  621 ASN A CA    1 
ATOM   4976  C  C     . ASN A 1 621 ? 130.410 120.644 79.449  1.00 47.04 ?  621 ASN A C     1 
ATOM   4977  O  O     . ASN A 1 621 ? 131.584 120.288 79.294  1.00 47.61 ?  621 ASN A O     1 
ATOM   4978  C  CB    . ASN A 1 621 ? 129.049 121.263 77.433  1.00 45.46 ?  621 ASN A CB    1 
ATOM   4979  C  CG    . ASN A 1 621 ? 128.105 122.334 77.937  1.00 50.47 ?  621 ASN A CG    1 
ATOM   4980  O  OD1   . ASN A 1 621 ? 127.364 122.124 78.896  1.00 53.07 ?  621 ASN A OD1   1 
ATOM   4981  N  ND2   . ASN A 1 621 ? 128.129 123.494 77.292  1.00 46.38 ?  621 ASN A ND2   1 
ATOM   4982  N  N     . ASN A 1 622 ? 130.038 121.437 80.455  1.00 40.61 ?  622 ASN A N     1 
ATOM   4983  C  CA    . ASN A 1 622 ? 130.992 121.975 81.417  1.00 37.99 ?  622 ASN A CA    1 
ATOM   4984  C  C     . ASN A 1 622 ? 130.929 121.260 82.763  1.00 39.49 ?  622 ASN A C     1 
ATOM   4985  O  O     . ASN A 1 622 ? 131.423 121.787 83.763  1.00 44.34 ?  622 ASN A O     1 
ATOM   4986  C  CB    . ASN A 1 622 ? 130.772 123.478 81.598  1.00 37.69 ?  622 ASN A CB    1 
ATOM   4987  C  CG    . ASN A 1 622 ? 129.410 123.809 82.179  1.00 39.58 ?  622 ASN A CG    1 
ATOM   4988  O  OD1   . ASN A 1 622 ? 128.697 122.935 82.667  1.00 44.38 ?  622 ASN A OD1   1 
ATOM   4989  N  ND2   . ASN A 1 622 ? 129.042 125.083 82.127  1.00 34.93 ?  622 ASN A ND2   1 
ATOM   4990  N  N     . TRP A 1 623 ? 130.325 120.071 82.807  1.00 36.02 ?  623 TRP A N     1 
ATOM   4991  C  CA    . TRP A 1 623 ? 130.243 119.333 84.065  1.00 36.48 ?  623 TRP A CA    1 
ATOM   4992  C  C     . TRP A 1 623 ? 131.630 119.003 84.600  1.00 38.08 ?  623 TRP A C     1 
ATOM   4993  O  O     . TRP A 1 623 ? 131.889 119.137 85.802  1.00 33.98 ?  623 TRP A O     1 
ATOM   4994  C  CB    . TRP A 1 623 ? 129.422 118.057 83.871  1.00 36.65 ?  623 TRP A CB    1 
ATOM   4995  C  CG    . TRP A 1 623 ? 129.405 117.149 85.066  1.00 35.78 ?  623 TRP A CG    1 
ATOM   4996  C  CD1   . TRP A 1 623 ? 130.347 116.222 85.406  1.00 34.35 ?  623 TRP A CD1   1 
ATOM   4997  C  CD2   . TRP A 1 623 ? 128.390 117.075 86.075  1.00 34.12 ?  623 TRP A CD2   1 
ATOM   4998  N  NE1   . TRP A 1 623 ? 129.986 115.582 86.564  1.00 35.06 ?  623 TRP A NE1   1 
ATOM   4999  C  CE2   . TRP A 1 623 ? 128.786 116.085 86.994  1.00 32.85 ?  623 TRP A CE2   1 
ATOM   5000  C  CE3   . TRP A 1 623 ? 127.184 117.750 86.289  1.00 32.92 ?  623 TRP A CE3   1 
ATOM   5001  C  CZ2   . TRP A 1 623 ? 128.024 115.757 88.111  1.00 35.36 ?  623 TRP A CZ2   1 
ATOM   5002  C  CZ3   . TRP A 1 623 ? 126.428 117.421 87.398  1.00 33.49 ?  623 TRP A CZ3   1 
ATOM   5003  C  CH2   . TRP A 1 623 ? 126.851 116.433 88.295  1.00 37.25 ?  623 TRP A CH2   1 
ATOM   5004  N  N     . PHE A 1 624 ? 132.538 118.570 83.723  1.00 42.26 ?  624 PHE A N     1 
ATOM   5005  C  CA    . PHE A 1 624 ? 133.868 118.163 84.154  1.00 36.47 ?  624 PHE A CA    1 
ATOM   5006  C  C     . PHE A 1 624 ? 134.730 119.338 84.590  1.00 37.14 ?  624 PHE A C     1 
ATOM   5007  O  O     . PHE A 1 624 ? 135.621 119.159 85.427  1.00 40.43 ?  624 PHE A O     1 
ATOM   5008  C  CB    . PHE A 1 624 ? 134.561 117.389 83.028  1.00 36.56 ?  624 PHE A CB    1 
ATOM   5009  C  CG    . PHE A 1 624 ? 136.059 117.377 83.126  1.00 41.53 ?  624 PHE A CG    1 
ATOM   5010  C  CD1   . PHE A 1 624 ? 136.706 116.446 83.922  1.00 41.76 ?  624 PHE A CD1   1 
ATOM   5011  C  CD2   . PHE A 1 624 ? 136.824 118.283 82.408  1.00 38.59 ?  624 PHE A CD2   1 
ATOM   5012  C  CE1   . PHE A 1 624 ? 138.085 116.425 84.010  1.00 37.98 ?  624 PHE A CE1   1 
ATOM   5013  C  CE2   . PHE A 1 624 ? 138.202 118.268 82.492  1.00 37.80 ?  624 PHE A CE2   1 
ATOM   5014  C  CZ    . PHE A 1 624 ? 138.834 117.337 83.294  1.00 39.35 ?  624 PHE A CZ    1 
ATOM   5015  N  N     . PHE A 1 625 ? 134.487 120.534 84.051  1.00 33.43 ?  625 PHE A N     1 
ATOM   5016  C  CA    . PHE A 1 625 ? 135.232 121.711 84.477  1.00 30.19 ?  625 PHE A CA    1 
ATOM   5017  C  C     . PHE A 1 625 ? 134.768 122.241 85.825  1.00 27.58 ?  625 PHE A C     1 
ATOM   5018  O  O     . PHE A 1 625 ? 135.498 123.012 86.456  1.00 31.10 ?  625 PHE A O     1 
ATOM   5019  C  CB    . PHE A 1 625 ? 135.125 122.813 83.422  1.00 24.81 ?  625 PHE A CB    1 
ATOM   5020  C  CG    . PHE A 1 625 ? 135.872 122.513 82.158  1.00 28.61 ?  625 PHE A CG    1 
ATOM   5021  C  CD1   . PHE A 1 625 ? 137.254 122.457 82.155  1.00 31.02 ?  625 PHE A CD1   1 
ATOM   5022  C  CD2   . PHE A 1 625 ? 135.194 122.288 80.973  1.00 32.99 ?  625 PHE A CD2   1 
ATOM   5023  C  CE1   . PHE A 1 625 ? 137.947 122.183 80.994  1.00 29.76 ?  625 PHE A CE1   1 
ATOM   5024  C  CE2   . PHE A 1 625 ? 135.882 122.012 79.809  1.00 29.83 ?  625 PHE A CE2   1 
ATOM   5025  C  CZ    . PHE A 1 625 ? 137.259 121.960 79.819  1.00 31.69 ?  625 PHE A CZ    1 
ATOM   5026  N  N     . TYR A 1 626 ? 133.582 121.849 86.278  1.00 26.30 ?  626 TYR A N     1 
ATOM   5027  C  CA    . TYR A 1 626 ? 133.106 122.213 87.610  1.00 24.54 ?  626 TYR A CA    1 
ATOM   5028  C  C     . TYR A 1 626 ? 133.588 121.214 88.654  1.00 26.72 ?  626 TYR A C     1 
ATOM   5029  O  O     . TYR A 1 626 ? 132.816 120.682 89.449  1.00 32.12 ?  626 TYR A O     1 
ATOM   5030  C  CB    . TYR A 1 626 ? 131.587 122.316 87.612  1.00 27.19 ?  626 TYR A CB    1 
ATOM   5031  C  CG    . TYR A 1 626 ? 131.070 123.702 87.313  1.00 29.11 ?  626 TYR A CG    1 
ATOM   5032  C  CD1   . TYR A 1 626 ? 131.110 124.700 88.278  1.00 30.20 ?  626 TYR A CD1   1 
ATOM   5033  C  CD2   . TYR A 1 626 ? 130.541 124.013 86.069  1.00 27.68 ?  626 TYR A CD2   1 
ATOM   5034  C  CE1   . TYR A 1 626 ? 130.639 125.967 88.010  1.00 31.36 ?  626 TYR A CE1   1 
ATOM   5035  C  CE2   . TYR A 1 626 ? 130.068 125.278 85.793  1.00 27.60 ?  626 TYR A CE2   1 
ATOM   5036  C  CZ    . TYR A 1 626 ? 130.118 126.251 86.768  1.00 27.48 ?  626 TYR A CZ    1 
ATOM   5037  O  OH    . TYR A 1 626 ? 129.647 127.513 86.499  1.00 28.03 ?  626 TYR A OH    1 
ATOM   5038  N  N     . LYS A 1 627 ? 134.893 120.964 88.654  1.00 31.12 ?  627 LYS A N     1 
ATOM   5039  C  CA    . LYS A 1 627 ? 135.477 120.031 89.603  1.00 22.95 ?  627 LYS A CA    1 
ATOM   5040  C  C     . LYS A 1 627 ? 135.323 120.560 91.023  1.00 22.58 ?  627 LYS A C     1 
ATOM   5041  O  O     . LYS A 1 627 ? 135.515 121.750 91.285  1.00 30.10 ?  627 LYS A O     1 
ATOM   5042  C  CB    . LYS A 1 627 ? 136.950 119.803 89.273  1.00 25.52 ?  627 LYS A CB    1 
ATOM   5043  C  CG    . LYS A 1 627 ? 137.621 118.718 90.089  1.00 27.84 ?  627 LYS A CG    1 
ATOM   5044  C  CD    . LYS A 1 627 ? 138.992 118.394 89.524  1.00 27.25 ?  627 LYS A CD    1 
ATOM   5045  C  CE    . LYS A 1 627 ? 139.709 117.353 90.361  1.00 35.49 ?  627 LYS A CE    1 
ATOM   5046  N  NZ    . LYS A 1 627 ? 141.103 117.140 89.888  1.00 33.70 1  627 LYS A NZ    1 
ATOM   5047  N  N     . GLU A 1 628 ? 134.970 119.669 91.941  1.00 29.56 ?  628 GLU A N     1 
ATOM   5048  C  CA    . GLU A 1 628 ? 134.758 120.067 93.322  1.00 30.84 ?  628 GLU A CA    1 
ATOM   5049  C  C     . GLU A 1 628 ? 136.089 120.277 94.030  1.00 33.93 ?  628 GLU A C     1 
ATOM   5050  O  O     . GLU A 1 628 ? 137.108 119.672 93.683  1.00 33.12 ?  628 GLU A O     1 
ATOM   5051  C  CB    . GLU A 1 628 ? 133.920 119.022 94.059  1.00 32.63 ?  628 GLU A CB    1 
ATOM   5052  C  CG    . GLU A 1 628 ? 132.483 118.944 93.573  1.00 31.08 ?  628 GLU A CG    1 
ATOM   5053  C  CD    . GLU A 1 628 ? 131.751 117.730 94.105  1.00 39.92 ?  628 GLU A CD    1 
ATOM   5054  O  OE1   . GLU A 1 628 ? 132.249 117.107 95.066  1.00 37.40 ?  628 GLU A OE1   1 
ATOM   5055  O  OE2   . GLU A 1 628 ? 130.676 117.399 93.562  1.00 35.79 -1 628 GLU A OE2   1 
ATOM   5056  N  N     . ALA A 1 629 ? 136.071 121.154 95.035  1.00 31.49 ?  629 ALA A N     1 
ATOM   5057  C  CA    . ALA A 1 629 ? 137.303 121.526 95.720  1.00 24.63 ?  629 ALA A CA    1 
ATOM   5058  C  C     . ALA A 1 629 ? 137.946 120.324 96.400  1.00 32.29 ?  629 ALA A C     1 
ATOM   5059  O  O     . ALA A 1 629 ? 139.173 120.171 96.376  1.00 32.41 ?  629 ALA A O     1 
ATOM   5060  C  CB    . ALA A 1 629 ? 137.021 122.632 96.735  1.00 27.46 ?  629 ALA A CB    1 
ATOM   5061  N  N     . TYR A 1 630 ? 137.135 119.463 97.017  1.00 34.86 ?  630 TYR A N     1 
ATOM   5062  C  CA    . TYR A 1 630 ? 137.688 118.312 97.722  1.00 29.83 ?  630 TYR A CA    1 
ATOM   5063  C  C     . TYR A 1 630 ? 138.417 117.370 96.776  1.00 33.81 ?  630 TYR A C     1 
ATOM   5064  O  O     . TYR A 1 630 ? 139.368 116.694 97.186  1.00 37.55 ?  630 TYR A O     1 
ATOM   5065  C  CB    . TYR A 1 630 ? 136.576 117.576 98.466  1.00 32.55 ?  630 TYR A CB    1 
ATOM   5066  C  CG    . TYR A 1 630 ? 135.815 118.454 99.431  1.00 33.05 ?  630 TYR A CG    1 
ATOM   5067  C  CD1   . TYR A 1 630 ? 136.351 118.787 100.667 1.00 28.38 ?  630 TYR A CD1   1 
ATOM   5068  C  CD2   . TYR A 1 630 ? 134.562 118.953 99.105  1.00 30.38 ?  630 TYR A CD2   1 
ATOM   5069  C  CE1   . TYR A 1 630 ? 135.661 119.589 101.551 1.00 28.79 ?  630 TYR A CE1   1 
ATOM   5070  C  CE2   . TYR A 1 630 ? 133.865 119.756 99.982  1.00 32.85 ?  630 TYR A CE2   1 
ATOM   5071  C  CZ    . TYR A 1 630 ? 134.418 120.070 101.204 1.00 36.39 ?  630 TYR A CZ    1 
ATOM   5072  O  OH    . TYR A 1 630 ? 133.723 120.870 102.081 1.00 42.84 ?  630 TYR A OH    1 
ATOM   5073  N  N     . ASP A 1 631 ? 137.998 117.312 95.515  1.00 33.06 ?  631 ASP A N     1 
ATOM   5074  C  CA    . ASP A 1 631 ? 138.681 116.509 94.511  1.00 31.55 ?  631 ASP A CA    1 
ATOM   5075  C  C     . ASP A 1 631 ? 139.886 117.218 93.910  1.00 34.55 ?  631 ASP A C     1 
ATOM   5076  O  O     . ASP A 1 631 ? 140.594 116.619 93.094  1.00 39.06 ?  631 ASP A O     1 
ATOM   5077  C  CB    . ASP A 1 631 ? 137.708 116.122 93.393  1.00 33.38 ?  631 ASP A CB    1 
ATOM   5078  C  CG    . ASP A 1 631 ? 136.427 115.508 93.922  1.00 40.82 ?  631 ASP A CG    1 
ATOM   5079  O  OD1   . ASP A 1 631 ? 136.488 114.787 94.938  1.00 42.06 ?  631 ASP A OD1   1 
ATOM   5080  O  OD2   . ASP A 1 631 ? 135.361 115.746 93.318  1.00 41.39 -1 631 ASP A OD2   1 
ATOM   5081  N  N     . MET A 1 632 ? 140.136 118.464 94.293  1.00 31.74 ?  632 MET A N     1 
ATOM   5082  C  CA    . MET A 1 632 ? 141.206 119.259 93.713  1.00 26.53 ?  632 MET A CA    1 
ATOM   5083  C  C     . MET A 1 632 ? 142.506 119.067 94.483  1.00 33.68 ?  632 MET A C     1 
ATOM   5084  O  O     . MET A 1 632 ? 142.508 118.743 95.672  1.00 36.23 ?  632 MET A O     1 
ATOM   5085  C  CB    . MET A 1 632 ? 140.832 120.742 93.709  1.00 30.33 ?  632 MET A CB    1 
ATOM   5086  C  CG    . MET A 1 632 ? 140.449 121.291 92.348  1.00 29.63 ?  632 MET A CG    1 
ATOM   5087  S  SD    . MET A 1 632 ? 139.432 122.772 92.463  1.00 41.20 ?  632 MET A SD    1 
ATOM   5088  C  CE    . MET A 1 632 ? 138.386 122.581 91.024  1.00 26.41 ?  632 MET A CE    1 
ATOM   5089  N  N     . ASP A 1 633 ? 143.619 119.271 93.782  1.00 32.99 ?  633 ASP A N     1 
ATOM   5090  C  CA    . ASP A 1 633 ? 144.933 119.290 94.411  1.00 26.74 ?  633 ASP A CA    1 
ATOM   5091  C  C     . ASP A 1 633 ? 145.089 120.610 95.155  1.00 27.86 ?  633 ASP A C     1 
ATOM   5092  O  O     . ASP A 1 633 ? 145.159 121.676 94.534  1.00 33.68 ?  633 ASP A O     1 
ATOM   5093  C  CB    . ASP A 1 633 ? 146.028 119.112 93.363  1.00 20.19 ?  633 ASP A CB    1 
ATOM   5094  C  CG    . ASP A 1 633 ? 147.417 119.069 93.968  1.00 34.04 ?  633 ASP A CG    1 
ATOM   5095  O  OD1   . ASP A 1 633 ? 147.530 119.038 95.212  1.00 32.83 ?  633 ASP A OD1   1 
ATOM   5096  O  OD2   . ASP A 1 633 ? 148.400 119.070 93.198  1.00 36.35 -1 633 ASP A OD2   1 
ATOM   5097  N  N     . MET A 1 634 ? 145.138 120.546 96.487  1.00 26.66 ?  634 MET A N     1 
ATOM   5098  C  CA    . MET A 1 634 ? 145.240 121.767 97.279  1.00 20.33 ?  634 MET A CA    1 
ATOM   5099  C  C     . MET A 1 634 ? 146.503 122.554 96.962  1.00 20.38 ?  634 MET A C     1 
ATOM   5100  O  O     . MET A 1 634 ? 146.543 123.762 97.211  1.00 23.75 ?  634 MET A O     1 
ATOM   5101  C  CB    . MET A 1 634 ? 145.189 121.437 98.770  1.00 18.29 ?  634 MET A CB    1 
ATOM   5102  C  CG    . MET A 1 634 ? 143.798 121.520 99.383  1.00 27.62 ?  634 MET A CG    1 
ATOM   5103  S  SD    . MET A 1 634 ? 142.812 122.893 98.752  1.00 39.60 ?  634 MET A SD    1 
ATOM   5104  C  CE    . MET A 1 634 ? 141.804 122.062 97.527  1.00 23.24 ?  634 MET A CE    1 
ATOM   5105  N  N     . PHE A 1 635 ? 147.532 121.902 96.415  1.00 24.05 ?  635 PHE A N     1 
ATOM   5106  C  CA    . PHE A 1 635 ? 148.719 122.635 95.987  1.00 18.01 ?  635 PHE A CA    1 
ATOM   5107  C  C     . PHE A 1 635 ? 148.404 123.552 94.813  1.00 20.24 ?  635 PHE A C     1 
ATOM   5108  O  O     . PHE A 1 635 ? 148.892 124.685 94.755  1.00 25.08 ?  635 PHE A O     1 
ATOM   5109  C  CB    . PHE A 1 635 ? 149.840 121.660 95.632  1.00 16.95 ?  635 PHE A CB    1 
ATOM   5110  C  CG    . PHE A 1 635 ? 150.726 121.310 96.792  1.00 19.59 ?  635 PHE A CG    1 
ATOM   5111  C  CD1   . PHE A 1 635 ? 150.186 121.065 98.043  1.00 22.38 ?  635 PHE A CD1   1 
ATOM   5112  C  CD2   . PHE A 1 635 ? 152.097 121.231 96.634  1.00 19.99 ?  635 PHE A CD2   1 
ATOM   5113  C  CE1   . PHE A 1 635 ? 150.996 120.745 99.113  1.00 18.18 ?  635 PHE A CE1   1 
ATOM   5114  C  CE2   . PHE A 1 635 ? 152.913 120.913 97.702  1.00 21.64 ?  635 PHE A CE2   1 
ATOM   5115  C  CZ    . PHE A 1 635 ? 152.361 120.669 98.942  1.00 20.29 ?  635 PHE A CZ    1 
ATOM   5116  N  N     . LYS A 1 636 ? 147.578 123.090 93.873  1.00 23.58 ?  636 LYS A N     1 
ATOM   5117  C  CA    . LYS A 1 636 ? 147.180 123.945 92.761  1.00 23.59 ?  636 LYS A CA    1 
ATOM   5118  C  C     . LYS A 1 636 ? 146.261 125.070 93.217  1.00 20.43 ?  636 LYS A C     1 
ATOM   5119  O  O     . LYS A 1 636 ? 146.332 126.184 92.685  1.00 30.82 ?  636 LYS A O     1 
ATOM   5120  C  CB    . LYS A 1 636 ? 146.506 123.111 91.672  1.00 23.62 ?  636 LYS A CB    1 
ATOM   5121  C  CG    . LYS A 1 636 ? 147.300 121.885 91.260  1.00 22.38 ?  636 LYS A CG    1 
ATOM   5122  C  CD    . LYS A 1 636 ? 148.747 122.241 90.970  1.00 30.04 ?  636 LYS A CD    1 
ATOM   5123  C  CE    . LYS A 1 636 ? 149.068 122.117 89.491  1.00 32.09 ?  636 LYS A CE    1 
ATOM   5124  N  NZ    . LYS A 1 636 ? 150.449 122.578 89.184  1.00 33.16 1  636 LYS A NZ    1 
ATOM   5125  N  N     . VAL A 1 637 ? 145.395 124.804 94.196  1.00 19.67 ?  637 VAL A N     1 
ATOM   5126  C  CA    . VAL A 1 637 ? 144.575 125.867 94.768  1.00 12.60 ?  637 VAL A CA    1 
ATOM   5127  C  C     . VAL A 1 637 ? 145.458 126.909 95.441  1.00 23.32 ?  637 VAL A C     1 
ATOM   5128  O  O     . VAL A 1 637 ? 145.224 128.118 95.320  1.00 29.42 ?  637 VAL A O     1 
ATOM   5129  C  CB    . VAL A 1 637 ? 143.540 125.277 95.745  1.00 16.96 ?  637 VAL A CB    1 
ATOM   5130  C  CG1   . VAL A 1 637 ? 142.622 126.366 96.275  1.00 17.95 ?  637 VAL A CG1   1 
ATOM   5131  C  CG2   . VAL A 1 637 ? 142.738 124.178 95.068  1.00 23.83 ?  637 VAL A CG2   1 
ATOM   5132  N  N     . VAL A 1 638 ? 146.485 126.456 96.163  1.00 19.97 ?  638 VAL A N     1 
ATOM   5133  C  CA    . VAL A 1 638 ? 147.438 127.378 96.772  1.00 16.81 ?  638 VAL A CA    1 
ATOM   5134  C  C     . VAL A 1 638 ? 148.150 128.190 95.699  1.00 13.76 ?  638 VAL A C     1 
ATOM   5135  O  O     . VAL A 1 638 ? 148.366 129.396 95.856  1.00 26.75 ?  638 VAL A O     1 
ATOM   5136  C  CB    . VAL A 1 638 ? 148.438 126.608 97.656  1.00 21.09 ?  638 VAL A CB    1 
ATOM   5137  C  CG1   . VAL A 1 638 ? 149.650 127.470 97.962  1.00 12.35 ?  638 VAL A CG1   1 
ATOM   5138  C  CG2   . VAL A 1 638 ? 147.769 126.152 98.940  1.00 17.66 ?  638 VAL A CG2   1 
ATOM   5139  N  N     . ASP A 1 639 ? 148.533 127.543 94.597  1.00 17.64 ?  639 ASP A N     1 
ATOM   5140  C  CA    . ASP A 1 639 ? 149.180 128.260 93.504  1.00 13.68 ?  639 ASP A CA    1 
ATOM   5141  C  C     . ASP A 1 639 ? 148.270 129.342 92.938  1.00 19.11 ?  639 ASP A C     1 
ATOM   5142  O  O     . ASP A 1 639 ? 148.710 130.470 92.689  1.00 29.72 ?  639 ASP A O     1 
ATOM   5143  C  CB    . ASP A 1 639 ? 149.584 127.282 92.401  1.00 15.64 ?  639 ASP A CB    1 
ATOM   5144  C  CG    . ASP A 1 639 ? 150.906 126.603 92.681  1.00 31.15 ?  639 ASP A CG    1 
ATOM   5145  O  OD1   . ASP A 1 639 ? 151.811 127.264 93.231  1.00 30.96 ?  639 ASP A OD1   1 
ATOM   5146  O  OD2   . ASP A 1 639 ? 151.040 125.407 92.349  1.00 34.85 -1 639 ASP A OD2   1 
ATOM   5147  N  N     . MET A 1 640 ? 146.995 129.016 92.728  1.00 14.24 ?  640 MET A N     1 
ATOM   5148  C  CA    . MET A 1 640 ? 146.060 129.996 92.186  1.00 21.16 ?  640 MET A CA    1 
ATOM   5149  C  C     . MET A 1 640 ? 145.858 131.159 93.151  1.00 14.03 ?  640 MET A C     1 
ATOM   5150  O  O     . MET A 1 640 ? 145.850 132.327 92.740  1.00 21.70 ?  640 MET A O     1 
ATOM   5151  C  CB    . MET A 1 640 ? 144.727 129.321 91.866  1.00 21.46 ?  640 MET A CB    1 
ATOM   5152  C  CG    . MET A 1 640 ? 143.532 130.255 91.864  1.00 22.08 ?  640 MET A CG    1 
ATOM   5153  S  SD    . MET A 1 640 ? 143.536 131.343 90.430  1.00 37.25 ?  640 MET A SD    1 
ATOM   5154  C  CE    . MET A 1 640 ? 142.542 130.391 89.289  1.00 19.97 ?  640 MET A CE    1 
ATOM   5155  N  N     . ILE A 1 641 ? 145.699 130.858 94.441  1.00 16.90 ?  641 ILE A N     1 
ATOM   5156  C  CA    . ILE A 1 641 ? 145.483 131.911 95.427  1.00 15.84 ?  641 ILE A CA    1 
ATOM   5157  C  C     . ILE A 1 641 ? 146.716 132.799 95.546  1.00 17.07 ?  641 ILE A C     1 
ATOM   5158  O  O     . ILE A 1 641 ? 146.605 134.020 95.698  1.00 27.77 ?  641 ILE A O     1 
ATOM   5159  C  CB    . ILE A 1 641 ? 145.084 131.297 96.780  1.00 22.78 ?  641 ILE A CB    1 
ATOM   5160  C  CG1   . ILE A 1 641 ? 143.779 130.515 96.639  1.00 15.27 ?  641 ILE A CG1   1 
ATOM   5161  C  CG2   . ILE A 1 641 ? 144.939 132.379 97.834  1.00 16.29 ?  641 ILE A CG2   1 
ATOM   5162  C  CD1   . ILE A 1 641 ? 142.714 131.254 95.856  1.00 12.64 ?  641 ILE A CD1   1 
ATOM   5163  N  N     . ALA A 1 642 ? 147.911 132.204 95.478  1.00 7.07  ?  642 ALA A N     1 
ATOM   5164  C  CA    . ALA A 1 642 ? 149.136 132.993 95.511  1.00 13.08 ?  642 ALA A CA    1 
ATOM   5165  C  C     . ALA A 1 642 ? 149.269 133.856 94.265  1.00 9.87  ?  642 ALA A C     1 
ATOM   5166  O  O     . ALA A 1 642 ? 149.763 134.987 94.337  1.00 22.51 ?  642 ALA A O     1 
ATOM   5167  C  CB    . ALA A 1 642 ? 150.348 132.076 95.662  1.00 14.78 ?  642 ALA A CB    1 
ATOM   5168  N  N     . THR A 1 643 ? 148.843 133.339 93.111  1.00 16.00 ?  643 THR A N     1 
ATOM   5169  C  CA    . THR A 1 643 ? 148.838 134.150 91.900  1.00 16.27 ?  643 THR A CA    1 
ATOM   5170  C  C     . THR A 1 643 ? 147.919 135.353 92.061  1.00 19.67 ?  643 THR A C     1 
ATOM   5171  O  O     . THR A 1 643 ? 148.285 136.483 91.718  1.00 17.44 ?  643 THR A O     1 
ATOM   5172  C  CB    . THR A 1 643 ? 148.412 133.304 90.700  1.00 16.71 ?  643 THR A CB    1 
ATOM   5173  O  OG1   . THR A 1 643 ? 149.298 132.186 90.560  1.00 28.34 ?  643 THR A OG1   1 
ATOM   5174  C  CG2   . THR A 1 643 ? 148.442 134.130 89.426  1.00 17.21 ?  643 THR A CG2   1 
ATOM   5175  N  N     . ILE A 1 644 ? 146.714 135.126 92.589  1.00 16.31 ?  644 ILE A N     1 
ATOM   5176  C  CA    . ILE A 1 644 ? 145.801 136.237 92.844  1.00 14.27 ?  644 ILE A CA    1 
ATOM   5177  C  C     . ILE A 1 644 ? 146.378 137.169 93.901  1.00 6.91  ?  644 ILE A C     1 
ATOM   5178  O  O     . ILE A 1 644 ? 146.329 138.397 93.762  1.00 18.71 ?  644 ILE A O     1 
ATOM   5179  C  CB    . ILE A 1 644 ? 144.414 135.710 93.257  1.00 17.71 ?  644 ILE A CB    1 
ATOM   5180  C  CG1   . ILE A 1 644 ? 143.799 134.874 92.134  1.00 16.60 ?  644 ILE A CG1   1 
ATOM   5181  C  CG2   . ILE A 1 644 ? 143.492 136.863 93.626  1.00 7.29  ?  644 ILE A CG2   1 
ATOM   5182  C  CD1   . ILE A 1 644 ? 142.590 134.080 92.565  1.00 16.45 ?  644 ILE A CD1   1 
ATOM   5183  N  N     . GLN A 1 645 ? 146.944 136.599 94.968  1.00 12.73 ?  645 GLN A N     1 
ATOM   5184  C  CA    . GLN A 1 645 ? 147.371 137.396 96.112  1.00 5.74  ?  645 GLN A CA    1 
ATOM   5185  C  C     . GLN A 1 645 ? 148.467 138.394 95.764  1.00 15.51 ?  645 GLN A C     1 
ATOM   5186  O  O     . GLN A 1 645 ? 148.623 139.392 96.475  1.00 29.01 ?  645 GLN A O     1 
ATOM   5187  C  CB    . GLN A 1 645 ? 147.848 136.483 97.243  1.00 3.53  ?  645 GLN A CB    1 
ATOM   5188  C  CG    . GLN A 1 645 ? 148.306 137.236 98.481  1.00 9.86  ?  645 GLN A CG    1 
ATOM   5189  C  CD    . GLN A 1 645 ? 147.150 137.819 99.269  1.00 13.12 ?  645 GLN A CD    1 
ATOM   5190  O  OE1   . GLN A 1 645 ? 146.525 137.132 100.072 1.00 13.09 ?  645 GLN A OE1   1 
ATOM   5191  N  NE2   . GLN A 1 645 ? 146.857 139.091 99.035  1.00 2.50  ?  645 GLN A NE2   1 
ATOM   5192  N  N     . GLN A 1 646 ? 149.229 138.156 94.699  1.00 18.98 ?  646 GLN A N     1 
ATOM   5193  C  CA    . GLN A 1 646 ? 150.274 139.100 94.330  1.00 9.12  ?  646 GLN A CA    1 
ATOM   5194  C  C     . GLN A 1 646 ? 149.714 140.432 93.848  1.00 12.44 ?  646 GLN A C     1 
ATOM   5195  O  O     . GLN A 1 646 ? 150.475 141.396 93.730  1.00 15.54 ?  646 GLN A O     1 
ATOM   5196  C  CB    . GLN A 1 646 ? 151.179 138.493 93.258  1.00 15.66 ?  646 GLN A CB    1 
ATOM   5197  C  CG    . GLN A 1 646 ? 150.568 138.449 91.874  1.00 22.58 ?  646 GLN A CG    1 
ATOM   5198  C  CD    . GLN A 1 646 ? 151.469 137.767 90.863  1.00 26.10 ?  646 GLN A CD    1 
ATOM   5199  O  OE1   . GLN A 1 646 ? 152.492 138.316 90.458  1.00 31.75 ?  646 GLN A OE1   1 
ATOM   5200  N  NE2   . GLN A 1 646 ? 151.087 136.567 90.446  1.00 17.02 ?  646 GLN A NE2   1 
ATOM   5201  N  N     . HIS A 1 647 ? 148.412 140.511 93.582  1.00 21.22 ?  647 HIS A N     1 
ATOM   5202  C  CA    . HIS A 1 647 ? 147.772 141.748 93.161  1.00 9.59  ?  647 HIS A CA    1 
ATOM   5203  C  C     . HIS A 1 647 ? 146.762 142.266 94.174  1.00 4.58  ?  647 HIS A C     1 
ATOM   5204  O  O     . HIS A 1 647 ? 146.168 143.323 93.951  1.00 19.79 ?  647 HIS A O     1 
ATOM   5205  C  CB    . HIS A 1 647 ? 147.092 141.551 91.803  1.00 9.55  ?  647 HIS A CB    1 
ATOM   5206  C  CG    . HIS A 1 647 ? 147.971 140.899 90.781  1.00 11.48 ?  647 HIS A CG    1 
ATOM   5207  N  ND1   . HIS A 1 647 ? 149.092 141.511 90.266  1.00 12.35 ?  647 HIS A ND1   1 
ATOM   5208  C  CD2   . HIS A 1 647 ? 147.900 139.684 90.191  1.00 9.90  ?  647 HIS A CD2   1 
ATOM   5209  C  CE1   . HIS A 1 647 ? 149.670 140.704 89.397  1.00 14.00 ?  647 HIS A CE1   1 
ATOM   5210  N  NE2   . HIS A 1 647 ? 148.967 139.589 89.331  1.00 14.85 ?  647 HIS A NE2   1 
ATOM   5211  N  N     . ILE A 1 648 ? 146.553 141.553 95.276  1.00 8.38  ?  648 ILE A N     1 
ATOM   5212  C  CA    . ILE A 1 648 ? 145.674 141.990 96.353  1.00 11.23 ?  648 ILE A CA    1 
ATOM   5213  C  C     . ILE A 1 648 ? 146.540 142.552 97.470  1.00 14.39 ?  648 ILE A C     1 
ATOM   5214  O  O     . ILE A 1 648 ? 147.462 141.880 97.947  1.00 22.87 ?  648 ILE A O     1 
ATOM   5215  C  CB    . ILE A 1 648 ? 144.798 140.832 96.862  1.00 14.37 ?  648 ILE A CB    1 
ATOM   5216  C  CG1   . ILE A 1 648 ? 144.112 140.118 95.695  1.00 13.82 ?  648 ILE A CG1   1 
ATOM   5217  C  CG2   . ILE A 1 648 ? 143.769 141.337 97.861  1.00 4.66  ?  648 ILE A CG2   1 
ATOM   5218  C  CD1   . ILE A 1 648 ? 143.307 141.028 94.801  1.00 3.40  ?  648 ILE A CD1   1 
ATOM   5219  N  N     . ASP A 1 649 ? 146.258 143.790 97.878  1.00 8.54  ?  649 ASP A N     1 
ATOM   5220  C  CA    . ASP A 1 649 ? 147.047 144.405 98.938  1.00 2.67  ?  649 ASP A CA    1 
ATOM   5221  C  C     . ASP A 1 649 ? 146.668 143.872 100.314 1.00 8.36  ?  649 ASP A C     1 
ATOM   5222  O  O     . ASP A 1 649 ? 147.520 143.811 101.206 1.00 26.53 ?  649 ASP A O     1 
ATOM   5223  C  CB    . ASP A 1 649 ? 146.906 145.928 98.888  1.00 17.18 ?  649 ASP A CB    1 
ATOM   5224  C  CG    . ASP A 1 649 ? 145.460 146.385 98.915  1.00 17.71 ?  649 ASP A CG    1 
ATOM   5225  O  OD1   . ASP A 1 649 ? 144.798 146.333 97.859  1.00 21.42 ?  649 ASP A OD1   1 
ATOM   5226  O  OD2   . ASP A 1 649 ? 144.987 146.804 99.990  1.00 19.13 -1 649 ASP A OD2   1 
ATOM   5227  N  N     . GLN A 1 650 ? 145.410 143.495 100.504 1.00 12.94 ?  650 GLN A N     1 
ATOM   5228  C  CA    . GLN A 1 650 ? 144.968 142.798 101.702 1.00 0.00  ?  650 GLN A CA    1 
ATOM   5229  C  C     . GLN A 1 650 ? 145.016 141.290 101.459 1.00 4.79  ?  650 GLN A C     1 
ATOM   5230  O  O     . GLN A 1 650 ? 145.622 140.810 100.498 1.00 18.53 ?  650 GLN A O     1 
ATOM   5231  C  CB    . GLN A 1 650 ? 143.584 143.284 102.114 1.00 7.15  ?  650 GLN A CB    1 
ATOM   5232  C  CG    . GLN A 1 650 ? 143.564 144.737 102.551 1.00 3.35  ?  650 GLN A CG    1 
ATOM   5233  C  CD    . GLN A 1 650 ? 142.209 145.171 103.055 1.00 8.71  ?  650 GLN A CD    1 
ATOM   5234  O  OE1   . GLN A 1 650 ? 141.790 144.789 104.146 1.00 19.62 ?  650 GLN A OE1   1 
ATOM   5235  N  NE2   . GLN A 1 650 ? 141.514 145.979 102.264 1.00 8.07  ?  650 GLN A NE2   1 
ATOM   5236  N  N     . GLY A 1 651 ? 144.393 140.518 102.347 1.00 7.53  ?  651 GLY A N     1 
ATOM   5237  C  CA    . GLY A 1 651 ? 144.402 139.075 102.237 1.00 10.36 ?  651 GLY A CA    1 
ATOM   5238  C  C     . GLY A 1 651 ? 143.252 138.527 101.411 1.00 1.38  ?  651 GLY A C     1 
ATOM   5239  O  O     . GLY A 1 651 ? 142.446 139.253 100.835 1.00 8.76  ?  651 GLY A O     1 
ATOM   5240  N  N     . ILE A 1 652 ? 143.201 137.198 101.351 1.00 17.84 ?  652 ILE A N     1 
ATOM   5241  C  CA    . ILE A 1 652 ? 142.153 136.459 100.659 1.00 0.46  ?  652 ILE A CA    1 
ATOM   5242  C  C     . ILE A 1 652 ? 141.679 135.345 101.579 1.00 2.56  ?  652 ILE A C     1 
ATOM   5243  O  O     . ILE A 1 652 ? 142.492 134.553 102.065 1.00 17.59 ?  652 ILE A O     1 
ATOM   5244  C  CB    . ILE A 1 652 ? 142.651 135.870 99.325  1.00 10.04 ?  652 ILE A CB    1 
ATOM   5245  C  CG1   . ILE A 1 652 ? 143.281 136.955 98.451  1.00 6.60  ?  652 ILE A CG1   1 
ATOM   5246  C  CG2   . ILE A 1 652 ? 141.516 135.160 98.600  1.00 8.14  ?  652 ILE A CG2   1 
ATOM   5247  C  CD1   . ILE A 1 652 ? 143.941 136.419 97.205  1.00 11.05 ?  652 ILE A CD1   1 
ATOM   5248  N  N     . SER A 1 653 ? 140.373 135.281 101.816 1.00 2.74  ?  653 SER A N     1 
ATOM   5249  C  CA    . SER A 1 653 ? 139.810 134.190 102.602 1.00 7.42  ?  653 SER A CA    1 
ATOM   5250  C  C     . SER A 1 653 ? 140.046 132.882 101.856 1.00 12.02 ?  653 SER A C     1 
ATOM   5251  O  O     . SER A 1 653 ? 139.450 132.642 100.802 1.00 21.43 ?  653 SER A O     1 
ATOM   5252  C  CB    . SER A 1 653 ? 138.326 134.426 102.854 1.00 8.07  ?  653 SER A CB    1 
ATOM   5253  O  OG    . SER A 1 653 ? 138.130 135.187 104.031 1.00 13.84 ?  653 SER A OG    1 
ATOM   5254  N  N     . PHE A 1 654 ? 140.914 132.039 102.401 1.00 15.20 ?  654 PHE A N     1 
ATOM   5255  C  CA    . PHE A 1 654 ? 141.385 130.836 101.725 1.00 5.12  ?  654 PHE A CA    1 
ATOM   5256  C  C     . PHE A 1 654 ? 140.998 129.625 102.565 1.00 14.46 ?  654 PHE A C     1 
ATOM   5257  O  O     . PHE A 1 654 ? 141.641 129.331 103.578 1.00 20.38 ?  654 PHE A O     1 
ATOM   5258  C  CB    . PHE A 1 654 ? 142.896 130.903 101.507 1.00 8.01  ?  654 PHE A CB    1 
ATOM   5259  C  CG    . PHE A 1 654 ? 143.453 129.753 100.719 1.00 16.28 ?  654 PHE A CG    1 
ATOM   5260  C  CD1   . PHE A 1 654 ? 142.628 128.955 99.945  1.00 18.59 ?  654 PHE A CD1   1 
ATOM   5261  C  CD2   . PHE A 1 654 ? 144.807 129.475 100.747 1.00 14.04 ?  654 PHE A CD2   1 
ATOM   5262  C  CE1   . PHE A 1 654 ? 143.143 127.900 99.221  1.00 15.60 ?  654 PHE A CE1   1 
ATOM   5263  C  CE2   . PHE A 1 654 ? 145.328 128.422 100.023 1.00 17.76 ?  654 PHE A CE2   1 
ATOM   5264  C  CZ    . PHE A 1 654 ? 144.495 127.635 99.260  1.00 11.94 ?  654 PHE A CZ    1 
ATOM   5265  N  N     . THR A 1 655 ? 139.951 128.926 102.141 1.00 21.33 ?  655 THR A N     1 
ATOM   5266  C  CA    . THR A 1 655 ? 139.507 127.712 102.809 1.00 17.27 ?  655 THR A CA    1 
ATOM   5267  C  C     . THR A 1 655 ? 140.229 126.508 102.221 1.00 17.65 ?  655 THR A C     1 
ATOM   5268  O  O     . THR A 1 655 ? 140.351 126.383 101.000 1.00 18.34 ?  655 THR A O     1 
ATOM   5269  C  CB    . THR A 1 655 ? 137.993 127.537 102.671 1.00 21.24 ?  655 THR A CB    1 
ATOM   5270  O  OG1   . THR A 1 655 ? 137.325 128.583 103.384 1.00 25.30 ?  655 THR A OG1   1 
ATOM   5271  C  CG2   . THR A 1 655 ? 137.558 126.193 103.228 1.00 21.11 ?  655 THR A CG2   1 
ATOM   5272  N  N     . LEU A 1 656 ? 140.711 125.630 103.094 1.00 21.36 ?  656 LEU A N     1 
ATOM   5273  C  CA    . LEU A 1 656 ? 141.332 124.385 102.671 1.00 24.93 ?  656 LEU A CA    1 
ATOM   5274  C  C     . LEU A 1 656 ? 140.283 123.284 102.650 1.00 23.08 ?  656 LEU A C     1 
ATOM   5275  O  O     . LEU A 1 656 ? 139.585 123.063 103.644 1.00 26.02 ?  656 LEU A O     1 
ATOM   5276  C  CB    . LEU A 1 656 ? 142.484 124.005 103.603 1.00 27.30 ?  656 LEU A CB    1 
ATOM   5277  C  CG    . LEU A 1 656 ? 143.665 124.974 103.657 1.00 25.09 ?  656 LEU A CG    1 
ATOM   5278  C  CD1   . LEU A 1 656 ? 144.808 124.370 104.454 1.00 25.52 ?  656 LEU A CD1   1 
ATOM   5279  C  CD2   . LEU A 1 656 ? 144.117 125.351 102.257 1.00 18.64 ?  656 LEU A CD2   1 
ATOM   5280  N  N     . PHE A 1 657 ? 140.172 122.602 101.518 1.00 22.62 ?  657 PHE A N     1 
ATOM   5281  C  CA    . PHE A 1 657 ? 139.189 121.544 101.322 1.00 23.75 ?  657 PHE A CA    1 
ATOM   5282  C  C     . PHE A 1 657 ? 139.923 120.210 101.365 1.00 29.80 ?  657 PHE A C     1 
ATOM   5283  O  O     . PHE A 1 657 ? 140.645 119.861 100.427 1.00 29.31 ?  657 PHE A O     1 
ATOM   5284  C  CB    . PHE A 1 657 ? 138.447 121.738 100.004 1.00 26.07 ?  657 PHE A CB    1 
ATOM   5285  C  CG    . PHE A 1 657 ? 137.837 123.101 99.858  1.00 29.61 ?  657 PHE A CG    1 
ATOM   5286  C  CD1   . PHE A 1 657 ? 136.600 123.383 100.410 1.00 26.86 ?  657 PHE A CD1   1 
ATOM   5287  C  CD2   . PHE A 1 657 ? 138.510 124.106 99.186  1.00 29.43 ?  657 PHE A CD2   1 
ATOM   5288  C  CE1   . PHE A 1 657 ? 136.041 124.637 100.283 1.00 33.03 ?  657 PHE A CE1   1 
ATOM   5289  C  CE2   . PHE A 1 657 ? 137.955 125.363 99.055  1.00 29.56 ?  657 PHE A CE2   1 
ATOM   5290  C  CZ    . PHE A 1 657 ? 136.718 125.628 99.605  1.00 28.58 ?  657 PHE A CZ    1 
ATOM   5291  N  N     . LEU A 1 658 ? 139.734 119.471 102.453 1.00 31.15 ?  658 LEU A N     1 
ATOM   5292  C  CA    . LEU A 1 658 ? 140.505 118.271 102.734 1.00 37.05 ?  658 LEU A CA    1 
ATOM   5293  C  C     . LEU A 1 658 ? 139.601 117.048 102.725 1.00 39.77 ?  658 LEU A C     1 
ATOM   5294  O  O     . LEU A 1 658 ? 138.476 117.090 103.230 1.00 39.32 ?  658 LEU A O     1 
ATOM   5295  C  CB    . LEU A 1 658 ? 141.207 118.378 104.089 1.00 37.70 ?  658 LEU A CB    1 
ATOM   5296  C  CG    . LEU A 1 658 ? 141.691 119.776 104.477 1.00 35.10 ?  658 LEU A CG    1 
ATOM   5297  C  CD1   . LEU A 1 658 ? 141.868 119.873 105.981 1.00 30.32 ?  658 LEU A CD1   1 
ATOM   5298  C  CD2   . LEU A 1 658 ? 142.978 120.119 103.752 1.00 36.23 ?  658 LEU A CD2   1 
ATOM   5299  N  N     . LYS A 1 659 ? 140.100 115.962 102.144 1.00 45.15 ?  659 LYS A N     1 
ATOM   5300  C  CA    . LYS A 1 659 ? 139.420 114.681 102.229 1.00 44.20 ?  659 LYS A CA    1 
ATOM   5301  C  C     . LYS A 1 659 ? 139.655 114.054 103.597 1.00 46.29 ?  659 LYS A C     1 
ATOM   5302  O  O     . LYS A 1 659 ? 140.666 114.313 104.257 1.00 47.06 ?  659 LYS A O     1 
ATOM   5303  C  CB    . LYS A 1 659 ? 139.904 113.741 101.126 1.00 43.72 ?  659 LYS A CB    1 
ATOM   5304  C  CG    . LYS A 1 659 ? 139.663 114.265 99.721  1.00 46.24 ?  659 LYS A CG    1 
ATOM   5305  C  CD    . LYS A 1 659 ? 140.077 113.248 98.670  1.00 45.93 ?  659 LYS A CD    1 
ATOM   5306  C  CE    . LYS A 1 659 ? 139.851 113.785 97.267  1.00 45.96 ?  659 LYS A CE    1 
ATOM   5307  N  NZ    . LYS A 1 659 ? 139.890 112.707 96.241  1.00 49.03 1  659 LYS A NZ    1 
ATOM   5308  N  N     . ASP A 1 660 ? 138.705 113.222 104.025 1.00 51.38 ?  660 ASP A N     1 
ATOM   5309  C  CA    . ASP A 1 660 ? 138.826 112.572 105.324 1.00 51.18 ?  660 ASP A CA    1 
ATOM   5310  C  C     . ASP A 1 660 ? 140.055 111.676 105.408 1.00 52.59 ?  660 ASP A C     1 
ATOM   5311  O  O     . ASP A 1 660 ? 140.530 111.396 106.513 1.00 49.41 ?  660 ASP A O     1 
ATOM   5312  C  CB    . ASP A 1 660 ? 137.568 111.759 105.631 1.00 51.32 ?  660 ASP A CB    1 
ATOM   5313  C  CG    . ASP A 1 660 ? 137.154 110.865 104.479 1.00 52.96 ?  660 ASP A CG    1 
ATOM   5314  O  OD1   . ASP A 1 660 ? 136.388 111.332 103.609 1.00 52.20 ?  660 ASP A OD1   1 
ATOM   5315  O  OD2   . ASP A 1 660 ? 137.594 109.697 104.443 1.00 53.50 -1 660 ASP A OD2   1 
ATOM   5316  N  N     . THR A 1 661 ? 140.582 111.224 104.269 1.00 51.72 ?  661 THR A N     1 
ATOM   5317  C  CA    . THR A 1 661 ? 141.741 110.340 104.273 1.00 49.45 ?  661 THR A CA    1 
ATOM   5318  C  C     . THR A 1 661 ? 143.059 111.088 104.419 1.00 50.80 ?  661 THR A C     1 
ATOM   5319  O  O     . THR A 1 661 ? 144.095 110.449 104.633 1.00 54.64 ?  661 THR A O     1 
ATOM   5320  C  CB    . THR A 1 661 ? 141.773 109.505 102.992 1.00 52.39 ?  661 THR A CB    1 
ATOM   5321  O  OG1   . THR A 1 661 ? 141.745 110.372 101.853 1.00 52.82 ?  661 THR A OG1   1 
ATOM   5322  C  CG2   . THR A 1 661 ? 140.580 108.564 102.940 1.00 53.59 ?  661 THR A CG2   1 
ATOM   5323  N  N     . MET A 1 662 ? 143.051 112.414 104.307 1.00 49.01 ?  662 MET A N     1 
ATOM   5324  C  CA    . MET A 1 662 ? 144.282 113.179 104.451 1.00 46.87 ?  662 MET A CA    1 
ATOM   5325  C  C     . MET A 1 662 ? 144.697 113.238 105.915 1.00 48.12 ?  662 MET A C     1 
ATOM   5326  O  O     . MET A 1 662 ? 143.898 113.594 106.787 1.00 48.49 ?  662 MET A O     1 
ATOM   5327  C  CB    . MET A 1 662 ? 144.106 114.589 103.891 1.00 45.07 ?  662 MET A CB    1 
ATOM   5328  C  CG    . MET A 1 662 ? 143.684 114.634 102.435 1.00 49.04 ?  662 MET A CG    1 
ATOM   5329  S  SD    . MET A 1 662 ? 143.658 116.310 101.772 1.00 59.62 ?  662 MET A SD    1 
ATOM   5330  C  CE    . MET A 1 662 ? 145.310 116.863 102.186 1.00 46.79 ?  662 MET A CE    1 
ATOM   5331  N  N     . THR A 1 663 ? 145.952 112.890 106.183 1.00 42.22 ?  663 THR A N     1 
ATOM   5332  C  CA    . THR A 1 663 ? 146.484 112.903 107.534 1.00 37.71 ?  663 THR A CA    1 
ATOM   5333  C  C     . THR A 1 663 ? 146.816 114.333 107.956 1.00 41.47 ?  663 THR A C     1 
ATOM   5334  O  O     . THR A 1 663 ? 146.720 115.281 107.172 1.00 43.87 ?  663 THR A O     1 
ATOM   5335  C  CB    . THR A 1 663 ? 147.718 112.011 107.626 1.00 37.17 ?  663 THR A CB    1 
ATOM   5336  O  OG1   . THR A 1 663 ? 148.799 112.619 106.911 1.00 35.34 ?  663 THR A OG1   1 
ATOM   5337  C  CG2   . THR A 1 663 ? 147.430 110.643 107.028 1.00 43.66 ?  663 THR A CG2   1 
ATOM   5338  N  N     . THR A 1 664 ? 147.214 114.494 109.219 1.00 36.41 ?  664 THR A N     1 
ATOM   5339  C  CA    . THR A 1 664 ? 147.655 115.805 109.677 1.00 37.31 ?  664 THR A CA    1 
ATOM   5340  C  C     . THR A 1 664 ? 148.913 116.249 108.947 1.00 34.11 ?  664 THR A C     1 
ATOM   5341  O  O     . THR A 1 664 ? 149.163 117.453 108.817 1.00 41.32 ?  664 THR A O     1 
ATOM   5342  C  CB    . THR A 1 664 ? 147.894 115.790 111.188 1.00 34.39 ?  664 THR A CB    1 
ATOM   5343  O  OG1   . THR A 1 664 ? 148.830 114.756 111.516 1.00 35.91 ?  664 THR A OG1   1 
ATOM   5344  C  CG2   . THR A 1 664 ? 146.590 115.545 111.928 1.00 35.43 ?  664 THR A CG2   1 
ATOM   5345  N  N     . ARG A 1 665 ? 149.714 115.299 108.462 1.00 35.86 ?  665 ARG A N     1 
ATOM   5346  C  CA    . ARG A 1 665 ? 150.900 115.660 107.693 1.00 36.15 ?  665 ARG A CA    1 
ATOM   5347  C  C     . ARG A 1 665 ? 150.522 116.327 106.378 1.00 38.51 ?  665 ARG A C     1 
ATOM   5348  O  O     . ARG A 1 665 ? 151.209 117.248 105.928 1.00 39.30 ?  665 ARG A O     1 
ATOM   5349  C  CB    . ARG A 1 665 ? 151.765 114.427 107.439 1.00 33.67 ?  665 ARG A CB    1 
ATOM   5350  C  CG    . ARG A 1 665 ? 153.250 114.737 107.341 1.00 36.12 ?  665 ARG A CG    1 
ATOM   5351  C  CD    . ARG A 1 665 ? 153.980 113.716 106.486 1.00 35.15 ?  665 ARG A CD    1 
ATOM   5352  N  NE    . ARG A 1 665 ? 153.641 113.841 105.075 1.00 41.17 ?  665 ARG A NE    1 
ATOM   5353  C  CZ    . ARG A 1 665 ? 154.470 113.565 104.078 1.00 41.27 ?  665 ARG A CZ    1 
ATOM   5354  N  NH1   . ARG A 1 665 ? 155.705 113.145 104.302 1.00 36.02 1  665 ARG A NH1   1 
ATOM   5355  N  NH2   . ARG A 1 665 ? 154.051 113.716 102.824 1.00 41.06 ?  665 ARG A NH2   1 
ATOM   5356  N  N     . ASP A 1 666 ? 149.443 115.869 105.740 1.00 35.19 ?  666 ASP A N     1 
ATOM   5357  C  CA    . ASP A 1 666 ? 148.995 116.511 104.509 1.00 33.62 ?  666 ASP A CA    1 
ATOM   5358  C  C     . ASP A 1 666 ? 148.569 117.953 104.762 1.00 34.50 ?  666 ASP A C     1 
ATOM   5359  O  O     . ASP A 1 666 ? 148.903 118.854 103.984 1.00 35.97 ?  666 ASP A O     1 
ATOM   5360  C  CB    . ASP A 1 666 ? 147.851 115.711 103.887 1.00 36.42 ?  666 ASP A CB    1 
ATOM   5361  C  CG    . ASP A 1 666 ? 148.264 114.303 103.508 1.00 42.38 ?  666 ASP A CG    1 
ATOM   5362  O  OD1   . ASP A 1 666 ? 149.336 114.143 102.889 1.00 41.00 ?  666 ASP A OD1   1 
ATOM   5363  O  OD2   . ASP A 1 666 ? 147.517 113.356 103.828 1.00 42.92 -1 666 ASP A OD2   1 
ATOM   5364  N  N     . LEU A 1 667 ? 147.837 118.191 105.851 1.00 31.91 ?  667 LEU A N     1 
ATOM   5365  C  CA    . LEU A 1 667 ? 147.451 119.554 106.199 1.00 27.34 ?  667 LEU A CA    1 
ATOM   5366  C  C     . LEU A 1 667 ? 148.671 120.409 106.515 1.00 26.05 ?  667 LEU A C     1 
ATOM   5367  O  O     . LEU A 1 667 ? 148.753 121.571 106.096 1.00 31.33 ?  667 LEU A O     1 
ATOM   5368  C  CB    . LEU A 1 667 ? 146.480 119.536 107.379 1.00 34.59 ?  667 LEU A CB    1 
ATOM   5369  C  CG    . LEU A 1 667 ? 145.565 120.751 107.528 1.00 34.46 ?  667 LEU A CG    1 
ATOM   5370  C  CD1   . LEU A 1 667 ? 144.847 121.043 106.222 1.00 30.86 ?  667 LEU A CD1   1 
ATOM   5371  C  CD2   . LEU A 1 667 ? 144.566 120.531 108.650 1.00 27.50 ?  667 LEU A CD2   1 
ATOM   5372  N  N     . ASN A 1 668 ? 149.633 119.853 107.253 1.00 26.84 ?  668 ASN A N     1 
ATOM   5373  C  CA    . ASN A 1 668 ? 150.850 120.598 107.558 1.00 22.67 ?  668 ASN A CA    1 
ATOM   5374  C  C     . ASN A 1 668 ? 151.614 120.941 106.288 1.00 24.12 ?  668 ASN A C     1 
ATOM   5375  O  O     . ASN A 1 668 ? 152.136 122.053 106.153 1.00 29.24 ?  668 ASN A O     1 
ATOM   5376  C  CB    . ASN A 1 668 ? 151.732 119.798 108.515 1.00 26.11 ?  668 ASN A CB    1 
ATOM   5377  C  CG    . ASN A 1 668 ? 151.404 120.060 109.969 1.00 24.21 ?  668 ASN A CG    1 
ATOM   5378  O  OD1   . ASN A 1 668 ? 150.949 121.145 110.328 1.00 28.33 ?  668 ASN A OD1   1 
ATOM   5379  N  ND2   . ASN A 1 668 ? 151.634 119.065 110.815 1.00 31.48 ?  668 ASN A ND2   1 
ATOM   5380  N  N     . ARG A 1 669 ? 151.698 119.999 105.349 1.00 26.16 ?  669 ARG A N     1 
ATOM   5381  C  CA    . ARG A 1 669 ? 152.373 120.264 104.084 1.00 27.33 ?  669 ARG A CA    1 
ATOM   5382  C  C     . ARG A 1 669 ? 151.639 121.325 103.278 1.00 21.77 ?  669 ARG A C     1 
ATOM   5383  O  O     . ARG A 1 669 ? 152.272 122.158 102.624 1.00 23.42 ?  669 ARG A O     1 
ATOM   5384  C  CB    . ARG A 1 669 ? 152.507 118.974 103.277 1.00 25.51 ?  669 ARG A CB    1 
ATOM   5385  C  CG    . ARG A 1 669 ? 153.884 118.342 103.348 1.00 27.72 ?  669 ARG A CG    1 
ATOM   5386  C  CD    . ARG A 1 669 ? 153.904 116.983 102.670 1.00 31.23 ?  669 ARG A CD    1 
ATOM   5387  N  NE    . ARG A 1 669 ? 153.944 117.092 101.216 1.00 32.73 ?  669 ARG A NE    1 
ATOM   5388  C  CZ    . ARG A 1 669 ? 154.894 117.716 100.535 1.00 30.20 ?  669 ARG A CZ    1 
ATOM   5389  N  NH1   . ARG A 1 669 ? 155.915 118.296 101.144 1.00 28.83 1  669 ARG A NH1   1 
ATOM   5390  N  NH2   . ARG A 1 669 ? 154.820 117.757 99.208  1.00 31.07 ?  669 ARG A NH2   1 
ATOM   5391  N  N     . ILE A 1 670 ? 150.305 121.308 103.304 1.00 20.63 ?  670 ILE A N     1 
ATOM   5392  C  CA    . ILE A 1 670 ? 149.548 122.338 102.596 1.00 21.74 ?  670 ILE A CA    1 
ATOM   5393  C  C     . ILE A 1 670 ? 149.828 123.710 103.197 1.00 24.68 ?  670 ILE A C     1 
ATOM   5394  O  O     . ILE A 1 670 ? 150.040 124.690 102.473 1.00 24.61 ?  670 ILE A O     1 
ATOM   5395  C  CB    . ILE A 1 670 ? 148.044 122.009 102.613 1.00 28.30 ?  670 ILE A CB    1 
ATOM   5396  C  CG1   . ILE A 1 670 ? 147.739 120.847 101.667 1.00 22.76 ?  670 ILE A CG1   1 
ATOM   5397  C  CG2   . ILE A 1 670 ? 147.230 123.230 102.227 1.00 25.42 ?  670 ILE A CG2   1 
ATOM   5398  C  CD1   . ILE A 1 670 ? 146.478 120.096 102.017 1.00 24.66 ?  670 ILE A CD1   1 
ATOM   5399  N  N     . ASP A 1 671 ? 149.838 123.801 104.527 1.00 24.26 ?  671 ASP A N     1 
ATOM   5400  C  CA    . ASP A 1 671 ? 150.147 125.073 105.176 1.00 17.88 ?  671 ASP A CA    1 
ATOM   5401  C  C     . ASP A 1 671 ? 151.569 125.526 104.863 1.00 19.78 ?  671 ASP A C     1 
ATOM   5402  O  O     . ASP A 1 671 ? 151.813 126.714 104.615 1.00 22.58 ?  671 ASP A O     1 
ATOM   5403  C  CB    . ASP A 1 671 ? 149.942 124.961 106.687 1.00 21.90 ?  671 ASP A CB    1 
ATOM   5404  C  CG    . ASP A 1 671 ? 148.648 124.262 107.050 1.00 31.39 ?  671 ASP A CG    1 
ATOM   5405  O  OD1   . ASP A 1 671 ? 147.831 124.008 106.142 1.00 37.35 ?  671 ASP A OD1   1 
ATOM   5406  O  OD2   . ASP A 1 671 ? 148.449 123.960 108.247 1.00 35.50 -1 671 ASP A OD2   1 
ATOM   5407  N  N     . LEU A 1 672 ? 152.524 124.594 104.872 1.00 17.20 ?  672 LEU A N     1 
ATOM   5408  C  CA    . LEU A 1 672 ? 153.910 124.948 104.589 1.00 13.21 ?  672 LEU A CA    1 
ATOM   5409  C  C     . LEU A 1 672 ? 154.082 125.406 103.149 1.00 17.50 ?  672 LEU A C     1 
ATOM   5410  O  O     . LEU A 1 672 ? 154.858 126.327 102.873 1.00 20.21 ?  672 LEU A O     1 
ATOM   5411  C  CB    . LEU A 1 672 ? 154.826 123.762 104.888 1.00 20.55 ?  672 LEU A CB    1 
ATOM   5412  C  CG    . LEU A 1 672 ? 154.962 123.353 106.356 1.00 22.69 ?  672 LEU A CG    1 
ATOM   5413  C  CD1   . LEU A 1 672 ? 155.835 122.116 106.483 1.00 14.55 ?  672 LEU A CD1   1 
ATOM   5414  C  CD2   . LEU A 1 672 ? 155.522 124.498 107.181 1.00 21.59 ?  672 LEU A CD2   1 
ATOM   5415  N  N     . TYR A 1 673 ? 153.375 124.769 102.214 1.00 20.66 ?  673 TYR A N     1 
ATOM   5416  C  CA    . TYR A 1 673 ? 153.430 125.192 100.820 1.00 18.14 ?  673 TYR A CA    1 
ATOM   5417  C  C     . TYR A 1 673 ? 152.772 126.553 100.635 1.00 15.50 ?  673 TYR A C     1 
ATOM   5418  O  O     . TYR A 1 673 ? 153.248 127.375 99.843  1.00 13.78 ?  673 TYR A O     1 
ATOM   5419  C  CB    . TYR A 1 673 ? 152.767 124.141 99.931  1.00 9.21  ?  673 TYR A CB    1 
ATOM   5420  C  CG    . TYR A 1 673 ? 152.864 124.437 98.454  1.00 16.93 ?  673 TYR A CG    1 
ATOM   5421  C  CD1   . TYR A 1 673 ? 154.055 124.252 97.769  1.00 14.05 ?  673 TYR A CD1   1 
ATOM   5422  C  CD2   . TYR A 1 673 ? 151.765 124.905 97.747  1.00 12.97 ?  673 TYR A CD2   1 
ATOM   5423  C  CE1   . TYR A 1 673 ? 154.150 124.523 96.421  1.00 17.27 ?  673 TYR A CE1   1 
ATOM   5424  C  CE2   . TYR A 1 673 ? 151.851 125.179 96.398  1.00 13.98 ?  673 TYR A CE2   1 
ATOM   5425  C  CZ    . TYR A 1 673 ? 153.046 124.986 95.741  1.00 18.52 ?  673 TYR A CZ    1 
ATOM   5426  O  OH    . TYR A 1 673 ? 153.140 125.256 94.397  1.00 23.10 ?  673 TYR A OH    1 
ATOM   5427  N  N     . ALA A 1 674 ? 151.675 126.808 101.353 1.00 16.43 ?  674 ALA A N     1 
ATOM   5428  C  CA    . ALA A 1 674 ? 151.048 128.124 101.295 1.00 14.42 ?  674 ALA A CA    1 
ATOM   5429  C  C     . ALA A 1 674 ? 151.990 129.200 101.813 1.00 17.93 ?  674 ALA A C     1 
ATOM   5430  O  O     . ALA A 1 674 ? 152.109 130.275 101.214 1.00 25.93 ?  674 ALA A O     1 
ATOM   5431  C  CB    . ALA A 1 674 ? 149.745 128.121 102.090 1.00 14.68 ?  674 ALA A CB    1 
ATOM   5432  N  N     . HIS A 1 675 ? 152.671 128.929 102.928 1.00 12.83 ?  675 HIS A N     1 
ATOM   5433  C  CA    . HIS A 1 675 ? 153.654 129.877 103.441 1.00 14.42 ?  675 HIS A CA    1 
ATOM   5434  C  C     . HIS A 1 675 ? 154.800 130.065 102.456 1.00 15.87 ?  675 HIS A C     1 
ATOM   5435  O  O     . HIS A 1 675 ? 155.295 131.183 102.271 1.00 23.85 ?  675 HIS A O     1 
ATOM   5436  C  CB    . HIS A 1 675 ? 154.181 129.406 104.795 1.00 16.66 ?  675 HIS A CB    1 
ATOM   5437  C  CG    . HIS A 1 675 ? 155.401 130.140 105.253 1.00 17.85 ?  675 HIS A CG    1 
ATOM   5438  N  ND1   . HIS A 1 675 ? 156.672 129.623 105.128 1.00 21.81 ?  675 HIS A ND1   1 
ATOM   5439  C  CD2   . HIS A 1 675 ? 155.546 131.360 105.823 1.00 13.70 ?  675 HIS A CD2   1 
ATOM   5440  C  CE1   . HIS A 1 675 ? 157.547 130.489 105.606 1.00 22.54 ?  675 HIS A CE1   1 
ATOM   5441  N  NE2   . HIS A 1 675 ? 156.890 131.551 106.034 1.00 21.60 ?  675 HIS A NE2   1 
ATOM   5442  N  N     . HIS A 1 676 ? 155.236 128.980 101.817 1.00 19.54 ?  676 HIS A N     1 
ATOM   5443  C  CA    . HIS A 1 676 ? 156.316 129.060 100.839 1.00 13.67 ?  676 HIS A CA    1 
ATOM   5444  C  C     . HIS A 1 676 ? 155.901 129.863 99.613  1.00 17.84 ?  676 HIS A C     1 
ATOM   5445  O  O     . HIS A 1 676 ? 156.723 130.569 99.019  1.00 19.01 ?  676 HIS A O     1 
ATOM   5446  C  CB    . HIS A 1 676 ? 156.751 127.652 100.437 1.00 19.36 ?  676 HIS A CB    1 
ATOM   5447  C  CG    . HIS A 1 676 ? 157.690 127.614 99.272  1.00 24.14 ?  676 HIS A CG    1 
ATOM   5448  N  ND1   . HIS A 1 676 ? 158.992 128.059 99.349  1.00 23.04 ?  676 HIS A ND1   1 
ATOM   5449  C  CD2   . HIS A 1 676 ? 157.514 127.182 98.001  1.00 19.65 ?  676 HIS A CD2   1 
ATOM   5450  C  CE1   . HIS A 1 676 ? 159.579 127.901 98.177  1.00 25.39 ?  676 HIS A CE1   1 
ATOM   5451  N  NE2   . HIS A 1 676 ? 158.704 127.371 97.341  1.00 27.08 ?  676 HIS A NE2   1 
ATOM   5452  N  N     . ARG A 1 677 ? 154.635 129.767 99.218  1.00 19.33 ?  677 ARG A N     1 
ATOM   5453  C  CA    . ARG A 1 677 ? 154.153 130.395 97.996  1.00 15.91 ?  677 ARG A CA    1 
ATOM   5454  C  C     . ARG A 1 677 ? 153.687 131.829 98.201  1.00 16.61 ?  677 ARG A C     1 
ATOM   5455  O  O     . ARG A 1 677 ? 153.220 132.453 97.244  1.00 26.31 ?  677 ARG A O     1 
ATOM   5456  C  CB    . ARG A 1 677 ? 153.016 129.566 97.395  1.00 18.02 ?  677 ARG A CB    1 
ATOM   5457  C  CG    . ARG A 1 677 ? 153.482 128.315 96.675  1.00 20.37 ?  677 ARG A CG    1 
ATOM   5458  C  CD    . ARG A 1 677 ? 154.138 128.655 95.348  1.00 17.36 ?  677 ARG A CD    1 
ATOM   5459  N  NE    . ARG A 1 677 ? 153.202 129.282 94.423  1.00 22.72 ?  677 ARG A NE    1 
ATOM   5460  C  CZ    . ARG A 1 677 ? 153.358 130.494 93.907  1.00 28.42 ?  677 ARG A CZ    1 
ATOM   5461  N  NH1   . ARG A 1 677 ? 154.412 131.238 94.197  1.00 27.11 1  677 ARG A NH1   1 
ATOM   5462  N  NH2   . ARG A 1 677 ? 152.432 130.971 93.082  1.00 23.61 ?  677 ARG A NH2   1 
ATOM   5463  N  N     . GLY A 1 678 ? 153.802 132.366 99.411  1.00 20.75 ?  678 GLY A N     1 
ATOM   5464  C  CA    . GLY A 1 678 ? 153.392 133.725 99.685  1.00 8.11  ?  678 GLY A CA    1 
ATOM   5465  C  C     . GLY A 1 678 ? 151.995 133.888 100.237 1.00 6.78  ?  678 GLY A C     1 
ATOM   5466  O  O     . GLY A 1 678 ? 151.540 135.027 100.387 1.00 19.62 ?  678 GLY A O     1 
ATOM   5467  N  N     . ILE A 1 679 ? 151.299 132.792 100.547 1.00 11.83 ?  679 ILE A N     1 
ATOM   5468  C  CA    . ILE A 1 679 ? 149.947 132.891 101.078 1.00 6.57  ?  679 ILE A CA    1 
ATOM   5469  C  C     . ILE A 1 679 ? 149.982 133.636 102.403 1.00 14.24 ?  679 ILE A C     1 
ATOM   5470  O  O     . ILE A 1 679 ? 150.801 133.340 103.280 1.00 26.21 ?  679 ILE A O     1 
ATOM   5471  C  CB    . ILE A 1 679 ? 149.329 131.494 101.229 1.00 12.90 ?  679 ILE A CB    1 
ATOM   5472  C  CG1   . ILE A 1 679 ? 149.151 130.837 99.857  1.00 10.07 ?  679 ILE A CG1   1 
ATOM   5473  C  CG2   . ILE A 1 679 ? 148.004 131.570 101.969 1.00 9.37  ?  679 ILE A CG2   1 
ATOM   5474  C  CD1   . ILE A 1 679 ? 148.219 131.581 98.936  1.00 11.69 ?  679 ILE A CD1   1 
ATOM   5475  N  N     . LYS A 1 680 ? 149.089 134.614 102.553 1.00 10.38 ?  680 LYS A N     1 
ATOM   5476  C  CA    . LYS A 1 680 ? 149.094 135.449 103.748 1.00 0.00  ?  680 LYS A CA    1 
ATOM   5477  C  C     . LYS A 1 680 ? 148.312 134.806 104.886 1.00 2.35  ?  680 LYS A C     1 
ATOM   5478  O  O     . LYS A 1 680 ? 148.776 134.778 106.030 1.00 17.00 ?  680 LYS A O     1 
ATOM   5479  C  CB    . LYS A 1 680 ? 148.526 136.830 103.421 1.00 7.57  ?  680 LYS A CB    1 
ATOM   5480  C  CG    . LYS A 1 680 ? 149.455 137.714 102.611 1.00 1.39  ?  680 LYS A CG    1 
ATOM   5481  C  CD    . LYS A 1 680 ? 148.751 138.986 102.180 1.00 0.95  ?  680 LYS A CD    1 
ATOM   5482  C  CE    . LYS A 1 680 ? 149.627 139.826 101.269 1.00 3.31  ?  680 LYS A CE    1 
ATOM   5483  N  NZ    . LYS A 1 680 ? 148.907 141.030 100.775 1.00 7.74  1  680 LYS A NZ    1 
ATOM   5484  N  N     . THR A 1 681 ? 147.124 134.286 104.594 1.00 7.02  ?  681 THR A N     1 
ATOM   5485  C  CA    . THR A 1 681 ? 146.266 133.700 105.610 1.00 8.47  ?  681 THR A CA    1 
ATOM   5486  C  C     . THR A 1 681 ? 145.640 132.423 105.073 1.00 6.78  ?  681 THR A C     1 
ATOM   5487  O  O     . THR A 1 681 ? 145.488 132.249 103.862 1.00 23.08 ?  681 THR A O     1 
ATOM   5488  C  CB    . THR A 1 681 ? 145.157 134.672 106.053 1.00 18.71 ?  681 THR A CB    1 
ATOM   5489  O  OG1   . THR A 1 681 ? 144.495 135.205 104.899 1.00 20.93 ?  681 THR A OG1   1 
ATOM   5490  C  CG2   . THR A 1 681 ? 145.735 135.819 106.867 1.00 4.47  ?  681 THR A CG2   1 
ATOM   5491  N  N     . ILE A 1 682 ? 145.283 131.529 105.990 1.00 14.55 ?  682 ILE A N     1 
ATOM   5492  C  CA    . ILE A 1 682 ? 144.507 130.333 105.682 1.00 9.87  ?  682 ILE A CA    1 
ATOM   5493  C  C     . ILE A 1 682 ? 143.256 130.379 106.546 1.00 9.32  ?  682 ILE A C     1 
ATOM   5494  O  O     . ILE A 1 682 ? 143.350 130.497 107.773 1.00 16.81 ?  682 ILE A O     1 
ATOM   5495  C  CB    . ILE A 1 682 ? 145.308 129.047 105.932 1.00 11.95 ?  682 ILE A CB    1 
ATOM   5496  C  CG1   . ILE A 1 682 ? 146.679 129.135 105.261 1.00 6.77  ?  682 ILE A CG1   1 
ATOM   5497  C  CG2   . ILE A 1 682 ? 144.545 127.846 105.416 1.00 20.21 ?  682 ILE A CG2   1 
ATOM   5498  C  CD1   . ILE A 1 682 ? 147.582 127.966 105.568 1.00 22.66 ?  682 ILE A CD1   1 
ATOM   5499  N  N     . TYR A 1 683 ? 142.087 130.302 105.909 1.00 14.36 ?  683 TYR A N     1 
ATOM   5500  C  CA    . TYR A 1 683 ? 140.840 130.570 106.625 1.00 8.32  ?  683 TYR A CA    1 
ATOM   5501  C  C     . TYR A 1 683 ? 140.335 129.342 107.376 1.00 18.43 ?  683 TYR A C     1 
ATOM   5502  O  O     . TYR A 1 683 ? 140.292 129.326 108.608 1.00 34.55 ?  683 TYR A O     1 
ATOM   5503  C  CB    . TYR A 1 683 ? 139.781 131.077 105.641 1.00 10.02 ?  683 TYR A CB    1 
ATOM   5504  C  CG    . TYR A 1 683 ? 138.493 131.515 106.291 1.00 15.54 ?  683 TYR A CG    1 
ATOM   5505  C  CD1   . TYR A 1 683 ? 138.467 131.929 107.615 1.00 4.29  ?  683 TYR A CD1   1 
ATOM   5506  C  CD2   . TYR A 1 683 ? 137.302 131.526 105.579 1.00 11.18 ?  683 TYR A CD2   1 
ATOM   5507  C  CE1   . TYR A 1 683 ? 137.296 132.333 108.212 1.00 6.88  ?  683 TYR A CE1   1 
ATOM   5508  C  CE2   . TYR A 1 683 ? 136.124 131.933 106.169 1.00 15.90 ?  683 TYR A CE2   1 
ATOM   5509  C  CZ    . TYR A 1 683 ? 136.128 132.335 107.487 1.00 9.16  ?  683 TYR A CZ    1 
ATOM   5510  O  OH    . TYR A 1 683 ? 134.956 132.741 108.079 1.00 25.35 ?  683 TYR A OH    1 
ATOM   5511  N  N     . TYR A 1 684 ? 139.974 128.291 106.649 1.00 21.25 ?  684 TYR A N     1 
ATOM   5512  C  CA    . TYR A 1 684 ? 139.311 127.147 107.251 1.00 20.69 ?  684 TYR A CA    1 
ATOM   5513  C  C     . TYR A 1 684 ? 139.872 125.863 106.668 1.00 27.70 ?  684 TYR A C     1 
ATOM   5514  O  O     . TYR A 1 684 ? 140.332 125.826 105.525 1.00 27.91 ?  684 TYR A O     1 
ATOM   5515  C  CB    . TYR A 1 684 ? 137.794 127.182 107.029 1.00 22.55 ?  684 TYR A CB    1 
ATOM   5516  C  CG    . TYR A 1 684 ? 137.015 127.806 108.160 1.00 17.78 ?  684 TYR A CG    1 
ATOM   5517  C  CD1   . TYR A 1 684 ? 136.113 128.833 107.921 1.00 22.27 ?  684 TYR A CD1   1 
ATOM   5518  C  CD2   . TYR A 1 684 ? 137.178 127.369 109.466 1.00 24.81 ?  684 TYR A CD2   1 
ATOM   5519  C  CE1   . TYR A 1 684 ? 135.395 129.406 108.950 1.00 19.37 ?  684 TYR A CE1   1 
ATOM   5520  C  CE2   . TYR A 1 684 ? 136.465 127.937 110.504 1.00 28.52 ?  684 TYR A CE2   1 
ATOM   5521  C  CZ    . TYR A 1 684 ? 135.575 128.956 110.239 1.00 25.95 ?  684 TYR A CZ    1 
ATOM   5522  O  OH    . TYR A 1 684 ? 134.861 129.527 111.268 1.00 30.12 ?  684 TYR A OH    1 
ATOM   5523  N  N     . ALA A 1 685 ? 139.830 124.810 107.474 1.00 27.05 ?  685 ALA A N     1 
ATOM   5524  C  CA    . ALA A 1 685 ? 140.138 123.458 107.032 1.00 24.07 ?  685 ALA A CA    1 
ATOM   5525  C  C     . ALA A 1 685 ? 138.808 122.716 106.959 1.00 27.04 ?  685 ALA A C     1 
ATOM   5526  O  O     . ALA A 1 685 ? 138.301 122.218 107.965 1.00 37.09 ?  685 ALA A O     1 
ATOM   5527  C  CB    . ALA A 1 685 ? 141.122 122.777 107.973 1.00 25.34 ?  685 ALA A CB    1 
ATOM   5528  N  N     . ARG A 1 686 ? 138.239 122.656 105.759 1.00 27.20 ?  686 ARG A N     1 
ATOM   5529  C  CA    . ARG A 1 686 ? 136.997 121.935 105.526 1.00 27.31 ?  686 ARG A CA    1 
ATOM   5530  C  C     . ARG A 1 686 ? 137.313 120.520 105.066 1.00 35.40 ?  686 ARG A C     1 
ATOM   5531  O  O     . ARG A 1 686 ? 138.081 120.325 104.118 1.00 37.84 ?  686 ARG A O     1 
ATOM   5532  C  CB    . ARG A 1 686 ? 136.138 122.649 104.483 1.00 35.96 ?  686 ARG A CB    1 
ATOM   5533  C  CG    . ARG A 1 686 ? 135.452 123.904 104.986 1.00 35.93 ?  686 ARG A CG    1 
ATOM   5534  C  CD    . ARG A 1 686 ? 134.222 124.217 104.152 1.00 36.37 ?  686 ARG A CD    1 
ATOM   5535  N  NE    . ARG A 1 686 ? 133.170 123.224 104.339 1.00 40.91 ?  686 ARG A NE    1 
ATOM   5536  C  CZ    . ARG A 1 686 ? 131.912 123.514 104.642 1.00 40.00 ?  686 ARG A CZ    1 
ATOM   5537  N  NH1   . ARG A 1 686 ? 131.508 124.764 104.796 1.00 38.08 1  686 ARG A NH1   1 
ATOM   5538  N  NH2   . ARG A 1 686 ? 131.037 122.524 104.795 1.00 34.97 ?  686 ARG A NH2   1 
ATOM   5539  N  N     . THR A 1 687 ? 136.723 119.538 105.737 1.00 37.97 ?  687 THR A N     1 
ATOM   5540  C  CA    . THR A 1 687 ? 136.926 118.135 105.413 1.00 40.41 ?  687 THR A CA    1 
ATOM   5541  C  C     . THR A 1 687 ? 135.639 117.548 104.849 1.00 40.78 ?  687 THR A C     1 
ATOM   5542  O  O     . THR A 1 687 ? 134.549 117.803 105.369 1.00 44.07 ?  687 THR A O     1 
ATOM   5543  C  CB    . THR A 1 687 ? 137.369 117.340 106.644 1.00 41.96 ?  687 THR A CB    1 
ATOM   5544  O  OG1   . THR A 1 687 ? 138.591 117.888 107.153 1.00 44.55 ?  687 THR A OG1   1 
ATOM   5545  C  CG2   . THR A 1 687 ? 137.592 115.882 106.282 1.00 37.91 ?  687 THR A CG2   1 
ATOM   5546  N  N     . LYS A 1 688 ? 135.774 116.768 103.783 1.00 44.78 ?  688 LYS A N     1 
ATOM   5547  C  CA    . LYS A 1 688 ? 134.626 116.142 103.139 1.00 44.60 ?  688 LYS A CA    1 
ATOM   5548  C  C     . LYS A 1 688 ? 134.175 114.907 103.912 1.00 48.36 ?  688 LYS A C     1 
ATOM   5549  O  O     . LYS A 1 688 ? 134.971 114.271 104.602 1.00 49.47 ?  688 LYS A O     1 
ATOM   5550  C  CB    . LYS A 1 688 ? 134.962 115.767 101.695 1.00 44.44 ?  688 LYS A CB    1 
ATOM   5551  C  CG    . LYS A 1 688 ? 133.746 115.532 100.818 1.00 41.12 ?  688 LYS A CG    1 
ATOM   5552  C  CD    . LYS A 1 688 ? 134.075 114.595 99.670  1.00 42.19 ?  688 LYS A CD    1 
ATOM   5553  C  CE    . LYS A 1 688 ? 133.195 114.869 98.464  1.00 44.47 ?  688 LYS A CE    1 
ATOM   5554  N  NZ    . LYS A 1 688 ? 132.376 113.682 98.096  1.00 48.98 ?  688 LYS A NZ    1 
ATOM   5555  N  N     . VAL B 1 6   ? 153.946 117.460 163.879 1.00 71.22 ?  6   VAL B N     1 
ATOM   5556  C  CA    . VAL B 1 6   ? 152.937 118.408 164.332 1.00 71.80 ?  6   VAL B CA    1 
ATOM   5557  C  C     . VAL B 1 6   ? 153.547 119.426 165.287 1.00 71.79 ?  6   VAL B C     1 
ATOM   5558  O  O     . VAL B 1 6   ? 154.311 119.065 166.182 1.00 71.31 ?  6   VAL B O     1 
ATOM   5559  C  CB    . VAL B 1 6   ? 151.753 117.687 164.994 0.43 75.82 ?  6   VAL B CB    1 
ATOM   5560  C  CG1   . VAL B 1 6   ? 150.794 118.697 165.603 0.84 73.49 ?  6   VAL B CG1   1 
ATOM   5561  C  CG2   . VAL B 1 6   ? 151.036 116.812 163.979 0.98 74.68 ?  6   VAL B CG2   1 
ATOM   5562  N  N     . PRO B 1 7   ? 153.217 120.699 165.087 1.00 63.32 ?  7   PRO B N     1 
ATOM   5563  C  CA    . PRO B 1 7   ? 153.741 121.746 165.976 1.00 59.19 ?  7   PRO B CA    1 
ATOM   5564  C  C     . PRO B 1 7   ? 153.364 121.514 167.429 1.00 60.15 ?  7   PRO B C     1 
ATOM   5565  O  O     . PRO B 1 7   ? 152.292 120.977 167.723 1.00 62.72 ?  7   PRO B O     1 
ATOM   5566  C  CB    . PRO B 1 7   ? 153.093 123.028 165.438 1.00 61.28 ?  7   PRO B CB    1 
ATOM   5567  C  CG    . PRO B 1 7   ? 152.618 122.712 164.061 1.00 63.19 ?  7   PRO B CG    1 
ATOM   5568  C  CD    . PRO B 1 7   ? 152.685 121.238 163.825 1.00 62.23 ?  7   PRO B CD    1 
ATOM   5569  N  N     . LYS B 1 8   ? 154.243 121.917 168.349 1.00 58.92 ?  8   LYS B N     1 
ATOM   5570  C  CA    . LYS B 1 8   ? 153.966 121.730 169.770 1.00 58.81 ?  8   LYS B CA    1 
ATOM   5571  C  C     . LYS B 1 8   ? 152.725 122.501 170.201 1.00 60.29 ?  8   LYS B C     1 
ATOM   5572  O  O     . LYS B 1 8   ? 151.899 121.989 170.966 1.00 62.54 ?  8   LYS B O     1 
ATOM   5573  C  CB    . LYS B 1 8   ? 155.175 122.159 170.600 1.00 58.70 ?  8   LYS B CB    1 
ATOM   5574  C  CG    . LYS B 1 8   ? 154.931 122.161 172.098 1.00 59.51 ?  8   LYS B CG    1 
ATOM   5575  C  CD    . LYS B 1 8   ? 156.147 122.681 172.849 1.00 60.94 ?  8   LYS B CD    1 
ATOM   5576  C  CE    . LYS B 1 8   ? 155.874 122.787 174.339 1.00 59.69 ?  8   LYS B CE    1 
ATOM   5577  N  NZ    . LYS B 1 8   ? 157.030 123.366 175.078 1.00 58.68 1  8   LYS B NZ    1 
ATOM   5578  N  N     . TRP B 1 9   ? 152.576 123.738 169.720 1.00 59.06 ?  9   TRP B N     1 
ATOM   5579  C  CA    . TRP B 1 9   ? 151.406 124.528 170.088 1.00 54.81 ?  9   TRP B CA    1 
ATOM   5580  C  C     . TRP B 1 9   ? 150.126 123.873 169.589 1.00 54.14 ?  9   TRP B C     1 
ATOM   5581  O  O     . TRP B 1 9   ? 149.092 123.923 170.263 1.00 57.27 ?  9   TRP B O     1 
ATOM   5582  C  CB    . TRP B 1 9   ? 151.527 125.949 169.539 1.00 55.32 ?  9   TRP B CB    1 
ATOM   5583  C  CG    . TRP B 1 9   ? 151.895 126.021 168.092 1.00 52.28 ?  9   TRP B CG    1 
ATOM   5584  C  CD1   . TRP B 1 9   ? 151.038 126.096 167.033 1.00 51.80 ?  9   TRP B CD1   1 
ATOM   5585  C  CD2   . TRP B 1 9   ? 153.216 126.039 167.540 1.00 52.73 ?  9   TRP B CD2   1 
ATOM   5586  N  NE1   . TRP B 1 9   ? 151.744 126.156 165.857 1.00 51.91 ?  9   TRP B NE1   1 
ATOM   5587  C  CE2   . TRP B 1 9   ? 153.083 126.124 166.141 1.00 54.06 ?  9   TRP B CE2   1 
ATOM   5588  C  CE3   . TRP B 1 9   ? 154.498 125.992 168.095 1.00 52.40 ?  9   TRP B CE3   1 
ATOM   5589  C  CZ2   . TRP B 1 9   ? 154.182 126.158 165.288 1.00 53.08 ?  9   TRP B CZ2   1 
ATOM   5590  C  CZ3   . TRP B 1 9   ? 155.588 126.027 167.246 1.00 54.60 ?  9   TRP B CZ3   1 
ATOM   5591  C  CH2   . TRP B 1 9   ? 155.423 126.109 165.859 1.00 54.01 ?  9   TRP B CH2   1 
ATOM   5592  N  N     . ILE B 1 10  ? 150.173 123.264 168.405 1.00 57.82 ?  10  ILE B N     1 
ATOM   5593  C  CA    . ILE B 1 10  ? 148.993 122.592 167.872 1.00 58.12 ?  10  ILE B CA    1 
ATOM   5594  C  C     . ILE B 1 10  ? 148.647 121.370 168.713 1.00 57.87 ?  10  ILE B C     1 
ATOM   5595  O  O     . ILE B 1 10  ? 147.468 121.068 168.936 1.00 59.84 ?  10  ILE B O     1 
ATOM   5596  C  CB    . ILE B 1 10  ? 149.211 122.227 166.394 1.00 56.85 ?  10  ILE B CB    1 
ATOM   5597  C  CG1   . ILE B 1 10  ? 148.740 123.371 165.496 1.00 58.22 ?  10  ILE B CG1   1 
ATOM   5598  C  CG2   . ILE B 1 10  ? 148.481 120.942 166.053 1.00 57.86 ?  10  ILE B CG2   1 
ATOM   5599  C  CD1   . ILE B 1 10  ? 148.999 123.141 164.030 1.00 59.43 ?  10  ILE B CD1   1 
ATOM   5600  N  N     . GLN B 1 11  ? 149.661 120.644 169.189 1.00 60.46 ?  11  GLN B N     1 
ATOM   5601  C  CA    . GLN B 1 11  ? 149.398 119.528 170.091 1.00 61.16 ?  11  GLN B CA    1 
ATOM   5602  C  C     . GLN B 1 11  ? 148.775 120.013 171.393 1.00 60.47 ?  11  GLN B C     1 
ATOM   5603  O  O     . GLN B 1 11  ? 147.854 119.381 171.923 1.00 62.33 ?  11  GLN B O     1 
ATOM   5604  C  CB    . GLN B 1 11  ? 150.684 118.751 170.367 1.00 61.84 ?  11  GLN B CB    1 
ATOM   5605  C  CG    . GLN B 1 11  ? 151.240 118.022 169.156 1.00 64.00 ?  11  GLN B CG    1 
ATOM   5606  C  CD    . GLN B 1 11  ? 152.551 117.323 169.448 1.00 65.38 ?  11  GLN B CD    1 
ATOM   5607  O  OE1   . GLN B 1 11  ? 153.286 117.713 170.354 1.00 63.22 ?  11  GLN B OE1   1 
ATOM   5608  N  NE2   . GLN B 1 11  ? 152.851 116.282 168.679 1.00 63.35 ?  11  GLN B NE2   1 
ATOM   5609  N  N     . LEU B 1 12  ? 149.266 121.133 171.925 1.00 59.28 ?  12  LEU B N     1 
ATOM   5610  C  CA    . LEU B 1 12  ? 148.664 121.695 173.129 1.00 57.80 ?  12  LEU B CA    1 
ATOM   5611  C  C     . LEU B 1 12  ? 147.213 122.091 172.884 1.00 59.59 ?  12  LEU B C     1 
ATOM   5612  O  O     . LEU B 1 12  ? 146.343 121.854 173.729 1.00 60.35 ?  12  LEU B O     1 
ATOM   5613  C  CB    . LEU B 1 12  ? 149.476 122.897 173.610 1.00 56.35 ?  12  LEU B CB    1 
ATOM   5614  C  CG    . LEU B 1 12  ? 150.737 122.589 174.418 1.00 57.99 ?  12  LEU B CG    1 
ATOM   5615  C  CD1   . LEU B 1 12  ? 151.665 123.792 174.440 1.00 58.06 ?  12  LEU B CD1   1 
ATOM   5616  C  CD2   . LEU B 1 12  ? 150.375 122.160 175.831 1.00 58.85 ?  12  LEU B CD2   1 
ATOM   5617  N  N     . ASN B 1 13  ? 146.935 122.700 171.729 1.00 57.31 ?  13  ASN B N     1 
ATOM   5618  C  CA    . ASN B 1 13  ? 145.572 123.102 171.402 1.00 54.74 ?  13  ASN B CA    1 
ATOM   5619  C  C     . ASN B 1 13  ? 144.660 121.890 171.259 1.00 58.08 ?  13  ASN B C     1 
ATOM   5620  O  O     . ASN B 1 13  ? 143.527 121.890 171.754 1.00 62.06 ?  13  ASN B O     1 
ATOM   5621  C  CB    . ASN B 1 13  ? 145.570 123.937 170.122 1.00 57.67 ?  13  ASN B CB    1 
ATOM   5622  C  CG    . ASN B 1 13  ? 144.173 124.189 169.593 1.00 56.43 ?  13  ASN B CG    1 
ATOM   5623  O  OD1   . ASN B 1 13  ? 143.707 123.501 168.688 1.00 57.89 ?  13  ASN B OD1   1 
ATOM   5624  N  ND2   . ASN B 1 13  ? 143.500 125.185 170.154 1.00 55.93 ?  13  ASN B ND2   1 
ATOM   5625  N  N     . ASN B 1 14  ? 145.136 120.844 170.579 1.00 60.09 ?  14  ASN B N     1 
ATOM   5626  C  CA    . ASN B 1 14  ? 144.328 119.642 170.410 1.00 57.54 ?  14  ASN B CA    1 
ATOM   5627  C  C     . ASN B 1 14  ? 143.994 118.985 171.740 1.00 58.65 ?  14  ASN B C     1 
ATOM   5628  O  O     . ASN B 1 14  ? 143.029 118.218 171.815 1.00 61.30 ?  14  ASN B O     1 
ATOM   5629  C  CB    . ASN B 1 14  ? 145.045 118.647 169.498 1.00 58.96 ?  14  ASN B CB    1 
ATOM   5630  C  CG    . ASN B 1 14  ? 145.092 119.110 168.056 1.00 59.82 ?  14  ASN B CG    1 
ATOM   5631  O  OD1   . ASN B 1 14  ? 145.725 118.481 167.210 1.00 60.88 ?  14  ASN B OD1   1 
ATOM   5632  N  ND2   . ASN B 1 14  ? 144.420 120.217 167.770 1.00 60.27 ?  14  ASN B ND2   1 
ATOM   5633  N  N     . GLU B 1 15  ? 144.766 119.268 172.789 1.00 63.90 ?  15  GLU B N     1 
ATOM   5634  C  CA    . GLU B 1 15  ? 144.437 118.780 174.121 1.00 63.78 ?  15  GLU B CA    1 
ATOM   5635  C  C     . GLU B 1 15  ? 143.176 119.426 174.675 1.00 65.18 ?  15  GLU B C     1 
ATOM   5636  O  O     . GLU B 1 15  ? 142.662 118.964 175.699 1.00 64.21 ?  15  GLU B O     1 
ATOM   5637  C  CB    . GLU B 1 15  ? 145.610 119.026 175.072 1.00 63.55 ?  15  GLU B CB    1 
ATOM   5638  C  CG    . GLU B 1 15  ? 145.432 118.417 176.453 1.00 65.72 ?  15  GLU B CG    1 
ATOM   5639  C  CD    . GLU B 1 15  ? 146.752 118.018 177.085 1.00 67.86 ?  15  GLU B CD    1 
ATOM   5640  O  OE1   . GLU B 1 15  ? 146.770 117.039 177.862 1.00 66.86 ?  15  GLU B OE1   1 
ATOM   5641  O  OE2   . GLU B 1 15  ? 147.772 118.682 176.806 1.00 67.63 -1 15  GLU B OE2   1 
ATOM   5642  N  N     . ILE B 1 16  ? 142.674 120.481 174.030 1.00 64.83 ?  16  ILE B N     1 
ATOM   5643  C  CA    . ILE B 1 16  ? 141.418 121.094 174.453 1.00 62.78 ?  16  ILE B CA    1 
ATOM   5644  C  C     . ILE B 1 16  ? 140.304 120.055 174.459 1.00 63.00 ?  16  ILE B C     1 
ATOM   5645  O  O     . ILE B 1 16  ? 139.546 119.932 175.428 1.00 63.39 ?  16  ILE B O     1 
ATOM   5646  C  CB    . ILE B 1 16  ? 141.068 122.282 173.539 1.00 62.92 ?  16  ILE B CB    1 
ATOM   5647  C  CG1   . ILE B 1 16  ? 142.035 123.447 173.757 1.00 61.45 ?  16  ILE B CG1   1 
ATOM   5648  C  CG2   . ILE B 1 16  ? 139.633 122.731 173.777 1.00 63.29 ?  16  ILE B CG2   1 
ATOM   5649  C  CD1   . ILE B 1 16  ? 141.891 124.117 175.095 1.00 61.70 ?  16  ILE B CD1   1 
ATOM   5650  N  N     . MET B 1 17  ? 140.196 119.287 173.373 1.00 64.80 ?  17  MET B N     1 
ATOM   5651  C  CA    . MET B 1 17  ? 139.106 118.331 173.227 1.00 65.03 ?  17  MET B CA    1 
ATOM   5652  C  C     . MET B 1 17  ? 139.287 117.094 174.094 1.00 64.56 ?  17  MET B C     1 
ATOM   5653  O  O     . MET B 1 17  ? 138.304 116.394 174.361 1.00 64.64 ?  17  MET B O     1 
ATOM   5654  C  CB    . MET B 1 17  ? 138.967 117.923 171.761 1.00 65.08 ?  17  MET B CB    1 
ATOM   5655  C  CG    . MET B 1 17  ? 138.500 119.045 170.855 1.00 64.77 ?  17  MET B CG    1 
ATOM   5656  S  SD    . MET B 1 17  ? 137.435 120.223 171.704 1.00 70.79 ?  17  MET B SD    1 
ATOM   5657  C  CE    . MET B 1 17  ? 135.829 119.716 171.096 1.00 65.85 ?  17  MET B CE    1 
ATOM   5658  N  N     . ILE B 1 18  ? 140.508 116.806 174.538 1.00 65.95 ?  18  ILE B N     1 
ATOM   5659  C  CA    . ILE B 1 18  ? 140.754 115.639 175.377 1.00 67.12 ?  18  ILE B CA    1 
ATOM   5660  C  C     . ILE B 1 18  ? 140.125 115.883 176.740 1.00 67.95 ?  18  ILE B C     1 
ATOM   5661  O  O     . ILE B 1 18  ? 140.643 116.661 177.548 1.00 69.06 ?  18  ILE B O     1 
ATOM   5662  C  CB    . ILE B 1 18  ? 142.258 115.338 175.498 1.00 67.46 ?  18  ILE B CB    1 
ATOM   5663  C  CG1   . ILE B 1 18  ? 142.752 114.592 174.258 1.00 67.61 ?  18  ILE B CG1   1 
ATOM   5664  C  CG2   . ILE B 1 18  ? 142.541 114.534 176.755 1.00 66.97 ?  18  ILE B CG2   1 
ATOM   5665  C  CD1   . ILE B 1 18  ? 144.092 115.073 173.749 1.00 68.44 ?  18  ILE B CD1   1 
ATOM   5666  N  N     . GLN B 1 19  ? 139.003 115.220 177.003 1.00 71.29 ?  19  GLN B N     1 
ATOM   5667  C  CA    . GLN B 1 19  ? 138.267 115.452 178.238 1.00 71.26 ?  19  GLN B CA    1 
ATOM   5668  C  C     . GLN B 1 19  ? 139.049 114.921 179.432 1.00 72.15 ?  19  GLN B C     1 
ATOM   5669  O  O     . GLN B 1 19  ? 139.545 113.791 179.413 1.00 74.43 ?  19  GLN B O     1 
ATOM   5670  C  CB    . GLN B 1 19  ? 136.893 114.790 178.166 1.00 71.94 ?  19  GLN B CB    1 
ATOM   5671  C  CG    . GLN B 1 19  ? 135.970 115.392 177.118 1.00 70.92 ?  19  GLN B CG    1 
ATOM   5672  C  CD    . GLN B 1 19  ? 134.956 116.346 177.717 1.00 72.03 ?  19  GLN B CD    1 
ATOM   5673  O  OE1   . GLN B 1 19  ? 135.150 117.561 177.707 1.00 72.82 ?  19  GLN B OE1   1 
ATOM   5674  N  NE2   . GLN B 1 19  ? 133.866 115.800 178.241 1.00 72.55 ?  19  GLN B NE2   1 
ATOM   5675  N  N     . LYS B 1 20  ? 139.159 115.744 180.471 1.00 74.08 ?  20  LYS B N     1 
ATOM   5676  C  CA    . LYS B 1 20  ? 139.792 115.356 181.725 1.00 75.80 ?  20  LYS B CA    1 
ATOM   5677  C  C     . LYS B 1 20  ? 138.799 115.606 182.848 1.00 76.47 ?  20  LYS B C     1 
ATOM   5678  O  O     . LYS B 1 20  ? 138.338 116.739 183.028 1.00 74.85 ?  20  LYS B O     1 
ATOM   5679  C  CB    . LYS B 1 20  ? 141.089 116.135 181.956 1.00 73.30 ?  20  LYS B CB    1 
ATOM   5680  C  CG    . LYS B 1 20  ? 141.297 116.598 183.387 1.00 73.86 ?  20  LYS B CG    1 
ATOM   5681  C  CD    . LYS B 1 20  ? 142.774 116.808 183.680 1.00 75.64 ?  20  LYS B CD    1 
ATOM   5682  C  CE    . LYS B 1 20  ? 142.984 117.505 185.013 1.00 76.33 ?  20  LYS B CE    1 
ATOM   5683  N  NZ    . LYS B 1 20  ? 144.382 117.350 185.500 1.00 75.39 1  20  LYS B NZ    1 
ATOM   5684  N  N     . ASP B 1 21  ? 138.472 114.557 183.600 1.00 78.89 ?  21  ASP B N     1 
ATOM   5685  C  CA    . ASP B 1 21  ? 137.416 114.628 184.607 1.00 78.53 ?  21  ASP B CA    1 
ATOM   5686  C  C     . ASP B 1 21  ? 136.076 114.971 183.957 1.00 78.34 ?  21  ASP B C     1 
ATOM   5687  O  O     . ASP B 1 21  ? 135.245 115.678 184.530 1.00 76.62 ?  21  ASP B O     1 
ATOM   5688  C  CB    . ASP B 1 21  ? 137.766 115.637 185.704 1.00 78.82 ?  21  ASP B CB    1 
ATOM   5689  C  CG    . ASP B 1 21  ? 136.819 115.571 186.887 1.00 79.68 ?  21  ASP B CG    1 
ATOM   5690  O  OD1   . ASP B 1 21  ? 135.897 114.727 186.868 1.00 79.69 ?  21  ASP B OD1   1 
ATOM   5691  O  OD2   . ASP B 1 21  ? 136.994 116.363 187.836 1.00 78.43 -1 21  ASP B OD2   1 
ATOM   5692  N  N     . GLY B 1 22  ? 135.870 114.467 182.742 1.00 75.88 ?  22  GLY B N     1 
ATOM   5693  C  CA    . GLY B 1 22  ? 134.659 114.760 182.003 1.00 75.32 ?  22  GLY B CA    1 
ATOM   5694  C  C     . GLY B 1 22  ? 134.501 116.202 181.583 1.00 75.66 ?  22  GLY B C     1 
ATOM   5695  O  O     . GLY B 1 22  ? 133.398 116.601 181.197 1.00 74.57 ?  22  GLY B O     1 
ATOM   5696  N  N     . LYS B 1 23  ? 135.566 116.998 181.644 1.00 71.81 ?  23  LYS B N     1 
ATOM   5697  C  CA    . LYS B 1 23  ? 135.509 118.417 181.329 1.00 69.41 ?  23  LYS B CA    1 
ATOM   5698  C  C     . LYS B 1 23  ? 136.571 118.757 180.296 1.00 70.13 ?  23  LYS B C     1 
ATOM   5699  O  O     . LYS B 1 23  ? 137.676 118.207 180.325 1.00 71.59 ?  23  LYS B O     1 
ATOM   5700  C  CB    . LYS B 1 23  ? 135.713 119.271 182.585 1.00 69.88 ?  23  LYS B CB    1 
ATOM   5701  C  CG    . LYS B 1 23  ? 134.452 119.497 183.397 1.00 69.55 ?  23  LYS B CG    1 
ATOM   5702  C  CD    . LYS B 1 23  ? 134.547 120.780 184.203 1.00 69.23 ?  23  LYS B CD    1 
ATOM   5703  C  CE    . LYS B 1 23  ? 134.564 120.493 185.694 1.00 70.35 ?  23  LYS B CE    1 
ATOM   5704  N  NZ    . LYS B 1 23  ? 135.476 121.416 186.423 1.00 69.04 1  23  LYS B NZ    1 
ATOM   5705  N  N     . PHE B 1 24  ? 136.232 119.666 179.388 1.00 65.90 ?  24  PHE B N     1 
ATOM   5706  C  CA    . PHE B 1 24  ? 137.192 120.120 178.394 1.00 63.90 ?  24  PHE B CA    1 
ATOM   5707  C  C     . PHE B 1 24  ? 138.342 120.857 179.069 1.00 64.99 ?  24  PHE B C     1 
ATOM   5708  O  O     . PHE B 1 24  ? 138.142 121.613 180.023 1.00 63.07 ?  24  PHE B O     1 
ATOM   5709  C  CB    . PHE B 1 24  ? 136.512 121.031 177.372 1.00 61.73 ?  24  PHE B CB    1 
ATOM   5710  C  CG    . PHE B 1 24  ? 135.694 120.293 176.352 1.00 62.89 ?  24  PHE B CG    1 
ATOM   5711  C  CD1   . PHE B 1 24  ? 136.307 119.588 175.332 1.00 64.72 ?  24  PHE B CD1   1 
ATOM   5712  C  CD2   . PHE B 1 24  ? 134.312 120.305 176.414 1.00 63.05 ?  24  PHE B CD2   1 
ATOM   5713  C  CE1   . PHE B 1 24  ? 135.557 118.909 174.393 1.00 63.96 ?  24  PHE B CE1   1 
ATOM   5714  C  CE2   . PHE B 1 24  ? 133.558 119.628 175.478 1.00 62.28 ?  24  PHE B CE2   1 
ATOM   5715  C  CZ    . PHE B 1 24  ? 134.181 118.929 174.467 1.00 62.62 ?  24  PHE B CZ    1 
ATOM   5716  N  N     . GLN B 1 25  ? 139.554 120.630 178.568 1.00 66.03 ?  25  GLN B N     1 
ATOM   5717  C  CA    . GLN B 1 25  ? 140.750 121.273 179.111 1.00 64.65 ?  25  GLN B CA    1 
ATOM   5718  C  C     . GLN B 1 25  ? 140.934 122.639 178.452 1.00 64.47 ?  25  GLN B C     1 
ATOM   5719  O  O     . GLN B 1 25  ? 141.789 122.850 177.591 1.00 67.27 ?  25  GLN B O     1 
ATOM   5720  C  CB    . GLN B 1 25  ? 141.969 120.382 178.911 1.00 65.60 ?  25  GLN B CB    1 
ATOM   5721  C  CG    . GLN B 1 25  ? 141.889 119.049 179.632 1.00 65.05 ?  25  GLN B CG    1 
ATOM   5722  C  CD    . GLN B 1 25  ? 143.053 118.139 179.297 1.00 66.24 ?  25  GLN B CD    1 
ATOM   5723  O  OE1   . GLN B 1 25  ? 144.108 118.205 179.927 1.00 65.74 ?  25  GLN B OE1   1 
ATOM   5724  N  NE2   . GLN B 1 25  ? 142.865 117.281 178.301 1.00 65.73 ?  25  GLN B NE2   1 
ATOM   5725  N  N     . PHE B 1 26  ? 140.101 123.585 178.888 1.00 56.80 ?  26  PHE B N     1 
ATOM   5726  C  CA    . PHE B 1 26  ? 140.119 124.916 178.293 1.00 57.18 ?  26  PHE B CA    1 
ATOM   5727  C  C     . PHE B 1 26  ? 141.416 125.655 178.592 1.00 58.23 ?  26  PHE B C     1 
ATOM   5728  O  O     . PHE B 1 26  ? 141.863 126.471 177.778 1.00 57.57 ?  26  PHE B O     1 
ATOM   5729  C  CB    . PHE B 1 26  ? 138.919 125.726 178.784 1.00 55.35 ?  26  PHE B CB    1 
ATOM   5730  C  CG    . PHE B 1 26  ? 137.601 125.223 178.269 1.00 55.07 ?  26  PHE B CG    1 
ATOM   5731  C  CD1   . PHE B 1 26  ? 137.400 125.033 176.912 1.00 54.07 ?  26  PHE B CD1   1 
ATOM   5732  C  CD2   . PHE B 1 26  ? 136.563 124.940 179.140 1.00 54.85 ?  26  PHE B CD2   1 
ATOM   5733  C  CE1   . PHE B 1 26  ? 136.190 124.572 176.435 1.00 55.22 ?  26  PHE B CE1   1 
ATOM   5734  C  CE2   . PHE B 1 26  ? 135.351 124.479 178.668 1.00 55.24 ?  26  PHE B CE2   1 
ATOM   5735  C  CZ    . PHE B 1 26  ? 135.164 124.294 177.314 1.00 54.19 ?  26  PHE B CZ    1 
ATOM   5736  N  N     . ASP B 1 27  ? 142.038 125.386 179.743 1.00 63.25 ?  27  ASP B N     1 
ATOM   5737  C  CA    . ASP B 1 27  ? 143.298 126.041 180.074 1.00 61.34 ?  27  ASP B CA    1 
ATOM   5738  C  C     . ASP B 1 27  ? 144.412 125.669 179.104 1.00 61.34 ?  27  ASP B C     1 
ATOM   5739  O  O     . ASP B 1 27  ? 145.438 126.357 179.064 1.00 62.82 ?  27  ASP B O     1 
ATOM   5740  C  CB    . ASP B 1 27  ? 143.715 125.690 181.503 1.00 62.48 ?  27  ASP B CB    1 
ATOM   5741  C  CG    . ASP B 1 27  ? 143.444 124.240 181.849 1.00 67.13 ?  27  ASP B CG    1 
ATOM   5742  O  OD1   . ASP B 1 27  ? 142.298 123.784 181.651 1.00 67.32 ?  27  ASP B OD1   1 
ATOM   5743  O  OD2   . ASP B 1 27  ? 144.378 123.554 182.317 1.00 64.32 -1 27  ASP B OD2   1 
ATOM   5744  N  N     . LYS B 1 28  ? 144.236 124.599 178.327 1.00 59.53 ?  28  LYS B N     1 
ATOM   5745  C  CA    . LYS B 1 28  ? 145.260 124.195 177.373 1.00 61.01 ?  28  LYS B CA    1 
ATOM   5746  C  C     . LYS B 1 28  ? 145.417 125.190 176.231 1.00 63.11 ?  28  LYS B C     1 
ATOM   5747  O  O     . LYS B 1 28  ? 146.445 125.171 175.548 1.00 64.90 ?  28  LYS B O     1 
ATOM   5748  C  CB    . LYS B 1 28  ? 144.938 122.809 176.812 1.00 60.60 ?  28  LYS B CB    1 
ATOM   5749  C  CG    . LYS B 1 28  ? 145.296 121.665 177.743 1.00 63.35 ?  28  LYS B CG    1 
ATOM   5750  C  CD    . LYS B 1 28  ? 146.795 121.440 177.790 1.00 63.05 ?  28  LYS B CD    1 
ATOM   5751  C  CE    . LYS B 1 28  ? 147.218 120.854 179.126 1.00 63.28 ?  28  LYS B CE    1 
ATOM   5752  N  NZ    . LYS B 1 28  ? 146.815 121.728 180.261 1.00 61.44 1  28  LYS B NZ    1 
ATOM   5753  N  N     . ASP B 1 29  ? 144.423 126.051 176.005 1.00 58.76 ?  29  ASP B N     1 
ATOM   5754  C  CA    . ASP B 1 29  ? 144.523 127.019 174.917 1.00 54.37 ?  29  ASP B CA    1 
ATOM   5755  C  C     . ASP B 1 29  ? 145.492 128.142 175.263 1.00 55.40 ?  29  ASP B C     1 
ATOM   5756  O  O     . ASP B 1 29  ? 146.216 128.633 174.390 1.00 56.37 ?  29  ASP B O     1 
ATOM   5757  C  CB    . ASP B 1 29  ? 143.141 127.579 174.585 1.00 54.64 ?  29  ASP B CB    1 
ATOM   5758  C  CG    . ASP B 1 29  ? 142.969 127.865 173.107 1.00 57.44 ?  29  ASP B CG    1 
ATOM   5759  O  OD1   . ASP B 1 29  ? 143.529 127.110 172.285 1.00 58.95 ?  29  ASP B OD1   1 
ATOM   5760  O  OD2   . ASP B 1 29  ? 142.268 128.839 172.767 1.00 56.07 -1 29  ASP B OD2   1 
ATOM   5761  N  N     . LYS B 1 30  ? 145.519 128.565 176.528 1.00 55.49 ?  30  LYS B N     1 
ATOM   5762  C  CA    . LYS B 1 30  ? 146.515 129.545 176.949 1.00 55.27 ?  30  LYS B CA    1 
ATOM   5763  C  C     . LYS B 1 30  ? 147.923 128.987 176.793 1.00 56.41 ?  30  LYS B C     1 
ATOM   5764  O  O     . LYS B 1 30  ? 148.821 129.672 176.290 1.00 57.78 ?  30  LYS B O     1 
ATOM   5765  C  CB    . LYS B 1 30  ? 146.260 129.967 178.396 1.00 56.36 ?  30  LYS B CB    1 
ATOM   5766  C  CG    . LYS B 1 30  ? 147.451 130.633 179.068 1.00 58.91 ?  30  LYS B CG    1 
ATOM   5767  C  CD    . LYS B 1 30  ? 147.713 132.016 178.494 1.00 59.23 ?  30  LYS B CD    1 
ATOM   5768  C  CE    . LYS B 1 30  ? 149.179 132.398 178.624 1.00 58.72 ?  30  LYS B CE    1 
ATOM   5769  N  NZ    . LYS B 1 30  ? 149.732 132.948 177.354 1.00 56.91 1  30  LYS B NZ    1 
ATOM   5770  N  N     . GLU B 1 31  ? 148.130 127.735 177.208 1.00 56.55 ?  31  GLU B N     1 
ATOM   5771  C  CA    . GLU B 1 31  ? 149.412 127.085 176.966 1.00 56.86 ?  31  GLU B CA    1 
ATOM   5772  C  C     . GLU B 1 31  ? 149.679 126.954 175.474 1.00 56.41 ?  31  GLU B C     1 
ATOM   5773  O  O     . GLU B 1 31  ? 150.817 127.124 175.022 1.00 56.82 ?  31  GLU B O     1 
ATOM   5774  C  CB    . GLU B 1 31  ? 149.447 125.713 177.638 1.00 57.67 ?  31  GLU B CB    1 
ATOM   5775  C  CG    . GLU B 1 31  ? 149.656 125.757 179.141 1.00 59.14 ?  31  GLU B CG    1 
ATOM   5776  C  CD    . GLU B 1 31  ? 148.932 124.637 179.859 1.00 62.13 ?  31  GLU B CD    1 
ATOM   5777  O  OE1   . GLU B 1 31  ? 148.887 123.513 179.317 1.00 62.68 ?  31  GLU B OE1   1 
ATOM   5778  O  OE2   . GLU B 1 31  ? 148.411 124.879 180.968 1.00 60.15 -1 31  GLU B OE2   1 
ATOM   5779  N  N     . ALA B 1 32  ? 148.643 126.649 174.692 1.00 51.13 ?  32  ALA B N     1 
ATOM   5780  C  CA    . ALA B 1 32  ? 148.820 126.534 173.250 1.00 48.66 ?  32  ALA B CA    1 
ATOM   5781  C  C     . ALA B 1 32  ? 149.265 127.857 172.641 1.00 49.72 ?  32  ALA B C     1 
ATOM   5782  O  O     . ALA B 1 32  ? 150.174 127.886 171.806 1.00 48.78 ?  32  ALA B O     1 
ATOM   5783  C  CB    . ALA B 1 32  ? 147.525 126.050 172.597 1.00 50.11 ?  32  ALA B CB    1 
ATOM   5784  N  N     . VAL B 1 33  ? 148.648 128.965 173.054 1.00 53.80 ?  33  VAL B N     1 
ATOM   5785  C  CA    . VAL B 1 33  ? 149.021 130.266 172.502 1.00 51.79 ?  33  VAL B CA    1 
ATOM   5786  C  C     . VAL B 1 33  ? 150.422 130.661 172.955 1.00 52.05 ?  33  VAL B C     1 
ATOM   5787  O  O     . VAL B 1 33  ? 151.212 131.204 172.172 1.00 51.98 ?  33  VAL B O     1 
ATOM   5788  C  CB    . VAL B 1 33  ? 147.974 131.330 172.876 1.00 48.71 ?  33  VAL B CB    1 
ATOM   5789  C  CG1   . VAL B 1 33  ? 148.111 131.738 174.333 1.00 50.36 ?  33  VAL B CG1   1 
ATOM   5790  C  CG2   . VAL B 1 33  ? 148.104 132.542 171.970 1.00 50.20 ?  33  VAL B CG2   1 
ATOM   5791  N  N     . HIS B 1 34  ? 150.752 130.404 174.222 1.00 51.12 ?  34  HIS B N     1 
ATOM   5792  C  CA    . HIS B 1 34  ? 152.091 130.722 174.706 1.00 50.31 ?  34  HIS B CA    1 
ATOM   5793  C  C     . HIS B 1 34  ? 153.152 129.932 173.950 1.00 53.18 ?  34  HIS B C     1 
ATOM   5794  O  O     . HIS B 1 34  ? 154.187 130.484 173.558 1.00 54.82 ?  34  HIS B O     1 
ATOM   5795  C  CB    . HIS B 1 34  ? 152.188 130.448 176.205 1.00 54.11 ?  34  HIS B CB    1 
ATOM   5796  C  CG    . HIS B 1 34  ? 153.470 130.913 176.821 1.00 55.25 ?  34  HIS B CG    1 
ATOM   5797  N  ND1   . HIS B 1 34  ? 154.538 130.070 177.042 1.00 53.96 ?  34  HIS B ND1   1 
ATOM   5798  C  CD2   . HIS B 1 34  ? 153.856 132.131 177.267 1.00 55.26 ?  34  HIS B CD2   1 
ATOM   5799  C  CE1   . HIS B 1 34  ? 155.526 130.750 177.595 1.00 54.06 ?  34  HIS B CE1   1 
ATOM   5800  N  NE2   . HIS B 1 34  ? 155.138 132.003 177.741 1.00 56.25 ?  34  HIS B NE2   1 
ATOM   5801  N  N     . SER B 1 35  ? 152.915 128.635 173.745 1.00 55.43 ?  35  SER B N     1 
ATOM   5802  C  CA    . SER B 1 35  ? 153.851 127.821 172.980 1.00 52.25 ?  35  SER B CA    1 
ATOM   5803  C  C     . SER B 1 35  ? 153.947 128.306 171.542 1.00 52.47 ?  35  SER B C     1 
ATOM   5804  O  O     . SER B 1 35  ? 155.047 128.417 170.989 1.00 55.50 ?  35  SER B O     1 
ATOM   5805  C  CB    . SER B 1 35  ? 153.428 126.353 173.024 1.00 54.18 ?  35  SER B CB    1 
ATOM   5806  O  OG    . SER B 1 35  ? 154.038 125.619 171.981 1.00 57.69 ?  35  SER B OG    1 
ATOM   5807  N  N     . TYR B 1 36  ? 152.804 128.603 170.919 1.00 52.24 ?  36  TYR B N     1 
ATOM   5808  C  CA    . TYR B 1 36  ? 152.809 129.134 169.563 1.00 49.64 ?  36  TYR B CA    1 
ATOM   5809  C  C     . TYR B 1 36  ? 153.709 130.352 169.468 1.00 48.93 ?  36  TYR B C     1 
ATOM   5810  O  O     . TYR B 1 36  ? 154.610 130.411 168.625 1.00 50.52 ?  36  TYR B O     1 
ATOM   5811  C  CB    . TYR B 1 36  ? 151.383 129.487 169.141 1.00 48.54 ?  36  TYR B CB    1 
ATOM   5812  C  CG    . TYR B 1 36  ? 151.281 130.172 167.799 1.00 48.68 ?  36  TYR B CG    1 
ATOM   5813  C  CD1   . TYR B 1 36  ? 151.724 129.550 166.641 1.00 48.99 ?  36  TYR B CD1   1 
ATOM   5814  C  CD2   . TYR B 1 36  ? 150.736 131.445 167.690 1.00 47.07 ?  36  TYR B CD2   1 
ATOM   5815  C  CE1   . TYR B 1 36  ? 151.629 130.174 165.414 1.00 47.59 ?  36  TYR B CE1   1 
ATOM   5816  C  CE2   . TYR B 1 36  ? 150.636 132.077 166.468 1.00 46.68 ?  36  TYR B CE2   1 
ATOM   5817  C  CZ    . TYR B 1 36  ? 151.082 131.437 165.333 1.00 48.68 ?  36  TYR B CZ    1 
ATOM   5818  O  OH    . TYR B 1 36  ? 150.986 132.064 164.114 1.00 49.59 ?  36  TYR B OH    1 
ATOM   5819  N  N     . PHE B 1 37  ? 153.501 131.326 170.352 1.00 53.82 ?  37  PHE B N     1 
ATOM   5820  C  CA    . PHE B 1 37  ? 154.342 132.514 170.332 1.00 53.91 ?  37  PHE B CA    1 
ATOM   5821  C  C     . PHE B 1 37  ? 155.805 132.142 170.517 1.00 53.80 ?  37  PHE B C     1 
ATOM   5822  O  O     . PHE B 1 37  ? 156.610 132.298 169.592 1.00 56.45 ?  37  PHE B O     1 
ATOM   5823  C  CB    . PHE B 1 37  ? 153.883 133.513 171.394 1.00 53.21 ?  37  PHE B CB    1 
ATOM   5824  C  CG    . PHE B 1 37  ? 152.963 134.569 170.859 1.00 53.35 ?  37  PHE B CG    1 
ATOM   5825  C  CD1   . PHE B 1 37  ? 153.474 135.723 170.292 1.00 53.37 ?  37  PHE B CD1   1 
ATOM   5826  C  CD2   . PHE B 1 37  ? 151.591 134.398 170.897 1.00 54.29 ?  37  PHE B CD2   1 
ATOM   5827  C  CE1   . PHE B 1 37  ? 152.634 136.694 169.788 1.00 53.62 ?  37  PHE B CE1   1 
ATOM   5828  C  CE2   . PHE B 1 37  ? 150.747 135.366 170.394 1.00 53.68 ?  37  PHE B CE2   1 
ATOM   5829  C  CZ    . PHE B 1 37  ? 151.269 136.514 169.839 1.00 53.77 ?  37  PHE B CZ    1 
ATOM   5830  N  N     . VAL B 1 38  ? 156.141 131.561 171.671 1.00 54.84 ?  38  VAL B N     1 
ATOM   5831  C  CA    . VAL B 1 38  ? 157.537 131.348 172.042 1.00 56.79 ?  38  VAL B CA    1 
ATOM   5832  C  C     . VAL B 1 38  ? 158.282 130.521 171.003 1.00 56.86 ?  38  VAL B C     1 
ATOM   5833  O  O     . VAL B 1 38  ? 159.494 130.688 170.827 1.00 57.58 ?  38  VAL B O     1 
ATOM   5834  C  CB    . VAL B 1 38  ? 157.614 130.694 173.435 1.00 56.33 ?  38  VAL B CB    1 
ATOM   5835  C  CG1   . VAL B 1 38  ? 158.875 129.859 173.557 1.00 57.40 ?  38  VAL B CG1   1 
ATOM   5836  C  CG2   . VAL B 1 38  ? 157.556 131.752 174.524 1.00 54.65 ?  38  VAL B CG2   1 
ATOM   5837  N  N     . ASP B 1 39  ? 157.591 129.621 170.300 1.00 55.26 ?  39  ASP B N     1 
ATOM   5838  C  CA    . ASP B 1 39  ? 158.272 128.704 169.398 1.00 55.07 ?  39  ASP B CA    1 
ATOM   5839  C  C     . ASP B 1 39  ? 158.222 129.115 167.932 1.00 57.32 ?  39  ASP B C     1 
ATOM   5840  O  O     . ASP B 1 39  ? 159.094 128.692 167.166 1.00 61.25 ?  39  ASP B O     1 
ATOM   5841  C  CB    . ASP B 1 39  ? 157.690 127.292 169.538 1.00 57.43 ?  39  ASP B CB    1 
ATOM   5842  C  CG    . ASP B 1 39  ? 157.753 126.775 170.961 1.00 61.80 ?  39  ASP B CG    1 
ATOM   5843  O  OD1   . ASP B 1 39  ? 158.654 127.206 171.710 1.00 60.48 ?  39  ASP B OD1   1 
ATOM   5844  O  OD2   . ASP B 1 39  ? 156.903 125.937 171.330 1.00 61.41 -1 39  ASP B OD2   1 
ATOM   5845  N  N     . TYR B 1 40  ? 157.241 129.913 167.513 1.00 55.65 ?  40  TYR B N     1 
ATOM   5846  C  CA    . TYR B 1 40  ? 157.147 130.318 166.117 1.00 56.27 ?  40  TYR B CA    1 
ATOM   5847  C  C     . TYR B 1 40  ? 157.201 131.825 165.932 1.00 59.84 ?  40  TYR B C     1 
ATOM   5848  O  O     . TYR B 1 40  ? 157.959 132.310 165.087 1.00 59.13 ?  40  TYR B O     1 
ATOM   5849  C  CB    . TYR B 1 40  ? 155.855 129.756 165.501 1.00 54.62 ?  40  TYR B CB    1 
ATOM   5850  C  CG    . TYR B 1 40  ? 155.709 130.027 164.022 1.00 57.18 ?  40  TYR B CG    1 
ATOM   5851  C  CD1   . TYR B 1 40  ? 155.125 131.200 163.566 1.00 56.89 ?  40  TYR B CD1   1 
ATOM   5852  C  CD2   . TYR B 1 40  ? 156.159 129.112 163.081 1.00 57.49 ?  40  TYR B CD2   1 
ATOM   5853  C  CE1   . TYR B 1 40  ? 154.990 131.454 162.218 1.00 56.96 ?  40  TYR B CE1   1 
ATOM   5854  C  CE2   . TYR B 1 40  ? 156.029 129.356 161.728 1.00 58.71 ?  40  TYR B CE2   1 
ATOM   5855  C  CZ    . TYR B 1 40  ? 155.445 130.530 161.303 1.00 58.49 ?  40  TYR B CZ    1 
ATOM   5856  O  OH    . TYR B 1 40  ? 155.312 130.779 159.957 1.00 60.97 ?  40  TYR B OH    1 
ATOM   5857  N  N     . ILE B 1 41  ? 156.422 132.585 166.700 1.00 57.19 ?  41  ILE B N     1 
ATOM   5858  C  CA    . ILE B 1 41  ? 156.260 134.005 166.401 1.00 54.39 ?  41  ILE B CA    1 
ATOM   5859  C  C     . ILE B 1 41  ? 157.527 134.771 166.752 1.00 54.64 ?  41  ILE B C     1 
ATOM   5860  O  O     . ILE B 1 41  ? 158.021 135.584 165.962 1.00 57.54 ?  41  ILE B O     1 
ATOM   5861  C  CB    . ILE B 1 41  ? 155.031 134.571 167.134 1.00 54.01 ?  41  ILE B CB    1 
ATOM   5862  C  CG1   . ILE B 1 41  ? 153.746 133.997 166.538 1.00 53.69 ?  41  ILE B CG1   1 
ATOM   5863  C  CG2   . ILE B 1 41  ? 155.021 136.088 167.064 1.00 53.29 ?  41  ILE B CG2   1 
ATOM   5864  C  CD1   . ILE B 1 41  ? 153.615 134.212 165.053 1.00 51.15 ?  41  ILE B CD1   1 
ATOM   5865  N  N     . ASN B 1 42  ? 158.076 134.521 167.942 1.00 54.90 ?  42  ASN B N     1 
ATOM   5866  C  CA    . ASN B 1 42  ? 159.314 135.186 168.330 1.00 57.86 ?  42  ASN B CA    1 
ATOM   5867  C  C     . ASN B 1 42  ? 160.464 134.782 167.416 1.00 59.81 ?  42  ASN B C     1 
ATOM   5868  O  O     . ASN B 1 42  ? 161.310 135.611 167.064 1.00 60.21 ?  42  ASN B O     1 
ATOM   5869  C  CB    . ASN B 1 42  ? 159.644 134.872 169.788 1.00 58.43 ?  42  ASN B CB    1 
ATOM   5870  C  CG    . ASN B 1 42  ? 158.569 135.350 170.745 1.00 56.92 ?  42  ASN B CG    1 
ATOM   5871  O  OD1   . ASN B 1 42  ? 157.662 136.085 170.359 1.00 58.97 ?  42  ASN B OD1   1 
ATOM   5872  N  ND2   . ASN B 1 42  ? 158.670 134.939 172.003 1.00 57.21 ?  42  ASN B ND2   1 
ATOM   5873  N  N     . GLN B 1 43  ? 160.512 133.508 167.022 1.00 60.35 ?  43  GLN B N     1 
ATOM   5874  C  CA    . GLN B 1 43  ? 161.579 133.042 166.143 1.00 59.27 ?  43  GLN B CA    1 
ATOM   5875  C  C     . GLN B 1 43  ? 161.496 133.703 164.772 1.00 58.62 ?  43  GLN B C     1 
ATOM   5876  O  O     . GLN B 1 43  ? 162.508 134.165 164.232 1.00 60.00 ?  43  GLN B O     1 
ATOM   5877  C  CB    . GLN B 1 43  ? 161.519 131.520 166.009 1.00 59.80 ?  43  GLN B CB    1 
ATOM   5878  C  CG    . GLN B 1 43  ? 161.105 130.794 167.278 1.00 59.57 ?  43  GLN B CG    1 
ATOM   5879  C  CD    . GLN B 1 43  ? 162.085 130.993 168.418 1.00 61.93 ?  43  GLN B CD    1 
ATOM   5880  O  OE1   . GLN B 1 43  ? 162.932 131.885 168.378 1.00 60.27 ?  43  GLN B OE1   1 
ATOM   5881  N  NE2   . GLN B 1 43  ? 161.971 130.160 169.445 1.00 60.23 ?  43  GLN B NE2   1 
ATOM   5882  N  N     . ASN B 1 44  ? 160.297 133.762 164.195 1.00 59.37 ?  44  ASN B N     1 
ATOM   5883  C  CA    . ASN B 1 44  ? 160.096 134.276 162.848 1.00 59.15 ?  44  ASN B CA    1 
ATOM   5884  C  C     . ASN B 1 44  ? 159.813 135.772 162.815 1.00 58.96 ?  44  ASN B C     1 
ATOM   5885  O  O     . ASN B 1 44  ? 159.440 136.295 161.760 1.00 60.09 ?  44  ASN B O     1 
ATOM   5886  C  CB    . ASN B 1 44  ? 158.960 133.517 162.158 1.00 58.97 ?  44  ASN B CB    1 
ATOM   5887  C  CG    . ASN B 1 44  ? 159.125 132.013 162.249 1.00 60.59 ?  44  ASN B CG    1 
ATOM   5888  O  OD1   . ASN B 1 44  ? 159.519 131.480 163.286 1.00 60.04 ?  44  ASN B OD1   1 
ATOM   5889  N  ND2   . ASN B 1 44  ? 158.823 131.319 161.158 1.00 61.38 ?  44  ASN B ND2   1 
ATOM   5890  N  N     . THR B 1 45  ? 159.977 136.468 163.935 1.00 58.43 ?  45  THR B N     1 
ATOM   5891  C  CA    . THR B 1 45  ? 159.800 137.914 163.982 1.00 60.95 ?  45  THR B CA    1 
ATOM   5892  C  C     . THR B 1 45  ? 161.137 138.586 163.696 1.00 60.44 ?  45  THR B C     1 
ATOM   5893  O  O     . THR B 1 45  ? 162.121 138.345 164.403 1.00 60.64 ?  45  THR B O     1 
ATOM   5894  C  CB    . THR B 1 45  ? 159.257 138.353 165.341 1.00 59.91 ?  45  THR B CB    1 
ATOM   5895  O  OG1   . THR B 1 45  ? 157.944 137.811 165.532 1.00 60.33 ?  45  THR B OG1   1 
ATOM   5896  C  CG2   . THR B 1 45  ? 159.189 139.868 165.425 1.00 57.53 ?  45  THR B CG2   1 
ATOM   5897  N  N     . VAL B 1 46  ? 161.171 139.426 162.659 1.00 61.75 ?  46  VAL B N     1 
ATOM   5898  C  CA    . VAL B 1 46  ? 162.399 140.132 162.321 1.00 60.80 ?  46  VAL B CA    1 
ATOM   5899  C  C     . VAL B 1 46  ? 162.838 140.982 163.503 1.00 61.78 ?  46  VAL B C     1 
ATOM   5900  O  O     . VAL B 1 46  ? 162.012 141.485 164.275 1.00 61.93 ?  46  VAL B O     1 
ATOM   5901  C  CB    . VAL B 1 46  ? 162.203 140.991 161.061 1.00 60.37 ?  46  VAL B CB    1 
ATOM   5902  C  CG1   . VAL B 1 46  ? 163.495 141.703 160.700 1.00 59.83 ?  46  VAL B CG1   1 
ATOM   5903  C  CG2   . VAL B 1 46  ? 161.721 140.133 159.903 1.00 59.44 ?  46  VAL B CG2   1 
ATOM   5904  N  N     . PHE B 1 47  ? 164.149 141.145 163.649 1.00 65.67 ?  47  PHE B N     1 
ATOM   5905  C  CA    . PHE B 1 47  ? 164.724 141.895 164.757 1.00 65.84 ?  47  PHE B CA    1 
ATOM   5906  C  C     . PHE B 1 47  ? 165.177 143.264 164.270 1.00 66.98 ?  47  PHE B C     1 
ATOM   5907  O  O     . PHE B 1 47  ? 165.849 143.372 163.240 1.00 67.85 ?  47  PHE B O     1 
ATOM   5908  C  CB    . PHE B 1 47  ? 165.901 141.142 165.377 1.00 67.07 ?  47  PHE B CB    1 
ATOM   5909  C  CG    . PHE B 1 47  ? 166.722 141.974 166.320 1.00 66.52 ?  47  PHE B CG    1 
ATOM   5910  C  CD1   . PHE B 1 47  ? 167.994 142.390 165.970 1.00 66.70 ?  47  PHE B CD1   1 
ATOM   5911  C  CD2   . PHE B 1 47  ? 166.219 142.339 167.559 1.00 66.64 ?  47  PHE B CD2   1 
ATOM   5912  C  CE1   . PHE B 1 47  ? 168.751 143.156 166.837 1.00 68.38 ?  47  PHE B CE1   1 
ATOM   5913  C  CE2   . PHE B 1 47  ? 166.972 143.103 168.430 1.00 67.17 ?  47  PHE B CE2   1 
ATOM   5914  C  CZ    . PHE B 1 47  ? 168.239 143.512 168.069 1.00 67.51 ?  47  PHE B CZ    1 
ATOM   5915  N  N     . PHE B 1 48  ? 164.803 144.302 165.013 1.00 64.38 ?  48  PHE B N     1 
ATOM   5916  C  CA    . PHE B 1 48  ? 165.218 145.667 164.728 1.00 63.41 ?  48  PHE B CA    1 
ATOM   5917  C  C     . PHE B 1 48  ? 165.760 146.289 166.005 1.00 65.01 ?  48  PHE B C     1 
ATOM   5918  O  O     . PHE B 1 48  ? 165.165 146.148 167.077 1.00 66.11 ?  48  PHE B O     1 
ATOM   5919  C  CB    . PHE B 1 48  ? 164.056 146.499 164.175 1.00 62.50 ?  48  PHE B CB    1 
ATOM   5920  C  CG    . PHE B 1 48  ? 163.592 146.062 162.816 1.00 61.79 ?  48  PHE B CG    1 
ATOM   5921  C  CD1   . PHE B 1 48  ? 164.230 146.509 161.673 1.00 62.51 ?  48  PHE B CD1   1 
ATOM   5922  C  CD2   . PHE B 1 48  ? 162.520 145.196 162.681 1.00 62.87 ?  48  PHE B CD2   1 
ATOM   5923  C  CE1   . PHE B 1 48  ? 163.805 146.107 160.421 1.00 62.69 ?  48  PHE B CE1   1 
ATOM   5924  C  CE2   . PHE B 1 48  ? 162.090 144.790 161.433 1.00 63.33 ?  48  PHE B CE2   1 
ATOM   5925  C  CZ    . PHE B 1 48  ? 162.735 145.246 160.302 1.00 62.40 ?  48  PHE B CZ    1 
ATOM   5926  N  N     . HIS B 1 49  ? 166.897 146.978 165.884 1.00 66.19 ?  49  HIS B N     1 
ATOM   5927  C  CA    . HIS B 1 49  ? 167.562 147.510 167.068 1.00 66.99 ?  49  HIS B CA    1 
ATOM   5928  C  C     . HIS B 1 49  ? 166.684 148.526 167.788 1.00 68.58 ?  49  HIS B C     1 
ATOM   5929  O  O     . HIS B 1 49  ? 166.633 148.549 169.022 1.00 68.66 ?  49  HIS B O     1 
ATOM   5930  C  CB    . HIS B 1 49  ? 168.904 148.130 166.679 1.00 68.16 ?  49  HIS B CB    1 
ATOM   5931  C  CG    . HIS B 1 49  ? 169.915 147.131 166.211 1.00 70.31 ?  49  HIS B CG    1 
ATOM   5932  N  ND1   . HIS B 1 49  ? 169.953 146.661 164.916 1.00 69.87 ?  49  HIS B ND1   1 
ATOM   5933  C  CD2   . HIS B 1 49  ? 170.923 146.507 166.867 1.00 68.93 ?  49  HIS B CD2   1 
ATOM   5934  C  CE1   . HIS B 1 49  ? 170.942 145.794 164.794 1.00 68.33 ?  49  HIS B CE1   1 
ATOM   5935  N  NE2   . HIS B 1 49  ? 171.545 145.682 165.962 1.00 69.18 ?  49  HIS B NE2   1 
ATOM   5936  N  N     . ASN B 1 50  ? 165.987 149.373 167.035 1.00 67.68 ?  50  ASN B N     1 
ATOM   5937  C  CA    . ASN B 1 50  ? 165.105 150.373 167.617 1.00 65.85 ?  50  ASN B CA    1 
ATOM   5938  C  C     . ASN B 1 50  ? 163.911 150.566 166.692 1.00 64.59 ?  50  ASN B C     1 
ATOM   5939  O  O     . ASN B 1 50  ? 163.842 149.989 165.602 1.00 63.73 ?  50  ASN B O     1 
ATOM   5940  C  CB    . ASN B 1 50  ? 165.847 151.693 167.856 1.00 64.40 ?  50  ASN B CB    1 
ATOM   5941  C  CG    . ASN B 1 50  ? 166.900 151.966 166.801 1.00 65.74 ?  50  ASN B CG    1 
ATOM   5942  O  OD1   . ASN B 1 50  ? 166.742 151.594 165.640 1.00 66.16 ?  50  ASN B OD1   1 
ATOM   5943  N  ND2   . ASN B 1 50  ? 167.983 152.621 167.202 1.00 66.48 ?  50  ASN B ND2   1 
ATOM   5944  N  N     . LEU B 1 51  ? 162.959 151.387 167.140 1.00 60.91 ?  51  LEU B N     1 
ATOM   5945  C  CA    . LEU B 1 51  ? 161.792 151.684 166.316 1.00 60.80 ?  51  LEU B CA    1 
ATOM   5946  C  C     . LEU B 1 51  ? 162.160 152.532 165.108 1.00 60.47 ?  51  LEU B C     1 
ATOM   5947  O  O     . LEU B 1 51  ? 161.539 152.399 164.048 1.00 61.02 ?  51  LEU B O     1 
ATOM   5948  C  CB    . LEU B 1 51  ? 160.724 152.389 167.151 1.00 60.35 ?  51  LEU B CB    1 
ATOM   5949  C  CG    . LEU B 1 51  ? 159.494 152.890 166.392 1.00 59.64 ?  51  LEU B CG    1 
ATOM   5950  C  CD1   . LEU B 1 51  ? 158.773 151.742 165.703 1.00 59.45 ?  51  LEU B CD1   1 
ATOM   5951  C  CD2   . LEU B 1 51  ? 158.557 153.632 167.329 1.00 58.36 ?  51  LEU B CD2   1 
ATOM   5952  N  N     . LYS B 1 52  ? 163.150 153.412 165.248 1.00 61.57 ?  52  LYS B N     1 
ATOM   5953  C  CA    . LYS B 1 52  ? 163.558 154.256 164.130 1.00 61.65 ?  52  LYS B CA    1 
ATOM   5954  C  C     . LYS B 1 52  ? 164.070 153.402 162.977 1.00 61.32 ?  52  LYS B C     1 
ATOM   5955  O  O     . LYS B 1 52  ? 163.700 153.612 161.813 1.00 61.55 ?  52  LYS B O     1 
ATOM   5956  C  CB    . LYS B 1 52  ? 164.626 155.246 164.602 1.00 59.50 ?  52  LYS B CB    1 
ATOM   5957  C  CG    . LYS B 1 52  ? 164.775 156.504 163.757 1.00 60.36 ?  52  LYS B CG    1 
ATOM   5958  C  CD    . LYS B 1 52  ? 165.080 156.215 162.306 1.00 62.69 ?  52  LYS B CD    1 
ATOM   5959  C  CE    . LYS B 1 52  ? 165.483 157.485 161.581 1.00 63.70 ?  52  LYS B CE    1 
ATOM   5960  N  NZ    . LYS B 1 52  ? 164.358 158.459 161.511 1.00 61.64 1  52  LYS B NZ    1 
ATOM   5961  N  N     . GLU B 1 53  ? 164.919 152.418 163.286 1.00 62.63 ?  53  GLU B N     1 
ATOM   5962  C  CA    . GLU B 1 53  ? 165.435 151.521 162.258 1.00 63.18 ?  53  GLU B CA    1 
ATOM   5963  C  C     . GLU B 1 53  ? 164.317 150.709 161.618 1.00 64.15 ?  53  GLU B C     1 
ATOM   5964  O  O     . GLU B 1 53  ? 164.300 150.520 160.398 1.00 62.89 ?  53  GLU B O     1 
ATOM   5965  C  CB    . GLU B 1 53  ? 166.491 150.593 162.856 1.00 62.43 ?  53  GLU B CB    1 
ATOM   5966  C  CG    . GLU B 1 53  ? 167.028 149.557 161.885 1.00 63.21 ?  53  GLU B CG    1 
ATOM   5967  C  CD    . GLU B 1 53  ? 167.809 148.458 162.578 1.00 66.91 ?  53  GLU B CD    1 
ATOM   5968  O  OE1   . GLU B 1 53  ? 168.307 148.697 163.699 1.00 67.30 ?  53  GLU B OE1   1 
ATOM   5969  O  OE2   . GLU B 1 53  ? 167.917 147.352 162.007 1.00 65.68 -1 53  GLU B OE2   1 
ATOM   5970  N  N     . LYS B 1 54  ? 163.384 150.204 162.429 1.00 62.96 ?  54  LYS B N     1 
ATOM   5971  C  CA    . LYS B 1 54  ? 162.273 149.434 161.881 1.00 60.21 ?  54  LYS B CA    1 
ATOM   5972  C  C     . LYS B 1 54  ? 161.435 150.280 160.932 1.00 56.85 ?  54  LYS B C     1 
ATOM   5973  O  O     . LYS B 1 54  ? 161.059 149.823 159.846 1.00 60.10 ?  54  LYS B O     1 
ATOM   5974  C  CB    . LYS B 1 54  ? 161.408 148.884 163.013 1.00 59.39 ?  54  LYS B CB    1 
ATOM   5975  C  CG    . LYS B 1 54  ? 160.498 147.741 162.599 1.00 61.35 ?  54  LYS B CG    1 
ATOM   5976  C  CD    . LYS B 1 54  ? 159.146 147.848 163.280 1.00 59.66 ?  54  LYS B CD    1 
ATOM   5977  C  CE    . LYS B 1 54  ? 158.444 146.505 163.328 1.00 60.39 ?  54  LYS B CE    1 
ATOM   5978  N  NZ    . LYS B 1 54  ? 158.757 145.765 164.579 1.00 60.10 1  54  LYS B NZ    1 
ATOM   5979  N  N     . LEU B 1 55  ? 161.132 151.517 161.326 1.00 57.53 ?  55  LEU B N     1 
ATOM   5980  C  CA    . LEU B 1 55  ? 160.345 152.395 160.470 1.00 58.31 ?  55  LEU B CA    1 
ATOM   5981  C  C     . LEU B 1 55  ? 161.084 152.712 159.179 1.00 59.79 ?  55  LEU B C     1 
ATOM   5982  O  O     . LEU B 1 55  ? 160.485 152.716 158.097 1.00 62.77 ?  55  LEU B O     1 
ATOM   5983  C  CB    . LEU B 1 55  ? 159.989 153.678 161.221 1.00 59.74 ?  55  LEU B CB    1 
ATOM   5984  C  CG    . LEU B 1 55  ? 158.902 153.527 162.287 1.00 60.26 ?  55  LEU B CG    1 
ATOM   5985  C  CD1   . LEU B 1 55  ? 158.648 154.843 163.001 1.00 59.51 ?  55  LEU B CD1   1 
ATOM   5986  C  CD2   . LEU B 1 55  ? 157.623 153.001 161.661 1.00 58.76 ?  55  LEU B CD2   1 
ATOM   5987  N  N     . ASP B 1 56  ? 162.389 152.981 159.269 1.00 63.38 ?  56  ASP B N     1 
ATOM   5988  C  CA    . ASP B 1 56  ? 163.163 153.242 158.060 1.00 62.93 ?  56  ASP B CA    1 
ATOM   5989  C  C     . ASP B 1 56  ? 163.158 152.034 157.134 1.00 61.71 ?  56  ASP B C     1 
ATOM   5990  O  O     . ASP B 1 56  ? 162.942 152.170 155.925 1.00 63.50 ?  56  ASP B O     1 
ATOM   5991  C  CB    . ASP B 1 56  ? 164.594 153.633 158.426 1.00 63.86 ?  56  ASP B CB    1 
ATOM   5992  C  CG    . ASP B 1 56  ? 164.671 154.995 159.076 1.00 64.66 ?  56  ASP B CG    1 
ATOM   5993  O  OD1   . ASP B 1 56  ? 163.692 155.763 158.963 1.00 65.30 ?  56  ASP B OD1   1 
ATOM   5994  O  OD2   . ASP B 1 56  ? 165.709 155.303 159.698 1.00 63.09 -1 56  ASP B OD2   1 
ATOM   5995  N  N     . TYR B 1 57  ? 163.378 150.839 157.684 1.00 60.06 ?  57  TYR B N     1 
ATOM   5996  C  CA    . TYR B 1 57  ? 163.377 149.635 156.860 1.00 60.41 ?  57  TYR B CA    1 
ATOM   5997  C  C     . TYR B 1 57  ? 162.023 149.433 156.197 1.00 59.60 ?  57  TYR B C     1 
ATOM   5998  O  O     . TYR B 1 57  ? 161.949 149.075 155.015 1.00 60.58 ?  57  TYR B O     1 
ATOM   5999  C  CB    . TYR B 1 57  ? 163.766 148.425 157.717 1.00 59.86 ?  57  TYR B CB    1 
ATOM   6000  C  CG    . TYR B 1 57  ? 163.755 147.077 157.013 1.00 62.65 ?  57  TYR B CG    1 
ATOM   6001  C  CD1   . TYR B 1 57  ? 162.579 146.532 156.510 1.00 61.65 ?  57  TYR B CD1   1 
ATOM   6002  C  CD2   . TYR B 1 57  ? 164.928 146.353 156.852 1.00 62.64 ?  57  TYR B CD2   1 
ATOM   6003  C  CE1   . TYR B 1 57  ? 162.572 145.309 155.872 1.00 62.17 ?  57  TYR B CE1   1 
ATOM   6004  C  CE2   . TYR B 1 57  ? 164.931 145.128 156.214 1.00 61.99 ?  57  TYR B CE2   1 
ATOM   6005  C  CZ    . TYR B 1 57  ? 163.749 144.612 155.727 1.00 62.25 ?  57  TYR B CZ    1 
ATOM   6006  O  OH    . TYR B 1 57  ? 163.739 143.393 155.090 1.00 62.16 ?  57  TYR B OH    1 
ATOM   6007  N  N     . LEU B 1 58  ? 160.938 149.652 156.941 1.00 56.72 ?  58  LEU B N     1 
ATOM   6008  C  CA    . LEU B 1 58  ? 159.609 149.428 156.384 1.00 56.41 ?  58  LEU B CA    1 
ATOM   6009  C  C     . LEU B 1 58  ? 159.278 150.449 155.301 1.00 54.72 ?  58  LEU B C     1 
ATOM   6010  O  O     . LEU B 1 58  ? 158.650 150.107 154.293 1.00 54.88 ?  58  LEU B O     1 
ATOM   6011  C  CB    . LEU B 1 58  ? 158.569 149.458 157.503 1.00 54.88 ?  58  LEU B CB    1 
ATOM   6012  C  CG    . LEU B 1 58  ? 158.644 148.268 158.462 1.00 54.81 ?  58  LEU B CG    1 
ATOM   6013  C  CD1   . LEU B 1 58  ? 157.870 148.546 159.736 1.00 56.03 ?  58  LEU B CD1   1 
ATOM   6014  C  CD2   . LEU B 1 58  ? 158.125 147.010 157.787 1.00 54.22 ?  58  LEU B CD2   1 
ATOM   6015  N  N     . VAL B 1 59  ? 159.686 151.704 155.491 1.00 58.44 ?  59  VAL B N     1 
ATOM   6016  C  CA    . VAL B 1 59  ? 159.392 152.736 154.500 1.00 60.84 ?  59  VAL B CA    1 
ATOM   6017  C  C     . VAL B 1 59  ? 160.226 152.527 153.240 1.00 62.35 ?  59  VAL B C     1 
ATOM   6018  O  O     . VAL B 1 59  ? 159.703 152.551 152.119 1.00 61.66 ?  59  VAL B O     1 
ATOM   6019  C  CB    . VAL B 1 59  ? 159.619 154.134 155.099 1.00 59.39 ?  59  VAL B CB    1 
ATOM   6020  C  CG1   . VAL B 1 59  ? 159.511 155.193 154.018 1.00 59.69 ?  59  VAL B CG1   1 
ATOM   6021  C  CG2   . VAL B 1 59  ? 158.619 154.400 156.213 1.00 59.38 ?  59  VAL B CG2   1 
ATOM   6022  N  N     . GLU B 1 60  ? 161.536 152.321 153.402 1.00 63.79 ?  60  GLU B N     1 
ATOM   6023  C  CA    . GLU B 1 60  ? 162.411 152.193 152.240 1.00 63.65 ?  60  GLU B CA    1 
ATOM   6024  C  C     . GLU B 1 60  ? 162.079 150.951 151.423 1.00 64.59 ?  60  GLU B C     1 
ATOM   6025  O  O     . GLU B 1 60  ? 162.109 150.985 150.188 1.00 64.55 ?  60  GLU B O     1 
ATOM   6026  C  CB    . GLU B 1 60  ? 163.877 152.170 152.677 1.00 63.53 ?  60  GLU B CB    1 
ATOM   6027  C  CG    . GLU B 1 60  ? 164.234 153.204 153.729 1.00 64.97 ?  60  GLU B CG    1 
ATOM   6028  C  CD    . GLU B 1 60  ? 165.732 153.372 153.893 1.00 65.82 ?  60  GLU B CD    1 
ATOM   6029  O  OE1   . GLU B 1 60  ? 166.159 153.940 154.921 1.00 65.63 ?  60  GLU B OE1   1 
ATOM   6030  O  OE2   . GLU B 1 60  ? 166.482 152.930 152.998 1.00 65.44 -1 60  GLU B OE2   1 
ATOM   6031  N  N     . ASN B 1 61  ? 161.756 149.845 152.092 1.00 60.99 ?  61  ASN B N     1 
ATOM   6032  C  CA    . ASN B 1 61  ? 161.490 148.588 151.407 1.00 59.00 ?  61  ASN B CA    1 
ATOM   6033  C  C     . ASN B 1 61  ? 160.079 148.508 150.838 1.00 60.44 ?  61  ASN B C     1 
ATOM   6034  O  O     . ASN B 1 61  ? 159.607 147.407 150.530 1.00 61.07 ?  61  ASN B O     1 
ATOM   6035  C  CB    . ASN B 1 61  ? 161.746 147.412 152.350 1.00 59.83 ?  61  ASN B CB    1 
ATOM   6036  C  CG    . ASN B 1 61  ? 163.224 147.122 152.523 1.00 62.45 ?  61  ASN B CG    1 
ATOM   6037  O  OD1   . ASN B 1 61  ? 163.789 146.281 151.824 1.00 62.32 ?  61  ASN B OD1   1 
ATOM   6038  N  ND2   . ASN B 1 61  ? 163.859 147.820 153.455 1.00 61.82 ?  61  ASN B ND2   1 
ATOM   6039  N  N     . GLN B 1 62  ? 159.402 149.647 150.691 1.00 58.23 ?  62  GLN B N     1 
ATOM   6040  C  CA    . GLN B 1 62  ? 158.096 149.706 150.037 1.00 59.45 ?  62  GLN B CA    1 
ATOM   6041  C  C     . GLN B 1 62  ? 157.051 148.890 150.796 1.00 59.25 ?  62  GLN B C     1 
ATOM   6042  O  O     . GLN B 1 62  ? 156.137 148.313 150.203 1.00 60.07 ?  62  GLN B O     1 
ATOM   6043  C  CB    . GLN B 1 62  ? 158.192 149.245 148.582 1.00 59.80 ?  62  GLN B CB    1 
ATOM   6044  C  CG    . GLN B 1 62  ? 159.185 150.033 147.742 1.00 58.76 ?  62  GLN B CG    1 
ATOM   6045  C  CD    . GLN B 1 62  ? 159.016 151.532 147.889 1.00 60.56 ?  62  GLN B CD    1 
ATOM   6046  O  OE1   . GLN B 1 62  ? 159.441 152.122 148.881 1.00 61.95 ?  62  GLN B OE1   1 
ATOM   6047  N  NE2   . GLN B 1 62  ? 158.394 152.158 146.897 1.00 60.55 ?  62  GLN B NE2   1 
ATOM   6048  N  N     . TYR B 1 63  ? 157.187 148.837 152.119 1.00 55.32 ?  63  TYR B N     1 
ATOM   6049  C  CA    . TYR B 1 63  ? 156.201 148.188 152.974 1.00 54.92 ?  63  TYR B CA    1 
ATOM   6050  C  C     . TYR B 1 63  ? 155.161 149.157 153.515 1.00 54.34 ?  63  TYR B C     1 
ATOM   6051  O  O     . TYR B 1 63  ? 153.981 148.807 153.603 1.00 54.52 ?  63  TYR B O     1 
ATOM   6052  C  CB    . TYR B 1 63  ? 156.890 147.483 154.146 1.00 55.05 ?  63  TYR B CB    1 
ATOM   6053  C  CG    . TYR B 1 63  ? 157.511 146.154 153.786 1.00 55.07 ?  63  TYR B CG    1 
ATOM   6054  C  CD1   . TYR B 1 63  ? 156.750 145.144 153.215 1.00 55.40 ?  63  TYR B CD1   1 
ATOM   6055  C  CD2   . TYR B 1 63  ? 158.856 145.909 154.020 1.00 54.98 ?  63  TYR B CD2   1 
ATOM   6056  C  CE1   . TYR B 1 63  ? 157.312 143.927 152.885 1.00 56.61 ?  63  TYR B CE1   1 
ATOM   6057  C  CE2   . TYR B 1 63  ? 159.428 144.697 153.695 1.00 55.13 ?  63  TYR B CE2   1 
ATOM   6058  C  CZ    . TYR B 1 63  ? 158.652 143.709 153.127 1.00 59.02 ?  63  TYR B CZ    1 
ATOM   6059  O  OH    . TYR B 1 63  ? 159.218 142.499 152.802 1.00 59.51 ?  63  TYR B OH    1 
ATOM   6060  N  N     . TYR B 1 64  ? 155.573 150.370 153.874 1.00 52.38 ?  64  TYR B N     1 
ATOM   6061  C  CA    . TYR B 1 64  ? 154.685 151.382 154.423 1.00 50.15 ?  64  TYR B CA    1 
ATOM   6062  C  C     . TYR B 1 64  ? 154.604 152.575 153.482 1.00 54.26 ?  64  TYR B C     1 
ATOM   6063  O  O     . TYR B 1 64  ? 155.542 152.860 152.733 1.00 57.81 ?  64  TYR B O     1 
ATOM   6064  C  CB    . TYR B 1 64  ? 155.163 151.864 155.796 1.00 49.22 ?  64  TYR B CB    1 
ATOM   6065  C  CG    . TYR B 1 64  ? 154.876 150.914 156.931 1.00 51.83 ?  64  TYR B CG    1 
ATOM   6066  C  CD1   . TYR B 1 64  ? 154.004 149.847 156.769 1.00 49.70 ?  64  TYR B CD1   1 
ATOM   6067  C  CD2   . TYR B 1 64  ? 155.475 151.089 158.169 1.00 52.20 ?  64  TYR B CD2   1 
ATOM   6068  C  CE1   . TYR B 1 64  ? 153.742 148.979 157.809 1.00 47.75 ?  64  TYR B CE1   1 
ATOM   6069  C  CE2   . TYR B 1 64  ? 155.218 150.229 159.212 1.00 50.63 ?  64  TYR B CE2   1 
ATOM   6070  C  CZ    . TYR B 1 64  ? 154.354 149.175 159.028 1.00 50.89 ?  64  TYR B CZ    1 
ATOM   6071  O  OH    . TYR B 1 64  ? 154.098 148.317 160.071 1.00 52.81 ?  64  TYR B OH    1 
ATOM   6072  N  N     . GLU B 1 65  ? 153.472 153.269 153.531 1.00 58.95 ?  65  GLU B N     1 
ATOM   6073  C  CA    . GLU B 1 65  ? 153.331 154.545 152.844 1.00 54.85 ?  65  GLU B CA    1 
ATOM   6074  C  C     . GLU B 1 65  ? 154.004 155.627 153.679 1.00 58.41 ?  65  GLU B C     1 
ATOM   6075  O  O     . GLU B 1 65  ? 153.628 155.851 154.834 1.00 59.30 ?  65  GLU B O     1 
ATOM   6076  C  CB    . GLU B 1 65  ? 151.858 154.871 152.615 1.00 53.95 ?  65  GLU B CB    1 
ATOM   6077  C  CG    . GLU B 1 65  ? 151.161 153.941 151.635 1.00 55.54 ?  65  GLU B CG    1 
ATOM   6078  C  CD    . GLU B 1 65  ? 149.677 154.230 151.513 1.00 59.40 ?  65  GLU B CD    1 
ATOM   6079  O  OE1   . GLU B 1 65  ? 149.142 154.980 152.356 1.00 58.44 ?  65  GLU B OE1   1 
ATOM   6080  O  OE2   . GLU B 1 65  ? 149.045 153.709 150.570 1.00 58.34 -1 65  GLU B OE2   1 
ATOM   6081  N  N     . GLU B 1 66  ? 155.003 156.294 153.101 1.00 60.04 ?  66  GLU B N     1 
ATOM   6082  C  CA    . GLU B 1 66  ? 155.768 157.286 153.845 1.00 60.90 ?  66  GLU B CA    1 
ATOM   6083  C  C     . GLU B 1 66  ? 154.995 158.575 154.087 1.00 59.82 ?  66  GLU B C     1 
ATOM   6084  O  O     . GLU B 1 66  ? 155.352 159.331 154.996 1.00 58.64 ?  66  GLU B O     1 
ATOM   6085  C  CB    . GLU B 1 66  ? 157.075 157.603 153.113 1.00 60.59 ?  66  GLU B CB    1 
ATOM   6086  C  CG    . GLU B 1 66  ? 156.890 158.296 151.772 1.00 60.27 ?  66  GLU B CG    1 
ATOM   6087  C  CD    . GLU B 1 66  ? 156.533 157.329 150.660 1.00 62.64 ?  66  GLU B CD    1 
ATOM   6088  O  OE1   . GLU B 1 66  ? 155.590 156.531 150.844 1.00 60.54 ?  66  GLU B OE1   1 
ATOM   6089  O  OE2   . GLU B 1 66  ? 157.196 157.366 149.603 1.00 63.06 -1 66  GLU B OE2   1 
ATOM   6090  N  N     . GLU B 1 67  ? 153.950 158.842 153.302 1.00 58.67 ?  67  GLU B N     1 
ATOM   6091  C  CA    . GLU B 1 67  ? 153.243 160.113 153.419 1.00 57.19 ?  67  GLU B CA    1 
ATOM   6092  C  C     . GLU B 1 67  ? 152.562 160.250 154.776 1.00 58.31 ?  67  GLU B C     1 
ATOM   6093  O  O     . GLU B 1 67  ? 152.676 161.288 155.439 1.00 58.16 ?  67  GLU B O     1 
ATOM   6094  C  CB    . GLU B 1 67  ? 152.223 160.254 152.288 1.00 57.54 ?  67  GLU B CB    1 
ATOM   6095  C  CG    . GLU B 1 67  ? 152.801 160.042 150.899 1.00 57.43 ?  67  GLU B CG    1 
ATOM   6096  C  CD    . GLU B 1 67  ? 152.448 158.687 150.320 1.00 60.26 ?  67  GLU B CD    1 
ATOM   6097  O  OE1   . GLU B 1 67  ? 151.247 158.438 150.082 1.00 61.69 ?  67  GLU B OE1   1 
ATOM   6098  O  OE2   . GLU B 1 67  ? 153.368 157.871 150.103 1.00 59.48 -1 67  GLU B OE2   1 
ATOM   6099  N  N     . PHE B 1 68  ? 151.845 159.209 155.210 1.00 53.23 ?  68  PHE B N     1 
ATOM   6100  C  CA    . PHE B 1 68  ? 151.101 159.312 156.461 1.00 49.62 ?  68  PHE B CA    1 
ATOM   6101  C  C     . PHE B 1 68  ? 152.029 159.331 157.668 1.00 49.25 ?  68  PHE B C     1 
ATOM   6102  O  O     . PHE B 1 68  ? 151.712 159.966 158.680 1.00 51.75 ?  68  PHE B O     1 
ATOM   6103  C  CB    . PHE B 1 68  ? 150.087 158.172 156.573 1.00 50.52 ?  68  PHE B CB    1 
ATOM   6104  C  CG    . PHE B 1 68  ? 150.607 156.953 157.281 1.00 50.26 ?  68  PHE B CG    1 
ATOM   6105  C  CD1   . PHE B 1 68  ? 151.305 155.979 156.589 1.00 50.23 ?  68  PHE B CD1   1 
ATOM   6106  C  CD2   . PHE B 1 68  ? 150.386 156.775 158.635 1.00 47.60 ?  68  PHE B CD2   1 
ATOM   6107  C  CE1   . PHE B 1 68  ? 151.780 154.858 157.236 1.00 48.45 ?  68  PHE B CE1   1 
ATOM   6108  C  CE2   . PHE B 1 68  ? 150.858 155.656 159.287 1.00 47.29 ?  68  PHE B CE2   1 
ATOM   6109  C  CZ    . PHE B 1 68  ? 151.555 154.696 158.586 1.00 49.87 ?  68  PHE B CZ    1 
ATOM   6110  N  N     . LEU B 1 69  ? 153.170 158.646 157.587 1.00 52.57 ?  69  LEU B N     1 
ATOM   6111  C  CA    . LEU B 1 69  ? 154.139 158.673 158.674 1.00 51.01 ?  69  LEU B CA    1 
ATOM   6112  C  C     . LEU B 1 69  ? 154.924 159.977 158.724 1.00 52.61 ?  69  LEU B C     1 
ATOM   6113  O  O     . LEU B 1 69  ? 155.546 160.270 159.749 1.00 54.42 ?  69  LEU B O     1 
ATOM   6114  C  CB    . LEU B 1 69  ? 155.106 157.496 158.549 1.00 50.68 ?  69  LEU B CB    1 
ATOM   6115  C  CG    . LEU B 1 69  ? 154.622 156.155 159.103 1.00 52.11 ?  69  LEU B CG    1 
ATOM   6116  C  CD1   . LEU B 1 69  ? 155.546 155.033 158.664 1.00 50.25 ?  69  LEU B CD1   1 
ATOM   6117  C  CD2   . LEU B 1 69  ? 154.521 156.208 160.618 1.00 51.59 ?  69  LEU B CD2   1 
ATOM   6118  N  N     . SER B 1 70  ? 154.908 160.760 157.645 1.00 56.41 ?  70  SER B N     1 
ATOM   6119  C  CA    . SER B 1 70  ? 155.635 162.022 157.608 1.00 51.99 ?  70  SER B CA    1 
ATOM   6120  C  C     . SER B 1 70  ? 154.923 163.138 158.360 1.00 54.26 ?  70  SER B C     1 
ATOM   6121  O  O     . SER B 1 70  ? 155.513 164.207 158.547 1.00 54.38 ?  70  SER B O     1 
ATOM   6122  C  CB    . SER B 1 70  ? 155.868 162.449 156.159 1.00 52.30 ?  70  SER B CB    1 
ATOM   6123  O  OG    . SER B 1 70  ? 154.701 163.028 155.605 1.00 53.84 ?  70  SER B OG    1 
ATOM   6124  N  N     . LEU B 1 71  ? 153.680 162.921 158.790 1.00 48.97 ?  71  LEU B N     1 
ATOM   6125  C  CA    . LEU B 1 71  ? 152.938 163.936 159.526 1.00 46.80 ?  71  LEU B CA    1 
ATOM   6126  C  C     . LEU B 1 71  ? 153.285 163.966 161.007 1.00 48.65 ?  71  LEU B C     1 
ATOM   6127  O  O     . LEU B 1 71  ? 152.800 164.849 161.721 1.00 48.52 ?  71  LEU B O     1 
ATOM   6128  C  CB    . LEU B 1 71  ? 151.434 163.713 159.358 1.00 47.76 ?  71  LEU B CB    1 
ATOM   6129  C  CG    . LEU B 1 71  ? 150.941 163.477 157.930 1.00 50.60 ?  71  LEU B CG    1 
ATOM   6130  C  CD1   . LEU B 1 71  ? 149.500 162.998 157.929 1.00 48.23 ?  71  LEU B CD1   1 
ATOM   6131  C  CD2   . LEU B 1 71  ? 151.091 164.741 157.101 1.00 47.53 ?  71  LEU B CD2   1 
ATOM   6132  N  N     . TYR B 1 72  ? 154.103 163.032 161.481 1.00 46.98 ?  72  TYR B N     1 
ATOM   6133  C  CA    . TYR B 1 72  ? 154.492 162.960 162.881 1.00 48.27 ?  72  TYR B CA    1 
ATOM   6134  C  C     . TYR B 1 72  ? 156.004 163.066 163.003 1.00 49.47 ?  72  TYR B C     1 
ATOM   6135  O  O     . TYR B 1 72  ? 156.743 162.461 162.221 1.00 50.17 ?  72  TYR B O     1 
ATOM   6136  C  CB    . TYR B 1 72  ? 154.037 161.647 163.524 1.00 47.83 ?  72  TYR B CB    1 
ATOM   6137  C  CG    . TYR B 1 72  ? 152.559 161.368 163.426 1.00 44.54 ?  72  TYR B CG    1 
ATOM   6138  C  CD1   . TYR B 1 72  ? 151.681 161.818 164.401 1.00 45.65 ?  72  TYR B CD1   1 
ATOM   6139  C  CD2   . TYR B 1 72  ? 152.043 160.641 162.364 1.00 42.27 ?  72  TYR B CD2   1 
ATOM   6140  C  CE1   . TYR B 1 72  ? 150.330 161.558 164.316 1.00 44.51 ?  72  TYR B CE1   1 
ATOM   6141  C  CE2   . TYR B 1 72  ? 150.695 160.376 162.270 1.00 43.12 ?  72  TYR B CE2   1 
ATOM   6142  C  CZ    . TYR B 1 72  ? 149.842 160.836 163.249 1.00 43.65 ?  72  TYR B CZ    1 
ATOM   6143  O  OH    . TYR B 1 72  ? 148.498 160.573 163.157 1.00 45.48 ?  72  TYR B OH    1 
ATOM   6144  N  N     . SER B 1 73  ? 156.459 163.835 163.987 1.00 53.22 ?  73  SER B N     1 
ATOM   6145  C  CA    . SER B 1 73  ? 157.847 163.740 164.400 1.00 53.40 ?  73  SER B CA    1 
ATOM   6146  C  C     . SER B 1 73  ? 158.102 162.356 164.980 1.00 55.37 ?  73  SER B C     1 
ATOM   6147  O  O     . SER B 1 73  ? 157.216 161.740 165.580 1.00 56.47 ?  73  SER B O     1 
ATOM   6148  C  CB    . SER B 1 73  ? 158.177 164.820 165.430 1.00 53.52 ?  73  SER B CB    1 
ATOM   6149  O  OG    . SER B 1 73  ? 157.690 164.466 166.712 1.00 53.84 ?  73  SER B OG    1 
ATOM   6150  N  N     . PHE B 1 74  ? 159.324 161.855 164.793 1.00 58.57 ?  74  PHE B N     1 
ATOM   6151  C  CA    . PHE B 1 74  ? 159.611 160.500 165.253 1.00 55.78 ?  74  PHE B CA    1 
ATOM   6152  C  C     . PHE B 1 74  ? 159.382 160.358 166.752 1.00 57.34 ?  74  PHE B C     1 
ATOM   6153  O  O     . PHE B 1 74  ? 159.110 159.253 167.233 1.00 59.32 ?  74  PHE B O     1 
ATOM   6154  C  CB    . PHE B 1 74  ? 161.040 160.097 164.900 1.00 56.37 ?  74  PHE B CB    1 
ATOM   6155  C  CG    . PHE B 1 74  ? 161.402 158.720 165.376 1.00 58.50 ?  74  PHE B CG    1 
ATOM   6156  C  CD1   . PHE B 1 74  ? 160.869 157.600 164.760 1.00 57.38 ?  74  PHE B CD1   1 
ATOM   6157  C  CD2   . PHE B 1 74  ? 162.253 158.546 166.453 1.00 57.76 ?  74  PHE B CD2   1 
ATOM   6158  C  CE1   . PHE B 1 74  ? 161.189 156.333 165.202 1.00 59.23 ?  74  PHE B CE1   1 
ATOM   6159  C  CE2   . PHE B 1 74  ? 162.577 157.279 166.898 1.00 57.76 ?  74  PHE B CE2   1 
ATOM   6160  C  CZ    . PHE B 1 74  ? 162.044 156.173 166.273 1.00 58.74 ?  74  PHE B CZ    1 
ATOM   6161  N  N     . GLU B 1 75  ? 159.479 161.455 167.503 1.00 57.08 ?  75  GLU B N     1 
ATOM   6162  C  CA    . GLU B 1 75  ? 159.152 161.399 168.923 1.00 58.59 ?  75  GLU B CA    1 
ATOM   6163  C  C     . GLU B 1 75  ? 157.694 161.008 169.131 1.00 59.43 ?  75  GLU B C     1 
ATOM   6164  O  O     . GLU B 1 75  ? 157.381 160.177 169.993 1.00 60.88 ?  75  GLU B O     1 
ATOM   6165  C  CB    . GLU B 1 75  ? 159.446 162.745 169.584 1.00 57.15 ?  75  GLU B CB    1 
ATOM   6166  C  CG    . GLU B 1 75  ? 160.925 163.040 169.762 1.00 58.75 ?  75  GLU B CG    1 
ATOM   6167  C  CD    . GLU B 1 75  ? 161.629 161.993 170.602 1.00 63.37 ?  75  GLU B CD    1 
ATOM   6168  O  OE1   . GLU B 1 75  ? 161.148 161.702 171.717 1.00 63.27 ?  75  GLU B OE1   1 
ATOM   6169  O  OE2   . GLU B 1 75  ? 162.666 161.463 170.149 1.00 61.33 -1 75  GLU B OE2   1 
ATOM   6170  N  N     . ASP B 1 76  ? 156.788 161.587 168.341 1.00 54.43 ?  76  ASP B N     1 
ATOM   6171  C  CA    . ASP B 1 76  ? 155.373 161.258 168.472 1.00 52.61 ?  76  ASP B CA    1 
ATOM   6172  C  C     . ASP B 1 76  ? 155.094 159.819 168.052 1.00 52.27 ?  76  ASP B C     1 
ATOM   6173  O  O     . ASP B 1 76  ? 154.291 159.127 168.687 1.00 55.28 ?  76  ASP B O     1 
ATOM   6174  C  CB    . ASP B 1 76  ? 154.531 162.230 167.648 1.00 53.89 ?  76  ASP B CB    1 
ATOM   6175  C  CG    . ASP B 1 76  ? 154.605 163.650 168.174 1.00 55.39 ?  76  ASP B CG    1 
ATOM   6176  O  OD1   . ASP B 1 76  ? 154.515 163.833 169.405 1.00 55.40 ?  76  ASP B OD1   1 
ATOM   6177  O  OD2   . ASP B 1 76  ? 154.747 164.582 167.355 1.00 56.07 -1 76  ASP B OD2   1 
ATOM   6178  N  N     . ILE B 1 77  ? 155.739 159.355 166.980 1.00 49.21 ?  77  ILE B N     1 
ATOM   6179  C  CA    . ILE B 1 77  ? 155.568 157.967 166.560 1.00 49.91 ?  77  ILE B CA    1 
ATOM   6180  C  C     . ILE B 1 77  ? 156.058 157.021 167.648 1.00 48.30 ?  77  ILE B C     1 
ATOM   6181  O  O     . ILE B 1 77  ? 155.423 155.999 167.939 1.00 49.81 ?  77  ILE B O     1 
ATOM   6182  C  CB    . ILE B 1 77  ? 156.293 157.719 165.225 1.00 50.14 ?  77  ILE B CB    1 
ATOM   6183  C  CG1   . ILE B 1 77  ? 155.629 158.518 164.102 1.00 49.52 ?  77  ILE B CG1   1 
ATOM   6184  C  CG2   . ILE B 1 77  ? 156.304 156.236 164.894 1.00 49.43 ?  77  ILE B CG2   1 
ATOM   6185  C  CD1   . ILE B 1 77  ? 156.423 158.540 162.819 1.00 49.59 ?  77  ILE B CD1   1 
ATOM   6186  N  N     . LYS B 1 78  ? 157.199 157.343 168.260 1.00 50.52 ?  78  LYS B N     1 
ATOM   6187  C  CA    . LYS B 1 78  ? 157.712 156.524 169.351 1.00 52.84 ?  78  LYS B CA    1 
ATOM   6188  C  C     . LYS B 1 78  ? 156.751 156.520 170.532 1.00 51.60 ?  78  LYS B C     1 
ATOM   6189  O  O     . LYS B 1 78  ? 156.534 155.479 171.160 1.00 54.07 ?  78  LYS B O     1 
ATOM   6190  C  CB    . LYS B 1 78  ? 159.092 157.026 169.778 1.00 53.36 ?  78  LYS B CB    1 
ATOM   6191  C  CG    . LYS B 1 78  ? 159.826 156.103 170.734 1.00 52.49 ?  78  LYS B CG    1 
ATOM   6192  C  CD    . LYS B 1 78  ? 161.238 156.602 171.001 1.00 54.69 ?  78  LYS B CD    1 
ATOM   6193  C  CE    . LYS B 1 78  ? 161.667 156.316 172.430 1.00 53.89 ?  78  LYS B CE    1 
ATOM   6194  N  NZ    . LYS B 1 78  ? 161.931 157.570 173.190 1.00 53.15 1  78  LYS B NZ    1 
ATOM   6195  N  N     . GLU B 1 79  ? 156.171 157.678 170.854 1.00 49.46 ?  79  GLU B N     1 
ATOM   6196  C  CA    . GLU B 1 79  ? 155.203 157.736 171.944 1.00 48.04 ?  79  GLU B CA    1 
ATOM   6197  C  C     . GLU B 1 79  ? 153.982 156.876 171.642 1.00 48.82 ?  79  GLU B C     1 
ATOM   6198  O  O     . GLU B 1 79  ? 153.481 156.164 172.520 1.00 50.05 ?  79  GLU B O     1 
ATOM   6199  C  CB    . GLU B 1 79  ? 154.788 159.184 172.202 1.00 49.01 ?  79  GLU B CB    1 
ATOM   6200  C  CG    . GLU B 1 79  ? 155.452 159.812 173.416 1.00 51.41 ?  79  GLU B CG    1 
ATOM   6201  C  CD    . GLU B 1 79  ? 155.694 158.811 174.527 1.00 54.22 ?  79  GLU B CD    1 
ATOM   6202  O  OE1   . GLU B 1 79  ? 154.759 158.556 175.316 1.00 54.73 ?  79  GLU B OE1   1 
ATOM   6203  O  OE2   . GLU B 1 79  ? 156.821 158.278 174.613 1.00 53.47 -1 79  GLU B OE2   1 
ATOM   6204  N  N     . VAL B 1 80  ? 153.493 156.924 170.402 1.00 44.17 ?  80  VAL B N     1 
ATOM   6205  C  CA    . VAL B 1 80  ? 152.334 156.119 170.029 1.00 41.84 ?  80  VAL B CA    1 
ATOM   6206  C  C     . VAL B 1 80  ? 152.659 154.634 170.130 1.00 46.95 ?  80  VAL B C     1 
ATOM   6207  O  O     . VAL B 1 80  ? 151.865 153.840 170.654 1.00 47.24 ?  80  VAL B O     1 
ATOM   6208  C  CB    . VAL B 1 80  ? 151.853 156.500 168.616 1.00 44.04 ?  80  VAL B CB    1 
ATOM   6209  C  CG1   . VAL B 1 80  ? 150.740 155.570 168.160 1.00 43.48 ?  80  VAL B CG1   1 
ATOM   6210  C  CG2   . VAL B 1 80  ? 151.393 157.947 168.587 1.00 43.56 ?  80  VAL B CG2   1 
ATOM   6211  N  N     . PHE B 1 81  ? 153.829 154.233 169.631 1.00 46.81 ?  81  PHE B N     1 
ATOM   6212  C  CA    . PHE B 1 81  ? 154.211 152.826 169.697 1.00 42.94 ?  81  PHE B CA    1 
ATOM   6213  C  C     . PHE B 1 81  ? 154.390 152.368 171.140 1.00 46.11 ?  81  PHE B C     1 
ATOM   6214  O  O     . PHE B 1 81  ? 154.023 151.241 171.486 1.00 47.25 ?  81  PHE B O     1 
ATOM   6215  C  CB    . PHE B 1 81  ? 155.482 152.588 168.884 1.00 42.74 ?  81  PHE B CB    1 
ATOM   6216  C  CG    . PHE B 1 81  ? 155.221 152.251 167.445 1.00 39.78 ?  81  PHE B CG    1 
ATOM   6217  C  CD1   . PHE B 1 81  ? 154.897 153.242 166.537 1.00 43.14 ?  81  PHE B CD1   1 
ATOM   6218  C  CD2   . PHE B 1 81  ? 155.292 150.943 167.003 1.00 41.98 ?  81  PHE B CD2   1 
ATOM   6219  C  CE1   . PHE B 1 81  ? 154.654 152.934 165.213 1.00 45.50 ?  81  PHE B CE1   1 
ATOM   6220  C  CE2   . PHE B 1 81  ? 155.048 150.629 165.681 1.00 42.11 ?  81  PHE B CE2   1 
ATOM   6221  C  CZ    . PHE B 1 81  ? 154.730 151.627 164.785 1.00 43.10 ?  81  PHE B CZ    1 
ATOM   6222  N  N     . LYS B 1 82  ? 154.950 153.226 171.995 1.00 45.24 ?  82  LYS B N     1 
ATOM   6223  C  CA    . LYS B 1 82  ? 155.050 152.896 173.413 1.00 44.33 ?  82  LYS B CA    1 
ATOM   6224  C  C     . LYS B 1 82  ? 153.669 152.741 174.034 1.00 45.15 ?  82  LYS B C     1 
ATOM   6225  O  O     . LYS B 1 82  ? 153.447 151.849 174.860 1.00 46.39 ?  82  LYS B O     1 
ATOM   6226  C  CB    . LYS B 1 82  ? 155.850 153.969 174.150 1.00 45.21 ?  82  LYS B CB    1 
ATOM   6227  C  CG    . LYS B 1 82  ? 157.262 154.170 173.631 1.00 48.52 ?  82  LYS B CG    1 
ATOM   6228  C  CD    . LYS B 1 82  ? 158.171 154.731 174.712 1.00 50.57 ?  82  LYS B CD    1 
ATOM   6229  C  CE    . LYS B 1 82  ? 159.627 154.384 174.449 1.00 49.94 ?  82  LYS B CE    1 
ATOM   6230  N  NZ    . LYS B 1 82  ? 159.775 153.453 173.298 1.00 52.44 1  82  LYS B NZ    1 
ATOM   6231  N  N     . THR B 1 83  ? 152.729 153.607 173.652 1.00 44.66 ?  83  THR B N     1 
ATOM   6232  C  CA    . THR B 1 83  ? 151.365 153.481 174.147 1.00 44.49 ?  83  THR B CA    1 
ATOM   6233  C  C     . THR B 1 83  ? 150.762 152.142 173.748 1.00 44.38 ?  83  THR B C     1 
ATOM   6234  O  O     . THR B 1 83  ? 150.113 151.475 174.562 1.00 42.46 ?  83  THR B O     1 
ATOM   6235  C  CB    . THR B 1 83  ? 150.506 154.630 173.622 1.00 41.84 ?  83  THR B CB    1 
ATOM   6236  O  OG1   . THR B 1 83  ? 151.051 155.879 174.067 1.00 46.55 ?  83  THR B OG1   1 
ATOM   6237  C  CG2   . THR B 1 83  ? 149.078 154.501 174.125 1.00 43.58 ?  83  THR B CG2   1 
ATOM   6238  N  N     . ALA B 1 84  ? 150.966 151.731 172.495 1.00 42.38 ?  84  ALA B N     1 
ATOM   6239  C  CA    . ALA B 1 84  ? 150.469 150.427 172.067 1.00 40.25 ?  84  ALA B CA    1 
ATOM   6240  C  C     . ALA B 1 84  ? 151.139 149.299 172.842 1.00 40.87 ?  84  ALA B C     1 
ATOM   6241  O  O     . ALA B 1 84  ? 150.474 148.348 173.268 1.00 46.06 ?  84  ALA B O     1 
ATOM   6242  C  CB    . ALA B 1 84  ? 150.682 150.250 170.566 1.00 39.61 ?  84  ALA B CB    1 
ATOM   6243  N  N     . TYR B 1 85  ? 152.455 149.388 173.038 1.00 46.99 ?  85  TYR B N     1 
ATOM   6244  C  CA    . TYR B 1 85  ? 153.195 148.330 173.714 1.00 43.73 ?  85  TYR B CA    1 
ATOM   6245  C  C     . TYR B 1 85  ? 153.038 148.361 175.228 1.00 45.98 ?  85  TYR B C     1 
ATOM   6246  O  O     . TYR B 1 85  ? 153.203 147.321 175.874 1.00 45.42 ?  85  TYR B O     1 
ATOM   6247  C  CB    . TYR B 1 85  ? 154.679 148.417 173.352 1.00 42.93 ?  85  TYR B CB    1 
ATOM   6248  C  CG    . TYR B 1 85  ? 155.054 147.601 172.137 1.00 42.52 ?  85  TYR B CG    1 
ATOM   6249  C  CD1   . TYR B 1 85  ? 155.149 146.219 172.209 1.00 44.89 ?  85  TYR B CD1   1 
ATOM   6250  C  CD2   . TYR B 1 85  ? 155.308 148.213 170.918 1.00 45.35 ?  85  TYR B CD2   1 
ATOM   6251  C  CE1   . TYR B 1 85  ? 155.491 145.469 171.102 1.00 45.34 ?  85  TYR B CE1   1 
ATOM   6252  C  CE2   . TYR B 1 85  ? 155.651 147.473 169.805 1.00 45.77 ?  85  TYR B CE2   1 
ATOM   6253  C  CZ    . TYR B 1 85  ? 155.740 146.100 169.903 1.00 46.03 ?  85  TYR B CZ    1 
ATOM   6254  O  OH    . TYR B 1 85  ? 156.080 145.357 168.799 1.00 50.43 ?  85  TYR B OH    1 
ATOM   6255  N  N     . ALA B 1 86  ? 152.726 149.522 175.808 1.00 47.59 ?  86  ALA B N     1 
ATOM   6256  C  CA    . ALA B 1 86  ? 152.624 149.615 177.261 1.00 43.98 ?  86  ALA B CA    1 
ATOM   6257  C  C     . ALA B 1 86  ? 151.543 148.697 177.814 1.00 45.34 ?  86  ALA B C     1 
ATOM   6258  O  O     . ALA B 1 86  ? 151.633 148.259 178.966 1.00 47.43 ?  86  ALA B O     1 
ATOM   6259  C  CB    . ALA B 1 86  ? 152.353 151.061 177.676 1.00 44.33 ?  86  ALA B CB    1 
ATOM   6260  N  N     . LYS B 1 87  ? 150.519 148.393 177.016 1.00 45.81 ?  87  LYS B N     1 
ATOM   6261  C  CA    . LYS B 1 87  ? 149.424 147.556 177.490 1.00 45.91 ?  87  LYS B CA    1 
ATOM   6262  C  C     . LYS B 1 87  ? 149.858 146.123 177.769 1.00 48.49 ?  87  LYS B C     1 
ATOM   6263  O  O     . LYS B 1 87  ? 149.211 145.440 178.570 1.00 47.12 ?  87  LYS B O     1 
ATOM   6264  C  CB    . LYS B 1 87  ? 148.282 147.556 176.474 1.00 47.53 ?  87  LYS B CB    1 
ATOM   6265  C  CG    . LYS B 1 87  ? 146.920 147.270 177.077 1.00 48.20 ?  87  LYS B CG    1 
ATOM   6266  C  CD    . LYS B 1 87  ? 146.190 146.191 176.296 1.00 46.35 ?  87  LYS B CD    1 
ATOM   6267  C  CE    . LYS B 1 87  ? 144.754 146.045 176.769 1.00 45.89 ?  87  LYS B CE    1 
ATOM   6268  N  NZ    . LYS B 1 87  ? 144.630 146.260 178.236 1.00 46.33 1  87  LYS B NZ    1 
ATOM   6269  N  N     . LYS B 1 88  ? 150.933 145.655 177.137 1.00 50.02 ?  88  LYS B N     1 
ATOM   6270  C  CA    . LYS B 1 88  ? 151.368 144.265 177.264 1.00 45.05 ?  88  LYS B CA    1 
ATOM   6271  C  C     . LYS B 1 88  ? 150.234 143.314 176.887 1.00 43.42 ?  88  LYS B C     1 
ATOM   6272  O  O     . LYS B 1 88  ? 149.939 142.346 177.591 1.00 47.99 ?  88  LYS B O     1 
ATOM   6273  C  CB    . LYS B 1 88  ? 151.884 143.977 178.675 1.00 45.92 ?  88  LYS B CB    1 
ATOM   6274  C  CG    . LYS B 1 88  ? 152.812 145.044 179.225 1.00 47.07 ?  88  LYS B CG    1 
ATOM   6275  C  CD    . LYS B 1 88  ? 154.260 144.743 178.881 1.00 48.45 ?  88  LYS B CD    1 
ATOM   6276  C  CE    . LYS B 1 88  ? 154.849 143.719 179.834 1.00 49.55 ?  88  LYS B CE    1 
ATOM   6277  N  NZ    . LYS B 1 88  ? 154.735 144.157 181.253 1.00 48.03 1  88  LYS B NZ    1 
ATOM   6278  N  N     . PHE B 1 89  ? 149.590 143.605 175.760 1.00 42.54 ?  89  PHE B N     1 
ATOM   6279  C  CA    . PHE B 1 89  ? 148.455 142.809 175.320 1.00 38.86 ?  89  PHE B CA    1 
ATOM   6280  C  C     . PHE B 1 89  ? 148.876 141.370 175.052 1.00 41.78 ?  89  PHE B C     1 
ATOM   6281  O  O     . PHE B 1 89  ? 149.902 141.111 174.417 1.00 43.45 ?  89  PHE B O     1 
ATOM   6282  C  CB    . PHE B 1 89  ? 147.839 143.416 174.059 1.00 40.58 ?  89  PHE B CB    1 
ATOM   6283  C  CG    . PHE B 1 89  ? 146.809 142.540 173.411 1.00 38.45 ?  89  PHE B CG    1 
ATOM   6284  C  CD1   . PHE B 1 89  ? 145.505 142.523 173.873 1.00 37.30 ?  89  PHE B CD1   1 
ATOM   6285  C  CD2   . PHE B 1 89  ? 147.145 141.726 172.344 1.00 39.93 ?  89  PHE B CD2   1 
ATOM   6286  C  CE1   . PHE B 1 89  ? 144.559 141.713 173.283 1.00 39.83 ?  89  PHE B CE1   1 
ATOM   6287  C  CE2   . PHE B 1 89  ? 146.201 140.915 171.749 1.00 36.99 ?  89  PHE B CE2   1 
ATOM   6288  C  CZ    . PHE B 1 89  ? 144.906 140.909 172.220 1.00 37.52 ?  89  PHE B CZ    1 
ATOM   6289  N  N     . ARG B 1 90  ? 148.067 140.432 175.535 1.00 46.37 ?  90  ARG B N     1 
ATOM   6290  C  CA    . ARG B 1 90  ? 148.301 139.009 175.336 1.00 42.24 ?  90  ARG B CA    1 
ATOM   6291  C  C     . ARG B 1 90  ? 147.070 138.391 174.692 1.00 44.30 ?  90  ARG B C     1 
ATOM   6292  O  O     . ARG B 1 90  ? 145.947 138.621 175.149 1.00 47.76 ?  90  ARG B O     1 
ATOM   6293  C  CB    . ARG B 1 90  ? 148.613 138.307 176.660 1.00 46.37 ?  90  ARG B CB    1 
ATOM   6294  C  CG    . ARG B 1 90  ? 149.857 138.822 177.356 1.00 47.77 ?  90  ARG B CG    1 
ATOM   6295  C  CD    . ARG B 1 90  ? 151.103 138.519 176.546 1.00 48.86 ?  90  ARG B CD    1 
ATOM   6296  N  NE    . ARG B 1 90  ? 152.301 139.072 177.165 1.00 49.24 ?  90  ARG B NE    1 
ATOM   6297  C  CZ    . ARG B 1 90  ? 152.945 140.141 176.722 1.00 49.26 ?  90  ARG B CZ    1 
ATOM   6298  N  NH1   . ARG B 1 90  ? 152.537 140.799 175.650 1.00 49.65 1  90  ARG B NH1   1 
ATOM   6299  N  NH2   . ARG B 1 90  ? 154.029 140.560 177.368 1.00 48.11 ?  90  ARG B NH2   1 
ATOM   6300  N  N     . PHE B 1 91  ? 147.282 137.622 173.635 1.00 40.35 ?  91  PHE B N     1 
ATOM   6301  C  CA    . PHE B 1 91  ? 146.181 136.900 173.015 1.00 39.15 ?  91  PHE B CA    1 
ATOM   6302  C  C     . PHE B 1 91  ? 145.672 135.829 173.973 1.00 43.83 ?  91  PHE B C     1 
ATOM   6303  O  O     . PHE B 1 91  ? 146.472 135.050 174.503 1.00 46.77 ?  91  PHE B O     1 
ATOM   6304  C  CB    . PHE B 1 91  ? 146.625 136.270 171.699 1.00 38.31 ?  91  PHE B CB    1 
ATOM   6305  C  CG    . PHE B 1 91  ? 146.788 137.257 170.581 1.00 40.70 ?  91  PHE B CG    1 
ATOM   6306  C  CD1   . PHE B 1 91  ? 145.688 137.702 169.867 1.00 41.68 ?  91  PHE B CD1   1 
ATOM   6307  C  CD2   . PHE B 1 91  ? 148.038 137.741 170.244 1.00 41.13 ?  91  PHE B CD2   1 
ATOM   6308  C  CE1   . PHE B 1 91  ? 145.835 138.610 168.838 1.00 40.33 ?  91  PHE B CE1   1 
ATOM   6309  C  CE2   . PHE B 1 91  ? 148.190 138.649 169.217 1.00 41.67 ?  91  PHE B CE2   1 
ATOM   6310  C  CZ    . PHE B 1 91  ? 147.088 139.084 168.513 1.00 38.79 ?  91  PHE B CZ    1 
ATOM   6311  N  N     . PRO B 1 92  ? 144.362 135.757 174.224 1.00 43.98 ?  92  PRO B N     1 
ATOM   6312  C  CA    . PRO B 1 92  ? 143.858 134.779 175.197 1.00 42.98 ?  92  PRO B CA    1 
ATOM   6313  C  C     . PRO B 1 92  ? 143.747 133.369 174.650 1.00 44.07 ?  92  PRO B C     1 
ATOM   6314  O  O     . PRO B 1 92  ? 143.607 132.428 175.443 1.00 45.15 ?  92  PRO B O     1 
ATOM   6315  C  CB    . PRO B 1 92  ? 142.480 135.336 175.563 1.00 45.11 ?  92  PRO B CB    1 
ATOM   6316  C  CG    . PRO B 1 92  ? 142.033 136.012 174.307 1.00 44.05 ?  92  PRO B CG    1 
ATOM   6317  C  CD    . PRO B 1 92  ? 143.276 136.569 173.646 1.00 42.67 ?  92  PRO B CD    1 
ATOM   6318  N  N     . SER B 1 93  ? 143.808 133.188 173.334 1.00 41.81 ?  93  SER B N     1 
ATOM   6319  C  CA    . SER B 1 93  ? 143.654 131.878 172.725 1.00 40.61 ?  93  SER B CA    1 
ATOM   6320  C  C     . SER B 1 93  ? 144.621 131.750 171.559 1.00 42.30 ?  93  SER B C     1 
ATOM   6321  O  O     . SER B 1 93  ? 145.106 132.743 171.013 1.00 44.47 ?  93  SER B O     1 
ATOM   6322  C  CB    . SER B 1 93  ? 142.213 131.644 172.253 1.00 43.98 ?  93  SER B CB    1 
ATOM   6323  O  OG    . SER B 1 93  ? 141.999 132.192 170.965 1.00 45.31 ?  93  SER B OG    1 
ATOM   6324  N  N     . PHE B 1 94  ? 144.902 130.501 171.185 1.00 44.94 ?  94  PHE B N     1 
ATOM   6325  C  CA    . PHE B 1 94  ? 145.812 130.253 170.072 1.00 43.39 ?  94  PHE B CA    1 
ATOM   6326  C  C     . PHE B 1 94  ? 145.233 130.757 168.757 1.00 41.45 ?  94  PHE B C     1 
ATOM   6327  O  O     . PHE B 1 94  ? 145.968 131.265 167.903 1.00 45.37 ?  94  PHE B O     1 
ATOM   6328  C  CB    . PHE B 1 94  ? 146.132 128.763 169.973 1.00 43.45 ?  94  PHE B CB    1 
ATOM   6329  C  CG    . PHE B 1 94  ? 146.683 128.352 168.638 1.00 43.45 ?  94  PHE B CG    1 
ATOM   6330  C  CD1   . PHE B 1 94  ? 147.937 128.772 168.232 1.00 42.49 ?  94  PHE B CD1   1 
ATOM   6331  C  CD2   . PHE B 1 94  ? 145.938 127.564 167.780 1.00 45.55 ?  94  PHE B CD2   1 
ATOM   6332  C  CE1   . PHE B 1 94  ? 148.442 128.402 167.000 1.00 43.20 ?  94  PHE B CE1   1 
ATOM   6333  C  CE2   . PHE B 1 94  ? 146.437 127.191 166.548 1.00 43.74 ?  94  PHE B CE2   1 
ATOM   6334  C  CZ    . PHE B 1 94  ? 147.691 127.611 166.159 1.00 42.28 ?  94  PHE B CZ    1 
ATOM   6335  N  N     . MET B 1 95  ? 143.918 130.616 168.569 1.00 42.07 ?  95  MET B N     1 
ATOM   6336  C  CA    . MET B 1 95  ? 143.320 130.967 167.286 1.00 40.51 ?  95  MET B CA    1 
ATOM   6337  C  C     . MET B 1 95  ? 143.415 132.462 167.010 1.00 44.61 ?  95  MET B C     1 
ATOM   6338  O  O     . MET B 1 95  ? 143.589 132.868 165.860 1.00 47.46 ?  95  MET B O     1 
ATOM   6339  C  CB    . MET B 1 95  ? 141.866 130.504 167.236 1.00 45.56 ?  95  MET B CB    1 
ATOM   6340  C  CG    . MET B 1 95  ? 141.375 130.168 165.838 1.00 47.18 ?  95  MET B CG    1 
ATOM   6341  S  SD    . MET B 1 95  ? 142.468 129.029 164.968 1.00 58.80 ?  95  MET B SD    1 
ATOM   6342  C  CE    . MET B 1 95  ? 142.497 127.656 166.115 1.00 47.39 ?  95  MET B CE    1 
ATOM   6343  N  N     . SER B 1 96  ? 143.301 133.297 168.044 1.00 38.62 ?  96  SER B N     1 
ATOM   6344  C  CA    . SER B 1 96  ? 143.400 134.740 167.834 1.00 34.16 ?  96  SER B CA    1 
ATOM   6345  C  C     . SER B 1 96  ? 144.758 135.118 167.259 1.00 37.96 ?  96  SER B C     1 
ATOM   6346  O  O     . SER B 1 96  ? 144.849 135.795 166.226 1.00 40.50 ?  96  SER B O     1 
ATOM   6347  C  CB    . SER B 1 96  ? 143.150 135.475 169.149 1.00 39.21 ?  96  SER B CB    1 
ATOM   6348  O  OG    . SER B 1 96  ? 142.002 134.972 169.804 1.00 48.18 ?  96  SER B OG    1 
ATOM   6349  N  N     . ALA B 1 97  ? 145.833 134.680 167.920 1.00 39.34 ?  97  ALA B N     1 
ATOM   6350  C  CA    . ALA B 1 97  ? 147.176 134.993 167.450 1.00 37.47 ?  97  ALA B CA    1 
ATOM   6351  C  C     . ALA B 1 97  ? 147.451 134.346 166.101 1.00 38.76 ?  97  ALA B C     1 
ATOM   6352  O  O     . ALA B 1 97  ? 148.086 134.956 165.234 1.00 41.59 ?  97  ALA B O     1 
ATOM   6353  C  CB    . ALA B 1 97  ? 148.209 134.550 168.483 1.00 38.84 ?  97  ALA B CB    1 
ATOM   6354  N  N     . PHE B 1 98  ? 146.989 133.111 165.905 1.00 36.26 ?  98  PHE B N     1 
ATOM   6355  C  CA    . PHE B 1 98  ? 147.191 132.448 164.623 1.00 36.34 ?  98  PHE B CA    1 
ATOM   6356  C  C     . PHE B 1 98  ? 146.529 133.231 163.497 1.00 40.58 ?  98  PHE B C     1 
ATOM   6357  O  O     . PHE B 1 98  ? 147.144 133.483 162.455 1.00 44.37 ?  98  PHE B O     1 
ATOM   6358  C  CB    . PHE B 1 98  ? 146.649 131.021 164.678 1.00 40.04 ?  98  PHE B CB    1 
ATOM   6359  C  CG    . PHE B 1 98  ? 146.737 130.290 163.371 1.00 43.09 ?  98  PHE B CG    1 
ATOM   6360  C  CD1   . PHE B 1 98  ? 147.928 129.715 162.963 1.00 43.71 ?  98  PHE B CD1   1 
ATOM   6361  C  CD2   . PHE B 1 98  ? 145.633 130.187 162.543 1.00 42.58 ?  98  PHE B CD2   1 
ATOM   6362  C  CE1   . PHE B 1 98  ? 148.013 129.046 161.760 1.00 43.05 ?  98  PHE B CE1   1 
ATOM   6363  C  CE2   . PHE B 1 98  ? 145.712 129.521 161.338 1.00 44.08 ?  98  PHE B CE2   1 
ATOM   6364  C  CZ    . PHE B 1 98  ? 146.903 128.950 160.946 1.00 43.95 ?  98  PHE B CZ    1 
ATOM   6365  N  N     . LYS B 1 99  ? 145.275 133.640 163.698 1.00 39.75 ?  99  LYS B N     1 
ATOM   6366  C  CA    . LYS B 1 99  ? 144.566 134.396 162.675 1.00 40.49 ?  99  LYS B CA    1 
ATOM   6367  C  C     . LYS B 1 99  ? 145.263 135.719 162.398 1.00 41.72 ?  99  LYS B C     1 
ATOM   6368  O  O     . LYS B 1 99  ? 145.460 136.098 161.238 1.00 43.38 ?  99  LYS B O     1 
ATOM   6369  C  CB    . LYS B 1 99  ? 143.118 134.631 163.107 1.00 41.00 ?  99  LYS B CB    1 
ATOM   6370  C  CG    . LYS B 1 99  ? 142.248 133.386 163.081 1.00 45.10 ?  99  LYS B CG    1 
ATOM   6371  C  CD    . LYS B 1 99  ? 142.426 132.611 161.789 1.00 44.72 ?  99  LYS B CD    1 
ATOM   6372  C  CE    . LYS B 1 99  ? 141.089 132.331 161.128 1.00 42.86 ?  99  LYS B CE    1 
ATOM   6373  N  NZ    . LYS B 1 99  ? 141.215 132.183 159.653 1.00 45.26 1  99  LYS B NZ    1 
ATOM   6374  N  N     . PHE B 1 100 ? 145.658 136.436 163.454 1.00 37.29 ?  100 PHE B N     1 
ATOM   6375  C  CA    . PHE B 1 100 ? 146.321 137.716 163.238 1.00 36.78 ?  100 PHE B CA    1 
ATOM   6376  C  C     . PHE B 1 100 ? 147.614 137.539 162.454 1.00 37.00 ?  100 PHE B C     1 
ATOM   6377  O  O     . PHE B 1 100 ? 147.828 138.197 161.432 1.00 42.39 ?  100 PHE B O     1 
ATOM   6378  C  CB    . PHE B 1 100 ? 146.601 138.414 164.567 1.00 37.42 ?  100 PHE B CB    1 
ATOM   6379  C  CG    . PHE B 1 100 ? 147.412 139.668 164.415 1.00 39.02 ?  100 PHE B CG    1 
ATOM   6380  C  CD1   . PHE B 1 100 ? 146.852 140.809 163.865 1.00 38.29 ?  100 PHE B CD1   1 
ATOM   6381  C  CD2   . PHE B 1 100 ? 148.742 139.698 164.794 1.00 34.34 ?  100 PHE B CD2   1 
ATOM   6382  C  CE1   . PHE B 1 100 ? 147.598 141.959 163.712 1.00 39.20 ?  100 PHE B CE1   1 
ATOM   6383  C  CE2   . PHE B 1 100 ? 149.494 140.845 164.644 1.00 37.15 ?  100 PHE B CE2   1 
ATOM   6384  C  CZ    . PHE B 1 100 ? 148.922 141.977 164.102 1.00 39.31 ?  100 PHE B CZ    1 
ATOM   6385  N  N     . TYR B 1 101 ? 148.481 136.634 162.905 1.00 40.77 ?  101 TYR B N     1 
ATOM   6386  C  CA    . TYR B 1 101 ? 149.794 136.486 162.297 1.00 40.40 ?  101 TYR B CA    1 
ATOM   6387  C  C     . TYR B 1 101 ? 149.763 135.724 160.981 1.00 40.20 ?  101 TYR B C     1 
ATOM   6388  O  O     . TYR B 1 101 ? 150.795 135.652 160.307 1.00 47.74 ?  101 TYR B O     1 
ATOM   6389  C  CB    . TYR B 1 101 ? 150.744 135.806 163.283 1.00 39.30 ?  101 TYR B CB    1 
ATOM   6390  C  CG    . TYR B 1 101 ? 151.173 136.731 164.395 1.00 39.69 ?  101 TYR B CG    1 
ATOM   6391  C  CD1   . TYR B 1 101 ? 152.119 137.721 164.173 1.00 36.35 ?  101 TYR B CD1   1 
ATOM   6392  C  CD2   . TYR B 1 101 ? 150.607 136.639 165.658 1.00 41.02 ?  101 TYR B CD2   1 
ATOM   6393  C  CE1   . TYR B 1 101 ? 152.504 138.577 165.181 1.00 38.63 ?  101 TYR B CE1   1 
ATOM   6394  C  CE2   . TYR B 1 101 ? 150.984 137.493 166.672 1.00 39.74 ?  101 TYR B CE2   1 
ATOM   6395  C  CZ    . TYR B 1 101 ? 151.933 138.459 166.429 1.00 40.12 ?  101 TYR B CZ    1 
ATOM   6396  O  OH    . TYR B 1 101 ? 152.315 139.312 167.437 1.00 39.35 ?  101 TYR B OH    1 
ATOM   6397  N  N     . ASN B 1 102 ? 148.622 135.153 160.598 1.00 43.08 ?  102 ASN B N     1 
ATOM   6398  C  CA    . ASN B 1 102 ? 148.501 134.539 159.285 1.00 43.24 ?  102 ASN B CA    1 
ATOM   6399  C  C     . ASN B 1 102 ? 147.765 135.407 158.275 1.00 43.01 ?  102 ASN B C     1 
ATOM   6400  O  O     . ASN B 1 102 ? 147.991 135.246 157.070 1.00 44.96 ?  102 ASN B O     1 
ATOM   6401  C  CB    . ASN B 1 102 ? 147.788 133.186 159.395 1.00 41.97 ?  102 ASN B CB    1 
ATOM   6402  C  CG    . ASN B 1 102 ? 148.713 132.076 159.849 1.00 47.53 ?  102 ASN B CG    1 
ATOM   6403  O  OD1   . ASN B 1 102 ? 149.555 132.273 160.724 1.00 49.01 ?  102 ASN B OD1   1 
ATOM   6404  N  ND2   . ASN B 1 102 ? 148.564 130.902 159.250 1.00 46.37 ?  102 ASN B ND2   1 
ATOM   6405  N  N     . ASP B 1 103 ? 146.905 136.320 158.720 1.00 41.74 ?  103 ASP B N     1 
ATOM   6406  C  CA    . ASP B 1 103 ? 146.118 137.142 157.809 1.00 41.03 ?  103 ASP B CA    1 
ATOM   6407  C  C     . ASP B 1 103 ? 146.517 138.609 157.797 1.00 40.03 ?  103 ASP B C     1 
ATOM   6408  O  O     . ASP B 1 103 ? 146.625 139.199 156.721 1.00 45.56 ?  103 ASP B O     1 
ATOM   6409  C  CB    . ASP B 1 103 ? 144.629 137.037 158.161 1.00 41.56 ?  103 ASP B CB    1 
ATOM   6410  C  CG    . ASP B 1 103 ? 144.173 135.605 158.355 1.00 44.06 ?  103 ASP B CG    1 
ATOM   6411  O  OD1   . ASP B 1 103 ? 144.937 134.810 158.941 1.00 45.77 ?  103 ASP B OD1   1 
ATOM   6412  O  OD2   . ASP B 1 103 ? 143.047 135.275 157.926 1.00 48.17 -1 103 ASP B OD2   1 
ATOM   6413  N  N     . TYR B 1 104 ? 146.742 139.219 158.959 1.00 35.25 ?  104 TYR B N     1 
ATOM   6414  C  CA    . TYR B 1 104 ? 146.907 140.663 159.051 1.00 39.29 ?  104 TYR B CA    1 
ATOM   6415  C  C     . TYR B 1 104 ? 148.321 141.107 159.387 1.00 40.58 ?  104 TYR B C     1 
ATOM   6416  O  O     . TYR B 1 104 ? 148.696 142.227 159.036 1.00 44.14 ?  104 TYR B O     1 
ATOM   6417  C  CB    . TYR B 1 104 ? 145.943 141.236 160.099 1.00 37.09 ?  104 TYR B CB    1 
ATOM   6418  C  CG    . TYR B 1 104 ? 144.511 140.805 159.882 1.00 39.90 ?  104 TYR B CG    1 
ATOM   6419  C  CD1   . TYR B 1 104 ? 144.039 139.612 160.415 1.00 34.86 ?  104 TYR B CD1   1 
ATOM   6420  C  CD2   . TYR B 1 104 ? 143.637 141.577 159.131 1.00 38.68 ?  104 TYR B CD2   1 
ATOM   6421  C  CE1   . TYR B 1 104 ? 142.736 139.208 160.214 1.00 37.19 ?  104 TYR B CE1   1 
ATOM   6422  C  CE2   . TYR B 1 104 ? 142.332 141.181 158.925 1.00 37.12 ?  104 TYR B CE2   1 
ATOM   6423  C  CZ    . TYR B 1 104 ? 141.886 139.995 159.469 1.00 40.17 ?  104 TYR B CZ    1 
ATOM   6424  O  OH    . TYR B 1 104 ? 140.587 139.595 159.266 1.00 39.01 ?  104 TYR B OH    1 
ATOM   6425  N  N     . ALA B 1 105 ? 149.111 140.269 160.051 1.00 43.93 ?  105 ALA B N     1 
ATOM   6426  C  CA    . ALA B 1 105 ? 150.477 140.652 160.384 1.00 40.43 ?  105 ALA B CA    1 
ATOM   6427  C  C     . ALA B 1 105 ? 151.301 140.822 159.117 1.00 44.75 ?  105 ALA B C     1 
ATOM   6428  O  O     . ALA B 1 105 ? 151.346 139.931 158.264 1.00 44.56 ?  105 ALA B O     1 
ATOM   6429  C  CB    . ALA B 1 105 ? 151.115 139.605 161.296 1.00 39.65 ?  105 ALA B CB    1 
ATOM   6430  N  N     . LEU B 1 106 ? 151.953 141.976 158.993 1.00 49.54 ?  106 LEU B N     1 
ATOM   6431  C  CA    . LEU B 1 106 ? 152.786 142.236 157.827 1.00 46.86 ?  106 LEU B CA    1 
ATOM   6432  C  C     . LEU B 1 106 ? 153.957 141.264 157.786 1.00 49.23 ?  106 LEU B C     1 
ATOM   6433  O  O     . LEU B 1 106 ? 154.660 141.074 158.783 1.00 47.13 ?  106 LEU B O     1 
ATOM   6434  C  CB    . LEU B 1 106 ? 153.293 143.677 157.848 1.00 47.92 ?  106 LEU B CB    1 
ATOM   6435  C  CG    . LEU B 1 106 ? 154.202 144.096 156.689 1.00 45.94 ?  106 LEU B CG    1 
ATOM   6436  C  CD1   . LEU B 1 106 ? 153.402 144.258 155.409 1.00 45.49 ?  106 LEU B CD1   1 
ATOM   6437  C  CD2   . LEU B 1 106 ? 154.943 145.379 157.024 1.00 48.66 ?  106 LEU B CD2   1 
ATOM   6438  N  N     . LYS B 1 107 ? 154.165 140.651 156.626 1.00 55.82 ?  107 LYS B N     1 
ATOM   6439  C  CA    . LYS B 1 107 ? 155.242 139.698 156.417 1.00 54.78 ?  107 LYS B CA    1 
ATOM   6440  C  C     . LYS B 1 107 ? 156.133 140.169 155.278 1.00 56.39 ?  107 LYS B C     1 
ATOM   6441  O  O     . LYS B 1 107 ? 155.700 140.917 154.397 1.00 58.89 ?  107 LYS B O     1 
ATOM   6442  C  CB    . LYS B 1 107 ? 154.698 138.300 156.107 1.00 54.78 ?  107 LYS B CB    1 
ATOM   6443  C  CG    . LYS B 1 107 ? 154.517 137.423 157.331 1.00 53.47 ?  107 LYS B CG    1 
ATOM   6444  C  CD    . LYS B 1 107 ? 153.540 136.297 157.057 1.00 55.25 ?  107 LYS B CD    1 
ATOM   6445  C  CE    . LYS B 1 107 ? 152.668 136.026 158.268 1.00 55.87 ?  107 LYS B CE    1 
ATOM   6446  N  NZ    . LYS B 1 107 ? 152.745 134.607 158.711 1.00 56.81 1  107 LYS B NZ    1 
ATOM   6447  N  N     . THR B 1 108 ? 157.388 139.727 155.308 1.00 63.32 ?  108 THR B N     1 
ATOM   6448  C  CA    . THR B 1 108 ? 158.324 140.059 154.247 1.00 62.76 ?  108 THR B CA    1 
ATOM   6449  C  C     . THR B 1 108 ? 157.763 139.626 152.894 1.00 62.84 ?  108 THR B C     1 
ATOM   6450  O  O     . THR B 1 108 ? 156.835 138.819 152.803 1.00 63.04 ?  108 THR B O     1 
ATOM   6451  C  CB    . THR B 1 108 ? 159.677 139.396 154.499 1.00 61.77 ?  108 THR B CB    1 
ATOM   6452  O  OG1   . THR B 1 108 ? 159.493 137.987 154.688 1.00 64.87 ?  108 THR B OG1   1 
ATOM   6453  C  CG2   . THR B 1 108 ? 160.333 139.984 155.738 1.00 58.88 ?  108 THR B CG2   1 
ATOM   6454  N  N     . ASN B 1 109 ? 158.348 140.178 151.827 1.00 63.95 ?  109 ASN B N     1 
ATOM   6455  C  CA    . ASN B 1 109 ? 157.818 139.933 150.489 1.00 64.76 ?  109 ASN B CA    1 
ATOM   6456  C  C     . ASN B 1 109 ? 157.778 138.446 150.159 1.00 67.24 ?  109 ASN B C     1 
ATOM   6457  O  O     . ASN B 1 109 ? 156.964 138.017 149.334 1.00 66.93 ?  109 ASN B O     1 
ATOM   6458  C  CB    . ASN B 1 109 ? 158.648 140.685 149.447 1.00 63.21 ?  109 ASN B CB    1 
ATOM   6459  C  CG    . ASN B 1 109 ? 159.126 142.034 149.944 1.00 65.72 ?  109 ASN B CG    1 
ATOM   6460  O  OD1   . ASN B 1 109 ? 159.903 142.118 150.895 1.00 67.07 ?  109 ASN B OD1   1 
ATOM   6461  N  ND2   . ASN B 1 109 ? 158.658 143.100 149.304 1.00 64.37 ?  109 ASN B ND2   1 
ATOM   6462  N  N     . ASP B 1 110 ? 158.640 137.650 150.785 1.00 69.11 ?  110 ASP B N     1 
ATOM   6463  C  CA    . ASP B 1 110 ? 158.643 136.207 150.592 1.00 69.08 ?  110 ASP B CA    1 
ATOM   6464  C  C     . ASP B 1 110 ? 157.693 135.481 151.537 1.00 70.67 ?  110 ASP B C     1 
ATOM   6465  O  O     . ASP B 1 110 ? 157.594 134.252 151.470 1.00 70.16 ?  110 ASP B O     1 
ATOM   6466  C  CB    . ASP B 1 110 ? 160.064 135.657 150.758 1.00 68.81 ?  110 ASP B CB    1 
ATOM   6467  C  CG    . ASP B 1 110 ? 160.566 135.756 152.185 1.00 71.80 ?  110 ASP B CG    1 
ATOM   6468  O  OD1   . ASP B 1 110 ? 159.934 136.469 152.993 1.00 72.04 ?  110 ASP B OD1   1 
ATOM   6469  O  OD2   . ASP B 1 110 ? 161.597 135.125 152.499 1.00 71.42 -1 110 ASP B OD2   1 
ATOM   6470  N  N     . LYS B 1 111 ? 156.995 136.209 152.409 1.00 68.77 ?  111 LYS B N     1 
ATOM   6471  C  CA    . LYS B 1 111 ? 156.081 135.607 153.378 1.00 68.39 ?  111 LYS B CA    1 
ATOM   6472  C  C     . LYS B 1 111 ? 156.804 134.589 154.256 1.00 69.29 ?  111 LYS B C     1 
ATOM   6473  O  O     . LYS B 1 111 ? 156.267 133.531 154.586 1.00 70.03 ?  111 LYS B O     1 
ATOM   6474  C  CB    . LYS B 1 111 ? 154.877 134.969 152.682 1.00 68.72 ?  111 LYS B CB    1 
ATOM   6475  C  CG    . LYS B 1 111 ? 153.873 135.973 152.140 1.00 69.14 ?  111 LYS B CG    1 
ATOM   6476  C  CD    . LYS B 1 111 ? 154.338 136.564 150.819 1.00 69.28 ?  111 LYS B CD    1 
ATOM   6477  C  CE    . LYS B 1 111 ? 153.474 137.743 150.404 1.00 69.63 ?  111 LYS B CE    1 
ATOM   6478  N  NZ    . LYS B 1 111 ? 153.575 138.875 151.367 1.00 69.38 1  111 LYS B NZ    1 
ATOM   6479  N  N     . LYS B 1 112 ? 158.036 134.912 154.637 1.00 68.98 ?  112 LYS B N     1 
ATOM   6480  C  CA    . LYS B 1 112 ? 158.862 134.045 155.466 1.00 68.89 ?  112 LYS B CA    1 
ATOM   6481  C  C     . LYS B 1 112 ? 159.027 134.551 156.889 1.00 68.08 ?  112 LYS B C     1 
ATOM   6482  O  O     . LYS B 1 112 ? 158.997 133.754 157.830 1.00 68.93 ?  112 LYS B O     1 
ATOM   6483  C  CB    . LYS B 1 112 ? 160.246 133.870 154.825 1.00 68.36 ?  112 LYS B CB    1 
ATOM   6484  C  CG    . LYS B 1 112 ? 161.359 133.496 155.793 1.00 68.62 ?  112 LYS B CG    1 
ATOM   6485  C  CD    . LYS B 1 112 ? 161.064 132.190 156.514 1.00 69.50 ?  112 LYS B CD    1 
ATOM   6486  C  CE    . LYS B 1 112 ? 161.690 132.172 157.899 1.00 69.40 ?  112 LYS B CE    1 
ATOM   6487  N  NZ    . LYS B 1 112 ? 161.158 133.255 158.769 1.00 68.38 1  112 LYS B NZ    1 
ATOM   6488  N  N     . LYS B 1 113 ? 159.194 135.857 157.074 1.00 62.09 ?  113 LYS B N     1 
ATOM   6489  C  CA    . LYS B 1 113 ? 159.390 136.456 158.384 1.00 60.97 ?  113 LYS B CA    1 
ATOM   6490  C  C     . LYS B 1 113 ? 158.235 137.394 158.707 1.00 61.58 ?  113 LYS B C     1 
ATOM   6491  O  O     . LYS B 1 113 ? 157.476 137.814 157.830 1.00 60.32 ?  113 LYS B O     1 
ATOM   6492  C  CB    . LYS B 1 113 ? 160.723 137.211 158.449 1.00 60.66 ?  113 LYS B CB    1 
ATOM   6493  C  CG    . LYS B 1 113 ? 161.927 136.326 158.706 1.00 61.33 ?  113 LYS B CG    1 
ATOM   6494  C  CD    . LYS B 1 113 ? 161.976 135.881 160.156 1.00 63.61 ?  113 LYS B CD    1 
ATOM   6495  C  CE    . LYS B 1 113 ? 163.245 135.101 160.451 1.00 62.03 ?  113 LYS B CE    1 
ATOM   6496  N  NZ    . LYS B 1 113 ? 163.266 134.601 161.852 1.00 61.63 1  113 LYS B NZ    1 
ATOM   6497  N  N     . ILE B 1 114 ? 158.110 137.721 159.990 1.00 55.72 ?  114 ILE B N     1 
ATOM   6498  C  CA    . ILE B 1 114 ? 157.067 138.610 160.490 1.00 53.62 ?  114 ILE B CA    1 
ATOM   6499  C  C     . ILE B 1 114 ? 157.696 139.967 160.769 1.00 54.58 ?  114 ILE B C     1 
ATOM   6500  O  O     . ILE B 1 114 ? 158.630 140.076 161.572 1.00 56.68 ?  114 ILE B O     1 
ATOM   6501  C  CB    . ILE B 1 114 ? 156.399 138.046 161.753 1.00 54.14 ?  114 ILE B CB    1 
ATOM   6502  C  CG1   . ILE B 1 114 ? 155.625 136.768 161.425 1.00 54.38 ?  114 ILE B CG1   1 
ATOM   6503  C  CG2   . ILE B 1 114 ? 155.481 139.082 162.381 1.00 54.93 ?  114 ILE B CG2   1 
ATOM   6504  C  CD1   . ILE B 1 114 ? 155.332 135.909 162.634 1.00 52.29 ?  114 ILE B CD1   1 
ATOM   6505  N  N     . LEU B 1 115 ? 157.181 141.003 160.107 1.00 51.13 ?  115 LEU B N     1 
ATOM   6506  C  CA    . LEU B 1 115 ? 157.661 142.363 160.312 1.00 51.57 ?  115 LEU B CA    1 
ATOM   6507  C  C     . LEU B 1 115 ? 156.815 143.158 161.296 1.00 51.66 ?  115 LEU B C     1 
ATOM   6508  O  O     . LEU B 1 115 ? 157.311 144.137 161.863 1.00 51.75 ?  115 LEU B O     1 
ATOM   6509  C  CB    . LEU B 1 115 ? 157.714 143.115 158.978 1.00 51.71 ?  115 LEU B CB    1 
ATOM   6510  C  CG    . LEU B 1 115 ? 158.900 142.791 158.070 1.00 50.05 ?  115 LEU B CG    1 
ATOM   6511  C  CD1   . LEU B 1 115 ? 158.658 143.332 156.674 1.00 49.98 ?  115 LEU B CD1   1 
ATOM   6512  C  CD2   . LEU B 1 115 ? 160.186 143.354 158.652 1.00 52.37 ?  115 LEU B CD2   1 
ATOM   6513  N  N     . GLU B 1 116 ? 155.563 142.767 161.510 1.00 50.83 ?  116 GLU B N     1 
ATOM   6514  C  CA    . GLU B 1 116 ? 154.651 143.479 162.393 1.00 47.69 ?  116 GLU B CA    1 
ATOM   6515  C  C     . GLU B 1 116 ? 154.132 142.553 163.481 1.00 46.32 ?  116 GLU B C     1 
ATOM   6516  O  O     . GLU B 1 116 ? 153.772 141.403 163.213 1.00 48.09 ?  116 GLU B O     1 
ATOM   6517  C  CB    . GLU B 1 116 ? 153.463 144.053 161.620 1.00 47.33 ?  116 GLU B CB    1 
ATOM   6518  C  CG    . GLU B 1 116 ? 153.623 145.493 161.186 1.00 48.08 ?  116 GLU B CG    1 
ATOM   6519  C  CD    . GLU B 1 116 ? 152.462 145.964 160.337 1.00 49.28 ?  116 GLU B CD    1 
ATOM   6520  O  OE1   . GLU B 1 116 ? 151.549 145.154 160.078 1.00 47.76 ?  116 GLU B OE1   1 
ATOM   6521  O  OE2   . GLU B 1 116 ? 152.458 147.145 159.936 1.00 50.76 -1 116 GLU B OE2   1 
ATOM   6522  N  N     . ARG B 1 117 ? 154.094 143.065 164.706 1.00 41.46 ?  117 ARG B N     1 
ATOM   6523  C  CA    . ARG B 1 117 ? 153.359 142.427 165.782 1.00 41.30 ?  117 ARG B CA    1 
ATOM   6524  C  C     . ARG B 1 117 ? 151.969 143.053 165.870 1.00 43.58 ?  117 ARG B C     1 
ATOM   6525  O  O     . ARG B 1 117 ? 151.614 143.949 165.101 1.00 45.06 ?  117 ARG B O     1 
ATOM   6526  C  CB    . ARG B 1 117 ? 154.112 142.558 167.104 1.00 44.32 ?  117 ARG B CB    1 
ATOM   6527  C  CG    . ARG B 1 117 ? 155.594 142.253 167.009 1.00 44.87 ?  117 ARG B CG    1 
ATOM   6528  C  CD    . ARG B 1 117 ? 155.836 140.857 166.462 1.00 47.44 ?  117 ARG B CD    1 
ATOM   6529  N  NE    . ARG B 1 117 ? 155.531 139.816 167.438 1.00 46.63 ?  117 ARG B NE    1 
ATOM   6530  C  CZ    . ARG B 1 117 ? 156.059 139.741 168.652 1.00 48.01 ?  117 ARG B CZ    1 
ATOM   6531  N  NH1   . ARG B 1 117 ? 156.929 140.638 169.086 1.00 47.56 1  117 ARG B NH1   1 
ATOM   6532  N  NH2   . ARG B 1 117 ? 155.707 138.738 169.451 1.00 47.81 ?  117 ARG B NH2   1 
ATOM   6533  N  N     . TYR B 1 118 ? 151.166 142.579 166.822 1.00 41.39 ?  118 TYR B N     1 
ATOM   6534  C  CA    . TYR B 1 118 ? 149.856 143.186 167.029 1.00 36.05 ?  118 TYR B CA    1 
ATOM   6535  C  C     . TYR B 1 118 ? 149.996 144.654 167.411 1.00 36.86 ?  118 TYR B C     1 
ATOM   6536  O  O     . TYR B 1 118 ? 149.256 145.509 166.909 1.00 36.77 ?  118 TYR B O     1 
ATOM   6537  C  CB    . TYR B 1 118 ? 149.084 142.417 168.099 1.00 33.74 ?  118 TYR B CB    1 
ATOM   6538  C  CG    . TYR B 1 118 ? 147.609 142.734 168.135 1.00 36.39 ?  118 TYR B CG    1 
ATOM   6539  C  CD1   . TYR B 1 118 ? 146.813 142.540 167.015 1.00 32.81 ?  118 TYR B CD1   1 
ATOM   6540  C  CD2   . TYR B 1 118 ? 147.012 143.227 169.286 1.00 37.20 ?  118 TYR B CD2   1 
ATOM   6541  C  CE1   . TYR B 1 118 ? 145.467 142.828 167.040 1.00 33.45 ?  118 TYR B CE1   1 
ATOM   6542  C  CE2   . TYR B 1 118 ? 145.664 143.515 169.321 1.00 33.90 ?  118 TYR B CE2   1 
ATOM   6543  C  CZ    . TYR B 1 118 ? 144.897 143.313 168.195 1.00 37.27 ?  118 TYR B CZ    1 
ATOM   6544  O  OH    . TYR B 1 118 ? 143.552 143.602 168.223 1.00 41.16 ?  118 TYR B OH    1 
ATOM   6545  N  N     . GLU B 1 119 ? 150.951 144.964 168.289 1.00 42.55 ?  119 GLU B N     1 
ATOM   6546  C  CA    . GLU B 1 119 ? 151.172 146.349 168.687 1.00 36.31 ?  119 GLU B CA    1 
ATOM   6547  C  C     . GLU B 1 119 ? 151.607 147.205 167.504 1.00 41.45 ?  119 GLU B C     1 
ATOM   6548  O  O     . GLU B 1 119 ? 151.176 148.354 167.373 1.00 43.98 ?  119 GLU B O     1 
ATOM   6549  C  CB    . GLU B 1 119 ? 152.211 146.414 169.806 1.00 39.22 ?  119 GLU B CB    1 
ATOM   6550  C  CG    . GLU B 1 119 ? 151.689 145.973 171.161 1.00 36.97 ?  119 GLU B CG    1 
ATOM   6551  C  CD    . GLU B 1 119 ? 151.761 144.474 171.354 1.00 43.98 ?  119 GLU B CD    1 
ATOM   6552  O  OE1   . GLU B 1 119 ? 151.693 143.740 170.345 1.00 44.85 ?  119 GLU B OE1   1 
ATOM   6553  O  OE2   . GLU B 1 119 ? 151.882 144.028 172.514 1.00 48.91 -1 119 GLU B OE2   1 
ATOM   6554  N  N     . ASP B 1 120 ? 152.466 146.668 166.636 1.00 44.13 ?  120 ASP B N     1 
ATOM   6555  C  CA    . ASP B 1 120 ? 152.924 147.439 165.484 1.00 39.61 ?  120 ASP B CA    1 
ATOM   6556  C  C     . ASP B 1 120 ? 151.769 147.763 164.543 1.00 40.19 ?  120 ASP B C     1 
ATOM   6557  O  O     . ASP B 1 120 ? 151.626 148.902 164.084 1.00 43.73 ?  120 ASP B O     1 
ATOM   6558  C  CB    . ASP B 1 120 ? 154.027 146.678 164.748 1.00 42.08 ?  120 ASP B CB    1 
ATOM   6559  C  CG    . ASP B 1 120 ? 155.242 146.427 165.617 1.00 48.21 ?  120 ASP B CG    1 
ATOM   6560  O  OD1   . ASP B 1 120 ? 155.803 147.406 166.153 1.00 48.42 ?  120 ASP B OD1   1 
ATOM   6561  O  OD2   . ASP B 1 120 ? 155.642 145.253 165.760 1.00 48.19 -1 120 ASP B OD2   1 
ATOM   6562  N  N     . ARG B 1 121 ? 150.933 146.767 164.242 1.00 38.70 ?  121 ARG B N     1 
ATOM   6563  C  CA    . ARG B 1 121 ? 149.783 147.009 163.378 1.00 34.15 ?  121 ARG B CA    1 
ATOM   6564  C  C     . ARG B 1 121 ? 148.820 148.002 164.014 1.00 37.85 ?  121 ARG B C     1 
ATOM   6565  O  O     . ARG B 1 121 ? 148.306 148.902 163.337 1.00 38.98 ?  121 ARG B O     1 
ATOM   6566  C  CB    . ARG B 1 121 ? 149.073 145.692 163.067 1.00 35.06 ?  121 ARG B CB    1 
ATOM   6567  C  CG    . ARG B 1 121 ? 147.896 145.820 162.111 1.00 33.76 ?  121 ARG B CG    1 
ATOM   6568  C  CD    . ARG B 1 121 ? 148.317 145.589 160.669 1.00 34.49 ?  121 ARG B CD    1 
ATOM   6569  N  NE    . ARG B 1 121 ? 149.168 146.662 160.166 1.00 38.32 ?  121 ARG B NE    1 
ATOM   6570  C  CZ    . ARG B 1 121 ? 148.783 147.577 159.287 1.00 36.58 ?  121 ARG B CZ    1 
ATOM   6571  N  NH1   . ARG B 1 121 ? 147.563 147.577 158.779 1.00 36.22 1  121 ARG B NH1   1 
ATOM   6572  N  NH2   . ARG B 1 121 ? 149.645 148.515 158.909 1.00 38.63 ?  121 ARG B NH2   1 
ATOM   6573  N  N     . ILE B 1 122 ? 148.563 147.859 165.317 1.00 34.10 ?  122 ILE B N     1 
ATOM   6574  C  CA    . ILE B 1 122 ? 147.667 148.785 166.002 1.00 28.86 ?  122 ILE B CA    1 
ATOM   6575  C  C     . ILE B 1 122 ? 148.218 150.203 165.940 1.00 32.66 ?  122 ILE B C     1 
ATOM   6576  O  O     . ILE B 1 122 ? 147.480 151.159 165.675 1.00 36.59 ?  122 ILE B O     1 
ATOM   6577  C  CB    . ILE B 1 122 ? 147.437 148.333 167.456 1.00 34.88 ?  122 ILE B CB    1 
ATOM   6578  C  CG1   . ILE B 1 122 ? 146.653 147.020 167.496 1.00 32.72 ?  122 ILE B CG1   1 
ATOM   6579  C  CG2   . ILE B 1 122 ? 146.702 149.410 168.240 1.00 32.93 ?  122 ILE B CG2   1 
ATOM   6580  C  CD1   . ILE B 1 122 ? 145.490 146.979 166.542 1.00 32.81 ?  122 ILE B CD1   1 
ATOM   6581  N  N     . SER B 1 123 ? 149.518 150.366 166.191 1.00 36.22 ?  123 SER B N     1 
ATOM   6582  C  CA    . SER B 1 123 ? 150.121 151.694 166.167 1.00 31.64 ?  123 SER B CA    1 
ATOM   6583  C  C     . SER B 1 123 ? 150.071 152.300 164.772 1.00 33.17 ?  123 SER B C     1 
ATOM   6584  O  O     . SER B 1 123 ? 149.795 153.494 164.618 1.00 35.89 ?  123 SER B O     1 
ATOM   6585  C  CB    . SER B 1 123 ? 151.565 151.624 166.668 1.00 35.47 ?  123 SER B CB    1 
ATOM   6586  O  OG    . SER B 1 123 ? 151.625 151.107 167.983 1.00 40.71 ?  123 SER B OG    1 
ATOM   6587  N  N     . ILE B 1 124 ? 150.344 151.497 163.742 1.00 33.64 ?  124 ILE B N     1 
ATOM   6588  C  CA    . ILE B 1 124 ? 150.293 152.014 162.378 1.00 33.53 ?  124 ILE B CA    1 
ATOM   6589  C  C     . ILE B 1 124 ? 148.875 152.444 162.026 1.00 34.79 ?  124 ILE B C     1 
ATOM   6590  O  O     . ILE B 1 124 ? 148.662 153.502 161.422 1.00 34.99 ?  124 ILE B O     1 
ATOM   6591  C  CB    . ILE B 1 124 ? 150.834 150.971 161.386 1.00 39.81 ?  124 ILE B CB    1 
ATOM   6592  C  CG1   . ILE B 1 124 ? 152.346 150.817 161.554 1.00 40.04 ?  124 ILE B CG1   1 
ATOM   6593  C  CG2   . ILE B 1 124 ? 150.493 151.365 159.958 1.00 37.06 ?  124 ILE B CG2   1 
ATOM   6594  C  CD1   . ILE B 1 124 ? 153.125 152.070 161.224 1.00 37.38 ?  124 ILE B CD1   1 
ATOM   6595  N  N     . VAL B 1 125 ? 147.883 151.634 162.403 1.00 34.47 ?  125 VAL B N     1 
ATOM   6596  C  CA    . VAL B 1 125 ? 146.493 151.985 162.123 1.00 29.71 ?  125 VAL B CA    1 
ATOM   6597  C  C     . VAL B 1 125 ? 146.101 153.256 162.867 1.00 25.63 ?  125 VAL B C     1 
ATOM   6598  O  O     . VAL B 1 125 ? 145.402 154.119 162.324 1.00 31.47 ?  125 VAL B O     1 
ATOM   6599  C  CB    . VAL B 1 125 ? 145.565 150.809 162.476 1.00 34.08 ?  125 VAL B CB    1 
ATOM   6600  C  CG1   . VAL B 1 125 ? 144.111 151.225 162.352 1.00 30.22 ?  125 VAL B CG1   1 
ATOM   6601  C  CG2   . VAL B 1 125 ? 145.860 149.617 161.580 1.00 28.40 ?  125 VAL B CG2   1 
ATOM   6602  N  N     . ALA B 1 126 ? 146.534 153.389 164.122 1.00 24.38 ?  126 ALA B N     1 
ATOM   6603  C  CA    . ALA B 1 126 ? 146.204 154.578 164.900 1.00 28.06 ?  126 ALA B CA    1 
ATOM   6604  C  C     . ALA B 1 126 ? 146.855 155.824 164.315 1.00 31.07 ?  126 ALA B C     1 
ATOM   6605  O  O     . ALA B 1 126 ? 146.237 156.893 164.276 1.00 33.55 ?  126 ALA B O     1 
ATOM   6606  C  CB    . ALA B 1 126 ? 146.624 154.388 166.357 1.00 30.21 ?  126 ALA B CB    1 
ATOM   6607  N  N     . LEU B 1 127 ? 148.105 155.710 163.863 1.00 34.66 ?  127 LEU B N     1 
ATOM   6608  C  CA    . LEU B 1 127 ? 148.774 156.851 163.248 1.00 29.43 ?  127 LEU B CA    1 
ATOM   6609  C  C     . LEU B 1 127 ? 148.120 157.220 161.924 1.00 29.40 ?  127 LEU B C     1 
ATOM   6610  O  O     . LEU B 1 127 ? 148.022 158.404 161.581 1.00 34.33 ?  127 LEU B O     1 
ATOM   6611  C  CB    . LEU B 1 127 ? 150.259 156.546 163.052 1.00 32.39 ?  127 LEU B CB    1 
ATOM   6612  C  CG    . LEU B 1 127 ? 151.124 156.517 164.314 1.00 32.68 ?  127 LEU B CG    1 
ATOM   6613  C  CD1   . LEU B 1 127 ? 152.456 155.845 164.036 1.00 37.16 ?  127 LEU B CD1   1 
ATOM   6614  C  CD2   . LEU B 1 127 ? 151.336 157.918 164.857 1.00 32.27 ?  127 LEU B CD2   1 
ATOM   6615  N  N     . PHE B 1 128 ? 147.671 156.220 161.164 1.00 32.02 ?  128 PHE B N     1 
ATOM   6616  C  CA    . PHE B 1 128 ? 146.937 156.494 159.935 1.00 33.45 ?  128 PHE B CA    1 
ATOM   6617  C  C     . PHE B 1 128 ? 145.619 157.201 160.230 1.00 30.39 ?  128 PHE B C     1 
ATOM   6618  O  O     . PHE B 1 128 ? 145.237 158.141 159.525 1.00 38.92 ?  128 PHE B O     1 
ATOM   6619  C  CB    . PHE B 1 128 ? 146.698 155.186 159.177 1.00 30.62 ?  128 PHE B CB    1 
ATOM   6620  C  CG    . PHE B 1 128 ? 145.703 155.301 158.063 1.00 33.33 ?  128 PHE B CG    1 
ATOM   6621  C  CD1   . PHE B 1 128 ? 146.073 155.826 156.838 1.00 36.79 ?  128 PHE B CD1   1 
ATOM   6622  C  CD2   . PHE B 1 128 ? 144.397 154.878 158.238 1.00 34.22 ?  128 PHE B CD2   1 
ATOM   6623  C  CE1   . PHE B 1 128 ? 145.159 155.930 155.809 1.00 36.17 ?  128 PHE B CE1   1 
ATOM   6624  C  CE2   . PHE B 1 128 ? 143.478 154.980 157.214 1.00 33.83 ?  128 PHE B CE2   1 
ATOM   6625  C  CZ    . PHE B 1 128 ? 143.860 155.508 155.998 1.00 34.21 ?  128 PHE B CZ    1 
ATOM   6626  N  N     . PHE B 1 129 ? 144.911 156.759 161.272 1.00 29.93 ?  129 PHE B N     1 
ATOM   6627  C  CA    . PHE B 1 129 ? 143.644 157.385 161.635 1.00 27.26 ?  129 PHE B CA    1 
ATOM   6628  C  C     . PHE B 1 129 ? 143.844 158.821 162.104 1.00 27.36 ?  129 PHE B C     1 
ATOM   6629  O  O     . PHE B 1 129 ? 143.093 159.720 161.709 1.00 34.41 ?  129 PHE B O     1 
ATOM   6630  C  CB    . PHE B 1 129 ? 142.952 156.569 162.727 1.00 25.10 ?  129 PHE B CB    1 
ATOM   6631  C  CG    . PHE B 1 129 ? 142.312 155.307 162.233 1.00 24.05 ?  129 PHE B CG    1 
ATOM   6632  C  CD1   . PHE B 1 129 ? 141.964 155.163 160.902 1.00 27.86 ?  129 PHE B CD1   1 
ATOM   6633  C  CD2   . PHE B 1 129 ? 142.050 154.265 163.105 1.00 25.80 ?  129 PHE B CD2   1 
ATOM   6634  C  CE1   . PHE B 1 129 ? 141.372 154.002 160.449 1.00 27.45 ?  129 PHE B CE1   1 
ATOM   6635  C  CE2   . PHE B 1 129 ? 141.458 153.101 162.657 1.00 25.75 ?  129 PHE B CE2   1 
ATOM   6636  C  CZ    . PHE B 1 129 ? 141.119 152.970 161.327 1.00 28.81 ?  129 PHE B CZ    1 
ATOM   6637  N  N     . ALA B 1 130 ? 144.852 159.054 162.948 1.00 32.00 ?  130 ALA B N     1 
ATOM   6638  C  CA    . ALA B 1 130 ? 145.007 160.361 163.576 1.00 33.63 ?  130 ALA B CA    1 
ATOM   6639  C  C     . ALA B 1 130 ? 145.331 161.448 162.561 1.00 40.38 ?  130 ALA B C     1 
ATOM   6640  O  O     . ALA B 1 130 ? 145.072 162.628 162.821 1.00 45.65 ?  130 ALA B O     1 
ATOM   6641  C  CB    . ALA B 1 130 ? 146.089 160.298 164.652 1.00 35.72 ?  130 ALA B CB    1 
ATOM   6642  N  N     . ASN B 1 131 ? 145.891 161.079 161.410 1.00 42.21 ?  131 ASN B N     1 
ATOM   6643  C  CA    . ASN B 1 131 ? 146.168 162.034 160.339 1.00 42.29 ?  131 ASN B CA    1 
ATOM   6644  C  C     . ASN B 1 131 ? 147.025 163.197 160.837 1.00 39.98 ?  131 ASN B C     1 
ATOM   6645  O  O     . ASN B 1 131 ? 146.787 164.358 160.499 1.00 43.09 ?  131 ASN B O     1 
ATOM   6646  C  CB    . ASN B 1 131 ? 144.868 162.543 159.715 1.00 40.56 ?  131 ASN B CB    1 
ATOM   6647  C  CG    . ASN B 1 131 ? 145.088 163.225 158.382 1.00 43.24 ?  131 ASN B CG    1 
ATOM   6648  O  OD1   . ASN B 1 131 ? 145.836 162.735 157.537 1.00 45.35 ?  131 ASN B OD1   1 
ATOM   6649  N  ND2   . ASN B 1 131 ? 144.431 164.360 158.184 1.00 40.55 ?  131 ASN B ND2   1 
ATOM   6650  N  N     . GLY B 1 132 ? 148.032 162.884 161.650 1.00 43.78 ?  132 GLY B N     1 
ATOM   6651  C  CA    . GLY B 1 132 ? 148.946 163.882 162.160 1.00 43.02 ?  132 GLY B CA    1 
ATOM   6652  C  C     . GLY B 1 132 ? 148.692 164.340 163.579 1.00 45.94 ?  132 GLY B C     1 
ATOM   6653  O  O     . GLY B 1 132 ? 149.411 165.226 164.060 1.00 49.85 ?  132 GLY B O     1 
ATOM   6654  N  N     . ASP B 1 133 ? 147.705 163.773 164.265 1.00 46.67 ?  133 ASP B N     1 
ATOM   6655  C  CA    . ASP B 1 133 ? 147.396 164.133 165.643 1.00 43.16 ?  133 ASP B CA    1 
ATOM   6656  C  C     . ASP B 1 133 ? 147.955 163.062 166.572 1.00 47.28 ?  133 ASP B C     1 
ATOM   6657  O  O     . ASP B 1 133 ? 147.508 161.911 166.538 1.00 49.37 ?  133 ASP B O     1 
ATOM   6658  C  CB    . ASP B 1 133 ? 145.889 164.287 165.841 1.00 46.65 ?  133 ASP B CB    1 
ATOM   6659  C  CG    . ASP B 1 133 ? 145.540 165.010 167.125 1.00 50.59 ?  133 ASP B CG    1 
ATOM   6660  O  OD1   . ASP B 1 133 ? 146.373 165.011 168.056 1.00 48.86 ?  133 ASP B OD1   1 
ATOM   6661  O  OD2   . ASP B 1 133 ? 144.432 165.579 167.204 1.00 49.37 -1 133 ASP B OD2   1 
ATOM   6662  N  N     . THR B 1 134 ? 148.924 163.445 167.405 1.00 47.44 ?  134 THR B N     1 
ATOM   6663  C  CA    . THR B 1 134 ? 149.575 162.470 168.275 1.00 45.03 ?  134 THR B CA    1 
ATOM   6664  C  C     . THR B 1 134 ? 148.655 162.032 169.408 1.00 46.86 ?  134 THR B C     1 
ATOM   6665  O  O     . THR B 1 134 ? 148.589 160.842 169.734 1.00 50.29 ?  134 THR B O     1 
ATOM   6666  C  CB    . THR B 1 134 ? 150.875 163.047 168.830 1.00 48.82 ?  134 THR B CB    1 
ATOM   6667  O  OG1   . THR B 1 134 ? 151.751 163.374 167.744 1.00 52.88 ?  134 THR B OG1   1 
ATOM   6668  C  CG2   . THR B 1 134 ? 151.560 162.038 169.738 1.00 46.52 ?  134 THR B CG2   1 
ATOM   6669  N  N     . GLU B 1 135 ? 147.945 162.976 170.029 1.00 47.80 ?  135 GLU B N     1 
ATOM   6670  C  CA    . GLU B 1 135 ? 147.004 162.607 171.082 1.00 45.55 ?  135 GLU B CA    1 
ATOM   6671  C  C     . GLU B 1 135 ? 145.868 161.759 170.526 1.00 48.24 ?  135 GLU B C     1 
ATOM   6672  O  O     . GLU B 1 135 ? 145.443 160.781 171.154 1.00 51.24 ?  135 GLU B O     1 
ATOM   6673  C  CB    . GLU B 1 135 ? 146.461 163.862 171.763 1.00 48.34 ?  135 GLU B CB    1 
ATOM   6674  C  CG    . GLU B 1 135 ? 146.405 163.769 173.278 1.00 51.71 ?  135 GLU B CG    1 
ATOM   6675  C  CD    . GLU B 1 135 ? 147.689 163.225 173.874 1.00 54.19 ?  135 GLU B CD    1 
ATOM   6676  O  OE1   . GLU B 1 135 ? 148.777 163.689 173.472 1.00 51.32 ?  135 GLU B OE1   1 
ATOM   6677  O  OE2   . GLU B 1 135 ? 147.611 162.334 174.746 1.00 53.53 -1 135 GLU B OE2   1 
ATOM   6678  N  N     . LYS B 1 136 ? 145.361 162.120 169.346 1.00 38.66 ?  136 LYS B N     1 
ATOM   6679  C  CA    . LYS B 1 136 ? 144.336 161.306 168.705 1.00 37.35 ?  136 LYS B CA    1 
ATOM   6680  C  C     . LYS B 1 136 ? 144.876 159.926 168.358 1.00 40.63 ?  136 LYS B C     1 
ATOM   6681  O  O     . LYS B 1 136 ? 144.166 158.922 168.482 1.00 43.48 ?  136 LYS B O     1 
ATOM   6682  C  CB    . LYS B 1 136 ? 143.810 162.015 167.457 1.00 42.97 ?  136 LYS B CB    1 
ATOM   6683  C  CG    . LYS B 1 136 ? 142.568 161.383 166.856 1.00 43.16 ?  136 LYS B CG    1 
ATOM   6684  C  CD    . LYS B 1 136 ? 141.317 161.817 167.598 1.00 42.12 ?  136 LYS B CD    1 
ATOM   6685  C  CE    . LYS B 1 136 ? 140.079 161.669 166.728 1.00 43.86 ?  136 LYS B CE    1 
ATOM   6686  N  NZ    . LYS B 1 136 ? 139.966 162.765 165.727 1.00 45.48 1  136 LYS B NZ    1 
ATOM   6687  N  N     . ALA B 1 137 ? 146.133 159.855 167.914 1.00 39.55 ?  137 ALA B N     1 
ATOM   6688  C  CA    . ALA B 1 137 ? 146.743 158.561 167.628 1.00 34.83 ?  137 ALA B CA    1 
ATOM   6689  C  C     . ALA B 1 137 ? 146.843 157.712 168.888 1.00 36.53 ?  137 ALA B C     1 
ATOM   6690  O  O     . ALA B 1 137 ? 146.605 156.501 168.849 1.00 36.69 ?  137 ALA B O     1 
ATOM   6691  C  CB    . ALA B 1 137 ? 148.120 158.754 166.998 1.00 34.83 ?  137 ALA B CB    1 
ATOM   6692  N  N     . LYS B 1 138 ? 147.198 158.329 170.018 1.00 36.28 ?  138 LYS B N     1 
ATOM   6693  C  CA    . LYS B 1 138 ? 147.250 157.592 171.276 1.00 38.15 ?  138 LYS B CA    1 
ATOM   6694  C  C     . LYS B 1 138 ? 145.865 157.110 171.687 1.00 36.95 ?  138 LYS B C     1 
ATOM   6695  O  O     . LYS B 1 138 ? 145.713 155.994 172.197 1.00 36.98 ?  138 LYS B O     1 
ATOM   6696  C  CB    . LYS B 1 138 ? 147.861 158.463 172.373 1.00 42.16 ?  138 LYS B CB    1 
ATOM   6697  C  CG    . LYS B 1 138 ? 149.369 158.598 172.291 1.00 41.21 ?  138 LYS B CG    1 
ATOM   6698  C  CD    . LYS B 1 138 ? 149.885 159.604 173.304 1.00 38.44 ?  138 LYS B CD    1 
ATOM   6699  C  CE    . LYS B 1 138 ? 151.240 160.154 172.896 1.00 42.07 ?  138 LYS B CE    1 
ATOM   6700  N  NZ    . LYS B 1 138 ? 152.040 160.575 174.079 1.00 42.27 1  138 LYS B NZ    1 
ATOM   6701  N  N     . GLU B 1 139 ? 144.843 157.944 171.486 1.00 38.85 ?  139 GLU B N     1 
ATOM   6702  C  CA    . GLU B 1 139 ? 143.480 157.516 171.783 1.00 34.91 ?  139 GLU B CA    1 
ATOM   6703  C  C     . GLU B 1 139 ? 143.077 156.326 170.920 1.00 34.12 ?  139 GLU B C     1 
ATOM   6704  O  O     . GLU B 1 139 ? 142.461 155.372 171.409 1.00 37.10 ?  139 GLU B O     1 
ATOM   6705  C  CB    . GLU B 1 139 ? 142.507 158.678 171.586 1.00 35.50 ?  139 GLU B CB    1 
ATOM   6706  C  CG    . GLU B 1 139 ? 142.456 159.647 172.753 1.00 38.56 ?  139 GLU B CG    1 
ATOM   6707  C  CD    . GLU B 1 139 ? 142.035 161.041 172.334 1.00 46.22 ?  139 GLU B CD    1 
ATOM   6708  O  OE1   . GLU B 1 139 ? 141.325 161.167 171.314 1.00 44.64 ?  139 GLU B OE1   1 
ATOM   6709  O  OE2   . GLU B 1 139 ? 142.413 162.011 173.023 1.00 44.36 -1 139 GLU B OE2   1 
ATOM   6710  N  N     . TYR B 1 140 ? 143.420 156.363 169.631 1.00 30.27 ?  140 TYR B N     1 
ATOM   6711  C  CA    . TYR B 1 140 ? 143.121 155.237 168.751 1.00 28.66 ?  140 TYR B CA    1 
ATOM   6712  C  C     . TYR B 1 140 ? 143.877 153.987 169.181 1.00 27.60 ?  140 TYR B C     1 
ATOM   6713  O  O     . TYR B 1 140 ? 143.341 152.874 169.123 1.00 31.03 ?  140 TYR B O     1 
ATOM   6714  C  CB    . TYR B 1 140 ? 143.460 155.592 167.304 1.00 29.53 ?  140 TYR B CB    1 
ATOM   6715  C  CG    . TYR B 1 140 ? 142.461 156.503 166.634 1.00 30.49 ?  140 TYR B CG    1 
ATOM   6716  C  CD1   . TYR B 1 140 ? 141.119 156.157 166.555 1.00 33.25 ?  140 TYR B CD1   1 
ATOM   6717  C  CD2   . TYR B 1 140 ? 142.862 157.706 166.072 1.00 31.96 ?  140 TYR B CD2   1 
ATOM   6718  C  CE1   . TYR B 1 140 ? 140.205 156.987 165.939 1.00 30.48 ?  140 TYR B CE1   1 
ATOM   6719  C  CE2   . TYR B 1 140 ? 141.956 158.540 165.455 1.00 34.85 ?  140 TYR B CE2   1 
ATOM   6720  C  CZ    . TYR B 1 140 ? 140.629 158.177 165.391 1.00 27.48 ?  140 TYR B CZ    1 
ATOM   6721  O  OH    . TYR B 1 140 ? 139.725 159.010 164.777 1.00 35.22 ?  140 TYR B OH    1 
ATOM   6722  N  N     . VAL B 1 141 ? 145.134 154.151 169.597 1.00 37.61 ?  141 VAL B N     1 
ATOM   6723  C  CA    . VAL B 1 141 ? 145.921 153.015 170.068 1.00 33.06 ?  141 VAL B CA    1 
ATOM   6724  C  C     . VAL B 1 141 ? 145.275 152.400 171.299 1.00 29.85 ?  141 VAL B C     1 
ATOM   6725  O  O     . VAL B 1 141 ? 145.188 151.175 171.425 1.00 37.72 ?  141 VAL B O     1 
ATOM   6726  C  CB    . VAL B 1 141 ? 147.372 153.444 170.349 1.00 33.47 ?  141 VAL B CB    1 
ATOM   6727  C  CG1   . VAL B 1 141 ? 147.987 152.552 171.413 1.00 32.93 ?  141 VAL B CG1   1 
ATOM   6728  C  CG2   . VAL B 1 141 ? 148.195 153.395 169.076 1.00 33.37 ?  141 VAL B CG2   1 
ATOM   6729  N  N     . ASN B 1 142 ? 144.827 153.237 172.235 1.00 32.01 ?  142 ASN B N     1 
ATOM   6730  C  CA    . ASN B 1 142 ? 144.161 152.716 173.423 1.00 29.93 ?  142 ASN B CA    1 
ATOM   6731  C  C     . ASN B 1 142 ? 142.861 152.013 173.057 1.00 34.45 ?  142 ASN B C     1 
ATOM   6732  O  O     . ASN B 1 142 ? 142.526 150.970 173.631 1.00 37.53 ?  142 ASN B O     1 
ATOM   6733  C  CB    . ASN B 1 142 ? 143.901 153.845 174.418 1.00 28.26 ?  142 ASN B CB    1 
ATOM   6734  C  CG    . ASN B 1 142 ? 145.150 154.260 175.164 1.00 35.14 ?  142 ASN B CG    1 
ATOM   6735  O  OD1   . ASN B 1 142 ? 145.885 153.421 175.683 1.00 34.81 ?  142 ASN B OD1   1 
ATOM   6736  N  ND2   . ASN B 1 142 ? 145.400 155.562 175.221 1.00 38.07 ?  142 ASN B ND2   1 
ATOM   6737  N  N     . LEU B 1 143 ? 142.113 152.570 172.104 1.00 31.90 ?  143 LEU B N     1 
ATOM   6738  C  CA    . LEU B 1 143 ? 140.858 151.952 171.690 1.00 25.18 ?  143 LEU B CA    1 
ATOM   6739  C  C     . LEU B 1 143 ? 141.097 150.574 171.081 1.00 28.65 ?  143 LEU B C     1 
ATOM   6740  O  O     . LEU B 1 143 ? 140.412 149.603 171.423 1.00 32.22 ?  143 LEU B O     1 
ATOM   6741  C  CB    . LEU B 1 143 ? 140.135 152.864 170.698 1.00 26.45 ?  143 LEU B CB    1 
ATOM   6742  C  CG    . LEU B 1 143 ? 138.630 152.658 170.524 1.00 31.32 ?  143 LEU B CG    1 
ATOM   6743  C  CD1   . LEU B 1 143 ? 137.877 153.215 171.721 1.00 29.40 ?  143 LEU B CD1   1 
ATOM   6744  C  CD2   . LEU B 1 143 ? 138.146 153.302 169.236 1.00 30.09 ?  143 LEU B CD2   1 
ATOM   6745  N  N     . MET B 1 144 ? 142.070 150.470 170.172 1.00 33.31 ?  144 MET B N     1 
ATOM   6746  C  CA    . MET B 1 144 ? 142.302 149.207 169.477 1.00 29.92 ?  144 MET B CA    1 
ATOM   6747  C  C     . MET B 1 144 ? 142.993 148.177 170.367 1.00 25.46 ?  144 MET B C     1 
ATOM   6748  O  O     . MET B 1 144 ? 142.642 146.994 170.333 1.00 29.05 ?  144 MET B O     1 
ATOM   6749  C  CB    . MET B 1 144 ? 143.116 149.447 168.207 1.00 28.91 ?  144 MET B CB    1 
ATOM   6750  C  CG    . MET B 1 144 ? 142.368 150.215 167.131 1.00 27.41 ?  144 MET B CG    1 
ATOM   6751  S  SD    . MET B 1 144 ? 143.306 150.363 165.601 1.00 40.83 ?  144 MET B SD    1 
ATOM   6752  C  CE    . MET B 1 144 ? 143.442 152.142 165.463 1.00 29.96 ?  144 MET B CE    1 
ATOM   6753  N  N     . ILE B 1 145 ? 143.978 148.601 171.160 1.00 30.59 ?  145 ILE B N     1 
ATOM   6754  C  CA    . ILE B 1 145 ? 144.695 147.666 172.022 1.00 30.85 ?  145 ILE B CA    1 
ATOM   6755  C  C     . ILE B 1 145 ? 143.779 147.152 173.125 1.00 34.05 ?  145 ILE B C     1 
ATOM   6756  O  O     . ILE B 1 145 ? 143.853 145.981 173.515 1.00 40.32 ?  145 ILE B O     1 
ATOM   6757  C  CB    . ILE B 1 145 ? 145.967 148.324 172.588 1.00 33.09 ?  145 ILE B CB    1 
ATOM   6758  C  CG1   . ILE B 1 145 ? 147.046 147.268 172.837 1.00 34.34 ?  145 ILE B CG1   1 
ATOM   6759  C  CG2   . ILE B 1 145 ? 145.662 149.088 173.866 1.00 34.93 ?  145 ILE B CG2   1 
ATOM   6760  C  CD1   . ILE B 1 145 ? 147.541 146.589 171.580 1.00 32.49 ?  145 ILE B CD1   1 
ATOM   6761  N  N     . ASN B 1 146 ? 142.903 148.013 173.645 1.00 33.03 ?  146 ASN B N     1 
ATOM   6762  C  CA    . ASN B 1 146 ? 141.845 147.547 174.530 1.00 27.98 ?  146 ASN B CA    1 
ATOM   6763  C  C     . ASN B 1 146 ? 140.816 146.707 173.791 1.00 30.90 ?  146 ASN B C     1 
ATOM   6764  O  O     . ASN B 1 146 ? 139.964 146.088 174.435 1.00 34.77 ?  146 ASN B O     1 
ATOM   6765  C  CB    . ASN B 1 146 ? 141.159 148.734 175.208 1.00 28.88 ?  146 ASN B CB    1 
ATOM   6766  C  CG    . ASN B 1 146 ? 142.045 149.412 176.231 1.00 33.31 ?  146 ASN B CG    1 
ATOM   6767  O  OD1   . ASN B 1 146 ? 143.031 148.840 176.691 1.00 38.75 ?  146 ASN B OD1   1 
ATOM   6768  N  ND2   . ASN B 1 146 ? 141.695 150.640 176.596 1.00 35.88 ?  146 ASN B ND2   1 
ATOM   6769  N  N     . GLN B 1 147 ? 140.878 146.680 172.461 1.00 32.52 ?  147 GLN B N     1 
ATOM   6770  C  CA    . GLN B 1 147 ? 139.986 145.872 171.635 1.00 23.87 ?  147 GLN B CA    1 
ATOM   6771  C  C     . GLN B 1 147 ? 138.531 146.284 171.808 1.00 25.34 ?  147 GLN B C     1 
ATOM   6772  O  O     . GLN B 1 147 ? 137.620 145.469 171.652 1.00 32.91 ?  147 GLN B O     1 
ATOM   6773  C  CB    . GLN B 1 147 ? 140.167 144.382 171.926 1.00 29.39 ?  147 GLN B CB    1 
ATOM   6774  C  CG    . GLN B 1 147 ? 141.524 143.848 171.504 1.00 25.93 ?  147 GLN B CG    1 
ATOM   6775  C  CD    . GLN B 1 147 ? 141.551 142.341 171.403 1.00 27.96 ?  147 GLN B CD    1 
ATOM   6776  O  OE1   . GLN B 1 147 ? 140.933 141.643 172.205 1.00 38.08 ?  147 GLN B OE1   1 
ATOM   6777  N  NE2   . GLN B 1 147 ? 142.268 141.827 170.413 1.00 29.55 ?  147 GLN B NE2   1 
ATOM   6778  N  N     . GLU B 1 148 ? 138.304 147.557 172.136 1.00 27.46 ?  148 GLU B N     1 
ATOM   6779  C  CA    . GLU B 1 148 ? 136.950 148.093 172.160 1.00 21.60 ?  148 GLU B CA    1 
ATOM   6780  C  C     . GLU B 1 148 ? 136.423 148.349 170.756 1.00 24.47 ?  148 GLU B C     1 
ATOM   6781  O  O     . GLU B 1 148 ? 135.207 148.323 170.540 1.00 30.89 ?  148 GLU B O     1 
ATOM   6782  C  CB    . GLU B 1 148 ? 136.916 149.383 172.977 1.00 19.64 ?  148 GLU B CB    1 
ATOM   6783  C  CG    . GLU B 1 148 ? 137.405 149.220 174.402 1.00 24.15 ?  148 GLU B CG    1 
ATOM   6784  C  CD    . GLU B 1 148 ? 137.781 150.540 175.041 1.00 33.55 ?  148 GLU B CD    1 
ATOM   6785  O  OE1   . GLU B 1 148 ? 138.874 151.059 174.734 1.00 36.20 ?  148 GLU B OE1   1 
ATOM   6786  O  OE2   . GLU B 1 148 ? 136.987 151.059 175.852 1.00 38.62 -1 148 GLU B OE2   1 
ATOM   6787  N  N     . TYR B 1 149 ? 137.313 148.604 169.801 1.00 21.13 ?  149 TYR B N     1 
ATOM   6788  C  CA    . TYR B 1 149 ? 136.934 148.869 168.422 1.00 19.58 ?  149 TYR B CA    1 
ATOM   6789  C  C     . TYR B 1 149 ? 137.853 148.094 167.493 1.00 23.84 ?  149 TYR B C     1 
ATOM   6790  O  O     . TYR B 1 149 ? 139.072 148.081 167.691 1.00 28.18 ?  149 TYR B O     1 
ATOM   6791  C  CB    . TYR B 1 149 ? 137.001 150.366 168.104 1.00 22.74 ?  149 TYR B CB    1 
ATOM   6792  C  CG    . TYR B 1 149 ? 136.784 150.685 166.646 1.00 24.58 ?  149 TYR B CG    1 
ATOM   6793  C  CD1   . TYR B 1 149 ? 135.562 150.435 166.037 1.00 16.12 ?  149 TYR B CD1   1 
ATOM   6794  C  CD2   . TYR B 1 149 ? 137.799 151.234 165.876 1.00 20.86 ?  149 TYR B CD2   1 
ATOM   6795  C  CE1   . TYR B 1 149 ? 135.359 150.722 164.705 1.00 20.54 ?  149 TYR B CE1   1 
ATOM   6796  C  CE2   . TYR B 1 149 ? 137.604 151.526 164.543 1.00 21.12 ?  149 TYR B CE2   1 
ATOM   6797  C  CZ    . TYR B 1 149 ? 136.382 151.268 163.963 1.00 18.27 ?  149 TYR B CZ    1 
ATOM   6798  O  OH    . TYR B 1 149 ? 136.181 151.557 162.634 1.00 19.79 ?  149 TYR B OH    1 
ATOM   6799  N  N     . GLN B 1 150 ? 137.270 147.453 166.489 1.00 17.03 ?  150 GLN B N     1 
ATOM   6800  C  CA    . GLN B 1 150 ? 138.028 146.717 165.479 1.00 14.05 ?  150 GLN B CA    1 
ATOM   6801  C  C     . GLN B 1 150 ? 137.725 147.289 164.104 1.00 17.76 ?  150 GLN B C     1 
ATOM   6802  O  O     . GLN B 1 150 ? 136.597 147.120 163.602 1.00 25.64 ?  150 GLN B O     1 
ATOM   6803  C  CB    . GLN B 1 150 ? 137.689 145.228 165.524 1.00 17.05 ?  150 GLN B CB    1 
ATOM   6804  C  CG    . GLN B 1 150 ? 138.363 144.391 164.448 1.00 24.08 ?  150 GLN B CG    1 
ATOM   6805  C  CD    . GLN B 1 150 ? 139.866 144.578 164.412 1.00 22.70 ?  150 GLN B CD    1 
ATOM   6806  O  OE1   . GLN B 1 150 ? 140.577 144.137 165.312 1.00 27.40 ?  150 GLN B OE1   1 
ATOM   6807  N  NE2   . GLN B 1 150 ? 140.355 145.234 163.369 1.00 20.09 ?  150 GLN B NE2   1 
ATOM   6808  N  N     . PRO B 1 151 ? 138.670 147.968 163.456 1.00 23.46 ?  151 PRO B N     1 
ATOM   6809  C  CA    . PRO B 1 151 ? 138.445 148.387 162.069 1.00 16.90 ?  151 PRO B CA    1 
ATOM   6810  C  C     . PRO B 1 151 ? 138.240 147.178 161.172 1.00 19.23 ?  151 PRO B C     1 
ATOM   6811  O  O     . PRO B 1 151 ? 138.786 146.098 161.409 1.00 23.18 ?  151 PRO B O     1 
ATOM   6812  C  CB    . PRO B 1 151 ? 139.729 149.144 161.711 1.00 16.91 ?  151 PRO B CB    1 
ATOM   6813  C  CG    . PRO B 1 151 ? 140.329 149.531 163.017 1.00 17.70 ?  151 PRO B CG    1 
ATOM   6814  C  CD    . PRO B 1 151 ? 139.954 148.453 163.984 1.00 22.38 ?  151 PRO B CD    1 
ATOM   6815  N  N     . SER B 1 152 ? 137.430 147.366 160.131 1.00 26.94 ?  152 SER B N     1 
ATOM   6816  C  CA    . SER B 1 152 ? 137.123 146.283 159.205 1.00 20.38 ?  152 SER B CA    1 
ATOM   6817  C  C     . SER B 1 152 ? 138.402 145.653 158.670 1.00 24.29 ?  152 SER B C     1 
ATOM   6818  O  O     . SER B 1 152 ? 139.468 146.274 158.708 1.00 26.67 ?  152 SER B O     1 
ATOM   6819  C  CB    . SER B 1 152 ? 136.257 146.791 158.051 1.00 24.05 ?  152 SER B CB    1 
ATOM   6820  O  OG    . SER B 1 152 ? 137.022 147.569 157.147 1.00 28.88 ?  152 SER B OG    1 
ATOM   6821  N  N     . THR B 1 153 ? 138.306 144.422 158.176 1.00 30.33 ?  153 THR B N     1 
ATOM   6822  C  CA    . THR B 1 153 ? 139.484 143.738 157.653 1.00 24.21 ?  153 THR B CA    1 
ATOM   6823  C  C     . THR B 1 153 ? 140.236 144.554 156.612 1.00 31.06 ?  153 THR B C     1 
ATOM   6824  O  O     . THR B 1 153 ? 141.475 144.604 156.688 1.00 30.87 ?  153 THR B O     1 
ATOM   6825  C  CB    . THR B 1 153 ? 139.077 142.377 157.072 1.00 25.95 ?  153 THR B CB    1 
ATOM   6826  O  OG1   . THR B 1 153 ? 138.803 141.461 158.139 1.00 34.00 ?  153 THR B OG1   1 
ATOM   6827  C  CG2   . THR B 1 153 ? 140.191 141.812 156.204 1.00 29.49 ?  153 THR B CG2   1 
ATOM   6828  N  N     . PRO B 1 154 ? 139.588 145.195 155.635 1.00 27.98 ?  154 PRO B N     1 
ATOM   6829  C  CA    . PRO B 1 154 ? 140.354 146.022 154.686 1.00 24.02 ?  154 PRO B CA    1 
ATOM   6830  C  C     . PRO B 1 154 ? 141.141 147.135 155.356 1.00 25.34 ?  154 PRO B C     1 
ATOM   6831  O  O     . PRO B 1 154 ? 142.339 147.287 155.093 1.00 33.81 ?  154 PRO B O     1 
ATOM   6832  C  CB    . PRO B 1 154 ? 139.265 146.566 153.751 1.00 23.98 ?  154 PRO B CB    1 
ATOM   6833  C  CG    . PRO B 1 154 ? 138.162 145.578 153.847 1.00 24.86 ?  154 PRO B CG    1 
ATOM   6834  C  CD    . PRO B 1 154 ? 138.167 145.100 155.261 1.00 25.61 ?  154 PRO B CD    1 
ATOM   6835  N  N     . THR B 1 155 ? 140.499 147.922 156.220 1.00 28.84 ?  155 THR B N     1 
ATOM   6836  C  CA    . THR B 1 155 ? 141.202 149.010 156.894 1.00 26.26 ?  155 THR B CA    1 
ATOM   6837  C  C     . THR B 1 155 ? 142.307 148.475 157.795 1.00 26.47 ?  155 THR B C     1 
ATOM   6838  O  O     . THR B 1 155 ? 143.438 148.974 157.776 1.00 27.03 ?  155 THR B O     1 
ATOM   6839  C  CB    . THR B 1 155 ? 140.216 149.854 157.701 1.00 25.89 ?  155 THR B CB    1 
ATOM   6840  O  OG1   . THR B 1 155 ? 139.155 150.301 156.848 1.00 32.29 ?  155 THR B OG1   1 
ATOM   6841  C  CG2   . THR B 1 155 ? 140.918 151.057 158.311 1.00 23.96 ?  155 THR B CG2   1 
ATOM   6842  N  N     . PHE B 1 156 ? 141.997 147.452 158.594 1.00 28.77 ?  156 PHE B N     1 
ATOM   6843  C  CA    . PHE B 1 156 ? 142.981 146.918 159.529 1.00 29.52 ?  156 PHE B CA    1 
ATOM   6844  C  C     . PHE B 1 156 ? 144.196 146.364 158.797 1.00 31.57 ?  156 PHE B C     1 
ATOM   6845  O  O     . PHE B 1 156 ? 145.338 146.571 159.224 1.00 34.87 ?  156 PHE B O     1 
ATOM   6846  C  CB    . PHE B 1 156 ? 142.338 145.838 160.398 1.00 27.59 ?  156 PHE B CB    1 
ATOM   6847  C  CG    . PHE B 1 156 ? 143.142 145.476 161.612 1.00 32.83 ?  156 PHE B CG    1 
ATOM   6848  C  CD1   . PHE B 1 156 ? 143.454 146.432 162.562 1.00 27.40 ?  156 PHE B CD1   1 
ATOM   6849  C  CD2   . PHE B 1 156 ? 143.581 144.178 161.805 1.00 29.13 ?  156 PHE B CD2   1 
ATOM   6850  C  CE1   . PHE B 1 156 ? 144.193 146.101 163.679 1.00 27.88 ?  156 PHE B CE1   1 
ATOM   6851  C  CE2   . PHE B 1 156 ? 144.320 143.840 162.921 1.00 21.66 ?  156 PHE B CE2   1 
ATOM   6852  C  CZ    . PHE B 1 156 ? 144.626 144.803 163.859 1.00 31.62 ?  156 PHE B CZ    1 
ATOM   6853  N  N     . LEU B 1 157 ? 143.971 145.652 157.693 1.00 33.91 ?  157 LEU B N     1 
ATOM   6854  C  CA    . LEU B 1 157 ? 145.060 145.020 156.959 1.00 30.18 ?  157 LEU B CA    1 
ATOM   6855  C  C     . LEU B 1 157 ? 145.860 146.022 156.133 1.00 33.13 ?  157 LEU B C     1 
ATOM   6856  O  O     . LEU B 1 157 ? 147.091 145.931 156.073 1.00 41.80 ?  157 LEU B O     1 
ATOM   6857  C  CB    . LEU B 1 157 ? 144.501 143.920 156.057 1.00 34.45 ?  157 LEU B CB    1 
ATOM   6858  C  CG    . LEU B 1 157 ? 145.491 143.207 155.137 1.00 37.23 ?  157 LEU B CG    1 
ATOM   6859  C  CD1   . LEU B 1 157 ? 146.351 142.233 155.925 1.00 35.67 ?  157 LEU B CD1   1 
ATOM   6860  C  CD2   . LEU B 1 157 ? 144.758 142.498 154.010 1.00 35.10 ?  157 LEU B CD2   1 
ATOM   6861  N  N     . ASN B 1 158 ? 145.191 146.982 155.497 1.00 34.24 ?  158 ASN B N     1 
ATOM   6862  C  CA    . ASN B 1 158 ? 145.823 147.800 154.471 1.00 33.42 ?  158 ASN B CA    1 
ATOM   6863  C  C     . ASN B 1 158 ? 146.247 149.182 154.947 1.00 34.46 ?  158 ASN B C     1 
ATOM   6864  O  O     . ASN B 1 158 ? 147.052 149.826 154.267 1.00 35.86 ?  158 ASN B O     1 
ATOM   6865  C  CB    . ASN B 1 158 ? 144.879 147.962 153.274 1.00 34.46 ?  158 ASN B CB    1 
ATOM   6866  C  CG    . ASN B 1 158 ? 144.573 146.646 152.593 1.00 37.64 ?  158 ASN B CG    1 
ATOM   6867  O  OD1   . ASN B 1 158 ? 145.413 145.749 152.545 1.00 42.29 ?  158 ASN B OD1   1 
ATOM   6868  N  ND2   . ASN B 1 158 ? 143.363 146.522 152.064 1.00 38.70 ?  158 ASN B ND2   1 
ATOM   6869  N  N     . ALA B 1 159 ? 145.735 149.657 156.079 1.00 36.17 ?  159 ALA B N     1 
ATOM   6870  C  CA    . ALA B 1 159 ? 146.053 151.010 156.516 1.00 35.39 ?  159 ALA B CA    1 
ATOM   6871  C  C     . ALA B 1 159 ? 147.557 151.180 156.681 1.00 40.98 ?  159 ALA B C     1 
ATOM   6872  O  O     . ALA B 1 159 ? 148.219 150.374 157.339 1.00 45.47 ?  159 ALA B O     1 
ATOM   6873  C  CB    . ALA B 1 159 ? 145.337 151.325 157.829 1.00 33.17 ?  159 ALA B CB    1 
ATOM   6874  N  N     . GLY B 1 160 ? 148.094 152.238 156.078 1.00 46.22 ?  160 GLY B N     1 
ATOM   6875  C  CA    . GLY B 1 160 ? 149.505 152.544 156.189 1.00 44.34 ?  160 GLY B CA    1 
ATOM   6876  C  C     . GLY B 1 160 ? 150.431 151.693 155.350 1.00 44.83 ?  160 GLY B C     1 
ATOM   6877  O  O     . GLY B 1 160 ? 151.647 151.752 155.555 1.00 50.06 ?  160 GLY B O     1 
ATOM   6878  N  N     . ARG B 1 161 ? 149.904 150.907 154.416 1.00 45.47 ?  161 ARG B N     1 
ATOM   6879  C  CA    . ARG B 1 161 ? 150.713 150.032 153.581 1.00 44.83 ?  161 ARG B CA    1 
ATOM   6880  C  C     . ARG B 1 161 ? 150.753 150.555 152.152 1.00 49.26 ?  161 ARG B C     1 
ATOM   6881  O  O     . ARG B 1 161 ? 149.721 150.933 151.590 1.00 52.84 ?  161 ARG B O     1 
ATOM   6882  C  CB    . ARG B 1 161 ? 150.175 148.598 153.593 1.00 42.20 ?  161 ARG B CB    1 
ATOM   6883  C  CG    . ARG B 1 161 ? 150.338 147.883 154.922 1.00 45.66 ?  161 ARG B CG    1 
ATOM   6884  C  CD    . ARG B 1 161 ? 150.132 146.388 154.763 1.00 47.01 ?  161 ARG B CD    1 
ATOM   6885  N  NE    . ARG B 1 161 ? 149.971 145.716 156.046 1.00 48.17 ?  161 ARG B NE    1 
ATOM   6886  C  CZ    . ARG B 1 161 ? 149.631 144.443 156.185 1.00 47.62 ?  161 ARG B CZ    1 
ATOM   6887  N  NH1   . ARG B 1 161 ? 149.426 143.663 155.136 1.00 46.27 1  161 ARG B NH1   1 
ATOM   6888  N  NH2   . ARG B 1 161 ? 149.491 143.937 157.407 1.00 47.84 ?  161 ARG B NH2   1 
ATOM   6889  N  N     . LYS B 1 162 ? 151.953 150.573 151.570 1.00 56.98 ?  162 LYS B N     1 
ATOM   6890  C  CA    . LYS B 1 162 ? 152.110 151.059 150.203 1.00 55.92 ?  162 LYS B CA    1 
ATOM   6891  C  C     . LYS B 1 162 ? 151.406 150.143 149.208 1.00 55.34 ?  162 LYS B C     1 
ATOM   6892  O  O     . LYS B 1 162 ? 150.630 150.605 148.364 1.00 58.11 ?  162 LYS B O     1 
ATOM   6893  C  CB    . LYS B 1 162 ? 153.595 151.186 149.863 1.00 56.96 ?  162 LYS B CB    1 
ATOM   6894  C  CG    . LYS B 1 162 ? 153.877 151.489 148.401 1.00 58.29 ?  162 LYS B CG    1 
ATOM   6895  C  CD    . LYS B 1 162 ? 154.165 152.965 148.191 1.00 56.92 ?  162 LYS B CD    1 
ATOM   6896  C  CE    . LYS B 1 162 ? 155.472 153.367 148.852 1.00 57.96 ?  162 LYS B CE    1 
ATOM   6897  N  NZ    . LYS B 1 162 ? 155.438 154.774 149.333 1.00 59.35 1  162 LYS B NZ    1 
ATOM   6898  N  N     . ARG B 1 163 ? 151.667 148.840 149.291 1.00 56.78 ?  163 ARG B N     1 
ATOM   6899  C  CA    . ARG B 1 163 ? 151.046 147.865 148.393 1.00 59.81 ?  163 ARG B CA    1 
ATOM   6900  C  C     . ARG B 1 163 ? 149.767 147.311 149.021 1.00 60.44 ?  163 ARG B C     1 
ATOM   6901  O  O     . ARG B 1 163 ? 149.687 146.164 149.459 1.00 59.18 ?  163 ARG B O     1 
ATOM   6902  C  CB    . ARG B 1 163 ? 152.032 146.753 148.056 1.00 60.02 ?  163 ARG B CB    1 
ATOM   6903  C  CG    . ARG B 1 163 ? 153.216 147.206 147.221 1.00 59.81 ?  163 ARG B CG    1 
ATOM   6904  C  CD    . ARG B 1 163 ? 154.301 146.145 147.194 1.00 60.25 ?  163 ARG B CD    1 
ATOM   6905  N  NE    . ARG B 1 163 ? 154.971 146.020 148.483 1.00 61.40 ?  163 ARG B NE    1 
ATOM   6906  C  CZ    . ARG B 1 163 ? 155.595 144.927 148.898 1.00 62.84 ?  163 ARG B CZ    1 
ATOM   6907  N  NH1   . ARG B 1 163 ? 155.655 143.838 148.148 1.00 62.81 1  163 ARG B NH1   1 
ATOM   6908  N  NH2   . ARG B 1 163 ? 156.173 144.926 150.095 1.00 60.15 ?  163 ARG B NH2   1 
ATOM   6909  N  N     . ARG B 1 164 ? 148.751 148.166 149.055 1.00 58.13 ?  164 ARG B N     1 
ATOM   6910  C  CA    . ARG B 1 164 ? 147.494 147.878 149.725 1.00 52.84 ?  164 ARG B CA    1 
ATOM   6911  C  C     . ARG B 1 164 ? 146.324 148.053 148.767 1.00 52.28 ?  164 ARG B C     1 
ATOM   6912  O  O     . ARG B 1 164 ? 146.382 148.850 147.826 1.00 53.46 ?  164 ARG B O     1 
ATOM   6913  C  CB    . ARG B 1 164 ? 147.297 148.799 150.931 1.00 50.90 ?  164 ARG B CB    1 
ATOM   6914  C  CG    . ARG B 1 164 ? 146.868 150.205 150.542 1.00 51.16 ?  164 ARG B CG    1 
ATOM   6915  C  CD    . ARG B 1 164 ? 146.326 150.982 151.726 1.00 53.64 ?  164 ARG B CD    1 
ATOM   6916  N  NE    . ARG B 1 164 ? 145.664 152.213 151.309 1.00 54.05 ?  164 ARG B NE    1 
ATOM   6917  C  CZ    . ARG B 1 164 ? 145.693 153.349 151.992 1.00 56.05 ?  164 ARG B CZ    1 
ATOM   6918  N  NH1   . ARG B 1 164 ? 146.352 153.452 153.136 1.00 50.62 1  164 ARG B NH1   1 
ATOM   6919  N  NH2   . ARG B 1 164 ? 145.043 154.408 151.518 1.00 53.97 ?  164 ARG B NH2   1 
ATOM   6920  N  N     . GLY B 1 165 ? 145.259 147.297 149.018 1.00 49.55 ?  165 GLY B N     1 
ATOM   6921  C  CA    . GLY B 1 165 ? 143.990 147.543 148.373 1.00 47.34 ?  165 GLY B CA    1 
ATOM   6922  C  C     . GLY B 1 165 ? 143.238 148.668 149.055 1.00 50.15 ?  165 GLY B C     1 
ATOM   6923  O  O     . GLY B 1 165 ? 143.706 149.287 150.011 1.00 50.07 ?  165 GLY B O     1 
ATOM   6924  N  N     . GLU B 1 166 ? 142.041 148.937 148.548 1.00 41.91 ?  166 GLU B N     1 
ATOM   6925  C  CA    . GLU B 1 166 ? 141.220 149.986 149.131 1.00 40.23 ?  166 GLU B CA    1 
ATOM   6926  C  C     . GLU B 1 166 ? 140.773 149.599 150.537 1.00 40.11 ?  166 GLU B C     1 
ATOM   6927  O  O     . GLU B 1 166 ? 140.571 148.422 150.848 1.00 39.45 ?  166 GLU B O     1 
ATOM   6928  C  CB    . GLU B 1 166 ? 140.004 150.268 148.250 1.00 40.78 ?  166 GLU B CB    1 
ATOM   6929  C  CG    . GLU B 1 166 ? 140.315 151.110 147.026 1.00 42.66 ?  166 GLU B CG    1 
ATOM   6930  C  CD    . GLU B 1 166 ? 140.998 152.417 147.379 1.00 47.21 ?  166 GLU B CD    1 
ATOM   6931  O  OE1   . GLU B 1 166 ? 140.824 152.891 148.521 1.00 46.32 ?  166 GLU B OE1   1 
ATOM   6932  O  OE2   . GLU B 1 166 ? 141.711 152.969 146.515 1.00 45.81 -1 166 GLU B OE2   1 
ATOM   6933  N  N     . LEU B 1 167 ? 140.625 150.610 151.394 1.00 35.68 ?  167 LEU B N     1 
ATOM   6934  C  CA    . LEU B 1 167 ? 140.143 150.373 152.748 1.00 32.26 ?  167 LEU B CA    1 
ATOM   6935  C  C     . LEU B 1 167 ? 138.640 150.141 152.793 1.00 32.36 ?  167 LEU B C     1 
ATOM   6936  O  O     . LEU B 1 167 ? 138.135 149.630 153.798 1.00 34.58 ?  167 LEU B O     1 
ATOM   6937  C  CB    . LEU B 1 167 ? 140.520 151.544 153.658 1.00 34.94 ?  167 LEU B CB    1 
ATOM   6938  C  CG    . LEU B 1 167 ? 142.019 151.756 153.887 1.00 32.75 ?  167 LEU B CG    1 
ATOM   6939  C  CD1   . LEU B 1 167 ? 142.259 152.645 155.095 1.00 32.22 ?  167 LEU B CD1   1 
ATOM   6940  C  CD2   . LEU B 1 167 ? 142.735 150.426 154.045 1.00 32.47 ?  167 LEU B CD2   1 
ATOM   6941  N  N     . VAL B 1 168 ? 137.924 150.504 151.734 1.00 33.87 ?  168 VAL B N     1 
ATOM   6942  C  CA    . VAL B 1 168 ? 136.507 150.192 151.596 1.00 26.64 ?  168 VAL B CA    1 
ATOM   6943  C  C     . VAL B 1 168 ? 136.382 148.946 150.731 1.00 30.85 ?  168 VAL B C     1 
ATOM   6944  O  O     . VAL B 1 168 ? 137.016 148.847 149.675 1.00 33.76 ?  168 VAL B O     1 
ATOM   6945  C  CB    . VAL B 1 168 ? 135.741 151.374 150.980 1.00 29.73 ?  168 VAL B CB    1 
ATOM   6946  C  CG1   . VAL B 1 168 ? 134.272 151.024 150.814 1.00 30.93 ?  168 VAL B CG1   1 
ATOM   6947  C  CG2   . VAL B 1 168 ? 135.910 152.619 151.836 1.00 33.68 ?  168 VAL B CG2   1 
ATOM   6948  N  N     . SER B 1 169 ? 135.569 147.989 151.179 1.00 32.04 ?  169 SER B N     1 
ATOM   6949  C  CA    . SER B 1 169 ? 135.484 146.691 150.521 1.00 26.37 ?  169 SER B CA    1 
ATOM   6950  C  C     . SER B 1 169 ? 134.064 146.307 150.119 1.00 24.67 ?  169 SER B C     1 
ATOM   6951  O  O     . SER B 1 169 ? 133.861 145.200 149.610 1.00 33.18 ?  169 SER B O     1 
ATOM   6952  C  CB    . SER B 1 169 ? 136.080 145.607 151.425 1.00 30.72 ?  169 SER B CB    1 
ATOM   6953  O  OG    . SER B 1 169 ? 136.032 144.336 150.802 1.00 34.76 ?  169 SER B OG    1 
ATOM   6954  N  N     . CYS B 1 170 ? 133.080 147.180 150.324 1.00 26.04 ?  170 CYS B N     1 
ATOM   6955  C  CA    . CYS B 1 170 ? 131.693 146.890 149.972 1.00 21.21 ?  170 CYS B CA    1 
ATOM   6956  C  C     . CYS B 1 170 ? 131.174 148.002 149.068 1.00 19.19 ?  170 CYS B C     1 
ATOM   6957  O  O     . CYS B 1 170 ? 131.203 149.180 149.439 1.00 22.78 ?  170 CYS B O     1 
ATOM   6958  C  CB    . CYS B 1 170 ? 130.831 146.725 151.228 1.00 29.68 ?  170 CYS B CB    1 
ATOM   6959  S  SG    . CYS B 1 170 ? 129.985 148.204 151.833 1.00 55.25 ?  170 CYS B SG    1 
ATOM   6960  N  N     . PHE B 1 171 ? 130.723 147.628 147.872 1.00 15.23 ?  171 PHE B N     1 
ATOM   6961  C  CA    . PHE B 1 171 ? 130.227 148.573 146.882 1.00 11.10 ?  171 PHE B CA    1 
ATOM   6962  C  C     . PHE B 1 171 ? 128.900 148.086 146.324 1.00 9.50  ?  171 PHE B C     1 
ATOM   6963  O  O     . PHE B 1 171 ? 128.695 146.883 146.143 1.00 19.10 ?  171 PHE B O     1 
ATOM   6964  C  CB    . PHE B 1 171 ? 131.234 148.764 145.739 1.00 18.55 ?  171 PHE B CB    1 
ATOM   6965  C  CG    . PHE B 1 171 ? 132.615 149.112 146.203 1.00 18.39 ?  171 PHE B CG    1 
ATOM   6966  C  CD1   . PHE B 1 171 ? 132.947 150.422 146.499 1.00 14.76 ?  171 PHE B CD1   1 
ATOM   6967  C  CD2   . PHE B 1 171 ? 133.580 148.131 146.351 1.00 13.76 ?  171 PHE B CD2   1 
ATOM   6968  C  CE1   . PHE B 1 171 ? 134.214 150.747 146.933 1.00 14.78 ?  171 PHE B CE1   1 
ATOM   6969  C  CE2   . PHE B 1 171 ? 134.849 148.451 146.783 1.00 16.07 ?  171 PHE B CE2   1 
ATOM   6970  C  CZ    . PHE B 1 171 ? 135.166 149.761 147.074 1.00 12.80 ?  171 PHE B CZ    1 
ATOM   6971  N  N     . LEU B 1 172 ? 128.002 149.029 146.054 1.00 15.87 ?  172 LEU B N     1 
ATOM   6972  C  CA    . LEU B 1 172 ? 126.705 148.750 145.456 1.00 9.32  ?  172 LEU B CA    1 
ATOM   6973  C  C     . LEU B 1 172 ? 126.570 149.565 144.180 1.00 10.44 ?  172 LEU B C     1 
ATOM   6974  O  O     . LEU B 1 172 ? 126.764 150.785 144.197 1.00 16.85 ?  172 LEU B O     1 
ATOM   6975  C  CB    . LEU B 1 172 ? 125.565 149.080 146.423 1.00 15.54 ?  172 LEU B CB    1 
ATOM   6976  C  CG    . LEU B 1 172 ? 125.448 148.208 147.674 1.00 11.15 ?  172 LEU B CG    1 
ATOM   6977  C  CD1   . LEU B 1 172 ? 126.512 148.580 148.696 1.00 12.17 ?  172 LEU B CD1   1 
ATOM   6978  C  CD2   . LEU B 1 172 ? 124.057 148.324 148.274 1.00 10.83 ?  172 LEU B CD2   1 
ATOM   6979  N  N     . LEU B 1 173 ? 126.235 148.895 143.082 1.00 21.17 ?  173 LEU B N     1 
ATOM   6980  C  CA    . LEU B 1 173 ? 126.190 149.519 141.767 1.00 9.03  ?  173 LEU B CA    1 
ATOM   6981  C  C     . LEU B 1 173 ? 124.777 149.463 141.207 1.00 15.26 ?  173 LEU B C     1 
ATOM   6982  O  O     . LEU B 1 173 ? 124.178 148.387 141.125 1.00 25.70 ?  173 LEU B O     1 
ATOM   6983  C  CB    . LEU B 1 173 ? 127.156 148.831 140.799 1.00 15.52 ?  173 LEU B CB    1 
ATOM   6984  C  CG    . LEU B 1 173 ? 128.634 148.800 141.187 1.00 20.33 ?  173 LEU B CG    1 
ATOM   6985  C  CD1   . LEU B 1 173 ? 129.450 148.094 140.115 1.00 16.74 ?  173 LEU B CD1   1 
ATOM   6986  C  CD2   . LEU B 1 173 ? 129.155 150.204 141.428 1.00 15.13 ?  173 LEU B CD2   1 
ATOM   6987  N  N     . GLU B 1 174 ? 124.251 150.624 140.830 1.00 23.06 ?  174 GLU B N     1 
ATOM   6988  C  CA    . GLU B 1 174 ? 123.032 150.687 140.039 1.00 19.27 ?  174 GLU B CA    1 
ATOM   6989  C  C     . GLU B 1 174 ? 123.369 150.493 138.566 1.00 17.32 ?  174 GLU B C     1 
ATOM   6990  O  O     . GLU B 1 174 ? 124.346 151.051 138.061 1.00 26.14 ?  174 GLU B O     1 
ATOM   6991  C  CB    . GLU B 1 174 ? 122.328 152.028 140.240 1.00 23.43 ?  174 GLU B CB    1 
ATOM   6992  C  CG    . GLU B 1 174 ? 121.693 152.211 141.604 1.00 17.66 ?  174 GLU B CG    1 
ATOM   6993  C  CD    . GLU B 1 174 ? 120.220 151.867 141.609 1.00 23.21 ?  174 GLU B CD    1 
ATOM   6994  O  OE1   . GLU B 1 174 ? 119.648 151.677 140.516 1.00 30.48 ?  174 GLU B OE1   1 
ATOM   6995  O  OE2   . GLU B 1 174 ? 119.630 151.786 142.706 1.00 25.79 -1 174 GLU B OE2   1 
ATOM   6996  N  N     . VAL B 1 175 ? 122.555 149.698 137.879 1.00 18.77 ?  175 VAL B N     1 
ATOM   6997  C  CA    . VAL B 1 175 ? 122.741 149.416 136.462 1.00 19.51 ?  175 VAL B CA    1 
ATOM   6998  C  C     . VAL B 1 175 ? 121.528 149.934 135.704 1.00 18.54 ?  175 VAL B C     1 
ATOM   6999  O  O     . VAL B 1 175 ? 120.392 149.554 136.007 1.00 21.00 ?  175 VAL B O     1 
ATOM   7000  C  CB    . VAL B 1 175 ? 122.948 147.913 136.200 1.00 22.56 ?  175 VAL B CB    1 
ATOM   7001  C  CG1   . VAL B 1 175 ? 123.580 147.697 134.837 1.00 16.09 ?  175 VAL B CG1   1 
ATOM   7002  C  CG2   . VAL B 1 175 ? 123.800 147.297 137.295 1.00 18.87 ?  175 VAL B CG2   1 
ATOM   7003  N  N     . ASN B 1 176 ? 121.770 150.793 134.722 1.00 22.18 ?  176 ASN B N     1 
ATOM   7004  C  CA    . ASN B 1 176 ? 120.710 151.314 133.874 1.00 19.90 ?  176 ASN B CA    1 
ATOM   7005  C  C     . ASN B 1 176 ? 120.451 150.366 132.706 1.00 21.94 ?  176 ASN B C     1 
ATOM   7006  O  O     . ASN B 1 176 ? 121.298 149.554 132.328 1.00 29.28 ?  176 ASN B O     1 
ATOM   7007  C  CB    . ASN B 1 176 ? 121.068 152.707 133.360 1.00 15.03 ?  176 ASN B CB    1 
ATOM   7008  C  CG    . ASN B 1 176 ? 119.885 153.649 133.361 1.00 20.29 ?  176 ASN B CG    1 
ATOM   7009  O  OD1   . ASN B 1 176 ? 118.735 153.218 133.412 1.00 27.79 ?  176 ASN B OD1   1 
ATOM   7010  N  ND2   . ASN B 1 176 ? 120.161 154.945 133.308 1.00 19.69 ?  176 ASN B ND2   1 
ATOM   7011  N  N     . ASP B 1 177 ? 119.259 150.488 132.129 1.00 20.94 ?  177 ASP B N     1 
ATOM   7012  C  CA    . ASP B 1 177 ? 118.797 149.580 131.080 1.00 23.95 ?  177 ASP B CA    1 
ATOM   7013  C  C     . ASP B 1 177 ? 119.336 150.053 129.735 1.00 22.61 ?  177 ASP B C     1 
ATOM   7014  O  O     . ASP B 1 177 ? 118.651 150.731 128.969 1.00 25.78 ?  177 ASP B O     1 
ATOM   7015  C  CB    . ASP B 1 177 ? 117.276 149.501 131.083 1.00 20.59 ?  177 ASP B CB    1 
ATOM   7016  C  CG    . ASP B 1 177 ? 116.745 148.425 130.163 1.00 26.59 ?  177 ASP B CG    1 
ATOM   7017  O  OD1   . ASP B 1 177 ? 117.405 147.375 130.032 1.00 30.90 ?  177 ASP B OD1   1 
ATOM   7018  O  OD2   . ASP B 1 177 ? 115.662 148.629 129.579 1.00 26.29 -1 177 ASP B OD2   1 
ATOM   7019  N  N     . SER B 1 178 ? 120.581 149.688 129.444 1.00 20.40 ?  178 SER B N     1 
ATOM   7020  C  CA    . SER B 1 178 ? 121.206 150.008 128.168 1.00 19.79 ?  178 SER B CA    1 
ATOM   7021  C  C     . SER B 1 178 ? 122.514 149.237 128.069 1.00 20.76 ?  178 SER B C     1 
ATOM   7022  O  O     . SER B 1 178 ? 123.095 148.836 129.080 1.00 27.35 ?  178 SER B O     1 
ATOM   7023  C  CB    . SER B 1 178 ? 121.454 151.511 128.014 1.00 15.37 ?  178 SER B CB    1 
ATOM   7024  O  OG    . SER B 1 178 ? 122.686 151.889 128.598 1.00 18.83 ?  178 SER B OG    1 
ATOM   7025  N  N     . LEU B 1 179 ? 122.968 149.031 126.829 1.00 25.00 ?  179 LEU B N     1 
ATOM   7026  C  CA    . LEU B 1 179 ? 124.221 148.316 126.610 1.00 19.31 ?  179 LEU B CA    1 
ATOM   7027  C  C     . LEU B 1 179 ? 125.406 149.084 127.181 1.00 22.35 ?  179 LEU B C     1 
ATOM   7028  O  O     . LEU B 1 179 ? 126.311 148.486 127.775 1.00 23.18 ?  179 LEU B O     1 
ATOM   7029  C  CB    . LEU B 1 179 ? 124.422 148.052 125.118 1.00 20.33 ?  179 LEU B CB    1 
ATOM   7030  C  CG    . LEU B 1 179 ? 125.576 147.114 124.757 1.00 19.58 ?  179 LEU B CG    1 
ATOM   7031  C  CD1   . LEU B 1 179 ? 125.344 145.732 125.344 1.00 21.13 ?  179 LEU B CD1   1 
ATOM   7032  C  CD2   . LEU B 1 179 ? 125.758 147.040 123.252 1.00 20.77 ?  179 LEU B CD2   1 
ATOM   7033  N  N     . ASN B 1 180 ? 125.426 150.407 127.003 1.00 22.76 ?  180 ASN B N     1 
ATOM   7034  C  CA    . ASN B 1 180 ? 126.494 151.209 127.587 1.00 19.52 ?  180 ASN B CA    1 
ATOM   7035  C  C     . ASN B 1 180 ? 126.538 151.038 129.097 1.00 19.51 ?  180 ASN B C     1 
ATOM   7036  O  O     . ASN B 1 180 ? 127.612 150.860 129.682 1.00 22.73 ?  180 ASN B O     1 
ATOM   7037  C  CB    . ASN B 1 180 ? 126.306 152.684 127.231 1.00 21.95 ?  180 ASN B CB    1 
ATOM   7038  C  CG    . ASN B 1 180 ? 126.510 152.960 125.759 1.00 22.82 ?  180 ASN B CG    1 
ATOM   7039  O  OD1   . ASN B 1 180 ? 127.475 152.491 125.157 1.00 30.13 ?  180 ASN B OD1   1 
ATOM   7040  N  ND2   . ASN B 1 180 ? 125.606 153.732 125.172 1.00 27.44 ?  180 ASN B ND2   1 
ATOM   7041  N  N     . ASP B 1 181 ? 125.373 151.078 129.744 1.00 22.65 ?  181 ASP B N     1 
ATOM   7042  C  CA    . ASP B 1 181 ? 125.321 150.933 131.193 1.00 18.27 ?  181 ASP B CA    1 
ATOM   7043  C  C     . ASP B 1 181 ? 125.745 149.537 131.630 1.00 16.25 ?  181 ASP B C     1 
ATOM   7044  O  O     . ASP B 1 181 ? 126.435 149.387 132.640 1.00 26.24 ?  181 ASP B O     1 
ATOM   7045  C  CB    . ASP B 1 181 ? 123.919 151.261 131.698 1.00 22.11 ?  181 ASP B CB    1 
ATOM   7046  C  CG    . ASP B 1 181 ? 123.561 152.718 131.499 1.00 27.67 ?  181 ASP B CG    1 
ATOM   7047  O  OD1   . ASP B 1 181 ? 124.302 153.584 132.005 1.00 27.90 ?  181 ASP B OD1   1 
ATOM   7048  O  OD2   . ASP B 1 181 ? 122.545 152.997 130.831 1.00 33.09 -1 181 ASP B OD2   1 
ATOM   7049  N  N     . ILE B 1 182 ? 125.350 148.503 130.886 1.00 18.74 ?  182 ILE B N     1 
ATOM   7050  C  CA    . ILE B 1 182 ? 125.744 147.143 131.245 1.00 20.29 ?  182 ILE B CA    1 
ATOM   7051  C  C     . ILE B 1 182 ? 127.253 146.966 131.113 1.00 18.02 ?  182 ILE B C     1 
ATOM   7052  O  O     . ILE B 1 182 ? 127.903 146.374 131.985 1.00 22.60 ?  182 ILE B O     1 
ATOM   7053  C  CB    . ILE B 1 182 ? 124.975 146.122 130.386 1.00 23.79 ?  182 ILE B CB    1 
ATOM   7054  C  CG1   . ILE B 1 182 ? 123.529 145.999 130.870 1.00 22.48 ?  182 ILE B CG1   1 
ATOM   7055  C  CG2   . ILE B 1 182 ? 125.664 144.769 130.420 1.00 16.31 ?  182 ILE B CG2   1 
ATOM   7056  C  CD1   . ILE B 1 182 ? 122.594 145.397 129.849 1.00 21.31 ?  182 ILE B CD1   1 
ATOM   7057  N  N     . SER B 1 183 ? 127.833 147.463 130.021 1.00 21.31 ?  183 SER B N     1 
ATOM   7058  C  CA    . SER B 1 183 ? 129.276 147.358 129.840 1.00 21.13 ?  183 SER B CA    1 
ATOM   7059  C  C     . SER B 1 183 ? 130.022 148.143 130.912 1.00 19.61 ?  183 SER B C     1 
ATOM   7060  O  O     . SER B 1 183 ? 131.032 147.671 131.452 1.00 24.54 ?  183 SER B O     1 
ATOM   7061  C  CB    . SER B 1 183 ? 129.665 147.839 128.442 1.00 17.24 ?  183 SER B CB    1 
ATOM   7062  O  OG    . SER B 1 183 ? 129.615 149.251 128.356 1.00 31.53 ?  183 SER B OG    1 
ATOM   7063  N  N     . ARG B 1 184 ? 129.537 149.342 131.240 1.00 19.95 ?  184 ARG B N     1 
ATOM   7064  C  CA    . ARG B 1 184 ? 130.155 150.117 132.308 1.00 19.80 ?  184 ARG B CA    1 
ATOM   7065  C  C     . ARG B 1 184 ? 130.026 149.409 133.648 1.00 22.55 ?  184 ARG B C     1 
ATOM   7066  O  O     . ARG B 1 184 ? 130.937 149.468 134.476 1.00 24.43 ?  184 ARG B O     1 
ATOM   7067  C  CB    . ARG B 1 184 ? 129.536 151.511 132.378 1.00 19.35 ?  184 ARG B CB    1 
ATOM   7068  C  CG    . ARG B 1 184 ? 130.274 152.452 133.306 1.00 24.70 ?  184 ARG B CG    1 
ATOM   7069  C  CD    . ARG B 1 184 ? 131.733 152.557 132.916 1.00 25.62 ?  184 ARG B CD    1 
ATOM   7070  N  NE    . ARG B 1 184 ? 131.914 153.332 131.695 1.00 33.16 ?  184 ARG B NE    1 
ATOM   7071  C  CZ    . ARG B 1 184 ? 133.084 153.767 131.251 1.00 36.43 ?  184 ARG B CZ    1 
ATOM   7072  N  NH1   . ARG B 1 184 ? 134.209 153.506 131.897 1.00 27.27 1  184 ARG B NH1   1 
ATOM   7073  N  NH2   . ARG B 1 184 ? 133.127 154.481 130.131 1.00 30.06 ?  184 ARG B NH2   1 
ATOM   7074  N  N     . ALA B 1 185 ? 128.893 148.747 133.888 1.00 24.87 ?  185 ALA B N     1 
ATOM   7075  C  CA    . ALA B 1 185 ? 128.724 147.991 135.122 1.00 14.62 ?  185 ALA B CA    1 
ATOM   7076  C  C     . ALA B 1 185 ? 129.726 146.852 135.204 1.00 18.34 ?  185 ALA B C     1 
ATOM   7077  O  O     . ALA B 1 185 ? 130.318 146.615 136.262 1.00 19.91 ?  185 ALA B O     1 
ATOM   7078  C  CB    . ALA B 1 185 ? 127.296 147.457 135.219 1.00 13.71 ?  185 ALA B CB    1 
ATOM   7079  N  N     . ILE B 1 186 ? 129.931 146.137 134.099 1.00 24.67 ?  186 ILE B N     1 
ATOM   7080  C  CA    . ILE B 1 186 ? 130.925 145.064 134.089 1.00 22.88 ?  186 ILE B CA    1 
ATOM   7081  C  C     . ILE B 1 186 ? 132.312 145.629 134.374 1.00 21.01 ?  186 ILE B C     1 
ATOM   7082  O  O     . ILE B 1 186 ? 133.075 145.083 135.182 1.00 24.96 ?  186 ILE B O     1 
ATOM   7083  C  CB    . ILE B 1 186 ? 130.890 144.309 132.748 1.00 25.71 ?  186 ILE B CB    1 
ATOM   7084  C  CG1   . ILE B 1 186 ? 129.578 143.539 132.597 1.00 22.12 ?  186 ILE B CG1   1 
ATOM   7085  C  CG2   . ILE B 1 186 ? 132.079 143.368 132.637 1.00 19.04 ?  186 ILE B CG2   1 
ATOM   7086  C  CD1   . ILE B 1 186 ? 129.265 143.150 131.172 1.00 21.88 ?  186 ILE B CD1   1 
ATOM   7087  N  N     . ASP B 1 187 ? 132.652 146.742 133.719 1.00 21.86 ?  187 ASP B N     1 
ATOM   7088  C  CA    . ASP B 1 187 ? 133.964 147.349 133.920 1.00 20.72 ?  187 ASP B CA    1 
ATOM   7089  C  C     . ASP B 1 187 ? 134.153 147.797 135.365 1.00 25.75 ?  187 ASP B C     1 
ATOM   7090  O  O     . ASP B 1 187 ? 135.215 147.575 135.958 1.00 26.10 ?  187 ASP B O     1 
ATOM   7091  C  CB    . ASP B 1 187 ? 134.144 148.528 132.964 1.00 18.17 ?  187 ASP B CB    1 
ATOM   7092  C  CG    . ASP B 1 187 ? 135.250 149.468 133.398 1.00 31.04 ?  187 ASP B CG    1 
ATOM   7093  O  OD1   . ASP B 1 187 ? 136.355 148.986 133.723 1.00 28.37 ?  187 ASP B OD1   1 
ATOM   7094  O  OD2   . ASP B 1 187 ? 135.013 150.693 133.419 1.00 39.42 -1 187 ASP B OD2   1 
ATOM   7095  N  N     . ILE B 1 188 ? 133.135 148.433 135.945 1.00 26.86 ?  188 ILE B N     1 
ATOM   7096  C  CA    . ILE B 1 188 ? 133.229 148.919 137.317 1.00 19.95 ?  188 ILE B CA    1 
ATOM   7097  C  C     . ILE B 1 188 ? 133.325 147.755 138.291 1.00 25.91 ?  188 ILE B C     1 
ATOM   7098  O  O     . ILE B 1 188 ? 134.076 147.810 139.270 1.00 27.44 ?  188 ILE B O     1 
ATOM   7099  C  CB    . ILE B 1 188 ? 132.034 149.830 137.644 1.00 25.16 ?  188 ILE B CB    1 
ATOM   7100  C  CG1   . ILE B 1 188 ? 132.133 151.146 136.872 1.00 23.76 ?  188 ILE B CG1   1 
ATOM   7101  C  CG2   . ILE B 1 188 ? 131.955 150.088 139.140 1.00 21.08 ?  188 ILE B CG2   1 
ATOM   7102  C  CD1   . ILE B 1 188 ? 130.900 152.008 136.985 1.00 20.01 ?  188 ILE B CD1   1 
ATOM   7103  N  N     . SER B 1 189 ? 132.550 146.694 138.059 1.00 20.84 ?  189 SER B N     1 
ATOM   7104  C  CA    . SER B 1 189 ? 132.633 145.520 138.917 1.00 14.99 ?  189 SER B CA    1 
ATOM   7105  C  C     . SER B 1 189 ? 134.027 144.919 138.879 1.00 19.05 ?  189 SER B C     1 
ATOM   7106  O  O     . SER B 1 189 ? 134.578 144.541 139.918 1.00 25.64 ?  189 SER B O     1 
ATOM   7107  C  CB    . SER B 1 189 ? 131.591 144.486 138.495 1.00 21.93 ?  189 SER B CB    1 
ATOM   7108  O  OG    . SER B 1 189 ? 130.278 144.993 138.641 1.00 26.71 ?  189 SER B OG    1 
ATOM   7109  N  N     . MET B 1 190 ? 134.617 144.825 137.685 1.00 27.49 ?  190 MET B N     1 
ATOM   7110  C  CA    . MET B 1 190 ? 135.970 144.293 137.576 1.00 22.83 ?  190 MET B CA    1 
ATOM   7111  C  C     . MET B 1 190 ? 136.979 145.201 138.272 1.00 24.83 ?  190 MET B C     1 
ATOM   7112  O  O     . MET B 1 190 ? 137.889 144.718 138.953 1.00 27.49 ?  190 MET B O     1 
ATOM   7113  C  CB    . MET B 1 190 ? 136.328 144.099 136.105 1.00 21.60 ?  190 MET B CB    1 
ATOM   7114  C  CG    . MET B 1 190 ? 135.725 142.845 135.494 1.00 24.36 ?  190 MET B CG    1 
ATOM   7115  S  SD    . MET B 1 190 ? 136.886 141.902 134.497 1.00 40.38 ?  190 MET B SD    1 
ATOM   7116  C  CE    . MET B 1 190 ? 136.880 142.877 132.996 1.00 28.15 ?  190 MET B CE    1 
ATOM   7117  N  N     . GLN B 1 191 ? 136.826 146.518 138.118 1.00 22.77 ?  191 GLN B N     1 
ATOM   7118  C  CA    . GLN B 1 191 ? 137.734 147.455 138.772 1.00 22.47 ?  191 GLN B CA    1 
ATOM   7119  C  C     . GLN B 1 191 ? 137.639 147.356 140.289 1.00 23.48 ?  191 GLN B C     1 
ATOM   7120  O  O     . GLN B 1 191 ? 138.654 147.431 140.989 1.00 30.05 ?  191 GLN B O     1 
ATOM   7121  C  CB    . GLN B 1 191 ? 137.432 148.883 138.317 1.00 25.32 ?  191 GLN B CB    1 
ATOM   7122  C  CG    . GLN B 1 191 ? 137.584 149.124 136.827 1.00 21.80 ?  191 GLN B CG    1 
ATOM   7123  C  CD    . GLN B 1 191 ? 139.011 148.965 136.350 1.00 25.92 ?  191 GLN B CD    1 
ATOM   7124  O  OE1   . GLN B 1 191 ? 139.947 148.953 137.148 1.00 22.72 ?  191 GLN B OE1   1 
ATOM   7125  N  NE2   . GLN B 1 191 ? 139.186 148.844 135.040 1.00 26.51 ?  191 GLN B NE2   1 
ATOM   7126  N  N     . LEU B 1 192 ? 136.423 147.201 140.815 1.00 23.27 ?  192 LEU B N     1 
ATOM   7127  C  CA    . LEU B 1 192 ? 136.226 147.156 142.259 1.00 21.03 ?  192 LEU B CA    1 
ATOM   7128  C  C     . LEU B 1 192 ? 136.664 145.821 142.845 1.00 24.24 ?  192 LEU B C     1 
ATOM   7129  O  O     . LEU B 1 192 ? 137.207 145.780 143.954 1.00 33.46 ?  192 LEU B O     1 
ATOM   7130  C  CB    . LEU B 1 192 ? 134.761 147.436 142.599 1.00 21.12 ?  192 LEU B CB    1 
ATOM   7131  C  CG    . LEU B 1 192 ? 134.233 148.827 142.241 1.00 21.56 ?  192 LEU B CG    1 
ATOM   7132  C  CD1   . LEU B 1 192 ? 132.730 148.899 142.446 1.00 16.19 ?  192 LEU B CD1   1 
ATOM   7133  C  CD2   . LEU B 1 192 ? 134.941 149.901 143.046 1.00 16.21 ?  192 LEU B CD2   1 
ATOM   7134  N  N     . SER B 1 193 ? 136.432 144.721 142.126 1.00 24.20 ?  193 SER B N     1 
ATOM   7135  C  CA    . SER B 1 193 ? 136.925 143.429 142.585 1.00 21.04 ?  193 SER B CA    1 
ATOM   7136  C  C     . SER B 1 193 ? 138.443 143.361 142.510 1.00 27.93 ?  193 SER B C     1 
ATOM   7137  O  O     . SER B 1 193 ? 139.076 142.701 143.340 1.00 35.38 ?  193 SER B O     1 
ATOM   7138  C  CB    . SER B 1 193 ? 136.294 142.305 141.767 1.00 24.36 ?  193 SER B CB    1 
ATOM   7139  O  OG    . SER B 1 193 ? 134.884 142.328 141.883 1.00 37.63 ?  193 SER B OG    1 
ATOM   7140  N  N     . LYS B 1 194 ? 139.040 144.033 141.524 1.00 29.41 ?  194 LYS B N     1 
ATOM   7141  C  CA    . LYS B 1 194 ? 140.490 144.168 141.486 1.00 28.40 ?  194 LYS B CA    1 
ATOM   7142  C  C     . LYS B 1 194 ? 141.019 144.818 142.758 1.00 34.56 ?  194 LYS B C     1 
ATOM   7143  O  O     . LYS B 1 194 ? 142.146 144.534 143.179 1.00 36.23 ?  194 LYS B O     1 
ATOM   7144  C  CB    . LYS B 1 194 ? 140.898 144.978 140.254 1.00 28.18 ?  194 LYS B CB    1 
ATOM   7145  C  CG    . LYS B 1 194 ? 142.360 145.369 140.198 1.00 30.58 ?  194 LYS B CG    1 
ATOM   7146  C  CD    . LYS B 1 194 ? 142.620 146.283 139.013 1.00 32.32 ?  194 LYS B CD    1 
ATOM   7147  C  CE    . LYS B 1 194 ? 144.102 146.584 138.848 1.00 35.35 ?  194 LYS B CE    1 
ATOM   7148  N  NZ    . LYS B 1 194 ? 144.343 147.578 137.765 1.00 32.65 1  194 LYS B NZ    1 
ATOM   7149  N  N     . LEU B 1 195 ? 140.222 145.684 143.382 1.00 29.96 ?  195 LEU B N     1 
ATOM   7150  C  CA    . LEU B 1 195 ? 140.590 146.322 144.638 1.00 26.87 ?  195 LEU B CA    1 
ATOM   7151  C  C     . LEU B 1 195 ? 140.282 145.459 145.855 1.00 28.58 ?  195 LEU B C     1 
ATOM   7152  O  O     . LEU B 1 195 ? 140.589 145.870 146.978 1.00 40.29 ?  195 LEU B O     1 
ATOM   7153  C  CB    . LEU B 1 195 ? 139.873 147.666 144.773 1.00 34.53 ?  195 LEU B CB    1 
ATOM   7154  C  CG    . LEU B 1 195 ? 140.105 148.689 143.661 1.00 36.26 ?  195 LEU B CG    1 
ATOM   7155  C  CD1   . LEU B 1 195 ? 139.248 149.924 143.886 1.00 31.63 ?  195 LEU B CD1   1 
ATOM   7156  C  CD2   . LEU B 1 195 ? 141.574 149.059 143.566 1.00 30.96 ?  195 LEU B CD2   1 
ATOM   7157  N  N     . GLY B 1 196 ? 139.683 144.284 145.662 1.00 26.93 ?  196 GLY B N     1 
ATOM   7158  C  CA    . GLY B 1 196 ? 139.358 143.392 146.751 1.00 29.52 ?  196 GLY B CA    1 
ATOM   7159  C  C     . GLY B 1 196 ? 137.987 143.586 147.360 1.00 34.36 ?  196 GLY B C     1 
ATOM   7160  O  O     . GLY B 1 196 ? 137.587 142.780 148.209 1.00 34.21 ?  196 GLY B O     1 
ATOM   7161  N  N     . GLY B 1 197 ? 137.253 144.620 146.957 1.00 28.37 ?  197 GLY B N     1 
ATOM   7162  C  CA    . GLY B 1 197 ? 135.939 144.853 147.517 1.00 23.86 ?  197 GLY B CA    1 
ATOM   7163  C  C     . GLY B 1 197 ? 134.866 143.999 146.865 1.00 23.54 ?  197 GLY B C     1 
ATOM   7164  O  O     . GLY B 1 197 ? 134.931 143.663 145.684 1.00 27.42 ?  197 GLY B O     1 
ATOM   7165  N  N     . GLY B 1 198 ? 133.862 143.643 147.666 1.00 13.20 ?  198 GLY B N     1 
ATOM   7166  C  CA    . GLY B 1 198 ? 132.702 142.947 147.138 1.00 11.25 ?  198 GLY B CA    1 
ATOM   7167  C  C     . GLY B 1 198 ? 131.740 143.921 146.473 1.00 15.33 ?  198 GLY B C     1 
ATOM   7168  O  O     . GLY B 1 198 ? 131.506 145.026 146.958 1.00 17.15 ?  198 GLY B O     1 
ATOM   7169  N  N     . VAL B 1 199 ? 131.181 143.494 145.345 1.00 17.11 ?  199 VAL B N     1 
ATOM   7170  C  CA    . VAL B 1 199 ? 130.348 144.344 144.505 1.00 11.18 ?  199 VAL B CA    1 
ATOM   7171  C  C     . VAL B 1 199 ? 128.949 143.749 144.437 1.00 10.70 ?  199 VAL B C     1 
ATOM   7172  O  O     . VAL B 1 199 ? 128.784 142.570 144.107 1.00 15.52 ?  199 VAL B O     1 
ATOM   7173  C  CB    . VAL B 1 199 ? 130.939 144.504 143.092 1.00 15.15 ?  199 VAL B CB    1 
ATOM   7174  C  CG1   . VAL B 1 199 ? 130.143 145.526 142.298 1.00 10.87 ?  199 VAL B CG1   1 
ATOM   7175  C  CG2   . VAL B 1 199 ? 132.401 144.902 143.172 1.00 14.25 ?  199 VAL B CG2   1 
ATOM   7176  N  N     . SER B 1 200 ? 127.949 144.568 144.745 1.00 12.17 ?  200 SER B N     1 
ATOM   7177  C  CA    . SER B 1 200 ? 126.549 144.205 144.605 1.00 3.11  ?  200 SER B CA    1 
ATOM   7178  C  C     . SER B 1 200 ? 125.931 145.063 143.512 1.00 13.17 ?  200 SER B C     1 
ATOM   7179  O  O     . SER B 1 200 ? 126.120 146.283 143.495 1.00 22.36 ?  200 SER B O     1 
ATOM   7180  C  CB    . SER B 1 200 ? 125.794 144.392 145.922 1.00 6.79  ?  200 SER B CB    1 
ATOM   7181  O  OG    . SER B 1 200 ? 124.596 143.640 145.932 1.00 20.98 ?  200 SER B OG    1 
ATOM   7182  N  N     . LEU B 1 201 ? 125.202 144.429 142.600 1.00 16.32 ?  201 LEU B N     1 
ATOM   7183  C  CA    . LEU B 1 201 ? 124.614 145.111 141.459 1.00 7.40  ?  201 LEU B CA    1 
ATOM   7184  C  C     . LEU B 1 201 ? 123.100 144.967 141.493 1.00 9.06  ?  201 LEU B C     1 
ATOM   7185  O  O     . LEU B 1 201 ? 122.575 143.886 141.772 1.00 16.94 ?  201 LEU B O     1 
ATOM   7186  C  CB    . LEU B 1 201 ? 125.164 144.563 140.141 1.00 22.38 ?  201 LEU B CB    1 
ATOM   7187  C  CG    . LEU B 1 201 ? 126.645 144.848 139.880 1.00 16.51 ?  201 LEU B CG    1 
ATOM   7188  C  CD1   . LEU B 1 201 ? 127.472 143.586 140.050 1.00 18.91 ?  201 LEU B CD1   1 
ATOM   7189  C  CD2   . LEU B 1 201 ? 126.842 145.445 138.497 1.00 18.93 ?  201 LEU B CD2   1 
ATOM   7190  N  N     . ASN B 1 202 ? 122.409 146.067 141.215 1.00 12.73 ?  202 ASN B N     1 
ATOM   7191  C  CA    . ASN B 1 202 ? 120.956 146.085 141.131 1.00 13.50 ?  202 ASN B CA    1 
ATOM   7192  C  C     . ASN B 1 202 ? 120.558 145.887 139.675 1.00 21.99 ?  202 ASN B C     1 
ATOM   7193  O  O     . ASN B 1 202 ? 120.886 146.717 138.820 1.00 30.10 ?  202 ASN B O     1 
ATOM   7194  C  CB    . ASN B 1 202 ? 120.393 147.396 141.677 1.00 8.96  ?  202 ASN B CB    1 
ATOM   7195  C  CG    . ASN B 1 202 ? 118.917 147.308 141.999 1.00 11.60 ?  202 ASN B CG    1 
ATOM   7196  O  OD1   . ASN B 1 202 ? 118.367 146.219 142.147 1.00 24.55 ?  202 ASN B OD1   1 
ATOM   7197  N  ND2   . ASN B 1 202 ? 118.267 148.458 142.111 1.00 14.23 ?  202 ASN B ND2   1 
ATOM   7198  N  N     . LEU B 1 203 ? 119.859 144.789 139.396 1.00 13.29 ?  203 LEU B N     1 
ATOM   7199  C  CA    . LEU B 1 203 ? 119.456 144.444 138.041 1.00 12.69 ?  203 LEU B CA    1 
ATOM   7200  C  C     . LEU B 1 203 ? 117.970 144.666 137.798 1.00 12.56 ?  203 LEU B C     1 
ATOM   7201  O  O     . LEU B 1 203 ? 117.433 144.162 136.808 1.00 22.15 ?  203 LEU B O     1 
ATOM   7202  C  CB    . LEU B 1 203 ? 119.828 142.991 137.740 1.00 16.29 ?  203 LEU B CB    1 
ATOM   7203  C  CG    . LEU B 1 203 ? 121.293 142.610 137.966 1.00 20.17 ?  203 LEU B CG    1 
ATOM   7204  C  CD1   . LEU B 1 203 ? 121.575 141.219 137.424 1.00 19.83 ?  203 LEU B CD1   1 
ATOM   7205  C  CD2   . LEU B 1 203 ? 122.224 143.633 137.333 1.00 14.50 ?  203 LEU B CD2   1 
ATOM   7206  N  N     . SER B 1 204 ? 117.293 145.408 138.676 1.00 18.55 ?  204 SER B N     1 
ATOM   7207  C  CA    . SER B 1 204 ? 115.851 145.582 138.552 1.00 13.82 ?  204 SER B CA    1 
ATOM   7208  C  C     . SER B 1 204 ? 115.470 146.548 137.439 1.00 16.78 ?  204 SER B C     1 
ATOM   7209  O  O     . SER B 1 204 ? 114.331 146.506 136.966 1.00 30.11 ?  204 SER B O     1 
ATOM   7210  C  CB    . SER B 1 204 ? 115.267 146.062 139.879 1.00 17.67 ?  204 SER B CB    1 
ATOM   7211  O  OG    . SER B 1 204 ? 115.552 145.146 140.919 1.00 25.80 ?  204 SER B OG    1 
ATOM   7212  N  N     . LYS B 1 205 ? 116.386 147.416 137.012 1.00 17.66 ?  205 LYS B N     1 
ATOM   7213  C  CA    . LYS B 1 205 ? 116.094 148.334 135.920 1.00 16.64 ?  205 LYS B CA    1 
ATOM   7214  C  C     . LYS B 1 205 ? 116.334 147.720 134.550 1.00 20.34 ?  205 LYS B C     1 
ATOM   7215  O  O     . LYS B 1 205 ? 115.889 148.291 133.549 1.00 25.78 ?  205 LYS B O     1 
ATOM   7216  C  CB    . LYS B 1 205 ? 116.921 149.611 136.066 1.00 17.44 ?  205 LYS B CB    1 
ATOM   7217  C  CG    . LYS B 1 205 ? 116.477 150.504 137.207 1.00 17.56 ?  205 LYS B CG    1 
ATOM   7218  C  CD    . LYS B 1 205 ? 117.349 151.739 137.311 1.00 21.80 ?  205 LYS B CD    1 
ATOM   7219  C  CE    . LYS B 1 205 ? 116.741 152.767 138.250 1.00 27.15 ?  205 LYS B CE    1 
ATOM   7220  N  NZ    . LYS B 1 205 ? 116.611 152.250 139.638 1.00 19.73 1  205 LYS B NZ    1 
ATOM   7221  N  N     . LEU B 1 206 ? 117.019 146.582 134.477 1.00 23.50 ?  206 LEU B N     1 
ATOM   7222  C  CA    . LEU B 1 206 ? 117.168 145.879 133.212 1.00 18.04 ?  206 LEU B CA    1 
ATOM   7223  C  C     . LEU B 1 206 ? 115.832 145.284 132.788 1.00 22.84 ?  206 LEU B C     1 
ATOM   7224  O  O     . LEU B 1 206 ? 115.086 144.746 133.610 1.00 29.66 ?  206 LEU B O     1 
ATOM   7225  C  CB    . LEU B 1 206 ? 118.217 144.777 133.336 1.00 21.21 ?  206 LEU B CB    1 
ATOM   7226  C  CG    . LEU B 1 206 ? 119.596 145.184 133.855 1.00 24.90 ?  206 LEU B CG    1 
ATOM   7227  C  CD1   . LEU B 1 206 ? 120.509 143.972 133.934 1.00 20.27 ?  206 LEU B CD1   1 
ATOM   7228  C  CD2   . LEU B 1 206 ? 120.204 146.261 132.972 1.00 27.59 ?  206 LEU B CD2   1 
ATOM   7229  N  N     . ARG B 1 207 ? 115.530 145.382 131.498 1.00 25.66 ?  207 ARG B N     1 
ATOM   7230  C  CA    . ARG B 1 207 ? 114.283 144.825 131.000 1.00 19.38 ?  207 ARG B CA    1 
ATOM   7231  C  C     . ARG B 1 207 ? 114.339 143.303 131.006 1.00 27.98 ?  207 ARG B C     1 
ATOM   7232  O  O     . ARG B 1 207 ? 115.408 142.694 130.921 1.00 32.11 ?  207 ARG B O     1 
ATOM   7233  C  CB    . ARG B 1 207 ? 113.981 145.342 129.593 1.00 22.23 ?  207 ARG B CB    1 
ATOM   7234  C  CG    . ARG B 1 207 ? 115.165 145.375 128.656 1.00 24.60 ?  207 ARG B CG    1 
ATOM   7235  C  CD    . ARG B 1 207 ? 114.819 146.151 127.400 1.00 25.09 ?  207 ARG B CD    1 
ATOM   7236  N  NE    . ARG B 1 207 ? 115.236 147.544 127.502 1.00 28.91 ?  207 ARG B NE    1 
ATOM   7237  C  CZ    . ARG B 1 207 ? 115.120 148.435 126.528 1.00 26.60 ?  207 ARG B CZ    1 
ATOM   7238  N  NH1   . ARG B 1 207 ? 114.612 148.109 125.351 1.00 30.50 1  207 ARG B NH1   1 
ATOM   7239  N  NH2   . ARG B 1 207 ? 115.524 149.683 126.740 1.00 18.12 ?  207 ARG B NH2   1 
ATOM   7240  N  N     . ALA B 1 208 ? 113.167 142.689 131.120 1.00 31.28 ?  208 ALA B N     1 
ATOM   7241  C  CA    . ALA B 1 208 ? 113.075 141.247 131.252 1.00 23.27 ?  208 ALA B CA    1 
ATOM   7242  C  C     . ALA B 1 208 ? 113.330 140.565 129.911 1.00 33.70 ?  208 ALA B C     1 
ATOM   7243  O  O     . ALA B 1 208 ? 113.335 141.191 128.849 1.00 30.69 ?  208 ALA B O     1 
ATOM   7244  C  CB    . ALA B 1 208 ? 111.709 140.848 131.807 1.00 26.67 ?  208 ALA B CB    1 
ATOM   7245  N  N     . LYS B 1 209 ? 113.554 139.255 129.976 1.00 33.56 ?  209 LYS B N     1 
ATOM   7246  C  CA    . LYS B 1 209 ? 113.759 138.472 128.768 1.00 25.82 ?  209 LYS B CA    1 
ATOM   7247  C  C     . LYS B 1 209 ? 112.543 138.574 127.858 1.00 34.11 ?  209 LYS B C     1 
ATOM   7248  O  O     . LYS B 1 209 ? 111.397 138.508 128.313 1.00 37.27 ?  209 LYS B O     1 
ATOM   7249  C  CB    . LYS B 1 209 ? 114.033 137.012 129.127 1.00 28.65 ?  209 LYS B CB    1 
ATOM   7250  C  CG    . LYS B 1 209 ? 114.510 136.163 127.963 1.00 31.19 ?  209 LYS B CG    1 
ATOM   7251  C  CD    . LYS B 1 209 ? 114.672 134.709 128.373 1.00 33.94 ?  209 LYS B CD    1 
ATOM   7252  C  CE    . LYS B 1 209 ? 113.337 134.088 128.752 1.00 34.85 ?  209 LYS B CE    1 
ATOM   7253  N  NZ    . LYS B 1 209 ? 113.508 132.791 129.463 1.00 36.81 1  209 LYS B NZ    1 
ATOM   7254  N  N     . GLY B 1 210 ? 112.796 138.735 126.564 1.00 35.76 ?  210 GLY B N     1 
ATOM   7255  C  CA    . GLY B 1 210 ? 111.728 138.857 125.597 1.00 33.53 ?  210 GLY B CA    1 
ATOM   7256  C  C     . GLY B 1 210 ? 111.207 140.257 125.381 1.00 38.74 ?  210 GLY B C     1 
ATOM   7257  O  O     . GLY B 1 210 ? 110.103 140.416 124.850 1.00 43.88 ?  210 GLY B O     1 
ATOM   7258  N  N     . GLU B 1 211 ? 111.959 141.277 125.776 1.00 38.62 ?  211 GLU B N     1 
ATOM   7259  C  CA    . GLU B 1 211 ? 111.562 142.657 125.549 1.00 34.86 ?  211 GLU B CA    1 
ATOM   7260  C  C     . GLU B 1 211 ? 112.224 143.194 124.284 1.00 37.44 ?  211 GLU B C     1 
ATOM   7261  O  O     . GLU B 1 211 ? 113.204 142.641 123.780 1.00 37.18 ?  211 GLU B O     1 
ATOM   7262  C  CB    . GLU B 1 211 ? 111.924 143.528 126.753 1.00 33.52 ?  211 GLU B CB    1 
ATOM   7263  C  CG    . GLU B 1 211 ? 111.088 143.236 127.989 1.00 32.28 ?  211 GLU B CG    1 
ATOM   7264  C  CD    . GLU B 1 211 ? 110.713 144.489 128.754 1.00 36.70 ?  211 GLU B CD    1 
ATOM   7265  O  OE1   . GLU B 1 211 ? 109.879 145.268 128.248 1.00 38.81 ?  211 GLU B OE1   1 
ATOM   7266  O  OE2   . GLU B 1 211 ? 111.243 144.693 129.865 1.00 36.04 -1 211 GLU B OE2   1 
ATOM   7267  N  N     . ALA B 1 212 ? 111.669 144.286 123.770 1.00 39.59 ?  212 ALA B N     1 
ATOM   7268  C  CA    . ALA B 1 212 ? 112.132 144.846 122.509 1.00 38.04 ?  212 ALA B CA    1 
ATOM   7269  C  C     . ALA B 1 212 ? 113.383 145.692 122.706 1.00 40.28 ?  212 ALA B C     1 
ATOM   7270  O  O     . ALA B 1 212 ? 113.507 146.429 123.689 1.00 44.48 ?  212 ALA B O     1 
ATOM   7271  C  CB    . ALA B 1 212 ? 111.032 145.690 121.864 1.00 39.13 ?  212 ALA B CB    1 
ATOM   7272  N  N     . ILE B 1 213 ? 114.313 145.577 121.763 1.00 39.02 ?  213 ILE B N     1 
ATOM   7273  C  CA    . ILE B 1 213 ? 115.513 146.407 121.714 1.00 40.56 ?  213 ILE B CA    1 
ATOM   7274  C  C     . ILE B 1 213 ? 115.398 147.253 120.453 1.00 40.90 ?  213 ILE B C     1 
ATOM   7275  O  O     . ILE B 1 213 ? 115.586 146.751 119.339 1.00 43.16 ?  213 ILE B O     1 
ATOM   7276  C  CB    . ILE B 1 213 ? 116.801 145.577 121.708 1.00 41.77 ?  213 ILE B CB    1 
ATOM   7277  C  CG1   . ILE B 1 213 ? 116.811 144.583 122.869 1.00 40.24 ?  213 ILE B CG1   1 
ATOM   7278  C  CG2   . ILE B 1 213 ? 118.019 146.486 121.772 1.00 34.80 ?  213 ILE B CG2   1 
ATOM   7279  C  CD1   . ILE B 1 213 ? 117.936 143.576 122.790 1.00 37.24 ?  213 ILE B CD1   1 
ATOM   7280  N  N     . LYS B 1 214 ? 115.097 148.540 120.618 1.00 45.52 ?  214 LYS B N     1 
ATOM   7281  C  CA    . LYS B 1 214 ? 114.921 149.451 119.489 1.00 45.86 ?  214 LYS B CA    1 
ATOM   7282  C  C     . LYS B 1 214 ? 113.783 148.976 118.583 1.00 50.52 ?  214 LYS B C     1 
ATOM   7283  O  O     . LYS B 1 214 ? 113.977 148.642 117.413 1.00 49.88 ?  214 LYS B O     1 
ATOM   7284  C  CB    . LYS B 1 214 ? 116.226 149.609 118.703 1.00 46.76 ?  214 LYS B CB    1 
ATOM   7285  C  CG    . LYS B 1 214 ? 117.052 150.816 119.109 1.00 48.27 ?  214 LYS B CG    1 
ATOM   7286  C  CD    . LYS B 1 214 ? 116.292 152.108 118.861 1.00 49.61 ?  214 LYS B CD    1 
ATOM   7287  C  CE    . LYS B 1 214 ? 116.905 153.272 119.625 1.00 50.11 ?  214 LYS B CE    1 
ATOM   7288  N  NZ    . LYS B 1 214 ? 116.113 153.635 120.831 1.00 47.74 1  214 LYS B NZ    1 
ATOM   7289  N  N     . ASP B 1 215 ? 112.586 148.928 119.166 1.00 51.04 ?  215 ASP B N     1 
ATOM   7290  C  CA    . ASP B 1 215 ? 111.340 148.584 118.480 1.00 52.23 ?  215 ASP B CA    1 
ATOM   7291  C  C     . ASP B 1 215 ? 111.413 147.253 117.736 1.00 54.27 ?  215 ASP B C     1 
ATOM   7292  O  O     . ASP B 1 215 ? 110.646 147.022 116.796 1.00 54.60 ?  215 ASP B O     1 
ATOM   7293  C  CB    . ASP B 1 215 ? 110.887 149.717 117.539 1.00 55.74 ?  215 ASP B CB    1 
ATOM   7294  C  CG    . ASP B 1 215 ? 111.741 149.842 116.281 1.00 55.59 ?  215 ASP B CG    1 
ATOM   7295  O  OD1   . ASP B 1 215 ? 112.175 148.816 115.717 1.00 54.59 ?  215 ASP B OD1   1 
ATOM   7296  O  OD2   . ASP B 1 215 ? 111.980 150.990 115.852 1.00 54.52 -1 215 ASP B OD2   1 
ATOM   7297  N  N     . VAL B 1 216 ? 112.319 146.363 118.136 1.00 49.40 ?  216 VAL B N     1 
ATOM   7298  C  CA    . VAL B 1 216 ? 112.348 144.989 117.644 1.00 48.34 ?  216 VAL B CA    1 
ATOM   7299  C  C     . VAL B 1 216 ? 112.056 144.080 118.831 1.00 49.42 ?  216 VAL B C     1 
ATOM   7300  O  O     . VAL B 1 216 ? 112.784 144.097 119.831 1.00 50.00 ?  216 VAL B O     1 
ATOM   7301  C  CB    . VAL B 1 216 ? 113.689 144.640 116.975 1.00 48.97 ?  216 VAL B CB    1 
ATOM   7302  C  CG1   . VAL B 1 216 ? 114.149 145.786 116.089 1.00 48.25 ?  216 VAL B CG1   1 
ATOM   7303  C  CG2   . VAL B 1 216 ? 114.753 144.305 118.005 1.00 49.10 ?  216 VAL B CG2   1 
ATOM   7304  N  N     . GLU B 1 217 ? 110.984 143.302 118.727 1.00 51.48 ?  217 GLU B N     1 
ATOM   7305  C  CA    . GLU B 1 217 ? 110.463 142.574 119.874 1.00 51.06 ?  217 GLU B CA    1 
ATOM   7306  C  C     . GLU B 1 217 ? 111.271 141.311 120.146 1.00 48.90 ?  217 GLU B C     1 
ATOM   7307  O  O     . GLU B 1 217 ? 111.913 140.752 119.255 1.00 50.27 ?  217 GLU B O     1 
ATOM   7308  C  CB    . GLU B 1 217 ? 108.994 142.213 119.650 1.00 51.21 ?  217 GLU B CB    1 
ATOM   7309  C  CG    . GLU B 1 217 ? 108.064 143.415 119.589 1.00 50.36 ?  217 GLU B CG    1 
ATOM   7310  C  CD    . GLU B 1 217 ? 107.955 144.139 120.917 1.00 56.79 ?  217 GLU B CD    1 
ATOM   7311  O  OE1   . GLU B 1 217 ? 107.918 143.462 121.967 1.00 54.40 ?  217 GLU B OE1   1 
ATOM   7312  O  OE2   . GLU B 1 217 ? 107.907 145.387 120.911 1.00 54.39 -1 217 GLU B OE2   1 
ATOM   7313  N  N     . ASN B 1 218 ? 111.231 140.867 121.403 1.00 45.04 ?  218 ASN B N     1 
ATOM   7314  C  CA    . ASN B 1 218 ? 111.836 139.601 121.822 1.00 45.44 ?  218 ASN B CA    1 
ATOM   7315  C  C     . ASN B 1 218 ? 113.354 139.603 121.670 1.00 47.53 ?  218 ASN B C     1 
ATOM   7316  O  O     . ASN B 1 218 ? 113.976 138.544 121.557 1.00 48.65 ?  218 ASN B O     1 
ATOM   7317  C  CB    . ASN B 1 218 ? 111.232 138.424 121.055 1.00 45.49 ?  218 ASN B CB    1 
ATOM   7318  C  CG    . ASN B 1 218 ? 110.057 137.802 121.777 1.00 47.79 ?  218 ASN B CG    1 
ATOM   7319  O  OD1   . ASN B 1 218 ? 110.150 136.689 122.289 1.00 49.57 ?  218 ASN B OD1   1 
ATOM   7320  N  ND2   . ASN B 1 218 ? 108.943 138.522 121.821 1.00 49.63 ?  218 ASN B ND2   1 
ATOM   7321  N  N     . ALA B 1 219 ? 113.967 140.783 121.672 1.00 38.24 ?  219 ALA B N     1 
ATOM   7322  C  CA    . ALA B 1 219 ? 115.404 140.883 121.451 1.00 36.45 ?  219 ALA B CA    1 
ATOM   7323  C  C     . ALA B 1 219 ? 116.218 140.787 122.735 1.00 35.16 ?  219 ALA B C     1 
ATOM   7324  O  O     . ALA B 1 219 ? 117.404 140.445 122.680 1.00 35.39 ?  219 ALA B O     1 
ATOM   7325  C  CB    . ALA B 1 219 ? 115.734 142.195 120.735 1.00 37.36 ?  219 ALA B CB    1 
ATOM   7326  N  N     . THR B 1 220 ? 115.613 141.070 123.884 1.00 37.12 ?  220 THR B N     1 
ATOM   7327  C  CA    . THR B 1 220 ? 116.354 141.148 125.135 1.00 30.59 ?  220 THR B CA    1 
ATOM   7328  C  C     . THR B 1 220 ? 116.608 139.763 125.716 1.00 34.79 ?  220 THR B C     1 
ATOM   7329  O  O     . THR B 1 220 ? 115.739 138.887 125.683 1.00 38.67 ?  220 THR B O     1 
ATOM   7330  C  CB    . THR B 1 220 ? 115.595 142.002 126.150 1.00 30.57 ?  220 THR B CB    1 
ATOM   7331  O  OG1   . THR B 1 220 ? 115.290 143.275 125.570 1.00 34.91 ?  220 THR B OG1   1 
ATOM   7332  C  CG2   . THR B 1 220 ? 116.435 142.212 127.397 1.00 36.69 ?  220 THR B CG2   1 
ATOM   7333  N  N     . LYS B 1 221 ? 117.812 139.573 126.255 1.00 32.64 ?  221 LYS B N     1 
ATOM   7334  C  CA    . LYS B 1 221 ? 118.174 138.342 126.944 1.00 28.15 ?  221 LYS B CA    1 
ATOM   7335  C  C     . LYS B 1 221 ? 117.743 138.328 128.404 1.00 30.28 ?  221 LYS B C     1 
ATOM   7336  O  O     . LYS B 1 221 ? 117.773 137.265 129.031 1.00 32.61 ?  221 LYS B O     1 
ATOM   7337  C  CB    . LYS B 1 221 ? 119.688 138.111 126.862 1.00 33.82 ?  221 LYS B CB    1 
ATOM   7338  C  CG    . LYS B 1 221 ? 120.246 138.178 125.453 1.00 31.64 ?  221 LYS B CG    1 
ATOM   7339  C  CD    . LYS B 1 221 ? 120.807 136.834 125.021 1.00 30.57 ?  221 LYS B CD    1 
ATOM   7340  C  CE    . LYS B 1 221 ? 121.242 136.862 123.566 1.00 34.30 ?  221 LYS B CE    1 
ATOM   7341  N  NZ    . LYS B 1 221 ? 122.714 136.719 123.424 1.00 36.68 1  221 LYS B NZ    1 
ATOM   7342  N  N     . GLY B 1 222 ? 117.344 139.469 128.953 1.00 32.19 ?  222 GLY B N     1 
ATOM   7343  C  CA    . GLY B 1 222 ? 116.929 139.537 130.335 1.00 30.14 ?  222 GLY B CA    1 
ATOM   7344  C  C     . GLY B 1 222 ? 118.099 139.661 131.292 1.00 29.34 ?  222 GLY B C     1 
ATOM   7345  O  O     . GLY B 1 222 ? 119.260 139.826 130.906 1.00 31.42 ?  222 GLY B O     1 
ATOM   7346  N  N     . VAL B 1 223 ? 117.771 139.570 132.584 1.00 26.63 ?  223 VAL B N     1 
ATOM   7347  C  CA    . VAL B 1 223 ? 118.782 139.738 133.618 1.00 25.95 ?  223 VAL B CA    1 
ATOM   7348  C  C     . VAL B 1 223 ? 119.724 138.545 133.702 1.00 23.61 ?  223 VAL B C     1 
ATOM   7349  O  O     . VAL B 1 223 ? 120.810 138.668 134.272 1.00 27.64 ?  223 VAL B O     1 
ATOM   7350  C  CB    . VAL B 1 223 ? 118.129 139.996 134.990 1.00 27.02 ?  223 VAL B CB    1 
ATOM   7351  C  CG1   . VAL B 1 223 ? 117.081 141.091 134.885 1.00 19.80 ?  223 VAL B CG1   1 
ATOM   7352  C  CG2   . VAL B 1 223 ? 117.527 138.715 135.547 1.00 26.00 ?  223 VAL B CG2   1 
ATOM   7353  N  N     . VAL B 1 224 ? 119.344 137.389 133.156 1.00 25.89 ?  224 VAL B N     1 
ATOM   7354  C  CA    . VAL B 1 224 ? 120.206 136.214 133.260 1.00 25.77 ?  224 VAL B CA    1 
ATOM   7355  C  C     . VAL B 1 224 ? 121.434 136.335 132.360 1.00 27.73 ?  224 VAL B C     1 
ATOM   7356  O  O     . VAL B 1 224 ? 122.523 135.883 132.730 1.00 32.00 ?  224 VAL B O     1 
ATOM   7357  C  CB    . VAL B 1 224 ? 119.413 134.934 132.954 1.00 30.66 ?  224 VAL B CB    1 
ATOM   7358  C  CG1   . VAL B 1 224 ? 120.346 133.739 132.890 1.00 27.16 ?  224 VAL B CG1   1 
ATOM   7359  C  CG2   . VAL B 1 224 ? 118.342 134.716 134.009 1.00 26.16 ?  224 VAL B CG2   1 
ATOM   7360  N  N     . GLY B 1 225 ? 121.295 136.927 131.173 1.00 26.17 ?  225 GLY B N     1 
ATOM   7361  C  CA    . GLY B 1 225 ? 122.464 137.150 130.337 1.00 24.61 ?  225 GLY B CA    1 
ATOM   7362  C  C     . GLY B 1 225 ? 123.448 138.117 130.970 1.00 25.16 ?  225 GLY B C     1 
ATOM   7363  O  O     . GLY B 1 225 ? 124.662 137.882 130.966 1.00 32.16 ?  225 GLY B O     1 
ATOM   7364  N  N     . VAL B 1 226 ? 122.936 139.214 131.530 1.00 22.20 ?  226 VAL B N     1 
ATOM   7365  C  CA    . VAL B 1 226 ? 123.792 140.138 132.264 1.00 24.32 ?  226 VAL B CA    1 
ATOM   7366  C  C     . VAL B 1 226 ? 124.396 139.447 133.475 1.00 22.22 ?  226 VAL B C     1 
ATOM   7367  O  O     . VAL B 1 226 ? 125.528 139.743 133.868 1.00 24.90 ?  226 VAL B O     1 
ATOM   7368  C  CB    . VAL B 1 226 ? 123.001 141.398 132.664 1.00 25.42 ?  226 VAL B CB    1 
ATOM   7369  C  CG1   . VAL B 1 226 ? 123.878 142.339 133.473 1.00 23.80 ?  226 VAL B CG1   1 
ATOM   7370  C  CG2   . VAL B 1 226 ? 122.458 142.093 131.429 1.00 20.09 ?  226 VAL B CG2   1 
ATOM   7371  N  N     . MET B 1 227 ? 123.654 138.523 134.089 1.00 23.79 ?  227 MET B N     1 
ATOM   7372  C  CA    . MET B 1 227 ? 124.183 137.775 135.222 1.00 22.66 ?  227 MET B CA    1 
ATOM   7373  C  C     . MET B 1 227 ? 125.353 136.898 134.803 1.00 23.46 ?  227 MET B C     1 
ATOM   7374  O  O     . MET B 1 227 ? 126.342 136.786 135.530 1.00 27.26 ?  227 MET B O     1 
ATOM   7375  C  CB    . MET B 1 227 ? 123.081 136.924 135.850 1.00 20.00 ?  227 MET B CB    1 
ATOM   7376  C  CG    . MET B 1 227 ? 122.237 137.648 136.878 1.00 20.10 ?  227 MET B CG    1 
ATOM   7377  S  SD    . MET B 1 227 ? 120.853 136.640 137.438 1.00 37.71 ?  227 MET B SD    1 
ATOM   7378  C  CE    . MET B 1 227 ? 121.617 135.749 138.790 1.00 25.15 ?  227 MET B CE    1 
ATOM   7379  N  N     . LYS B 1 228 ? 125.250 136.251 133.642 1.00 26.29 ?  228 LYS B N     1 
ATOM   7380  C  CA    . LYS B 1 228 ? 126.370 135.462 133.137 1.00 24.72 ?  228 LYS B CA    1 
ATOM   7381  C  C     . LYS B 1 228 ? 127.570 136.350 132.839 1.00 23.89 ?  228 LYS B C     1 
ATOM   7382  O  O     . LYS B 1 228 ? 128.713 136.004 133.173 1.00 28.24 ?  228 LYS B O     1 
ATOM   7383  C  CB    . LYS B 1 228 ? 125.952 134.690 131.886 1.00 27.55 ?  228 LYS B CB    1 
ATOM   7384  C  CG    . LYS B 1 228 ? 124.803 133.723 132.098 1.00 29.63 ?  228 LYS B CG    1 
ATOM   7385  C  CD    . LYS B 1 228 ? 124.578 132.863 130.866 1.00 32.87 ?  228 LYS B CD    1 
ATOM   7386  C  CE    . LYS B 1 228 ? 123.101 132.742 130.532 1.00 34.75 ?  228 LYS B CE    1 
ATOM   7387  N  NZ    . LYS B 1 228 ? 122.678 133.724 129.496 1.00 32.61 1  228 LYS B NZ    1 
ATOM   7388  N  N     . LEU B 1 229 ? 127.327 137.503 132.212 1.00 22.85 ?  229 LEU B N     1 
ATOM   7389  C  CA    . LEU B 1 229 ? 128.406 138.456 131.973 1.00 23.92 ?  229 LEU B CA    1 
ATOM   7390  C  C     . LEU B 1 229 ? 129.095 138.835 133.278 1.00 20.23 ?  229 LEU B C     1 
ATOM   7391  O  O     . LEU B 1 229 ? 130.326 138.804 133.379 1.00 21.32 ?  229 LEU B O     1 
ATOM   7392  C  CB    . LEU B 1 229 ? 127.861 139.704 131.276 1.00 24.19 ?  229 LEU B CB    1 
ATOM   7393  C  CG    . LEU B 1 229 ? 127.637 139.653 129.765 1.00 21.86 ?  229 LEU B CG    1 
ATOM   7394  C  CD1   . LEU B 1 229 ? 126.734 140.796 129.335 1.00 25.03 ?  229 LEU B CD1   1 
ATOM   7395  C  CD2   . LEU B 1 229 ? 128.961 139.706 129.025 1.00 22.53 ?  229 LEU B CD2   1 
ATOM   7396  N  N     . LEU B 1 230 ? 128.307 139.194 134.293 1.00 24.38 ?  230 LEU B N     1 
ATOM   7397  C  CA    . LEU B 1 230 ? 128.863 139.627 135.570 1.00 19.42 ?  230 LEU B CA    1 
ATOM   7398  C  C     . LEU B 1 230 ? 129.589 138.492 136.277 1.00 14.02 ?  230 LEU B C     1 
ATOM   7399  O  O     . LEU B 1 230 ? 130.623 138.714 136.913 1.00 22.06 ?  230 LEU B O     1 
ATOM   7400  C  CB    . LEU B 1 230 ? 127.753 140.186 136.460 1.00 21.31 ?  230 LEU B CB    1 
ATOM   7401  C  CG    . LEU B 1 230 ? 127.172 141.536 136.045 1.00 24.40 ?  230 LEU B CG    1 
ATOM   7402  C  CD1   . LEU B 1 230 ? 125.914 141.840 136.841 1.00 26.46 ?  230 LEU B CD1   1 
ATOM   7403  C  CD2   . LEU B 1 230 ? 128.204 142.636 136.220 1.00 24.91 ?  230 LEU B CD2   1 
ATOM   7404  N  N     . ASP B 1 231 ? 129.054 137.274 136.200 1.00 25.52 ?  231 ASP B N     1 
ATOM   7405  C  CA    . ASP B 1 231 ? 129.711 136.136 136.827 1.00 27.18 ?  231 ASP B CA    1 
ATOM   7406  C  C     . ASP B 1 231 ? 131.074 135.883 136.199 1.00 27.18 ?  231 ASP B C     1 
ATOM   7407  O  O     . ASP B 1 231 ? 132.061 135.654 136.908 1.00 30.55 ?  231 ASP B O     1 
ATOM   7408  C  CB    . ASP B 1 231 ? 128.824 134.896 136.719 1.00 24.21 ?  231 ASP B CB    1 
ATOM   7409  C  CG    . ASP B 1 231 ? 129.524 133.636 137.176 1.00 39.00 ?  231 ASP B CG    1 
ATOM   7410  O  OD1   . ASP B 1 231 ? 129.855 133.539 138.376 1.00 41.43 ?  231 ASP B OD1   1 
ATOM   7411  O  OD2   . ASP B 1 231 ? 129.744 132.738 136.336 1.00 39.34 -1 231 ASP B OD2   1 
ATOM   7412  N  N     . ASN B 1 232 ? 131.155 135.941 134.868 1.00 31.93 ?  232 ASN B N     1 
ATOM   7413  C  CA    . ASN B 1 232 ? 132.452 135.786 134.221 1.00 28.68 ?  232 ASN B CA    1 
ATOM   7414  C  C     . ASN B 1 232 ? 133.387 136.942 134.564 1.00 25.71 ?  232 ASN B C     1 
ATOM   7415  O  O     . ASN B 1 232 ? 134.594 136.740 134.732 1.00 32.51 ?  232 ASN B O     1 
ATOM   7416  C  CB    . ASN B 1 232 ? 132.283 135.655 132.711 1.00 27.96 ?  232 ASN B CB    1 
ATOM   7417  C  CG    . ASN B 1 232 ? 133.210 134.618 132.117 1.00 32.58 ?  232 ASN B CG    1 
ATOM   7418  O  OD1   . ASN B 1 232 ? 134.431 134.756 132.176 1.00 34.93 ?  232 ASN B OD1   1 
ATOM   7419  N  ND2   . ASN B 1 232 ? 132.636 133.560 131.563 1.00 32.70 ?  232 ASN B ND2   1 
ATOM   7420  N  N     . ALA B 1 233 ? 132.851 138.160 134.661 1.00 20.16 ?  233 ALA B N     1 
ATOM   7421  C  CA    . ALA B 1 233 ? 133.686 139.305 135.009 1.00 20.33 ?  233 ALA B CA    1 
ATOM   7422  C  C     . ALA B 1 233 ? 134.263 139.161 136.413 1.00 25.62 ?  233 ALA B C     1 
ATOM   7423  O  O     . ALA B 1 233 ? 135.433 139.481 136.648 1.00 28.47 ?  233 ALA B O     1 
ATOM   7424  C  CB    . ALA B 1 233 ? 132.880 140.598 134.887 1.00 22.81 ?  233 ALA B CB    1 
ATOM   7425  N  N     . PHE B 1 234 ? 133.451 138.691 137.359 1.00 27.71 ?  234 PHE B N     1 
ATOM   7426  C  CA    . PHE B 1 234 ? 133.931 138.488 138.722 1.00 21.60 ?  234 PHE B CA    1 
ATOM   7427  C  C     . PHE B 1 234 ? 134.919 137.331 138.792 1.00 21.70 ?  234 PHE B C     1 
ATOM   7428  O  O     . PHE B 1 234 ? 135.892 137.387 139.551 1.00 30.60 ?  234 PHE B O     1 
ATOM   7429  C  CB    . PHE B 1 234 ? 132.753 138.249 139.666 1.00 20.77 ?  234 PHE B CB    1 
ATOM   7430  C  CG    . PHE B 1 234 ? 132.016 139.500 140.042 1.00 19.39 ?  234 PHE B CG    1 
ATOM   7431  C  CD1   . PHE B 1 234 ? 132.663 140.530 140.705 1.00 17.65 ?  234 PHE B CD1   1 
ATOM   7432  C  CD2   . PHE B 1 234 ? 130.675 139.649 139.734 1.00 21.24 ?  234 PHE B CD2   1 
ATOM   7433  C  CE1   . PHE B 1 234 ? 131.987 141.682 141.050 1.00 20.10 ?  234 PHE B CE1   1 
ATOM   7434  C  CE2   . PHE B 1 234 ? 129.995 140.799 140.075 1.00 22.40 ?  234 PHE B CE2   1 
ATOM   7435  C  CZ    . PHE B 1 234 ? 130.651 141.817 140.737 1.00 25.70 ?  234 PHE B CZ    1 
ATOM   7436  N  N     . ARG B 1 235 ? 134.684 136.274 138.013 1.00 31.13 ?  235 ARG B N     1 
ATOM   7437  C  CA    . ARG B 1 235 ? 135.631 135.166 137.981 1.00 26.11 ?  235 ARG B CA    1 
ATOM   7438  C  C     . ARG B 1 235 ? 136.974 135.607 137.416 1.00 29.72 ?  235 ARG B C     1 
ATOM   7439  O  O     . ARG B 1 235 ? 138.028 135.175 137.896 1.00 38.28 ?  235 ARG B O     1 
ATOM   7440  C  CB    . ARG B 1 235 ? 135.053 134.007 137.171 1.00 27.82 ?  235 ARG B CB    1 
ATOM   7441  C  CG    . ARG B 1 235 ? 134.546 132.855 138.022 1.00 35.95 ?  235 ARG B CG    1 
ATOM   7442  C  CD    . ARG B 1 235 ? 134.094 131.679 137.169 1.00 35.98 ?  235 ARG B CD    1 
ATOM   7443  N  NE    . ARG B 1 235 ? 132.865 131.970 136.443 1.00 36.53 ?  235 ARG B NE    1 
ATOM   7444  C  CZ    . ARG B 1 235 ? 132.814 132.311 135.162 1.00 38.45 ?  235 ARG B CZ    1 
ATOM   7445  N  NH1   . ARG B 1 235 ? 133.912 132.415 134.431 1.00 39.29 1  235 ARG B NH1   1 
ATOM   7446  N  NH2   . ARG B 1 235 ? 131.633 132.553 134.601 1.00 33.61 ?  235 ARG B NH2   1 
ATOM   7447  N  N     . TYR B 1 236 ? 136.959 136.467 136.396 1.00 30.26 ?  236 TYR B N     1 
ATOM   7448  C  CA    . TYR B 1 236 ? 138.207 136.952 135.818 1.00 27.97 ?  236 TYR B CA    1 
ATOM   7449  C  C     . TYR B 1 236 ? 138.962 137.836 136.802 1.00 27.48 ?  236 TYR B C     1 
ATOM   7450  O  O     . TYR B 1 236 ? 140.166 137.656 137.017 1.00 31.32 ?  236 TYR B O     1 
ATOM   7451  C  CB    . TYR B 1 236 ? 137.925 137.716 134.525 1.00 25.91 ?  236 TYR B CB    1 
ATOM   7452  C  CG    . TYR B 1 236 ? 139.164 138.291 133.883 1.00 28.92 ?  236 TYR B CG    1 
ATOM   7453  C  CD1   . TYR B 1 236 ? 140.016 137.491 133.136 1.00 22.51 ?  236 TYR B CD1   1 
ATOM   7454  C  CD2   . TYR B 1 236 ? 139.490 139.632 134.036 1.00 28.56 ?  236 TYR B CD2   1 
ATOM   7455  C  CE1   . TYR B 1 236 ? 141.150 138.010 132.551 1.00 23.34 ?  236 TYR B CE1   1 
ATOM   7456  C  CE2   . TYR B 1 236 ? 140.624 140.159 133.456 1.00 26.36 ?  236 TYR B CE2   1 
ATOM   7457  C  CZ    . TYR B 1 236 ? 141.450 139.345 132.714 1.00 25.39 ?  236 TYR B CZ    1 
ATOM   7458  O  OH    . TYR B 1 236 ? 142.580 139.864 132.133 1.00 31.15 ?  236 TYR B OH    1 
ATOM   7459  N  N     . ALA B 1 237 ? 138.270 138.800 137.406 1.00 33.74 ?  237 ALA B N     1 
ATOM   7460  C  CA    . ALA B 1 237 ? 138.885 139.724 138.357 1.00 34.91 ?  237 ALA B CA    1 
ATOM   7461  C  C     . ALA B 1 237 ? 138.749 139.156 139.769 1.00 42.38 ?  237 ALA B C     1 
ATOM   7462  O  O     . ALA B 1 237 ? 138.073 139.701 140.643 1.00 43.99 ?  237 ALA B O     1 
ATOM   7463  C  CB    . ALA B 1 237 ? 138.257 141.106 138.238 1.00 34.25 ?  237 ALA B CB    1 
ATOM   7464  N  N     . ASP B 1 238 ? 139.424 138.026 139.981 1.00 58.69 ?  238 ASP B N     1 
ATOM   7465  C  CA    . ASP B 1 238 ? 139.348 137.287 141.233 1.00 58.72 ?  238 ASP B CA    1 
ATOM   7466  C  C     . ASP B 1 238 ? 140.472 137.665 142.191 1.00 63.19 ?  238 ASP B C     1 
ATOM   7467  O  O     . ASP B 1 238 ? 140.938 136.824 142.966 1.00 64.11 ?  238 ASP B O     1 
ATOM   7468  C  CB    . ASP B 1 238 ? 139.358 135.782 140.969 1.00 58.39 ?  238 ASP B CB    1 
ATOM   7469  C  CG    . ASP B 1 238 ? 140.713 135.279 140.512 1.00 63.63 ?  238 ASP B CG    1 
ATOM   7470  O  OD1   . ASP B 1 238 ? 141.515 136.095 140.012 1.00 62.41 ?  238 ASP B OD1   1 
ATOM   7471  O  OD2   . ASP B 1 238 ? 140.978 134.067 140.658 1.00 62.74 -1 238 ASP B OD2   1 
ATOM   7472  N  N     . GLN B 1 239 ? 140.932 138.914 142.135 1.00 70.72 ?  239 GLN B N     1 
ATOM   7473  C  CA    . GLN B 1 239 ? 141.927 139.422 143.075 1.00 72.43 ?  239 GLN B CA    1 
ATOM   7474  C  C     . GLN B 1 239 ? 143.243 138.656 142.952 1.00 74.48 ?  239 GLN B C     1 
ATOM   7475  O  O     . GLN B 1 239 ? 143.825 138.205 143.941 1.00 73.10 ?  239 GLN B O     1 
ATOM   7476  C  CB    . GLN B 1 239 ? 141.396 139.370 144.508 1.00 71.23 ?  239 GLN B CB    1 
ATOM   7477  C  CG    . GLN B 1 239 ? 140.048 140.040 144.690 1.00 69.76 ?  239 GLN B CG    1 
ATOM   7478  C  CD    . GLN B 1 239 ? 139.422 139.727 146.032 1.00 71.81 ?  239 GLN B CD    1 
ATOM   7479  O  OE1   . GLN B 1 239 ? 140.112 139.653 147.049 1.00 72.08 ?  239 GLN B OE1   1 
ATOM   7480  N  NE2   . GLN B 1 239 ? 138.107 139.542 146.046 1.00 69.75 ?  239 GLN B NE2   1 
ATOM   7481  N  N     . MET B 1 240 ? 143.711 138.507 141.713 1.00 81.51 ?  240 MET B N     1 
ATOM   7482  C  CA    . MET B 1 240 ? 144.992 137.864 141.434 1.00 81.02 ?  240 MET B CA    1 
ATOM   7483  C  C     . MET B 1 240 ? 145.033 136.432 141.963 1.00 81.75 ?  240 MET B C     1 
ATOM   7484  O  O     . MET B 1 240 ? 146.109 135.877 142.201 1.00 81.47 ?  240 MET B O     1 
ATOM   7485  C  CB    . MET B 1 240 ? 146.149 138.681 142.013 1.00 79.98 ?  240 MET B CB    1 
ATOM   7486  C  CG    . MET B 1 240 ? 146.083 140.162 141.672 1.00 80.89 ?  240 MET B CG    1 
ATOM   7487  S  SD    . MET B 1 240 ? 147.694 140.965 141.664 1.00 87.62 ?  240 MET B SD    1 
ATOM   7488  C  CE    . MET B 1 240 ? 147.214 142.689 141.716 1.00 80.18 ?  240 MET B CE    1 
ATOM   7489  N  N     . GLY B 1 241 ? 143.863 135.827 142.152 1.00 79.74 ?  241 GLY B N     1 
ATOM   7490  C  CA    . GLY B 1 241 ? 143.766 134.468 142.641 1.00 79.44 ?  241 GLY B CA    1 
ATOM   7491  C  C     . GLY B 1 241 ? 143.857 134.313 144.143 1.00 81.57 ?  241 GLY B C     1 
ATOM   7492  O  O     . GLY B 1 241 ? 143.599 133.214 144.649 1.00 81.23 ?  241 GLY B O     1 
ATOM   7493  N  N     . GLN B 1 242 ? 144.215 135.371 144.873 1.00 86.15 ?  242 GLN B N     1 
ATOM   7494  C  CA    . GLN B 1 242 ? 144.303 135.281 146.325 1.00 85.28 ?  242 GLN B CA    1 
ATOM   7495  C  C     . GLN B 1 242 ? 142.928 135.219 146.978 1.00 87.22 ?  242 GLN B C     1 
ATOM   7496  O  O     . GLN B 1 242 ? 142.806 134.750 148.115 1.00 87.40 ?  242 GLN B O     1 
ATOM   7497  C  CB    . GLN B 1 242 ? 145.095 136.467 146.877 1.00 85.00 ?  242 GLN B CB    1 
ATOM   7498  C  CG    . GLN B 1 242 ? 146.538 136.521 146.399 1.00 87.21 ?  242 GLN B CG    1 
ATOM   7499  C  CD    . GLN B 1 242 ? 147.408 137.416 147.259 1.00 87.25 ?  242 GLN B CD    1 
ATOM   7500  O  OE1   . GLN B 1 242 ? 147.018 137.812 148.358 1.00 87.19 ?  242 GLN B OE1   1 
ATOM   7501  N  NE2   . GLN B 1 242 ? 148.597 137.741 146.762 1.00 85.90 ?  242 GLN B NE2   1 
ATOM   7502  N  N     . ARG B 1 243 ? 141.892 135.682 146.281 1.00 77.44 ?  243 ARG B N     1 
ATOM   7503  C  CA    . ARG B 1 243 ? 140.528 135.641 146.796 1.00 76.61 ?  243 ARG B CA    1 
ATOM   7504  C  C     . ARG B 1 243 ? 139.576 135.773 145.619 1.00 76.25 ?  243 ARG B C     1 
ATOM   7505  O  O     . ARG B 1 243 ? 139.530 136.829 144.981 1.00 74.78 ?  243 ARG B O     1 
ATOM   7506  C  CB    . ARG B 1 243 ? 140.288 136.756 147.816 1.00 75.91 ?  243 ARG B CB    1 
ATOM   7507  C  CG    . ARG B 1 243 ? 138.827 137.141 147.994 1.00 76.87 ?  243 ARG B CG    1 
ATOM   7508  C  CD    . ARG B 1 243 ? 138.599 137.835 149.328 1.00 77.01 ?  243 ARG B CD    1 
ATOM   7509  N  NE    . ARG B 1 243 ? 137.197 137.819 149.728 1.00 77.32 ?  243 ARG B NE    1 
ATOM   7510  C  CZ    . ARG B 1 243 ? 136.707 138.481 150.767 1.00 77.17 ?  243 ARG B CZ    1 
ATOM   7511  N  NH1   . ARG B 1 243 ? 137.481 139.222 151.542 1.00 74.45 1  243 ARG B NH1   1 
ATOM   7512  N  NH2   . ARG B 1 243 ? 135.407 138.396 151.036 1.00 77.42 ?  243 ARG B NH2   1 
ATOM   7513  N  N     . GLN B 1 244 ? 138.810 134.719 145.348 1.00 70.00 ?  244 GLN B N     1 
ATOM   7514  C  CA    . GLN B 1 244 ? 137.938 134.715 144.182 1.00 69.77 ?  244 GLN B CA    1 
ATOM   7515  C  C     . GLN B 1 244 ? 136.996 135.911 144.211 1.00 68.45 ?  244 GLN B C     1 
ATOM   7516  O  O     . GLN B 1 244 ? 136.422 136.247 145.250 1.00 67.65 ?  244 GLN B O     1 
ATOM   7517  C  CB    . GLN B 1 244 ? 137.134 133.415 144.124 1.00 68.17 ?  244 GLN B CB    1 
ATOM   7518  C  CG    . GLN B 1 244 ? 137.962 132.180 143.811 1.00 69.96 ?  244 GLN B CG    1 
ATOM   7519  C  CD    . GLN B 1 244 ? 137.116 130.925 143.699 1.00 69.44 ?  244 GLN B CD    1 
ATOM   7520  O  OE1   . GLN B 1 244 ? 136.201 130.707 144.492 1.00 67.64 ?  244 GLN B OE1   1 
ATOM   7521  N  NE2   . GLN B 1 244 ? 137.419 130.095 142.709 1.00 66.69 ?  244 GLN B NE2   1 
ATOM   7522  N  N     . GLY B 1 245 ? 136.843 136.558 143.058 1.00 51.71 ?  245 GLY B N     1 
ATOM   7523  C  CA    . GLY B 1 245 ? 135.948 137.691 142.946 1.00 49.76 ?  245 GLY B CA    1 
ATOM   7524  C  C     . GLY B 1 245 ? 134.532 137.335 143.344 1.00 48.89 ?  245 GLY B C     1 
ATOM   7525  O  O     . GLY B 1 245 ? 133.948 136.391 142.805 1.00 47.37 ?  245 GLY B O     1 
ATOM   7526  N  N     . SER B 1 246 ? 133.970 138.083 144.290 1.00 36.53 ?  246 SER B N     1 
ATOM   7527  C  CA    . SER B 1 246 ? 132.639 137.818 144.816 1.00 32.75 ?  246 SER B CA    1 
ATOM   7528  C  C     . SER B 1 246 ? 131.725 138.987 144.490 1.00 31.52 ?  246 SER B C     1 
ATOM   7529  O  O     . SER B 1 246 ? 132.045 140.140 144.800 1.00 27.84 ?  246 SER B O     1 
ATOM   7530  C  CB    . SER B 1 246 ? 132.679 137.584 146.329 1.00 31.49 ?  246 SER B CB    1 
ATOM   7531  O  OG    . SER B 1 246 ? 133.273 136.334 146.633 1.00 37.44 ?  246 SER B OG    1 
ATOM   7532  N  N     . GLY B 1 247 ? 130.588 138.685 143.868 1.00 20.76 ?  247 GLY B N     1 
ATOM   7533  C  CA    . GLY B 1 247 ? 129.614 139.702 143.547 1.00 9.87  ?  247 GLY B CA    1 
ATOM   7534  C  C     . GLY B 1 247 ? 128.216 139.221 143.871 1.00 14.49 ?  247 GLY B C     1 
ATOM   7535  O  O     . GLY B 1 247 ? 127.948 138.021 143.956 1.00 23.22 ?  247 GLY B O     1 
ATOM   7536  N  N     . ALA B 1 248 ? 127.325 140.187 144.054 1.00 17.60 ?  248 ALA B N     1 
ATOM   7537  C  CA    . ALA B 1 248 ? 125.930 139.913 144.353 1.00 16.56 ?  248 ALA B CA    1 
ATOM   7538  C  C     . ALA B 1 248 ? 125.053 140.628 143.340 1.00 14.06 ?  248 ALA B C     1 
ATOM   7539  O  O     . ALA B 1 248 ? 125.348 141.755 142.934 1.00 18.30 ?  248 ALA B O     1 
ATOM   7540  C  CB    . ALA B 1 248 ? 125.564 140.358 145.774 1.00 8.53  ?  248 ALA B CB    1 
ATOM   7541  N  N     . ALA B 1 249 ? 123.980 139.963 142.927 1.00 16.63 ?  249 ALA B N     1 
ATOM   7542  C  CA    . ALA B 1 249 ? 122.987 140.541 142.034 1.00 15.22 ?  249 ALA B CA    1 
ATOM   7543  C  C     . ALA B 1 249 ? 121.649 140.564 142.752 1.00 9.37  ?  249 ALA B C     1 
ATOM   7544  O  O     . ALA B 1 249 ? 121.256 139.569 143.368 1.00 21.90 ?  249 ALA B O     1 
ATOM   7545  C  CB    . ALA B 1 249 ? 122.884 139.748 140.729 1.00 15.46 ?  249 ALA B CB    1 
ATOM   7546  N  N     . TYR B 1 250 ? 120.960 141.695 142.681 1.00 9.10  ?  250 TYR B N     1 
ATOM   7547  C  CA    . TYR B 1 250 ? 119.664 141.859 143.318 1.00 10.63 ?  250 TYR B CA    1 
ATOM   7548  C  C     . TYR B 1 250 ? 118.606 142.125 142.261 1.00 9.21  ?  250 TYR B C     1 
ATOM   7549  O  O     . TYR B 1 250 ? 118.826 142.902 141.328 1.00 14.17 ?  250 TYR B O     1 
ATOM   7550  C  CB    . TYR B 1 250 ? 119.684 143.000 144.339 1.00 4.32  ?  250 TYR B CB    1 
ATOM   7551  C  CG    . TYR B 1 250 ? 120.268 142.606 145.676 1.00 13.55 ?  250 TYR B CG    1 
ATOM   7552  C  CD1   . TYR B 1 250 ? 121.633 142.407 145.823 1.00 5.37  ?  250 TYR B CD1   1 
ATOM   7553  C  CD2   . TYR B 1 250 ? 119.456 142.434 146.786 1.00 11.37 ?  250 TYR B CD2   1 
ATOM   7554  C  CE1   . TYR B 1 250 ? 122.173 142.044 147.037 1.00 1.19  ?  250 TYR B CE1   1 
ATOM   7555  C  CE2   . TYR B 1 250 ? 119.988 142.070 148.006 1.00 6.52  ?  250 TYR B CE2   1 
ATOM   7556  C  CZ    . TYR B 1 250 ? 121.346 141.878 148.126 1.00 6.94  ?  250 TYR B CZ    1 
ATOM   7557  O  OH    . TYR B 1 250 ? 121.882 141.519 149.339 1.00 12.71 ?  250 TYR B OH    1 
ATOM   7558  N  N     . LEU B 1 251 ? 117.463 141.466 142.407 1.00 12.70 ?  251 LEU B N     1 
ATOM   7559  C  CA    . LEU B 1 251 ? 116.338 141.650 141.508 1.00 14.35 ?  251 LEU B CA    1 
ATOM   7560  C  C     . LEU B 1 251 ? 115.072 141.796 142.332 1.00 7.35  ?  251 LEU B C     1 
ATOM   7561  O  O     . LEU B 1 251 ? 114.838 141.017 143.260 1.00 18.98 ?  251 LEU B O     1 
ATOM   7562  C  CB    . LEU B 1 251 ? 116.206 140.477 140.532 1.00 16.46 ?  251 LEU B CB    1 
ATOM   7563  C  CG    . LEU B 1 251 ? 115.389 140.768 139.273 1.00 14.88 ?  251 LEU B CG    1 
ATOM   7564  C  CD1   . LEU B 1 251 ? 116.170 141.669 138.329 1.00 11.96 ?  251 LEU B CD1   1 
ATOM   7565  C  CD2   . LEU B 1 251 ? 114.983 139.478 138.586 1.00 11.94 ?  251 LEU B CD2   1 
ATOM   7566  N  N     . ASN B 1 252 ? 114.264 142.798 142.000 1.00 19.74 ?  252 ASN B N     1 
ATOM   7567  C  CA    . ASN B 1 252 ? 112.974 142.946 142.650 1.00 15.62 ?  252 ASN B CA    1 
ATOM   7568  C  C     . ASN B 1 252 ? 112.095 141.743 142.333 1.00 16.47 ?  252 ASN B C     1 
ATOM   7569  O  O     . ASN B 1 252 ? 112.126 141.203 141.225 1.00 14.84 ?  252 ASN B O     1 
ATOM   7570  C  CB    . ASN B 1 252 ? 112.295 144.240 142.199 1.00 12.84 ?  252 ASN B CB    1 
ATOM   7571  C  CG    . ASN B 1 252 ? 111.182 144.668 143.133 1.00 22.34 ?  252 ASN B CG    1 
ATOM   7572  O  OD1   . ASN B 1 252 ? 110.095 144.093 143.125 1.00 31.43 ?  252 ASN B OD1   1 
ATOM   7573  N  ND2   . ASN B 1 252 ? 111.452 145.678 143.949 1.00 17.56 ?  252 ASN B ND2   1 
ATOM   7574  N  N     . ILE B 1 253 ? 111.309 141.319 143.324 1.00 13.22 ?  253 ILE B N     1 
ATOM   7575  C  CA    . ILE B 1 253 ? 110.485 140.126 143.158 1.00 18.45 ?  253 ILE B CA    1 
ATOM   7576  C  C     . ILE B 1 253 ? 109.464 140.316 142.046 1.00 17.23 ?  253 ILE B C     1 
ATOM   7577  O  O     . ILE B 1 253 ? 109.032 139.343 141.417 1.00 19.43 ?  253 ILE B O     1 
ATOM   7578  C  CB    . ILE B 1 253 ? 109.807 139.759 144.493 1.00 24.07 ?  253 ILE B CB    1 
ATOM   7579  C  CG1   . ILE B 1 253 ? 109.439 138.275 144.506 1.00 16.93 ?  253 ILE B CG1   1 
ATOM   7580  C  CG2   . ILE B 1 253 ? 108.582 140.630 144.730 1.00 15.17 ?  253 ILE B CG2   1 
ATOM   7581  C  CD1   . ILE B 1 253 ? 109.467 137.655 145.876 1.00 20.58 ?  253 ILE B CD1   1 
ATOM   7582  N  N     . PHE B 1 254 ? 109.064 141.556 141.779 1.00 23.37 ?  254 PHE B N     1 
ATOM   7583  C  CA    . PHE B 1 254 ? 108.083 141.832 140.739 1.00 16.78 ?  254 PHE B CA    1 
ATOM   7584  C  C     . PHE B 1 254 ? 108.694 141.903 139.347 1.00 16.01 ?  254 PHE B C     1 
ATOM   7585  O  O     . PHE B 1 254 ? 107.954 142.068 138.372 1.00 29.25 ?  254 PHE B O     1 
ATOM   7586  C  CB    . PHE B 1 254 ? 107.342 143.133 141.053 1.00 23.00 ?  254 PHE B CB    1 
ATOM   7587  C  CG    . PHE B 1 254 ? 106.325 142.997 142.146 1.00 25.89 ?  254 PHE B CG    1 
ATOM   7588  C  CD1   . PHE B 1 254 ? 105.183 142.240 141.955 1.00 24.24 ?  254 PHE B CD1   1 
ATOM   7589  C  CD2   . PHE B 1 254 ? 106.517 143.612 143.370 1.00 22.38 ?  254 PHE B CD2   1 
ATOM   7590  C  CE1   . PHE B 1 254 ? 104.246 142.109 142.958 1.00 23.61 ?  254 PHE B CE1   1 
ATOM   7591  C  CE2   . PHE B 1 254 ? 105.584 143.483 144.377 1.00 25.79 ?  254 PHE B CE2   1 
ATOM   7592  C  CZ    . PHE B 1 254 ? 104.447 142.732 144.171 1.00 25.04 ?  254 PHE B CZ    1 
ATOM   7593  N  N     . HIS B 1 255 ? 110.012 141.789 139.229 1.00 22.92 ?  255 HIS B N     1 
ATOM   7594  C  CA    . HIS B 1 255 ? 110.638 141.714 137.918 1.00 17.11 ?  255 HIS B CA    1 
ATOM   7595  C  C     . HIS B 1 255 ? 110.248 140.413 137.231 1.00 21.85 ?  255 HIS B C     1 
ATOM   7596  O  O     . HIS B 1 255 ? 110.168 139.357 137.864 1.00 29.52 ?  255 HIS B O     1 
ATOM   7597  C  CB    . HIS B 1 255 ? 112.157 141.811 138.045 1.00 17.93 ?  255 HIS B CB    1 
ATOM   7598  C  CG    . HIS B 1 255 ? 112.851 142.143 136.762 1.00 20.66 ?  255 HIS B CG    1 
ATOM   7599  N  ND1   . HIS B 1 255 ? 113.055 141.215 135.763 1.00 20.79 ?  255 HIS B ND1   1 
ATOM   7600  C  CD2   . HIS B 1 255 ? 113.393 143.299 136.315 1.00 15.43 ?  255 HIS B CD2   1 
ATOM   7601  C  CE1   . HIS B 1 255 ? 113.689 141.786 134.756 1.00 18.42 ?  255 HIS B CE1   1 
ATOM   7602  N  NE2   . HIS B 1 255 ? 113.907 143.051 135.067 1.00 14.47 ?  255 HIS B NE2   1 
ATOM   7603  N  N     . ARG B 1 256 ? 110.001 140.493 135.923 1.00 22.96 ?  256 ARG B N     1 
ATOM   7604  C  CA    . ARG B 1 256 ? 109.553 139.317 135.187 1.00 22.29 ?  256 ARG B CA    1 
ATOM   7605  C  C     . ARG B 1 256 ? 110.590 138.202 135.220 1.00 21.05 ?  256 ARG B C     1 
ATOM   7606  O  O     . ARG B 1 256 ? 110.229 137.020 135.245 1.00 24.44 ?  256 ARG B O     1 
ATOM   7607  C  CB    . ARG B 1 256 ? 109.225 139.696 133.743 1.00 28.47 ?  256 ARG B CB    1 
ATOM   7608  C  CG    . ARG B 1 256 ? 108.359 138.680 133.028 1.00 25.93 ?  256 ARG B CG    1 
ATOM   7609  C  CD    . ARG B 1 256 ? 108.993 138.231 131.726 1.00 30.06 ?  256 ARG B CD    1 
ATOM   7610  N  NE    . ARG B 1 256 ? 110.275 137.569 131.929 1.00 30.29 ?  256 ARG B NE    1 
ATOM   7611  C  CZ    . ARG B 1 256 ? 110.432 136.255 131.989 1.00 32.06 ?  256 ARG B CZ    1 
ATOM   7612  N  NH1   . ARG B 1 256 ? 109.402 135.431 131.891 1.00 28.20 1  256 ARG B NH1   1 
ATOM   7613  N  NH2   . ARG B 1 256 ? 111.653 135.754 132.157 1.00 28.53 ?  256 ARG B NH2   1 
ATOM   7614  N  N     . ASP B 1 257 ? 111.872 138.551 135.224 1.00 16.39 ?  257 ASP B N     1 
ATOM   7615  C  CA    . ASP B 1 257 ? 112.954 137.574 135.243 1.00 17.48 ?  257 ASP B CA    1 
ATOM   7616  C  C     . ASP B 1 257 ? 113.175 136.952 136.616 1.00 21.91 ?  257 ASP B C     1 
ATOM   7617  O  O     . ASP B 1 257 ? 114.195 136.284 136.814 1.00 25.32 ?  257 ASP B O     1 
ATOM   7618  C  CB    . ASP B 1 257 ? 114.254 138.222 134.761 1.00 26.04 ?  257 ASP B CB    1 
ATOM   7619  C  CG    . ASP B 1 257 ? 114.270 138.459 133.266 1.00 29.51 ?  257 ASP B CG    1 
ATOM   7620  O  OD1   . ASP B 1 257 ? 113.325 138.014 132.583 1.00 30.46 ?  257 ASP B OD1   1 
ATOM   7621  O  OD2   . ASP B 1 257 ? 115.226 139.089 132.774 1.00 28.05 -1 257 ASP B OD2   1 
ATOM   7622  N  N     . ILE B 1 258 ? 112.255 137.149 137.562 1.00 22.98 ?  258 ILE B N     1 
ATOM   7623  C  CA    . ILE B 1 258 ? 112.480 136.681 138.928 1.00 24.35 ?  258 ILE B CA    1 
ATOM   7624  C  C     . ILE B 1 258 ? 112.641 135.167 138.964 1.00 18.36 ?  258 ILE B C     1 
ATOM   7625  O  O     . ILE B 1 258 ? 113.501 134.637 139.679 1.00 27.67 ?  258 ILE B O     1 
ATOM   7626  C  CB    . ILE B 1 258 ? 111.341 137.154 139.852 1.00 26.38 ?  258 ILE B CB    1 
ATOM   7627  C  CG1   . ILE B 1 258 ? 111.663 136.814 141.310 1.00 24.14 ?  258 ILE B CG1   1 
ATOM   7628  C  CG2   . ILE B 1 258 ? 110.015 136.542 139.430 1.00 18.24 ?  258 ILE B CG2   1 
ATOM   7629  C  CD1   . ILE B 1 258 ? 112.924 137.472 141.828 1.00 11.71 ?  258 ILE B CD1   1 
ATOM   7630  N  N     . ASN B 1 259 ? 111.822 134.443 138.199 1.00 25.18 ?  259 ASN B N     1 
ATOM   7631  C  CA    . ASN B 1 259 ? 111.913 132.987 138.208 1.00 25.73 ?  259 ASN B CA    1 
ATOM   7632  C  C     . ASN B 1 259 ? 113.178 132.507 137.507 1.00 27.07 ?  259 ASN B C     1 
ATOM   7633  O  O     . ASN B 1 259 ? 113.848 131.586 137.988 1.00 24.79 ?  259 ASN B O     1 
ATOM   7634  C  CB    . ASN B 1 259 ? 110.671 132.380 137.560 1.00 26.38 ?  259 ASN B CB    1 
ATOM   7635  C  CG    . ASN B 1 259 ? 109.463 132.429 138.470 1.00 30.12 ?  259 ASN B CG    1 
ATOM   7636  O  OD1   . ASN B 1 259 ? 109.385 131.696 139.454 1.00 27.87 ?  259 ASN B OD1   1 
ATOM   7637  N  ND2   . ASN B 1 259 ? 108.512 133.295 138.144 1.00 30.12 ?  259 ASN B ND2   1 
ATOM   7638  N  N     . ASP B 1 260 ? 113.519 133.114 136.370 1.00 28.34 ?  260 ASP B N     1 
ATOM   7639  C  CA    . ASP B 1 260 ? 114.795 132.812 135.731 1.00 23.04 ?  260 ASP B CA    1 
ATOM   7640  C  C     . ASP B 1 260 ? 115.959 133.245 136.612 1.00 24.90 ?  260 ASP B C     1 
ATOM   7641  O  O     . ASP B 1 260 ? 116.973 132.545 136.703 1.00 28.41 ?  260 ASP B O     1 
ATOM   7642  C  CB    . ASP B 1 260 ? 114.871 133.490 134.365 1.00 25.95 ?  260 ASP B CB    1 
ATOM   7643  C  CG    . ASP B 1 260 ? 113.831 132.965 133.395 1.00 37.41 ?  260 ASP B CG    1 
ATOM   7644  O  OD1   . ASP B 1 260 ? 113.397 131.804 133.556 1.00 36.83 ?  260 ASP B OD1   1 
ATOM   7645  O  OD2   . ASP B 1 260 ? 113.447 133.713 132.472 1.00 36.61 -1 260 ASP B OD2   1 
ATOM   7646  N  N     . PHE B 1 261 ? 115.828 134.403 137.262 1.00 32.30 ?  261 PHE B N     1 
ATOM   7647  C  CA    . PHE B 1 261 ? 116.862 134.878 138.173 1.00 23.80 ?  261 PHE B CA    1 
ATOM   7648  C  C     . PHE B 1 261 ? 117.074 133.901 139.322 1.00 22.32 ?  261 PHE B C     1 
ATOM   7649  O  O     . PHE B 1 261 ? 118.215 133.590 139.682 1.00 20.91 ?  261 PHE B O     1 
ATOM   7650  C  CB    . PHE B 1 261 ? 116.473 136.269 138.685 1.00 17.89 ?  261 PHE B CB    1 
ATOM   7651  C  CG    . PHE B 1 261 ? 117.306 136.769 139.832 1.00 23.47 ?  261 PHE B CG    1 
ATOM   7652  C  CD1   . PHE B 1 261 ? 118.448 137.516 139.601 1.00 19.36 ?  261 PHE B CD1   1 
ATOM   7653  C  CD2   . PHE B 1 261 ? 116.920 136.534 141.140 1.00 20.63 ?  261 PHE B CD2   1 
ATOM   7654  C  CE1   . PHE B 1 261 ? 119.205 137.994 140.652 1.00 17.45 ?  261 PHE B CE1   1 
ATOM   7655  C  CE2   . PHE B 1 261 ? 117.674 137.009 142.194 1.00 20.67 ?  261 PHE B CE2   1 
ATOM   7656  C  CZ    . PHE B 1 261 ? 118.817 137.739 141.949 1.00 18.35 ?  261 PHE B CZ    1 
ATOM   7657  N  N     . LEU B 1 262 ? 115.984 133.397 139.905 1.00 25.93 ?  262 LEU B N     1 
ATOM   7658  C  CA    . LEU B 1 262 ? 116.103 132.422 140.983 1.00 25.19 ?  262 LEU B CA    1 
ATOM   7659  C  C     . LEU B 1 262 ? 116.632 131.085 140.484 1.00 28.19 ?  262 LEU B C     1 
ATOM   7660  O  O     . LEU B 1 262 ? 117.363 130.402 141.210 1.00 28.98 ?  262 LEU B O     1 
ATOM   7661  C  CB    . LEU B 1 262 ? 114.752 132.231 141.670 1.00 26.24 ?  262 LEU B CB    1 
ATOM   7662  C  CG    . LEU B 1 262 ? 114.240 133.414 142.491 1.00 25.45 ?  262 LEU B CG    1 
ATOM   7663  C  CD1   . LEU B 1 262 ? 112.858 133.117 143.042 1.00 26.03 ?  262 LEU B CD1   1 
ATOM   7664  C  CD2   . LEU B 1 262 ? 115.210 133.740 143.613 1.00 25.33 ?  262 LEU B CD2   1 
ATOM   7665  N  N     . ASP B 1 263 ? 116.281 130.695 139.257 1.00 37.38 ?  263 ASP B N     1 
ATOM   7666  C  CA    . ASP B 1 263 ? 116.693 129.398 138.738 1.00 30.44 ?  263 ASP B CA    1 
ATOM   7667  C  C     . ASP B 1 263 ? 118.192 129.318 138.482 1.00 34.98 ?  263 ASP B C     1 
ATOM   7668  O  O     . ASP B 1 263 ? 118.725 128.212 138.345 1.00 42.28 ?  263 ASP B O     1 
ATOM   7669  C  CB    . ASP B 1 263 ? 115.929 129.079 137.453 1.00 31.92 ?  263 ASP B CB    1 
ATOM   7670  C  CG    . ASP B 1 263 ? 114.499 128.660 137.718 1.00 42.55 ?  263 ASP B CG    1 
ATOM   7671  O  OD1   . ASP B 1 263 ? 114.199 128.265 138.864 1.00 40.70 ?  263 ASP B OD1   1 
ATOM   7672  O  OD2   . ASP B 1 263 ? 113.675 128.722 136.782 1.00 42.68 -1 263 ASP B OD2   1 
ATOM   7673  N  N     . THR B 1 264 ? 118.883 130.457 138.413 1.00 40.11 ?  264 THR B N     1 
ATOM   7674  C  CA    . THR B 1 264 ? 120.331 130.430 138.244 1.00 36.40 ?  264 THR B CA    1 
ATOM   7675  C  C     . THR B 1 264 ? 121.032 129.784 139.430 1.00 38.73 ?  264 THR B C     1 
ATOM   7676  O  O     . THR B 1 264 ? 122.201 129.403 139.312 1.00 39.65 ?  264 THR B O     1 
ATOM   7677  C  CB    . THR B 1 264 ? 120.869 131.846 138.035 1.00 36.12 ?  264 THR B CB    1 
ATOM   7678  O  OG1   . THR B 1 264 ? 120.608 132.636 139.202 1.00 39.75 ?  264 THR B OG1   1 
ATOM   7679  C  CG2   . THR B 1 264 ? 120.209 132.496 136.832 1.00 36.42 ?  264 THR B CG2   1 
ATOM   7680  N  N     . LYS B 1 265 ? 120.350 129.658 140.567 1.00 36.03 ?  265 LYS B N     1 
ATOM   7681  C  CA    . LYS B 1 265 ? 120.921 129.048 141.760 1.00 37.45 ?  265 LYS B CA    1 
ATOM   7682  C  C     . LYS B 1 265 ? 120.413 127.637 142.014 1.00 38.68 ?  265 LYS B C     1 
ATOM   7683  O  O     . LYS B 1 265 ? 120.758 127.048 143.043 1.00 44.06 ?  265 LYS B O     1 
ATOM   7684  C  CB    . LYS B 1 265 ? 120.646 129.925 142.987 1.00 38.86 ?  265 LYS B CB    1 
ATOM   7685  C  CG    . LYS B 1 265 ? 121.569 131.119 143.092 1.00 40.18 ?  265 LYS B CG    1 
ATOM   7686  C  CD    . LYS B 1 265 ? 123.011 130.683 142.925 1.00 38.64 ?  265 LYS B CD    1 
ATOM   7687  C  CE    . LYS B 1 265 ? 123.953 131.866 142.943 1.00 36.53 ?  265 LYS B CE    1 
ATOM   7688  N  NZ    . LYS B 1 265 ? 125.329 131.467 142.543 1.00 40.03 1  265 LYS B NZ    1 
ATOM   7689  N  N     . LYS B 1 266 ? 119.604 127.082 141.119 1.00 45.68 ?  266 LYS B N     1 
ATOM   7690  C  CA    . LYS B 1 266 ? 119.216 125.685 141.238 1.00 47.64 ?  266 LYS B CA    1 
ATOM   7691  C  C     . LYS B 1 266 ? 120.393 124.785 140.889 1.00 52.73 ?  266 LYS B C     1 
ATOM   7692  O  O     . LYS B 1 266 ? 121.105 125.018 139.909 1.00 50.50 ?  266 LYS B O     1 
ATOM   7693  C  CB    . LYS B 1 266 ? 118.029 125.374 140.328 1.00 45.49 ?  266 LYS B CB    1 
ATOM   7694  C  CG    . LYS B 1 266 ? 116.681 125.753 140.912 1.00 48.53 ?  266 LYS B CG    1 
ATOM   7695  C  CD    . LYS B 1 266 ? 115.546 125.342 139.988 1.00 50.08 ?  266 LYS B CD    1 
ATOM   7696  C  CE    . LYS B 1 266 ? 114.205 125.400 140.703 1.00 50.45 ?  266 LYS B CE    1 
ATOM   7697  N  NZ    . LYS B 1 266 ? 113.062 125.337 139.753 1.00 51.69 1  266 LYS B NZ    1 
ATOM   7698  N  N     . ILE B 1 267 ? 120.603 123.751 141.706 1.00 58.01 ?  267 ILE B N     1 
ATOM   7699  C  CA    . ILE B 1 267 ? 121.681 122.806 141.433 1.00 60.36 ?  267 ILE B CA    1 
ATOM   7700  C  C     . ILE B 1 267 ? 121.453 122.116 140.095 1.00 62.31 ?  267 ILE B C     1 
ATOM   7701  O  O     . ILE B 1 267 ? 122.384 121.951 139.297 1.00 60.80 ?  267 ILE B O     1 
ATOM   7702  C  CB    . ILE B 1 267 ? 121.808 121.791 142.584 1.00 61.48 ?  267 ILE B CB    1 
ATOM   7703  C  CG1   . ILE B 1 267 ? 120.428 121.459 143.154 1.00 61.67 ?  267 ILE B CG1   1 
ATOM   7704  C  CG2   . ILE B 1 267 ? 122.726 122.333 143.668 1.00 60.78 ?  267 ILE B CG2   1 
ATOM   7705  C  CD1   . ILE B 1 267 ? 120.471 120.568 144.374 1.00 61.28 ?  267 ILE B CD1   1 
ATOM   7706  N  N     . SER B 1 268 ? 120.214 121.708 139.827 1.00 62.02 ?  268 SER B N     1 
ATOM   7707  C  CA    . SER B 1 268 ? 119.862 121.089 138.555 1.00 62.91 ?  268 SER B CA    1 
ATOM   7708  C  C     . SER B 1 268 ? 119.933 122.056 137.381 1.00 64.82 ?  268 SER B C     1 
ATOM   7709  O  O     . SER B 1 268 ? 119.723 121.629 136.240 1.00 65.26 ?  268 SER B O     1 
ATOM   7710  C  CB    . SER B 1 268 ? 118.458 120.489 138.642 1.00 65.62 ?  268 SER B CB    1 
ATOM   7711  O  OG    . SER B 1 268 ? 117.504 121.477 138.991 1.00 63.67 ?  268 SER B OG    1 
ATOM   7712  N  N     . ALA B 1 269 ? 120.217 123.334 137.625 1.00 68.59 ?  269 ALA B N     1 
ATOM   7713  C  CA    . ALA B 1 269 ? 120.248 124.310 136.545 1.00 67.41 ?  269 ALA B CA    1 
ATOM   7714  C  C     . ALA B 1 269 ? 121.319 123.953 135.523 1.00 68.34 ?  269 ALA B C     1 
ATOM   7715  O  O     . ALA B 1 269 ? 122.397 123.463 135.870 1.00 67.67 ?  269 ALA B O     1 
ATOM   7716  C  CB    . ALA B 1 269 ? 120.501 125.710 137.106 1.00 65.07 ?  269 ALA B CB    1 
ATOM   7717  N  N     . ASP B 1 270 ? 121.011 124.198 134.252 1.00 71.68 ?  270 ASP B N     1 
ATOM   7718  C  CA    . ASP B 1 270 ? 121.982 123.970 133.193 1.00 71.95 ?  270 ASP B CA    1 
ATOM   7719  C  C     . ASP B 1 270 ? 123.178 124.898 133.364 1.00 73.10 ?  270 ASP B C     1 
ATOM   7720  O  O     . ASP B 1 270 ? 123.052 126.034 133.828 1.00 73.96 ?  270 ASP B O     1 
ATOM   7721  C  CB    . ASP B 1 270 ? 121.336 124.182 131.823 1.00 71.48 ?  270 ASP B CB    1 
ATOM   7722  C  CG    . ASP B 1 270 ? 122.247 123.778 130.678 1.00 74.76 ?  270 ASP B CG    1 
ATOM   7723  O  OD1   . ASP B 1 270 ? 123.366 124.324 130.582 1.00 72.79 ?  270 ASP B OD1   1 
ATOM   7724  O  OD2   . ASP B 1 270 ? 121.843 122.915 129.870 1.00 74.81 -1 270 ASP B OD2   1 
ATOM   7725  N  N     . GLU B 1 271 ? 124.355 124.401 132.976 1.00 72.29 ?  271 GLU B N     1 
ATOM   7726  C  CA    . GLU B 1 271 ? 125.572 125.191 133.126 1.00 74.01 ?  271 GLU B CA    1 
ATOM   7727  C  C     . GLU B 1 271 ? 125.496 126.494 132.342 1.00 72.52 ?  271 GLU B C     1 
ATOM   7728  O  O     . GLU B 1 271 ? 126.150 127.477 132.707 1.00 71.40 ?  271 GLU B O     1 
ATOM   7729  C  CB    . GLU B 1 271 ? 126.785 124.374 132.684 1.00 72.42 ?  271 GLU B CB    1 
ATOM   7730  C  CG    . GLU B 1 271 ? 127.153 123.251 133.638 1.00 72.18 ?  271 GLU B CG    1 
ATOM   7731  C  CD    . GLU B 1 271 ? 127.769 123.759 134.926 1.00 74.32 ?  271 GLU B CD    1 
ATOM   7732  O  OE1   . GLU B 1 271 ? 128.625 124.667 134.859 1.00 74.47 ?  271 GLU B OE1   1 
ATOM   7733  O  OE2   . GLU B 1 271 ? 127.395 123.255 136.006 1.00 73.06 -1 271 GLU B OE2   1 
ATOM   7734  N  N     . ASP B 1 272 ? 124.709 126.525 131.264 1.00 71.11 ?  272 ASP B N     1 
ATOM   7735  C  CA    . ASP B 1 272 ? 124.561 127.757 130.497 1.00 71.57 ?  272 ASP B CA    1 
ATOM   7736  C  C     . ASP B 1 272 ? 123.859 128.842 131.303 1.00 70.87 ?  272 ASP B C     1 
ATOM   7737  O  O     . ASP B 1 272 ? 124.233 130.016 131.214 1.00 70.56 ?  272 ASP B O     1 
ATOM   7738  C  CB    . ASP B 1 272 ? 123.802 127.481 129.197 1.00 70.27 ?  272 ASP B CB    1 
ATOM   7739  C  CG    . ASP B 1 272 ? 122.331 127.192 129.430 1.00 72.06 ?  272 ASP B CG    1 
ATOM   7740  O  OD1   . ASP B 1 272 ? 121.984 126.724 130.535 1.00 70.11 ?  272 ASP B OD1   1 
ATOM   7741  O  OD2   . ASP B 1 272 ? 121.523 127.435 128.509 1.00 71.58 -1 272 ASP B OD2   1 
ATOM   7742  N  N     . VAL B 1 273 ? 122.848 128.475 132.089 1.00 64.49 ?  273 VAL B N     1 
ATOM   7743  C  CA    . VAL B 1 273 ? 122.076 129.443 132.861 1.00 64.25 ?  273 VAL B CA    1 
ATOM   7744  C  C     . VAL B 1 273 ? 122.646 129.562 134.267 1.00 62.49 ?  273 VAL B C     1 
ATOM   7745  O  O     . VAL B 1 273 ? 122.592 130.634 134.880 1.00 62.53 ?  273 VAL B O     1 
ATOM   7746  C  CB    . VAL B 1 273 ? 120.587 129.058 132.907 1.00 64.83 ?  273 VAL B CB    1 
ATOM   7747  C  CG1   . VAL B 1 273 ? 119.913 129.703 134.108 1.00 62.29 ?  273 VAL B CG1   1 
ATOM   7748  C  CG2   . VAL B 1 273 ? 119.895 129.473 131.620 1.00 62.42 ?  273 VAL B CG2   1 
ATOM   7749  N  N     . ARG B 1 274 ? 123.192 128.467 134.789 1.00 62.19 ?  274 ARG B N     1 
ATOM   7750  C  CA    . ARG B 1 274 ? 123.715 128.477 136.147 1.00 61.09 ?  274 ARG B CA    1 
ATOM   7751  C  C     . ARG B 1 274 ? 124.801 129.533 136.293 1.00 59.75 ?  274 ARG B C     1 
ATOM   7752  O  O     . ARG B 1 274 ? 125.687 129.658 135.443 1.00 62.34 ?  274 ARG B O     1 
ATOM   7753  C  CB    . ARG B 1 274 ? 124.269 127.101 136.519 1.00 63.71 ?  274 ARG B CB    1 
ATOM   7754  C  CG    . ARG B 1 274 ? 125.787 127.019 136.468 1.00 63.60 ?  274 ARG B CG    1 
ATOM   7755  C  CD    . ARG B 1 274 ? 126.313 125.757 137.131 1.00 63.45 ?  274 ARG B CD    1 
ATOM   7756  N  NE    . ARG B 1 274 ? 125.858 125.626 138.511 1.00 63.48 ?  274 ARG B NE    1 
ATOM   7757  C  CZ    . ARG B 1 274 ? 125.142 124.608 138.969 1.00 65.86 ?  274 ARG B CZ    1 
ATOM   7758  N  NH1   . ARG B 1 274 ? 124.778 123.610 138.181 1.00 66.57 1  274 ARG B NH1   1 
ATOM   7759  N  NH2   . ARG B 1 274 ? 124.784 124.591 140.250 1.00 64.53 ?  274 ARG B NH2   1 
ATOM   7760  N  N     . VAL B 1 275 ? 124.717 130.306 137.371 1.00 45.55 ?  275 VAL B N     1 
ATOM   7761  C  CA    . VAL B 1 275 ? 125.750 131.256 137.760 1.00 45.60 ?  275 VAL B CA    1 
ATOM   7762  C  C     . VAL B 1 275 ? 126.412 130.720 139.020 1.00 47.96 ?  275 VAL B C     1 
ATOM   7763  O  O     . VAL B 1 275 ? 125.726 130.401 139.999 1.00 47.96 ?  275 VAL B O     1 
ATOM   7764  C  CB    . VAL B 1 275 ? 125.170 132.662 137.988 1.00 42.64 ?  275 VAL B CB    1 
ATOM   7765  C  CG1   . VAL B 1 275 ? 126.121 133.490 138.817 1.00 44.97 ?  275 VAL B CG1   1 
ATOM   7766  C  CG2   . VAL B 1 275 ? 124.887 133.342 136.657 1.00 40.18 ?  275 VAL B CG2   1 
ATOM   7767  N  N     . LYS B 1 276 ? 127.739 130.613 138.998 1.00 45.78 ?  276 LYS B N     1 
ATOM   7768  C  CA    . LYS B 1 276 ? 128.444 129.902 140.057 1.00 45.52 ?  276 LYS B CA    1 
ATOM   7769  C  C     . LYS B 1 276 ? 128.959 130.818 141.161 1.00 43.63 ?  276 LYS B C     1 
ATOM   7770  O  O     . LYS B 1 276 ? 128.801 130.503 142.343 1.00 49.13 ?  276 LYS B O     1 
ATOM   7771  C  CB    . LYS B 1 276 ? 129.608 129.102 139.466 1.00 47.07 ?  276 LYS B CB    1 
ATOM   7772  C  CG    . LYS B 1 276 ? 130.682 129.954 138.809 1.00 48.44 ?  276 LYS B CG    1 
ATOM   7773  C  CD    . LYS B 1 276 ? 131.663 129.100 138.024 1.00 48.48 ?  276 LYS B CD    1 
ATOM   7774  C  CE    . LYS B 1 276 ? 130.947 128.268 136.972 1.00 49.23 ?  276 LYS B CE    1 
ATOM   7775  N  NZ    . LYS B 1 276 ? 129.753 128.972 136.430 1.00 48.31 1  276 LYS B NZ    1 
ATOM   7776  N  N     . THR B 1 277 ? 129.575 131.945 140.807 1.00 38.25 ?  277 THR B N     1 
ATOM   7777  C  CA    . THR B 1 277 ? 130.251 132.797 141.777 1.00 39.10 ?  277 THR B CA    1 
ATOM   7778  C  C     . THR B 1 277 ? 129.485 134.076 142.093 1.00 37.84 ?  277 THR B C     1 
ATOM   7779  O  O     . THR B 1 277 ? 130.042 134.973 142.735 1.00 42.57 ?  277 THR B O     1 
ATOM   7780  C  CB    . THR B 1 277 ? 131.658 133.147 141.285 1.00 41.83 ?  277 THR B CB    1 
ATOM   7781  O  OG1   . THR B 1 277 ? 131.572 133.842 140.035 1.00 38.78 ?  277 THR B OG1   1 
ATOM   7782  C  CG2   . THR B 1 277 ? 132.485 131.883 141.102 1.00 41.64 ?  277 THR B CG2   1 
ATOM   7783  N  N     . LEU B 1 278 ? 128.233 134.187 141.666 1.00 29.04 ?  278 LEU B N     1 
ATOM   7784  C  CA    . LEU B 1 278 ? 127.443 135.392 141.887 1.00 26.38 ?  278 LEU B CA    1 
ATOM   7785  C  C     . LEU B 1 278 ? 126.356 135.102 142.913 1.00 26.26 ?  278 LEU B C     1 
ATOM   7786  O  O     . LEU B 1 278 ? 125.501 134.240 142.691 1.00 32.93 ?  278 LEU B O     1 
ATOM   7787  C  CB    . LEU B 1 278 ? 126.828 135.886 140.579 1.00 28.73 ?  278 LEU B CB    1 
ATOM   7788  C  CG    . LEU B 1 278 ? 126.373 137.343 140.523 1.00 29.60 ?  278 LEU B CG    1 
ATOM   7789  C  CD1   . LEU B 1 278 ? 127.571 138.270 140.415 1.00 25.07 ?  278 LEU B CD1   1 
ATOM   7790  C  CD2   . LEU B 1 278 ? 125.422 137.551 139.358 1.00 28.18 ?  278 LEU B CD2   1 
ATOM   7791  N  N     . SER B 1 279 ? 126.395 135.817 144.033 1.00 26.16 ?  279 SER B N     1 
ATOM   7792  C  CA    . SER B 1 279 ? 125.325 135.748 145.014 1.00 17.88 ?  279 SER B CA    1 
ATOM   7793  C  C     . SER B 1 279 ? 124.113 136.522 144.514 1.00 19.80 ?  279 SER B C     1 
ATOM   7794  O  O     . SER B 1 279 ? 124.239 137.515 143.792 1.00 26.95 ?  279 SER B O     1 
ATOM   7795  C  CB    . SER B 1 279 ? 125.790 136.308 146.358 1.00 18.48 ?  279 SER B CB    1 
ATOM   7796  O  OG    . SER B 1 279 ? 126.821 135.509 146.912 1.00 26.37 ?  279 SER B OG    1 
ATOM   7797  N  N     . ILE B 1 280 ? 122.928 136.059 144.898 1.00 16.54 ?  280 ILE B N     1 
ATOM   7798  C  CA    . ILE B 1 280 ? 121.679 136.651 144.439 1.00 20.51 ?  280 ILE B CA    1 
ATOM   7799  C  C     . ILE B 1 280 ? 120.825 137.015 145.643 1.00 17.69 ?  280 ILE B C     1 
ATOM   7800  O  O     . ILE B 1 280 ? 120.711 136.239 146.597 1.00 24.93 ?  280 ILE B O     1 
ATOM   7801  C  CB    . ILE B 1 280 ? 120.908 135.710 143.491 1.00 15.73 ?  280 ILE B CB    1 
ATOM   7802  C  CG1   . ILE B 1 280 ? 120.619 134.374 144.175 1.00 20.28 ?  280 ILE B CG1   1 
ATOM   7803  C  CG2   . ILE B 1 280 ? 121.682 135.507 142.202 1.00 18.14 ?  280 ILE B CG2   1 
ATOM   7804  C  CD1   . ILE B 1 280 ? 119.484 133.605 143.548 1.00 20.08 ?  280 ILE B CD1   1 
ATOM   7805  N  N     . GLY B 1 281 ? 120.238 138.203 145.598 1.00 11.91 ?  281 GLY B N     1 
ATOM   7806  C  CA    . GLY B 1 281 ? 119.276 138.614 146.597 1.00 5.48  ?  281 GLY B CA    1 
ATOM   7807  C  C     . GLY B 1 281 ? 117.999 139.092 145.938 1.00 11.20 ?  281 GLY B C     1 
ATOM   7808  O  O     . GLY B 1 281 ? 117.999 139.550 144.796 1.00 18.17 ?  281 GLY B O     1 
ATOM   7809  N  N     . VAL B 1 282 ? 116.904 138.973 146.678 1.00 17.78 ?  282 VAL B N     1 
ATOM   7810  C  CA    . VAL B 1 282 ? 115.581 139.349 146.198 1.00 15.80 ?  282 VAL B CA    1 
ATOM   7811  C  C     . VAL B 1 282 ? 115.060 140.494 147.054 1.00 14.77 ?  282 VAL B C     1 
ATOM   7812  O  O     . VAL B 1 282 ? 115.174 140.465 148.283 1.00 23.13 ?  282 VAL B O     1 
ATOM   7813  C  CB    . VAL B 1 282 ? 114.604 138.155 146.224 1.00 18.83 ?  282 VAL B CB    1 
ATOM   7814  C  CG1   . VAL B 1 282 ? 113.184 138.622 145.966 1.00 24.27 ?  282 VAL B CG1   1 
ATOM   7815  C  CG2   . VAL B 1 282 ? 115.013 137.118 145.195 1.00 18.11 ?  282 VAL B CG2   1 
ATOM   7816  N  N     . VAL B 1 283 ? 114.497 141.502 146.400 1.00 8.41  ?  283 VAL B N     1 
ATOM   7817  C  CA    . VAL B 1 283 ? 113.891 142.642 147.076 1.00 8.29  ?  283 VAL B CA    1 
ATOM   7818  C  C     . VAL B 1 283 ? 112.384 142.429 147.048 1.00 12.94 ?  283 VAL B C     1 
ATOM   7819  O  O     . VAL B 1 283 ? 111.767 142.432 145.979 1.00 24.86 ?  283 VAL B O     1 
ATOM   7820  C  CB    . VAL B 1 283 ? 114.288 143.968 146.416 1.00 10.39 ?  283 VAL B CB    1 
ATOM   7821  C  CG1   . VAL B 1 283 ? 113.876 145.141 147.291 1.00 10.02 ?  283 VAL B CG1   1 
ATOM   7822  C  CG2   . VAL B 1 283 ? 115.782 143.993 146.143 1.00 6.61  ?  283 VAL B CG2   1 
ATOM   7823  N  N     . ILE B 1 284 ? 111.790 142.243 148.220 1.00 15.70 ?  284 ILE B N     1 
ATOM   7824  C  CA    . ILE B 1 284 ? 110.382 141.886 148.346 1.00 15.72 ?  284 ILE B CA    1 
ATOM   7825  C  C     . ILE B 1 284 ? 109.642 143.083 148.942 1.00 21.28 ?  284 ILE B C     1 
ATOM   7826  O  O     . ILE B 1 284 ? 109.795 143.372 150.137 1.00 25.31 ?  284 ILE B O     1 
ATOM   7827  C  CB    . ILE B 1 284 ? 110.191 140.631 149.208 1.00 15.70 ?  284 ILE B CB    1 
ATOM   7828  C  CG1   . ILE B 1 284 ? 110.919 139.441 148.582 1.00 20.07 ?  284 ILE B CG1   1 
ATOM   7829  C  CG2   . ILE B 1 284 ? 108.714 140.328 149.380 1.00 17.05 ?  284 ILE B CG2   1 
ATOM   7830  C  CD1   . ILE B 1 284 ? 110.698 138.142 149.315 1.00 18.94 ?  284 ILE B CD1   1 
ATOM   7831  N  N     . PRO B 1 285 ? 108.843 143.802 148.160 1.00 24.50 ?  285 PRO B N     1 
ATOM   7832  C  CA    . PRO B 1 285 ? 107.983 144.838 148.738 1.00 26.39 ?  285 PRO B CA    1 
ATOM   7833  C  C     . PRO B 1 285 ? 106.851 144.223 149.546 1.00 28.51 ?  285 PRO B C     1 
ATOM   7834  O  O     . PRO B 1 285 ? 106.514 143.046 149.409 1.00 27.94 ?  285 PRO B O     1 
ATOM   7835  C  CB    . PRO B 1 285 ? 107.446 145.585 147.512 1.00 23.78 ?  285 PRO B CB    1 
ATOM   7836  C  CG    . PRO B 1 285 ? 108.370 145.213 146.394 1.00 22.92 ?  285 PRO B CG    1 
ATOM   7837  C  CD    . PRO B 1 285 ? 108.812 143.820 146.690 1.00 22.72 ?  285 PRO B CD    1 
ATOM   7838  N  N     . ASP B 1 286 ? 106.257 145.050 150.408 1.00 29.38 ?  286 ASP B N     1 
ATOM   7839  C  CA    . ASP B 1 286 ? 105.114 144.595 151.191 1.00 26.82 ?  286 ASP B CA    1 
ATOM   7840  C  C     . ASP B 1 286 ? 103.961 144.144 150.307 1.00 29.43 ?  286 ASP B C     1 
ATOM   7841  O  O     . ASP B 1 286 ? 103.128 143.350 150.753 1.00 33.67 ?  286 ASP B O     1 
ATOM   7842  C  CB    . ASP B 1 286 ? 104.641 145.703 152.133 1.00 27.51 ?  286 ASP B CB    1 
ATOM   7843  C  CG    . ASP B 1 286 ? 105.445 145.763 153.413 1.00 36.86 ?  286 ASP B CG    1 
ATOM   7844  O  OD1   . ASP B 1 286 ? 106.198 144.807 153.690 1.00 36.87 ?  286 ASP B OD1   1 
ATOM   7845  O  OD2   . ASP B 1 286 ? 105.327 146.770 154.139 1.00 39.91 -1 286 ASP B OD2   1 
ATOM   7846  N  N     . LYS B 1 287 ? 103.897 144.632 149.066 1.00 32.86 ?  287 LYS B N     1 
ATOM   7847  C  CA    . LYS B 1 287 ? 102.827 144.224 148.164 1.00 28.20 ?  287 LYS B CA    1 
ATOM   7848  C  C     . LYS B 1 287 ? 102.888 142.731 147.872 1.00 29.41 ?  287 LYS B C     1 
ATOM   7849  O  O     . LYS B 1 287 ? 101.854 142.056 147.843 1.00 31.45 ?  287 LYS B O     1 
ATOM   7850  C  CB    . LYS B 1 287 ? 102.902 145.028 146.866 1.00 31.58 ?  287 LYS B CB    1 
ATOM   7851  C  CG    . LYS B 1 287 ? 101.690 144.858 145.968 1.00 29.73 ?  287 LYS B CG    1 
ATOM   7852  C  CD    . LYS B 1 287 ? 100.416 145.209 146.711 1.00 33.27 ?  287 LYS B CD    1 
ATOM   7853  C  CE    . LYS B 1 287 ? 99.235  145.312 145.768 1.00 34.66 ?  287 LYS B CE    1 
ATOM   7854  N  NZ    . LYS B 1 287 ? 98.041  145.879 146.449 1.00 36.29 1  287 LYS B NZ    1 
ATOM   7855  N  N     . PHE B 1 288 ? 104.090 142.199 147.640 1.00 26.20 ?  288 PHE B N     1 
ATOM   7856  C  CA    . PHE B 1 288 ? 104.218 140.772 147.363 1.00 24.98 ?  288 PHE B CA    1 
ATOM   7857  C  C     . PHE B 1 288 ? 103.799 139.934 148.565 1.00 24.99 ?  288 PHE B C     1 
ATOM   7858  O  O     . PHE B 1 288 ? 103.120 138.912 148.412 1.00 33.36 ?  288 PHE B O     1 
ATOM   7859  C  CB    . PHE B 1 288 ? 105.651 140.440 146.954 1.00 28.00 ?  288 PHE B CB    1 
ATOM   7860  C  CG    . PHE B 1 288 ? 105.850 139.003 146.576 1.00 27.32 ?  288 PHE B CG    1 
ATOM   7861  C  CD1   . PHE B 1 288 ? 105.532 138.558 145.305 1.00 25.01 ?  288 PHE B CD1   1 
ATOM   7862  C  CD2   . PHE B 1 288 ? 106.350 138.094 147.492 1.00 25.08 ?  288 PHE B CD2   1 
ATOM   7863  C  CE1   . PHE B 1 288 ? 105.712 137.236 144.956 1.00 28.29 ?  288 PHE B CE1   1 
ATOM   7864  C  CE2   . PHE B 1 288 ? 106.529 136.771 147.148 1.00 26.64 ?  288 PHE B CE2   1 
ATOM   7865  C  CZ    . PHE B 1 288 ? 106.212 136.342 145.878 1.00 29.49 ?  288 PHE B CZ    1 
ATOM   7866  N  N     . VAL B 1 289 ? 104.204 140.343 149.767 1.00 33.02 ?  289 VAL B N     1 
ATOM   7867  C  CA    . VAL B 1 289 ? 103.819 139.606 150.966 1.00 30.50 ?  289 VAL B CA    1 
ATOM   7868  C  C     . VAL B 1 289 ? 102.311 139.666 151.161 1.00 30.11 ?  289 VAL B C     1 
ATOM   7869  O  O     . VAL B 1 289 ? 101.681 138.679 151.555 1.00 31.62 ?  289 VAL B O     1 
ATOM   7870  C  CB    . VAL B 1 289 ? 104.573 140.147 152.196 1.00 33.18 ?  289 VAL B CB    1 
ATOM   7871  C  CG1   . VAL B 1 289 ? 104.170 139.376 153.443 1.00 26.82 ?  289 VAL B CG1   1 
ATOM   7872  C  CG2   . VAL B 1 289 ? 106.073 140.065 151.975 1.00 27.72 ?  289 VAL B CG2   1 
ATOM   7873  N  N     . GLU B 1 290 ? 101.707 140.825 150.891 1.00 32.94 ?  290 GLU B N     1 
ATOM   7874  C  CA    . GLU B 1 290 ? 100.257 140.945 150.997 1.00 32.99 ?  290 GLU B CA    1 
ATOM   7875  C  C     . GLU B 1 290 ? 99.555  140.037 149.996 1.00 37.61 ?  290 GLU B C     1 
ATOM   7876  O  O     . GLU B 1 290 ? 98.563  139.380 150.329 1.00 42.86 ?  290 GLU B O     1 
ATOM   7877  C  CB    . GLU B 1 290 ? 99.839  142.400 150.790 1.00 34.40 ?  290 GLU B CB    1 
ATOM   7878  C  CG    . GLU B 1 290 ? 98.347  142.646 150.923 1.00 40.67 ?  290 GLU B CG    1 
ATOM   7879  C  CD    . GLU B 1 290 ? 97.906  143.921 150.235 1.00 46.34 ?  290 GLU B CD    1 
ATOM   7880  O  OE1   . GLU B 1 290 ? 98.637  144.930 150.324 1.00 47.28 ?  290 GLU B OE1   1 
ATOM   7881  O  OE2   . GLU B 1 290 ? 96.826  143.918 149.608 1.00 41.71 -1 290 GLU B OE2   1 
ATOM   7882  N  N     . LEU B 1 291 ? 100.055 139.990 148.758 1.00 35.80 ?  291 LEU B N     1 
ATOM   7883  C  CA    . LEU B 1 291 ? 99.455  139.123 147.748 1.00 29.14 ?  291 LEU B CA    1 
ATOM   7884  C  C     . LEU B 1 291 ? 99.570  137.658 148.143 1.00 32.47 ?  291 LEU B C     1 
ATOM   7885  O  O     . LEU B 1 291 ? 98.607  136.893 148.015 1.00 38.09 ?  291 LEU B O     1 
ATOM   7886  C  CB    . LEU B 1 291 ? 100.114 139.366 146.391 1.00 33.73 ?  291 LEU B CB    1 
ATOM   7887  C  CG    . LEU B 1 291 ? 99.973  140.768 145.794 1.00 34.16 ?  291 LEU B CG    1 
ATOM   7888  C  CD1   . LEU B 1 291 ? 100.922 140.954 144.618 1.00 26.85 ?  291 LEU B CD1   1 
ATOM   7889  C  CD2   . LEU B 1 291 ? 98.537  141.034 145.378 1.00 30.09 ?  291 LEU B CD2   1 
ATOM   7890  N  N     . ALA B 1 292 ? 100.746 137.245 148.624 1.00 33.87 ?  292 ALA B N     1 
ATOM   7891  C  CA    . ALA B 1 292 ? 100.930 135.858 149.038 1.00 32.72 ?  292 ALA B CA    1 
ATOM   7892  C  C     . ALA B 1 292 ? 100.049 135.518 150.232 1.00 30.27 ?  292 ALA B C     1 
ATOM   7893  O  O     . ALA B 1 292 ? 99.520  134.405 150.328 1.00 33.49 ?  292 ALA B O     1 
ATOM   7894  C  CB    . ALA B 1 292 ? 102.401 135.599 149.362 1.00 30.51 ?  292 ALA B CB    1 
ATOM   7895  N  N     . ARG B 1 293 ? 99.883  136.465 151.156 1.00 35.07 ?  293 ARG B N     1 
ATOM   7896  C  CA    . ARG B 1 293 ? 99.060  136.223 152.334 1.00 39.31 ?  293 ARG B CA    1 
ATOM   7897  C  C     . ARG B 1 293 ? 97.613  135.949 151.949 1.00 42.47 ?  293 ARG B C     1 
ATOM   7898  O  O     . ARG B 1 293 ? 96.965  135.069 152.526 1.00 46.76 ?  293 ARG B O     1 
ATOM   7899  C  CB    . ARG B 1 293 ? 99.149  137.420 153.280 1.00 38.96 ?  293 ARG B CB    1 
ATOM   7900  C  CG    . ARG B 1 293 ? 98.302  137.305 154.531 1.00 39.79 ?  293 ARG B CG    1 
ATOM   7901  C  CD    . ARG B 1 293 ? 98.272  138.628 155.272 1.00 40.12 ?  293 ARG B CD    1 
ATOM   7902  N  NE    . ARG B 1 293 ? 99.618  139.131 155.519 1.00 46.79 ?  293 ARG B NE    1 
ATOM   7903  C  CZ    . ARG B 1 293 ? 100.028 140.354 155.216 1.00 43.52 ?  293 ARG B CZ    1 
ATOM   7904  N  NH1   . ARG B 1 293 ? 99.216  141.236 154.656 1.00 40.47 1  293 ARG B NH1   1 
ATOM   7905  N  NH2   . ARG B 1 293 ? 101.284 140.701 155.479 1.00 39.58 ?  293 ARG B NH2   1 
ATOM   7906  N  N     . GLU B 1 294 ? 97.091  136.692 150.979 1.00 43.91 ?  294 GLU B N     1 
ATOM   7907  C  CA    . GLU B 1 294 ? 95.719  136.531 150.525 1.00 43.41 ?  294 GLU B CA    1 
ATOM   7908  C  C     . GLU B 1 294 ? 95.568  135.452 149.462 1.00 45.15 ?  294 GLU B C     1 
ATOM   7909  O  O     . GLU B 1 294 ? 94.443  135.173 149.038 1.00 48.19 ?  294 GLU B O     1 
ATOM   7910  C  CB    . GLU B 1 294 ? 95.186  137.862 149.986 1.00 41.69 ?  294 GLU B CB    1 
ATOM   7911  C  CG    . GLU B 1 294 ? 94.744  138.829 151.068 1.00 44.82 ?  294 GLU B CG    1 
ATOM   7912  C  CD    . GLU B 1 294 ? 95.169  140.254 150.783 1.00 50.68 ?  294 GLU B CD    1 
ATOM   7913  O  OE1   . GLU B 1 294 ? 95.202  140.639 149.595 1.00 54.03 ?  294 GLU B OE1   1 
ATOM   7914  O  OE2   . GLU B 1 294 ? 95.471  140.990 151.746 1.00 50.01 -1 294 GLU B OE2   1 
ATOM   7915  N  N     . ASP B 1 295 ? 96.665  134.841 149.023 1.00 44.36 ?  295 ASP B N     1 
ATOM   7916  C  CA    . ASP B 1 295 ? 96.663  133.800 148.002 1.00 44.02 ?  295 ASP B CA    1 
ATOM   7917  C  C     . ASP B 1 295 ? 96.167  134.306 146.653 1.00 49.42 ?  295 ASP B C     1 
ATOM   7918  O  O     . ASP B 1 295 ? 95.833  133.499 145.778 1.00 47.80 ?  295 ASP B O     1 
ATOM   7919  C  CB    . ASP B 1 295 ? 95.830  132.591 148.444 1.00 43.26 ?  295 ASP B CB    1 
ATOM   7920  C  CG    . ASP B 1 295 ? 96.481  131.269 148.085 1.00 51.14 ?  295 ASP B CG    1 
ATOM   7921  O  OD1   . ASP B 1 295 ? 97.601  131.286 147.534 1.00 50.13 ?  295 ASP B OD1   1 
ATOM   7922  O  OD2   . ASP B 1 295 ? 95.874  130.213 148.358 1.00 48.43 -1 295 ASP B OD2   1 
ATOM   7923  N  N     . LYS B 1 296 ? 96.111  135.620 146.465 1.00 48.35 ?  296 LYS B N     1 
ATOM   7924  C  CA    . LYS B 1 296 ? 95.654  136.185 145.205 1.00 48.05 ?  296 LYS B CA    1 
ATOM   7925  C  C     . LYS B 1 296 ? 96.701  135.990 144.116 1.00 46.29 ?  296 LYS B C     1 
ATOM   7926  O  O     . LYS B 1 296 ? 97.908  136.025 144.367 1.00 47.50 ?  296 LYS B O     1 
ATOM   7927  C  CB    . LYS B 1 296 ? 95.350  137.674 145.370 1.00 46.67 ?  296 LYS B CB    1 
ATOM   7928  C  CG    . LYS B 1 296 ? 94.276  137.981 146.397 1.00 47.44 ?  296 LYS B CG    1 
ATOM   7929  C  CD    . LYS B 1 296 ? 94.219  139.467 146.706 1.00 45.72 ?  296 LYS B CD    1 
ATOM   7930  C  CE    . LYS B 1 296 ? 92.950  139.823 147.462 1.00 47.69 ?  296 LYS B CE    1 
ATOM   7931  N  NZ    . LYS B 1 296 ? 92.179  138.609 147.850 1.00 48.50 1  296 LYS B NZ    1 
ATOM   7932  N  N     . ALA B 1 297 ? 96.223  135.780 142.892 1.00 42.92 ?  297 ALA B N     1 
ATOM   7933  C  CA    . ALA B 1 297 ? 97.124  135.701 141.750 1.00 43.43 ?  297 ALA B CA    1 
ATOM   7934  C  C     . ALA B 1 297 ? 97.872  137.016 141.588 1.00 46.22 ?  297 ALA B C     1 
ATOM   7935  O  O     . ALA B 1 297 ? 97.272  138.095 141.612 1.00 48.95 ?  297 ALA B O     1 
ATOM   7936  C  CB    . ALA B 1 297 ? 96.341  135.373 140.480 1.00 44.36 ?  297 ALA B CB    1 
ATOM   7937  N  N     . ALA B 1 298 ? 99.186  136.926 141.421 1.00 34.63 ?  298 ALA B N     1 
ATOM   7938  C  CA    . ALA B 1 298 ? 100.045 138.093 141.298 1.00 33.95 ?  298 ALA B CA    1 
ATOM   7939  C  C     . ALA B 1 298 ? 100.589 138.197 139.881 1.00 36.25 ?  298 ALA B C     1 
ATOM   7940  O  O     . ALA B 1 298 ? 100.502 137.261 139.081 1.00 38.45 ?  298 ALA B O     1 
ATOM   7941  C  CB    . ALA B 1 298 ? 101.194 138.032 142.311 1.00 36.65 ?  298 ALA B CB    1 
ATOM   7942  N  N     . TYR B 1 299 ? 101.160 139.357 139.578 1.00 32.89 ?  299 TYR B N     1 
ATOM   7943  C  CA    . TYR B 1 299 ? 101.718 139.637 138.265 1.00 27.75 ?  299 TYR B CA    1 
ATOM   7944  C  C     . TYR B 1 299 ? 103.149 140.127 138.408 1.00 31.69 ?  299 TYR B C     1 
ATOM   7945  O  O     . TYR B 1 299 ? 103.460 140.915 139.304 1.00 35.93 ?  299 TYR B O     1 
ATOM   7946  C  CB    . TYR B 1 299 ? 100.883 140.683 137.516 1.00 29.23 ?  299 TYR B CB    1 
ATOM   7947  C  CG    . TYR B 1 299 ? 99.507  140.199 137.127 1.00 32.39 ?  299 TYR B CG    1 
ATOM   7948  C  CD1   . TYR B 1 299 ? 99.294  139.561 135.914 1.00 32.50 ?  299 TYR B CD1   1 
ATOM   7949  C  CD2   . TYR B 1 299 ? 98.423  140.375 137.976 1.00 33.35 ?  299 TYR B CD2   1 
ATOM   7950  C  CE1   . TYR B 1 299 ? 98.039  139.114 135.555 1.00 34.83 ?  299 TYR B CE1   1 
ATOM   7951  C  CE2   . TYR B 1 299 ? 97.165  139.930 137.626 1.00 32.83 ?  299 TYR B CE2   1 
ATOM   7952  C  CZ    . TYR B 1 299 ? 96.979  139.301 136.415 1.00 35.71 ?  299 TYR B CZ    1 
ATOM   7953  O  OH    . TYR B 1 299 ? 95.725  138.858 136.061 1.00 39.10 ?  299 TYR B OH    1 
ATOM   7954  N  N     . VAL B 1 300 ? 104.017 139.648 137.523 1.00 31.74 ?  300 VAL B N     1 
ATOM   7955  C  CA    . VAL B 1 300 ? 105.371 140.163 137.378 1.00 28.56 ?  300 VAL B CA    1 
ATOM   7956  C  C     . VAL B 1 300 ? 105.422 140.957 136.083 1.00 27.71 ?  300 VAL B C     1 
ATOM   7957  O  O     . VAL B 1 300 ? 104.894 140.523 135.053 1.00 32.86 ?  300 VAL B O     1 
ATOM   7958  C  CB    . VAL B 1 300 ? 106.422 139.038 137.391 1.00 27.18 ?  300 VAL B CB    1 
ATOM   7959  C  CG1   . VAL B 1 300 ? 106.639 138.541 138.810 1.00 24.92 ?  300 VAL B CG1   1 
ATOM   7960  C  CG2   . VAL B 1 300 ? 105.996 137.897 136.483 1.00 24.65 ?  300 VAL B CG2   1 
ATOM   7961  N  N     . PHE B 1 301 ? 106.052 142.124 136.134 1.00 25.68 ?  301 PHE B N     1 
ATOM   7962  C  CA    . PHE B 1 301 ? 105.948 143.108 135.070 1.00 26.87 ?  301 PHE B CA    1 
ATOM   7963  C  C     . PHE B 1 301 ? 107.224 143.153 134.241 1.00 27.89 ?  301 PHE B C     1 
ATOM   7964  O  O     . PHE B 1 301 ? 108.312 142.822 134.720 1.00 33.84 ?  301 PHE B O     1 
ATOM   7965  C  CB    . PHE B 1 301 ? 105.652 144.495 135.646 1.00 25.04 ?  301 PHE B CB    1 
ATOM   7966  C  CG    . PHE B 1 301 ? 104.492 144.513 136.596 1.00 27.44 ?  301 PHE B CG    1 
ATOM   7967  C  CD1   . PHE B 1 301 ? 103.205 144.718 136.133 1.00 23.45 ?  301 PHE B CD1   1 
ATOM   7968  C  CD2   . PHE B 1 301 ? 104.688 144.314 137.951 1.00 26.71 ?  301 PHE B CD2   1 
ATOM   7969  C  CE1   . PHE B 1 301 ? 102.138 144.730 137.004 1.00 29.52 ?  301 PHE B CE1   1 
ATOM   7970  C  CE2   . PHE B 1 301 ? 103.624 144.324 138.827 1.00 29.30 ?  301 PHE B CE2   1 
ATOM   7971  C  CZ    . PHE B 1 301 ? 102.346 144.531 138.353 1.00 32.83 ?  301 PHE B CZ    1 
ATOM   7972  N  N     . TYR B 1 302 ? 107.070 143.557 132.983 1.00 26.11 ?  302 TYR B N     1 
ATOM   7973  C  CA    . TYR B 1 302 ? 108.208 143.830 132.121 1.00 28.19 ?  302 TYR B CA    1 
ATOM   7974  C  C     . TYR B 1 302 ? 108.677 145.257 132.369 1.00 25.47 ?  302 TYR B C     1 
ATOM   7975  O  O     . TYR B 1 302 ? 107.917 146.198 132.106 1.00 26.95 ?  302 TYR B O     1 
ATOM   7976  C  CB    . TYR B 1 302 ? 107.834 143.646 130.662 1.00 27.05 ?  302 TYR B CB    1 
ATOM   7977  C  CG    . TYR B 1 302 ? 107.596 142.207 130.266 1.00 25.57 ?  302 TYR B CG    1 
ATOM   7978  C  CD1   . TYR B 1 302 ? 106.448 141.536 130.668 1.00 27.78 ?  302 TYR B CD1   1 
ATOM   7979  C  CD2   . TYR B 1 302 ? 108.519 141.519 129.491 1.00 25.01 ?  302 TYR B CD2   1 
ATOM   7980  C  CE1   . TYR B 1 302 ? 106.226 140.223 130.310 1.00 22.94 ?  302 TYR B CE1   1 
ATOM   7981  C  CE2   . TYR B 1 302 ? 108.304 140.206 129.127 1.00 29.69 ?  302 TYR B CE2   1 
ATOM   7982  C  CZ    . TYR B 1 302 ? 107.156 139.563 129.538 1.00 31.65 ?  302 TYR B CZ    1 
ATOM   7983  O  OH    . TYR B 1 302 ? 106.940 138.254 129.179 1.00 36.08 ?  302 TYR B OH    1 
ATOM   7984  N  N     . PRO B 1 303 ? 109.891 145.464 132.875 1.00 26.33 ?  303 PRO B N     1 
ATOM   7985  C  CA    . PRO B 1 303 ? 110.287 146.819 133.292 1.00 24.96 ?  303 PRO B CA    1 
ATOM   7986  C  C     . PRO B 1 303 ? 110.269 147.844 132.173 1.00 27.12 ?  303 PRO B C     1 
ATOM   7987  O  O     . PRO B 1 303 ? 109.934 149.008 132.423 1.00 29.57 ?  303 PRO B O     1 
ATOM   7988  C  CB    . PRO B 1 303 ? 111.706 146.611 133.840 1.00 25.50 ?  303 PRO B CB    1 
ATOM   7989  C  CG    . PRO B 1 303 ? 111.775 145.163 134.181 1.00 24.33 ?  303 PRO B CG    1 
ATOM   7990  C  CD    . PRO B 1 303 ? 110.939 144.471 133.158 1.00 24.85 ?  303 PRO B CD    1 
ATOM   7991  N  N     . HIS B 1 304 ? 110.619 147.457 130.945 1.00 25.31 ?  304 HIS B N     1 
ATOM   7992  C  CA    . HIS B 1 304 ? 110.711 148.445 129.877 1.00 27.00 ?  304 HIS B CA    1 
ATOM   7993  C  C     . HIS B 1 304 ? 109.339 148.952 129.456 1.00 31.50 ?  304 HIS B C     1 
ATOM   7994  O  O     . HIS B 1 304 ? 109.197 150.127 129.105 1.00 38.10 ?  304 HIS B O     1 
ATOM   7995  C  CB    . HIS B 1 304 ? 111.455 147.865 128.677 1.00 28.11 ?  304 HIS B CB    1 
ATOM   7996  C  CG    . HIS B 1 304 ? 111.734 148.870 127.604 1.00 31.21 ?  304 HIS B CG    1 
ATOM   7997  N  ND1   . HIS B 1 304 ? 112.343 150.079 127.862 1.00 30.63 ?  304 HIS B ND1   1 
ATOM   7998  C  CD2   . HIS B 1 304 ? 111.488 148.849 126.273 1.00 33.73 ?  304 HIS B CD2   1 
ATOM   7999  C  CE1   . HIS B 1 304 ? 112.460 150.760 126.736 1.00 29.27 ?  304 HIS B CE1   1 
ATOM   8000  N  NE2   . HIS B 1 304 ? 111.950 150.035 125.757 1.00 33.08 ?  304 HIS B NE2   1 
ATOM   8001  N  N     . THR B 1 305 ? 108.323 148.088 129.481 1.00 32.76 ?  305 THR B N     1 
ATOM   8002  C  CA    . THR B 1 305 ? 106.969 148.550 129.200 1.00 29.31 ?  305 THR B CA    1 
ATOM   8003  C  C     . THR B 1 305 ? 106.527 149.588 130.224 1.00 27.87 ?  305 THR B C     1 
ATOM   8004  O  O     . THR B 1 305 ? 105.931 150.609 129.867 1.00 32.35 ?  305 THR B O     1 
ATOM   8005  C  CB    . THR B 1 305 ? 106.002 147.366 129.178 1.00 29.83 ?  305 THR B CB    1 
ATOM   8006  O  OG1   . THR B 1 305 ? 105.780 146.900 130.514 1.00 27.92 ?  305 THR B OG1   1 
ATOM   8007  C  CG2   . THR B 1 305 ? 106.571 146.233 128.342 1.00 26.96 ?  305 THR B CG2   1 
ATOM   8008  N  N     . ILE B 1 306 ? 106.829 149.350 131.503 1.00 33.23 ?  306 ILE B N     1 
ATOM   8009  C  CA    . ILE B 1 306 ? 106.492 150.318 132.541 1.00 28.31 ?  306 ILE B CA    1 
ATOM   8010  C  C     . ILE B 1 306 ? 107.256 151.617 132.328 1.00 29.72 ?  306 ILE B C     1 
ATOM   8011  O  O     . ILE B 1 306 ? 106.699 152.712 132.471 1.00 35.61 ?  306 ILE B O     1 
ATOM   8012  C  CB    . ILE B 1 306 ? 106.765 149.723 133.935 1.00 29.76 ?  306 ILE B CB    1 
ATOM   8013  C  CG1   . ILE B 1 306 ? 105.678 148.714 134.305 1.00 26.38 ?  306 ILE B CG1   1 
ATOM   8014  C  CG2   . ILE B 1 306 ? 106.862 150.828 134.978 1.00 28.58 ?  306 ILE B CG2   1 
ATOM   8015  C  CD1   . ILE B 1 306 ? 106.051 147.813 135.452 1.00 24.09 ?  306 ILE B CD1   1 
ATOM   8016  N  N     . TYR B 1 307 ? 108.545 151.521 131.997 1.00 34.43 ?  307 TYR B N     1 
ATOM   8017  C  CA    . TYR B 1 307 ? 109.336 152.726 131.772 1.00 31.36 ?  307 TYR B CA    1 
ATOM   8018  C  C     . TYR B 1 307 ? 108.777 153.544 130.614 1.00 29.85 ?  307 TYR B C     1 
ATOM   8019  O  O     . TYR B 1 307 ? 108.701 154.774 130.693 1.00 36.50 ?  307 TYR B O     1 
ATOM   8020  C  CB    . TYR B 1 307 ? 110.796 152.358 131.512 1.00 27.46 ?  307 TYR B CB    1 
ATOM   8021  C  CG    . TYR B 1 307 ? 111.695 153.554 131.306 1.00 34.47 ?  307 TYR B CG    1 
ATOM   8022  C  CD1   . TYR B 1 307 ? 112.260 154.216 132.386 1.00 31.14 ?  307 TYR B CD1   1 
ATOM   8023  C  CD2   . TYR B 1 307 ? 111.976 154.025 130.030 1.00 34.90 ?  307 TYR B CD2   1 
ATOM   8024  C  CE1   . TYR B 1 307 ? 113.078 155.312 132.204 1.00 30.15 ?  307 TYR B CE1   1 
ATOM   8025  C  CE2   . TYR B 1 307 ? 112.793 155.119 129.838 1.00 31.46 ?  307 TYR B CE2   1 
ATOM   8026  C  CZ    . TYR B 1 307 ? 113.342 155.759 130.928 1.00 32.46 ?  307 TYR B CZ    1 
ATOM   8027  O  OH    . TYR B 1 307 ? 114.158 156.850 130.742 1.00 34.70 ?  307 TYR B OH    1 
ATOM   8028  N  N     . LYS B 1 308 ? 108.390 152.875 129.528 1.00 34.00 ?  308 LYS B N     1 
ATOM   8029  C  CA    . LYS B 1 308 ? 107.818 153.585 128.388 1.00 32.68 ?  308 LYS B CA    1 
ATOM   8030  C  C     . LYS B 1 308 ? 106.466 154.195 128.735 1.00 32.72 ?  308 LYS B C     1 
ATOM   8031  O  O     . LYS B 1 308 ? 106.158 155.315 128.312 1.00 40.87 ?  308 LYS B O     1 
ATOM   8032  C  CB    . LYS B 1 308 ? 107.693 152.638 127.195 1.00 32.62 ?  308 LYS B CB    1 
ATOM   8033  C  CG    . LYS B 1 308 ? 109.025 152.171 126.635 1.00 33.82 ?  308 LYS B CG    1 
ATOM   8034  C  CD    . LYS B 1 308 ? 108.833 151.286 125.418 1.00 36.45 ?  308 LYS B CD    1 
ATOM   8035  C  CE    . LYS B 1 308 ? 107.714 150.281 125.637 1.00 38.24 ?  308 LYS B CE    1 
ATOM   8036  N  NZ    . LYS B 1 308 ? 108.236 148.899 125.816 1.00 36.79 1  308 LYS B NZ    1 
ATOM   8037  N  N     . GLU B 1 309 ? 105.646 153.476 129.505 1.00 31.67 ?  309 GLU B N     1 
ATOM   8038  C  CA    . GLU B 1 309 ? 104.306 153.962 129.814 1.00 34.22 ?  309 GLU B CA    1 
ATOM   8039  C  C     . GLU B 1 309 ? 104.342 155.144 130.777 1.00 36.38 ?  309 GLU B C     1 
ATOM   8040  O  O     . GLU B 1 309 ? 103.592 156.111 130.608 1.00 40.54 ?  309 GLU B O     1 
ATOM   8041  C  CB    . GLU B 1 309 ? 103.461 152.827 130.390 1.00 31.66 ?  309 GLU B CB    1 
ATOM   8042  C  CG    . GLU B 1 309 ? 102.145 153.275 130.995 1.00 37.37 ?  309 GLU B CG    1 
ATOM   8043  C  CD    . GLU B 1 309 ? 101.194 153.843 129.963 1.00 42.64 ?  309 GLU B CD    1 
ATOM   8044  O  OE1   . GLU B 1 309 ? 101.457 153.674 128.754 1.00 43.06 ?  309 GLU B OE1   1 
ATOM   8045  O  OE2   . GLU B 1 309 ? 100.184 154.461 130.361 1.00 41.52 -1 309 GLU B OE2   1 
ATOM   8046  N  N     . TYR B 1 310 ? 105.203 155.087 131.791 1.00 35.82 ?  310 TYR B N     1 
ATOM   8047  C  CA    . TYR B 1 310 ? 105.219 156.088 132.847 1.00 33.79 ?  310 TYR B CA    1 
ATOM   8048  C  C     . TYR B 1 310 ? 106.455 156.974 132.831 1.00 34.51 ?  310 TYR B C     1 
ATOM   8049  O  O     . TYR B 1 310 ? 106.460 158.007 133.510 1.00 36.36 ?  310 TYR B O     1 
ATOM   8050  C  CB    . TYR B 1 310 ? 105.104 155.407 134.218 1.00 31.60 ?  310 TYR B CB    1 
ATOM   8051  C  CG    . TYR B 1 310 ? 103.838 154.602 134.385 1.00 33.05 ?  310 TYR B CG    1 
ATOM   8052  C  CD1   . TYR B 1 310 ? 102.641 155.217 134.721 1.00 32.48 ?  310 TYR B CD1   1 
ATOM   8053  C  CD2   . TYR B 1 310 ? 103.837 153.228 134.192 1.00 29.80 ?  310 TYR B CD2   1 
ATOM   8054  C  CE1   . TYR B 1 310 ? 101.482 154.486 134.870 1.00 34.01 ?  310 TYR B CE1   1 
ATOM   8055  C  CE2   . TYR B 1 310 ? 102.683 152.489 134.338 1.00 33.22 ?  310 TYR B CE2   1 
ATOM   8056  C  CZ    . TYR B 1 310 ? 101.508 153.122 134.676 1.00 34.96 ?  310 TYR B CZ    1 
ATOM   8057  O  OH    . TYR B 1 310 ? 100.356 152.388 134.823 1.00 38.32 ?  310 TYR B OH    1 
ATOM   8058  N  N     . GLY B 1 311 ? 107.491 156.610 132.081 1.00 35.37 ?  311 GLY B N     1 
ATOM   8059  C  CA    . GLY B 1 311 ? 108.716 157.378 132.056 1.00 30.45 ?  311 GLY B CA    1 
ATOM   8060  C  C     . GLY B 1 311 ? 109.642 157.135 133.224 1.00 33.26 ?  311 GLY B C     1 
ATOM   8061  O  O     . GLY B 1 311 ? 110.697 157.777 133.300 1.00 38.61 ?  311 GLY B O     1 
ATOM   8062  N  N     . GLN B 1 312 ? 109.285 156.237 134.136 1.00 34.80 ?  312 GLN B N     1 
ATOM   8063  C  CA    . GLN B 1 312 ? 110.111 155.909 135.286 1.00 32.98 ?  312 GLN B CA    1 
ATOM   8064  C  C     . GLN B 1 312 ? 110.334 154.406 135.333 1.00 35.08 ?  312 GLN B C     1 
ATOM   8065  O  O     . GLN B 1 312 ? 109.586 153.626 134.740 1.00 39.51 ?  312 GLN B O     1 
ATOM   8066  C  CB    . GLN B 1 312 ? 109.470 156.381 136.599 1.00 34.26 ?  312 GLN B CB    1 
ATOM   8067  C  CG    . GLN B 1 312 ? 108.782 157.729 136.514 1.00 36.83 ?  312 GLN B CG    1 
ATOM   8068  C  CD    . GLN B 1 312 ? 107.811 157.956 137.655 1.00 42.15 ?  312 GLN B CD    1 
ATOM   8069  O  OE1   . GLN B 1 312 ? 106.601 158.048 137.447 1.00 41.87 ?  312 GLN B OE1   1 
ATOM   8070  N  NE2   . GLN B 1 312 ? 108.338 158.044 138.871 1.00 35.76 ?  312 GLN B NE2   1 
ATOM   8071  N  N     . HIS B 1 313 ? 111.384 154.007 136.044 1.00 29.29 ?  313 HIS B N     1 
ATOM   8072  C  CA    . HIS B 1 313 ? 111.660 152.592 136.229 1.00 28.67 ?  313 HIS B CA    1 
ATOM   8073  C  C     . HIS B 1 313 ? 110.705 151.990 137.253 1.00 31.24 ?  313 HIS B C     1 
ATOM   8074  O  O     . HIS B 1 313 ? 110.207 152.673 138.150 1.00 33.68 ?  313 HIS B O     1 
ATOM   8075  C  CB    . HIS B 1 313 ? 113.108 152.382 136.668 1.00 26.64 ?  313 HIS B CB    1 
ATOM   8076  C  CG    . HIS B 1 313 ? 114.116 152.802 135.644 1.00 31.26 ?  313 HIS B CG    1 
ATOM   8077  N  ND1   . HIS B 1 313 ? 114.802 153.994 135.718 1.00 33.56 ?  313 HIS B ND1   1 
ATOM   8078  C  CD2   . HIS B 1 313 ? 114.550 152.189 134.518 1.00 29.27 ?  313 HIS B CD2   1 
ATOM   8079  C  CE1   . HIS B 1 313 ? 115.617 154.097 134.684 1.00 32.43 ?  313 HIS B CE1   1 
ATOM   8080  N  NE2   . HIS B 1 313 ? 115.484 153.013 133.941 1.00 30.92 ?  313 HIS B NE2   1 
ATOM   8081  N  N     . MET B 1 314 ? 110.455 150.686 137.110 1.00 33.35 ?  314 MET B N     1 
ATOM   8082  C  CA    . MET B 1 314 ? 109.537 150.008 138.018 1.00 26.39 ?  314 MET B CA    1 
ATOM   8083  C  C     . MET B 1 314 ? 110.034 150.071 139.456 1.00 33.28 ?  314 MET B C     1 
ATOM   8084  O  O     . MET B 1 314 ? 109.244 150.286 140.384 1.00 34.74 ?  314 MET B O     1 
ATOM   8085  C  CB    . MET B 1 314 ? 109.342 148.556 137.580 1.00 27.71 ?  314 MET B CB    1 
ATOM   8086  C  CG    . MET B 1 314 ? 108.183 147.855 138.268 1.00 31.62 ?  314 MET B CG    1 
ATOM   8087  S  SD    . MET B 1 314 ? 108.331 146.059 138.254 1.00 44.06 ?  314 MET B SD    1 
ATOM   8088  C  CE    . MET B 1 314 ? 109.377 145.814 136.825 1.00 28.34 ?  314 MET B CE    1 
ATOM   8089  N  N     . ASP B 1 315 ? 111.339 149.892 139.667 1.00 27.60 ?  315 ASP B N     1 
ATOM   8090  C  CA    . ASP B 1 315 ? 111.893 149.944 141.013 1.00 34.62 ?  315 ASP B CA    1 
ATOM   8091  C  C     . ASP B 1 315 ? 112.070 151.367 141.527 1.00 35.11 ?  315 ASP B C     1 
ATOM   8092  O  O     . ASP B 1 315 ? 112.406 151.544 142.703 1.00 37.21 ?  315 ASP B O     1 
ATOM   8093  C  CB    . ASP B 1 315 ? 113.235 149.211 141.065 1.00 34.05 ?  315 ASP B CB    1 
ATOM   8094  C  CG    . ASP B 1 315 ? 114.202 149.694 140.012 1.00 37.86 ?  315 ASP B CG    1 
ATOM   8095  O  OD1   . ASP B 1 315 ? 113.744 150.045 138.905 1.00 38.45 ?  315 ASP B OD1   1 
ATOM   8096  O  OD2   . ASP B 1 315 ? 115.419 149.723 140.289 1.00 33.67 -1 315 ASP B OD2   1 
ATOM   8097  N  N     . GLU B 1 316 ? 111.863 152.374 140.684 1.00 29.30 ?  316 GLU B N     1 
ATOM   8098  C  CA    . GLU B 1 316 ? 111.850 153.761 141.125 1.00 28.25 ?  316 GLU B CA    1 
ATOM   8099  C  C     . GLU B 1 316 ? 110.476 154.218 141.592 1.00 36.50 ?  316 GLU B C     1 
ATOM   8100  O  O     . GLU B 1 316 ? 110.354 155.330 142.117 1.00 34.14 ?  316 GLU B O     1 
ATOM   8101  C  CB    . GLU B 1 316 ? 112.333 154.681 139.998 1.00 34.22 ?  316 GLU B CB    1 
ATOM   8102  C  CG    . GLU B 1 316 ? 113.823 154.608 139.739 1.00 33.75 ?  316 GLU B CG    1 
ATOM   8103  C  CD    . GLU B 1 316 ? 114.640 154.936 140.969 1.00 39.66 ?  316 GLU B CD    1 
ATOM   8104  O  OE1   . GLU B 1 316 ? 114.429 156.019 141.552 1.00 42.72 ?  316 GLU B OE1   1 
ATOM   8105  O  OE2   . GLU B 1 316 ? 115.492 154.109 141.354 1.00 38.84 -1 316 GLU B OE2   1 
ATOM   8106  N  N     . MET B 1 317 ? 109.449 153.394 141.416 1.00 41.05 ?  317 MET B N     1 
ATOM   8107  C  CA    . MET B 1 317 ? 108.082 153.731 141.774 1.00 37.51 ?  317 MET B CA    1 
ATOM   8108  C  C     . MET B 1 317 ? 107.657 152.960 143.016 1.00 37.60 ?  317 MET B C     1 
ATOM   8109  O  O     . MET B 1 317 ? 108.286 151.975 143.412 1.00 40.83 ?  317 MET B O     1 
ATOM   8110  C  CB    . MET B 1 317 ? 107.122 153.427 140.619 1.00 36.80 ?  317 MET B CB    1 
ATOM   8111  C  CG    . MET B 1 317 ? 107.598 153.909 139.260 1.00 33.38 ?  317 MET B CG    1 
ATOM   8112  S  SD    . MET B 1 317 ? 106.275 153.928 138.039 1.00 47.15 ?  317 MET B SD    1 
ATOM   8113  C  CE    . MET B 1 317 ? 107.222 153.946 136.521 1.00 38.32 ?  317 MET B CE    1 
ATOM   8114  N  N     . ASP B 1 318 ? 106.571 153.425 143.629 1.00 42.01 ?  318 ASP B N     1 
ATOM   8115  C  CA    . ASP B 1 318 ? 106.021 152.784 144.818 1.00 41.09 ?  318 ASP B CA    1 
ATOM   8116  C  C     . ASP B 1 318 ? 105.149 151.612 144.385 1.00 41.95 ?  318 ASP B C     1 
ATOM   8117  O  O     . ASP B 1 318 ? 104.039 151.808 143.879 1.00 43.92 ?  318 ASP B O     1 
ATOM   8118  C  CB    . ASP B 1 318 ? 105.225 153.790 145.644 1.00 41.53 ?  318 ASP B CB    1 
ATOM   8119  C  CG    . ASP B 1 318 ? 104.708 153.202 146.939 1.00 49.87 ?  318 ASP B CG    1 
ATOM   8120  O  OD1   . ASP B 1 318 ? 105.335 152.255 147.458 1.00 49.03 ?  318 ASP B OD1   1 
ATOM   8121  O  OD2   . ASP B 1 318 ? 103.672 153.689 147.440 1.00 53.23 -1 318 ASP B OD2   1 
ATOM   8122  N  N     . MET B 1 319 ? 105.650 150.391 144.581 1.00 39.81 ?  319 MET B N     1 
ATOM   8123  C  CA    . MET B 1 319 ? 104.902 149.211 144.160 1.00 34.96 ?  319 MET B CA    1 
ATOM   8124  C  C     . MET B 1 319 ? 103.582 149.093 144.911 1.00 33.65 ?  319 MET B C     1 
ATOM   8125  O  O     . MET B 1 319 ? 102.555 148.742 144.321 1.00 37.42 ?  319 MET B O     1 
ATOM   8126  C  CB    . MET B 1 319 ? 105.747 147.954 144.361 1.00 38.21 ?  319 MET B CB    1 
ATOM   8127  C  CG    . MET B 1 319 ? 105.034 146.666 143.993 1.00 39.00 ?  319 MET B CG    1 
ATOM   8128  S  SD    . MET B 1 319 ? 104.303 146.703 142.345 1.00 44.45 ?  319 MET B SD    1 
ATOM   8129  C  CE    . MET B 1 319 ? 105.770 146.712 141.323 1.00 35.22 ?  319 MET B CE    1 
ATOM   8130  N  N     . ASN B 1 320 ? 103.587 149.393 146.211 1.00 44.15 ?  320 ASN B N     1 
ATOM   8131  C  CA    . ASN B 1 320 ? 102.368 149.265 147.001 1.00 44.56 ?  320 ASN B CA    1 
ATOM   8132  C  C     . ASN B 1 320 ? 101.238 150.115 146.436 1.00 43.48 ?  320 ASN B C     1 
ATOM   8133  O  O     . ASN B 1 320 ? 100.062 149.778 146.609 1.00 44.34 ?  320 ASN B O     1 
ATOM   8134  C  CB    . ASN B 1 320 ? 102.646 149.646 148.455 1.00 42.46 ?  320 ASN B CB    1 
ATOM   8135  C  CG    . ASN B 1 320 ? 103.491 148.615 149.176 1.00 45.56 ?  320 ASN B CG    1 
ATOM   8136  O  OD1   . ASN B 1 320 ? 104.255 147.877 148.554 1.00 41.93 ?  320 ASN B OD1   1 
ATOM   8137  N  ND2   . ASN B 1 320 ? 103.359 148.561 150.496 1.00 45.01 ?  320 ASN B ND2   1 
ATOM   8138  N  N     . GLU B 1 321 ? 101.571 151.212 145.761 1.00 44.61 ?  321 GLU B N     1 
ATOM   8139  C  CA    . GLU B 1 321 ? 100.578 152.088 145.149 1.00 44.17 ?  321 GLU B CA    1 
ATOM   8140  C  C     . GLU B 1 321 ? 100.401 151.840 143.659 1.00 45.45 ?  321 GLU B C     1 
ATOM   8141  O  O     . GLU B 1 321 ? 99.283  151.947 143.146 1.00 47.33 ?  321 GLU B O     1 
ATOM   8142  C  CB    . GLU B 1 321 ? 100.959 153.553 145.374 1.00 44.45 ?  321 GLU B CB    1 
ATOM   8143  C  CG    . GLU B 1 321 ? 100.239 154.528 144.457 1.00 47.40 ?  321 GLU B CG    1 
ATOM   8144  C  CD    . GLU B 1 321 ? 101.150 155.626 143.941 1.00 51.98 ?  321 GLU B CD    1 
ATOM   8145  O  OE1   . GLU B 1 321 ? 100.800 156.262 142.924 1.00 51.32 ?  321 GLU B OE1   1 
ATOM   8146  O  OE2   . GLU B 1 321 ? 102.216 155.853 144.552 1.00 48.45 -1 321 GLU B OE2   1 
ATOM   8147  N  N     . MET B 1 322 ? 101.476 151.508 142.950 1.00 40.34 ?  322 MET B N     1 
ATOM   8148  C  CA    . MET B 1 322 ? 101.449 151.400 141.499 1.00 35.55 ?  322 MET B CA    1 
ATOM   8149  C  C     . MET B 1 322 ? 101.161 149.992 140.996 1.00 36.47 ?  322 MET B C     1 
ATOM   8150  O  O     . MET B 1 322 ? 101.065 149.800 139.781 1.00 43.32 ?  322 MET B O     1 
ATOM   8151  C  CB    . MET B 1 322 ? 102.779 151.886 140.913 1.00 38.97 ?  322 MET B CB    1 
ATOM   8152  C  CG    . MET B 1 322 ? 103.133 153.316 141.278 1.00 40.69 ?  322 MET B CG    1 
ATOM   8153  S  SD    . MET B 1 322 ? 102.096 154.526 140.439 1.00 49.44 ?  322 MET B SD    1 
ATOM   8154  C  CE    . MET B 1 322 ? 102.128 153.898 138.764 1.00 37.96 ?  322 MET B CE    1 
ATOM   8155  N  N     . TYR B 1 323 ? 101.019 149.005 141.881 1.00 30.83 ?  323 TYR B N     1 
ATOM   8156  C  CA    . TYR B 1 323 ? 100.793 147.638 141.422 1.00 33.09 ?  323 TYR B CA    1 
ATOM   8157  C  C     . TYR B 1 323 ? 99.460  147.513 140.694 1.00 34.82 ?  323 TYR B C     1 
ATOM   8158  O  O     . TYR B 1 323 ? 99.381  146.923 139.610 1.00 38.11 ?  323 TYR B O     1 
ATOM   8159  C  CB    . TYR B 1 323 ? 100.855 146.671 142.605 1.00 32.65 ?  323 TYR B CB    1 
ATOM   8160  C  CG    . TYR B 1 323 ? 100.522 145.241 142.246 1.00 31.38 ?  323 TYR B CG    1 
ATOM   8161  C  CD1   . TYR B 1 323 ? 101.477 144.406 141.685 1.00 29.11 ?  323 TYR B CD1   1 
ATOM   8162  C  CD2   . TYR B 1 323 ? 99.252  144.727 142.468 1.00 30.69 ?  323 TYR B CD2   1 
ATOM   8163  C  CE1   . TYR B 1 323 ? 101.178 143.103 141.355 1.00 29.01 ?  323 TYR B CE1   1 
ATOM   8164  C  CE2   . TYR B 1 323 ? 98.945  143.424 142.142 1.00 29.46 ?  323 TYR B CE2   1 
ATOM   8165  C  CZ    . TYR B 1 323 ? 99.911  142.616 141.585 1.00 30.76 ?  323 TYR B CZ    1 
ATOM   8166  O  OH    . TYR B 1 323 ? 99.608  141.316 141.260 1.00 34.31 ?  323 TYR B OH    1 
ATOM   8167  N  N     . ASP B 1 324 ? 98.396  148.064 141.280 1.00 38.67 ?  324 ASP B N     1 
ATOM   8168  C  CA    . ASP B 1 324 ? 97.085  147.987 140.644 1.00 38.13 ?  324 ASP B CA    1 
ATOM   8169  C  C     . ASP B 1 324 ? 97.062  148.762 139.333 1.00 39.69 ?  324 ASP B C     1 
ATOM   8170  O  O     . ASP B 1 324 ? 96.453  148.319 138.354 1.00 43.58 ?  324 ASP B O     1 
ATOM   8171  C  CB    . ASP B 1 324 ? 96.009  148.501 141.597 1.00 40.78 ?  324 ASP B CB    1 
ATOM   8172  C  CG    . ASP B 1 324 ? 95.681  147.507 142.692 1.00 44.96 ?  324 ASP B CG    1 
ATOM   8173  O  OD1   . ASP B 1 324 ? 96.066  146.326 142.560 1.00 43.95 ?  324 ASP B OD1   1 
ATOM   8174  O  OD2   . ASP B 1 324 ? 95.039  147.905 143.687 1.00 47.92 -1 324 ASP B OD2   1 
ATOM   8175  N  N     . LYS B 1 325 ? 97.717  149.923 139.298 1.00 40.35 ?  325 LYS B N     1 
ATOM   8176  C  CA    . LYS B 1 325 ? 97.788  150.693 138.060 1.00 38.99 ?  325 LYS B CA    1 
ATOM   8177  C  C     . LYS B 1 325 ? 98.533  149.926 136.975 1.00 38.53 ?  325 LYS B C     1 
ATOM   8178  O  O     . LYS B 1 325 ? 98.124  149.932 135.809 1.00 43.75 ?  325 LYS B O     1 
ATOM   8179  C  CB    . LYS B 1 325 ? 98.450  152.045 138.321 1.00 41.04 ?  325 LYS B CB    1 
ATOM   8180  C  CG    . LYS B 1 325 ? 97.642  152.959 139.227 1.00 40.79 ?  325 LYS B CG    1 
ATOM   8181  C  CD    . LYS B 1 325 ? 98.314  154.310 139.397 1.00 41.41 ?  325 LYS B CD    1 
ATOM   8182  C  CE    . LYS B 1 325 ? 97.561  155.174 140.393 1.00 43.51 ?  325 LYS B CE    1 
ATOM   8183  N  NZ    . LYS B 1 325 ? 98.349  156.367 140.804 1.00 47.04 1  325 LYS B NZ    1 
ATOM   8184  N  N     . PHE B 1 326 ? 99.632  149.259 137.338 1.00 36.38 ?  326 PHE B N     1 
ATOM   8185  C  CA    . PHE B 1 326 ? 100.349 148.438 136.370 1.00 36.01 ?  326 PHE B CA    1 
ATOM   8186  C  C     . PHE B 1 326 ? 99.477  147.294 135.872 1.00 33.17 ?  326 PHE B C     1 
ATOM   8187  O  O     . PHE B 1 326 ? 99.477  146.974 134.678 1.00 39.01 ?  326 PHE B O     1 
ATOM   8188  C  CB    . PHE B 1 326 ? 101.633 147.885 136.991 1.00 32.40 ?  326 PHE B CB    1 
ATOM   8189  C  CG    . PHE B 1 326 ? 102.630 148.937 137.380 1.00 33.99 ?  326 PHE B CG    1 
ATOM   8190  C  CD1   . PHE B 1 326 ? 102.541 150.223 136.878 1.00 34.14 ?  326 PHE B CD1   1 
ATOM   8191  C  CD2   . PHE B 1 326 ? 103.661 148.635 138.252 1.00 34.59 ?  326 PHE B CD2   1 
ATOM   8192  C  CE1   . PHE B 1 326 ? 103.460 151.187 137.242 1.00 32.80 ?  326 PHE B CE1   1 
ATOM   8193  C  CE2   . PHE B 1 326 ? 104.583 149.594 138.616 1.00 37.39 ?  326 PHE B CE2   1 
ATOM   8194  C  CZ    . PHE B 1 326 ? 104.483 150.871 138.110 1.00 37.04 ?  326 PHE B CZ    1 
ATOM   8195  N  N     . VAL B 1 327 ? 98.730  146.660 136.777 1.00 34.23 ?  327 VAL B N     1 
ATOM   8196  C  CA    . VAL B 1 327 ? 97.885  145.538 136.385 1.00 38.56 ?  327 VAL B CA    1 
ATOM   8197  C  C     . VAL B 1 327 ? 96.756  145.999 135.473 1.00 40.65 ?  327 VAL B C     1 
ATOM   8198  O  O     . VAL B 1 327 ? 96.336  145.261 134.572 1.00 43.61 ?  327 VAL B O     1 
ATOM   8199  C  CB    . VAL B 1 327 ? 97.343  144.818 137.633 1.00 34.79 ?  327 VAL B CB    1 
ATOM   8200  C  CG1   . VAL B 1 327 ? 96.353  143.737 137.234 1.00 37.26 ?  327 VAL B CG1   1 
ATOM   8201  C  CG2   . VAL B 1 327 ? 98.485  144.224 138.436 1.00 31.11 ?  327 VAL B CG2   1 
ATOM   8202  N  N     . ASP B 1 328 ? 96.244  147.210 135.683 1.00 41.63 ?  328 ASP B N     1 
ATOM   8203  C  CA    . ASP B 1 328 ? 95.132  147.726 134.899 1.00 38.98 ?  328 ASP B CA    1 
ATOM   8204  C  C     . ASP B 1 328 ? 95.569  148.467 133.643 1.00 42.38 ?  328 ASP B C     1 
ATOM   8205  O  O     . ASP B 1 328 ? 94.710  148.866 132.851 1.00 45.08 ?  328 ASP B O     1 
ATOM   8206  C  CB    . ASP B 1 328 ? 94.271  148.657 135.760 1.00 37.32 ?  328 ASP B CB    1 
ATOM   8207  C  CG    . ASP B 1 328 ? 93.451  147.907 136.786 1.00 47.02 ?  328 ASP B CG    1 
ATOM   8208  O  OD1   . ASP B 1 328 ? 93.319  148.406 137.923 1.00 48.18 ?  328 ASP B OD1   1 
ATOM   8209  O  OD2   . ASP B 1 328 ? 92.938  146.816 136.457 1.00 47.25 -1 328 ASP B OD2   1 
ATOM   8210  N  N     . ASN B 1 329 ? 96.870  148.656 133.437 1.00 40.90 ?  329 ASN B N     1 
ATOM   8211  C  CA    . ASN B 1 329 ? 97.355  149.389 132.274 1.00 39.35 ?  329 ASN B CA    1 
ATOM   8212  C  C     . ASN B 1 329 ? 97.572  148.429 131.114 1.00 40.86 ?  329 ASN B C     1 
ATOM   8213  O  O     . ASN B 1 329 ? 98.421  147.534 131.218 1.00 40.80 ?  329 ASN B O     1 
ATOM   8214  C  CB    . ASN B 1 329 ? 98.649  150.114 132.599 1.00 35.27 ?  329 ASN B CB    1 
ATOM   8215  C  CG    . ASN B 1 329 ? 98.968  151.206 131.602 1.00 38.52 ?  329 ASN B CG    1 
ATOM   8216  O  OD1   . ASN B 1 329 ? 99.057  150.958 130.401 1.00 45.56 ?  329 ASN B OD1   1 
ATOM   8217  N  ND2   . ASN B 1 329 ? 99.143  152.425 132.095 1.00 38.14 ?  329 ASN B ND2   1 
ATOM   8218  N  N     . PRO B 1 330 ? 96.842  148.569 130.004 1.00 42.59 ?  330 PRO B N     1 
ATOM   8219  C  CA    . PRO B 1 330 ? 97.057  147.661 128.867 1.00 39.90 ?  330 PRO B CA    1 
ATOM   8220  C  C     . PRO B 1 330 ? 98.421  147.809 128.219 1.00 38.78 ?  330 PRO B C     1 
ATOM   8221  O  O     . PRO B 1 330 ? 98.894  146.856 127.589 1.00 41.12 ?  330 PRO B O     1 
ATOM   8222  C  CB    . PRO B 1 330 ? 95.934  148.044 127.897 1.00 39.33 ?  330 PRO B CB    1 
ATOM   8223  C  CG    . PRO B 1 330 ? 95.641  149.468 128.222 1.00 38.66 ?  330 PRO B CG    1 
ATOM   8224  C  CD    . PRO B 1 330 ? 95.830  149.596 129.707 1.00 38.23 ?  330 PRO B CD    1 
ATOM   8225  N  N     . ARG B 1 331 ? 99.065  148.965 128.351 1.00 39.76 ?  331 ARG B N     1 
ATOM   8226  C  CA    . ARG B 1 331 ? 100.368 149.209 127.753 1.00 38.93 ?  331 ARG B CA    1 
ATOM   8227  C  C     . ARG B 1 331 ? 101.515 148.683 128.603 1.00 38.09 ?  331 ARG B C     1 
ATOM   8228  O  O     . ARG B 1 331 ? 102.675 148.796 128.194 1.00 38.70 ?  331 ARG B O     1 
ATOM   8229  C  CB    . ARG B 1 331 ? 100.556 150.707 127.499 1.00 38.97 ?  331 ARG B CB    1 
ATOM   8230  C  CG    . ARG B 1 331 ? 100.061 151.168 126.140 1.00 40.30 ?  331 ARG B CG    1 
ATOM   8231  C  CD    . ARG B 1 331 ? 99.274  152.460 126.257 1.00 41.83 ?  331 ARG B CD    1 
ATOM   8232  N  NE    . ARG B 1 331 ? 98.211  152.357 127.249 1.00 42.04 ?  331 ARG B NE    1 
ATOM   8233  C  CZ    . ARG B 1 331 ? 97.880  153.323 128.094 1.00 42.47 ?  331 ARG B CZ    1 
ATOM   8234  N  NH1   . ARG B 1 331 ? 98.510  154.486 128.095 1.00 43.60 1  331 ARG B NH1   1 
ATOM   8235  N  NH2   . ARG B 1 331 ? 96.892  153.118 128.960 1.00 40.30 ?  331 ARG B NH2   1 
ATOM   8236  N  N     . VAL B 1 332 ? 101.221 148.120 129.771 1.00 33.10 ?  332 VAL B N     1 
ATOM   8237  C  CA    . VAL B 1 332 ? 102.220 147.504 130.636 1.00 34.26 ?  332 VAL B CA    1 
ATOM   8238  C  C     . VAL B 1 332 ? 102.075 145.996 130.505 1.00 35.23 ?  332 VAL B C     1 
ATOM   8239  O  O     . VAL B 1 332 ? 100.992 145.445 130.744 1.00 35.12 ?  332 VAL B O     1 
ATOM   8240  C  CB    . VAL B 1 332 ? 102.063 147.949 132.098 1.00 33.10 ?  332 VAL B CB    1 
ATOM   8241  C  CG1   . VAL B 1 332 ? 102.925 147.088 133.010 1.00 30.16 ?  332 VAL B CG1   1 
ATOM   8242  C  CG2   . VAL B 1 332 ? 102.423 149.418 132.250 1.00 31.42 ?  332 VAL B CG2   1 
ATOM   8243  N  N     . LYS B 1 333 ? 103.158 145.329 130.123 1.00 35.77 ?  333 LYS B N     1 
ATOM   8244  C  CA    . LYS B 1 333 ? 103.162 143.882 129.982 1.00 28.47 ?  333 LYS B CA    1 
ATOM   8245  C  C     . LYS B 1 333 ? 103.475 143.231 131.321 1.00 29.81 ?  333 LYS B C     1 
ATOM   8246  O  O     . LYS B 1 333 ? 104.372 143.672 132.045 1.00 35.54 ?  333 LYS B O     1 
ATOM   8247  C  CB    . LYS B 1 333 ? 104.182 143.447 128.928 1.00 27.74 ?  333 LYS B CB    1 
ATOM   8248  C  CG    . LYS B 1 333 ? 103.972 142.040 128.396 1.00 34.16 ?  333 LYS B CG    1 
ATOM   8249  C  CD    . LYS B 1 333 ? 105.060 141.660 127.407 1.00 32.56 ?  333 LYS B CD    1 
ATOM   8250  C  CE    . LYS B 1 333 ? 104.868 140.244 126.892 1.00 35.52 ?  333 LYS B CE    1 
ATOM   8251  N  NZ    . LYS B 1 333 ? 105.923 139.865 125.912 1.00 41.63 1  333 LYS B NZ    1 
ATOM   8252  N  N     . LYS B 1 334 ? 102.729 142.179 131.647 1.00 32.18 ?  334 LYS B N     1 
ATOM   8253  C  CA    . LYS B 1 334 ? 102.880 141.510 132.928 1.00 29.24 ?  334 LYS B CA    1 
ATOM   8254  C  C     . LYS B 1 334 ? 102.596 140.027 132.755 1.00 33.45 ?  334 LYS B C     1 
ATOM   8255  O  O     . LYS B 1 334 ? 101.908 139.610 131.820 1.00 38.30 ?  334 LYS B O     1 
ATOM   8256  C  CB    . LYS B 1 334 ? 101.953 142.116 133.988 1.00 33.66 ?  334 LYS B CB    1 
ATOM   8257  C  CG    . LYS B 1 334 ? 100.477 141.916 133.708 1.00 33.14 ?  334 LYS B CG    1 
ATOM   8258  C  CD    . LYS B 1 334 ? 99.695  143.194 133.946 1.00 31.85 ?  334 LYS B CD    1 
ATOM   8259  C  CE    . LYS B 1 334 ? 99.460  143.942 132.647 1.00 35.68 ?  334 LYS B CE    1 
ATOM   8260  N  NZ    . LYS B 1 334 ? 99.002  145.339 132.873 1.00 34.45 1  334 LYS B NZ    1 
ATOM   8261  N  N     . GLU B 1 335 ? 103.138 139.232 133.674 1.00 35.26 ?  335 GLU B N     1 
ATOM   8262  C  CA    . GLU B 1 335 ? 102.993 137.785 133.659 1.00 32.76 ?  335 GLU B CA    1 
ATOM   8263  C  C     . GLU B 1 335 ? 102.365 137.329 134.967 1.00 34.49 ?  335 GLU B C     1 
ATOM   8264  O  O     . GLU B 1 335 ? 102.848 137.682 136.048 1.00 42.46 ?  335 GLU B O     1 
ATOM   8265  C  CB    . GLU B 1 335 ? 104.349 137.103 133.456 1.00 35.59 ?  335 GLU B CB    1 
ATOM   8266  C  CG    . GLU B 1 335 ? 104.263 135.659 133.004 1.00 37.32 ?  335 GLU B CG    1 
ATOM   8267  C  CD    . GLU B 1 335 ? 105.616 134.973 132.981 1.00 43.51 ?  335 GLU B CD    1 
ATOM   8268  O  OE1   . GLU B 1 335 ? 106.645 135.681 132.971 1.00 36.14 ?  335 GLU B OE1   1 
ATOM   8269  O  OE2   . GLU B 1 335 ? 105.650 133.725 132.975 1.00 49.28 -1 335 GLU B OE2   1 
ATOM   8270  N  N     . LYS B 1 336 ? 101.292 136.550 134.868 1.00 33.30 ?  336 LYS B N     1 
ATOM   8271  C  CA    . LYS B 1 336 ? 100.641 136.027 136.060 1.00 31.66 ?  336 LYS B CA    1 
ATOM   8272  C  C     . LYS B 1 336 ? 101.550 135.036 136.774 1.00 33.16 ?  336 LYS B C     1 
ATOM   8273  O  O     . LYS B 1 336 ? 102.189 134.188 136.146 1.00 35.59 ?  336 LYS B O     1 
ATOM   8274  C  CB    . LYS B 1 336 ? 99.318  135.356 135.693 1.00 36.15 ?  336 LYS B CB    1 
ATOM   8275  C  CG    . LYS B 1 336 ? 98.393  135.118 136.875 1.00 37.74 ?  336 LYS B CG    1 
ATOM   8276  C  CD    . LYS B 1 336 ? 98.327  133.643 137.234 1.00 36.67 ?  336 LYS B CD    1 
ATOM   8277  C  CE    . LYS B 1 336 ? 98.179  133.444 138.734 1.00 39.32 ?  336 LYS B CE    1 
ATOM   8278  N  NZ    . LYS B 1 336 ? 98.184  132.004 139.116 1.00 34.60 1  336 LYS B NZ    1 
ATOM   8279  N  N     . ILE B 1 337 ? 101.607 135.150 138.100 1.00 34.12 ?  337 ILE B N     1 
ATOM   8280  C  CA    . ILE B 1 337 ? 102.408 134.271 138.941 1.00 32.58 ?  337 ILE B CA    1 
ATOM   8281  C  C     . ILE B 1 337 ? 101.585 133.878 140.161 1.00 31.43 ?  337 ILE B C     1 
ATOM   8282  O  O     . ILE B 1 337 ? 100.541 134.462 140.451 1.00 38.39 ?  337 ILE B O     1 
ATOM   8283  C  CB    . ILE B 1 337 ? 103.734 134.925 139.383 1.00 30.85 ?  337 ILE B CB    1 
ATOM   8284  C  CG1   . ILE B 1 337 ? 103.456 136.118 140.300 1.00 32.57 ?  337 ILE B CG1   1 
ATOM   8285  C  CG2   . ILE B 1 337 ? 104.548 135.351 138.174 1.00 32.14 ?  337 ILE B CG2   1 
ATOM   8286  C  CD1   . ILE B 1 337 ? 104.493 136.317 141.376 1.00 30.24 ?  337 ILE B CD1   1 
ATOM   8287  N  N     . ASN B 1 338 ? 102.073 132.867 140.876 1.00 35.65 ?  338 ASN B N     1 
ATOM   8288  C  CA    . ASN B 1 338 ? 101.490 132.481 142.150 1.00 35.68 ?  338 ASN B CA    1 
ATOM   8289  C  C     . ASN B 1 338 ? 102.398 132.983 143.261 1.00 33.34 ?  338 ASN B C     1 
ATOM   8290  O  O     . ASN B 1 338 ? 103.497 132.437 143.440 1.00 36.63 ?  338 ASN B O     1 
ATOM   8291  C  CB    . ASN B 1 338 ? 101.326 130.966 142.235 1.00 33.54 ?  338 ASN B CB    1 
ATOM   8292  C  CG    . ASN B 1 338 ? 100.426 130.540 143.377 1.00 38.56 ?  338 ASN B CG    1 
ATOM   8293  O  OD1   . ASN B 1 338 ? 100.644 130.914 144.528 1.00 37.74 ?  338 ASN B OD1   1 
ATOM   8294  N  ND2   . ASN B 1 338 ? 99.405  129.754 143.062 1.00 38.81 ?  338 ASN B ND2   1 
ATOM   8295  N  N     . PRO B 1 339 ? 102.004 134.011 144.017 1.00 34.93 ?  339 PRO B N     1 
ATOM   8296  C  CA    . PRO B 1 339 ? 102.923 134.558 145.030 1.00 31.65 ?  339 PRO B CA    1 
ATOM   8297  C  C     . PRO B 1 339 ? 103.347 133.545 146.080 1.00 31.80 ?  339 PRO B C     1 
ATOM   8298  O  O     . PRO B 1 339 ? 104.512 133.543 146.495 1.00 34.62 ?  339 PRO B O     1 
ATOM   8299  C  CB    . PRO B 1 339 ? 102.120 135.716 145.637 1.00 34.58 ?  339 PRO B CB    1 
ATOM   8300  C  CG    . PRO B 1 339 ? 100.692 135.393 145.336 1.00 36.73 ?  339 PRO B CG    1 
ATOM   8301  C  CD    . PRO B 1 339 ? 100.706 134.704 144.011 1.00 35.88 ?  339 PRO B CD    1 
ATOM   8302  N  N     . ARG B 1 340 ? 102.436 132.676 146.523 1.00 36.07 ?  340 ARG B N     1 
ATOM   8303  C  CA    . ARG B 1 340 ? 102.809 131.679 147.520 1.00 29.21 ?  340 ARG B CA    1 
ATOM   8304  C  C     . ARG B 1 340 ? 103.744 130.634 146.930 1.00 30.63 ?  340 ARG B C     1 
ATOM   8305  O  O     . ARG B 1 340 ? 104.656 130.151 147.611 1.00 37.82 ?  340 ARG B O     1 
ATOM   8306  C  CB    . ARG B 1 340 ? 101.562 131.021 148.107 1.00 28.55 ?  340 ARG B CB    1 
ATOM   8307  C  CG    . ARG B 1 340 ? 100.751 131.955 148.976 1.00 32.05 ?  340 ARG B CG    1 
ATOM   8308  C  CD    . ARG B 1 340 ? 99.816  131.205 149.898 1.00 28.36 ?  340 ARG B CD    1 
ATOM   8309  N  NE    . ARG B 1 340 ? 98.958  132.128 150.628 1.00 35.17 ?  340 ARG B NE    1 
ATOM   8310  C  CZ    . ARG B 1 340 ? 98.016  131.764 151.484 1.00 35.59 ?  340 ARG B CZ    1 
ATOM   8311  N  NH1   . ARG B 1 340 ? 97.782  130.490 151.751 1.00 33.02 1  340 ARG B NH1   1 
ATOM   8312  N  NH2   . ARG B 1 340 ? 97.291  132.699 152.087 1.00 34.96 ?  340 ARG B NH2   1 
ATOM   8313  N  N     . LYS B 1 341 ? 103.541 130.274 145.663 1.00 33.14 ?  341 LYS B N     1 
ATOM   8314  C  CA    . LYS B 1 341 ? 104.477 129.372 145.005 1.00 31.41 ?  341 LYS B CA    1 
ATOM   8315  C  C     . LYS B 1 341 ? 105.860 130.000 144.908 1.00 28.60 ?  341 LYS B C     1 
ATOM   8316  O  O     . LYS B 1 341 ? 106.872 129.318 145.093 1.00 36.30 ?  341 LYS B O     1 
ATOM   8317  C  CB    . LYS B 1 341 ? 103.958 128.985 143.623 1.00 37.77 ?  341 LYS B CB    1 
ATOM   8318  C  CG    . LYS B 1 341 ? 103.307 127.616 143.575 1.00 35.05 ?  341 LYS B CG    1 
ATOM   8319  C  CD    . LYS B 1 341 ? 103.200 127.110 142.150 1.00 36.20 ?  341 LYS B CD    1 
ATOM   8320  C  CE    . LYS B 1 341 ? 104.496 127.337 141.391 1.00 36.30 ?  341 LYS B CE    1 
ATOM   8321  N  NZ    . LYS B 1 341 ? 104.288 127.330 139.919 1.00 37.55 1  341 LYS B NZ    1 
ATOM   8322  N  N     . LEU B 1 342 ? 105.925 131.302 144.620 1.00 25.64 ?  342 LEU B N     1 
ATOM   8323  C  CA    . LEU B 1 342 ? 107.214 131.987 144.578 1.00 26.84 ?  342 LEU B CA    1 
ATOM   8324  C  C     . LEU B 1 342 ? 107.864 132.031 145.957 1.00 25.53 ?  342 LEU B C     1 
ATOM   8325  O  O     . LEU B 1 342 ? 109.081 131.852 146.083 1.00 31.95 ?  342 LEU B O     1 
ATOM   8326  C  CB    . LEU B 1 342 ? 107.037 133.397 144.017 1.00 29.04 ?  342 LEU B CB    1 
ATOM   8327  C  CG    . LEU B 1 342 ? 108.313 134.176 143.698 1.00 27.45 ?  342 LEU B CG    1 
ATOM   8328  C  CD1   . LEU B 1 342 ? 109.269 133.328 142.877 1.00 25.48 ?  342 LEU B CD1   1 
ATOM   8329  C  CD2   . LEU B 1 342 ? 107.978 135.465 142.969 1.00 26.16 ?  342 LEU B CD2   1 
ATOM   8330  N  N     . LEU B 1 343 ? 107.072 132.270 147.004 1.00 28.69 ?  343 LEU B N     1 
ATOM   8331  C  CA    . LEU B 1 343 ? 107.611 132.244 148.359 1.00 24.58 ?  343 LEU B CA    1 
ATOM   8332  C  C     . LEU B 1 343 ? 108.173 130.869 148.702 1.00 29.71 ?  343 LEU B C     1 
ATOM   8333  O  O     . LEU B 1 343 ? 109.264 130.756 149.275 1.00 33.17 ?  343 LEU B O     1 
ATOM   8334  C  CB    . LEU B 1 343 ? 106.528 132.643 149.359 1.00 26.68 ?  343 LEU B CB    1 
ATOM   8335  C  CG    . LEU B 1 343 ? 106.576 134.077 149.883 1.00 32.46 ?  343 LEU B CG    1 
ATOM   8336  C  CD1   . LEU B 1 343 ? 105.555 134.273 150.990 1.00 27.63 ?  343 LEU B CD1   1 
ATOM   8337  C  CD2   . LEU B 1 343 ? 107.975 134.415 150.370 1.00 31.72 ?  343 LEU B CD2   1 
ATOM   8338  N  N     . GLU B 1 344 ? 107.436 129.811 148.361 1.00 36.15 ?  344 GLU B N     1 
ATOM   8339  C  CA    . GLU B 1 344 ? 107.902 128.458 148.643 1.00 31.00 ?  344 GLU B CA    1 
ATOM   8340  C  C     . GLU B 1 344 ? 109.137 128.118 147.819 1.00 27.49 ?  344 GLU B C     1 
ATOM   8341  O  O     . GLU B 1 344 ? 110.027 127.402 148.290 1.00 35.90 ?  344 GLU B O     1 
ATOM   8342  C  CB    . GLU B 1 344 ? 106.776 127.460 148.382 1.00 32.41 ?  344 GLU B CB    1 
ATOM   8343  C  CG    . GLU B 1 344 ? 105.525 127.737 149.199 1.00 34.14 ?  344 GLU B CG    1 
ATOM   8344  C  CD    . GLU B 1 344 ? 104.282 127.115 148.595 1.00 41.96 ?  344 GLU B CD    1 
ATOM   8345  O  OE1   . GLU B 1 344 ? 104.345 126.669 147.431 1.00 42.09 ?  344 GLU B OE1   1 
ATOM   8346  O  OE2   . GLU B 1 344 ? 103.241 127.077 149.283 1.00 39.34 -1 344 GLU B OE2   1 
ATOM   8347  N  N     . LYS B 1 345 ? 109.209 128.622 146.586 1.00 26.71 ?  345 LYS B N     1 
ATOM   8348  C  CA    . LYS B 1 345 ? 110.409 128.441 145.778 1.00 25.53 ?  345 LYS B CA    1 
ATOM   8349  C  C     . LYS B 1 345 ? 111.606 129.126 146.420 1.00 29.35 ?  345 LYS B C     1 
ATOM   8350  O  O     . LYS B 1 345 ? 112.707 128.568 146.448 1.00 33.79 ?  345 LYS B O     1 
ATOM   8351  C  CB    . LYS B 1 345 ? 110.174 128.980 144.367 1.00 27.37 ?  345 LYS B CB    1 
ATOM   8352  C  CG    . LYS B 1 345 ? 111.379 128.875 143.451 1.00 27.21 ?  345 LYS B CG    1 
ATOM   8353  C  CD    . LYS B 1 345 ? 111.042 129.342 142.049 1.00 29.89 ?  345 LYS B CD    1 
ATOM   8354  C  CE    . LYS B 1 345 ? 112.239 129.214 141.124 1.00 33.64 ?  345 LYS B CE    1 
ATOM   8355  N  NZ    . LYS B 1 345 ? 111.908 129.616 139.732 1.00 35.71 1  345 LYS B NZ    1 
ATOM   8356  N  N     . LEU B 1 346 ? 111.408 130.338 146.941 1.00 30.43 ?  346 LEU B N     1 
ATOM   8357  C  CA    . LEU B 1 346 ? 112.481 131.017 147.660 1.00 24.40 ?  346 LEU B CA    1 
ATOM   8358  C  C     . LEU B 1 346 ? 112.927 130.203 148.866 1.00 24.07 ?  346 LEU B C     1 
ATOM   8359  O  O     . LEU B 1 346 ? 114.129 130.049 149.113 1.00 25.69 ?  346 LEU B O     1 
ATOM   8360  C  CB    . LEU B 1 346 ? 112.024 132.407 148.101 1.00 24.07 ?  346 LEU B CB    1 
ATOM   8361  C  CG    . LEU B 1 346 ? 111.838 133.469 147.020 1.00 27.02 ?  346 LEU B CG    1 
ATOM   8362  C  CD1   . LEU B 1 346 ? 111.277 134.739 147.631 1.00 27.55 ?  346 LEU B CD1   1 
ATOM   8363  C  CD2   . LEU B 1 346 ? 113.148 133.747 146.310 1.00 26.09 ?  346 LEU B CD2   1 
ATOM   8364  N  N     . ALA B 1 347 ? 111.969 129.673 149.627 1.00 27.71 ?  347 ALA B N     1 
ATOM   8365  C  CA    . ALA B 1 347 ? 112.314 128.883 150.805 1.00 25.06 ?  347 ALA B CA    1 
ATOM   8366  C  C     . ALA B 1 347 ? 113.097 127.631 150.425 1.00 30.53 ?  347 ALA B C     1 
ATOM   8367  O  O     . ALA B 1 347 ? 114.099 127.298 151.069 1.00 35.78 ?  347 ALA B O     1 
ATOM   8368  C  CB    . ALA B 1 347 ? 111.049 128.511 151.577 1.00 25.87 ?  347 ALA B CB    1 
ATOM   8369  N  N     . MET B 1 348 ? 112.661 126.928 149.379 1.00 32.38 ?  348 MET B N     1 
ATOM   8370  C  CA    . MET B 1 348 ? 113.357 125.714 148.968 1.00 31.00 ?  348 MET B CA    1 
ATOM   8371  C  C     . MET B 1 348 ? 114.746 126.028 148.424 1.00 30.50 ?  348 MET B C     1 
ATOM   8372  O  O     . MET B 1 348 ? 115.703 125.291 148.691 1.00 32.57 ?  348 MET B O     1 
ATOM   8373  C  CB    . MET B 1 348 ? 112.527 124.955 147.932 1.00 32.60 ?  348 MET B CB    1 
ATOM   8374  C  CG    . MET B 1 348 ? 112.532 125.574 146.545 1.00 38.10 ?  348 MET B CG    1 
ATOM   8375  S  SD    . MET B 1 348 ? 113.616 124.717 145.388 1.00 54.11 ?  348 MET B SD    1 
ATOM   8376  C  CE    . MET B 1 348 ? 113.579 125.841 143.993 1.00 34.43 ?  348 MET B CE    1 
ATOM   8377  N  N     . LEU B 1 349 ? 114.878 127.116 147.663 1.00 31.09 ?  349 LEU B N     1 
ATOM   8378  C  CA    . LEU B 1 349 ? 116.184 127.495 147.140 1.00 27.14 ?  349 LEU B CA    1 
ATOM   8379  C  C     . LEU B 1 349 ? 117.134 127.880 148.264 1.00 27.69 ?  349 LEU B C     1 
ATOM   8380  O  O     . LEU B 1 349 ? 118.329 127.571 148.208 1.00 28.78 ?  349 LEU B O     1 
ATOM   8381  C  CB    . LEU B 1 349 ? 116.034 128.643 146.145 1.00 27.70 ?  349 LEU B CB    1 
ATOM   8382  C  CG    . LEU B 1 349 ? 117.116 128.745 145.070 1.00 33.11 ?  349 LEU B CG    1 
ATOM   8383  C  CD1   . LEU B 1 349 ? 116.630 128.129 143.770 1.00 34.14 ?  349 LEU B CD1   1 
ATOM   8384  C  CD2   . LEU B 1 349 ? 117.536 130.193 144.863 1.00 32.64 ?  349 LEU B CD2   1 
ATOM   8385  N  N     . ARG B 1 350 ? 116.623 128.556 149.295 1.00 26.66 ?  350 ARG B N     1 
ATOM   8386  C  CA    . ARG B 1 350 ? 117.465 128.900 150.435 1.00 21.97 ?  350 ARG B CA    1 
ATOM   8387  C  C     . ARG B 1 350 ? 117.856 127.659 151.224 1.00 30.07 ?  350 ARG B C     1 
ATOM   8388  O  O     . ARG B 1 350 ? 118.986 127.556 151.711 1.00 33.38 ?  350 ARG B O     1 
ATOM   8389  C  CB    . ARG B 1 350 ? 116.744 129.905 151.331 1.00 19.95 ?  350 ARG B CB    1 
ATOM   8390  C  CG    . ARG B 1 350 ? 116.401 131.209 150.638 1.00 25.27 ?  350 ARG B CG    1 
ATOM   8391  C  CD    . ARG B 1 350 ? 115.840 132.218 151.615 1.00 25.83 ?  350 ARG B CD    1 
ATOM   8392  N  NE    . ARG B 1 350 ? 116.900 132.801 152.428 1.00 38.19 ?  350 ARG B NE    1 
ATOM   8393  C  CZ    . ARG B 1 350 ? 116.755 133.184 153.687 1.00 32.23 ?  350 ARG B CZ    1 
ATOM   8394  N  NH1   . ARG B 1 350 ? 115.593 133.087 154.310 1.00 29.86 1  350 ARG B NH1   1 
ATOM   8395  N  NH2   . ARG B 1 350 ? 117.805 133.675 154.339 1.00 28.74 ?  350 ARG B NH2   1 
ATOM   8396  N  N     . SER B 1 351 ? 116.932 126.707 151.363 1.00 35.52 ?  351 SER B N     1 
ATOM   8397  C  CA    . SER B 1 351 ? 117.259 125.461 152.047 1.00 31.15 ?  351 SER B CA    1 
ATOM   8398  C  C     . SER B 1 351 ? 118.336 124.689 151.298 1.00 35.41 ?  351 SER B C     1 
ATOM   8399  O  O     . SER B 1 351 ? 119.248 124.124 151.912 1.00 42.58 ?  351 SER B O     1 
ATOM   8400  C  CB    . SER B 1 351 ? 116.002 124.607 152.207 1.00 32.65 ?  351 SER B CB    1 
ATOM   8401  O  OG    . SER B 1 351 ? 115.274 124.984 153.362 1.00 46.43 ?  351 SER B OG    1 
ATOM   8402  N  N     . GLU B 1 352 ? 118.245 124.646 149.968 1.00 33.71 ?  352 GLU B N     1 
ATOM   8403  C  CA    . GLU B 1 352 ? 119.196 123.861 149.189 1.00 32.65 ?  352 GLU B CA    1 
ATOM   8404  C  C     . GLU B 1 352 ? 120.551 124.553 149.072 1.00 35.54 ?  352 GLU B C     1 
ATOM   8405  O  O     . GLU B 1 352 ? 121.593 123.895 149.152 1.00 39.99 ?  352 GLU B O     1 
ATOM   8406  C  CB    . GLU B 1 352 ? 118.625 123.568 147.802 1.00 34.18 ?  352 GLU B CB    1 
ATOM   8407  C  CG    . GLU B 1 352 ? 119.334 124.290 146.671 1.00 39.71 ?  352 GLU B CG    1 
ATOM   8408  C  CD    . GLU B 1 352 ? 118.578 124.214 145.362 1.00 43.24 ?  352 GLU B CD    1 
ATOM   8409  O  OE1   . GLU B 1 352 ? 117.686 123.348 145.238 1.00 42.47 ?  352 GLU B OE1   1 
ATOM   8410  O  OE2   . GLU B 1 352 ? 118.878 125.019 144.456 1.00 42.15 -1 352 GLU B OE2   1 
ATOM   8411  N  N     . SER B 1 353 ? 120.562 125.875 148.885 1.00 35.25 ?  353 SER B N     1 
ATOM   8412  C  CA    . SER B 1 353 ? 121.796 126.606 148.633 1.00 31.52 ?  353 SER B CA    1 
ATOM   8413  C  C     . SER B 1 353 ? 122.022 127.800 149.548 1.00 26.89 ?  353 SER B C     1 
ATOM   8414  O  O     . SER B 1 353 ? 123.126 128.353 149.537 1.00 33.67 ?  353 SER B O     1 
ATOM   8415  C  CB    . SER B 1 353 ? 121.841 127.093 147.177 1.00 34.13 ?  353 SER B CB    1 
ATOM   8416  O  OG    . SER B 1 353 ? 120.891 128.120 146.950 1.00 35.87 ?  353 SER B OG    1 
ATOM   8417  N  N     . GLY B 1 354 ? 121.028 128.217 150.329 1.00 25.74 ?  354 GLY B N     1 
ATOM   8418  C  CA    . GLY B 1 354 ? 121.148 129.399 151.152 1.00 27.31 ?  354 GLY B CA    1 
ATOM   8419  C  C     . GLY B 1 354 ? 120.802 130.698 150.458 1.00 24.29 ?  354 GLY B C     1 
ATOM   8420  O  O     . GLY B 1 354 ? 120.802 131.748 151.110 1.00 27.63 ?  354 GLY B O     1 
ATOM   8421  N  N     . TYR B 1 355 ? 120.512 130.660 149.165 1.00 27.88 ?  355 TYR B N     1 
ATOM   8422  C  CA    . TYR B 1 355 ? 120.128 131.822 148.385 1.00 18.23 ?  355 TYR B CA    1 
ATOM   8423  C  C     . TYR B 1 355 ? 118.639 131.792 148.074 1.00 22.56 ?  355 TYR B C     1 
ATOM   8424  O  O     . TYR B 1 355 ? 117.999 130.738 148.141 1.00 32.04 ?  355 TYR B O     1 
ATOM   8425  C  CB    . TYR B 1 355 ? 120.916 131.890 147.070 1.00 26.40 ?  355 TYR B CB    1 
ATOM   8426  C  CG    . TYR B 1 355 ? 122.398 132.119 147.248 1.00 30.52 ?  355 TYR B CG    1 
ATOM   8427  C  CD1   . TYR B 1 355 ? 122.878 133.316 147.761 1.00 20.53 ?  355 TYR B CD1   1 
ATOM   8428  C  CD2   . TYR B 1 355 ? 123.317 131.142 146.892 1.00 26.62 ?  355 TYR B CD2   1 
ATOM   8429  C  CE1   . TYR B 1 355 ? 124.232 133.530 147.921 1.00 24.63 ?  355 TYR B CE1   1 
ATOM   8430  C  CE2   . TYR B 1 355 ? 124.670 131.347 147.047 1.00 24.77 ?  355 TYR B CE2   1 
ATOM   8431  C  CZ    . TYR B 1 355 ? 125.123 132.541 147.561 1.00 26.55 ?  355 TYR B CZ    1 
ATOM   8432  O  OH    . TYR B 1 355 ? 126.473 132.746 147.715 1.00 30.94 ?  355 TYR B OH    1 
ATOM   8433  N  N     . PRO B 1 356 ? 118.051 132.938 147.728 1.00 24.60 ?  356 PRO B N     1 
ATOM   8434  C  CA    . PRO B 1 356 ? 118.663 134.268 147.634 1.00 12.86 ?  356 PRO B CA    1 
ATOM   8435  C  C     . PRO B 1 356 ? 118.681 135.010 148.966 1.00 16.56 ?  356 PRO B C     1 
ATOM   8436  O  O     . PRO B 1 356 ? 118.042 134.592 149.927 1.00 23.01 ?  356 PRO B O     1 
ATOM   8437  C  CB    . PRO B 1 356 ? 117.764 134.972 146.614 1.00 17.42 ?  356 PRO B CB    1 
ATOM   8438  C  CG    . PRO B 1 356 ? 116.407 134.401 146.902 1.00 22.21 ?  356 PRO B CG    1 
ATOM   8439  C  CD    . PRO B 1 356 ? 116.655 132.951 147.255 1.00 19.89 ?  356 PRO B CD    1 
ATOM   8440  N  N     . TYR B 1 357 ? 119.418 136.114 149.052 1.00 21.42 ?  357 TYR B N     1 
ATOM   8441  C  CA    . TYR B 1 357 ? 119.224 137.042 150.153 1.00 15.45 ?  357 TYR B CA    1 
ATOM   8442  C  C     . TYR B 1 357 ? 117.847 137.683 150.034 1.00 16.10 ?  357 TYR B C     1 
ATOM   8443  O  O     . TYR B 1 357 ? 117.341 137.915 148.934 1.00 20.78 ?  357 TYR B O     1 
ATOM   8444  C  CB    . TYR B 1 357 ? 120.299 138.129 150.154 1.00 11.98 ?  357 TYR B CB    1 
ATOM   8445  C  CG    . TYR B 1 357 ? 121.716 137.630 149.994 1.00 14.29 ?  357 TYR B CG    1 
ATOM   8446  C  CD1   . TYR B 1 357 ? 122.094 136.387 150.474 1.00 14.00 ?  357 TYR B CD1   1 
ATOM   8447  C  CD2   . TYR B 1 357 ? 122.678 138.409 149.368 1.00 16.82 ?  357 TYR B CD2   1 
ATOM   8448  C  CE1   . TYR B 1 357 ? 123.387 135.930 150.334 1.00 17.50 ?  357 TYR B CE1   1 
ATOM   8449  C  CE2   . TYR B 1 357 ? 123.975 137.961 149.222 1.00 15.86 ?  357 TYR B CE2   1 
ATOM   8450  C  CZ    . TYR B 1 357 ? 124.323 136.721 149.707 1.00 19.47 ?  357 TYR B CZ    1 
ATOM   8451  O  OH    . TYR B 1 357 ? 125.613 136.269 149.566 1.00 29.92 ?  357 TYR B OH    1 
ATOM   8452  N  N     . ILE B 1 358 ? 117.237 137.971 151.177 1.00 17.75 ?  358 ILE B N     1 
ATOM   8453  C  CA    . ILE B 1 358 ? 115.907 138.562 151.222 1.00 12.47 ?  358 ILE B CA    1 
ATOM   8454  C  C     . ILE B 1 358 ? 116.035 139.983 151.750 1.00 17.94 ?  358 ILE B C     1 
ATOM   8455  O  O     . ILE B 1 358 ? 116.525 140.198 152.865 1.00 20.13 ?  358 ILE B O     1 
ATOM   8456  C  CB    . ILE B 1 358 ? 114.942 137.741 152.091 1.00 20.66 ?  358 ILE B CB    1 
ATOM   8457  C  CG1   . ILE B 1 358 ? 114.890 136.289 151.611 1.00 18.68 ?  358 ILE B CG1   1 
ATOM   8458  C  CG2   . ILE B 1 358 ? 113.558 138.366 152.077 1.00 15.10 ?  358 ILE B CG2   1 
ATOM   8459  C  CD1   . ILE B 1 358 ? 114.461 136.136 150.174 1.00 17.12 ?  358 ILE B CD1   1 
ATOM   8460  N  N     . MET B 1 359 ? 115.601 140.947 150.949 1.00 16.54 ?  359 MET B N     1 
ATOM   8461  C  CA    . MET B 1 359 ? 115.495 142.338 151.368 1.00 8.55  ?  359 MET B CA    1 
ATOM   8462  C  C     . MET B 1 359 ? 114.021 142.708 151.401 1.00 15.52 ?  359 MET B C     1 
ATOM   8463  O  O     . MET B 1 359 ? 113.344 142.664 150.369 1.00 18.17 ?  359 MET B O     1 
ATOM   8464  C  CB    . MET B 1 359 ? 116.266 143.262 150.423 1.00 14.17 ?  359 MET B CB    1 
ATOM   8465  C  CG    . MET B 1 359 ? 116.714 144.567 151.063 1.00 17.85 ?  359 MET B CG    1 
ATOM   8466  S  SD    . MET B 1 359 ? 116.894 145.924 149.892 1.00 31.27 ?  359 MET B SD    1 
ATOM   8467  C  CE    . MET B 1 359 ? 115.365 146.812 150.151 1.00 6.74  ?  359 MET B CE    1 
ATOM   8468  N  N     . PHE B 1 360 ? 113.524 143.060 152.582 1.00 13.75 ?  360 PHE B N     1 
ATOM   8469  C  CA    . PHE B 1 360 ? 112.146 143.521 152.735 1.00 9.65  ?  360 PHE B CA    1 
ATOM   8470  C  C     . PHE B 1 360 ? 112.148 145.025 152.495 1.00 13.77 ?  360 PHE B C     1 
ATOM   8471  O  O     . PHE B 1 360 ? 112.522 145.808 153.369 1.00 22.86 ?  360 PHE B O     1 
ATOM   8472  C  CB    . PHE B 1 360 ? 111.600 143.153 154.109 1.00 13.59 ?  360 PHE B CB    1 
ATOM   8473  C  CG    . PHE B 1 360 ? 111.463 141.673 154.324 1.00 17.20 ?  360 PHE B CG    1 
ATOM   8474  C  CD1   . PHE B 1 360 ? 110.663 140.910 153.489 1.00 17.03 ?  360 PHE B CD1   1 
ATOM   8475  C  CD2   . PHE B 1 360 ? 112.138 141.042 155.353 1.00 16.86 ?  360 PHE B CD2   1 
ATOM   8476  C  CE1   . PHE B 1 360 ? 110.537 139.549 153.680 1.00 19.11 ?  360 PHE B CE1   1 
ATOM   8477  C  CE2   . PHE B 1 360 ? 112.015 139.680 155.548 1.00 17.35 ?  360 PHE B CE2   1 
ATOM   8478  C  CZ    . PHE B 1 360 ? 111.214 138.934 154.711 1.00 16.26 ?  360 PHE B CZ    1 
ATOM   8479  N  N     . GLN B 1 361 ? 111.728 145.425 151.292 1.00 17.17 ?  361 GLN B N     1 
ATOM   8480  C  CA    . GLN B 1 361 ? 111.915 146.804 150.855 1.00 8.05  ?  361 GLN B CA    1 
ATOM   8481  C  C     . GLN B 1 361 ? 111.155 147.785 151.740 1.00 11.93 ?  361 GLN B C     1 
ATOM   8482  O  O     . GLN B 1 361 ? 111.686 148.839 152.107 1.00 16.63 ?  361 GLN B O     1 
ATOM   8483  C  CB    . GLN B 1 361 ? 111.478 146.948 149.398 1.00 17.68 ?  361 GLN B CB    1 
ATOM   8484  C  CG    . GLN B 1 361 ? 111.498 148.371 148.877 1.00 23.75 ?  361 GLN B CG    1 
ATOM   8485  C  CD    . GLN B 1 361 ? 112.177 148.483 147.530 1.00 19.90 ?  361 GLN B CD    1 
ATOM   8486  O  OE1   . GLN B 1 361 ? 112.186 147.534 146.749 1.00 23.37 ?  361 GLN B OE1   1 
ATOM   8487  N  NE2   . GLN B 1 361 ? 112.758 149.644 147.253 1.00 21.17 ?  361 GLN B NE2   1 
ATOM   8488  N  N     . ASP B 1 362 ? 109.911 147.461 152.094 1.00 22.00 ?  362 ASP B N     1 
ATOM   8489  C  CA    . ASP B 1 362 ? 109.112 148.394 152.880 1.00 19.82 ?  362 ASP B CA    1 
ATOM   8490  C  C     . ASP B 1 362 ? 109.591 148.471 154.323 1.00 18.30 ?  362 ASP B C     1 
ATOM   8491  O  O     . ASP B 1 362 ? 109.471 149.523 154.959 1.00 23.43 ?  362 ASP B O     1 
ATOM   8492  C  CB    . ASP B 1 362 ? 107.637 148.003 152.823 1.00 21.56 ?  362 ASP B CB    1 
ATOM   8493  C  CG    . ASP B 1 362 ? 106.986 148.392 151.511 1.00 30.35 ?  362 ASP B CG    1 
ATOM   8494  O  OD1   . ASP B 1 362 ? 107.218 147.695 150.502 1.00 31.69 ?  362 ASP B OD1   1 
ATOM   8495  O  OD2   . ASP B 1 362 ? 106.245 149.396 151.488 1.00 34.61 -1 362 ASP B OD2   1 
ATOM   8496  N  N     . ASN B 1 363 ? 110.134 147.375 154.855 1.00 20.36 ?  363 ASN B N     1 
ATOM   8497  C  CA    . ASN B 1 363 ? 110.766 147.435 156.169 1.00 11.06 ?  363 ASN B CA    1 
ATOM   8498  C  C     . ASN B 1 363 ? 111.973 148.363 156.145 1.00 15.96 ?  363 ASN B C     1 
ATOM   8499  O  O     . ASN B 1 363 ? 112.202 149.125 157.091 1.00 23.67 ?  363 ASN B O     1 
ATOM   8500  C  CB    . ASN B 1 363 ? 111.176 146.033 156.618 1.00 13.21 ?  363 ASN B CB    1 
ATOM   8501  C  CG    . ASN B 1 363 ? 110.048 145.282 157.291 1.00 15.44 ?  363 ASN B CG    1 
ATOM   8502  O  OD1   . ASN B 1 363 ? 109.016 145.858 157.628 1.00 25.26 ?  363 ASN B OD1   1 
ATOM   8503  N  ND2   . ASN B 1 363 ? 110.240 143.985 157.491 1.00 12.07 ?  363 ASN B ND2   1 
ATOM   8504  N  N     . VAL B 1 364 ? 112.758 148.307 155.070 1.00 14.39 ?  364 VAL B N     1 
ATOM   8505  C  CA    . VAL B 1 364 ? 113.933 149.162 154.947 1.00 12.62 ?  364 VAL B CA    1 
ATOM   8506  C  C     . VAL B 1 364 ? 113.530 150.626 154.837 1.00 12.74 ?  364 VAL B C     1 
ATOM   8507  O  O     . VAL B 1 364 ? 114.144 151.501 155.458 1.00 23.96 ?  364 VAL B O     1 
ATOM   8508  C  CB    . VAL B 1 364 ? 114.786 148.717 153.745 1.00 3.08  ?  364 VAL B CB    1 
ATOM   8509  C  CG1   . VAL B 1 364 ? 115.948 149.669 153.538 1.00 2.95  ?  364 VAL B CG1   1 
ATOM   8510  C  CG2   . VAL B 1 364 ? 115.282 147.297 153.945 1.00 5.13  ?  364 VAL B CG2   1 
ATOM   8511  N  N     . ASN B 1 365 ? 112.496 150.920 154.051 1.00 11.88 ?  365 ASN B N     1 
ATOM   8512  C  CA    . ASN B 1 365 ? 112.176 152.294 153.695 1.00 7.76  ?  365 ASN B CA    1 
ATOM   8513  C  C     . ASN B 1 365 ? 111.177 152.958 154.633 1.00 12.20 ?  365 ASN B C     1 
ATOM   8514  O  O     . ASN B 1 365 ? 111.060 154.187 154.610 1.00 18.39 ?  365 ASN B O     1 
ATOM   8515  C  CB    . ASN B 1 365 ? 111.641 152.353 152.261 1.00 12.75 ?  365 ASN B CB    1 
ATOM   8516  C  CG    . ASN B 1 365 ? 112.719 152.091 151.232 1.00 10.98 ?  365 ASN B CG    1 
ATOM   8517  O  OD1   . ASN B 1 365 ? 113.752 152.755 151.220 1.00 16.32 ?  365 ASN B OD1   1 
ATOM   8518  N  ND2   . ASN B 1 365 ? 112.485 151.119 150.363 1.00 16.41 ?  365 ASN B ND2   1 
ATOM   8519  N  N     . LYS B 1 366 ? 110.456 152.192 155.453 1.00 22.06 ?  366 LYS B N     1 
ATOM   8520  C  CA    . LYS B 1 366 ? 109.559 152.818 156.416 1.00 20.05 ?  366 LYS B CA    1 
ATOM   8521  C  C     . LYS B 1 366 ? 110.323 153.561 157.502 1.00 19.07 ?  366 LYS B C     1 
ATOM   8522  O  O     . LYS B 1 366 ? 109.762 154.462 158.135 1.00 26.64 ?  366 LYS B O     1 
ATOM   8523  C  CB    . LYS B 1 366 ? 108.632 151.773 157.039 1.00 17.73 ?  366 LYS B CB    1 
ATOM   8524  C  CG    . LYS B 1 366 ? 109.313 150.824 158.006 1.00 25.05 ?  366 LYS B CG    1 
ATOM   8525  C  CD    . LYS B 1 366 ? 108.291 150.097 158.860 1.00 25.50 ?  366 LYS B CD    1 
ATOM   8526  C  CE    . LYS B 1 366 ? 107.246 149.405 158.002 1.00 23.94 ?  366 LYS B CE    1 
ATOM   8527  N  NZ    . LYS B 1 366 ? 106.498 148.372 158.768 1.00 27.64 1  366 LYS B NZ    1 
ATOM   8528  N  N     . VAL B 1 367 ? 111.587 153.205 157.725 1.00 23.17 ?  367 VAL B N     1 
ATOM   8529  C  CA    . VAL B 1 367 ? 112.459 153.902 158.659 1.00 16.05 ?  367 VAL B CA    1 
ATOM   8530  C  C     . VAL B 1 367 ? 113.618 154.594 157.961 1.00 14.41 ?  367 VAL B C     1 
ATOM   8531  O  O     . VAL B 1 367 ? 114.469 155.181 158.636 1.00 23.62 ?  367 VAL B O     1 
ATOM   8532  C  CB    . VAL B 1 367 ? 112.987 152.948 159.750 1.00 13.36 ?  367 VAL B CB    1 
ATOM   8533  C  CG1   . VAL B 1 367 ? 111.855 152.500 160.653 1.00 14.06 ?  367 VAL B CG1   1 
ATOM   8534  C  CG2   . VAL B 1 367 ? 113.677 151.751 159.117 1.00 10.72 ?  367 VAL B CG2   1 
ATOM   8535  N  N     . HIS B 1 368 ? 113.677 154.544 156.634 1.00 17.11 ?  368 HIS B N     1 
ATOM   8536  C  CA    . HIS B 1 368 ? 114.802 155.110 155.906 1.00 4.16  ?  368 HIS B CA    1 
ATOM   8537  C  C     . HIS B 1 368 ? 114.801 156.628 156.031 1.00 14.95 ?  368 HIS B C     1 
ATOM   8538  O  O     . HIS B 1 368 ? 113.797 157.286 155.744 1.00 27.75 ?  368 HIS B O     1 
ATOM   8539  C  CB    . HIS B 1 368 ? 114.737 154.690 154.440 1.00 6.95  ?  368 HIS B CB    1 
ATOM   8540  C  CG    . HIS B 1 368 ? 115.894 155.165 153.620 1.00 13.98 ?  368 HIS B CG    1 
ATOM   8541  N  ND1   . HIS B 1 368 ? 115.750 155.620 152.328 1.00 14.53 ?  368 HIS B ND1   1 
ATOM   8542  C  CD2   . HIS B 1 368 ? 117.213 155.255 153.907 1.00 7.49  ?  368 HIS B CD2   1 
ATOM   8543  C  CE1   . HIS B 1 368 ? 116.933 155.965 151.852 1.00 15.00 ?  368 HIS B CE1   1 
ATOM   8544  N  NE2   . HIS B 1 368 ? 117.837 155.754 152.791 1.00 14.14 ?  368 HIS B NE2   1 
ATOM   8545  N  N     . ALA B 1 369 ? 115.936 157.183 156.456 1.00 18.35 ?  369 ALA B N     1 
ATOM   8546  C  CA    . ALA B 1 369 ? 116.029 158.612 156.724 1.00 13.28 ?  369 ALA B CA    1 
ATOM   8547  C  C     . ALA B 1 369 ? 116.260 159.444 155.471 1.00 17.10 ?  369 ALA B C     1 
ATOM   8548  O  O     . ALA B 1 369 ? 116.069 160.662 155.514 1.00 22.09 ?  369 ALA B O     1 
ATOM   8549  C  CB    . ALA B 1 369 ? 117.148 158.884 157.730 1.00 11.71 ?  369 ALA B CB    1 
ATOM   8550  N  N     . ASN B 1 370 ? 116.653 158.824 154.362 1.00 15.45 ?  370 ASN B N     1 
ATOM   8551  C  CA    . ASN B 1 370 ? 117.014 159.541 153.146 1.00 14.76 ?  370 ASN B CA    1 
ATOM   8552  C  C     . ASN B 1 370 ? 116.157 159.099 151.966 1.00 12.57 ?  370 ASN B C     1 
ATOM   8553  O  O     . ASN B 1 370 ? 116.653 158.898 150.857 1.00 22.93 ?  370 ASN B O     1 
ATOM   8554  C  CB    . ASN B 1 370 ? 118.497 159.359 152.831 1.00 8.88  ?  370 ASN B CB    1 
ATOM   8555  C  CG    . ASN B 1 370 ? 119.394 159.872 153.938 1.00 12.32 ?  370 ASN B CG    1 
ATOM   8556  O  OD1   . ASN B 1 370 ? 119.332 161.043 154.310 1.00 26.71 ?  370 ASN B OD1   1 
ATOM   8557  N  ND2   . ASN B 1 370 ? 120.230 158.997 154.476 1.00 19.98 ?  370 ASN B ND2   1 
ATOM   8558  N  N     . ASN B 1 371 ? 114.852 158.944 152.190 1.00 16.55 ?  371 ASN B N     1 
ATOM   8559  C  CA    . ASN B 1 371 ? 113.953 158.620 151.090 1.00 11.89 ?  371 ASN B CA    1 
ATOM   8560  C  C     . ASN B 1 371 ? 113.839 159.758 150.087 1.00 18.30 ?  371 ASN B C     1 
ATOM   8561  O  O     . ASN B 1 371 ? 113.508 159.512 148.923 1.00 19.21 ?  371 ASN B O     1 
ATOM   8562  C  CB    . ASN B 1 371 ? 112.567 158.258 151.624 1.00 10.15 ?  371 ASN B CB    1 
ATOM   8563  C  CG    . ASN B 1 371 ? 112.470 156.812 152.057 1.00 17.31 ?  371 ASN B CG    1 
ATOM   8564  O  OD1   . ASN B 1 371 ? 113.242 155.964 151.612 1.00 21.88 ?  371 ASN B OD1   1 
ATOM   8565  N  ND2   . ASN B 1 371 ? 111.515 156.522 152.927 1.00 18.49 ?  371 ASN B ND2   1 
ATOM   8566  N  N     . HIS B 1 372 ? 114.105 160.996 150.509 1.00 25.92 ?  372 HIS B N     1 
ATOM   8567  C  CA    . HIS B 1 372 ? 114.094 162.113 149.571 1.00 17.44 ?  372 HIS B CA    1 
ATOM   8568  C  C     . HIS B 1 372 ? 115.177 161.951 148.515 1.00 20.87 ?  372 HIS B C     1 
ATOM   8569  O  O     . HIS B 1 372 ? 114.962 162.266 147.338 1.00 28.82 ?  372 HIS B O     1 
ATOM   8570  C  CB    . HIS B 1 372 ? 114.264 163.432 150.323 1.00 19.41 ?  372 HIS B CB    1 
ATOM   8571  C  CG    . HIS B 1 372 ? 115.607 163.594 150.961 1.00 22.84 ?  372 HIS B CG    1 
ATOM   8572  N  ND1   . HIS B 1 372 ? 116.049 162.782 151.982 1.00 23.35 ?  372 HIS B ND1   1 
ATOM   8573  C  CD2   . HIS B 1 372 ? 116.610 164.471 150.717 1.00 19.45 ?  372 HIS B CD2   1 
ATOM   8574  C  CE1   . HIS B 1 372 ? 117.265 163.153 152.343 1.00 17.29 ?  372 HIS B CE1   1 
ATOM   8575  N  NE2   . HIS B 1 372 ? 117.627 164.176 151.591 1.00 23.41 ?  372 HIS B NE2   1 
ATOM   8576  N  N     . ILE B 1 373 ? 116.356 161.476 148.916 1.00 17.44 ?  373 ILE B N     1 
ATOM   8577  C  CA    . ILE B 1 373 ? 117.408 161.191 147.948 1.00 17.98 ?  373 ILE B CA    1 
ATOM   8578  C  C     . ILE B 1 373 ? 116.992 160.038 147.046 1.00 18.99 ?  373 ILE B C     1 
ATOM   8579  O  O     . ILE B 1 373 ? 117.099 160.114 145.817 1.00 30.91 ?  373 ILE B O     1 
ATOM   8580  C  CB    . ILE B 1 373 ? 118.734 160.893 148.669 1.00 22.75 ?  373 ILE B CB    1 
ATOM   8581  C  CG1   . ILE B 1 373 ? 119.130 162.070 149.563 1.00 17.32 ?  373 ILE B CG1   1 
ATOM   8582  C  CG2   . ILE B 1 373 ? 119.829 160.575 147.665 1.00 19.50 ?  373 ILE B CG2   1 
ATOM   8583  C  CD1   . ILE B 1 373 ? 120.274 161.772 150.502 1.00 13.19 ?  373 ILE B CD1   1 
ATOM   8584  N  N     . SER B 1 374 ? 116.507 158.955 147.643 1.00 13.52 ?  374 SER B N     1 
ATOM   8585  C  CA    . SER B 1 374 ? 116.007 157.805 146.908 1.00 8.78  ?  374 SER B CA    1 
ATOM   8586  C  C     . SER B 1 374 ? 115.530 156.772 147.915 1.00 12.49 ?  374 SER B C     1 
ATOM   8587  O  O     . SER B 1 374 ? 115.913 156.801 149.088 1.00 21.31 ?  374 SER B O     1 
ATOM   8588  C  CB    . SER B 1 374 ? 117.078 157.201 145.994 1.00 16.31 ?  374 SER B CB    1 
ATOM   8589  O  OG    . SER B 1 374 ? 116.532 156.195 145.162 1.00 27.62 ?  374 SER B OG    1 
ATOM   8590  N  N     . LYS B 1 375 ? 114.678 155.870 147.445 1.00 23.34 ?  375 LYS B N     1 
ATOM   8591  C  CA    . LYS B 1 375 ? 114.371 154.675 148.208 1.00 13.63 ?  375 LYS B CA    1 
ATOM   8592  C  C     . LYS B 1 375 ? 115.554 153.715 148.166 1.00 12.91 ?  375 LYS B C     1 
ATOM   8593  O  O     . LYS B 1 375 ? 116.399 153.765 147.269 1.00 27.18 ?  375 LYS B O     1 
ATOM   8594  C  CB    . LYS B 1 375 ? 113.122 153.988 147.654 1.00 12.06 ?  375 LYS B CB    1 
ATOM   8595  C  CG    . LYS B 1 375 ? 111.916 154.061 148.565 1.00 14.61 ?  375 LYS B CG    1 
ATOM   8596  C  CD    . LYS B 1 375 ? 111.344 155.460 148.617 1.00 17.92 ?  375 LYS B CD    1 
ATOM   8597  C  CE    . LYS B 1 375 ? 109.859 155.429 148.928 1.00 22.12 ?  375 LYS B CE    1 
ATOM   8598  N  NZ    . LYS B 1 375 ? 109.583 154.805 150.250 1.00 28.79 1  375 LYS B NZ    1 
ATOM   8599  N  N     . VAL B 1 376 ? 115.617 152.838 149.161 1.00 13.66 ?  376 VAL B N     1 
ATOM   8600  C  CA    . VAL B 1 376 ? 116.600 151.762 149.152 1.00 13.56 ?  376 VAL B CA    1 
ATOM   8601  C  C     . VAL B 1 376 ? 116.049 150.635 148.289 1.00 13.56 ?  376 VAL B C     1 
ATOM   8602  O  O     . VAL B 1 376 ? 114.966 150.105 148.559 1.00 25.71 ?  376 VAL B O     1 
ATOM   8603  C  CB    . VAL B 1 376 ? 116.913 151.276 150.574 1.00 10.05 ?  376 VAL B CB    1 
ATOM   8604  C  CG1   . VAL B 1 376 ? 117.923 150.143 150.533 1.00 0.39  ?  376 VAL B CG1   1 
ATOM   8605  C  CG2   . VAL B 1 376 ? 117.428 152.426 151.425 1.00 2.78  ?  376 VAL B CG2   1 
ATOM   8606  N  N     . LYS B 1 377 ? 116.791 150.271 147.243 1.00 16.68 ?  377 LYS B N     1 
ATOM   8607  C  CA    . LYS B 1 377 ? 116.320 149.300 146.266 1.00 14.19 ?  377 LYS B CA    1 
ATOM   8608  C  C     . LYS B 1 377 ? 116.969 147.932 146.388 1.00 11.30 ?  377 LYS B C     1 
ATOM   8609  O  O     . LYS B 1 377 ? 116.367 146.945 145.963 1.00 28.67 ?  377 LYS B O     1 
ATOM   8610  C  CB    . LYS B 1 377 ? 116.550 149.826 144.841 1.00 14.73 ?  377 LYS B CB    1 
ATOM   8611  C  CG    . LYS B 1 377 ? 115.863 151.145 144.552 1.00 11.34 ?  377 LYS B CG    1 
ATOM   8612  C  CD    . LYS B 1 377 ? 116.747 152.031 143.699 1.00 20.92 ?  377 LYS B CD    1 
ATOM   8613  C  CE    . LYS B 1 377 ? 116.489 153.498 143.976 1.00 23.81 ?  377 LYS B CE    1 
ATOM   8614  N  NZ    . LYS B 1 377 ? 117.544 154.358 143.375 1.00 28.54 1  377 LYS B NZ    1 
ATOM   8615  N  N     . PHE B 1 378 ? 118.169 147.849 146.948 1.00 13.04 ?  378 PHE B N     1 
ATOM   8616  C  CA    . PHE B 1 378 ? 118.877 146.582 147.066 1.00 7.75  ?  378 PHE B CA    1 
ATOM   8617  C  C     . PHE B 1 378 ? 119.913 146.717 148.173 1.00 10.04 ?  378 PHE B C     1 
ATOM   8618  O  O     . PHE B 1 378 ? 120.086 147.788 148.762 1.00 18.19 ?  378 PHE B O     1 
ATOM   8619  C  CB    . PHE B 1 378 ? 119.510 146.170 145.732 1.00 7.54  ?  378 PHE B CB    1 
ATOM   8620  C  CG    . PHE B 1 378 ? 120.638 147.059 145.283 1.00 12.21 ?  378 PHE B CG    1 
ATOM   8621  C  CD1   . PHE B 1 378 ? 120.455 148.424 145.147 1.00 13.29 ?  378 PHE B CD1   1 
ATOM   8622  C  CD2   . PHE B 1 378 ? 121.878 146.523 144.981 1.00 4.62  ?  378 PHE B CD2   1 
ATOM   8623  C  CE1   . PHE B 1 378 ? 121.486 149.238 144.729 1.00 9.48  ?  378 PHE B CE1   1 
ATOM   8624  C  CE2   . PHE B 1 378 ? 122.912 147.334 144.561 1.00 4.67  ?  378 PHE B CE2   1 
ATOM   8625  C  CZ    . PHE B 1 378 ? 122.715 148.692 144.434 1.00 11.63 ?  378 PHE B CZ    1 
ATOM   8626  N  N     . SER B 1 379 ? 120.596 145.618 148.454 1.00 12.18 ?  379 SER B N     1 
ATOM   8627  C  CA    . SER B 1 379 ? 121.602 145.556 149.501 1.00 0.75  ?  379 SER B CA    1 
ATOM   8628  C  C     . SER B 1 379 ? 122.945 145.164 148.888 1.00 5.11  ?  379 SER B C     1 
ATOM   8629  O  O     . SER B 1 379 ? 123.089 145.059 147.668 1.00 11.28 ?  379 SER B O     1 
ATOM   8630  C  CB    . SER B 1 379 ? 121.170 144.584 150.600 1.00 8.13  ?  379 SER B CB    1 
ATOM   8631  O  OG    . SER B 1 379 ? 121.790 144.901 151.830 1.00 10.48 ?  379 SER B OG    1 
ATOM   8632  N  N     . ASN B 1 380 ? 123.929 144.944 149.750 1.00 14.67 ?  380 ASN B N     1 
ATOM   8633  C  CA    . ASN B 1 380 ? 125.282 144.627 149.329 1.00 4.52  ?  380 ASN B CA    1 
ATOM   8634  C  C     . ASN B 1 380 ? 125.481 143.112 149.311 1.00 9.49  ?  380 ASN B C     1 
ATOM   8635  O  O     . ASN B 1 380 ? 124.532 142.334 149.436 1.00 12.78 ?  380 ASN B O     1 
ATOM   8636  C  CB    . ASN B 1 380 ? 126.288 145.325 150.242 1.00 11.89 ?  380 ASN B CB    1 
ATOM   8637  C  CG    . ASN B 1 380 ? 126.288 144.764 151.646 1.00 3.04  ?  380 ASN B CG    1 
ATOM   8638  O  OD1   . ASN B 1 380 ? 125.234 144.546 152.238 1.00 15.30 ?  380 ASN B OD1   1 
ATOM   8639  N  ND2   . ASN B 1 380 ? 127.473 144.535 152.191 1.00 6.55  ?  380 ASN B ND2   1 
ATOM   8640  N  N     . LEU B 1 381 ? 126.730 142.680 149.143 1.00 21.75 ?  381 LEU B N     1 
ATOM   8641  C  CA    . LEU B 1 381 ? 127.041 141.257 149.114 1.00 7.54  ?  381 LEU B CA    1 
ATOM   8642  C  C     . LEU B 1 381 ? 126.883 140.599 150.478 1.00 8.19  ?  381 LEU B C     1 
ATOM   8643  O  O     . LEU B 1 381 ? 126.836 139.367 150.556 1.00 19.16 ?  381 LEU B O     1 
ATOM   8644  C  CB    . LEU B 1 381 ? 128.464 141.052 148.590 1.00 14.25 ?  381 LEU B CB    1 
ATOM   8645  C  CG    . LEU B 1 381 ? 129.004 139.623 148.509 1.00 19.33 ?  381 LEU B CG    1 
ATOM   8646  C  CD1   . LEU B 1 381 ? 128.174 138.777 147.560 1.00 15.12 ?  381 LEU B CD1   1 
ATOM   8647  C  CD2   . LEU B 1 381 ? 130.459 139.638 148.083 1.00 18.96 ?  381 LEU B CD2   1 
ATOM   8648  N  N     . CYS B 1 382 ? 126.798 141.383 151.551 1.00 13.33 ?  382 CYS B N     1 
ATOM   8649  C  CA    . CYS B 1 382 ? 126.596 140.851 152.891 1.00 7.71  ?  382 CYS B CA    1 
ATOM   8650  C  C     . CYS B 1 382 ? 125.225 141.187 153.462 1.00 10.21 ?  382 CYS B C     1 
ATOM   8651  O  O     . CYS B 1 382 ? 124.899 140.731 154.561 1.00 12.39 ?  382 CYS B O     1 
ATOM   8652  C  CB    . CYS B 1 382 ? 127.693 141.362 153.832 1.00 17.51 ?  382 CYS B CB    1 
ATOM   8653  S  SG    . CYS B 1 382 ? 129.361 140.839 153.368 1.00 32.30 ?  382 CYS B SG    1 
ATOM   8654  N  N     . SER B 1 383 ? 124.418 141.973 152.747 1.00 9.99  ?  383 SER B N     1 
ATOM   8655  C  CA    . SER B 1 383 ? 123.018 142.215 153.089 1.00 5.40  ?  383 SER B CA    1 
ATOM   8656  C  C     . SER B 1 383 ? 122.852 143.075 154.340 1.00 10.84 ?  383 SER B C     1 
ATOM   8657  O  O     . SER B 1 383 ? 121.840 142.974 155.035 1.00 18.85 ?  383 SER B O     1 
ATOM   8658  C  CB    . SER B 1 383 ? 122.254 140.896 153.250 1.00 8.46  ?  383 SER B CB    1 
ATOM   8659  O  OG    . SER B 1 383 ? 122.759 140.137 154.336 1.00 24.20 ?  383 SER B OG    1 
ATOM   8660  N  N     . GLU B 1 384 ? 123.825 143.934 154.646 1.00 11.06 ?  384 GLU B N     1 
ATOM   8661  C  CA    . GLU B 1 384 ? 123.691 144.859 155.764 1.00 12.38 ?  384 GLU B CA    1 
ATOM   8662  C  C     . GLU B 1 384 ? 123.826 146.319 155.356 1.00 16.15 ?  384 GLU B C     1 
ATOM   8663  O  O     . GLU B 1 384 ? 123.769 147.196 156.225 1.00 30.46 ?  384 GLU B O     1 
ATOM   8664  C  CB    . GLU B 1 384 ? 124.709 144.529 156.869 1.00 7.12  ?  384 GLU B CB    1 
ATOM   8665  C  CG    . GLU B 1 384 ? 125.935 145.433 156.935 1.00 10.43 ?  384 GLU B CG    1 
ATOM   8666  C  CD    . GLU B 1 384 ? 126.848 145.300 155.734 1.00 18.68 ?  384 GLU B CD    1 
ATOM   8667  O  OE1   . GLU B 1 384 ? 127.746 146.152 155.574 1.00 27.16 ?  384 GLU B OE1   1 
ATOM   8668  O  OE2   . GLU B 1 384 ? 126.685 144.333 154.966 1.00 10.28 -1 384 GLU B OE2   1 
ATOM   8669  N  N     . VAL B 1 385 ? 123.982 146.610 154.069 1.00 12.79 ?  385 VAL B N     1 
ATOM   8670  C  CA    . VAL B 1 385 ? 124.106 147.977 153.576 1.00 7.03  ?  385 VAL B CA    1 
ATOM   8671  C  C     . VAL B 1 385 ? 122.772 148.382 152.966 1.00 18.03 ?  385 VAL B C     1 
ATOM   8672  O  O     . VAL B 1 385 ? 122.289 147.739 152.027 1.00 20.96 ?  385 VAL B O     1 
ATOM   8673  C  CB    . VAL B 1 385 ? 125.246 148.105 152.554 1.00 9.76  ?  385 VAL B CB    1 
ATOM   8674  C  CG1   . VAL B 1 385 ? 125.248 149.492 151.935 1.00 12.20 ?  385 VAL B CG1   1 
ATOM   8675  C  CG2   . VAL B 1 385 ? 126.577 147.806 153.212 1.00 6.52  ?  385 VAL B CG2   1 
ATOM   8676  N  N     . LEU B 1 386 ? 122.177 149.454 153.496 1.00 10.80 ?  386 LEU B N     1 
ATOM   8677  C  CA    . LEU B 1 386 ? 120.853 149.919 153.071 1.00 0.00  ?  386 LEU B CA    1 
ATOM   8678  C  C     . LEU B 1 386 ? 120.910 151.440 152.957 1.00 4.87  ?  386 LEU B C     1 
ATOM   8679  O  O     . LEU B 1 386 ? 120.674 152.157 153.933 1.00 17.00 ?  386 LEU B O     1 
ATOM   8680  C  CB    . LEU B 1 386 ? 119.777 149.462 154.046 1.00 7.07  ?  386 LEU B CB    1 
ATOM   8681  C  CG    . LEU B 1 386 ? 119.636 147.950 154.216 1.00 5.58  ?  386 LEU B CG    1 
ATOM   8682  C  CD1   . LEU B 1 386 ? 118.713 147.629 155.376 1.00 2.95  ?  386 LEU B CD1   1 
ATOM   8683  C  CD2   . LEU B 1 386 ? 119.131 147.315 152.929 1.00 4.78  ?  386 LEU B CD2   1 
ATOM   8684  N  N     . GLN B 1 387 ? 121.219 151.927 151.758 1.00 12.76 ?  387 GLN B N     1 
ATOM   8685  C  CA    . GLN B 1 387 ? 121.380 153.352 151.520 1.00 11.01 ?  387 GLN B CA    1 
ATOM   8686  C  C     . GLN B 1 387 ? 120.680 153.735 150.227 1.00 6.75  ?  387 GLN B C     1 
ATOM   8687  O  O     . GLN B 1 387 ? 120.458 152.904 149.344 1.00 16.76 ?  387 GLN B O     1 
ATOM   8688  C  CB    . GLN B 1 387 ? 122.860 153.747 151.452 1.00 7.73  ?  387 GLN B CB    1 
ATOM   8689  C  CG    . GLN B 1 387 ? 123.678 153.271 152.632 1.00 4.11  ?  387 GLN B CG    1 
ATOM   8690  C  CD    . GLN B 1 387 ? 125.130 153.665 152.522 1.00 9.97  ?  387 GLN B CD    1 
ATOM   8691  O  OE1   . GLN B 1 387 ? 125.496 154.514 151.713 1.00 21.43 ?  387 GLN B OE1   1 
ATOM   8692  N  NE2   . GLN B 1 387 ? 125.971 153.047 153.341 1.00 13.44 ?  387 GLN B NE2   1 
ATOM   8693  N  N     . ALA B 1 388 ? 120.327 155.012 150.131 1.00 13.69 ?  388 ALA B N     1 
ATOM   8694  C  CA    . ALA B 1 388 ? 119.750 155.538 148.904 1.00 11.11 ?  388 ALA B CA    1 
ATOM   8695  C  C     . ALA B 1 388 ? 120.793 155.554 147.795 1.00 9.99  ?  388 ALA B C     1 
ATOM   8696  O  O     . ALA B 1 388 ? 121.946 155.935 148.010 1.00 24.76 ?  388 ALA B O     1 
ATOM   8697  C  CB    . ALA B 1 388 ? 119.204 156.946 149.133 1.00 6.20  ?  388 ALA B CB    1 
ATOM   8698  N  N     . SER B 1 389 ? 120.386 155.125 146.606 1.00 11.05 ?  389 SER B N     1 
ATOM   8699  C  CA    . SER B 1 389 ? 121.249 155.143 145.438 1.00 9.13  ?  389 SER B CA    1 
ATOM   8700  C  C     . SER B 1 389 ? 120.504 155.769 144.270 1.00 13.57 ?  389 SER B C     1 
ATOM   8701  O  O     . SER B 1 389 ? 119.273 155.725 144.201 1.00 24.86 ?  389 SER B O     1 
ATOM   8702  C  CB    . SER B 1 389 ? 121.723 153.732 145.060 1.00 11.83 ?  389 SER B CB    1 
ATOM   8703  O  OG    . SER B 1 389 ? 120.629 152.846 144.910 1.00 23.90 ?  389 SER B OG    1 
ATOM   8704  N  N     . GLN B 1 390 ? 121.264 156.358 143.353 1.00 15.83 ?  390 GLN B N     1 
ATOM   8705  C  CA    . GLN B 1 390 ? 120.718 156.929 142.131 1.00 10.19 ?  390 GLN B CA    1 
ATOM   8706  C  C     . GLN B 1 390 ? 121.483 156.351 140.952 1.00 9.92  ?  390 GLN B C     1 
ATOM   8707  O  O     . GLN B 1 390 ? 122.717 156.358 140.946 1.00 23.55 ?  390 GLN B O     1 
ATOM   8708  C  CB    . GLN B 1 390 ? 120.806 158.457 142.144 1.00 12.79 ?  390 GLN B CB    1 
ATOM   8709  C  CG    . GLN B 1 390 ? 119.840 159.114 143.118 1.00 14.02 ?  390 GLN B CG    1 
ATOM   8710  C  CD    . GLN B 1 390 ? 120.109 160.591 143.307 1.00 20.40 ?  390 GLN B CD    1 
ATOM   8711  O  OE1   . GLN B 1 390 ? 121.119 161.115 142.838 1.00 26.95 ?  390 GLN B OE1   1 
ATOM   8712  N  NE2   . GLN B 1 390 ? 119.206 161.272 144.000 1.00 18.70 ?  390 GLN B NE2   1 
ATOM   8713  N  N     . VAL B 1 391 ? 120.749 155.844 139.962 1.00 19.03 ?  391 VAL B N     1 
ATOM   8714  C  CA    . VAL B 1 391 ? 121.384 155.174 138.837 1.00 14.40 ?  391 VAL B CA    1 
ATOM   8715  C  C     . VAL B 1 391 ? 122.095 156.194 137.957 1.00 18.47 ?  391 VAL B C     1 
ATOM   8716  O  O     . VAL B 1 391 ? 121.616 157.315 137.743 1.00 19.62 ?  391 VAL B O     1 
ATOM   8717  C  CB    . VAL B 1 391 ? 120.348 154.369 138.029 1.00 16.18 ?  391 VAL B CB    1 
ATOM   8718  C  CG1   . VAL B 1 391 ? 119.485 155.299 137.195 1.00 15.48 ?  391 VAL B CG1   1 
ATOM   8719  C  CG2   . VAL B 1 391 ? 121.043 153.342 137.154 1.00 17.29 ?  391 VAL B CG2   1 
ATOM   8720  N  N     . SER B 1 392 ? 123.257 155.802 137.446 1.00 26.57 ?  392 SER B N     1 
ATOM   8721  C  CA    . SER B 1 392 ? 124.015 156.628 136.522 1.00 16.30 ?  392 SER B CA    1 
ATOM   8722  C  C     . SER B 1 392 ? 123.593 156.336 135.089 1.00 25.60 ?  392 SER B C     1 
ATOM   8723  O  O     . SER B 1 392 ? 123.140 155.236 134.763 1.00 29.96 ?  392 SER B O     1 
ATOM   8724  C  CB    . SER B 1 392 ? 125.517 156.385 136.680 1.00 21.45 ?  392 SER B CB    1 
ATOM   8725  O  OG    . SER B 1 392 ? 125.945 156.659 138.001 1.00 28.69 ?  392 SER B OG    1 
ATOM   8726  N  N     . SER B 1 393 ? 123.742 157.339 134.234 1.00 30.13 ?  393 SER B N     1 
ATOM   8727  C  CA    . SER B 1 393 ? 123.457 157.213 132.808 1.00 27.72 ?  393 SER B CA    1 
ATOM   8728  C  C     . SER B 1 393 ? 124.781 157.332 132.063 1.00 27.50 ?  393 SER B C     1 
ATOM   8729  O  O     . SER B 1 393 ? 125.294 158.435 131.861 1.00 30.98 ?  393 SER B O     1 
ATOM   8730  C  CB    . SER B 1 393 ? 122.459 158.272 132.352 1.00 32.70 ?  393 SER B CB    1 
ATOM   8731  O  OG    . SER B 1 393 ? 122.404 158.342 130.939 1.00 37.26 ?  393 SER B OG    1 
ATOM   8732  N  N     . TYR B 1 394 ? 125.329 156.193 131.657 1.00 32.60 ?  394 TYR B N     1 
ATOM   8733  C  CA    . TYR B 1 394 ? 126.567 156.149 130.890 1.00 29.49 ?  394 TYR B CA    1 
ATOM   8734  C  C     . TYR B 1 394 ? 126.213 156.147 129.410 1.00 26.91 ?  394 TYR B C     1 
ATOM   8735  O  O     . TYR B 1 394 ? 125.514 155.246 128.935 1.00 32.29 ?  394 TYR B O     1 
ATOM   8736  C  CB    . TYR B 1 394 ? 127.393 154.919 131.263 1.00 26.95 ?  394 TYR B CB    1 
ATOM   8737  C  CG    . TYR B 1 394 ? 127.834 154.918 132.708 1.00 30.11 ?  394 TYR B CG    1 
ATOM   8738  C  CD1   . TYR B 1 394 ? 128.827 155.780 133.151 1.00 27.75 ?  394 TYR B CD1   1 
ATOM   8739  C  CD2   . TYR B 1 394 ? 127.249 154.064 133.631 1.00 24.55 ?  394 TYR B CD2   1 
ATOM   8740  C  CE1   . TYR B 1 394 ? 129.230 155.786 134.470 1.00 28.05 ?  394 TYR B CE1   1 
ATOM   8741  C  CE2   . TYR B 1 394 ? 127.644 154.063 134.953 1.00 25.11 ?  394 TYR B CE2   1 
ATOM   8742  C  CZ    . TYR B 1 394 ? 128.635 154.926 135.368 1.00 34.09 ?  394 TYR B CZ    1 
ATOM   8743  O  OH    . TYR B 1 394 ? 129.032 154.928 136.685 1.00 36.44 ?  394 TYR B OH    1 
ATOM   8744  N  N     . THR B 1 395 ? 126.689 157.154 128.692 1.00 34.03 ?  395 THR B N     1 
ATOM   8745  C  CA    . THR B 1 395 ? 126.309 157.386 127.311 1.00 35.09 ?  395 THR B CA    1 
ATOM   8746  C  C     . THR B 1 395 ? 127.406 156.892 126.369 1.00 34.98 ?  395 THR B C     1 
ATOM   8747  O  O     . THR B 1 395 ? 128.377 156.253 126.784 1.00 35.22 ?  395 THR B O     1 
ATOM   8748  C  CB    . THR B 1 395 ? 126.005 158.870 127.105 1.00 33.48 ?  395 THR B CB    1 
ATOM   8749  O  OG1   . THR B 1 395 ? 127.154 159.647 127.460 1.00 37.99 ?  395 THR B OG1   1 
ATOM   8750  C  CG2   . THR B 1 395 ? 124.835 159.292 127.977 1.00 31.09 ?  395 THR B CG2   1 
ATOM   8751  N  N     . ASP B 1 396 ? 127.247 157.184 125.081 1.00 36.25 ?  396 ASP B N     1 
ATOM   8752  C  CA    . ASP B 1 396 ? 128.225 156.771 124.091 1.00 36.37 ?  396 ASP B CA    1 
ATOM   8753  C  C     . ASP B 1 396 ? 129.539 157.522 124.285 1.00 36.41 ?  396 ASP B C     1 
ATOM   8754  O  O     . ASP B 1 396 ? 129.592 158.597 124.887 1.00 40.32 ?  396 ASP B O     1 
ATOM   8755  C  CB    . ASP B 1 396 ? 127.697 157.008 122.675 1.00 36.41 ?  396 ASP B CB    1 
ATOM   8756  C  CG    . ASP B 1 396 ? 126.314 156.429 122.464 1.00 42.76 ?  396 ASP B CG    1 
ATOM   8757  O  OD1   . ASP B 1 396 ? 126.075 155.284 122.898 1.00 39.73 ?  396 ASP B OD1   1 
ATOM   8758  O  OD2   . ASP B 1 396 ? 125.469 157.118 121.855 1.00 45.48 -1 396 ASP B OD2   1 
ATOM   8759  N  N     . TYR B 1 397 ? 130.611 156.932 123.763 1.00 37.62 ?  397 TYR B N     1 
ATOM   8760  C  CA    . TYR B 1 397 ? 131.915 157.576 123.805 1.00 38.54 ?  397 TYR B CA    1 
ATOM   8761  C  C     . TYR B 1 397 ? 131.838 158.970 123.196 1.00 40.30 ?  397 TYR B C     1 
ATOM   8762  O  O     . TYR B 1 397 ? 131.167 159.188 122.185 1.00 45.98 ?  397 TYR B O     1 
ATOM   8763  C  CB    . TYR B 1 397 ? 132.947 156.733 123.054 1.00 34.78 ?  397 TYR B CB    1 
ATOM   8764  C  CG    . TYR B 1 397 ? 134.369 156.981 123.497 1.00 35.71 ?  397 TYR B CG    1 
ATOM   8765  C  CD1   . TYR B 1 397 ? 134.940 156.231 124.515 1.00 36.78 ?  397 TYR B CD1   1 
ATOM   8766  C  CD2   . TYR B 1 397 ? 135.134 157.975 122.904 1.00 35.36 ?  397 TYR B CD2   1 
ATOM   8767  C  CE1   . TYR B 1 397 ? 136.238 156.457 124.921 1.00 36.03 ?  397 TYR B CE1   1 
ATOM   8768  C  CE2   . TYR B 1 397 ? 136.430 158.210 123.306 1.00 32.68 ?  397 TYR B CE2   1 
ATOM   8769  C  CZ    . TYR B 1 397 ? 136.978 157.448 124.315 1.00 35.18 ?  397 TYR B CZ    1 
ATOM   8770  O  OH    . TYR B 1 397 ? 138.271 157.681 124.716 1.00 39.83 ?  397 TYR B OH    1 
ATOM   8771  N  N     . ASP B 1 398 ? 132.533 159.915 123.823 1.00 39.08 ?  398 ASP B N     1 
ATOM   8772  C  CA    . ASP B 1 398 ? 132.586 161.325 123.450 1.00 46.27 ?  398 ASP B CA    1 
ATOM   8773  C  C     . ASP B 1 398 ? 131.348 162.079 123.922 1.00 45.80 ?  398 ASP B C     1 
ATOM   8774  O  O     . ASP B 1 398 ? 131.276 163.298 123.722 1.00 45.61 ?  398 ASP B O     1 
ATOM   8775  C  CB    . ASP B 1 398 ? 132.754 161.536 121.937 1.00 46.45 ?  398 ASP B CB    1 
ATOM   8776  C  CG    . ASP B 1 398 ? 134.106 161.074 121.432 1.00 50.07 ?  398 ASP B CG    1 
ATOM   8777  O  OD1   . ASP B 1 398 ? 135.089 161.157 122.200 1.00 51.09 ?  398 ASP B OD1   1 
ATOM   8778  O  OD2   . ASP B 1 398 ? 134.188 160.627 120.269 1.00 49.31 -1 398 ASP B OD2   1 
ATOM   8779  N  N     . GLU B 1 399 ? 130.377 161.409 124.533 1.00 45.21 ?  399 GLU B N     1 
ATOM   8780  C  CA    . GLU B 1 399 ? 129.254 162.069 125.174 1.00 41.95 ?  399 GLU B CA    1 
ATOM   8781  C  C     . GLU B 1 399 ? 129.515 162.185 126.669 1.00 45.19 ?  399 GLU B C     1 
ATOM   8782  O  O     . GLU B 1 399 ? 130.370 161.491 127.224 1.00 44.07 ?  399 GLU B O     1 
ATOM   8783  C  CB    . GLU B 1 399 ? 127.950 161.306 124.930 1.00 40.26 ?  399 GLU B CB    1 
ATOM   8784  C  CG    . GLU B 1 399 ? 127.429 161.408 123.508 1.00 43.18 ?  399 GLU B CG    1 
ATOM   8785  C  CD    . GLU B 1 399 ? 126.001 160.912 123.372 1.00 48.76 ?  399 GLU B CD    1 
ATOM   8786  O  OE1   . GLU B 1 399 ? 125.619 159.977 124.107 1.00 46.02 ?  399 GLU B OE1   1 
ATOM   8787  O  OE2   . GLU B 1 399 ? 125.260 161.456 122.526 1.00 49.74 -1 399 GLU B OE2   1 
ATOM   8788  N  N     . GLU B 1 400 ? 128.769 163.073 127.320 1.00 47.68 ?  400 GLU B N     1 
ATOM   8789  C  CA    . GLU B 1 400 ? 128.914 163.270 128.753 1.00 41.98 ?  400 GLU B CA    1 
ATOM   8790  C  C     . GLU B 1 400 ? 128.058 162.264 129.510 1.00 43.52 ?  400 GLU B C     1 
ATOM   8791  O  O     . GLU B 1 400 ? 126.873 162.090 129.206 1.00 41.72 ?  400 GLU B O     1 
ATOM   8792  C  CB    . GLU B 1 400 ? 128.525 164.695 129.142 1.00 42.12 ?  400 GLU B CB    1 
ATOM   8793  C  CG    . GLU B 1 400 ? 129.637 165.714 128.959 1.00 46.17 ?  400 GLU B CG    1 
ATOM   8794  C  CD    . GLU B 1 400 ? 130.993 165.191 129.398 1.00 50.67 ?  400 GLU B CD    1 
ATOM   8795  O  OE1   . GLU B 1 400 ? 131.040 164.323 130.295 1.00 49.35 ?  400 GLU B OE1   1 
ATOM   8796  O  OE2   . GLU B 1 400 ? 132.013 165.647 128.842 1.00 49.26 -1 400 GLU B OE2   1 
ATOM   8797  N  N     . ASP B 1 401 ? 128.661 161.600 130.491 1.00 39.92 ?  401 ASP B N     1 
ATOM   8798  C  CA    . ASP B 1 401 ? 127.945 160.636 131.311 1.00 35.02 ?  401 ASP B CA    1 
ATOM   8799  C  C     . ASP B 1 401 ? 127.198 161.342 132.433 1.00 34.68 ?  401 ASP B C     1 
ATOM   8800  O  O     . ASP B 1 401 ? 127.703 162.294 133.034 1.00 38.67 ?  401 ASP B O     1 
ATOM   8801  C  CB    . ASP B 1 401 ? 128.913 159.610 131.901 1.00 31.67 ?  401 ASP B CB    1 
ATOM   8802  C  CG    . ASP B 1 401 ? 129.438 158.640 130.867 1.00 41.34 ?  401 ASP B CG    1 
ATOM   8803  O  OD1   . ASP B 1 401 ? 128.677 158.285 129.941 1.00 46.91 ?  401 ASP B OD1   1 
ATOM   8804  O  OD2   . ASP B 1 401 ? 130.611 158.229 130.980 1.00 39.70 -1 401 ASP B OD2   1 
ATOM   8805  N  N     . GLU B 1 402 ? 125.988 160.868 132.713 1.00 32.62 ?  402 GLU B N     1 
ATOM   8806  C  CA    . GLU B 1 402 ? 125.213 161.345 133.855 1.00 30.27 ?  402 GLU B CA    1 
ATOM   8807  C  C     . GLU B 1 402 ? 125.566 160.459 135.041 1.00 24.13 ?  402 GLU B C     1 
ATOM   8808  O  O     . GLU B 1 402 ? 125.038 159.355 135.185 1.00 29.03 ?  402 GLU B O     1 
ATOM   8809  C  CB    . GLU B 1 402 ? 123.719 161.317 133.551 1.00 31.98 ?  402 GLU B CB    1 
ATOM   8810  C  CG    . GLU B 1 402 ? 122.861 162.054 134.571 1.00 35.22 ?  402 GLU B CG    1 
ATOM   8811  C  CD    . GLU B 1 402 ? 122.600 161.237 135.824 1.00 40.72 ?  402 GLU B CD    1 
ATOM   8812  O  OE1   . GLU B 1 402 ? 122.479 159.998 135.717 1.00 38.59 ?  402 GLU B OE1   1 
ATOM   8813  O  OE2   . GLU B 1 402 ? 122.518 161.834 136.919 1.00 37.10 -1 402 GLU B OE2   1 
ATOM   8814  N  N     . ILE B 1 403 ? 126.468 160.940 135.889 1.00 24.67 ?  403 ILE B N     1 
ATOM   8815  C  CA    . ILE B 1 403 ? 126.950 160.153 137.018 1.00 27.94 ?  403 ILE B CA    1 
ATOM   8816  C  C     . ILE B 1 403 ? 125.946 160.262 138.156 1.00 29.67 ?  403 ILE B C     1 
ATOM   8817  O  O     . ILE B 1 403 ? 125.595 161.366 138.588 1.00 24.12 ?  403 ILE B O     1 
ATOM   8818  C  CB    . ILE B 1 403 ? 128.344 160.619 137.463 1.00 21.11 ?  403 ILE B CB    1 
ATOM   8819  C  CG1   . ILE B 1 403 ? 129.339 160.497 136.306 1.00 24.43 ?  403 ILE B CG1   1 
ATOM   8820  C  CG2   . ILE B 1 403 ? 128.812 159.819 138.666 1.00 17.50 ?  403 ILE B CG2   1 
ATOM   8821  C  CD1   . ILE B 1 403 ? 129.314 159.155 135.620 1.00 24.81 ?  403 ILE B CD1   1 
ATOM   8822  N  N     . GLY B 1 404 ? 125.480 159.120 138.640 1.00 21.73 ?  404 GLY B N     1 
ATOM   8823  C  CA    . GLY B 1 404 ? 124.550 159.046 139.743 1.00 8.01  ?  404 GLY B CA    1 
ATOM   8824  C  C     . GLY B 1 404 ? 125.247 158.822 141.067 1.00 18.00 ?  404 GLY B C     1 
ATOM   8825  O  O     . GLY B 1 404 ? 126.377 159.273 141.288 1.00 29.33 ?  404 GLY B O     1 
ATOM   8826  N  N     . LEU B 1 405 ? 124.571 158.110 141.962 1.00 22.59 ?  405 LEU B N     1 
ATOM   8827  C  CA    . LEU B 1 405 ? 125.095 157.818 143.289 1.00 6.11  ?  405 LEU B CA    1 
ATOM   8828  C  C     . LEU B 1 405 ? 125.132 156.313 143.494 1.00 6.10  ?  405 LEU B C     1 
ATOM   8829  O  O     . LEU B 1 405 ? 124.084 155.661 143.524 1.00 16.38 ?  405 LEU B O     1 
ATOM   8830  C  CB    . LEU B 1 405 ? 124.247 158.485 144.373 1.00 17.98 ?  405 LEU B CB    1 
ATOM   8831  C  CG    . LEU B 1 405 ? 124.247 160.012 144.398 1.00 17.32 ?  405 LEU B CG    1 
ATOM   8832  C  CD1   . LEU B 1 405 ? 123.250 160.530 145.419 1.00 17.90 ?  405 LEU B CD1   1 
ATOM   8833  C  CD2   . LEU B 1 405 ? 125.641 160.542 144.682 1.00 16.09 ?  405 LEU B CD2   1 
ATOM   8834  N  N     . ASP B 1 406 ? 126.334 155.767 143.633 1.00 18.07 ?  406 ASP B N     1 
ATOM   8835  C  CA    . ASP B 1 406 ? 126.521 154.387 144.042 1.00 8.78  ?  406 ASP B CA    1 
ATOM   8836  C  C     . ASP B 1 406 ? 126.612 154.332 145.564 1.00 18.39 ?  406 ASP B C     1 
ATOM   8837  O  O     . ASP B 1 406 ? 126.511 155.345 146.257 1.00 25.39 ?  406 ASP B O     1 
ATOM   8838  C  CB    . ASP B 1 406 ? 127.761 153.790 143.376 1.00 14.27 ?  406 ASP B CB    1 
ATOM   8839  C  CG    . ASP B 1 406 ? 127.459 153.192 142.015 1.00 24.80 ?  406 ASP B CG    1 
ATOM   8840  O  OD1   . ASP B 1 406 ? 126.268 152.969 141.709 1.00 25.98 ?  406 ASP B OD1   1 
ATOM   8841  O  OD2   . ASP B 1 406 ? 128.412 152.949 141.248 1.00 33.29 -1 406 ASP B OD2   1 
ATOM   8842  N  N     . ILE B 1 407 ? 126.792 153.130 146.098 1.00 23.34 ?  407 ILE B N     1 
ATOM   8843  C  CA    . ILE B 1 407 ? 126.822 152.923 147.539 1.00 14.16 ?  407 ILE B CA    1 
ATOM   8844  C  C     . ILE B 1 407 ? 128.146 152.281 147.925 1.00 16.84 ?  407 ILE B C     1 
ATOM   8845  O  O     . ILE B 1 407 ? 128.614 151.346 147.266 1.00 21.85 ?  407 ILE B O     1 
ATOM   8846  C  CB    . ILE B 1 407 ? 125.635 152.064 148.020 1.00 15.36 ?  407 ILE B CB    1 
ATOM   8847  C  CG1   . ILE B 1 407 ? 124.315 152.794 147.771 1.00 5.71  ?  407 ILE B CG1   1 
ATOM   8848  C  CG2   . ILE B 1 407 ? 125.785 151.737 149.490 1.00 12.45 ?  407 ILE B CG2   1 
ATOM   8849  C  CD1   . ILE B 1 407 ? 123.186 151.880 147.359 1.00 16.82 ?  407 ILE B CD1   1 
ATOM   8850  N  N     . SER B 1 408 ? 128.752 152.805 148.986 1.00 21.78 ?  408 SER B N     1 
ATOM   8851  C  CA    . SER B 1 408 ? 129.920 152.200 149.607 1.00 18.49 ?  408 SER B CA    1 
ATOM   8852  C  C     . SER B 1 408 ? 130.050 152.760 151.013 1.00 20.79 ?  408 SER B C     1 
ATOM   8853  O  O     . SER B 1 408 ? 129.881 153.964 151.225 1.00 35.49 ?  408 SER B O     1 
ATOM   8854  C  CB    . SER B 1 408 ? 131.199 152.467 148.805 1.00 21.13 ?  408 SER B CB    1 
ATOM   8855  O  OG    . SER B 1 408 ? 131.567 153.834 148.865 1.00 27.24 ?  408 SER B OG    1 
ATOM   8856  N  N     . CYS B 1 409 ? 130.341 151.886 151.970 1.00 20.14 ?  409 CYS B N     1 
ATOM   8857  C  CA    . CYS B 1 409 ? 130.604 152.312 153.334 1.00 30.23 ?  409 CYS B CA    1 
ATOM   8858  C  C     . CYS B 1 409 ? 131.785 151.528 153.880 1.00 25.45 ?  409 CYS B C     1 
ATOM   8859  O  O     . CYS B 1 409 ? 131.933 150.333 153.615 1.00 32.43 ?  409 CYS B O     1 
ATOM   8860  C  CB    . CYS B 1 409 ? 129.373 152.132 154.241 1.00 22.01 ?  409 CYS B CB    1 
ATOM   8861  S  SG    . CYS B 1 409 ? 128.939 150.418 154.608 1.00 42.52 ?  409 CYS B SG    1 
ATOM   8862  N  N     . ASN B 1 410 ? 132.629 152.217 154.637 1.00 19.03 ?  410 ASN B N     1 
ATOM   8863  C  CA    . ASN B 1 410 ? 133.739 151.586 155.333 1.00 22.91 ?  410 ASN B CA    1 
ATOM   8864  C  C     . ASN B 1 410 ? 133.273 151.160 156.717 1.00 21.62 ?  410 ASN B C     1 
ATOM   8865  O  O     . ASN B 1 410 ? 132.583 151.912 157.410 1.00 22.49 ?  410 ASN B O     1 
ATOM   8866  C  CB    . ASN B 1 410 ? 134.938 152.531 155.430 1.00 22.82 ?  410 ASN B CB    1 
ATOM   8867  C  CG    . ASN B 1 410 ? 134.552 153.914 155.906 1.00 27.28 ?  410 ASN B CG    1 
ATOM   8868  O  OD1   . ASN B 1 410 ? 133.773 154.612 155.258 1.00 30.33 ?  410 ASN B OD1   1 
ATOM   8869  N  ND2   . ASN B 1 410 ? 135.102 154.321 157.040 1.00 30.30 ?  410 ASN B ND2   1 
ATOM   8870  N  N     . LEU B 1 411 ? 133.650 149.950 157.112 1.00 19.04 ?  411 LEU B N     1 
ATOM   8871  C  CA    . LEU B 1 411 ? 133.077 149.305 158.280 1.00 14.14 ?  411 LEU B CA    1 
ATOM   8872  C  C     . LEU B 1 411 ? 134.034 149.336 159.464 1.00 14.23 ?  411 LEU B C     1 
ATOM   8873  O  O     . LEU B 1 411 ? 135.258 149.364 159.307 1.00 22.28 ?  411 LEU B O     1 
ATOM   8874  C  CB    . LEU B 1 411 ? 132.699 147.853 157.976 1.00 20.10 ?  411 LEU B CB    1 
ATOM   8875  C  CG    . LEU B 1 411 ? 132.151 147.568 156.580 1.00 16.74 ?  411 LEU B CG    1 
ATOM   8876  C  CD1   . LEU B 1 411 ? 131.842 146.091 156.424 1.00 18.86 ?  411 LEU B CD1   1 
ATOM   8877  C  CD2   . LEU B 1 411 ? 130.919 148.410 156.315 1.00 18.00 ?  411 LEU B CD2   1 
ATOM   8878  N  N     . GLY B 1 412 ? 133.442 149.341 160.651 1.00 18.22 ?  412 GLY B N     1 
ATOM   8879  C  CA    . GLY B 1 412 ? 134.168 149.099 161.881 1.00 9.78  ?  412 GLY B CA    1 
ATOM   8880  C  C     . GLY B 1 412 ? 133.198 148.499 162.874 1.00 13.76 ?  412 GLY B C     1 
ATOM   8881  O  O     . GLY B 1 412 ? 131.989 148.744 162.814 1.00 22.99 ?  412 GLY B O     1 
ATOM   8882  N  N     . SER B 1 413 ? 133.736 147.703 163.788 1.00 13.81 ?  413 SER B N     1 
ATOM   8883  C  CA    . SER B 1 413 ? 132.921 146.962 164.740 1.00 11.40 ?  413 SER B CA    1 
ATOM   8884  C  C     . SER B 1 413 ? 133.304 147.338 166.160 1.00 15.77 ?  413 SER B C     1 
ATOM   8885  O  O     . SER B 1 413 ? 134.489 147.349 166.509 1.00 26.69 ?  413 SER B O     1 
ATOM   8886  C  CB    . SER B 1 413 ? 133.072 145.453 164.538 1.00 12.62 ?  413 SER B CB    1 
ATOM   8887  O  OG    . SER B 1 413 ? 132.284 145.004 163.452 1.00 26.47 ?  413 SER B OG    1 
ATOM   8888  N  N     . LEU B 1 414 ? 132.301 147.651 166.971 1.00 18.51 ?  414 LEU B N     1 
ATOM   8889  C  CA    . LEU B 1 414 ? 132.497 147.756 168.406 1.00 13.26 ?  414 LEU B CA    1 
ATOM   8890  C  C     . LEU B 1 414 ? 132.561 146.363 169.010 1.00 17.39 ?  414 LEU B C     1 
ATOM   8891  O  O     . LEU B 1 414 ? 131.775 145.481 168.656 1.00 21.11 ?  414 LEU B O     1 
ATOM   8892  C  CB    . LEU B 1 414 ? 131.364 148.550 169.055 1.00 18.94 ?  414 LEU B CB    1 
ATOM   8893  C  CG    . LEU B 1 414 ? 131.074 149.950 168.519 1.00 15.44 ?  414 LEU B CG    1 
ATOM   8894  C  CD1   . LEU B 1 414 ? 129.888 150.548 169.248 1.00 17.84 ?  414 LEU B CD1   1 
ATOM   8895  C  CD2   . LEU B 1 414 ? 132.297 150.838 168.656 1.00 20.50 ?  414 LEU B CD2   1 
ATOM   8896  N  N     . ASN B 1 415 ? 133.510 146.162 169.917 1.00 25.62 ?  415 ASN B N     1 
ATOM   8897  C  CA    . ASN B 1 415 ? 133.577 144.930 170.696 1.00 22.83 ?  415 ASN B CA    1 
ATOM   8898  C  C     . ASN B 1 415 ? 132.682 145.136 171.911 1.00 23.39 ?  415 ASN B C     1 
ATOM   8899  O  O     . ASN B 1 415 ? 133.057 145.819 172.865 1.00 33.12 ?  415 ASN B O     1 
ATOM   8900  C  CB    . ASN B 1 415 ? 135.013 144.607 171.088 1.00 24.78 ?  415 ASN B CB    1 
ATOM   8901  C  CG    . ASN B 1 415 ? 135.181 143.175 171.553 1.00 25.03 ?  415 ASN B CG    1 
ATOM   8902  O  OD1   . ASN B 1 415 ? 134.339 142.641 172.269 1.00 31.25 ?  415 ASN B OD1   1 
ATOM   8903  N  ND2   . ASN B 1 415 ? 136.272 142.545 171.139 1.00 25.30 ?  415 ASN B ND2   1 
ATOM   8904  N  N     . ILE B 1 416 ? 131.489 144.542 171.870 1.00 15.73 ?  416 ILE B N     1 
ATOM   8905  C  CA    . ILE B 1 416 ? 130.475 144.841 172.877 1.00 17.81 ?  416 ILE B CA    1 
ATOM   8906  C  C     . ILE B 1 416 ? 130.973 144.473 174.268 1.00 22.98 ?  416 ILE B C     1 
ATOM   8907  O  O     . ILE B 1 416 ? 130.790 145.232 175.227 1.00 27.39 ?  416 ILE B O     1 
ATOM   8908  C  CB    . ILE B 1 416 ? 129.155 144.123 172.535 1.00 23.52 ?  416 ILE B CB    1 
ATOM   8909  C  CG1   . ILE B 1 416 ? 128.515 144.758 171.301 1.00 19.24 ?  416 ILE B CG1   1 
ATOM   8910  C  CG2   . ILE B 1 416 ? 128.203 144.178 173.714 1.00 10.93 ?  416 ILE B CG2   1 
ATOM   8911  C  CD1   . ILE B 1 416 ? 127.378 143.955 170.714 1.00 16.26 ?  416 ILE B CD1   1 
ATOM   8912  N  N     . LEU B 1 417 ? 131.608 143.309 174.403 1.00 24.44 ?  417 LEU B N     1 
ATOM   8913  C  CA    . LEU B 1 417 ? 132.104 142.891 175.709 1.00 26.77 ?  417 LEU B CA    1 
ATOM   8914  C  C     . LEU B 1 417 ? 133.142 143.870 176.243 1.00 28.41 ?  417 LEU B C     1 
ATOM   8915  O  O     . LEU B 1 417 ? 133.090 144.273 177.411 1.00 34.53 ?  417 LEU B O     1 
ATOM   8916  C  CB    . LEU B 1 417 ? 132.689 141.480 175.619 1.00 31.25 ?  417 LEU B CB    1 
ATOM   8917  C  CG    . LEU B 1 417 ? 133.483 141.005 176.836 1.00 28.44 ?  417 LEU B CG    1 
ATOM   8918  C  CD1   . LEU B 1 417 ? 132.576 140.893 178.051 1.00 30.62 ?  417 LEU B CD1   1 
ATOM   8919  C  CD2   . LEU B 1 417 ? 134.163 139.680 176.552 1.00 31.30 ?  417 LEU B CD2   1 
ATOM   8920  N  N     . ASN B 1 418 ? 134.090 144.273 175.396 1.00 26.51 ?  418 ASN B N     1 
ATOM   8921  C  CA    . ASN B 1 418 ? 135.145 145.177 175.843 1.00 27.75 ?  418 ASN B CA    1 
ATOM   8922  C  C     . ASN B 1 418 ? 134.608 146.581 176.084 1.00 27.45 ?  418 ASN B C     1 
ATOM   8923  O  O     . ASN B 1 418 ? 135.029 147.257 177.029 1.00 30.46 ?  418 ASN B O     1 
ATOM   8924  C  CB    . ASN B 1 418 ? 136.280 145.201 174.820 1.00 29.75 ?  418 ASN B CB    1 
ATOM   8925  C  CG    . ASN B 1 418 ? 137.145 143.960 174.881 1.00 27.10 ?  418 ASN B CG    1 
ATOM   8926  O  OD1   . ASN B 1 418 ? 137.526 143.404 173.853 1.00 26.94 ?  418 ASN B OD1   1 
ATOM   8927  N  ND2   . ASN B 1 418 ? 137.460 143.519 176.091 1.00 31.68 ?  418 ASN B ND2   1 
ATOM   8928  N  N     . VAL B 1 419 ? 133.682 147.039 175.240 1.00 27.92 ?  419 VAL B N     1 
ATOM   8929  C  CA    . VAL B 1 419 ? 133.090 148.359 175.435 1.00 28.70 ?  419 VAL B CA    1 
ATOM   8930  C  C     . VAL B 1 419 ? 132.314 148.405 176.743 1.00 30.74 ?  419 VAL B C     1 
ATOM   8931  O  O     . VAL B 1 419 ? 132.370 149.396 177.482 1.00 32.93 ?  419 VAL B O     1 
ATOM   8932  C  CB    . VAL B 1 419 ? 132.201 148.729 174.234 1.00 27.36 ?  419 VAL B CB    1 
ATOM   8933  C  CG1   . VAL B 1 419 ? 131.305 149.903 174.580 1.00 27.55 ?  419 VAL B CG1   1 
ATOM   8934  C  CG2   . VAL B 1 419 ? 133.058 149.048 173.021 1.00 22.80 ?  419 VAL B CG2   1 
ATOM   8935  N  N     . MET B 1 420 ? 131.572 147.339 177.049 1.00 34.06 ?  420 MET B N     1 
ATOM   8936  C  CA    . MET B 1 420 ? 130.790 147.311 178.279 1.00 30.03 ?  420 MET B CA    1 
ATOM   8937  C  C     . MET B 1 420 ? 131.683 147.160 179.504 1.00 28.59 ?  420 MET B C     1 
ATOM   8938  O  O     . MET B 1 420 ? 131.405 147.746 180.556 1.00 32.07 ?  420 MET B O     1 
ATOM   8939  C  CB    . MET B 1 420 ? 129.759 146.185 178.215 1.00 29.07 ?  420 MET B CB    1 
ATOM   8940  C  CG    . MET B 1 420 ? 128.605 146.469 177.271 1.00 22.73 ?  420 MET B CG    1 
ATOM   8941  S  SD    . MET B 1 420 ? 127.486 147.732 177.904 1.00 42.68 ?  420 MET B SD    1 
ATOM   8942  C  CE    . MET B 1 420 ? 127.224 147.144 179.573 1.00 28.85 ?  420 MET B CE    1 
ATOM   8943  N  N     . GLU B 1 421 ? 132.756 146.374 179.391 1.00 37.15 ?  421 GLU B N     1 
ATOM   8944  C  CA    . GLU B 1 421 ? 133.681 146.228 180.510 1.00 34.95 ?  421 GLU B CA    1 
ATOM   8945  C  C     . GLU B 1 421 ? 134.379 147.545 180.826 1.00 34.49 ?  421 GLU B C     1 
ATOM   8946  O  O     . GLU B 1 421 ? 134.591 147.876 181.998 1.00 38.90 ?  421 GLU B O     1 
ATOM   8947  C  CB    . GLU B 1 421 ? 134.702 145.131 180.208 1.00 30.94 ?  421 GLU B CB    1 
ATOM   8948  C  CG    . GLU B 1 421 ? 136.054 145.642 179.743 1.00 37.61 ?  421 GLU B CG    1 
ATOM   8949  C  CD    . GLU B 1 421 ? 137.107 144.552 179.698 1.00 43.51 ?  421 GLU B CD    1 
ATOM   8950  O  OE1   . GLU B 1 421 ? 137.569 144.125 180.776 1.00 42.80 ?  421 GLU B OE1   1 
ATOM   8951  O  OE2   . GLU B 1 421 ? 137.472 144.122 178.583 1.00 39.06 -1 421 GLU B OE2   1 
ATOM   8952  N  N     . HIS B 1 422 ? 134.745 148.309 179.796 1.00 33.92 ?  422 HIS B N     1 
ATOM   8953  C  CA    . HIS B 1 422 ? 135.396 149.597 179.992 1.00 32.48 ?  422 HIS B CA    1 
ATOM   8954  C  C     . HIS B 1 422 ? 134.412 150.737 180.213 1.00 37.92 ?  422 HIS B C     1 
ATOM   8955  O  O     . HIS B 1 422 ? 134.845 151.852 180.521 1.00 39.30 ?  422 HIS B O     1 
ATOM   8956  C  CB    . HIS B 1 422 ? 136.288 149.927 178.792 1.00 31.39 ?  422 HIS B CB    1 
ATOM   8957  C  CG    . HIS B 1 422 ? 137.508 149.066 178.689 1.00 37.42 ?  422 HIS B CG    1 
ATOM   8958  N  ND1   . HIS B 1 422 ? 137.524 147.878 177.991 1.00 36.69 ?  422 HIS B ND1   1 
ATOM   8959  C  CD2   . HIS B 1 422 ? 138.756 149.225 179.190 1.00 37.38 ?  422 HIS B CD2   1 
ATOM   8960  C  CE1   . HIS B 1 422 ? 138.728 147.340 178.070 1.00 38.64 ?  422 HIS B CE1   1 
ATOM   8961  N  NE2   . HIS B 1 422 ? 139.494 148.137 178.792 1.00 38.15 ?  422 HIS B NE2   1 
ATOM   8962  N  N     . LYS B 1 423 ? 133.111 150.488 180.071 1.00 41.75 ?  423 LYS B N     1 
ATOM   8963  C  CA    . LYS B 1 423 ? 132.094 151.522 180.248 1.00 38.97 ?  423 LYS B CA    1 
ATOM   8964  C  C     . LYS B 1 423 ? 132.391 152.728 179.360 1.00 40.81 ?  423 LYS B C     1 
ATOM   8965  O  O     . LYS B 1 423 ? 132.363 153.880 179.797 1.00 42.37 ?  423 LYS B O     1 
ATOM   8966  C  CB    . LYS B 1 423 ? 131.988 151.935 181.716 1.00 39.08 ?  423 LYS B CB    1 
ATOM   8967  C  CG    . LYS B 1 423 ? 131.364 150.886 182.616 1.00 40.16 ?  423 LYS B CG    1 
ATOM   8968  C  CD    . LYS B 1 423 ? 131.459 151.286 184.078 1.00 43.62 ?  423 LYS B CD    1 
ATOM   8969  C  CE    . LYS B 1 423 ? 131.761 150.087 184.963 1.00 44.11 ?  423 LYS B CE    1 
ATOM   8970  N  NZ    . LYS B 1 423 ? 130.645 149.102 184.967 1.00 44.86 1  423 LYS B NZ    1 
ATOM   8971  N  N     . SER B 1 424 ? 132.674 152.450 178.091 1.00 34.79 ?  424 SER B N     1 
ATOM   8972  C  CA    . SER B 1 424 ? 133.144 153.455 177.144 1.00 30.35 ?  424 SER B CA    1 
ATOM   8973  C  C     . SER B 1 424 ? 132.349 153.391 175.847 1.00 30.17 ?  424 SER B C     1 
ATOM   8974  O  O     . SER B 1 424 ? 132.904 153.381 174.747 1.00 38.81 ?  424 SER B O     1 
ATOM   8975  C  CB    . SER B 1 424 ? 134.633 153.277 176.868 1.00 33.76 ?  424 SER B CB    1 
ATOM   8976  O  OG    . SER B 1 424 ? 134.888 152.028 176.252 1.00 32.33 ?  424 SER B OG    1 
ATOM   8977  N  N     . ILE B 1 425 ? 131.021 153.347 175.958 1.00 30.70 ?  425 ILE B N     1 
ATOM   8978  C  CA    . ILE B 1 425 ? 130.186 153.356 174.761 1.00 25.53 ?  425 ILE B CA    1 
ATOM   8979  C  C     . ILE B 1 425 ? 130.335 154.679 174.021 1.00 30.94 ?  425 ILE B C     1 
ATOM   8980  O  O     . ILE B 1 425 ? 130.550 154.707 172.804 1.00 33.11 ?  425 ILE B O     1 
ATOM   8981  C  CB    . ILE B 1 425 ? 128.717 153.076 175.122 1.00 28.64 ?  425 ILE B CB    1 
ATOM   8982  C  CG1   . ILE B 1 425 ? 128.544 151.632 175.592 1.00 31.40 ?  425 ILE B CG1   1 
ATOM   8983  C  CG2   . ILE B 1 425 ? 127.816 153.361 173.931 1.00 27.41 ?  425 ILE B CG2   1 
ATOM   8984  C  CD1   . ILE B 1 425 ? 127.123 151.287 175.972 1.00 32.31 ?  425 ILE B CD1   1 
ATOM   8985  N  N     . GLU B 1 426 ? 130.239 155.795 174.745 1.00 31.97 ?  426 GLU B N     1 
ATOM   8986  C  CA    . GLU B 1 426 ? 130.316 157.104 174.103 1.00 29.03 ?  426 GLU B CA    1 
ATOM   8987  C  C     . GLU B 1 426 ? 131.677 157.326 173.457 1.00 29.47 ?  426 GLU B C     1 
ATOM   8988  O  O     . GLU B 1 426 ? 131.769 157.661 172.269 1.00 36.02 ?  426 GLU B O     1 
ATOM   8989  C  CB    . GLU B 1 426 ? 130.021 158.202 175.124 1.00 27.18 ?  426 GLU B CB    1 
ATOM   8990  C  CG    . GLU B 1 426 ? 130.346 159.601 174.639 1.00 32.04 ?  426 GLU B CG    1 
ATOM   8991  C  CD    . GLU B 1 426 ? 130.100 160.655 175.697 1.00 39.22 ?  426 GLU B CD    1 
ATOM   8992  O  OE1   . GLU B 1 426 ? 129.734 160.288 176.832 1.00 39.49 ?  426 GLU B OE1   1 
ATOM   8993  O  OE2   . GLU B 1 426 ? 130.271 161.855 175.393 1.00 39.36 -1 426 GLU B OE2   1 
ATOM   8994  N  N     . LYS B 1 427 ? 132.750 157.141 174.228 1.00 31.23 ?  427 LYS B N     1 
ATOM   8995  C  CA    . LYS B 1 427 ? 134.090 157.397 173.711 1.00 30.44 ?  427 LYS B CA    1 
ATOM   8996  C  C     . LYS B 1 427 ? 134.425 156.455 172.562 1.00 33.86 ?  427 LYS B C     1 
ATOM   8997  O  O     . LYS B 1 427 ? 134.955 156.880 171.529 1.00 34.92 ?  427 LYS B O     1 
ATOM   8998  C  CB    . LYS B 1 427 ? 135.118 157.262 174.836 1.00 31.07 ?  427 LYS B CB    1 
ATOM   8999  C  CG    . LYS B 1 427 ? 136.556 157.467 174.394 1.00 35.81 ?  427 LYS B CG    1 
ATOM   9000  C  CD    . LYS B 1 427 ? 137.535 157.108 175.500 1.00 37.25 ?  427 LYS B CD    1 
ATOM   9001  C  CE    . LYS B 1 427 ? 137.463 155.629 175.847 1.00 37.06 ?  427 LYS B CE    1 
ATOM   9002  N  NZ    . LYS B 1 427 ? 137.387 154.773 174.631 1.00 37.56 1  427 LYS B NZ    1 
ATOM   9003  N  N     . THR B 1 428 ? 134.124 155.166 172.728 1.00 29.29 ?  428 THR B N     1 
ATOM   9004  C  CA    . THR B 1 428 ? 134.413 154.203 171.672 1.00 24.88 ?  428 THR B CA    1 
ATOM   9005  C  C     . THR B 1 428 ? 133.633 154.525 170.406 1.00 24.36 ?  428 THR B C     1 
ATOM   9006  O  O     . THR B 1 428 ? 134.189 154.495 169.303 1.00 29.13 ?  428 THR B O     1 
ATOM   9007  C  CB    . THR B 1 428 ? 134.094 152.784 172.147 1.00 23.23 ?  428 THR B CB    1 
ATOM   9008  O  OG1   . THR B 1 428 ? 134.931 152.452 173.262 1.00 29.92 ?  428 THR B OG1   1 
ATOM   9009  C  CG2   . THR B 1 428 ? 134.330 151.782 171.030 1.00 19.13 ?  428 THR B CG2   1 
ATOM   9010  N  N     . VAL B 1 429 ? 132.346 154.848 170.545 1.00 20.59 ?  429 VAL B N     1 
ATOM   9011  C  CA    . VAL B 1 429 ? 131.526 155.144 169.375 1.00 24.86 ?  429 VAL B CA    1 
ATOM   9012  C  C     . VAL B 1 429 ? 132.047 156.382 168.660 1.00 22.70 ?  429 VAL B C     1 
ATOM   9013  O  O     . VAL B 1 429 ? 132.153 156.404 167.428 1.00 25.40 ?  429 VAL B O     1 
ATOM   9014  C  CB    . VAL B 1 429 ? 130.049 155.302 169.783 1.00 22.28 ?  429 VAL B CB    1 
ATOM   9015  C  CG1   . VAL B 1 429 ? 129.253 155.933 168.656 1.00 19.02 ?  429 VAL B CG1   1 
ATOM   9016  C  CG2   . VAL B 1 429 ? 129.458 153.956 170.166 1.00 20.46 ?  429 VAL B CG2   1 
ATOM   9017  N  N     . LYS B 1 430 ? 132.385 157.429 169.413 1.00 24.60 ?  430 LYS B N     1 
ATOM   9018  C  CA    . LYS B 1 430 ? 132.860 158.656 168.782 1.00 18.25 ?  430 LYS B CA    1 
ATOM   9019  C  C     . LYS B 1 430 ? 134.206 158.450 168.098 1.00 21.53 ?  430 LYS B C     1 
ATOM   9020  O  O     . LYS B 1 430 ? 134.422 158.942 166.983 1.00 27.81 ?  430 LYS B O     1 
ATOM   9021  C  CB    . LYS B 1 430 ? 132.931 159.776 169.818 1.00 22.02 ?  430 LYS B CB    1 
ATOM   9022  C  CG    . LYS B 1 430 ? 131.577 160.101 170.426 1.00 22.89 ?  430 LYS B CG    1 
ATOM   9023  C  CD    . LYS B 1 430 ? 131.565 161.457 171.098 1.00 30.33 ?  430 LYS B CD    1 
ATOM   9024  C  CE    . LYS B 1 430 ? 130.155 161.850 171.500 1.00 29.82 ?  430 LYS B CE    1 
ATOM   9025  N  NZ    . LYS B 1 430 ? 130.113 163.177 172.172 1.00 32.31 1  430 LYS B NZ    1 
ATOM   9026  N  N     . LEU B 1 431 ? 135.123 157.718 168.737 1.00 25.33 ?  431 LEU B N     1 
ATOM   9027  C  CA    . LEU B 1 431 ? 136.414 157.452 168.108 1.00 21.07 ?  431 LEU B CA    1 
ATOM   9028  C  C     . LEU B 1 431 ? 136.256 156.596 166.857 1.00 25.84 ?  431 LEU B C     1 
ATOM   9029  O  O     . LEU B 1 431 ? 136.929 156.835 165.845 1.00 31.65 ?  431 LEU B O     1 
ATOM   9030  C  CB    . LEU B 1 431 ? 137.353 156.780 169.106 1.00 29.95 ?  431 LEU B CB    1 
ATOM   9031  C  CG    . LEU B 1 431 ? 138.359 157.706 169.788 1.00 31.49 ?  431 LEU B CG    1 
ATOM   9032  C  CD1   . LEU B 1 431 ? 139.330 156.907 170.637 1.00 28.39 ?  431 LEU B CD1   1 
ATOM   9033  C  CD2   . LEU B 1 431 ? 139.101 158.541 168.757 1.00 31.55 ?  431 LEU B CD2   1 
ATOM   9034  N  N     . ALA B 1 432 ? 135.382 155.589 166.906 1.00 23.66 ?  432 ALA B N     1 
ATOM   9035  C  CA    . ALA B 1 432 ? 135.131 154.772 165.726 1.00 15.83 ?  432 ALA B CA    1 
ATOM   9036  C  C     . ALA B 1 432 ? 134.523 155.604 164.606 1.00 20.11 ?  432 ALA B C     1 
ATOM   9037  O  O     . ALA B 1 432 ? 134.868 155.423 163.434 1.00 24.25 ?  432 ALA B O     1 
ATOM   9038  C  CB    . ALA B 1 432 ? 134.217 153.600 166.084 1.00 20.56 ?  432 ALA B CB    1 
ATOM   9039  N  N     . THR B 1 433 ? 133.610 156.514 164.947 1.00 25.32 ?  433 THR B N     1 
ATOM   9040  C  CA    . THR B 1 433 ? 133.040 157.403 163.940 1.00 21.27 ?  433 THR B CA    1 
ATOM   9041  C  C     . THR B 1 433 ? 134.117 158.274 163.311 1.00 20.87 ?  433 THR B C     1 
ATOM   9042  O  O     . THR B 1 433 ? 134.134 158.469 162.092 1.00 28.18 ?  433 THR B O     1 
ATOM   9043  C  CB    . THR B 1 433 ? 131.944 158.268 164.563 1.00 19.09 ?  433 THR B CB    1 
ATOM   9044  O  OG1   . THR B 1 433 ? 130.907 157.429 165.084 1.00 25.14 ?  433 THR B OG1   1 
ATOM   9045  C  CG2   . THR B 1 433 ? 131.352 159.209 163.526 1.00 19.05 ?  433 THR B CG2   1 
ATOM   9046  N  N     . ASP B 1 434 ? 135.027 158.807 164.128 1.00 24.19 ?  434 ASP B N     1 
ATOM   9047  C  CA    . ASP B 1 434 ? 136.118 159.614 163.589 1.00 19.08 ?  434 ASP B CA    1 
ATOM   9048  C  C     . ASP B 1 434 ? 136.994 158.800 162.645 1.00 19.62 ?  434 ASP B C     1 
ATOM   9049  O  O     . ASP B 1 434 ? 137.358 159.269 161.560 1.00 28.11 ?  434 ASP B O     1 
ATOM   9050  C  CB    . ASP B 1 434 ? 136.957 160.195 164.726 1.00 22.44 ?  434 ASP B CB    1 
ATOM   9051  C  CG    . ASP B 1 434 ? 136.190 161.190 165.567 1.00 32.03 ?  434 ASP B CG    1 
ATOM   9052  O  OD1   . ASP B 1 434 ? 135.281 161.852 165.026 1.00 35.18 ?  434 ASP B OD1   1 
ATOM   9053  O  OD2   . ASP B 1 434 ? 136.498 161.315 166.770 1.00 37.12 -1 434 ASP B OD2   1 
ATOM   9054  N  N     . SER B 1 435 ? 137.342 157.574 163.041 1.00 18.53 ?  435 SER B N     1 
ATOM   9055  C  CA    . SER B 1 435 ? 138.202 156.749 162.197 1.00 17.05 ?  435 SER B CA    1 
ATOM   9056  C  C     . SER B 1 435 ? 137.507 156.376 160.892 1.00 17.99 ?  435 SER B C     1 
ATOM   9057  O  O     . SER B 1 435 ? 138.131 156.380 159.824 1.00 25.67 ?  435 SER B O     1 
ATOM   9058  C  CB    . SER B 1 435 ? 138.636 155.495 162.955 1.00 19.74 ?  435 SER B CB    1 
ATOM   9059  O  OG    . SER B 1 435 ? 137.551 154.606 163.145 1.00 21.93 ?  435 SER B OG    1 
ATOM   9060  N  N     . LEU B 1 436 ? 136.212 156.059 160.956 1.00 22.63 ?  436 LEU B N     1 
ATOM   9061  C  CA    . LEU B 1 436 ? 135.471 155.722 159.745 1.00 11.68 ?  436 LEU B CA    1 
ATOM   9062  C  C     . LEU B 1 436 ? 135.331 156.932 158.833 1.00 18.40 ?  436 LEU B C     1 
ATOM   9063  O  O     . LEU B 1 436 ? 135.408 156.805 157.606 1.00 22.34 ?  436 LEU B O     1 
ATOM   9064  C  CB    . LEU B 1 436 ? 134.100 155.157 160.112 1.00 19.84 ?  436 LEU B CB    1 
ATOM   9065  C  CG    . LEU B 1 436 ? 134.098 153.776 160.768 1.00 19.63 ?  436 LEU B CG    1 
ATOM   9066  C  CD1   . LEU B 1 436 ? 132.810 153.555 161.542 1.00 15.43 ?  436 LEU B CD1   1 
ATOM   9067  C  CD2   . LEU B 1 436 ? 134.296 152.686 159.731 1.00 18.72 ?  436 LEU B CD2   1 
ATOM   9068  N  N     . THR B 1 437 ? 135.129 158.116 159.414 1.00 22.43 ?  437 THR B N     1 
ATOM   9069  C  CA    . THR B 1 437 ? 135.091 159.335 158.617 1.00 19.37 ?  437 THR B CA    1 
ATOM   9070  C  C     . THR B 1 437 ? 136.425 159.580 157.931 1.00 24.19 ?  437 THR B C     1 
ATOM   9071  O  O     . THR B 1 437 ? 136.466 159.965 156.759 1.00 27.35 ?  437 THR B O     1 
ATOM   9072  C  CB    . THR B 1 437 ? 134.715 160.527 159.497 1.00 21.85 ?  437 THR B CB    1 
ATOM   9073  O  OG1   . THR B 1 437 ? 133.572 160.192 160.292 1.00 21.50 ?  437 THR B OG1   1 
ATOM   9074  C  CG2   . THR B 1 437 ? 134.392 161.738 158.640 1.00 22.83 ?  437 THR B CG2   1 
ATOM   9075  N  N     . HIS B 1 438 ? 137.531 159.366 158.646 1.00 21.96 ?  438 HIS B N     1 
ATOM   9076  C  CA    . HIS B 1 438 ? 138.843 159.522 158.026 1.00 21.04 ?  438 HIS B CA    1 
ATOM   9077  C  C     . HIS B 1 438 ? 139.035 158.530 156.886 1.00 22.02 ?  438 HIS B C     1 
ATOM   9078  O  O     . HIS B 1 438 ? 139.554 158.889 155.821 1.00 29.69 ?  438 HIS B O     1 
ATOM   9079  C  CB    . HIS B 1 438 ? 139.949 159.353 159.068 1.00 24.00 ?  438 HIS B CB    1 
ATOM   9080  C  CG    . HIS B 1 438 ? 141.328 159.422 158.494 1.00 28.07 ?  438 HIS B CG    1 
ATOM   9081  N  ND1   . HIS B 1 438 ? 141.957 160.616 158.209 1.00 27.95 ?  438 HIS B ND1   1 
ATOM   9082  C  CD2   . HIS B 1 438 ? 142.197 158.447 158.140 1.00 28.47 ?  438 HIS B CD2   1 
ATOM   9083  C  CE1   . HIS B 1 438 ? 143.154 160.371 157.709 1.00 31.12 ?  438 HIS B CE1   1 
ATOM   9084  N  NE2   . HIS B 1 438 ? 143.325 159.064 157.656 1.00 34.12 ?  438 HIS B NE2   1 
ATOM   9085  N  N     . VAL B 1 439 ? 138.626 157.278 157.090 1.00 22.41 ?  439 VAL B N     1 
ATOM   9086  C  CA    . VAL B 1 439 ? 138.767 156.277 156.036 1.00 22.78 ?  439 VAL B CA    1 
ATOM   9087  C  C     . VAL B 1 439 ? 137.952 156.677 154.814 1.00 30.90 ?  439 VAL B C     1 
ATOM   9088  O  O     . VAL B 1 439 ? 138.418 156.564 153.674 1.00 33.18 ?  439 VAL B O     1 
ATOM   9089  C  CB    . VAL B 1 439 ? 138.363 154.886 156.556 1.00 21.05 ?  439 VAL B CB    1 
ATOM   9090  C  CG1   . VAL B 1 439 ? 138.356 153.877 155.417 1.00 20.49 ?  439 VAL B CG1   1 
ATOM   9091  C  CG2   . VAL B 1 439 ? 139.301 154.443 157.659 1.00 20.13 ?  439 VAL B CG2   1 
ATOM   9092  N  N     . SER B 1 440 ? 136.723 157.148 155.031 1.00 31.55 ?  440 SER B N     1 
ATOM   9093  C  CA    . SER B 1 440 ? 135.895 157.593 153.916 1.00 19.31 ?  440 SER B CA    1 
ATOM   9094  C  C     . SER B 1 440 ? 136.523 158.786 153.203 1.00 26.01 ?  440 SER B C     1 
ATOM   9095  O  O     . SER B 1 440 ? 136.507 158.860 151.969 1.00 34.00 ?  440 SER B O     1 
ATOM   9096  C  CB    . SER B 1 440 ? 134.492 157.938 154.418 1.00 24.86 ?  440 SER B CB    1 
ATOM   9097  O  OG    . SER B 1 440 ? 133.649 158.336 153.354 1.00 32.69 ?  440 SER B OG    1 
ATOM   9098  N  N     . GLU B 1 441 ? 137.081 159.730 153.963 1.00 30.60 ?  441 GLU B N     1 
ATOM   9099  C  CA    . GLU B 1 441 ? 137.668 160.924 153.364 1.00 26.11 ?  441 GLU B CA    1 
ATOM   9100  C  C     . GLU B 1 441 ? 138.900 160.585 152.535 1.00 32.14 ?  441 GLU B C     1 
ATOM   9101  O  O     . GLU B 1 441 ? 139.116 161.171 151.468 1.00 39.73 ?  441 GLU B O     1 
ATOM   9102  C  CB    . GLU B 1 441 ? 138.018 161.935 154.453 1.00 24.91 ?  441 GLU B CB    1 
ATOM   9103  C  CG    . GLU B 1 441 ? 136.840 162.769 154.919 1.00 31.91 ?  441 GLU B CG    1 
ATOM   9104  C  CD    . GLU B 1 441 ? 136.989 163.235 156.352 1.00 36.89 ?  441 GLU B CD    1 
ATOM   9105  O  OE1   . GLU B 1 441 ? 138.007 162.893 156.990 1.00 37.93 ?  441 GLU B OE1   1 
ATOM   9106  O  OE2   . GLU B 1 441 ? 136.085 163.942 156.841 1.00 35.63 -1 441 GLU B OE2   1 
ATOM   9107  N  N     . THR B 1 442 ? 139.722 159.651 153.007 1.00 28.82 ?  442 THR B N     1 
ATOM   9108  C  CA    . THR B 1 442 ? 140.941 159.287 152.297 1.00 29.22 ?  442 THR B CA    1 
ATOM   9109  C  C     . THR B 1 442 ? 140.699 158.284 151.178 1.00 30.71 ?  442 THR B C     1 
ATOM   9110  O  O     . THR B 1 442 ? 141.652 157.910 150.486 1.00 35.88 ?  442 THR B O     1 
ATOM   9111  C  CB    . THR B 1 442 ? 141.979 158.720 153.271 1.00 33.26 ?  442 THR B CB    1 
ATOM   9112  O  OG1   . THR B 1 442 ? 141.483 157.510 153.857 1.00 32.55 ?  442 THR B OG1   1 
ATOM   9113  C  CG2   . THR B 1 442 ? 142.276 159.724 154.372 1.00 32.77 ?  442 THR B CG2   1 
ATOM   9114  N  N     . THR B 1 443 ? 139.462 157.841 150.981 1.00 30.98 ?  443 THR B N     1 
ATOM   9115  C  CA    . THR B 1 443 ? 139.141 156.893 149.927 1.00 34.44 ?  443 THR B CA    1 
ATOM   9116  C  C     . THR B 1 443 ? 138.765 157.630 148.649 1.00 37.02 ?  443 THR B C     1 
ATOM   9117  O  O     . THR B 1 443 ? 137.996 158.595 148.676 1.00 38.02 ?  443 THR B O     1 
ATOM   9118  C  CB    . THR B 1 443 ? 137.993 155.975 150.353 1.00 35.69 ?  443 THR B CB    1 
ATOM   9119  O  OG1   . THR B 1 443 ? 138.425 155.140 151.434 1.00 41.22 ?  443 THR B OG1   1 
ATOM   9120  C  CG2   . THR B 1 443 ? 137.552 155.103 149.191 1.00 27.44 ?  443 THR B CG2   1 
ATOM   9121  N  N     . ASP B 1 444 ? 139.320 157.172 147.531 1.00 43.97 ?  444 ASP B N     1 
ATOM   9122  C  CA    . ASP B 1 444 ? 139.016 157.758 146.228 1.00 44.95 ?  444 ASP B CA    1 
ATOM   9123  C  C     . ASP B 1 444 ? 139.191 156.679 145.170 1.00 44.31 ?  444 ASP B C     1 
ATOM   9124  O  O     . ASP B 1 444 ? 140.321 156.291 144.860 1.00 46.24 ?  444 ASP B O     1 
ATOM   9125  C  CB    . ASP B 1 444 ? 139.911 158.960 145.938 1.00 43.68 ?  444 ASP B CB    1 
ATOM   9126  C  CG    . ASP B 1 444 ? 139.555 159.650 144.635 1.00 47.91 ?  444 ASP B CG    1 
ATOM   9127  O  OD1   . ASP B 1 444 ? 138.599 159.204 143.966 1.00 42.91 ?  444 ASP B OD1   1 
ATOM   9128  O  OD2   . ASP B 1 444 ? 140.229 160.639 144.281 1.00 48.55 -1 444 ASP B OD2   1 
ATOM   9129  N  N     . ILE B 1 445 ? 138.080 156.197 144.625 1.00 37.83 ?  445 ILE B N     1 
ATOM   9130  C  CA    . ILE B 1 445 ? 138.090 155.223 143.541 1.00 39.79 ?  445 ILE B CA    1 
ATOM   9131  C  C     . ILE B 1 445 ? 137.989 156.001 142.237 1.00 40.05 ?  445 ILE B C     1 
ATOM   9132  O  O     . ILE B 1 445 ? 136.996 156.692 141.989 1.00 42.83 ?  445 ILE B O     1 
ATOM   9133  C  CB    . ILE B 1 445 ? 136.952 154.202 143.677 1.00 35.85 ?  445 ILE B CB    1 
ATOM   9134  C  CG1   . ILE B 1 445 ? 137.215 153.257 144.852 1.00 32.95 ?  445 ILE B CG1   1 
ATOM   9135  C  CG2   . ILE B 1 445 ? 136.795 153.408 142.391 1.00 38.72 ?  445 ILE B CG2   1 
ATOM   9136  C  CD1   . ILE B 1 445 ? 136.991 153.880 146.208 1.00 38.05 ?  445 ILE B CD1   1 
ATOM   9137  N  N     . ARG B 1 446 ? 139.016 155.888 141.400 1.00 42.92 ?  446 ARG B N     1 
ATOM   9138  C  CA    . ARG B 1 446 ? 139.109 156.660 140.169 1.00 46.69 ?  446 ARG B CA    1 
ATOM   9139  C  C     . ARG B 1 446 ? 138.587 155.903 138.953 1.00 43.27 ?  446 ARG B C     1 
ATOM   9140  O  O     . ARG B 1 446 ? 138.769 156.370 137.824 1.00 41.76 ?  446 ARG B O     1 
ATOM   9141  C  CB    . ARG B 1 446 ? 140.556 157.099 139.936 1.00 45.08 ?  446 ARG B CB    1 
ATOM   9142  C  CG    . ARG B 1 446 ? 141.582 156.007 140.170 1.00 43.24 ?  446 ARG B CG    1 
ATOM   9143  C  CD    . ARG B 1 446 ? 142.925 156.592 140.578 1.00 47.81 ?  446 ARG B CD    1 
ATOM   9144  N  NE    . ARG B 1 446 ? 142.865 157.247 141.879 1.00 48.84 ?  446 ARG B NE    1 
ATOM   9145  C  CZ    . ARG B 1 446 ? 142.672 158.548 142.059 1.00 51.38 ?  446 ARG B CZ    1 
ATOM   9146  N  NH1   . ARG B 1 446 ? 142.511 159.370 141.036 1.00 48.10 1  446 ARG B NH1   1 
ATOM   9147  N  NH2   . ARG B 1 446 ? 142.639 159.034 143.296 1.00 51.16 ?  446 ARG B NH2   1 
ATOM   9148  N  N     . ASN B 1 447 ? 137.946 154.754 139.157 1.00 34.72 ?  447 ASN B N     1 
ATOM   9149  C  CA    . ASN B 1 447 ? 137.346 153.996 138.071 1.00 29.19 ?  447 ASN B CA    1 
ATOM   9150  C  C     . ASN B 1 447 ? 135.879 153.679 138.315 1.00 31.91 ?  447 ASN B C     1 
ATOM   9151  O  O     . ASN B 1 447 ? 135.278 152.945 137.523 1.00 38.57 ?  447 ASN B O     1 
ATOM   9152  C  CB    . ASN B 1 447 ? 138.123 152.694 137.839 1.00 33.24 ?  447 ASN B CB    1 
ATOM   9153  C  CG    . ASN B 1 447 ? 139.150 152.823 136.736 1.00 32.27 ?  447 ASN B CG    1 
ATOM   9154  O  OD1   . ASN B 1 447 ? 138.958 153.572 135.780 1.00 31.06 ?  447 ASN B OD1   1 
ATOM   9155  N  ND2   . ASN B 1 447 ? 140.254 152.103 136.870 1.00 34.04 ?  447 ASN B ND2   1 
ATOM   9156  N  N     . ALA B 1 448 ? 135.290 154.206 139.386 1.00 33.90 ?  448 ALA B N     1 
ATOM   9157  C  CA    . ALA B 1 448 ? 133.866 154.053 139.682 1.00 29.51 ?  448 ALA B CA    1 
ATOM   9158  C  C     . ALA B 1 448 ? 133.313 155.442 139.970 1.00 28.58 ?  448 ALA B C     1 
ATOM   9159  O  O     . ALA B 1 448 ? 133.199 155.850 141.133 1.00 29.20 ?  448 ALA B O     1 
ATOM   9160  C  CB    . ALA B 1 448 ? 133.640 153.099 140.854 1.00 23.92 ?  448 ALA B CB    1 
ATOM   9161  N  N     . PRO B 1 449 ? 132.968 156.203 138.926 1.00 31.23 ?  449 PRO B N     1 
ATOM   9162  C  CA    . PRO B 1 449 ? 132.578 157.606 139.151 1.00 23.20 ?  449 PRO B CA    1 
ATOM   9163  C  C     . PRO B 1 449 ? 131.408 157.762 140.104 1.00 21.51 ?  449 PRO B C     1 
ATOM   9164  O  O     . PRO B 1 449 ? 131.420 158.668 140.946 1.00 23.97 ?  449 PRO B O     1 
ATOM   9165  C  CB    . PRO B 1 449 ? 132.228 158.104 137.741 1.00 18.40 ?  449 PRO B CB    1 
ATOM   9166  C  CG    . PRO B 1 449 ? 132.810 157.104 136.808 1.00 27.06 ?  449 PRO B CG    1 
ATOM   9167  C  CD    . PRO B 1 449 ? 132.814 155.801 137.521 1.00 24.14 ?  449 PRO B CD    1 
ATOM   9168  N  N     . ALA B 1 450 ? 130.397 156.899 140.000 1.00 25.02 ?  450 ALA B N     1 
ATOM   9169  C  CA    . ALA B 1 450 ? 129.262 156.985 140.909 1.00 19.74 ?  450 ALA B CA    1 
ATOM   9170  C  C     . ALA B 1 450 ? 129.682 156.676 142.339 1.00 22.25 ?  450 ALA B C     1 
ATOM   9171  O  O     . ALA B 1 450 ? 129.226 157.332 143.280 1.00 23.39 ?  450 ALA B O     1 
ATOM   9172  C  CB    . ALA B 1 450 ? 128.149 156.043 140.454 1.00 15.61 ?  450 ALA B CB    1 
ATOM   9173  N  N     . VAL B 1 451 ? 130.560 155.690 142.522 1.00 20.96 ?  451 VAL B N     1 
ATOM   9174  C  CA    . VAL B 1 451 ? 131.025 155.346 143.863 1.00 18.19 ?  451 VAL B CA    1 
ATOM   9175  C  C     . VAL B 1 451 ? 131.793 156.510 144.473 1.00 17.76 ?  451 VAL B C     1 
ATOM   9176  O  O     . VAL B 1 451 ? 131.573 156.885 145.629 1.00 20.30 ?  451 VAL B O     1 
ATOM   9177  C  CB    . VAL B 1 451 ? 131.878 154.065 143.824 1.00 24.52 ?  451 VAL B CB    1 
ATOM   9178  C  CG1   . VAL B 1 451 ? 132.639 153.892 145.126 1.00 21.03 ?  451 VAL B CG1   1 
ATOM   9179  C  CG2   . VAL B 1 451 ? 131.003 152.856 143.549 1.00 15.83 ?  451 VAL B CG2   1 
ATOM   9180  N  N     . ARG B 1 452 ? 132.710 157.100 143.706 1.00 23.95 ?  452 ARG B N     1 
ATOM   9181  C  CA    . ARG B 1 452 ? 133.488 158.224 144.217 1.00 21.77 ?  452 ARG B CA    1 
ATOM   9182  C  C     . ARG B 1 452 ? 132.592 159.416 144.532 1.00 21.03 ?  452 ARG B C     1 
ATOM   9183  O  O     . ARG B 1 452 ? 132.731 160.049 145.588 1.00 31.17 ?  452 ARG B O     1 
ATOM   9184  C  CB    . ARG B 1 452 ? 134.567 158.605 143.204 1.00 18.84 ?  452 ARG B CB    1 
ATOM   9185  C  CG    . ARG B 1 452 ? 135.120 160.007 143.364 1.00 27.98 ?  452 ARG B CG    1 
ATOM   9186  C  CD    . ARG B 1 452 ? 135.876 160.436 142.120 1.00 29.08 ?  452 ARG B CD    1 
ATOM   9187  N  NE    . ARG B 1 452 ? 137.285 160.072 142.179 1.00 35.21 ?  452 ARG B NE    1 
ATOM   9188  C  CZ    . ARG B 1 452 ? 138.124 160.150 141.154 1.00 37.50 ?  452 ARG B CZ    1 
ATOM   9189  N  NH1   . ARG B 1 452 ? 137.727 160.584 139.968 1.00 33.79 1  452 ARG B NH1   1 
ATOM   9190  N  NH2   . ARG B 1 452 ? 139.390 159.785 141.323 1.00 37.02 ?  452 ARG B NH2   1 
ATOM   9191  N  N     . ARG B 1 453 ? 131.654 159.725 143.635 1.00 18.02 ?  453 ARG B N     1 
ATOM   9192  C  CA    . ARG B 1 453 ? 130.757 160.851 143.858 1.00 19.82 ?  453 ARG B CA    1 
ATOM   9193  C  C     . ARG B 1 453 ? 129.888 160.629 145.089 1.00 25.39 ?  453 ARG B C     1 
ATOM   9194  O  O     . ARG B 1 453 ? 129.691 161.548 145.890 1.00 31.17 ?  453 ARG B O     1 
ATOM   9195  C  CB    . ARG B 1 453 ? 129.888 161.082 142.622 1.00 23.22 ?  453 ARG B CB    1 
ATOM   9196  C  CG    . ARG B 1 453 ? 129.007 162.310 142.717 1.00 27.77 ?  453 ARG B CG    1 
ATOM   9197  C  CD    . ARG B 1 453 ? 127.700 162.126 141.974 1.00 21.77 ?  453 ARG B CD    1 
ATOM   9198  N  NE    . ARG B 1 453 ? 126.736 163.158 142.339 1.00 26.82 ?  453 ARG B NE    1 
ATOM   9199  C  CZ    . ARG B 1 453 ? 125.446 163.120 142.037 1.00 27.02 ?  453 ARG B CZ    1 
ATOM   9200  N  NH1   . ARG B 1 453 ? 124.924 162.113 141.356 1.00 26.72 1  453 ARG B NH1   1 
ATOM   9201  N  NH2   . ARG B 1 453 ? 124.659 164.118 142.430 1.00 28.04 ?  453 ARG B NH2   1 
ATOM   9202  N  N     . ALA B 1 454 ? 129.362 159.414 145.260 1.00 27.72 ?  454 ALA B N     1 
ATOM   9203  C  CA    . ALA B 1 454 ? 128.510 159.131 146.407 1.00 14.33 ?  454 ALA B CA    1 
ATOM   9204  C  C     . ALA B 1 454 ? 129.308 159.135 147.703 1.00 18.86 ?  454 ALA B C     1 
ATOM   9205  O  O     . ALA B 1 454 ? 128.804 159.565 148.743 1.00 28.10 ?  454 ALA B O     1 
ATOM   9206  C  CB    . ALA B 1 454 ? 127.799 157.795 146.217 1.00 18.22 ?  454 ALA B CB    1 
ATOM   9207  N  N     . ASN B 1 455 ? 130.551 158.656 147.667 1.00 17.98 ?  455 ASN B N     1 
ATOM   9208  C  CA    . ASN B 1 455 ? 131.390 158.727 148.856 1.00 15.20 ?  455 ASN B CA    1 
ATOM   9209  C  C     . ASN B 1 455 ? 131.656 160.173 149.245 1.00 23.03 ?  455 ASN B C     1 
ATOM   9210  O  O     . ASN B 1 455 ? 131.645 160.519 150.432 1.00 32.89 ?  455 ASN B O     1 
ATOM   9211  C  CB    . ASN B 1 455 ? 132.700 157.977 148.621 1.00 20.30 ?  455 ASN B CB    1 
ATOM   9212  C  CG    . ASN B 1 455 ? 133.675 158.139 149.768 1.00 25.78 ?  455 ASN B CG    1 
ATOM   9213  O  OD1   . ASN B 1 455 ? 133.422 157.682 150.881 1.00 31.11 ?  455 ASN B OD1   1 
ATOM   9214  N  ND2   . ASN B 1 455 ? 134.796 158.797 149.504 1.00 27.15 ?  455 ASN B ND2   1 
ATOM   9215  N  N     . LYS B 1 456 ? 131.901 161.034 148.257 1.00 24.15 ?  456 LYS B N     1 
ATOM   9216  C  CA    . LYS B 1 456 ? 132.153 162.438 148.557 1.00 22.80 ?  456 LYS B CA    1 
ATOM   9217  C  C     . LYS B 1 456 ? 130.893 163.158 149.028 1.00 24.96 ?  456 LYS B C     1 
ATOM   9218  O  O     . LYS B 1 456 ? 130.975 164.052 149.878 1.00 31.43 ?  456 LYS B O     1 
ATOM   9219  C  CB    . LYS B 1 456 ? 132.742 163.133 147.330 1.00 24.57 ?  456 LYS B CB    1 
ATOM   9220  C  CG    . LYS B 1 456 ? 132.831 164.643 147.446 1.00 27.03 ?  456 LYS B CG    1 
ATOM   9221  C  CD    . LYS B 1 456 ? 132.940 165.289 146.075 1.00 31.73 ?  456 LYS B CD    1 
ATOM   9222  C  CE    . LYS B 1 456 ? 132.081 164.568 145.041 1.00 34.13 ?  456 LYS B CE    1 
ATOM   9223  N  NZ    . LYS B 1 456 ? 130.644 164.504 145.428 1.00 28.46 1  456 LYS B NZ    1 
ATOM   9224  N  N     . ALA B 1 457 ? 129.725 162.788 148.500 1.00 23.93 ?  457 ALA B N     1 
ATOM   9225  C  CA    . ALA B 1 457 ? 128.491 163.516 148.777 1.00 19.98 ?  457 ALA B CA    1 
ATOM   9226  C  C     . ALA B 1 457 ? 127.782 163.037 150.042 1.00 26.52 ?  457 ALA B C     1 
ATOM   9227  O  O     . ALA B 1 457 ? 127.323 163.856 150.843 1.00 30.93 ?  457 ALA B O     1 
ATOM   9228  C  CB    . ALA B 1 457 ? 127.546 163.407 147.576 1.00 21.07 ?  457 ALA B CB    1 
ATOM   9229  N  N     . MET B 1 458 ? 127.677 161.723 150.234 1.00 25.53 ?  458 MET B N     1 
ATOM   9230  C  CA    . MET B 1 458 ? 126.891 161.170 151.331 1.00 19.36 ?  458 MET B CA    1 
ATOM   9231  C  C     . MET B 1 458 ? 127.716 160.903 152.581 1.00 24.85 ?  458 MET B C     1 
ATOM   9232  O  O     . MET B 1 458 ? 127.167 160.932 153.687 1.00 28.07 ?  458 MET B O     1 
ATOM   9233  C  CB    . MET B 1 458 ? 126.207 159.872 150.890 1.00 22.28 ?  458 MET B CB    1 
ATOM   9234  C  CG    . MET B 1 458 ? 125.564 159.936 149.515 1.00 18.67 ?  458 MET B CG    1 
ATOM   9235  S  SD    . MET B 1 458 ? 123.847 160.480 149.569 1.00 37.41 ?  458 MET B SD    1 
ATOM   9236  C  CE    . MET B 1 458 ? 123.087 159.151 150.498 1.00 23.56 ?  458 MET B CE    1 
ATOM   9237  N  N     . LYS B 1 459 ? 129.016 160.650 152.435 1.00 21.35 ?  459 LYS B N     1 
ATOM   9238  C  CA    . LYS B 1 459 ? 129.891 160.414 153.582 1.00 22.35 ?  459 LYS B CA    1 
ATOM   9239  C  C     . LYS B 1 459 ? 129.352 159.286 154.456 1.00 21.24 ?  459 LYS B C     1 
ATOM   9240  O  O     . LYS B 1 459 ? 129.246 159.410 155.678 1.00 30.68 ?  459 LYS B O     1 
ATOM   9241  C  CB    . LYS B 1 459 ? 130.077 161.692 154.397 1.00 21.89 ?  459 LYS B CB    1 
ATOM   9242  C  CG    . LYS B 1 459 ? 130.077 162.955 153.559 1.00 25.61 ?  459 LYS B CG    1 
ATOM   9243  C  CD    . LYS B 1 459 ? 129.969 164.195 154.422 1.00 28.28 ?  459 LYS B CD    1 
ATOM   9244  C  CE    . LYS B 1 459 ? 130.159 165.448 153.593 1.00 29.22 ?  459 LYS B CE    1 
ATOM   9245  N  NZ    . LYS B 1 459 ? 131.254 165.283 152.599 1.00 29.30 1  459 LYS B NZ    1 
ATOM   9246  N  N     . SER B 1 460 ? 129.003 158.172 153.821 1.00 20.43 ?  460 SER B N     1 
ATOM   9247  C  CA    . SER B 1 460 ? 128.387 157.060 154.527 1.00 15.23 ?  460 SER B CA    1 
ATOM   9248  C  C     . SER B 1 460 ? 129.442 156.187 155.191 1.00 24.20 ?  460 SER B C     1 
ATOM   9249  O  O     . SER B 1 460 ? 130.475 155.868 154.597 1.00 29.27 ?  460 SER B O     1 
ATOM   9250  C  CB    . SER B 1 460 ? 127.547 156.222 153.564 1.00 14.47 ?  460 SER B CB    1 
ATOM   9251  O  OG    . SER B 1 460 ? 126.263 156.792 153.390 1.00 32.84 ?  460 SER B OG    1 
ATOM   9252  N  N     . ILE B 1 461 ? 129.172 155.804 156.438 1.00 18.20 ?  461 ILE B N     1 
ATOM   9253  C  CA    . ILE B 1 461 ? 130.038 154.913 157.195 1.00 18.97 ?  461 ILE B CA    1 
ATOM   9254  C  C     . ILE B 1 461 ? 129.179 153.809 157.791 1.00 18.31 ?  461 ILE B C     1 
ATOM   9255  O  O     . ILE B 1 461 ? 127.970 153.961 157.974 1.00 21.72 ?  461 ILE B O     1 
ATOM   9256  C  CB    . ILE B 1 461 ? 130.811 155.649 158.311 1.00 16.04 ?  461 ILE B CB    1 
ATOM   9257  C  CG1   . ILE B 1 461 ? 129.834 156.289 159.300 1.00 12.65 ?  461 ILE B CG1   1 
ATOM   9258  C  CG2   . ILE B 1 461 ? 131.737 156.696 157.714 1.00 15.38 ?  461 ILE B CG2   1 
ATOM   9259  C  CD1   . ILE B 1 461 ? 130.483 156.814 160.554 1.00 11.35 ?  461 ILE B CD1   1 
ATOM   9260  N  N     . GLY B 1 462 ? 129.817 152.682 158.081 1.00 13.17 ?  462 GLY B N     1 
ATOM   9261  C  CA    . GLY B 1 462 ? 129.130 151.623 158.788 1.00 6.67  ?  462 GLY B CA    1 
ATOM   9262  C  C     . GLY B 1 462 ? 129.829 151.245 160.074 1.00 9.90  ?  462 GLY B C     1 
ATOM   9263  O  O     . GLY B 1 462 ? 130.911 150.652 160.049 1.00 23.48 ?  462 GLY B O     1 
ATOM   9264  N  N     . LEU B 1 463 ? 129.214 151.568 161.205 1.00 8.79  ?  463 LEU B N     1 
ATOM   9265  C  CA    . LEU B 1 463 ? 129.745 151.214 162.514 1.00 8.52  ?  463 LEU B CA    1 
ATOM   9266  C  C     . LEU B 1 463 ? 128.967 150.009 163.025 1.00 15.81 ?  463 LEU B C     1 
ATOM   9267  O  O     . LEU B 1 463 ? 127.797 150.130 163.401 1.00 25.08 ?  463 LEU B O     1 
ATOM   9268  C  CB    . LEU B 1 463 ? 129.649 152.390 163.483 1.00 16.15 ?  463 LEU B CB    1 
ATOM   9269  C  CG    . LEU B 1 463 ? 130.130 152.108 164.907 1.00 12.91 ?  463 LEU B CG    1 
ATOM   9270  C  CD1   . LEU B 1 463 ? 131.521 151.498 164.886 1.00 2.01  ?  463 LEU B CD1   1 
ATOM   9271  C  CD2   . LEU B 1 463 ? 130.111 153.376 165.743 1.00 17.29 ?  463 LEU B CD2   1 
ATOM   9272  N  N     . GLY B 1 464 ? 129.617 148.847 163.034 1.00 10.55 ?  464 GLY B N     1 
ATOM   9273  C  CA    . GLY B 1 464 ? 128.999 147.619 163.474 1.00 9.06  ?  464 GLY B CA    1 
ATOM   9274  C  C     . GLY B 1 464 ? 129.354 147.272 164.907 1.00 10.00 ?  464 GLY B C     1 
ATOM   9275  O  O     . GLY B 1 464 ? 130.037 148.012 165.616 1.00 18.09 ?  464 GLY B O     1 
ATOM   9276  N  N     . ALA B 1 465 ? 128.871 146.109 165.332 1.00 13.87 ?  465 ALA B N     1 
ATOM   9277  C  CA    . ALA B 1 465 ? 129.144 145.593 166.661 1.00 7.97  ?  465 ALA B CA    1 
ATOM   9278  C  C     . ALA B 1 465 ? 129.360 144.091 166.574 1.00 12.94 ?  465 ALA B C     1 
ATOM   9279  O  O     . ALA B 1 465 ? 128.843 143.425 165.675 1.00 25.28 ?  465 ALA B O     1 
ATOM   9280  C  CB    . ALA B 1 465 ? 128.009 145.912 167.639 1.00 14.86 ?  465 ALA B CB    1 
ATOM   9281  N  N     . MET B 1 466 ? 130.135 143.566 167.517 1.00 18.95 ?  466 MET B N     1 
ATOM   9282  C  CA    . MET B 1 466 ? 130.401 142.140 167.598 1.00 18.06 ?  466 MET B CA    1 
ATOM   9283  C  C     . MET B 1 466 ? 130.475 141.736 169.062 1.00 14.24 ?  466 MET B C     1 
ATOM   9284  O  O     . MET B 1 466 ? 130.546 142.580 169.959 1.00 20.30 ?  466 MET B O     1 
ATOM   9285  C  CB    . MET B 1 466 ? 131.692 141.762 166.862 1.00 19.86 ?  466 MET B CB    1 
ATOM   9286  C  CG    . MET B 1 466 ? 132.963 142.252 167.535 1.00 23.32 ?  466 MET B CG    1 
ATOM   9287  S  SD    . MET B 1 466 ? 134.373 142.284 166.416 1.00 37.88 ?  466 MET B SD    1 
ATOM   9288  C  CE    . MET B 1 466 ? 135.282 143.682 167.066 1.00 28.84 ?  466 MET B CE    1 
ATOM   9289  N  N     . ASN B 1 467 ? 130.451 140.426 169.299 1.00 17.11 ?  467 ASN B N     1 
ATOM   9290  C  CA    . ASN B 1 467 ? 130.555 139.863 170.641 1.00 17.90 ?  467 ASN B CA    1 
ATOM   9291  C  C     . ASN B 1 467 ? 129.285 140.081 171.459 1.00 21.64 ?  467 ASN B C     1 
ATOM   9292  O  O     . ASN B 1 467 ? 129.342 140.183 172.686 1.00 26.22 ?  467 ASN B O     1 
ATOM   9293  C  CB    . ASN B 1 467 ? 131.764 140.434 171.389 1.00 21.91 ?  467 ASN B CB    1 
ATOM   9294  C  CG    . ASN B 1 467 ? 132.517 139.378 172.167 1.00 23.82 ?  467 ASN B CG    1 
ATOM   9295  O  OD1   . ASN B 1 467 ? 132.312 138.182 171.974 1.00 27.00 ?  467 ASN B OD1   1 
ATOM   9296  N  ND2   . ASN B 1 467 ? 133.402 139.818 173.052 1.00 21.84 ?  467 ASN B ND2   1 
ATOM   9297  N  N     . LEU B 1 468 ? 128.131 140.164 170.797 1.00 17.03 ?  468 LEU B N     1 
ATOM   9298  C  CA    . LEU B 1 468 ? 126.874 140.260 171.531 1.00 15.95 ?  468 LEU B CA    1 
ATOM   9299  C  C     . LEU B 1 468 ? 126.575 138.961 172.267 1.00 23.12 ?  468 LEU B C     1 
ATOM   9300  O  O     . LEU B 1 468 ? 126.322 138.963 173.478 1.00 23.55 ?  468 LEU B O     1 
ATOM   9301  C  CB    . LEU B 1 468 ? 125.735 140.616 170.576 1.00 22.00 ?  468 LEU B CB    1 
ATOM   9302  C  CG    . LEU B 1 468 ? 124.318 140.518 171.144 1.00 16.70 ?  468 LEU B CG    1 
ATOM   9303  C  CD1   . LEU B 1 468 ? 124.151 141.444 172.337 1.00 14.92 ?  468 LEU B CD1   1 
ATOM   9304  C  CD2   . LEU B 1 468 ? 123.281 140.818 170.076 1.00 14.32 ?  468 LEU B CD2   1 
ATOM   9305  N  N     . HIS B 1 469 ? 126.619 137.834 171.552 1.00 22.46 ?  469 HIS B N     1 
ATOM   9306  C  CA    . HIS B 1 469 ? 126.406 136.547 172.201 1.00 16.17 ?  469 HIS B CA    1 
ATOM   9307  C  C     . HIS B 1 469 ? 127.515 136.245 173.195 1.00 24.07 ?  469 HIS B C     1 
ATOM   9308  O  O     . HIS B 1 469 ? 127.256 135.716 174.279 1.00 35.85 ?  469 HIS B O     1 
ATOM   9309  C  CB    . HIS B 1 469 ? 126.307 135.431 171.165 1.00 20.11 ?  469 HIS B CB    1 
ATOM   9310  C  CG    . HIS B 1 469 ? 125.755 134.153 171.715 1.00 25.67 ?  469 HIS B CG    1 
ATOM   9311  N  ND1   . HIS B 1 469 ? 125.709 132.984 170.987 1.00 29.59 ?  469 HIS B ND1   1 
ATOM   9312  C  CD2   . HIS B 1 469 ? 125.226 133.860 172.927 1.00 25.29 ?  469 HIS B CD2   1 
ATOM   9313  C  CE1   . HIS B 1 469 ? 125.177 132.028 171.725 1.00 25.47 ?  469 HIS B CE1   1 
ATOM   9314  N  NE2   . HIS B 1 469 ? 124.875 132.533 172.908 1.00 25.34 ?  469 HIS B NE2   1 
ATOM   9315  N  N     . GLY B 1 470 ? 128.761 136.562 172.843 1.00 25.67 ?  470 GLY B N     1 
ATOM   9316  C  CA    . GLY B 1 470 ? 129.850 136.353 173.782 1.00 21.66 ?  470 GLY B CA    1 
ATOM   9317  C  C     . GLY B 1 470 ? 129.662 137.149 175.057 1.00 19.03 ?  470 GLY B C     1 
ATOM   9318  O  O     . GLY B 1 470 ? 129.776 136.615 176.163 1.00 30.54 ?  470 GLY B O     1 
ATOM   9319  N  N     . TYR B 1 471 ? 129.344 138.438 174.918 1.00 22.10 ?  471 TYR B N     1 
ATOM   9320  C  CA    . TYR B 1 471 ? 129.159 139.278 176.095 1.00 24.98 ?  471 TYR B CA    1 
ATOM   9321  C  C     . TYR B 1 471 ? 127.988 138.793 176.938 1.00 23.95 ?  471 TYR B C     1 
ATOM   9322  O  O     . TYR B 1 471 ? 128.064 138.785 178.172 1.00 28.10 ?  471 TYR B O     1 
ATOM   9323  C  CB    . TYR B 1 471 ? 128.947 140.734 175.680 1.00 24.16 ?  471 TYR B CB    1 
ATOM   9324  C  CG    . TYR B 1 471 ? 128.497 141.617 176.821 1.00 23.97 ?  471 TYR B CG    1 
ATOM   9325  C  CD1   . TYR B 1 471 ? 129.403 142.061 177.773 1.00 24.42 ?  471 TYR B CD1   1 
ATOM   9326  C  CD2   . TYR B 1 471 ? 127.167 141.982 176.962 1.00 20.01 ?  471 TYR B CD2   1 
ATOM   9327  C  CE1   . TYR B 1 471 ? 129.001 142.857 178.822 1.00 23.07 ?  471 TYR B CE1   1 
ATOM   9328  C  CE2   . TYR B 1 471 ? 126.755 142.774 178.011 1.00 20.19 ?  471 TYR B CE2   1 
ATOM   9329  C  CZ    . TYR B 1 471 ? 127.677 143.210 178.937 1.00 24.85 ?  471 TYR B CZ    1 
ATOM   9330  O  OH    . TYR B 1 471 ? 127.272 144.003 179.983 1.00 34.60 ?  471 TYR B OH    1 
ATOM   9331  N  N     . LEU B 1 472 ? 126.890 138.394 176.293 1.00 26.58 ?  472 LEU B N     1 
ATOM   9332  C  CA    . LEU B 1 472 ? 125.727 137.934 177.042 1.00 27.71 ?  472 LEU B CA    1 
ATOM   9333  C  C     . LEU B 1 472 ? 126.011 136.619 177.760 1.00 26.91 ?  472 LEU B C     1 
ATOM   9334  O  O     . LEU B 1 472 ? 125.657 136.459 178.933 1.00 33.10 ?  472 LEU B O     1 
ATOM   9335  C  CB    . LEU B 1 472 ? 124.524 137.789 176.110 1.00 29.46 ?  472 LEU B CB    1 
ATOM   9336  C  CG    . LEU B 1 472 ? 123.966 139.082 175.510 1.00 28.19 ?  472 LEU B CG    1 
ATOM   9337  C  CD1   . LEU B 1 472 ? 122.966 138.771 174.409 1.00 26.17 ?  472 LEU B CD1   1 
ATOM   9338  C  CD2   . LEU B 1 472 ? 123.334 139.952 176.584 1.00 21.83 ?  472 LEU B CD2   1 
ATOM   9339  N  N     . ALA B 1 473 ? 126.645 135.666 177.073 1.00 27.82 ?  473 ALA B N     1 
ATOM   9340  C  CA    . ALA B 1 473 ? 126.946 134.377 177.686 1.00 24.62 ?  473 ALA B CA    1 
ATOM   9341  C  C     . ALA B 1 473 ? 127.928 134.526 178.839 1.00 30.11 ?  473 ALA B C     1 
ATOM   9342  O  O     . ALA B 1 473 ? 127.782 133.865 179.873 1.00 37.40 ?  473 ALA B O     1 
ATOM   9343  C  CB    . ALA B 1 473 ? 127.490 133.413 176.634 1.00 25.88 ?  473 ALA B CB    1 
ATOM   9344  N  N     . GLN B 1 474 ? 128.936 135.386 178.685 1.00 30.67 ?  474 GLN B N     1 
ATOM   9345  C  CA    . GLN B 1 474 ? 129.882 135.614 179.770 1.00 29.65 ?  474 GLN B CA    1 
ATOM   9346  C  C     . GLN B 1 474 ? 129.262 136.371 180.936 1.00 31.10 ?  474 GLN B C     1 
ATOM   9347  O  O     . GLN B 1 474 ? 129.897 136.478 181.989 1.00 36.95 ?  474 GLN B O     1 
ATOM   9348  C  CB    . GLN B 1 474 ? 131.108 136.366 179.252 1.00 28.86 ?  474 GLN B CB    1 
ATOM   9349  C  CG    . GLN B 1 474 ? 131.682 135.790 177.971 1.00 32.52 ?  474 GLN B CG    1 
ATOM   9350  C  CD    . GLN B 1 474 ? 133.180 135.967 177.865 1.00 35.60 ?  474 GLN B CD    1 
ATOM   9351  O  OE1   . GLN B 1 474 ? 133.875 136.096 178.872 1.00 41.40 ?  474 GLN B OE1   1 
ATOM   9352  N  NE2   . GLN B 1 474 ? 133.687 135.977 176.639 1.00 36.26 ?  474 GLN B NE2   1 
ATOM   9353  N  N     . ASN B 1 475 ? 128.048 136.894 180.776 1.00 29.95 ?  475 ASN B N     1 
ATOM   9354  C  CA    . ASN B 1 475 ? 127.337 137.572 181.850 1.00 31.17 ?  475 ASN B CA    1 
ATOM   9355  C  C     . ASN B 1 475 ? 126.124 136.786 182.330 1.00 31.20 ?  475 ASN B C     1 
ATOM   9356  O  O     . ASN B 1 475 ? 125.276 137.342 183.035 1.00 32.29 ?  475 ASN B O     1 
ATOM   9357  C  CB    . ASN B 1 475 ? 126.918 138.973 181.404 1.00 32.60 ?  475 ASN B CB    1 
ATOM   9358  C  CG    . ASN B 1 475 ? 128.068 139.957 181.427 1.00 28.65 ?  475 ASN B CG    1 
ATOM   9359  O  OD1   . ASN B 1 475 ? 128.327 140.603 182.441 1.00 35.73 ?  475 ASN B OD1   1 
ATOM   9360  N  ND2   . ASN B 1 475 ? 128.771 140.069 180.309 1.00 26.39 ?  475 ASN B ND2   1 
ATOM   9361  N  N     . GLY B 1 476 ? 126.020 135.512 181.965 1.00 32.89 ?  476 GLY B N     1 
ATOM   9362  C  CA    . GLY B 1 476 ? 124.920 134.679 182.416 1.00 33.00 ?  476 GLY B CA    1 
ATOM   9363  C  C     . GLY B 1 476 ? 123.562 135.076 181.882 1.00 35.02 ?  476 GLY B C     1 
ATOM   9364  O  O     . GLY B 1 476 ? 122.567 135.006 182.616 1.00 40.12 ?  476 GLY B O     1 
ATOM   9365  N  N     . ILE B 1 477 ? 123.490 135.489 180.619 1.00 28.29 ?  477 ILE B N     1 
ATOM   9366  C  CA    . ILE B 1 477 ? 122.243 135.895 179.986 1.00 31.19 ?  477 ILE B CA    1 
ATOM   9367  C  C     . ILE B 1 477 ? 122.033 135.042 178.745 1.00 35.05 ?  477 ILE B C     1 
ATOM   9368  O  O     . ILE B 1 477 ? 122.936 134.918 177.910 1.00 38.62 ?  477 ILE B O     1 
ATOM   9369  C  CB    . ILE B 1 477 ? 122.247 137.391 179.625 1.00 29.43 ?  477 ILE B CB    1 
ATOM   9370  C  CG1   . ILE B 1 477 ? 122.405 138.245 180.884 1.00 32.14 ?  477 ILE B CG1   1 
ATOM   9371  C  CG2   . ILE B 1 477 ? 120.973 137.763 178.888 1.00 28.25 ?  477 ILE B CG2   1 
ATOM   9372  C  CD1   . ILE B 1 477 ? 122.826 139.668 180.606 1.00 34.18 ?  477 ILE B CD1   1 
ATOM   9373  N  N     . ALA B 1 478 ? 120.847 134.450 178.631 1.00 31.43 ?  478 ALA B N     1 
ATOM   9374  C  CA    . ALA B 1 478 ? 120.522 133.652 177.458 1.00 28.17 ?  478 ALA B CA    1 
ATOM   9375  C  C     . ALA B 1 478 ? 120.264 134.551 176.257 1.00 30.07 ?  478 ALA B C     1 
ATOM   9376  O  O     . ALA B 1 478 ? 119.603 135.587 176.366 1.00 34.68 ?  478 ALA B O     1 
ATOM   9377  C  CB    . ALA B 1 478 ? 119.302 132.774 177.732 1.00 31.53 ?  478 ALA B CB    1 
ATOM   9378  N  N     . TYR B 1 479 ? 120.795 134.146 175.102 1.00 28.16 ?  479 TYR B N     1 
ATOM   9379  C  CA    . TYR B 1 479 ? 120.633 134.948 173.894 1.00 21.99 ?  479 TYR B CA    1 
ATOM   9380  C  C     . TYR B 1 479 ? 119.160 135.164 173.567 1.00 28.70 ?  479 TYR B C     1 
ATOM   9381  O  O     . TYR B 1 479 ? 118.769 136.244 173.108 1.00 35.70 ?  479 TYR B O     1 
ATOM   9382  C  CB    . TYR B 1 479 ? 121.353 134.283 172.722 1.00 21.99 ?  479 TYR B CB    1 
ATOM   9383  C  CG    . TYR B 1 479 ? 121.427 135.136 171.478 1.00 27.97 ?  479 TYR B CG    1 
ATOM   9384  C  CD1   . TYR B 1 479 ? 120.394 135.142 170.551 1.00 27.56 ?  479 TYR B CD1   1 
ATOM   9385  C  CD2   . TYR B 1 479 ? 122.535 135.936 171.228 1.00 25.04 ?  479 TYR B CD2   1 
ATOM   9386  C  CE1   . TYR B 1 479 ? 120.459 135.921 169.415 1.00 27.63 ?  479 TYR B CE1   1 
ATOM   9387  C  CE2   . TYR B 1 479 ? 122.610 136.717 170.095 1.00 23.31 ?  479 TYR B CE2   1 
ATOM   9388  C  CZ    . TYR B 1 479 ? 121.570 136.706 169.191 1.00 30.75 ?  479 TYR B CZ    1 
ATOM   9389  O  OH    . TYR B 1 479 ? 121.641 137.484 168.059 1.00 31.97 ?  479 TYR B OH    1 
ATOM   9390  N  N     . GLU B 1 480 ? 118.328 134.150 173.796 1.00 32.01 ?  480 GLU B N     1 
ATOM   9391  C  CA    . GLU B 1 480 ? 116.907 134.220 173.483 1.00 33.40 ?  480 GLU B CA    1 
ATOM   9392  C  C     . GLU B 1 480 ? 116.072 134.808 174.611 1.00 35.70 ?  480 GLU B C     1 
ATOM   9393  O  O     . GLU B 1 480 ? 114.850 134.916 174.466 1.00 38.45 ?  480 GLU B O     1 
ATOM   9394  C  CB    . GLU B 1 480 ? 116.376 132.828 173.134 1.00 33.39 ?  480 GLU B CB    1 
ATOM   9395  C  CG    . GLU B 1 480 ? 117.004 132.206 171.901 1.00 33.82 ?  480 GLU B CG    1 
ATOM   9396  C  CD    . GLU B 1 480 ? 117.021 130.693 171.968 1.00 41.67 ?  480 GLU B CD    1 
ATOM   9397  O  OE1   . GLU B 1 480 ? 117.971 130.133 172.553 1.00 42.71 ?  480 GLU B OE1   1 
ATOM   9398  O  OE2   . GLU B 1 480 ? 116.081 130.062 171.441 1.00 40.94 -1 480 GLU B OE2   1 
ATOM   9399  N  N     . SER B 1 481 ? 116.687 135.184 175.723 1.00 33.91 ?  481 SER B N     1 
ATOM   9400  C  CA    . SER B 1 481 ? 115.931 135.685 176.857 1.00 30.22 ?  481 SER B CA    1 
ATOM   9401  C  C     . SER B 1 481 ? 115.469 137.121 176.620 1.00 33.51 ?  481 SER B C     1 
ATOM   9402  O  O     . SER B 1 481 ? 116.081 137.860 175.846 1.00 35.88 ?  481 SER B O     1 
ATOM   9403  C  CB    . SER B 1 481 ? 116.773 135.619 178.126 1.00 30.82 ?  481 SER B CB    1 
ATOM   9404  O  OG    . SER B 1 481 ? 117.468 136.833 178.339 1.00 37.89 ?  481 SER B OG    1 
ATOM   9405  N  N     . PRO B 1 482 ? 114.377 137.534 177.268 1.00 37.40 ?  482 PRO B N     1 
ATOM   9406  C  CA    . PRO B 1 482 ? 113.981 138.948 177.193 1.00 32.29 ?  482 PRO B CA    1 
ATOM   9407  C  C     . PRO B 1 482 ? 115.028 139.888 177.759 1.00 32.66 ?  482 PRO B C     1 
ATOM   9408  O  O     . PRO B 1 482 ? 115.103 141.046 177.330 1.00 37.68 ?  482 PRO B O     1 
ATOM   9409  C  CB    . PRO B 1 482 ? 112.680 138.991 178.007 1.00 33.04 ?  482 PRO B CB    1 
ATOM   9410  C  CG    . PRO B 1 482 ? 112.184 137.588 178.013 1.00 33.92 ?  482 PRO B CG    1 
ATOM   9411  C  CD    . PRO B 1 482 ? 113.408 136.728 178.027 1.00 36.39 ?  482 PRO B CD    1 
ATOM   9412  N  N     . GLU B 1 483 ? 115.836 139.427 178.715 1.00 35.55 ?  483 GLU B N     1 
ATOM   9413  C  CA    . GLU B 1 483 ? 116.896 140.268 179.263 1.00 31.13 ?  483 GLU B CA    1 
ATOM   9414  C  C     . GLU B 1 483 ? 117.956 140.575 178.213 1.00 31.58 ?  483 GLU B C     1 
ATOM   9415  O  O     . GLU B 1 483 ? 118.483 141.692 178.162 1.00 36.22 ?  483 GLU B O     1 
ATOM   9416  C  CB    . GLU B 1 483 ? 117.522 139.594 180.483 1.00 32.09 ?  483 GLU B CB    1 
ATOM   9417  C  CG    . GLU B 1 483 ? 116.594 139.501 181.683 1.00 38.17 ?  483 GLU B CG    1 
ATOM   9418  C  CD    . GLU B 1 483 ? 115.631 138.331 181.589 1.00 42.81 ?  483 GLU B CD    1 
ATOM   9419  O  OE1   . GLU B 1 483 ? 115.410 137.829 180.468 1.00 42.10 ?  483 GLU B OE1   1 
ATOM   9420  O  OE2   . GLU B 1 483 ? 115.093 137.914 182.635 1.00 39.91 -1 483 GLU B OE2   1 
ATOM   9421  N  N     . ALA B 1 484 ? 118.289 139.593 177.373 1.00 26.67 ?  484 ALA B N     1 
ATOM   9422  C  CA    . ALA B 1 484 ? 119.241 139.839 176.297 1.00 28.69 ?  484 ALA B CA    1 
ATOM   9423  C  C     . ALA B 1 484 ? 118.711 140.889 175.329 1.00 28.99 ?  484 ALA B C     1 
ATOM   9424  O  O     . ALA B 1 484 ? 119.455 141.775 174.892 1.00 28.87 ?  484 ALA B O     1 
ATOM   9425  C  CB    . ALA B 1 484 ? 119.553 138.537 175.563 1.00 25.26 ?  484 ALA B CB    1 
ATOM   9426  N  N     . ARG B 1 485 ? 117.427 140.804 174.981 1.00 32.02 ?  485 ARG B N     1 
ATOM   9427  C  CA    . ARG B 1 485 ? 116.837 141.806 174.101 1.00 25.69 ?  485 ARG B CA    1 
ATOM   9428  C  C     . ARG B 1 485 ? 116.800 143.174 174.769 1.00 24.10 ?  485 ARG B C     1 
ATOM   9429  O  O     . ARG B 1 485 ? 116.995 144.196 174.105 1.00 29.83 ?  485 ARG B O     1 
ATOM   9430  C  CB    . ARG B 1 485 ? 115.437 141.371 173.673 1.00 27.04 ?  485 ARG B CB    1 
ATOM   9431  C  CG    . ARG B 1 485 ? 115.435 140.298 172.601 1.00 22.16 ?  485 ARG B CG    1 
ATOM   9432  C  CD    . ARG B 1 485 ? 114.039 140.057 172.059 1.00 26.40 ?  485 ARG B CD    1 
ATOM   9433  N  NE    . ARG B 1 485 ? 113.125 139.584 173.091 1.00 31.54 ?  485 ARG B NE    1 
ATOM   9434  C  CZ    . ARG B 1 485 ? 113.035 138.322 173.489 1.00 30.91 ?  485 ARG B CZ    1 
ATOM   9435  N  NH1   . ARG B 1 485 ? 113.793 137.376 172.963 1.00 29.90 1  485 ARG B NH1   1 
ATOM   9436  N  NH2   . ARG B 1 485 ? 112.159 138.003 174.436 1.00 30.42 ?  485 ARG B NH2   1 
ATOM   9437  N  N     . ASP B 1 486 ? 116.550 143.216 176.078 1.00 27.54 ?  486 ASP B N     1 
ATOM   9438  C  CA    . ASP B 1 486 ? 116.578 144.485 176.797 1.00 28.12 ?  486 ASP B CA    1 
ATOM   9439  C  C     . ASP B 1 486 ? 117.965 145.112 176.746 1.00 30.60 ?  486 ASP B C     1 
ATOM   9440  O  O     . ASP B 1 486 ? 118.116 146.315 176.485 1.00 34.22 ?  486 ASP B O     1 
ATOM   9441  C  CB    . ASP B 1 486 ? 116.133 144.269 178.244 1.00 31.64 ?  486 ASP B CB    1 
ATOM   9442  C  CG    . ASP B 1 486 ? 115.872 145.566 178.974 1.00 40.39 ?  486 ASP B CG    1 
ATOM   9443  O  OD1   . ASP B 1 486 ? 114.991 146.332 178.530 1.00 41.83 ?  486 ASP B OD1   1 
ATOM   9444  O  OD2   . ASP B 1 486 ? 116.544 145.820 179.995 1.00 40.69 -1 486 ASP B OD2   1 
ATOM   9445  N  N     . PHE B 1 487 ? 118.998 144.301 176.986 1.00 27.28 ?  487 PHE B N     1 
ATOM   9446  C  CA    . PHE B 1 487 ? 120.358 144.820 176.904 1.00 24.33 ?  487 PHE B CA    1 
ATOM   9447  C  C     . PHE B 1 487 ? 120.678 145.300 175.499 1.00 25.48 ?  487 PHE B C     1 
ATOM   9448  O  O     . PHE B 1 487 ? 121.303 146.348 175.326 1.00 30.45 ?  487 PHE B O     1 
ATOM   9449  C  CB    . PHE B 1 487 ? 121.381 143.770 177.327 1.00 29.11 ?  487 PHE B CB    1 
ATOM   9450  C  CG    . PHE B 1 487 ? 122.760 144.054 176.804 1.00 29.48 ?  487 PHE B CG    1 
ATOM   9451  C  CD1   . PHE B 1 487 ? 123.587 144.957 177.452 1.00 26.23 ?  487 PHE B CD1   1 
ATOM   9452  C  CD2   . PHE B 1 487 ? 123.215 143.453 175.643 1.00 23.81 ?  487 PHE B CD2   1 
ATOM   9453  C  CE1   . PHE B 1 487 ? 124.846 145.237 176.962 1.00 27.58 ?  487 PHE B CE1   1 
ATOM   9454  C  CE2   . PHE B 1 487 ? 124.473 143.733 175.149 1.00 23.27 ?  487 PHE B CE2   1 
ATOM   9455  C  CZ    . PHE B 1 487 ? 125.289 144.625 175.810 1.00 27.42 ?  487 PHE B CZ    1 
ATOM   9456  N  N     . ALA B 1 488 ? 120.294 144.526 174.482 1.00 24.59 ?  488 ALA B N     1 
ATOM   9457  C  CA    . ALA B 1 488 ? 120.575 144.940 173.113 1.00 17.74 ?  488 ALA B CA    1 
ATOM   9458  C  C     . ALA B 1 488 ? 119.878 146.252 172.792 1.00 23.48 ?  488 ALA B C     1 
ATOM   9459  O  O     . ALA B 1 488 ? 120.472 147.152 172.189 1.00 31.84 ?  488 ALA B O     1 
ATOM   9460  C  CB    . ALA B 1 488 ? 120.149 143.847 172.133 1.00 21.84 ?  488 ALA B CB    1 
ATOM   9461  N  N     . ASN B 1 489 ? 118.619 146.384 173.212 1.00 22.02 ?  489 ASN B N     1 
ATOM   9462  C  CA    . ASN B 1 489 ? 117.889 147.628 173.019 1.00 23.04 ?  489 ASN B CA    1 
ATOM   9463  C  C     . ASN B 1 489 ? 118.643 148.801 173.629 1.00 23.63 ?  489 ASN B C     1 
ATOM   9464  O  O     . ASN B 1 489 ? 118.914 149.798 172.953 1.00 28.23 ?  489 ASN B O     1 
ATOM   9465  C  CB    . ASN B 1 489 ? 116.493 147.502 173.630 1.00 24.09 ?  489 ASN B CB    1 
ATOM   9466  C  CG    . ASN B 1 489 ? 115.584 148.649 173.256 1.00 29.67 ?  489 ASN B CG    1 
ATOM   9467  O  OD1   . ASN B 1 489 ? 115.479 149.020 172.087 1.00 35.37 ?  489 ASN B OD1   1 
ATOM   9468  N  ND2   . ASN B 1 489 ? 114.917 149.218 174.249 1.00 31.41 ?  489 ASN B ND2   1 
ATOM   9469  N  N     . THR B 1 490 ? 119.017 148.687 174.905 1.00 19.49 ?  490 THR B N     1 
ATOM   9470  C  CA    . THR B 1 490 ? 119.679 149.804 175.574 1.00 22.26 ?  490 THR B CA    1 
ATOM   9471  C  C     . THR B 1 490 ? 121.029 150.113 174.934 1.00 21.80 ?  490 THR B C     1 
ATOM   9472  O  O     . THR B 1 490 ? 121.351 151.276 174.657 1.00 22.37 ?  490 THR B O     1 
ATOM   9473  C  CB    . THR B 1 490 ? 119.847 149.503 177.063 1.00 31.63 ?  490 THR B CB    1 
ATOM   9474  O  OG1   . THR B 1 490 ? 118.576 149.157 177.627 1.00 36.88 ?  490 THR B OG1   1 
ATOM   9475  C  CG2   . THR B 1 490 ? 120.405 150.713 177.793 1.00 24.29 ?  490 THR B CG2   1 
ATOM   9476  N  N     . PHE B 1 491 ? 121.829 149.075 174.682 1.00 20.04 ?  491 PHE B N     1 
ATOM   9477  C  CA    . PHE B 1 491 ? 123.176 149.274 174.165 1.00 18.35 ?  491 PHE B CA    1 
ATOM   9478  C  C     . PHE B 1 491 ? 123.148 149.913 172.785 1.00 20.84 ?  491 PHE B C     1 
ATOM   9479  O  O     . PHE B 1 491 ? 123.904 150.849 172.505 1.00 21.23 ?  491 PHE B O     1 
ATOM   9480  C  CB    . PHE B 1 491 ? 123.919 147.938 174.124 1.00 22.35 ?  491 PHE B CB    1 
ATOM   9481  C  CG    . PHE B 1 491 ? 125.302 148.028 173.543 1.00 18.15 ?  491 PHE B CG    1 
ATOM   9482  C  CD1   . PHE B 1 491 ? 125.508 147.887 172.182 1.00 15.74 ?  491 PHE B CD1   1 
ATOM   9483  C  CD2   . PHE B 1 491 ? 126.397 148.245 174.361 1.00 17.90 ?  491 PHE B CD2   1 
ATOM   9484  C  CE1   . PHE B 1 491 ? 126.776 147.971 171.648 1.00 18.09 ?  491 PHE B CE1   1 
ATOM   9485  C  CE2   . PHE B 1 491 ? 127.667 148.328 173.830 1.00 15.78 ?  491 PHE B CE2   1 
ATOM   9486  C  CZ    . PHE B 1 491 ? 127.857 148.191 172.474 1.00 20.51 ?  491 PHE B CZ    1 
ATOM   9487  N  N     . PHE B 1 492 ? 122.279 149.422 171.900 1.00 20.20 ?  492 PHE B N     1 
ATOM   9488  C  CA    . PHE B 1 492 ? 122.258 149.964 170.552 1.00 11.01 ?  492 PHE B CA    1 
ATOM   9489  C  C     . PHE B 1 492 ? 121.544 151.305 170.487 1.00 13.80 ?  492 PHE B C     1 
ATOM   9490  O  O     . PHE B 1 492 ? 121.876 152.127 169.630 1.00 23.62 ?  492 PHE B O     1 
ATOM   9491  C  CB    . PHE B 1 492 ? 121.645 148.947 169.593 1.00 14.78 ?  492 PHE B CB    1 
ATOM   9492  C  CG    . PHE B 1 492 ? 122.568 147.806 169.281 1.00 18.57 ?  492 PHE B CG    1 
ATOM   9493  C  CD1   . PHE B 1 492 ? 123.608 147.968 168.382 1.00 16.18 ?  492 PHE B CD1   1 
ATOM   9494  C  CD2   . PHE B 1 492 ? 122.416 146.581 169.908 1.00 14.80 ?  492 PHE B CD2   1 
ATOM   9495  C  CE1   . PHE B 1 492 ? 124.467 146.926 168.100 1.00 12.60 ?  492 PHE B CE1   1 
ATOM   9496  C  CE2   . PHE B 1 492 ? 123.271 145.537 169.633 1.00 14.11 ?  492 PHE B CE2   1 
ATOM   9497  C  CZ    . PHE B 1 492 ? 124.298 145.708 168.726 1.00 13.84 ?  492 PHE B CZ    1 
ATOM   9498  N  N     . MET B 1 493 ? 120.605 151.575 171.398 1.00 13.16 ?  493 MET B N     1 
ATOM   9499  C  CA    . MET B 1 493 ? 120.100 152.935 171.523 1.00 15.58 ?  493 MET B CA    1 
ATOM   9500  C  C     . MET B 1 493 ? 121.219 153.894 171.899 1.00 17.23 ?  493 MET B C     1 
ATOM   9501  O  O     . MET B 1 493 ? 121.332 154.983 171.328 1.00 24.60 ?  493 MET B O     1 
ATOM   9502  C  CB    . MET B 1 493 ? 118.983 152.996 172.562 1.00 17.88 ?  493 MET B CB    1 
ATOM   9503  C  CG    . MET B 1 493 ? 118.327 154.359 172.670 1.00 19.02 ?  493 MET B CG    1 
ATOM   9504  S  SD    . MET B 1 493 ? 118.989 155.339 174.030 1.00 37.09 ?  493 MET B SD    1 
ATOM   9505  C  CE    . MET B 1 493 ? 119.011 154.129 175.346 1.00 26.08 ?  493 MET B CE    1 
ATOM   9506  N  N     . MET B 1 494 ? 122.060 153.504 172.861 1.00 16.96 ?  494 MET B N     1 
ATOM   9507  C  CA    . MET B 1 494 ? 123.182 154.356 173.241 1.00 17.12 ?  494 MET B CA    1 
ATOM   9508  C  C     . MET B 1 494 ? 124.157 154.533 172.083 1.00 21.67 ?  494 MET B C     1 
ATOM   9509  O  O     . MET B 1 494 ? 124.668 155.636 171.849 1.00 26.32 ?  494 MET B O     1 
ATOM   9510  C  CB    . MET B 1 494 ? 123.898 153.768 174.456 1.00 17.99 ?  494 MET B CB    1 
ATOM   9511  C  CG    . MET B 1 494 ? 123.100 153.837 175.744 1.00 22.17 ?  494 MET B CG    1 
ATOM   9512  S  SD    . MET B 1 494 ? 124.055 153.298 177.171 1.00 40.07 ?  494 MET B SD    1 
ATOM   9513  C  CE    . MET B 1 494 ? 125.497 154.347 177.025 1.00 26.77 ?  494 MET B CE    1 
ATOM   9514  N  N     . VAL B 1 495 ? 124.431 153.451 171.353 1.00 17.30 ?  495 VAL B N     1 
ATOM   9515  C  CA    . VAL B 1 495 ? 125.348 153.526 170.219 1.00 10.11 ?  495 VAL B CA    1 
ATOM   9516  C  C     . VAL B 1 495 ? 124.809 154.484 169.166 1.00 19.83 ?  495 VAL B C     1 
ATOM   9517  O  O     . VAL B 1 495 ? 125.542 155.325 168.636 1.00 27.47 ?  495 VAL B O     1 
ATOM   9518  C  CB    . VAL B 1 495 ? 125.591 152.125 169.632 1.00 17.76 ?  495 VAL B CB    1 
ATOM   9519  C  CG1   . VAL B 1 495 ? 126.316 152.229 168.299 1.00 9.69  ?  495 VAL B CG1   1 
ATOM   9520  C  CG2   . VAL B 1 495 ? 126.376 151.268 170.609 1.00 14.71 ?  495 VAL B CG2   1 
ATOM   9521  N  N     . ASN B 1 496 ? 123.519 154.368 168.846 1.00 19.62 ?  496 ASN B N     1 
ATOM   9522  C  CA    . ASN B 1 496 ? 122.908 155.267 167.875 1.00 14.17 ?  496 ASN B CA    1 
ATOM   9523  C  C     . ASN B 1 496 ? 122.943 156.707 168.362 1.00 16.20 ?  496 ASN B C     1 
ATOM   9524  O  O     . ASN B 1 496 ? 123.244 157.625 167.591 1.00 21.58 ?  496 ASN B O     1 
ATOM   9525  C  CB    . ASN B 1 496 ? 121.471 154.827 167.596 1.00 14.61 ?  496 ASN B CB    1 
ATOM   9526  C  CG    . ASN B 1 496 ? 120.884 155.496 166.375 1.00 15.84 ?  496 ASN B CG    1 
ATOM   9527  O  OD1   . ASN B 1 496 ? 121.571 155.702 165.378 1.00 19.80 ?  496 ASN B OD1   1 
ATOM   9528  N  ND2   . ASN B 1 496 ? 119.606 155.838 166.447 1.00 18.30 ?  496 ASN B ND2   1 
ATOM   9529  N  N     . PHE B 1 497 ? 122.636 156.927 169.641 1.00 17.62 ?  497 PHE B N     1 
ATOM   9530  C  CA    . PHE B 1 497 ? 122.655 158.275 170.192 1.00 14.40 ?  497 PHE B CA    1 
ATOM   9531  C  C     . PHE B 1 497 ? 124.032 158.903 170.045 1.00 20.22 ?  497 PHE B C     1 
ATOM   9532  O  O     . PHE B 1 497 ? 124.165 160.039 169.576 1.00 22.36 ?  497 PHE B O     1 
ATOM   9533  C  CB    . PHE B 1 497 ? 122.230 158.238 171.661 1.00 18.20 ?  497 PHE B CB    1 
ATOM   9534  C  CG    . PHE B 1 497 ? 122.308 159.567 172.355 1.00 24.43 ?  497 PHE B CG    1 
ATOM   9535  C  CD1   . PHE B 1 497 ? 121.223 160.426 172.361 1.00 23.90 ?  497 PHE B CD1   1 
ATOM   9536  C  CD2   . PHE B 1 497 ? 123.463 159.950 173.017 1.00 21.05 ?  497 PHE B CD2   1 
ATOM   9537  C  CE1   . PHE B 1 497 ? 121.292 161.645 173.003 1.00 19.70 ?  497 PHE B CE1   1 
ATOM   9538  C  CE2   . PHE B 1 497 ? 123.538 161.170 173.658 1.00 20.99 ?  497 PHE B CE2   1 
ATOM   9539  C  CZ    . PHE B 1 497 ? 122.450 162.017 173.651 1.00 19.80 ?  497 PHE B CZ    1 
ATOM   9540  N  N     . TYR B 1 498 ? 125.075 158.165 170.419 1.00 28.07 ?  498 TYR B N     1 
ATOM   9541  C  CA    . TYR B 1 498 ? 126.413 158.739 170.385 1.00 21.75 ?  498 TYR B CA    1 
ATOM   9542  C  C     . TYR B 1 498 ? 126.957 158.852 168.968 1.00 23.40 ?  498 TYR B C     1 
ATOM   9543  O  O     . TYR B 1 498 ? 127.712 159.784 168.681 1.00 29.16 ?  498 TYR B O     1 
ATOM   9544  C  CB    . TYR B 1 498 ? 127.352 157.926 171.277 1.00 17.94 ?  498 TYR B CB    1 
ATOM   9545  C  CG    . TYR B 1 498 ? 127.074 158.156 172.741 1.00 24.35 ?  498 TYR B CG    1 
ATOM   9546  C  CD1   . TYR B 1 498 ? 127.230 159.416 173.302 1.00 22.55 ?  498 TYR B CD1   1 
ATOM   9547  C  CD2   . TYR B 1 498 ? 126.625 157.128 173.557 1.00 27.23 ?  498 TYR B CD2   1 
ATOM   9548  C  CE1   . TYR B 1 498 ? 126.968 159.641 174.635 1.00 24.84 ?  498 TYR B CE1   1 
ATOM   9549  C  CE2   . TYR B 1 498 ? 126.357 157.343 174.893 1.00 23.86 ?  498 TYR B CE2   1 
ATOM   9550  C  CZ    . TYR B 1 498 ? 126.532 158.602 175.426 1.00 28.61 ?  498 TYR B CZ    1 
ATOM   9551  O  OH    . TYR B 1 498 ? 126.268 158.823 176.757 1.00 35.01 ?  498 TYR B OH    1 
ATOM   9552  N  N     . SER B 1 499 ? 126.562 157.958 168.060 1.00 16.85 ?  499 SER B N     1 
ATOM   9553  C  CA    . SER B 1 499 ? 126.972 158.116 166.669 1.00 10.53 ?  499 SER B CA    1 
ATOM   9554  C  C     . SER B 1 499 ? 126.299 159.327 166.036 1.00 16.71 ?  499 SER B C     1 
ATOM   9555  O  O     . SER B 1 499 ? 126.937 160.073 165.285 1.00 24.20 ?  499 SER B O     1 
ATOM   9556  C  CB    . SER B 1 499 ? 126.668 156.845 165.875 1.00 12.73 ?  499 SER B CB    1 
ATOM   9557  O  OG    . SER B 1 499 ? 125.278 156.676 165.673 1.00 24.19 ?  499 SER B OG    1 
ATOM   9558  N  N     . ILE B 1 500 ? 125.018 159.553 166.341 1.00 15.58 ?  500 ILE B N     1 
ATOM   9559  C  CA    . ILE B 1 500 ? 124.340 160.749 165.850 1.00 21.40 ?  500 ILE B CA    1 
ATOM   9560  C  C     . ILE B 1 500 ? 124.985 162.000 166.427 1.00 18.40 ?  500 ILE B C     1 
ATOM   9561  O  O     . ILE B 1 500 ? 125.182 162.998 165.724 1.00 26.15 ?  500 ILE B O     1 
ATOM   9562  C  CB    . ILE B 1 500 ? 122.837 160.687 166.179 1.00 21.98 ?  500 ILE B CB    1 
ATOM   9563  C  CG1   . ILE B 1 500 ? 122.150 159.598 165.358 1.00 19.04 ?  500 ILE B CG1   1 
ATOM   9564  C  CG2   . ILE B 1 500 ? 122.182 162.036 165.927 1.00 14.37 ?  500 ILE B CG2   1 
ATOM   9565  C  CD1   . ILE B 1 500 ? 120.744 159.299 165.810 1.00 18.77 ?  500 ILE B CD1   1 
ATOM   9566  N  N     . GLN B 1 501 ? 125.308 161.974 167.721 1.00 20.08 ?  501 GLN B N     1 
ATOM   9567  C  CA    . GLN B 1 501 ? 125.947 163.128 168.341 1.00 22.88 ?  501 GLN B CA    1 
ATOM   9568  C  C     . GLN B 1 501 ? 127.305 163.410 167.709 1.00 24.65 ?  501 GLN B C     1 
ATOM   9569  O  O     . GLN B 1 501 ? 127.645 164.568 167.449 1.00 30.79 ?  501 GLN B O     1 
ATOM   9570  C  CB    . GLN B 1 501 ? 126.088 162.903 169.845 1.00 25.69 ?  501 GLN B CB    1 
ATOM   9571  C  CG    . GLN B 1 501 ? 126.084 164.182 170.659 1.00 23.11 ?  501 GLN B CG    1 
ATOM   9572  C  CD    . GLN B 1 501 ? 126.216 163.928 172.144 1.00 28.63 ?  501 GLN B CD    1 
ATOM   9573  O  OE1   . GLN B 1 501 ? 127.139 163.248 172.590 1.00 33.60 ?  501 GLN B OE1   1 
ATOM   9574  N  NE2   . GLN B 1 501 ? 125.287 164.471 172.922 1.00 30.29 ?  501 GLN B NE2   1 
ATOM   9575  N  N     . ARG B 1 502 ? 128.091 162.364 167.449 1.00 24.27 ?  502 ARG B N     1 
ATOM   9576  C  CA    . ARG B 1 502 ? 129.388 162.559 166.810 1.00 19.87 ?  502 ARG B CA    1 
ATOM   9577  C  C     . ARG B 1 502 ? 129.233 163.073 165.385 1.00 20.10 ?  502 ARG B C     1 
ATOM   9578  O  O     . ARG B 1 502 ? 130.022 163.911 164.937 1.00 26.81 ?  502 ARG B O     1 
ATOM   9579  C  CB    . ARG B 1 502 ? 130.188 161.258 166.826 1.00 21.06 ?  502 ARG B CB    1 
ATOM   9580  C  CG    . ARG B 1 502 ? 131.656 161.450 166.493 1.00 20.31 ?  502 ARG B CG    1 
ATOM   9581  C  CD    . ARG B 1 502 ? 132.258 162.587 167.299 1.00 22.83 ?  502 ARG B CD    1 
ATOM   9582  N  NE    . ARG B 1 502 ? 133.576 162.962 166.807 1.00 27.20 ?  502 ARG B NE    1 
ATOM   9583  C  CZ    . ARG B 1 502 ? 134.008 164.211 166.700 1.00 26.41 ?  502 ARG B CZ    1 
ATOM   9584  N  NH1   . ARG B 1 502 ? 133.253 165.237 167.054 1.00 26.45 1  502 ARG B NH1   1 
ATOM   9585  N  NH2   . ARG B 1 502 ? 135.231 164.436 166.226 1.00 27.21 ?  502 ARG B NH2   1 
ATOM   9586  N  N     . SER B 1 503 ? 128.238 162.575 164.650 1.00 17.99 ?  503 SER B N     1 
ATOM   9587  C  CA    . SER B 1 503 ? 128.005 163.074 163.299 1.00 20.29 ?  503 SER B CA    1 
ATOM   9588  C  C     . SER B 1 503 ? 127.634 164.551 163.319 1.00 22.62 ?  503 SER B C     1 
ATOM   9589  O  O     . SER B 1 503 ? 128.130 165.337 162.503 1.00 26.70 ?  503 SER B O     1 
ATOM   9590  C  CB    . SER B 1 503 ? 126.912 162.249 162.621 1.00 18.12 ?  503 SER B CB    1 
ATOM   9591  O  OG    . SER B 1 503 ? 126.831 162.540 161.239 1.00 20.14 ?  503 SER B OG    1 
ATOM   9592  N  N     . ALA B 1 504 ? 126.772 164.951 164.255 1.00 25.26 ?  504 ALA B N     1 
ATOM   9593  C  CA    . ALA B 1 504 ? 126.415 166.360 164.379 1.00 24.91 ?  504 ALA B CA    1 
ATOM   9594  C  C     . ALA B 1 504 ? 127.621 167.203 164.776 1.00 28.92 ?  504 ALA B C     1 
ATOM   9595  O  O     . ALA B 1 504 ? 127.802 168.318 164.274 1.00 34.95 ?  504 ALA B O     1 
ATOM   9596  C  CB    . ALA B 1 504 ? 125.283 166.526 165.391 1.00 27.76 ?  504 ALA B CB    1 
ATOM   9597  N  N     . GLU B 1 505 ? 128.457 166.690 165.681 1.00 27.15 ?  505 GLU B N     1 
ATOM   9598  C  CA    . GLU B 1 505 ? 129.651 167.422 166.085 1.00 27.66 ?  505 GLU B CA    1 
ATOM   9599  C  C     . GLU B 1 505 ? 130.616 167.588 164.919 1.00 28.31 ?  505 GLU B C     1 
ATOM   9600  O  O     . GLU B 1 505 ? 131.227 168.649 164.757 1.00 33.46 ?  505 GLU B O     1 
ATOM   9601  C  CB    . GLU B 1 505 ? 130.336 166.708 167.249 1.00 26.68 ?  505 GLU B CB    1 
ATOM   9602  C  CG    . GLU B 1 505 ? 129.567 166.761 168.555 1.00 26.34 ?  505 GLU B CG    1 
ATOM   9603  C  CD    . GLU B 1 505 ? 130.056 165.737 169.558 1.00 36.22 ?  505 GLU B CD    1 
ATOM   9604  O  OE1   . GLU B 1 505 ? 130.975 164.963 169.220 1.00 38.16 ?  505 GLU B OE1   1 
ATOM   9605  O  OE2   . GLU B 1 505 ? 129.525 165.706 170.687 1.00 35.37 -1 505 GLU B OE2   1 
ATOM   9606  N  N     . ILE B 1 506 ? 130.774 166.546 164.102 1.00 27.77 ?  506 ILE B N     1 
ATOM   9607  C  CA    . ILE B 1 506 ? 131.635 166.642 162.929 1.00 24.77 ?  506 ILE B CA    1 
ATOM   9608  C  C     . ILE B 1 506 ? 131.068 167.646 161.935 1.00 27.53 ?  506 ILE B C     1 
ATOM   9609  O  O     . ILE B 1 506 ? 131.809 168.431 161.333 1.00 33.89 ?  506 ILE B O     1 
ATOM   9610  C  CB    . ILE B 1 506 ? 131.825 165.256 162.288 1.00 26.78 ?  506 ILE B CB    1 
ATOM   9611  C  CG1   . ILE B 1 506 ? 132.550 164.318 163.252 1.00 25.97 ?  506 ILE B CG1   1 
ATOM   9612  C  CG2   . ILE B 1 506 ? 132.584 165.373 160.976 1.00 22.78 ?  506 ILE B CG2   1 
ATOM   9613  C  CD1   . ILE B 1 506 ? 132.489 162.863 162.847 1.00 22.06 ?  506 ILE B CD1   1 
ATOM   9614  N  N     . ALA B 1 507 ? 129.747 167.638 161.744 1.00 28.01 ?  507 ALA B N     1 
ATOM   9615  C  CA    . ALA B 1 507 ? 129.130 168.602 160.842 1.00 27.59 ?  507 ALA B CA    1 
ATOM   9616  C  C     . ALA B 1 507 ? 129.348 170.028 161.333 1.00 30.50 ?  507 ALA B C     1 
ATOM   9617  O  O     . ALA B 1 507 ? 129.611 170.935 160.536 1.00 35.15 ?  507 ALA B O     1 
ATOM   9618  C  CB    . ALA B 1 507 ? 127.639 168.304 160.693 1.00 24.03 ?  507 ALA B CB    1 
ATOM   9619  N  N     . LYS B 1 508 ? 129.237 170.243 162.645 1.00 32.99 ?  508 LYS B N     1 
ATOM   9620  C  CA    . LYS B 1 508 ? 129.477 171.570 163.202 1.00 32.99 ?  508 LYS B CA    1 
ATOM   9621  C  C     . LYS B 1 508 ? 130.940 171.978 163.056 1.00 38.20 ?  508 LYS B C     1 
ATOM   9622  O  O     . LYS B 1 508 ? 131.237 173.123 162.696 1.00 41.38 ?  508 LYS B O     1 
ATOM   9623  C  CB    . LYS B 1 508 ? 129.054 171.604 164.670 1.00 37.16 ?  508 LYS B CB    1 
ATOM   9624  C  CG    . LYS B 1 508 ? 129.307 172.931 165.363 1.00 36.90 ?  508 LYS B CG    1 
ATOM   9625  C  CD    . LYS B 1 508 ? 129.041 172.830 166.854 1.00 36.48 ?  508 LYS B CD    1 
ATOM   9626  C  CE    . LYS B 1 508 ? 129.185 174.180 167.535 1.00 38.41 ?  508 LYS B CE    1 
ATOM   9627  N  NZ    . LYS B 1 508 ? 128.289 174.308 168.716 1.00 41.12 1  508 LYS B NZ    1 
ATOM   9628  N  N     . GLU B 1 509 ? 131.866 171.058 163.335 1.00 36.41 ?  509 GLU B N     1 
ATOM   9629  C  CA    . GLU B 1 509 ? 133.286 171.380 163.243 1.00 35.24 ?  509 GLU B CA    1 
ATOM   9630  C  C     . GLU B 1 509 ? 133.684 171.712 161.812 1.00 39.96 ?  509 GLU B C     1 
ATOM   9631  O  O     . GLU B 1 509 ? 134.409 172.683 161.568 1.00 46.39 ?  509 GLU B O     1 
ATOM   9632  C  CB    . GLU B 1 509 ? 134.123 170.215 163.770 1.00 36.97 ?  509 GLU B CB    1 
ATOM   9633  C  CG    . GLU B 1 509 ? 134.023 169.996 165.268 1.00 42.20 ?  509 GLU B CG    1 
ATOM   9634  C  CD    . GLU B 1 509 ? 134.451 168.601 165.681 1.00 45.11 ?  509 GLU B CD    1 
ATOM   9635  O  OE1   . GLU B 1 509 ? 135.073 167.901 164.853 1.00 40.82 ?  509 GLU B OE1   1 
ATOM   9636  O  OE2   . GLU B 1 509 ? 134.169 168.207 166.831 1.00 45.03 -1 509 GLU B OE2   1 
ATOM   9637  N  N     . LYS B 1 510 ? 133.221 170.915 160.852 1.00 36.39 ?  510 LYS B N     1 
ATOM   9638  C  CA    . LYS B 1 510 ? 133.528 171.137 159.448 1.00 30.78 ?  510 LYS B CA    1 
ATOM   9639  C  C     . LYS B 1 510 ? 132.555 172.091 158.773 1.00 35.81 ?  510 LYS B C     1 
ATOM   9640  O  O     . LYS B 1 510 ? 132.798 172.489 157.629 1.00 40.55 ?  510 LYS B O     1 
ATOM   9641  C  CB    . LYS B 1 510 ? 133.537 169.803 158.695 1.00 31.36 ?  510 LYS B CB    1 
ATOM   9642  C  CG    . LYS B 1 510 ? 134.470 168.771 159.295 1.00 30.66 ?  510 LYS B CG    1 
ATOM   9643  C  CD    . LYS B 1 510 ? 134.611 167.561 158.392 1.00 34.56 ?  510 LYS B CD    1 
ATOM   9644  C  CE    . LYS B 1 510 ? 135.641 166.590 158.943 1.00 36.99 ?  510 LYS B CE    1 
ATOM   9645  N  NZ    . LYS B 1 510 ? 136.323 165.826 157.865 1.00 36.65 1  510 LYS B NZ    1 
ATOM   9646  N  N     . GLY B 1 511 ? 131.473 172.466 159.446 1.00 37.01 ?  511 GLY B N     1 
ATOM   9647  C  CA    . GLY B 1 511 ? 130.498 173.358 158.841 1.00 31.61 ?  511 GLY B CA    1 
ATOM   9648  C  C     . GLY B 1 511 ? 129.926 172.821 157.549 1.00 39.14 ?  511 GLY B C     1 
ATOM   9649  O  O     . GLY B 1 511 ? 129.743 173.580 156.589 1.00 42.68 ?  511 GLY B O     1 
ATOM   9650  N  N     . GLU B 1 512 ? 129.643 171.523 157.500 1.00 34.42 ?  512 GLU B N     1 
ATOM   9651  C  CA    . GLU B 1 512 ? 129.125 170.908 156.288 1.00 32.01 ?  512 GLU B CA    1 
ATOM   9652  C  C     . GLU B 1 512 ? 128.429 169.605 156.646 1.00 30.67 ?  512 GLU B C     1 
ATOM   9653  O  O     . GLU B 1 512 ? 128.949 168.813 157.435 1.00 34.30 ?  512 GLU B O     1 
ATOM   9654  C  CB    . GLU B 1 512 ? 130.244 170.663 155.269 1.00 32.78 ?  512 GLU B CB    1 
ATOM   9655  C  CG    . GLU B 1 512 ? 130.803 169.252 155.279 1.00 33.98 ?  512 GLU B CG    1 
ATOM   9656  C  CD    . GLU B 1 512 ? 132.039 169.112 154.415 1.00 41.23 ?  512 GLU B CD    1 
ATOM   9657  O  OE1   . GLU B 1 512 ? 133.016 169.854 154.648 1.00 36.93 ?  512 GLU B OE1   1 
ATOM   9658  O  OE2   . GLU B 1 512 ? 132.034 168.259 153.502 1.00 40.07 -1 512 GLU B OE2   1 
ATOM   9659  N  N     . THR B 1 513 ? 127.252 169.402 156.071 1.00 31.80 ?  513 THR B N     1 
ATOM   9660  C  CA    . THR B 1 513 ? 126.476 168.181 156.211 1.00 25.56 ?  513 THR B CA    1 
ATOM   9661  C  C     . THR B 1 513 ? 126.638 167.334 154.953 1.00 25.94 ?  513 THR B C     1 
ATOM   9662  O  O     . THR B 1 513 ? 127.436 167.643 154.064 1.00 33.67 ?  513 THR B O     1 
ATOM   9663  C  CB    . THR B 1 513 ? 125.004 168.504 156.472 1.00 26.31 ?  513 THR B CB    1 
ATOM   9664  O  OG1   . THR B 1 513 ? 124.501 169.331 155.417 1.00 31.98 ?  513 THR B OG1   1 
ATOM   9665  C  CG2   . THR B 1 513 ? 124.846 169.231 157.796 1.00 24.74 ?  513 THR B CG2   1 
ATOM   9666  N  N     . PHE B 1 514 ? 125.872 166.252 154.881 1.00 20.95 ?  514 PHE B N     1 
ATOM   9667  C  CA    . PHE B 1 514 ? 125.901 165.429 153.685 1.00 20.76 ?  514 PHE B CA    1 
ATOM   9668  C  C     . PHE B 1 514 ? 124.903 165.955 152.659 1.00 22.22 ?  514 PHE B C     1 
ATOM   9669  O  O     . PHE B 1 514 ? 123.939 166.652 152.986 1.00 28.30 ?  514 PHE B O     1 
ATOM   9670  C  CB    . PHE B 1 514 ? 125.611 163.965 154.024 1.00 19.94 ?  514 PHE B CB    1 
ATOM   9671  C  CG    . PHE B 1 514 ? 124.226 163.715 154.546 1.00 17.63 ?  514 PHE B CG    1 
ATOM   9672  C  CD1   . PHE B 1 514 ? 123.190 163.399 153.684 1.00 19.14 ?  514 PHE B CD1   1 
ATOM   9673  C  CD2   . PHE B 1 514 ? 123.963 163.774 155.903 1.00 18.27 ?  514 PHE B CD2   1 
ATOM   9674  C  CE1   . PHE B 1 514 ? 121.919 163.159 154.164 1.00 17.45 ?  514 PHE B CE1   1 
ATOM   9675  C  CE2   . PHE B 1 514 ? 122.695 163.534 156.388 1.00 17.57 ?  514 PHE B CE2   1 
ATOM   9676  C  CZ    . PHE B 1 514 ? 121.672 163.226 155.517 1.00 16.43 ?  514 PHE B CZ    1 
ATOM   9677  N  N     . ASP B 1 515 ? 125.157 165.620 151.397 1.00 23.74 ?  515 ASP B N     1 
ATOM   9678  C  CA    . ASP B 1 515 ? 124.347 166.145 150.306 1.00 25.34 ?  515 ASP B CA    1 
ATOM   9679  C  C     . ASP B 1 515 ? 122.879 165.794 150.504 1.00 29.27 ?  515 ASP B C     1 
ATOM   9680  O  O     . ASP B 1 515 ? 122.529 164.634 150.734 1.00 35.69 ?  515 ASP B O     1 
ATOM   9681  C  CB    . ASP B 1 515 ? 124.848 165.599 148.971 1.00 30.93 ?  515 ASP B CB    1 
ATOM   9682  C  CG    . ASP B 1 515 ? 125.876 166.502 148.323 1.00 34.35 ?  515 ASP B CG    1 
ATOM   9683  O  OD1   . ASP B 1 515 ? 126.693 167.096 149.056 1.00 32.53 ?  515 ASP B OD1   1 
ATOM   9684  O  OD2   . ASP B 1 515 ? 125.865 166.619 147.080 1.00 36.50 -1 515 ASP B OD2   1 
ATOM   9685  N  N     . GLN B 1 516 ? 122.020 166.807 150.401 1.00 29.97 ?  516 GLN B N     1 
ATOM   9686  C  CA    . GLN B 1 516 ? 120.579 166.646 150.561 1.00 28.79 ?  516 GLN B CA    1 
ATOM   9687  C  C     . GLN B 1 516 ? 120.201 166.260 151.987 1.00 25.94 ?  516 GLN B C     1 
ATOM   9688  O  O     . GLN B 1 516 ? 119.239 165.522 152.204 1.00 33.29 ?  516 GLN B O     1 
ATOM   9689  C  CB    . GLN B 1 516 ? 120.020 165.625 149.567 1.00 24.51 ?  516 GLN B CB    1 
ATOM   9690  C  CG    . GLN B 1 516 ? 120.215 166.016 148.112 1.00 25.76 ?  516 GLN B CG    1 
ATOM   9691  C  CD    . GLN B 1 516 ? 119.721 164.955 147.153 1.00 31.96 ?  516 GLN B CD    1 
ATOM   9692  O  OE1   . GLN B 1 516 ? 118.519 164.820 146.926 1.00 34.39 ?  516 GLN B OE1   1 
ATOM   9693  N  NE2   . GLN B 1 516 ? 120.646 164.193 146.581 1.00 30.64 ?  516 GLN B NE2   1 
ATOM   9694  N  N     . TYR B 1 517 ? 120.954 166.755 152.970 1.00 24.99 ?  517 TYR B N     1 
ATOM   9695  C  CA    . TYR B 1 517 ? 120.600 166.505 154.363 1.00 23.11 ?  517 TYR B CA    1 
ATOM   9696  C  C     . TYR B 1 517 ? 119.302 167.208 154.737 1.00 29.20 ?  517 TYR B C     1 
ATOM   9697  O  O     . TYR B 1 517 ? 118.518 166.688 155.539 1.00 34.83 ?  517 TYR B O     1 
ATOM   9698  C  CB    . TYR B 1 517 ? 121.730 166.958 155.289 1.00 21.35 ?  517 TYR B CB    1 
ATOM   9699  C  CG    . TYR B 1 517 ? 121.244 167.307 156.675 1.00 27.43 ?  517 TYR B CG    1 
ATOM   9700  C  CD1   . TYR B 1 517 ? 121.049 166.320 157.632 1.00 20.15 ?  517 TYR B CD1   1 
ATOM   9701  C  CD2   . TYR B 1 517 ? 120.960 168.622 157.022 1.00 30.35 ?  517 TYR B CD2   1 
ATOM   9702  C  CE1   . TYR B 1 517 ? 120.596 166.633 158.894 1.00 23.61 ?  517 TYR B CE1   1 
ATOM   9703  C  CE2   . TYR B 1 517 ? 120.507 168.943 158.283 1.00 22.65 ?  517 TYR B CE2   1 
ATOM   9704  C  CZ    . TYR B 1 517 ? 120.325 167.945 159.214 1.00 25.88 ?  517 TYR B CZ    1 
ATOM   9705  O  OH    . TYR B 1 517 ? 119.873 168.261 160.473 1.00 37.57 ?  517 TYR B OH    1 
ATOM   9706  N  N     . GLU B 1 518 ? 119.060 168.393 154.170 1.00 30.47 ?  518 GLU B N     1 
ATOM   9707  C  CA    . GLU B 1 518 ? 117.910 169.193 154.579 1.00 28.56 ?  518 GLU B CA    1 
ATOM   9708  C  C     . GLU B 1 518 ? 116.599 168.450 154.369 1.00 34.91 ?  518 GLU B C     1 
ATOM   9709  O  O     . GLU B 1 518 ? 115.636 168.673 155.111 1.00 38.31 ?  518 GLU B O     1 
ATOM   9710  C  CB    . GLU B 1 518 ? 117.899 170.518 153.816 1.00 29.56 ?  518 GLU B CB    1 
ATOM   9711  C  CG    . GLU B 1 518 ? 119.037 171.457 154.182 1.00 36.20 ?  518 GLU B CG    1 
ATOM   9712  C  CD    . GLU B 1 518 ? 120.355 171.062 153.541 1.00 42.46 ?  518 GLU B CD    1 
ATOM   9713  O  OE1   . GLU B 1 518 ? 120.352 170.155 152.683 1.00 38.18 ?  518 GLU B OE1   1 
ATOM   9714  O  OE2   . GLU B 1 518 ? 121.392 171.659 153.897 1.00 41.86 -1 518 GLU B OE2   1 
ATOM   9715  N  N     . GLY B 1 519 ? 116.537 167.574 153.372 1.00 26.37 ?  519 GLY B N     1 
ATOM   9716  C  CA    . GLY B 1 519 ? 115.352 166.784 153.125 1.00 21.66 ?  519 GLY B CA    1 
ATOM   9717  C  C     . GLY B 1 519 ? 115.246 165.505 153.919 1.00 19.89 ?  519 GLY B C     1 
ATOM   9718  O  O     . GLY B 1 519 ? 114.232 164.811 153.822 1.00 27.64 ?  519 GLY B O     1 
ATOM   9719  N  N     . SER B 1 520 ? 116.260 165.172 154.712 1.00 19.98 ?  520 SER B N     1 
ATOM   9720  C  CA    . SER B 1 520 ? 116.272 163.925 155.457 1.00 23.41 ?  520 SER B CA    1 
ATOM   9721  C  C     . SER B 1 520 ? 115.384 164.021 156.694 1.00 24.67 ?  520 SER B C     1 
ATOM   9722  O  O     . SER B 1 520 ? 114.976 165.104 157.120 1.00 24.89 ?  520 SER B O     1 
ATOM   9723  C  CB    . SER B 1 520 ? 117.701 163.559 155.863 1.00 19.58 ?  520 SER B CB    1 
ATOM   9724  O  OG    . SER B 1 520 ? 118.236 164.513 156.760 1.00 20.83 ?  520 SER B OG    1 
ATOM   9725  N  N     . THR B 1 521 ? 115.079 162.855 157.268 1.00 21.34 ?  521 THR B N     1 
ATOM   9726  C  CA    . THR B 1 521 ? 114.294 162.814 158.495 1.00 22.05 ?  521 THR B CA    1 
ATOM   9727  C  C     . THR B 1 521 ? 115.055 163.387 159.683 1.00 26.63 ?  521 THR B C     1 
ATOM   9728  O  O     . THR B 1 521 ? 114.427 163.816 160.656 1.00 28.63 ?  521 THR B O     1 
ATOM   9729  C  CB    . THR B 1 521 ? 113.857 161.380 158.795 1.00 24.85 ?  521 THR B CB    1 
ATOM   9730  O  OG1   . THR B 1 521 ? 115.009 160.534 158.875 1.00 29.00 ?  521 THR B OG1   1 
ATOM   9731  C  CG2   . THR B 1 521 ? 112.933 160.869 157.704 1.00 18.47 ?  521 THR B CG2   1 
ATOM   9732  N  N     . TYR B 1 522 ? 116.389 163.395 159.632 1.00 28.02 ?  522 TYR B N     1 
ATOM   9733  C  CA    . TYR B 1 522 ? 117.158 164.086 160.661 1.00 20.40 ?  522 TYR B CA    1 
ATOM   9734  C  C     . TYR B 1 522 ? 116.874 165.581 160.642 1.00 27.20 ?  522 TYR B C     1 
ATOM   9735  O  O     . TYR B 1 522 ? 116.697 166.202 161.697 1.00 27.72 ?  522 TYR B O     1 
ATOM   9736  C  CB    . TYR B 1 522 ? 118.653 163.834 160.465 1.00 16.19 ?  522 TYR B CB    1 
ATOM   9737  C  CG    . TYR B 1 522 ? 119.050 162.378 160.420 1.00 17.59 ?  522 TYR B CG    1 
ATOM   9738  C  CD1   . TYR B 1 522 ? 119.069 161.607 161.573 1.00 24.12 ?  522 TYR B CD1   1 
ATOM   9739  C  CD2   . TYR B 1 522 ? 119.424 161.779 159.226 1.00 19.66 ?  522 TYR B CD2   1 
ATOM   9740  C  CE1   . TYR B 1 522 ? 119.441 160.280 161.537 1.00 20.26 ?  522 TYR B CE1   1 
ATOM   9741  C  CE2   . TYR B 1 522 ? 119.794 160.454 159.179 1.00 20.09 ?  522 TYR B CE2   1 
ATOM   9742  C  CZ    . TYR B 1 522 ? 119.801 159.709 160.337 1.00 21.38 ?  522 TYR B CZ    1 
ATOM   9743  O  OH    . TYR B 1 522 ? 120.169 158.388 160.290 1.00 28.32 ?  522 TYR B OH    1 
ATOM   9744  N  N     . ALA B 1 523 ? 116.827 166.177 159.449 1.00 28.62 ?  523 ALA B N     1 
ATOM   9745  C  CA    . ALA B 1 523 ? 116.610 167.616 159.344 1.00 26.64 ?  523 ALA B CA    1 
ATOM   9746  C  C     . ALA B 1 523 ? 115.216 168.003 159.814 1.00 29.69 ?  523 ALA B C     1 
ATOM   9747  O  O     . ALA B 1 523 ? 115.050 168.997 160.530 1.00 34.53 ?  523 ALA B O     1 
ATOM   9748  C  CB    . ALA B 1 523 ? 116.838 168.073 157.904 1.00 23.24 ?  523 ALA B CB    1 
ATOM   9749  N  N     . THR B 1 524 ? 114.202 167.232 159.425 1.00 30.33 ?  524 THR B N     1 
ATOM   9750  C  CA    . THR B 1 524 ? 112.830 167.526 159.812 1.00 28.21 ?  524 THR B CA    1 
ATOM   9751  C  C     . THR B 1 524 ? 112.505 167.081 161.231 1.00 33.32 ?  524 THR B C     1 
ATOM   9752  O  O     . THR B 1 524 ? 111.463 167.482 161.762 1.00 41.68 ?  524 THR B O     1 
ATOM   9753  C  CB    . THR B 1 524 ? 111.853 166.867 158.835 1.00 31.39 ?  524 THR B CB    1 
ATOM   9754  O  OG1   . THR B 1 524 ? 111.744 165.470 159.131 1.00 33.45 ?  524 THR B OG1   1 
ATOM   9755  C  CG2   . THR B 1 524 ? 112.340 167.039 157.406 1.00 31.26 ?  524 THR B CG2   1 
ATOM   9756  N  N     . GLY B 1 525 ? 113.360 166.272 161.851 1.00 25.82 ?  525 GLY B N     1 
ATOM   9757  C  CA    . GLY B 1 525 ? 113.131 165.800 163.199 1.00 23.97 ?  525 GLY B CA    1 
ATOM   9758  C  C     . GLY B 1 525 ? 112.275 164.560 163.311 1.00 31.06 ?  525 GLY B C     1 
ATOM   9759  O  O     . GLY B 1 525 ? 112.119 164.035 164.420 1.00 33.46 ?  525 GLY B O     1 
ATOM   9760  N  N     . GLU B 1 526 ? 111.715 164.071 162.204 1.00 34.44 ?  526 GLU B N     1 
ATOM   9761  C  CA    . GLU B 1 526 ? 110.900 162.864 162.248 1.00 32.81 ?  526 GLU B CA    1 
ATOM   9762  C  C     . GLU B 1 526 ? 111.706 161.642 162.666 1.00 33.62 ?  526 GLU B C     1 
ATOM   9763  O  O     . GLU B 1 526 ? 111.120 160.657 163.129 1.00 38.82 ?  526 GLU B O     1 
ATOM   9764  C  CB    . GLU B 1 526 ? 110.249 162.627 160.885 1.00 31.26 ?  526 GLU B CB    1 
ATOM   9765  C  CG    . GLU B 1 526 ? 109.541 161.292 160.750 1.00 34.63 ?  526 GLU B CG    1 
ATOM   9766  C  CD    . GLU B 1 526 ? 109.463 160.817 159.312 1.00 40.41 ?  526 GLU B CD    1 
ATOM   9767  O  OE1   . GLU B 1 526 ? 109.385 161.672 158.405 1.00 40.78 ?  526 GLU B OE1   1 
ATOM   9768  O  OE2   . GLU B 1 526 ? 109.482 159.589 159.087 1.00 38.91 -1 526 GLU B OE2   1 
ATOM   9769  N  N     . TYR B 1 527 ? 113.031 161.683 162.514 1.00 30.89 ?  527 TYR B N     1 
ATOM   9770  C  CA    . TYR B 1 527 ? 113.860 160.552 162.913 1.00 25.77 ?  527 TYR B CA    1 
ATOM   9771  C  C     . TYR B 1 527 ? 113.790 160.313 164.416 1.00 25.82 ?  527 TYR B C     1 
ATOM   9772  O  O     . TYR B 1 527 ? 113.769 159.163 164.869 1.00 34.11 ?  527 TYR B O     1 
ATOM   9773  C  CB    . TYR B 1 527 ? 115.306 160.788 162.475 1.00 21.19 ?  527 TYR B CB    1 
ATOM   9774  C  CG    . TYR B 1 527 ? 116.249 159.666 162.836 1.00 24.55 ?  527 TYR B CG    1 
ATOM   9775  C  CD1   . TYR B 1 527 ? 116.938 159.674 164.041 1.00 26.74 ?  527 TYR B CD1   1 
ATOM   9776  C  CD2   . TYR B 1 527 ? 116.450 158.598 161.973 1.00 22.26 ?  527 TYR B CD2   1 
ATOM   9777  C  CE1   . TYR B 1 527 ? 117.798 158.652 164.377 1.00 21.36 ?  527 TYR B CE1   1 
ATOM   9778  C  CE2   . TYR B 1 527 ? 117.309 157.572 162.302 1.00 22.47 ?  527 TYR B CE2   1 
ATOM   9779  C  CZ    . TYR B 1 527 ? 117.980 157.604 163.503 1.00 21.56 ?  527 TYR B CZ    1 
ATOM   9780  O  OH    . TYR B 1 527 ? 118.838 156.583 163.834 1.00 30.62 ?  527 TYR B OH    1 
ATOM   9781  N  N     . PHE B 1 528 ? 113.750 161.384 165.201 1.00 27.85 ?  528 PHE B N     1 
ATOM   9782  C  CA    . PHE B 1 528 ? 113.865 161.307 166.651 1.00 24.84 ?  528 PHE B CA    1 
ATOM   9783  C  C     . PHE B 1 528 ? 112.527 161.098 167.348 1.00 32.72 ?  528 PHE B C     1 
ATOM   9784  O  O     . PHE B 1 528 ? 112.476 161.149 168.580 1.00 39.46 ?  528 PHE B O     1 
ATOM   9785  C  CB    . PHE B 1 528 ? 114.528 162.576 167.190 1.00 27.02 ?  528 PHE B CB    1 
ATOM   9786  C  CG    . PHE B 1 528 ? 115.878 162.854 166.599 1.00 29.85 ?  528 PHE B CG    1 
ATOM   9787  C  CD1   . PHE B 1 528 ? 116.000 163.588 165.432 1.00 25.93 ?  528 PHE B CD1   1 
ATOM   9788  C  CD2   . PHE B 1 528 ? 117.028 162.389 167.213 1.00 28.56 ?  528 PHE B CD2   1 
ATOM   9789  C  CE1   . PHE B 1 528 ? 117.241 163.846 164.888 1.00 31.23 ?  528 PHE B CE1   1 
ATOM   9790  C  CE2   . PHE B 1 528 ? 118.271 162.646 166.674 1.00 25.26 ?  528 PHE B CE2   1 
ATOM   9791  C  CZ    . PHE B 1 528 ? 118.378 163.374 165.509 1.00 31.64 ?  528 PHE B CZ    1 
ATOM   9792  N  N     . ASP B 1 529 ? 111.448 160.870 166.597 1.00 35.68 ?  529 ASP B N     1 
ATOM   9793  C  CA    . ASP B 1 529 ? 110.125 160.776 167.208 1.00 32.02 ?  529 ASP B CA    1 
ATOM   9794  C  C     . ASP B 1 529 ? 110.078 159.681 168.268 1.00 35.56 ?  529 ASP B C     1 
ATOM   9795  O  O     . ASP B 1 529 ? 109.668 159.922 169.410 1.00 40.17 ?  529 ASP B O     1 
ATOM   9796  C  CB    . ASP B 1 529 ? 109.071 160.529 166.130 1.00 31.36 ?  529 ASP B CB    1 
ATOM   9797  C  CG    . ASP B 1 529 ? 108.693 161.792 165.384 1.00 39.26 ?  529 ASP B CG    1 
ATOM   9798  O  OD1   . ASP B 1 529 ? 109.071 162.888 165.844 1.00 41.28 ?  529 ASP B OD1   1 
ATOM   9799  O  OD2   . ASP B 1 529 ? 108.019 161.688 164.338 1.00 43.00 -1 529 ASP B OD2   1 
ATOM   9800  N  N     . LYS B 1 530 ? 110.504 158.468 167.909 1.00 36.05 ?  530 LYS B N     1 
ATOM   9801  C  CA    . LYS B 1 530 ? 110.444 157.360 168.856 1.00 35.90 ?  530 LYS B CA    1 
ATOM   9802  C  C     . LYS B 1 530 ? 111.421 157.547 170.007 1.00 34.72 ?  530 LYS B C     1 
ATOM   9803  O  O     . LYS B 1 530 ? 111.173 157.062 171.115 1.00 35.86 ?  530 LYS B O     1 
ATOM   9804  C  CB    . LYS B 1 530 ? 110.715 156.038 168.138 1.00 37.23 ?  530 LYS B CB    1 
ATOM   9805  C  CG    . LYS B 1 530 ? 112.183 155.660 168.052 1.00 32.20 ?  530 LYS B CG    1 
ATOM   9806  C  CD    . LYS B 1 530 ? 112.380 154.455 167.151 1.00 33.95 ?  530 LYS B CD    1 
ATOM   9807  C  CE    . LYS B 1 530 ? 113.805 153.946 167.212 1.00 28.68 ?  530 LYS B CE    1 
ATOM   9808  N  NZ    . LYS B 1 530 ? 114.278 153.486 165.880 1.00 39.97 1  530 LYS B NZ    1 
ATOM   9809  N  N     . TYR B 1 531 ? 112.533 158.241 169.768 1.00 34.71 ?  531 TYR B N     1 
ATOM   9810  C  CA    . TYR B 1 531 ? 113.513 158.451 170.825 1.00 27.57 ?  531 TYR B CA    1 
ATOM   9811  C  C     . TYR B 1 531 ? 113.059 159.524 171.806 1.00 30.02 ?  531 TYR B C     1 
ATOM   9812  O  O     . TYR B 1 531 ? 113.333 159.427 173.007 1.00 35.02 ?  531 TYR B O     1 
ATOM   9813  C  CB    . TYR B 1 531 ? 114.865 158.812 170.215 1.00 24.68 ?  531 TYR B CB    1 
ATOM   9814  C  CG    . TYR B 1 531 ? 115.564 157.640 169.575 1.00 26.42 ?  531 TYR B CG    1 
ATOM   9815  C  CD1   . TYR B 1 531 ? 115.898 156.518 170.319 1.00 22.60 ?  531 TYR B CD1   1 
ATOM   9816  C  CD2   . TYR B 1 531 ? 115.886 157.650 168.225 1.00 22.88 ?  531 TYR B CD2   1 
ATOM   9817  C  CE1   . TYR B 1 531 ? 116.538 155.444 169.742 1.00 28.30 ?  531 TYR B CE1   1 
ATOM   9818  C  CE2   . TYR B 1 531 ? 116.526 156.580 167.639 1.00 21.17 ?  531 TYR B CE2   1 
ATOM   9819  C  CZ    . TYR B 1 531 ? 116.850 155.479 168.402 1.00 27.96 ?  531 TYR B CZ    1 
ATOM   9820  O  OH    . TYR B 1 531 ? 117.488 154.408 167.824 1.00 33.71 ?  531 TYR B OH    1 
ATOM   9821  N  N     . VAL B 1 532 ? 112.367 160.553 171.314 1.00 35.80 ?  532 VAL B N     1 
ATOM   9822  C  CA    . VAL B 1 532 ? 111.853 161.590 172.199 1.00 35.17 ?  532 VAL B CA    1 
ATOM   9823  C  C     . VAL B 1 532 ? 110.557 161.173 172.879 1.00 36.03 ?  532 VAL B C     1 
ATOM   9824  O  O     . VAL B 1 532 ? 110.210 161.732 173.926 1.00 41.18 ?  532 VAL B O     1 
ATOM   9825  C  CB    . VAL B 1 532 ? 111.639 162.907 171.435 1.00 36.50 ?  532 VAL B CB    1 
ATOM   9826  C  CG1   . VAL B 1 532 ? 112.967 163.458 170.943 1.00 32.12 ?  532 VAL B CG1   1 
ATOM   9827  C  CG2   . VAL B 1 532 ? 110.682 162.697 170.275 1.00 33.58 ?  532 VAL B CG2   1 
ATOM   9828  N  N     . SER B 1 533 ? 109.832 160.205 172.318 1.00 40.40 ?  533 SER B N     1 
ATOM   9829  C  CA    . SER B 1 533 ? 108.575 159.760 172.902 1.00 39.17 ?  533 SER B CA    1 
ATOM   9830  C  C     . SER B 1 533 ? 108.700 158.482 173.721 1.00 42.01 ?  533 SER B C     1 
ATOM   9831  O  O     . SER B 1 533 ? 107.821 158.209 174.545 1.00 47.43 ?  533 SER B O     1 
ATOM   9832  C  CB    . SER B 1 533 ? 107.527 159.544 171.802 1.00 43.03 ?  533 SER B CB    1 
ATOM   9833  O  OG    . SER B 1 533 ? 107.749 158.324 171.118 1.00 45.93 ?  533 SER B OG    1 
ATOM   9834  N  N     . THR B 1 534 ? 109.757 157.701 173.522 1.00 40.08 ?  534 THR B N     1 
ATOM   9835  C  CA    . THR B 1 534 ? 109.915 156.413 174.180 1.00 38.23 ?  534 THR B CA    1 
ATOM   9836  C  C     . THR B 1 534 ? 111.223 156.376 174.958 1.00 40.92 ?  534 THR B C     1 
ATOM   9837  O  O     . THR B 1 534 ? 112.180 157.085 174.634 1.00 46.26 ?  534 THR B O     1 
ATOM   9838  C  CB    . THR B 1 534 ? 109.885 155.262 173.166 1.00 40.66 ?  534 THR B CB    1 
ATOM   9839  O  OG1   . THR B 1 534 ? 108.756 155.414 172.298 1.00 43.43 ?  534 THR B OG1   1 
ATOM   9840  C  CG2   . THR B 1 534 ? 109.793 153.922 173.879 1.00 38.02 ?  534 THR B CG2   1 
ATOM   9841  N  N     . ASP B 1 535 ? 111.252 155.539 175.991 1.00 40.17 ?  535 ASP B N     1 
ATOM   9842  C  CA    . ASP B 1 535 ? 112.433 155.334 176.816 1.00 35.63 ?  535 ASP B CA    1 
ATOM   9843  C  C     . ASP B 1 535 ? 113.043 153.975 176.502 1.00 38.73 ?  535 ASP B C     1 
ATOM   9844  O  O     . ASP B 1 535 ? 112.323 152.991 176.306 1.00 43.90 ?  535 ASP B O     1 
ATOM   9845  C  CB    . ASP B 1 535 ? 112.088 155.423 178.304 1.00 37.79 ?  535 ASP B CB    1 
ATOM   9846  C  CG    . ASP B 1 535 ? 113.272 155.111 179.196 1.00 44.82 ?  535 ASP B CG    1 
ATOM   9847  O  OD1   . ASP B 1 535 ? 114.208 155.936 179.255 1.00 43.22 ?  535 ASP B OD1   1 
ATOM   9848  O  OD2   . ASP B 1 535 ? 113.267 154.039 179.837 1.00 46.02 -1 535 ASP B OD2   1 
ATOM   9849  N  N     . PHE B 1 536 ? 114.374 153.925 176.455 1.00 30.54 ?  536 PHE B N     1 
ATOM   9850  C  CA    . PHE B 1 536 ? 115.090 152.704 176.110 1.00 30.22 ?  536 PHE B CA    1 
ATOM   9851  C  C     . PHE B 1 536 ? 116.048 152.264 177.212 1.00 36.58 ?  536 PHE B C     1 
ATOM   9852  O  O     . PHE B 1 536 ? 116.945 151.454 176.962 1.00 40.33 ?  536 PHE B O     1 
ATOM   9853  C  CB    . PHE B 1 536 ? 115.836 152.882 174.787 1.00 29.35 ?  536 PHE B CB    1 
ATOM   9854  C  CG    . PHE B 1 536 ? 114.929 153.038 173.601 1.00 29.86 ?  536 PHE B CG    1 
ATOM   9855  C  CD1   . PHE B 1 536 ? 114.477 151.931 172.909 1.00 28.90 ?  536 PHE B CD1   1 
ATOM   9856  C  CD2   . PHE B 1 536 ? 114.520 154.293 173.184 1.00 27.78 ?  536 PHE B CD2   1 
ATOM   9857  C  CE1   . PHE B 1 536 ? 113.641 152.070 171.821 1.00 28.87 ?  536 PHE B CE1   1 
ATOM   9858  C  CE2   . PHE B 1 536 ? 113.683 154.437 172.097 1.00 32.52 ?  536 PHE B CE2   1 
ATOM   9859  C  CZ    . PHE B 1 536 ? 113.244 153.324 171.415 1.00 29.13 ?  536 PHE B CZ    1 
ATOM   9860  N  N     . SER B 1 537 ? 115.877 152.782 178.424 1.00 35.00 ?  537 SER B N     1 
ATOM   9861  C  CA    . SER B 1 537 ? 116.658 152.298 179.547 1.00 33.99 ?  537 SER B CA    1 
ATOM   9862  C  C     . SER B 1 537 ? 116.245 150.869 179.889 1.00 36.38 ?  537 SER B C     1 
ATOM   9863  O  O     . SER B 1 537 ? 115.106 150.466 179.638 1.00 38.06 ?  537 SER B O     1 
ATOM   9864  C  CB    . SER B 1 537 ? 116.472 153.203 180.761 1.00 34.55 ?  537 SER B CB    1 
ATOM   9865  O  OG    . SER B 1 537 ? 115.134 153.167 181.226 1.00 38.01 ?  537 SER B OG    1 
ATOM   9866  N  N     . PRO B 1 538 ? 117.152 150.078 180.457 1.00 37.20 ?  538 PRO B N     1 
ATOM   9867  C  CA    . PRO B 1 538 ? 116.838 148.666 180.704 1.00 35.98 ?  538 PRO B CA    1 
ATOM   9868  C  C     . PRO B 1 538 ? 115.619 148.514 181.602 1.00 40.09 ?  538 PRO B C     1 
ATOM   9869  O  O     . PRO B 1 538 ? 115.463 149.222 182.599 1.00 39.19 ?  538 PRO B O     1 
ATOM   9870  C  CB    . PRO B 1 538 ? 118.107 148.131 181.380 1.00 39.36 ?  538 PRO B CB    1 
ATOM   9871  C  CG    . PRO B 1 538 ? 119.175 149.124 181.054 1.00 35.26 ?  538 PRO B CG    1 
ATOM   9872  C  CD    . PRO B 1 538 ? 118.485 150.444 180.961 1.00 36.12 ?  538 PRO B CD    1 
ATOM   9873  N  N     . LYS B 1 539 ? 114.750 147.575 181.235 1.00 41.89 ?  539 LYS B N     1 
ATOM   9874  C  CA    . LYS B 1 539 ? 113.572 147.258 182.032 1.00 41.12 ?  539 LYS B CA    1 
ATOM   9875  C  C     . LYS B 1 539 ? 113.840 146.187 183.079 1.00 45.49 ?  539 LYS B C     1 
ATOM   9876  O  O     . LYS B 1 539 ? 112.983 145.955 183.938 1.00 47.07 ?  539 LYS B O     1 
ATOM   9877  C  CB    . LYS B 1 539 ? 112.423 146.806 181.124 1.00 42.61 ?  539 LYS B CB    1 
ATOM   9878  C  CG    . LYS B 1 539 ? 111.953 147.863 180.139 1.00 42.38 ?  539 LYS B CG    1 
ATOM   9879  C  CD    . LYS B 1 539 ? 111.901 149.238 180.784 1.00 47.31 ?  539 LYS B CD    1 
ATOM   9880  C  CE    . LYS B 1 539 ? 111.953 150.344 179.739 1.00 46.28 ?  539 LYS B CE    1 
ATOM   9881  N  NZ    . LYS B 1 539 ? 113.021 150.111 178.728 1.00 46.35 1  539 LYS B NZ    1 
ATOM   9882  N  N     . TYR B 1 540 ? 115.000 145.540 183.030 1.00 46.15 ?  540 TYR B N     1 
ATOM   9883  C  CA    . TYR B 1 540 ? 115.385 144.519 183.992 1.00 41.44 ?  540 TYR B CA    1 
ATOM   9884  C  C     . TYR B 1 540 ? 116.502 145.058 184.871 1.00 43.48 ?  540 TYR B C     1 
ATOM   9885  O  O     . TYR B 1 540 ? 117.448 145.674 184.369 1.00 45.99 ?  540 TYR B O     1 
ATOM   9886  C  CB    . TYR B 1 540 ? 115.840 143.242 183.282 1.00 41.48 ?  540 TYR B CB    1 
ATOM   9887  C  CG    . TYR B 1 540 ? 114.752 142.566 182.485 1.00 43.98 ?  540 TYR B CG    1 
ATOM   9888  C  CD1   . TYR B 1 540 ? 113.873 141.679 183.089 1.00 45.96 ?  540 TYR B CD1   1 
ATOM   9889  C  CD2   . TYR B 1 540 ? 114.602 142.815 181.128 1.00 42.31 ?  540 TYR B CD2   1 
ATOM   9890  C  CE1   . TYR B 1 540 ? 112.876 141.058 182.365 1.00 43.72 ?  540 TYR B CE1   1 
ATOM   9891  C  CE2   . TYR B 1 540 ? 113.608 142.200 180.396 1.00 44.37 ?  540 TYR B CE2   1 
ATOM   9892  C  CZ    . TYR B 1 540 ? 112.747 141.322 181.019 1.00 45.46 ?  540 TYR B CZ    1 
ATOM   9893  O  OH    . TYR B 1 540 ? 111.755 140.706 180.294 1.00 43.31 ?  540 TYR B OH    1 
ATOM   9894  N  N     . GLU B 1 541 ? 116.388 144.830 186.180 1.00 48.82 ?  541 GLU B N     1 
ATOM   9895  C  CA    . GLU B 1 541 ? 117.418 145.302 187.098 1.00 48.21 ?  541 GLU B CA    1 
ATOM   9896  C  C     . GLU B 1 541 ? 118.774 144.697 186.759 1.00 46.27 ?  541 GLU B C     1 
ATOM   9897  O  O     . GLU B 1 541 ? 119.807 145.368 186.868 1.00 44.50 ?  541 GLU B O     1 
ATOM   9898  C  CB    . GLU B 1 541 ? 117.029 144.976 188.539 1.00 47.31 ?  541 GLU B CB    1 
ATOM   9899  C  CG    . GLU B 1 541 ? 118.211 144.844 189.484 1.00 48.41 ?  541 GLU B CG    1 
ATOM   9900  C  CD    . GLU B 1 541 ? 118.423 146.088 190.324 1.00 52.24 ?  541 GLU B CD    1 
ATOM   9901  O  OE1   . GLU B 1 541 ? 117.738 147.100 190.070 1.00 50.96 ?  541 GLU B OE1   1 
ATOM   9902  O  OE2   . GLU B 1 541 ? 119.275 146.054 191.236 1.00 51.97 -1 541 GLU B OE2   1 
ATOM   9903  N  N     . LYS B 1 542 ? 118.791 143.428 186.346 1.00 45.82 ?  542 LYS B N     1 
ATOM   9904  C  CA    . LYS B 1 542 ? 120.052 142.787 185.990 1.00 45.19 ?  542 LYS B CA    1 
ATOM   9905  C  C     . LYS B 1 542 ? 120.720 143.495 184.818 1.00 46.86 ?  542 LYS B C     1 
ATOM   9906  O  O     . LYS B 1 542 ? 121.931 143.741 184.840 1.00 45.85 ?  542 LYS B O     1 
ATOM   9907  C  CB    . LYS B 1 542 ? 119.814 141.313 185.666 1.00 43.78 ?  542 LYS B CB    1 
ATOM   9908  C  CG    . LYS B 1 542 ? 120.997 140.620 185.013 1.00 45.43 ?  542 LYS B CG    1 
ATOM   9909  C  CD    . LYS B 1 542 ? 120.738 139.132 184.849 1.00 43.49 ?  542 LYS B CD    1 
ATOM   9910  C  CE    . LYS B 1 542 ? 121.925 138.433 184.208 1.00 44.77 ?  542 LYS B CE    1 
ATOM   9911  N  NZ    . LYS B 1 542 ? 123.197 138.738 184.919 1.00 44.10 1  542 LYS B NZ    1 
ATOM   9912  N  N     . ILE B 1 543 ? 119.947 143.831 183.783 1.00 40.46 ?  543 ILE B N     1 
ATOM   9913  C  CA    . ILE B 1 543 ? 120.508 144.554 182.646 1.00 38.64 ?  543 ILE B CA    1 
ATOM   9914  C  C     . ILE B 1 543 ? 120.883 145.974 183.050 1.00 39.44 ?  543 ILE B C     1 
ATOM   9915  O  O     . ILE B 1 543 ? 121.932 146.492 182.648 1.00 39.86 ?  543 ILE B O     1 
ATOM   9916  C  CB    . ILE B 1 543 ? 119.524 144.544 181.461 1.00 41.51 ?  543 ILE B CB    1 
ATOM   9917  C  CG1   . ILE B 1 543 ? 119.126 143.109 181.108 1.00 40.39 ?  543 ILE B CG1   1 
ATOM   9918  C  CG2   . ILE B 1 543 ? 120.137 145.239 180.255 1.00 37.78 ?  543 ILE B CG2   1 
ATOM   9919  C  CD1   . ILE B 1 543 ? 120.298 142.171 180.948 1.00 36.40 ?  543 ILE B CD1   1 
ATOM   9920  N  N     . ALA B 1 544 ? 120.036 146.627 183.850 1.00 42.33 ?  544 ALA B N     1 
ATOM   9921  C  CA    . ALA B 1 544 ? 120.339 147.982 184.296 1.00 41.15 ?  544 ALA B CA    1 
ATOM   9922  C  C     . ALA B 1 544 ? 121.644 148.035 185.076 1.00 44.37 ?  544 ALA B C     1 
ATOM   9923  O  O     . ALA B 1 544 ? 122.365 149.038 185.012 1.00 48.94 ?  544 ALA B O     1 
ATOM   9924  C  CB    . ALA B 1 544 ? 119.188 148.525 185.145 1.00 42.19 ?  544 ALA B CB    1 
ATOM   9925  N  N     . ASN B 1 545 ? 121.966 146.974 185.819 1.00 44.48 ?  545 ASN B N     1 
ATOM   9926  C  CA    . ASN B 1 545 ? 123.235 146.933 186.535 1.00 46.86 ?  545 ASN B CA    1 
ATOM   9927  C  C     . ASN B 1 545 ? 124.415 146.845 185.576 1.00 46.16 ?  545 ASN B C     1 
ATOM   9928  O  O     . ASN B 1 545 ? 125.484 147.396 185.860 1.00 45.80 ?  545 ASN B O     1 
ATOM   9929  C  CB    . ASN B 1 545 ? 123.254 145.754 187.508 1.00 46.95 ?  545 ASN B CB    1 
ATOM   9930  C  CG    . ASN B 1 545 ? 122.302 145.945 188.671 1.00 48.81 ?  545 ASN B CG    1 
ATOM   9931  O  OD1   . ASN B 1 545 ? 121.827 147.053 188.924 1.00 47.23 ?  545 ASN B OD1   1 
ATOM   9932  N  ND2   . ASN B 1 545 ? 122.018 144.865 189.386 1.00 47.44 ?  545 ASN B ND2   1 
ATOM   9933  N  N     . LEU B 1 546 ? 124.244 146.156 184.445 1.00 44.26 ?  546 LEU B N     1 
ATOM   9934  C  CA    . LEU B 1 546 ? 125.326 146.048 183.472 1.00 40.06 ?  546 LEU B CA    1 
ATOM   9935  C  C     . LEU B 1 546 ? 125.792 147.415 182.993 1.00 40.00 ?  546 LEU B C     1 
ATOM   9936  O  O     . LEU B 1 546 ? 126.951 147.569 182.593 1.00 46.59 ?  546 LEU B O     1 
ATOM   9937  C  CB    . LEU B 1 546 ? 124.879 145.198 182.283 1.00 40.36 ?  546 LEU B CB    1 
ATOM   9938  C  CG    . LEU B 1 546 ? 124.633 143.711 182.540 1.00 41.74 ?  546 LEU B CG    1 
ATOM   9939  C  CD1   . LEU B 1 546 ? 124.121 143.034 181.280 1.00 39.22 ?  546 LEU B CD1   1 
ATOM   9940  C  CD2   . LEU B 1 546 ? 125.899 143.035 183.036 1.00 39.32 ?  546 LEU B CD2   1 
ATOM   9941  N  N     . PHE B 1 547 ? 124.912 148.414 183.022 1.00 39.64 ?  547 PHE B N     1 
ATOM   9942  C  CA    . PHE B 1 547 ? 125.231 149.756 182.561 1.00 39.96 ?  547 PHE B CA    1 
ATOM   9943  C  C     . PHE B 1 547 ? 125.644 150.686 183.694 1.00 41.09 ?  547 PHE B C     1 
ATOM   9944  O  O     . PHE B 1 547 ? 125.752 151.896 183.479 1.00 43.01 ?  547 PHE B O     1 
ATOM   9945  C  CB    . PHE B 1 547 ? 124.040 150.352 181.808 1.00 36.97 ?  547 PHE B CB    1 
ATOM   9946  C  CG    . PHE B 1 547 ? 123.787 149.714 180.472 1.00 39.61 ?  547 PHE B CG    1 
ATOM   9947  C  CD1   . PHE B 1 547 ? 124.410 150.191 179.333 1.00 37.89 ?  547 PHE B CD1   1 
ATOM   9948  C  CD2   . PHE B 1 547 ? 122.925 148.637 180.358 1.00 35.61 ?  547 PHE B CD2   1 
ATOM   9949  C  CE1   . PHE B 1 547 ? 124.179 149.606 178.104 1.00 35.86 ?  547 PHE B CE1   1 
ATOM   9950  C  CE2   . PHE B 1 547 ? 122.690 148.050 179.132 1.00 34.78 ?  547 PHE B CE2   1 
ATOM   9951  C  CZ    . PHE B 1 547 ? 123.317 148.535 178.004 1.00 37.61 ?  547 PHE B CZ    1 
ATOM   9952  N  N     . GLU B 1 548 ? 125.869 150.152 184.893 1.00 46.99 ?  548 GLU B N     1 
ATOM   9953  C  CA    . GLU B 1 548 ? 126.313 150.982 186.004 1.00 47.86 ?  548 GLU B CA    1 
ATOM   9954  C  C     . GLU B 1 548 ? 127.626 151.672 185.656 1.00 49.17 ?  548 GLU B C     1 
ATOM   9955  O  O     . GLU B 1 548 ? 128.528 151.071 185.068 1.00 49.27 ?  548 GLU B O     1 
ATOM   9956  C  CB    . GLU B 1 548 ? 126.478 150.137 187.268 1.00 45.92 ?  548 GLU B CB    1 
ATOM   9957  C  CG    . GLU B 1 548 ? 125.806 150.726 188.496 1.00 49.22 ?  548 GLU B CG    1 
ATOM   9958  C  CD    . GLU B 1 548 ? 124.345 151.049 188.261 1.00 52.10 ?  548 GLU B CD    1 
ATOM   9959  O  OE1   . GLU B 1 548 ? 123.527 150.107 188.211 1.00 51.58 ?  548 GLU B OE1   1 
ATOM   9960  O  OE2   . GLU B 1 548 ? 124.011 152.245 188.127 1.00 50.86 -1 548 GLU B OE2   1 
ATOM   9961  N  N     . GLY B 1 549 ? 127.730 152.945 186.028 1.00 47.05 ?  549 GLY B N     1 
ATOM   9962  C  CA    . GLY B 1 549 ? 128.870 153.753 185.656 1.00 45.36 ?  549 GLY B CA    1 
ATOM   9963  C  C     . GLY B 1 549 ? 128.806 154.332 184.262 1.00 48.67 ?  549 GLY B C     1 
ATOM   9964  O  O     . GLY B 1 549 ? 129.763 154.994 183.839 1.00 50.81 ?  549 GLY B O     1 
ATOM   9965  N  N     . MET B 1 550 ? 127.715 154.107 183.536 1.00 43.00 ?  550 MET B N     1 
ATOM   9966  C  CA    . MET B 1 550 ? 127.538 154.613 182.182 1.00 41.17 ?  550 MET B CA    1 
ATOM   9967  C  C     . MET B 1 550 ? 126.213 155.356 182.112 1.00 42.60 ?  550 MET B C     1 
ATOM   9968  O  O     . MET B 1 550 ? 125.191 154.851 182.588 1.00 46.77 ?  550 MET B O     1 
ATOM   9969  C  CB    . MET B 1 550 ? 127.563 153.474 181.160 1.00 42.48 ?  550 MET B CB    1 
ATOM   9970  C  CG    . MET B 1 550 ? 128.513 153.694 180.000 1.00 44.18 ?  550 MET B CG    1 
ATOM   9971  S  SD    . MET B 1 550 ? 128.499 152.315 178.839 1.00 54.77 ?  550 MET B SD    1 
ATOM   9972  C  CE    . MET B 1 550 ? 128.303 150.931 179.956 1.00 42.26 ?  550 MET B CE    1 
ATOM   9973  N  N     . HIS B 1 551 ? 126.233 156.548 181.526 1.00 39.41 ?  551 HIS B N     1 
ATOM   9974  C  CA    . HIS B 1 551 ? 125.020 157.347 181.398 1.00 39.36 ?  551 HIS B CA    1 
ATOM   9975  C  C     . HIS B 1 551 ? 124.188 156.829 180.232 1.00 40.81 ?  551 HIS B C     1 
ATOM   9976  O  O     . HIS B 1 551 ? 124.665 156.779 179.093 1.00 38.65 ?  551 HIS B O     1 
ATOM   9977  C  CB    . HIS B 1 551 ? 125.369 158.819 181.197 1.00 41.90 ?  551 HIS B CB    1 
ATOM   9978  C  CG    . HIS B 1 551 ? 124.184 159.679 180.889 1.00 44.64 ?  551 HIS B CG    1 
ATOM   9979  N  ND1   . HIS B 1 551 ? 123.144 159.856 181.775 1.00 43.07 ?  551 HIS B ND1   1 
ATOM   9980  C  CD2   . HIS B 1 551 ? 123.871 160.408 179.792 1.00 44.02 ?  551 HIS B CD2   1 
ATOM   9981  C  CE1   . HIS B 1 551 ? 122.242 160.658 181.238 1.00 44.18 ?  551 HIS B CE1   1 
ATOM   9982  N  NE2   . HIS B 1 551 ? 122.660 161.008 180.035 1.00 45.73 ?  551 HIS B NE2   1 
ATOM   9983  N  N     . ILE B 1 552 ? 122.948 156.446 180.515 1.00 38.73 ?  552 ILE B N     1 
ATOM   9984  C  CA    . ILE B 1 552 ? 122.020 155.973 179.495 1.00 38.50 ?  552 ILE B CA    1 
ATOM   9985  C  C     . ILE B 1 552 ? 121.197 157.167 179.020 1.00 35.56 ?  552 ILE B C     1 
ATOM   9986  O  O     . ILE B 1 552 ? 120.470 157.760 179.832 1.00 40.60 ?  552 ILE B O     1 
ATOM   9987  C  CB    . ILE B 1 552 ? 121.112 154.861 180.031 1.00 38.77 ?  552 ILE B CB    1 
ATOM   9988  C  CG1   . ILE B 1 552 ? 121.951 153.697 180.562 1.00 34.67 ?  552 ILE B CG1   1 
ATOM   9989  C  CG2   . ILE B 1 552 ? 120.157 154.383 178.947 1.00 37.31 ?  552 ILE B CG2   1 
ATOM   9990  C  CD1   . ILE B 1 552 ? 121.130 152.556 181.113 1.00 35.87 ?  552 ILE B CD1   1 
ATOM   9991  N  N     . PRO B 1 553 ? 121.283 157.553 177.749 1.00 38.72 ?  553 PRO B N     1 
ATOM   9992  C  CA    . PRO B 1 553 ? 120.531 158.724 177.287 1.00 36.71 ?  553 PRO B CA    1 
ATOM   9993  C  C     . PRO B 1 553 ? 119.039 158.560 177.527 1.00 36.88 ?  553 PRO B C     1 
ATOM   9994  O  O     . PRO B 1 553 ? 118.461 157.498 177.288 1.00 43.43 ?  553 PRO B O     1 
ATOM   9995  C  CB    . PRO B 1 553 ? 120.859 158.784 175.791 1.00 34.32 ?  553 PRO B CB    1 
ATOM   9996  C  CG    . PRO B 1 553 ? 122.171 158.088 175.669 1.00 30.49 ?  553 PRO B CG    1 
ATOM   9997  C  CD    . PRO B 1 553 ? 122.144 156.995 176.693 1.00 32.56 ?  553 PRO B CD    1 
ATOM   9998  N  N     . THR B 1 554 ? 118.415 159.634 177.998 1.00 37.89 ?  554 THR B N     1 
ATOM   9999  C  CA    . THR B 1 554 ? 116.992 159.659 178.285 1.00 37.00 ?  554 THR B CA    1 
ATOM   10000 C  C     . THR B 1 554 ? 116.245 160.367 177.159 1.00 37.88 ?  554 THR B C     1 
ATOM   10001 O  O     . THR B 1 554 ? 116.814 160.731 176.128 1.00 34.90 ?  554 THR B O     1 
ATOM   10002 C  CB    . THR B 1 554 ? 116.731 160.341 179.631 1.00 35.52 ?  554 THR B CB    1 
ATOM   10003 O  OG1   . THR B 1 554 ? 116.575 161.751 179.429 1.00 41.88 ?  554 THR B OG1   1 
ATOM   10004 C  CG2   . THR B 1 554 ? 117.889 160.101 180.582 1.00 36.34 ?  554 THR B CG2   1 
ATOM   10005 N  N     . THR B 1 555 ? 114.940 160.562 177.362 1.00 39.27 ?  555 THR B N     1 
ATOM   10006 C  CA    . THR B 1 555 ? 114.154 161.318 176.393 1.00 35.50 ?  555 THR B CA    1 
ATOM   10007 C  C     . THR B 1 555 ? 114.628 162.764 176.318 1.00 38.65 ?  555 THR B C     1 
ATOM   10008 O  O     . THR B 1 555 ? 114.639 163.365 175.238 1.00 40.90 ?  555 THR B O     1 
ATOM   10009 C  CB    . THR B 1 555 ? 112.669 161.259 176.749 1.00 39.08 ?  555 THR B CB    1 
ATOM   10010 O  OG1   . THR B 1 555 ? 112.510 161.373 178.169 1.00 46.63 ?  555 THR B OG1   1 
ATOM   10011 C  CG2   . THR B 1 555 ? 112.062 159.947 176.278 1.00 36.88 ?  555 THR B CG2   1 
ATOM   10012 N  N     . GLU B 1 556 ? 115.010 163.344 177.457 1.00 36.28 ?  556 GLU B N     1 
ATOM   10013 C  CA    . GLU B 1 556 ? 115.557 164.697 177.450 1.00 37.65 ?  556 GLU B CA    1 
ATOM   10014 C  C     . GLU B 1 556 ? 116.858 164.758 176.659 1.00 38.58 ?  556 GLU B C     1 
ATOM   10015 O  O     . GLU B 1 556 ? 117.087 165.704 175.894 1.00 41.85 ?  556 GLU B O     1 
ATOM   10016 C  CB    . GLU B 1 556 ? 115.776 165.183 178.882 1.00 40.88 ?  556 GLU B CB    1 
ATOM   10017 C  CG    . GLU B 1 556 ? 114.513 165.658 179.576 1.00 40.96 ?  556 GLU B CG    1 
ATOM   10018 C  CD    . GLU B 1 556 ? 113.463 166.153 178.600 1.00 45.78 ?  556 GLU B CD    1 
ATOM   10019 O  OE1   . GLU B 1 556 ? 113.608 167.284 178.094 1.00 45.57 ?  556 GLU B OE1   1 
ATOM   10020 O  OE2   . GLU B 1 556 ? 112.493 165.410 178.342 1.00 44.51 -1 556 GLU B OE2   1 
ATOM   10021 N  N     . ASP B 1 557 ? 117.726 163.761 176.836 1.00 38.22 ?  557 ASP B N     1 
ATOM   10022 C  CA    . ASP B 1 557 ? 118.963 163.717 176.064 1.00 34.24 ?  557 ASP B CA    1 
ATOM   10023 C  C     . ASP B 1 557 ? 118.672 163.619 174.574 1.00 35.60 ?  557 ASP B C     1 
ATOM   10024 O  O     . ASP B 1 557 ? 119.334 164.271 173.759 1.00 38.51 ?  557 ASP B O     1 
ATOM   10025 C  CB    . ASP B 1 557 ? 119.827 162.542 176.521 1.00 34.88 ?  557 ASP B CB    1 
ATOM   10026 C  CG    . ASP B 1 557 ? 120.244 162.656 177.971 1.00 41.94 ?  557 ASP B CG    1 
ATOM   10027 O  OD1   . ASP B 1 557 ? 120.737 163.732 178.367 1.00 42.98 ?  557 ASP B OD1   1 
ATOM   10028 O  OD2   . ASP B 1 557 ? 120.079 161.668 178.718 1.00 42.56 -1 557 ASP B OD2   1 
ATOM   10029 N  N     . TRP B 1 558 ? 117.681 162.811 174.198 1.00 29.20 ?  558 TRP B N     1 
ATOM   10030 C  CA    . TRP B 1 558 ? 117.337 162.676 172.788 1.00 24.56 ?  558 TRP B CA    1 
ATOM   10031 C  C     . TRP B 1 558 ? 116.734 163.961 172.235 1.00 31.45 ?  558 TRP B C     1 
ATOM   10032 O  O     . TRP B 1 558 ? 116.977 164.314 171.078 1.00 36.12 ?  558 TRP B O     1 
ATOM   10033 C  CB    . TRP B 1 558 ? 116.387 161.499 172.593 1.00 29.12 ?  558 TRP B CB    1 
ATOM   10034 C  CG    . TRP B 1 558 ? 117.102 160.197 172.457 1.00 23.94 ?  558 TRP B CG    1 
ATOM   10035 C  CD1   . TRP B 1 558 ? 117.189 159.210 173.390 1.00 26.64 ?  558 TRP B CD1   1 
ATOM   10036 C  CD2   . TRP B 1 558 ? 117.841 159.742 171.319 1.00 26.13 ?  558 TRP B CD2   1 
ATOM   10037 N  NE1   . TRP B 1 558 ? 117.933 158.165 172.904 1.00 28.23 ?  558 TRP B NE1   1 
ATOM   10038 C  CE2   . TRP B 1 558 ? 118.344 158.466 171.633 1.00 24.27 ?  558 TRP B CE2   1 
ATOM   10039 C  CE3   . TRP B 1 558 ? 118.121 160.287 170.063 1.00 29.00 ?  558 TRP B CE3   1 
ATOM   10040 C  CZ2   . TRP B 1 558 ? 119.112 157.726 170.738 1.00 22.98 ?  558 TRP B CZ2   1 
ATOM   10041 C  CZ3   . TRP B 1 558 ? 118.885 159.552 169.177 1.00 21.22 ?  558 TRP B CZ3   1 
ATOM   10042 C  CH2   . TRP B 1 558 ? 119.371 158.286 169.518 1.00 17.09 ?  558 TRP B CH2   1 
ATOM   10043 N  N     . LYS B 1 559 ? 115.945 164.676 173.039 1.00 36.13 ?  559 LYS B N     1 
ATOM   10044 C  CA    . LYS B 1 559 ? 115.429 165.969 172.598 1.00 34.21 ?  559 LYS B CA    1 
ATOM   10045 C  C     . LYS B 1 559 ? 116.560 166.968 172.391 1.00 36.21 ?  559 LYS B C     1 
ATOM   10046 O  O     . LYS B 1 559 ? 116.563 167.730 171.415 1.00 37.20 ?  559 LYS B O     1 
ATOM   10047 C  CB    . LYS B 1 559 ? 114.421 166.510 173.611 1.00 34.94 ?  559 LYS B CB    1 
ATOM   10048 C  CG    . LYS B 1 559 ? 113.138 165.707 173.712 1.00 38.21 ?  559 LYS B CG    1 
ATOM   10049 C  CD    . LYS B 1 559 ? 112.275 166.212 174.854 1.00 36.54 ?  559 LYS B CD    1 
ATOM   10050 C  CE    . LYS B 1 559 ? 111.309 165.144 175.335 1.00 37.80 ?  559 LYS B CE    1 
ATOM   10051 N  NZ    . LYS B 1 559 ? 110.823 165.425 176.714 1.00 39.75 1  559 LYS B NZ    1 
ATOM   10052 N  N     . LYS B 1 560 ? 117.529 166.984 173.308 1.00 33.95 ?  560 LYS B N     1 
ATOM   10053 C  CA    . LYS B 1 560 ? 118.677 167.870 173.148 1.00 31.38 ?  560 LYS B CA    1 
ATOM   10054 C  C     . LYS B 1 560 ? 119.475 167.513 171.902 1.00 34.63 ?  560 LYS B C     1 
ATOM   10055 O  O     . LYS B 1 560 ? 119.921 168.400 171.167 1.00 37.58 ?  560 LYS B O     1 
ATOM   10056 C  CB    . LYS B 1 560 ? 119.561 167.815 174.392 1.00 33.86 ?  560 LYS B CB    1 
ATOM   10057 C  CG    . LYS B 1 560 ? 119.038 168.639 175.555 1.00 34.94 ?  560 LYS B CG    1 
ATOM   10058 C  CD    . LYS B 1 560 ? 119.996 168.603 176.732 1.00 39.27 ?  560 LYS B CD    1 
ATOM   10059 C  CE    . LYS B 1 560 ? 119.363 169.199 177.977 1.00 38.99 ?  560 LYS B CE    1 
ATOM   10060 N  NZ    . LYS B 1 560 ? 118.057 168.559 178.301 1.00 40.71 1  560 LYS B NZ    1 
ATOM   10061 N  N     . LEU B 1 561 ? 119.667 166.217 171.648 1.00 32.21 ?  561 LEU B N     1 
ATOM   10062 C  CA    . LEU B 1 561 ? 120.371 165.795 170.440 1.00 27.38 ?  561 LEU B CA    1 
ATOM   10063 C  C     . LEU B 1 561 ? 119.596 166.177 169.187 1.00 29.09 ?  561 LEU B C     1 
ATOM   10064 O  O     . LEU B 1 561 ? 120.191 166.572 168.180 1.00 34.43 ?  561 LEU B O     1 
ATOM   10065 C  CB    . LEU B 1 561 ? 120.625 164.288 170.476 1.00 28.19 ?  561 LEU B CB    1 
ATOM   10066 C  CG    . LEU B 1 561 ? 121.323 163.701 169.246 1.00 27.51 ?  561 LEU B CG    1 
ATOM   10067 C  CD1   . LEU B 1 561 ? 122.682 164.351 169.038 1.00 24.75 ?  561 LEU B CD1   1 
ATOM   10068 C  CD2   . LEU B 1 561 ? 121.462 162.193 169.372 1.00 25.79 ?  561 LEU B CD2   1 
ATOM   10069 N  N     . LYS B 1 562 ? 118.270 166.051 169.224 1.00 28.65 ?  562 LYS B N     1 
ATOM   10070 C  CA    . LYS B 1 562 ? 117.445 166.457 168.092 1.00 32.32 ?  562 LYS B CA    1 
ATOM   10071 C  C     . LYS B 1 562 ? 117.598 167.946 167.814 1.00 30.88 ?  562 LYS B C     1 
ATOM   10072 O  O     . LYS B 1 562 ? 117.755 168.363 166.660 1.00 35.23 ?  562 LYS B O     1 
ATOM   10073 C  CB    . LYS B 1 562 ? 115.985 166.098 168.370 1.00 27.08 ?  562 LYS B CB    1 
ATOM   10074 C  CG    . LYS B 1 562 ? 114.986 166.648 167.372 1.00 32.00 ?  562 LYS B CG    1 
ATOM   10075 C  CD    . LYS B 1 562 ? 113.569 166.440 167.876 1.00 30.74 ?  562 LYS B CD    1 
ATOM   10076 C  CE    . LYS B 1 562 ? 112.543 167.008 166.915 1.00 32.43 ?  562 LYS B CE    1 
ATOM   10077 N  NZ    . LYS B 1 562 ? 111.180 166.479 167.191 1.00 32.80 1  562 LYS B NZ    1 
ATOM   10078 N  N     . ALA B 1 563 ? 117.566 168.765 168.867 1.00 27.19 ?  563 ALA B N     1 
ATOM   10079 C  CA    . ALA B 1 563 ? 117.765 170.200 168.691 1.00 32.52 ?  563 ALA B CA    1 
ATOM   10080 C  C     . ALA B 1 563 ? 119.158 170.500 168.150 1.00 31.99 ?  563 ALA B C     1 
ATOM   10081 O  O     . ALA B 1 563 ? 119.323 171.353 167.270 1.00 36.24 ?  563 ALA B O     1 
ATOM   10082 C  CB    . ALA B 1 563 ? 117.532 170.927 170.015 1.00 33.39 ?  563 ALA B CB    1 
ATOM   10083 N  N     . PHE B 1 564 ? 120.172 169.801 168.662 1.00 33.62 ?  564 PHE B N     1 
ATOM   10084 C  CA    . PHE B 1 564 ? 121.537 170.010 168.195 1.00 27.88 ?  564 PHE B CA    1 
ATOM   10085 C  C     . PHE B 1 564 ? 121.672 169.659 166.718 1.00 31.91 ?  564 PHE B C     1 
ATOM   10086 O  O     . PHE B 1 564 ? 122.334 170.376 165.959 1.00 36.35 ?  564 PHE B O     1 
ATOM   10087 C  CB    . PHE B 1 564 ? 122.501 169.181 169.042 1.00 28.98 ?  564 PHE B CB    1 
ATOM   10088 C  CG    . PHE B 1 564 ? 123.948 169.489 168.799 1.00 32.85 ?  564 PHE B CG    1 
ATOM   10089 C  CD1   . PHE B 1 564 ? 124.561 170.552 169.440 1.00 32.39 ?  564 PHE B CD1   1 
ATOM   10090 C  CD2   . PHE B 1 564 ? 124.699 168.711 167.935 1.00 34.80 ?  564 PHE B CD2   1 
ATOM   10091 C  CE1   . PHE B 1 564 ? 125.893 170.834 169.219 1.00 33.94 ?  564 PHE B CE1   1 
ATOM   10092 C  CE2   . PHE B 1 564 ? 126.031 168.990 167.711 1.00 32.00 ?  564 PHE B CE2   1 
ATOM   10093 C  CZ    . PHE B 1 564 ? 126.629 170.053 168.353 1.00 34.70 ?  564 PHE B CZ    1 
ATOM   10094 N  N     . VAL B 1 565 ? 121.055 168.556 166.294 1.00 33.07 ?  565 VAL B N     1 
ATOM   10095 C  CA    . VAL B 1 565 ? 121.110 168.161 164.891 1.00 29.10 ?  565 VAL B CA    1 
ATOM   10096 C  C     . VAL B 1 565 ? 120.373 169.171 164.024 1.00 32.80 ?  565 VAL B C     1 
ATOM   10097 O  O     . VAL B 1 565 ? 120.847 169.543 162.944 1.00 39.06 ?  565 VAL B O     1 
ATOM   10098 C  CB    . VAL B 1 565 ? 120.545 166.741 164.714 1.00 30.01 ?  565 VAL B CB    1 
ATOM   10099 C  CG1   . VAL B 1 565 ? 120.202 166.484 163.257 1.00 28.45 ?  565 VAL B CG1   1 
ATOM   10100 C  CG2   . VAL B 1 565 ? 121.539 165.713 165.218 1.00 31.49 ?  565 VAL B CG2   1 
ATOM   10101 N  N     . ALA B 1 566 ? 119.205 169.633 164.476 1.00 33.21 ?  566 ALA B N     1 
ATOM   10102 C  CA    . ALA B 1 566 ? 118.479 170.647 163.722 1.00 32.18 ?  566 ALA B CA    1 
ATOM   10103 C  C     . ALA B 1 566 ? 119.293 171.924 163.584 1.00 37.45 ?  566 ALA B C     1 
ATOM   10104 O  O     . ALA B 1 566 ? 119.211 172.605 162.556 1.00 43.18 ?  566 ALA B O     1 
ATOM   10105 C  CB    . ALA B 1 566 ? 117.136 170.941 164.390 1.00 31.25 ?  566 ALA B CB    1 
ATOM   10106 N  N     . GLU B 1 567 ? 120.075 172.269 164.606 1.00 37.46 ?  567 GLU B N     1 
ATOM   10107 C  CA    . GLU B 1 567 ? 120.904 173.468 164.540 1.00 33.68 ?  567 GLU B CA    1 
ATOM   10108 C  C     . GLU B 1 567 ? 122.115 173.279 163.633 1.00 37.71 ?  567 GLU B C     1 
ATOM   10109 O  O     . GLU B 1 567 ? 122.473 174.189 162.878 1.00 43.31 ?  567 GLU B O     1 
ATOM   10110 C  CB    . GLU B 1 567 ? 121.352 173.871 165.945 1.00 36.04 ?  567 GLU B CB    1 
ATOM   10111 C  CG    . GLU B 1 567 ? 122.572 174.776 165.974 1.00 40.69 ?  567 GLU B CG    1 
ATOM   10112 C  CD    . GLU B 1 567 ? 122.210 176.248 165.988 1.00 46.45 ?  567 GLU B CD    1 
ATOM   10113 O  OE1   . GLU B 1 567 ? 121.327 176.638 166.779 1.00 45.30 ?  567 GLU B OE1   1 
ATOM   10114 O  OE2   . GLU B 1 567 ? 122.813 177.016 165.209 1.00 45.51 -1 567 GLU B OE2   1 
ATOM   10115 N  N     . HIS B 1 568 ? 122.759 172.112 163.689 1.00 37.50 ?  568 HIS B N     1 
ATOM   10116 C  CA    . HIS B 1 568 ? 124.028 171.904 163.007 1.00 33.92 ?  568 HIS B CA    1 
ATOM   10117 C  C     . HIS B 1 568 ? 123.971 170.893 161.872 1.00 32.05 ?  568 HIS B C     1 
ATOM   10118 O  O     . HIS B 1 568 ? 124.854 170.913 161.010 1.00 38.68 ?  568 HIS B O     1 
ATOM   10119 C  CB    . HIS B 1 568 ? 125.101 171.456 164.010 1.00 34.66 ?  568 HIS B CB    1 
ATOM   10120 C  CG    . HIS B 1 568 ? 125.307 172.417 165.136 1.00 36.90 ?  568 HIS B CG    1 
ATOM   10121 N  ND1   . HIS B 1 568 ? 125.954 173.623 164.976 1.00 34.79 ?  568 HIS B ND1   1 
ATOM   10122 C  CD2   . HIS B 1 568 ? 124.945 172.354 166.439 1.00 37.62 ?  568 HIS B CD2   1 
ATOM   10123 C  CE1   . HIS B 1 568 ? 125.985 174.260 166.133 1.00 36.68 ?  568 HIS B CE1   1 
ATOM   10124 N  NE2   . HIS B 1 568 ? 125.379 173.512 167.037 1.00 38.18 ?  568 HIS B NE2   1 
ATOM   10125 N  N     . GLY B 1 569 ? 122.972 170.023 161.844 1.00 27.67 ?  569 GLY B N     1 
ATOM   10126 C  CA    . GLY B 1 569 ? 122.885 169.020 160.805 1.00 28.71 ?  569 GLY B CA    1 
ATOM   10127 C  C     . GLY B 1 569 ? 123.691 167.778 161.117 1.00 26.28 ?  569 GLY B C     1 
ATOM   10128 O  O     . GLY B 1 569 ? 124.215 167.583 162.217 1.00 34.99 ?  569 GLY B O     1 
ATOM   10129 N  N     . MET B 1 570 ? 123.787 166.915 160.110 1.00 22.57 ?  570 MET B N     1 
ATOM   10130 C  CA    . MET B 1 570 ? 124.478 165.641 160.232 1.00 21.03 ?  570 MET B CA    1 
ATOM   10131 C  C     . MET B 1 570 ? 125.529 165.520 159.141 1.00 21.30 ?  570 MET B C     1 
ATOM   10132 O  O     . MET B 1 570 ? 125.293 165.908 157.994 1.00 27.49 ?  570 MET B O     1 
ATOM   10133 C  CB    . MET B 1 570 ? 123.500 164.463 160.145 1.00 25.90 ?  570 MET B CB    1 
ATOM   10134 C  CG    . MET B 1 570 ? 122.457 164.437 161.246 1.00 23.56 ?  570 MET B CG    1 
ATOM   10135 S  SD    . MET B 1 570 ? 122.924 163.369 162.617 1.00 37.03 ?  570 MET B SD    1 
ATOM   10136 C  CE    . MET B 1 570 ? 122.879 161.765 161.824 1.00 20.38 ?  570 MET B CE    1 
ATOM   10137 N  N     . TYR B 1 571 ? 126.690 164.977 159.506 1.00 14.87 ?  571 TYR B N     1 
ATOM   10138 C  CA    . TYR B 1 571 ? 127.763 164.789 158.539 1.00 16.84 ?  571 TYR B CA    1 
ATOM   10139 C  C     . TYR B 1 571 ? 127.586 163.521 157.713 1.00 18.26 ?  571 TYR B C     1 
ATOM   10140 O  O     . TYR B 1 571 ? 127.953 163.501 156.534 1.00 19.79 ?  571 TYR B O     1 
ATOM   10141 C  CB    . TYR B 1 571 ? 129.113 164.758 159.258 1.00 20.56 ?  571 TYR B CB    1 
ATOM   10142 C  CG    . TYR B 1 571 ? 130.303 164.851 158.332 1.00 22.30 ?  571 TYR B CG    1 
ATOM   10143 C  CD1   . TYR B 1 571 ? 130.678 166.062 157.769 1.00 23.13 ?  571 TYR B CD1   1 
ATOM   10144 C  CD2   . TYR B 1 571 ? 131.049 163.724 158.018 1.00 18.21 ?  571 TYR B CD2   1 
ATOM   10145 C  CE1   . TYR B 1 571 ? 131.765 166.149 156.923 1.00 25.01 ?  571 TYR B CE1   1 
ATOM   10146 C  CE2   . TYR B 1 571 ? 132.135 163.801 157.172 1.00 19.87 ?  571 TYR B CE2   1 
ATOM   10147 C  CZ    . TYR B 1 571 ? 132.489 165.016 156.628 1.00 26.44 ?  571 TYR B CZ    1 
ATOM   10148 O  OH    . TYR B 1 571 ? 133.572 165.098 155.785 1.00 27.94 ?  571 TYR B OH    1 
ATOM   10149 N  N     . HIS B 1 572 ? 127.027 162.467 158.299 1.00 19.64 ?  572 HIS B N     1 
ATOM   10150 C  CA    . HIS B 1 572 ? 126.911 161.170 157.648 1.00 8.22  ?  572 HIS B CA    1 
ATOM   10151 C  C     . HIS B 1 572 ? 125.458 160.900 157.289 1.00 17.00 ?  572 HIS B C     1 
ATOM   10152 O  O     . HIS B 1 572 ? 124.571 161.013 158.142 1.00 30.89 ?  572 HIS B O     1 
ATOM   10153 C  CB    . HIS B 1 572 ? 127.441 160.052 158.551 1.00 15.06 ?  572 HIS B CB    1 
ATOM   10154 C  CG    . HIS B 1 572 ? 128.787 160.337 159.138 1.00 15.57 ?  572 HIS B CG    1 
ATOM   10155 N  ND1   . HIS B 1 572 ? 128.952 161.032 160.316 1.00 14.05 ?  572 HIS B ND1   1 
ATOM   10156 C  CD2   . HIS B 1 572 ? 130.033 160.018 158.713 1.00 11.66 ?  572 HIS B CD2   1 
ATOM   10157 C  CE1   . HIS B 1 572 ? 130.240 161.130 160.591 1.00 17.53 ?  572 HIS B CE1   1 
ATOM   10158 N  NE2   . HIS B 1 572 ? 130.918 160.523 159.632 1.00 19.08 ?  572 HIS B NE2   1 
ATOM   10159 N  N     . SER B 1 573 ? 125.216 160.548 156.024 1.00 11.24 ?  573 SER B N     1 
ATOM   10160 C  CA    . SER B 1 573 ? 123.882 160.115 155.622 1.00 7.01  ?  573 SER B CA    1 
ATOM   10161 C  C     . SER B 1 573 ? 123.510 158.805 156.302 1.00 11.95 ?  573 SER B C     1 
ATOM   10162 O  O     . SER B 1 573 ? 122.355 158.605 156.693 1.00 23.89 ?  573 SER B O     1 
ATOM   10163 C  CB    . SER B 1 573 ? 123.808 159.975 154.103 1.00 17.01 ?  573 SER B CB    1 
ATOM   10164 O  OG    . SER B 1 573 ? 124.813 159.105 153.620 1.00 21.17 ?  573 SER B OG    1 
ATOM   10165 N  N     . TYR B 1 574 ? 124.478 157.903 156.443 1.00 16.52 ?  574 TYR B N     1 
ATOM   10166 C  CA    . TYR B 1 574 ? 124.292 156.625 157.110 1.00 2.93  ?  574 TYR B CA    1 
ATOM   10167 C  C     . TYR B 1 574 ? 125.488 156.381 158.014 1.00 5.83  ?  574 TYR B C     1 
ATOM   10168 O  O     . TYR B 1 574 ? 126.620 156.717 157.657 1.00 14.66 ?  574 TYR B O     1 
ATOM   10169 C  CB    . TYR B 1 574 ? 124.137 155.488 156.095 1.00 11.53 ?  574 TYR B CB    1 
ATOM   10170 C  CG    . TYR B 1 574 ? 123.059 155.750 155.073 1.00 5.70  ?  574 TYR B CG    1 
ATOM   10171 C  CD1   . TYR B 1 574 ? 121.743 155.388 155.318 1.00 8.35  ?  574 TYR B CD1   1 
ATOM   10172 C  CD2   . TYR B 1 574 ? 123.351 156.382 153.874 1.00 4.45  ?  574 TYR B CD2   1 
ATOM   10173 C  CE1   . TYR B 1 574 ? 120.754 155.635 154.392 1.00 9.82  ?  574 TYR B CE1   1 
ATOM   10174 C  CE2   . TYR B 1 574 ? 122.367 156.634 152.943 1.00 11.25 ?  574 TYR B CE2   1 
ATOM   10175 C  CZ    . TYR B 1 574 ? 121.070 156.255 153.206 1.00 9.02  ?  574 TYR B CZ    1 
ATOM   10176 O  OH    . TYR B 1 574 ? 120.084 156.501 152.282 1.00 20.05 ?  574 TYR B OH    1 
ATOM   10177 N  N     . ARG B 1 575 ? 125.236 155.808 159.186 1.00 11.93 ?  575 ARG B N     1 
ATOM   10178 C  CA    . ARG B 1 575 ? 126.277 155.656 160.194 1.00 5.22  ?  575 ARG B CA    1 
ATOM   10179 C  C     . ARG B 1 575 ? 126.495 154.222 160.646 1.00 12.80 ?  575 ARG B C     1 
ATOM   10180 O  O     . ARG B 1 575 ? 127.644 153.806 160.812 1.00 17.98 ?  575 ARG B O     1 
ATOM   10181 C  CB    . ARG B 1 575 ? 125.950 156.517 161.420 1.00 10.84 ?  575 ARG B CB    1 
ATOM   10182 C  CG    . ARG B 1 575 ? 125.943 158.010 161.158 1.00 7.13  ?  575 ARG B CG    1 
ATOM   10183 C  CD    . ARG B 1 575 ? 125.111 158.732 162.203 1.00 11.90 ?  575 ARG B CD    1 
ATOM   10184 N  NE    . ARG B 1 575 ? 123.693 158.425 162.072 1.00 18.34 ?  575 ARG B NE    1 
ATOM   10185 C  CZ    . ARG B 1 575 ? 123.015 157.639 162.895 1.00 10.55 ?  575 ARG B CZ    1 
ATOM   10186 N  NH1   . ARG B 1 575 ? 123.598 157.053 163.928 1.00 14.31 1  575 ARG B NH1   1 
ATOM   10187 N  NH2   . ARG B 1 575 ? 121.722 157.429 162.675 1.00 13.09 ?  575 ARG B NH2   1 
ATOM   10188 N  N     . LEU B 1 576 ? 125.431 153.451 160.847 1.00 21.19 ?  576 LEU B N     1 
ATOM   10189 C  CA    . LEU B 1 576 ? 125.512 152.165 161.526 1.00 8.21  ?  576 LEU B CA    1 
ATOM   10190 C  C     . LEU B 1 576 ? 125.054 151.049 160.601 1.00 8.63  ?  576 LEU B C     1 
ATOM   10191 O  O     . LEU B 1 576 ? 123.994 151.147 159.977 1.00 15.77 ?  576 LEU B O     1 
ATOM   10192 C  CB    . LEU B 1 576 ? 124.665 152.171 162.801 1.00 7.14  ?  576 LEU B CB    1 
ATOM   10193 C  CG    . LEU B 1 576 ? 124.947 153.299 163.795 1.00 13.98 ?  576 LEU B CG    1 
ATOM   10194 C  CD1   . LEU B 1 576 ? 123.973 153.252 164.957 1.00 11.13 ?  576 LEU B CD1   1 
ATOM   10195 C  CD2   . LEU B 1 576 ? 126.380 153.233 164.296 1.00 10.10 ?  576 LEU B CD2   1 
ATOM   10196 N  N     . CYS B 1 577 ? 125.857 149.990 160.521 1.00 7.75  ?  577 CYS B N     1 
ATOM   10197 C  CA    . CYS B 1 577 ? 125.475 148.771 159.821 1.00 4.24  ?  577 CYS B CA    1 
ATOM   10198 C  C     . CYS B 1 577 ? 126.284 147.625 160.408 1.00 18.34 ?  577 CYS B C     1 
ATOM   10199 O  O     . CYS B 1 577 ? 127.507 147.733 160.538 1.00 21.00 ?  577 CYS B O     1 
ATOM   10200 C  CB    . CYS B 1 577 ? 125.704 148.892 158.308 1.00 8.23  ?  577 CYS B CB    1 
ATOM   10201 S  SG    . CYS B 1 577 ? 127.403 148.618 157.747 1.00 27.90 ?  577 CYS B SG    1 
ATOM   10202 N  N     . ILE B 1 578 ? 125.604 146.544 160.772 1.00 13.66 ?  578 ILE B N     1 
ATOM   10203 C  CA    . ILE B 1 578 ? 126.230 145.408 161.439 1.00 6.85  ?  578 ILE B CA    1 
ATOM   10204 C  C     . ILE B 1 578 ? 126.582 144.383 160.368 1.00 7.36  ?  578 ILE B C     1 
ATOM   10205 O  O     . ILE B 1 578 ? 125.751 143.563 159.973 1.00 19.17 ?  578 ILE B O     1 
ATOM   10206 C  CB    . ILE B 1 578 ? 125.324 144.817 162.522 1.00 11.03 ?  578 ILE B CB    1 
ATOM   10207 C  CG1   . ILE B 1 578 ? 124.978 145.885 163.561 1.00 2.78  ?  578 ILE B CG1   1 
ATOM   10208 C  CG2   . ILE B 1 578 ? 125.998 143.625 163.187 1.00 8.01  ?  578 ILE B CG2   1 
ATOM   10209 C  CD1   . ILE B 1 578 ? 124.058 145.401 164.651 1.00 11.67 ?  578 ILE B CD1   1 
ATOM   10210 N  N     . ALA B 1 579 ? 127.824 144.431 159.896 1.00 14.16 ?  579 ALA B N     1 
ATOM   10211 C  CA    . ALA B 1 579 ? 128.322 143.485 158.914 1.00 8.68  ?  579 ALA B CA    1 
ATOM   10212 C  C     . ALA B 1 579 ? 128.714 142.170 159.581 1.00 19.94 ?  579 ALA B C     1 
ATOM   10213 O  O     . ALA B 1 579 ? 128.904 142.110 160.799 1.00 22.30 ?  579 ALA B O     1 
ATOM   10214 C  CB    . ALA B 1 579 ? 129.513 144.077 158.171 1.00 9.26  ?  579 ALA B CB    1 
ATOM   10215 N  N     . PRO B 1 580 ? 128.840 141.095 158.800 1.00 28.70 ?  580 PRO B N     1 
ATOM   10216 C  CA    . PRO B 1 580 ? 129.122 139.782 159.405 1.00 22.76 ?  580 PRO B CA    1 
ATOM   10217 C  C     . PRO B 1 580 ? 130.395 139.743 160.235 1.00 23.37 ?  580 PRO B C     1 
ATOM   10218 O  O     . PRO B 1 580 ? 130.432 139.034 161.248 1.00 33.54 ?  580 PRO B O     1 
ATOM   10219 C  CB    . PRO B 1 580 ? 129.203 138.842 158.192 1.00 21.40 ?  580 PRO B CB    1 
ATOM   10220 C  CG    . PRO B 1 580 ? 129.302 139.725 156.994 1.00 21.75 ?  580 PRO B CG    1 
ATOM   10221 C  CD    . PRO B 1 580 ? 128.638 141.008 157.346 1.00 20.65 ?  580 PRO B CD    1 
ATOM   10222 N  N     . THR B 1 581 ? 131.440 140.468 159.840 1.00 20.16 ?  581 THR B N     1 
ATOM   10223 C  CA    . THR B 1 581 ? 132.661 140.602 160.637 1.00 30.93 ?  581 THR B CA    1 
ATOM   10224 C  C     . THR B 1 581 ? 133.222 139.230 161.027 1.00 34.10 ?  581 THR B C     1 
ATOM   10225 O  O     . THR B 1 581 ? 133.348 138.874 162.199 1.00 36.38 ?  581 THR B O     1 
ATOM   10226 C  CB    . THR B 1 581 ? 132.414 141.500 161.861 1.00 36.09 ?  581 THR B CB    1 
ATOM   10227 O  OG1   . THR B 1 581 ? 133.645 142.111 162.270 1.00 43.91 ?  581 THR B OG1   1 
ATOM   10228 C  CG2   . THR B 1 581 ? 131.787 140.743 163.028 1.00 21.24 ?  581 THR B CG2   1 
ATOM   10229 N  N     . GLY B 1 582 ? 133.585 138.464 160.004 1.00 32.54 ?  582 GLY B N     1 
ATOM   10230 C  CA    . GLY B 1 582 ? 133.981 137.086 160.218 1.00 34.45 ?  582 GLY B CA    1 
ATOM   10231 C  C     . GLY B 1 582 ? 135.431 136.863 160.598 1.00 36.13 ?  582 GLY B C     1 
ATOM   10232 O  O     . GLY B 1 582 ? 135.715 136.252 161.632 1.00 38.25 ?  582 GLY B O     1 
ATOM   10233 N  N     . SER B 1 583 ? 136.360 137.350 159.774 1.00 36.88 ?  583 SER B N     1 
ATOM   10234 C  CA    . SER B 1 583 ? 137.764 136.990 159.953 1.00 37.59 ?  583 SER B CA    1 
ATOM   10235 C  C     . SER B 1 583 ? 138.359 137.628 161.203 1.00 38.38 ?  583 SER B C     1 
ATOM   10236 O  O     . SER B 1 583 ? 139.091 136.969 161.951 1.00 37.49 ?  583 SER B O     1 
ATOM   10237 C  CB    . SER B 1 583 ? 138.568 137.387 158.715 1.00 43.19 ?  583 SER B CB    1 
ATOM   10238 O  OG    . SER B 1 583 ? 138.366 136.465 157.658 1.00 44.44 ?  583 SER B OG    1 
ATOM   10239 N  N     . ILE B 1 584 ? 138.058 138.906 161.452 1.00 33.74 ?  584 ILE B N     1 
ATOM   10240 C  CA    . ILE B 1 584 ? 138.675 139.613 162.573 1.00 31.28 ?  584 ILE B CA    1 
ATOM   10241 C  C     . ILE B 1 584 ? 138.046 139.277 163.915 1.00 32.00 ?  584 ILE B C     1 
ATOM   10242 O  O     . ILE B 1 584 ? 138.513 139.779 164.944 1.00 34.92 ?  584 ILE B O     1 
ATOM   10243 C  CB    . ILE B 1 584 ? 138.621 141.140 162.373 1.00 33.45 ?  584 ILE B CB    1 
ATOM   10244 C  CG1   . ILE B 1 584 ? 137.174 141.615 162.244 1.00 33.13 ?  584 ILE B CG1   1 
ATOM   10245 C  CG2   . ILE B 1 584 ? 139.450 141.552 161.167 1.00 29.97 ?  584 ILE B CG2   1 
ATOM   10246 C  CD1   . ILE B 1 584 ? 137.034 142.964 161.573 1.00 35.27 ?  584 ILE B CD1   1 
ATOM   10247 N  N     . SER B 1 585 ? 137.000 138.450 163.938 1.00 31.66 ?  585 SER B N     1 
ATOM   10248 C  CA    . SER B 1 585 ? 136.415 138.053 165.213 1.00 30.44 ?  585 SER B CA    1 
ATOM   10249 C  C     . SER B 1 585 ? 137.373 137.187 166.021 1.00 29.39 ?  585 SER B C     1 
ATOM   10250 O  O     . SER B 1 585 ? 137.361 137.239 167.255 1.00 29.89 ?  585 SER B O     1 
ATOM   10251 C  CB    . SER B 1 585 ? 135.095 137.319 164.983 1.00 29.93 ?  585 SER B CB    1 
ATOM   10252 O  OG    . SER B 1 585 ? 135.290 136.124 164.249 1.00 39.68 ?  585 SER B OG    1 
ATOM   10253 N  N     . TYR B 1 586 ? 138.199 136.383 165.349 1.00 35.14 ?  586 TYR B N     1 
ATOM   10254 C  CA    . TYR B 1 586 ? 139.196 135.584 166.053 1.00 36.08 ?  586 TYR B CA    1 
ATOM   10255 C  C     . TYR B 1 586 ? 140.233 136.472 166.726 1.00 34.29 ?  586 TYR B C     1 
ATOM   10256 O  O     . TYR B 1 586 ? 140.584 136.260 167.892 1.00 34.58 ?  586 TYR B O     1 
ATOM   10257 C  CB    . TYR B 1 586 ? 139.867 134.613 165.083 1.00 34.42 ?  586 TYR B CB    1 
ATOM   10258 C  CG    . TYR B 1 586 ? 138.933 133.568 164.521 1.00 36.44 ?  586 TYR B CG    1 
ATOM   10259 C  CD1   . TYR B 1 586 ? 138.416 132.566 165.329 1.00 36.35 ?  586 TYR B CD1   1 
ATOM   10260 C  CD2   . TYR B 1 586 ? 138.563 133.589 163.185 1.00 36.65 ?  586 TYR B CD2   1 
ATOM   10261 C  CE1   . TYR B 1 586 ? 137.561 131.612 164.821 1.00 38.78 ?  586 TYR B CE1   1 
ATOM   10262 C  CE2   . TYR B 1 586 ? 137.708 132.638 162.668 1.00 36.52 ?  586 TYR B CE2   1 
ATOM   10263 C  CZ    . TYR B 1 586 ? 137.210 131.652 163.489 1.00 37.31 ?  586 TYR B CZ    1 
ATOM   10264 O  OH    . TYR B 1 586 ? 136.358 130.703 162.979 1.00 38.93 ?  586 TYR B OH    1 
ATOM   10265 N  N     . VAL B 1 587 ? 140.732 137.478 166.004 1.00 30.68 ?  587 VAL B N     1 
ATOM   10266 C  CA    . VAL B 1 587 ? 141.714 138.391 166.581 1.00 28.31 ?  587 VAL B CA    1 
ATOM   10267 C  C     . VAL B 1 587 ? 141.128 139.104 167.790 1.00 33.41 ?  587 VAL B C     1 
ATOM   10268 O  O     . VAL B 1 587 ? 141.782 139.238 168.831 1.00 37.74 ?  587 VAL B O     1 
ATOM   10269 C  CB    . VAL B 1 587 ? 142.200 139.393 165.516 1.00 32.65 ?  587 VAL B CB    1 
ATOM   10270 C  CG1   . VAL B 1 587 ? 143.307 140.268 166.078 1.00 32.87 ?  587 VAL B CG1   1 
ATOM   10271 C  CG2   . VAL B 1 587 ? 142.669 138.658 164.273 1.00 34.75 ?  587 VAL B CG2   1 
ATOM   10272 N  N     . GLN B 1 588 ? 139.885 139.571 167.674 1.00 32.81 ?  588 GLN B N     1 
ATOM   10273 C  CA    . GLN B 1 588 ? 139.222 140.239 168.782 1.00 24.95 ?  588 GLN B CA    1 
ATOM   10274 C  C     . GLN B 1 588 ? 138.785 139.276 169.875 1.00 29.83 ?  588 GLN B C     1 
ATOM   10275 O  O     . GLN B 1 588 ? 138.414 139.731 170.961 1.00 36.11 ?  588 GLN B O     1 
ATOM   10276 C  CB    . GLN B 1 588 ? 138.014 141.021 168.271 1.00 27.27 ?  588 GLN B CB    1 
ATOM   10277 C  CG    . GLN B 1 588 ? 138.377 142.291 167.529 1.00 27.65 ?  588 GLN B CG    1 
ATOM   10278 C  CD    . GLN B 1 588 ? 138.702 143.431 168.468 1.00 29.46 ?  588 GLN B CD    1 
ATOM   10279 O  OE1   . GLN B 1 588 ? 138.091 143.571 169.525 1.00 34.73 ?  588 GLN B OE1   1 
ATOM   10280 N  NE2   . GLN B 1 588 ? 139.674 144.250 168.090 1.00 30.69 ?  588 GLN B NE2   1 
ATOM   10281 N  N     . SER B 1 589 ? 138.822 137.970 169.618 1.00 32.78 ?  589 SER B N     1 
ATOM   10282 C  CA    . SER B 1 589 ? 138.411 136.970 170.600 1.00 27.91 ?  589 SER B CA    1 
ATOM   10283 C  C     . SER B 1 589 ? 136.935 137.140 170.951 1.00 28.60 ?  589 SER B C     1 
ATOM   10284 O  O     . SER B 1 589 ? 136.538 137.112 172.117 1.00 32.54 ?  589 SER B O     1 
ATOM   10285 C  CB    . SER B 1 589 ? 139.291 137.042 171.849 1.00 29.83 ?  589 SER B CB    1 
ATOM   10286 O  OG    . SER B 1 589 ? 139.234 135.832 172.583 1.00 41.59 ?  589 SER B OG    1 
ATOM   10287 N  N     . SER B 1 590 ? 136.117 137.318 169.918 1.00 27.27 ?  590 SER B N     1 
ATOM   10288 C  CA    . SER B 1 590 ? 134.720 137.681 170.079 1.00 24.39 ?  590 SER B CA    1 
ATOM   10289 C  C     . SER B 1 590 ? 133.847 136.820 169.180 1.00 25.29 ?  590 SER B C     1 
ATOM   10290 O  O     . SER B 1 590 ? 134.312 136.226 168.206 1.00 29.76 ?  590 SER B O     1 
ATOM   10291 C  CB    . SER B 1 590 ? 134.495 139.166 169.758 1.00 21.87 ?  590 SER B CB    1 
ATOM   10292 O  OG    . SER B 1 590 ? 134.290 139.360 168.371 1.00 25.08 ?  590 SER B OG    1 
ATOM   10293 N  N     . THR B 1 591 ? 132.566 136.751 169.531 1.00 26.07 ?  591 THR B N     1 
ATOM   10294 C  CA    . THR B 1 591 ? 131.589 136.110 168.664 1.00 20.99 ?  591 THR B CA    1 
ATOM   10295 C  C     . THR B 1 591 ? 131.288 137.006 167.468 1.00 24.62 ?  591 THR B C     1 
ATOM   10296 O  O     . THR B 1 591 ? 131.229 138.232 167.588 1.00 22.99 ?  591 THR B O     1 
ATOM   10297 C  CB    . THR B 1 591 ? 130.305 135.803 169.434 1.00 23.57 ?  591 THR B CB    1 
ATOM   10298 O  OG1   . THR B 1 591 ? 129.622 137.025 169.741 1.00 35.10 ?  591 THR B OG1   1 
ATOM   10299 C  CG2   . THR B 1 591 ? 130.621 135.065 170.725 1.00 22.04 ?  591 THR B CG2   1 
ATOM   10300 N  N     . ALA B 1 592 ? 131.104 136.387 166.307 1.00 23.83 ?  592 ALA B N     1 
ATOM   10301 C  CA    . ALA B 1 592 ? 130.948 137.145 165.074 1.00 24.16 ?  592 ALA B CA    1 
ATOM   10302 C  C     . ALA B 1 592 ? 129.659 137.957 165.096 1.00 26.99 ?  592 ALA B C     1 
ATOM   10303 O  O     . ALA B 1 592 ? 128.581 137.425 165.380 1.00 28.88 ?  592 ALA B O     1 
ATOM   10304 C  CB    . ALA B 1 592 ? 130.961 136.204 163.871 1.00 24.66 ?  592 ALA B CB    1 
ATOM   10305 N  N     . SER B 1 593 ? 129.777 139.243 164.795 1.00 25.38 ?  593 SER B N     1 
ATOM   10306 C  CA    . SER B 1 593 ? 128.638 140.148 164.631 1.00 11.61 ?  593 SER B CA    1 
ATOM   10307 C  C     . SER B 1 593 ? 127.742 140.062 165.867 1.00 14.91 ?  593 SER B C     1 
ATOM   10308 O  O     . SER B 1 593 ? 128.220 139.870 166.989 1.00 25.38 ?  593 SER B O     1 
ATOM   10309 C  CB    . SER B 1 593 ? 127.941 139.833 163.321 1.00 25.21 ?  593 SER B CB    1 
ATOM   10310 O  OG    . SER B 1 593 ? 126.995 140.832 162.990 1.00 29.60 ?  593 SER B OG    1 
ATOM   10311 N  N     . VAL B 1 594 ? 126.432 140.209 165.672 1.00 20.69 ?  594 VAL B N     1 
ATOM   10312 C  CA    . VAL B 1 594 ? 125.457 140.060 166.744 1.00 19.49 ?  594 VAL B CA    1 
ATOM   10313 C  C     . VAL B 1 594 ? 124.763 138.704 166.690 1.00 16.38 ?  594 VAL B C     1 
ATOM   10314 O  O     . VAL B 1 594 ? 123.821 138.462 167.447 1.00 19.31 ?  594 VAL B O     1 
ATOM   10315 C  CB    . VAL B 1 594 ? 124.427 141.201 166.716 1.00 22.91 ?  594 VAL B CB    1 
ATOM   10316 C  CG1   . VAL B 1 594 ? 125.077 142.512 167.126 1.00 13.82 ?  594 VAL B CG1   1 
ATOM   10317 C  CG2   . VAL B 1 594 ? 123.804 141.317 165.337 1.00 22.91 ?  594 VAL B CG2   1 
ATOM   10318 N  N     . MET B 1 595 ? 125.209 137.815 165.807 1.00 25.11 ?  595 MET B N     1 
ATOM   10319 C  CA    . MET B 1 595 ? 124.571 136.521 165.655 1.00 21.12 ?  595 MET B CA    1 
ATOM   10320 C  C     . MET B 1 595 ? 124.964 135.591 166.803 1.00 25.32 ?  595 MET B C     1 
ATOM   10321 O  O     . MET B 1 595 ? 126.030 135.747 167.404 1.00 30.70 ?  595 MET B O     1 
ATOM   10322 C  CB    . MET B 1 595 ? 124.964 135.887 164.325 1.00 21.78 ?  595 MET B CB    1 
ATOM   10323 C  CG    . MET B 1 595 ? 124.629 136.732 163.110 1.00 25.79 ?  595 MET B CG    1 
ATOM   10324 S  SD    . MET B 1 595 ? 123.017 136.352 162.404 1.00 35.97 ?  595 MET B SD    1 
ATOM   10325 C  CE    . MET B 1 595 ? 121.965 137.348 163.451 1.00 15.95 ?  595 MET B CE    1 
ATOM   10326 N  N     . PRO B 1 596 ? 124.117 134.620 167.130 1.00 32.84 ?  596 PRO B N     1 
ATOM   10327 C  CA    . PRO B 1 596 ? 124.513 133.594 168.097 1.00 23.07 ?  596 PRO B CA    1 
ATOM   10328 C  C     . PRO B 1 596 ? 125.566 132.665 167.510 1.00 26.02 ?  596 PRO B C     1 
ATOM   10329 O  O     . PRO B 1 596 ? 125.687 132.499 166.295 1.00 31.41 ?  596 PRO B O     1 
ATOM   10330 C  CB    . PRO B 1 596 ? 123.206 132.852 168.385 1.00 24.93 ?  596 PRO B CB    1 
ATOM   10331 C  CG    . PRO B 1 596 ? 122.384 133.056 167.161 1.00 29.89 ?  596 PRO B CG    1 
ATOM   10332 C  CD    . PRO B 1 596 ? 122.754 134.406 166.614 1.00 28.33 ?  596 PRO B CD    1 
ATOM   10333 N  N     . ILE B 1 597 ? 126.340 132.054 168.406 1.00 27.93 ?  597 ILE B N     1 
ATOM   10334 C  CA    . ILE B 1 597 ? 127.444 131.203 167.988 1.00 30.87 ?  597 ILE B CA    1 
ATOM   10335 C  C     . ILE B 1 597 ? 126.909 129.974 167.268 1.00 32.24 ?  597 ILE B C     1 
ATOM   10336 O  O     . ILE B 1 597 ? 125.875 129.406 167.646 1.00 34.85 ?  597 ILE B O     1 
ATOM   10337 C  CB    . ILE B 1 597 ? 128.305 130.803 169.198 1.00 30.75 ?  597 ILE B CB    1 
ATOM   10338 C  CG1   . ILE B 1 597 ? 127.489 129.952 170.172 1.00 31.41 ?  597 ILE B CG1   1 
ATOM   10339 C  CG2   . ILE B 1 597 ? 128.858 132.036 169.889 1.00 29.59 ?  597 ILE B CG2   1 
ATOM   10340 C  CD1   . ILE B 1 597 ? 128.329 129.159 171.141 1.00 30.86 ?  597 ILE B CD1   1 
ATOM   10341 N  N     . MET B 1 598 ? 127.614 129.559 166.215 1.00 43.18 ?  598 MET B N     1 
ATOM   10342 C  CA    . MET B 1 598 ? 127.232 128.351 165.494 1.00 41.72 ?  598 MET B CA    1 
ATOM   10343 C  C     . MET B 1 598 ? 127.632 127.094 166.256 1.00 41.97 ?  598 MET B C     1 
ATOM   10344 O  O     . MET B 1 598 ? 126.896 126.101 166.248 1.00 47.60 ?  598 MET B O     1 
ATOM   10345 C  CB    . MET B 1 598 ? 127.864 128.350 164.101 1.00 41.24 ?  598 MET B CB    1 
ATOM   10346 C  CG    . MET B 1 598 ? 127.091 129.149 163.068 1.00 40.38 ?  598 MET B CG    1 
ATOM   10347 S  SD    . MET B 1 598 ? 127.986 129.318 161.513 1.00 59.59 ?  598 MET B SD    1 
ATOM   10348 C  CE    . MET B 1 598 ? 129.145 130.618 161.925 1.00 43.59 ?  598 MET B CE    1 
ATOM   10349 N  N     . GLU B 1 599 ? 128.786 127.117 166.918 1.00 43.28 ?  599 GLU B N     1 
ATOM   10350 C  CA    . GLU B 1 599 ? 129.285 125.958 167.643 1.00 43.32 ?  599 GLU B CA    1 
ATOM   10351 C  C     . GLU B 1 599 ? 130.118 126.427 168.825 1.00 40.08 ?  599 GLU B C     1 
ATOM   10352 O  O     . GLU B 1 599 ? 130.857 127.407 168.720 1.00 46.95 ?  599 GLU B O     1 
ATOM   10353 C  CB    . GLU B 1 599 ? 130.117 125.046 166.734 1.00 44.95 ?  599 GLU B CB    1 
ATOM   10354 C  CG    . GLU B 1 599 ? 131.128 125.783 165.874 1.00 43.40 ?  599 GLU B CG    1 
ATOM   10355 C  CD    . GLU B 1 599 ? 131.241 125.198 164.482 1.00 48.73 ?  599 GLU B CD    1 
ATOM   10356 O  OE1   . GLU B 1 599 ? 130.192 125.000 163.833 1.00 52.84 ?  599 GLU B OE1   1 
ATOM   10357 O  OE2   . GLU B 1 599 ? 132.376 124.933 164.034 1.00 47.86 -1 599 GLU B OE2   1 
ATOM   10358 N  N     . ARG B 1 600 ? 129.996 125.713 169.946 1.00 39.89 ?  600 ARG B N     1 
ATOM   10359 C  CA    . ARG B 1 600 ? 130.720 126.100 171.152 1.00 37.05 ?  600 ARG B CA    1 
ATOM   10360 C  C     . ARG B 1 600 ? 132.225 126.028 170.938 1.00 38.03 ?  600 ARG B C     1 
ATOM   10361 O  O     . ARG B 1 600 ? 132.967 126.908 171.391 1.00 44.05 ?  600 ARG B O     1 
ATOM   10362 C  CB    . ARG B 1 600 ? 130.302 125.210 172.321 1.00 37.40 ?  600 ARG B CB    1 
ATOM   10363 C  CG    . ARG B 1 600 ? 128.989 125.617 172.958 1.00 37.89 ?  600 ARG B CG    1 
ATOM   10364 C  CD    . ARG B 1 600 ? 128.698 124.785 174.190 1.00 38.17 ?  600 ARG B CD    1 
ATOM   10365 N  NE    . ARG B 1 600 ? 127.368 125.052 174.725 1.00 37.44 ?  600 ARG B NE    1 
ATOM   10366 C  CZ    . ARG B 1 600 ? 126.266 124.437 174.321 1.00 41.28 ?  600 ARG B CZ    1 
ATOM   10367 N  NH1   . ARG B 1 600 ? 126.296 123.518 173.370 1.00 41.31 1  600 ARG B NH1   1 
ATOM   10368 N  NH2   . ARG B 1 600 ? 125.103 124.752 174.884 1.00 39.74 ?  600 ARG B NH2   1 
ATOM   10369 N  N     . ILE B 1 601 ? 132.696 124.987 170.260 1.00 42.59 ?  601 ILE B N     1 
ATOM   10370 C  CA    . ILE B 1 601 ? 134.106 124.824 169.931 1.00 42.97 ?  601 ILE B CA    1 
ATOM   10371 C  C     . ILE B 1 601 ? 134.207 124.650 168.424 1.00 44.04 ?  601 ILE B C     1 
ATOM   10372 O  O     . ILE B 1 601 ? 133.535 123.786 167.848 1.00 45.36 ?  601 ILE B O     1 
ATOM   10373 C  CB    . ILE B 1 601 ? 134.735 123.632 170.669 1.00 42.45 ?  601 ILE B CB    1 
ATOM   10374 C  CG1   . ILE B 1 601 ? 134.480 123.745 172.173 1.00 42.85 ?  601 ILE B CG1   1 
ATOM   10375 C  CG2   . ILE B 1 601 ? 136.225 123.561 170.385 1.00 39.80 ?  601 ILE B CG2   1 
ATOM   10376 C  CD1   . ILE B 1 601 ? 134.878 122.517 172.954 1.00 41.67 ?  601 ILE B CD1   1 
ATOM   10377 N  N     . GLU B 1 602 ? 135.043 125.466 167.792 1.00 51.23 ?  602 GLU B N     1 
ATOM   10378 C  CA    . GLU B 1 602 ? 135.176 125.468 166.342 1.00 49.11 ?  602 GLU B CA    1 
ATOM   10379 C  C     . GLU B 1 602 ? 136.334 124.564 165.939 1.00 51.58 ?  602 GLU B C     1 
ATOM   10380 O  O     . GLU B 1 602 ? 137.467 124.759 166.393 1.00 54.51 ?  602 GLU B O     1 
ATOM   10381 C  CB    . GLU B 1 602 ? 135.397 126.890 165.828 1.00 48.75 ?  602 GLU B CB    1 
ATOM   10382 C  CG    . GLU B 1 602 ? 134.681 127.203 164.528 1.00 52.63 ?  602 GLU B CG    1 
ATOM   10383 C  CD    . GLU B 1 602 ? 134.223 128.647 164.449 1.00 57.30 ?  602 GLU B CD    1 
ATOM   10384 O  OE1   . GLU B 1 602 ? 135.068 129.550 164.622 1.00 56.56 ?  602 GLU B OE1   1 
ATOM   10385 O  OE2   . GLU B 1 602 ? 133.019 128.879 164.211 1.00 53.97 -1 602 GLU B OE2   1 
ATOM   10386 N  N     . GLU B 1 603 ? 136.048 123.581 165.092 1.00 58.91 ?  603 GLU B N     1 
ATOM   10387 C  CA    . GLU B 1 603 ? 137.059 122.670 164.573 1.00 58.18 ?  603 GLU B CA    1 
ATOM   10388 C  C     . GLU B 1 603 ? 137.462 123.127 163.178 1.00 56.93 ?  603 GLU B C     1 
ATOM   10389 O  O     . GLU B 1 603 ? 136.637 123.130 162.259 1.00 58.99 ?  603 GLU B O     1 
ATOM   10390 C  CB    . GLU B 1 603 ? 136.535 121.235 164.538 1.00 59.66 ?  603 GLU B CB    1 
ATOM   10391 C  CG    . GLU B 1 603 ? 137.616 120.181 164.687 1.00 61.99 ?  603 GLU B CG    1 
ATOM   10392 C  CD    . GLU B 1 603 ? 137.268 118.886 163.982 1.00 62.91 ?  603 GLU B CD    1 
ATOM   10393 O  OE1   . GLU B 1 603 ? 137.166 118.893 162.739 1.00 62.22 ?  603 GLU B OE1   1 
ATOM   10394 O  OE2   . GLU B 1 603 ? 137.099 117.859 164.674 1.00 59.89 -1 603 GLU B OE2   1 
ATOM   10395 N  N     . ARG B 1 604 ? 138.724 123.513 163.026 1.00 60.45 ?  604 ARG B N     1 
ATOM   10396 C  CA    . ARG B 1 604 ? 139.251 123.991 161.760 1.00 60.95 ?  604 ARG B CA    1 
ATOM   10397 C  C     . ARG B 1 604 ? 140.428 123.125 161.338 1.00 62.05 ?  604 ARG B C     1 
ATOM   10398 O  O     . ARG B 1 604 ? 141.107 122.521 162.175 1.00 61.95 ?  604 ARG B O     1 
ATOM   10399 C  CB    . ARG B 1 604 ? 139.704 125.453 161.855 1.00 61.78 ?  604 ARG B CB    1 
ATOM   10400 C  CG    . ARG B 1 604 ? 138.636 126.429 162.324 1.00 62.24 ?  604 ARG B CG    1 
ATOM   10401 C  CD    . ARG B 1 604 ? 137.502 126.570 161.321 1.00 62.05 ?  604 ARG B CD    1 
ATOM   10402 N  NE    . ARG B 1 604 ? 136.383 125.690 161.634 1.00 63.95 ?  604 ARG B NE    1 
ATOM   10403 C  CZ    . ARG B 1 604 ? 135.114 125.973 161.373 1.00 60.40 ?  604 ARG B CZ    1 
ATOM   10404 N  NH1   . ARG B 1 604 ? 134.765 127.107 160.791 1.00 60.18 1  604 ARG B NH1   1 
ATOM   10405 N  NH2   . ARG B 1 604 ? 134.172 125.098 161.709 1.00 60.78 ?  604 ARG B NH2   1 
ATOM   10406 N  N     . THR B 1 605 ? 140.661 123.065 160.031 1.00 66.27 ?  605 THR B N     1 
ATOM   10407 C  CA    . THR B 1 605 ? 141.815 122.377 159.468 1.00 67.23 ?  605 THR B CA    1 
ATOM   10408 C  C     . THR B 1 605 ? 142.714 123.408 158.797 1.00 67.54 ?  605 THR B C     1 
ATOM   10409 O  O     . THR B 1 605 ? 142.267 124.154 157.918 1.00 67.15 ?  605 THR B O     1 
ATOM   10410 C  CB    . THR B 1 605 ? 141.384 121.287 158.482 1.00 67.78 ?  605 THR B CB    1 
ATOM   10411 O  OG1   . THR B 1 605 ? 142.392 120.270 158.422 1.00 69.23 ?  605 THR B OG1   1 
ATOM   10412 C  CG2   . THR B 1 605 ? 141.155 121.855 157.087 1.00 66.03 ?  605 THR B CG2   1 
ATOM   10413 N  N     . TYR B 1 606 ? 143.967 123.473 159.239 1.00 67.96 ?  606 TYR B N     1 
ATOM   10414 C  CA    . TYR B 1 606 ? 144.973 124.365 158.666 1.00 67.94 ?  606 TYR B CA    1 
ATOM   10415 C  C     . TYR B 1 606 ? 146.151 123.495 158.243 1.00 68.56 ?  606 TYR B C     1 
ATOM   10416 O  O     . TYR B 1 606 ? 146.921 123.026 159.087 1.00 67.62 ?  606 TYR B O     1 
ATOM   10417 C  CB    . TYR B 1 606 ? 145.385 125.443 159.664 1.00 66.19 ?  606 TYR B CB    1 
ATOM   10418 C  CG    . TYR B 1 606 ? 144.280 126.431 159.969 1.00 66.72 ?  606 TYR B CG    1 
ATOM   10419 C  CD1   . TYR B 1 606 ? 143.965 127.448 159.077 1.00 65.48 ?  606 TYR B CD1   1 
ATOM   10420 C  CD2   . TYR B 1 606 ? 143.544 126.338 161.141 1.00 66.10 ?  606 TYR B CD2   1 
ATOM   10421 C  CE1   . TYR B 1 606 ? 142.952 128.347 159.349 1.00 66.55 ?  606 TYR B CE1   1 
ATOM   10422 C  CE2   . TYR B 1 606 ? 142.530 127.232 161.422 1.00 65.31 ?  606 TYR B CE2   1 
ATOM   10423 C  CZ    . TYR B 1 606 ? 142.239 128.234 160.523 1.00 67.77 ?  606 TYR B CZ    1 
ATOM   10424 O  OH    . TYR B 1 606 ? 141.228 129.125 160.802 1.00 68.60 ?  606 TYR B OH    1 
ATOM   10425 N  N     . GLY B 1 607 ? 146.289 123.280 156.939 1.00 74.62 ?  607 GLY B N     1 
ATOM   10426 C  CA    . GLY B 1 607 ? 147.242 122.289 156.469 1.00 73.81 ?  607 GLY B CA    1 
ATOM   10427 C  C     . GLY B 1 607 ? 146.738 120.903 156.815 1.00 74.20 ?  607 GLY B C     1 
ATOM   10428 O  O     . GLY B 1 607 ? 145.570 120.569 156.589 1.00 74.61 ?  607 GLY B O     1 
ATOM   10429 N  N     . ASN B 1 608 ? 147.621 120.077 157.371 1.00 76.14 ?  608 ASN B N     1 
ATOM   10430 C  CA    . ASN B 1 608 ? 147.252 118.758 157.864 1.00 77.98 ?  608 ASN B CA    1 
ATOM   10431 C  C     . ASN B 1 608 ? 146.990 118.750 159.363 1.00 78.57 ?  608 ASN B C     1 
ATOM   10432 O  O     . ASN B 1 608 ? 146.761 117.681 159.938 1.00 78.12 ?  608 ASN B O     1 
ATOM   10433 C  CB    . ASN B 1 608 ? 148.337 117.739 157.513 1.00 78.21 ?  608 ASN B CB    1 
ATOM   10434 C  CG    . ASN B 1 608 ? 148.357 117.395 156.036 1.00 78.30 ?  608 ASN B CG    1 
ATOM   10435 O  OD1   . ASN B 1 608 ? 147.400 117.669 155.312 1.00 77.12 ?  608 ASN B OD1   1 
ATOM   10436 N  ND2   . ASN B 1 608 ? 149.449 116.791 155.584 1.00 78.65 ?  608 ASN B ND2   1 
ATOM   10437 N  N     . SER B 1 609 ? 147.015 119.913 160.006 1.00 75.09 ?  609 SER B N     1 
ATOM   10438 C  CA    . SER B 1 609 ? 146.801 120.036 161.440 1.00 74.37 ?  609 SER B CA    1 
ATOM   10439 C  C     . SER B 1 609 ? 145.419 120.618 161.700 1.00 72.38 ?  609 SER B C     1 
ATOM   10440 O  O     . SER B 1 609 ? 145.055 121.647 161.121 1.00 71.38 ?  609 SER B O     1 
ATOM   10441 C  CB    . SER B 1 609 ? 147.875 120.919 162.077 1.00 72.78 ?  609 SER B CB    1 
ATOM   10442 O  OG    . SER B 1 609 ? 147.820 122.235 161.556 1.00 72.95 ?  609 SER B OG    1 
ATOM   10443 N  N     . LYS B 1 610 ? 144.659 119.960 162.569 1.00 65.50 ?  610 LYS B N     1 
ATOM   10444 C  CA    . LYS B 1 610 ? 143.324 120.406 162.943 1.00 65.25 ?  610 LYS B CA    1 
ATOM   10445 C  C     . LYS B 1 610 ? 143.405 121.208 164.235 1.00 64.63 ?  610 LYS B C     1 
ATOM   10446 O  O     . LYS B 1 610 ? 144.011 120.761 165.214 1.00 62.87 ?  610 LYS B O     1 
ATOM   10447 C  CB    . LYS B 1 610 ? 142.381 119.213 163.106 1.00 64.82 ?  610 LYS B CB    1 
ATOM   10448 C  CG    . LYS B 1 610 ? 142.656 118.364 164.333 1.00 63.67 ?  610 LYS B CG    1 
ATOM   10449 C  CD    . LYS B 1 610 ? 141.389 117.707 164.847 1.00 65.66 ?  610 LYS B CD    1 
ATOM   10450 C  CE    . LYS B 1 610 ? 140.831 116.726 163.828 1.00 66.01 ?  610 LYS B CE    1 
ATOM   10451 N  NZ    . LYS B 1 610 ? 139.345 116.659 163.864 1.00 65.07 1  610 LYS B NZ    1 
ATOM   10452 N  N     . THR B 1 611 ? 142.799 122.391 164.231 1.00 64.13 ?  611 THR B N     1 
ATOM   10453 C  CA    . THR B 1 611 ? 142.840 123.305 165.363 1.00 61.57 ?  611 THR B CA    1 
ATOM   10454 C  C     . THR B 1 611 ? 141.467 123.388 166.013 1.00 57.97 ?  611 THR B C     1 
ATOM   10455 O  O     . THR B 1 611 ? 140.440 123.325 165.329 1.00 58.79 ?  611 THR B O     1 
ATOM   10456 C  CB    . THR B 1 611 ? 143.292 124.702 164.930 1.00 62.28 ?  611 THR B CB    1 
ATOM   10457 O  OG1   . THR B 1 611 ? 142.767 124.992 163.629 1.00 60.67 ?  611 THR B OG1   1 
ATOM   10458 C  CG2   . THR B 1 611 ? 144.809 124.777 164.883 1.00 60.09 ?  611 THR B CG2   1 
ATOM   10459 N  N     . TYR B 1 612 ? 141.456 123.528 167.333 1.00 54.96 ?  612 TYR B N     1 
ATOM   10460 C  CA    . TYR B 1 612 ? 140.227 123.586 168.113 1.00 53.11 ?  612 TYR B CA    1 
ATOM   10461 C  C     . TYR B 1 612 ? 140.073 124.980 168.702 1.00 55.32 ?  612 TYR B C     1 
ATOM   10462 O  O     . TYR B 1 612 ? 140.966 125.461 169.408 1.00 58.02 ?  612 TYR B O     1 
ATOM   10463 C  CB    . TYR B 1 612 ? 140.244 122.537 169.225 1.00 56.10 ?  612 TYR B CB    1 
ATOM   10464 C  CG    . TYR B 1 612 ? 140.028 121.128 168.728 1.00 57.49 ?  612 TYR B CG    1 
ATOM   10465 C  CD1   . TYR B 1 612 ? 138.858 120.774 168.072 1.00 57.63 ?  612 TYR B CD1   1 
ATOM   10466 C  CD2   . TYR B 1 612 ? 140.999 120.153 168.907 1.00 58.61 ?  612 TYR B CD2   1 
ATOM   10467 C  CE1   . TYR B 1 612 ? 138.659 119.487 167.614 1.00 58.58 ?  612 TYR B CE1   1 
ATOM   10468 C  CE2   . TYR B 1 612 ? 140.810 118.864 168.451 1.00 59.11 ?  612 TYR B CE2   1 
ATOM   10469 C  CZ    . TYR B 1 612 ? 139.639 118.537 167.806 1.00 59.68 ?  612 TYR B CZ    1 
ATOM   10470 O  OH    . TYR B 1 612 ? 139.443 117.253 167.350 1.00 60.10 ?  612 TYR B OH    1 
ATOM   10471 N  N     . TYR B 1 613 ? 138.946 125.623 168.414 1.00 48.81 ?  613 TYR B N     1 
ATOM   10472 C  CA    . TYR B 1 613 ? 138.675 126.975 168.902 1.00 42.77 ?  613 TYR B CA    1 
ATOM   10473 C  C     . TYR B 1 613 ? 137.409 126.992 169.744 1.00 40.43 ?  613 TYR B C     1 
ATOM   10474 O  O     . TYR B 1 613 ? 136.294 127.013 169.195 1.00 42.33 ?  613 TYR B O     1 
ATOM   10475 C  CB    . TYR B 1 613 ? 138.551 127.959 167.740 1.00 40.04 ?  613 TYR B CB    1 
ATOM   10476 C  CG    . TYR B 1 613 ? 138.335 129.387 168.182 1.00 41.62 ?  613 TYR B CG    1 
ATOM   10477 C  CD1   . TYR B 1 613 ? 139.276 130.041 168.965 1.00 43.04 ?  613 TYR B CD1   1 
ATOM   10478 C  CD2   . TYR B 1 613 ? 137.193 130.083 167.813 1.00 42.55 ?  613 TYR B CD2   1 
ATOM   10479 C  CE1   . TYR B 1 613 ? 139.084 131.346 169.370 1.00 43.84 ?  613 TYR B CE1   1 
ATOM   10480 C  CE2   . TYR B 1 613 ? 136.993 131.388 168.214 1.00 43.15 ?  613 TYR B CE2   1 
ATOM   10481 C  CZ    . TYR B 1 613 ? 137.941 132.015 168.992 1.00 44.16 ?  613 TYR B CZ    1 
ATOM   10482 O  OH    . TYR B 1 613 ? 137.745 133.317 169.392 1.00 43.98 ?  613 TYR B OH    1 
ATOM   10483 N  N     . PRO B 1 614 ? 137.521 126.981 171.069 1.00 38.60 ?  614 PRO B N     1 
ATOM   10484 C  CA    . PRO B 1 614 ? 136.336 127.187 171.903 1.00 39.14 ?  614 PRO B CA    1 
ATOM   10485 C  C     . PRO B 1 614 ? 135.814 128.605 171.749 1.00 40.77 ?  614 PRO B C     1 
ATOM   10486 O  O     . PRO B 1 614 ? 136.559 129.537 171.435 1.00 40.12 ?  614 PRO B O     1 
ATOM   10487 C  CB    . PRO B 1 614 ? 136.848 126.933 173.327 1.00 40.52 ?  614 PRO B CB    1 
ATOM   10488 C  CG    . PRO B 1 614 ? 138.191 126.283 173.160 1.00 41.36 ?  614 PRO B CG    1 
ATOM   10489 C  CD    . PRO B 1 614 ? 138.736 126.803 171.876 1.00 39.12 ?  614 PRO B CD    1 
ATOM   10490 N  N     . MET B 1 615 ? 134.516 128.763 171.972 1.00 41.25 ?  615 MET B N     1 
ATOM   10491 C  CA    . MET B 1 615 ? 133.927 130.089 171.897 1.00 36.95 ?  615 MET B CA    1 
ATOM   10492 C  C     . MET B 1 615 ? 134.573 130.992 172.944 1.00 36.93 ?  615 MET B C     1 
ATOM   10493 O  O     . MET B 1 615 ? 134.776 130.567 174.088 1.00 38.64 ?  615 MET B O     1 
ATOM   10494 C  CB    . MET B 1 615 ? 132.415 130.022 172.114 1.00 35.74 ?  615 MET B CB    1 
ATOM   10495 C  CG    . MET B 1 615 ? 131.615 129.931 170.827 1.00 36.58 ?  615 MET B CG    1 
ATOM   10496 S  SD    . MET B 1 615 ? 132.307 130.925 169.492 1.00 53.27 ?  615 MET B SD    1 
ATOM   10497 C  CE    . MET B 1 615 ? 133.295 129.701 168.636 1.00 38.98 ?  615 MET B CE    1 
ATOM   10498 N  N     . PRO B 1 616 ? 134.917 132.228 172.591 1.00 42.14 ?  616 PRO B N     1 
ATOM   10499 C  CA    . PRO B 1 616 ? 135.652 133.085 173.528 1.00 36.76 ?  616 PRO B CA    1 
ATOM   10500 C  C     . PRO B 1 616 ? 134.942 133.194 174.868 1.00 35.68 ?  616 PRO B C     1 
ATOM   10501 O  O     . PRO B 1 616 ? 133.757 133.525 174.940 1.00 41.07 ?  616 PRO B O     1 
ATOM   10502 C  CB    . PRO B 1 616 ? 135.705 134.431 172.802 1.00 35.33 ?  616 PRO B CB    1 
ATOM   10503 C  CG    . PRO B 1 616 ? 135.598 134.077 171.359 1.00 37.92 ?  616 PRO B CG    1 
ATOM   10504 C  CD    . PRO B 1 616 ? 134.687 132.890 171.297 1.00 39.13 ?  616 PRO B CD    1 
ATOM   10505 N  N     . GLY B 1 617 ? 135.685 132.924 175.938 1.00 35.20 ?  617 GLY B N     1 
ATOM   10506 C  CA    . GLY B 1 617 ? 135.128 132.907 177.271 1.00 37.36 ?  617 GLY B CA    1 
ATOM   10507 C  C     . GLY B 1 617 ? 134.425 131.625 177.653 1.00 40.77 ?  617 GLY B C     1 
ATOM   10508 O  O     . GLY B 1 617 ? 133.893 131.540 178.766 1.00 41.32 ?  617 GLY B O     1 
ATOM   10509 N  N     . LEU B 1 618 ? 134.406 130.626 176.772 1.00 41.06 ?  618 LEU B N     1 
ATOM   10510 C  CA    . LEU B 1 618 ? 133.709 129.383 177.066 1.00 38.42 ?  618 LEU B CA    1 
ATOM   10511 C  C     . LEU B 1 618 ? 134.331 128.691 178.272 1.00 40.27 ?  618 LEU B C     1 
ATOM   10512 O  O     . LEU B 1 618 ? 135.554 128.668 178.436 1.00 45.75 ?  618 LEU B O     1 
ATOM   10513 C  CB    . LEU B 1 618 ? 133.743 128.459 175.849 1.00 38.42 ?  618 LEU B CB    1 
ATOM   10514 C  CG    . LEU B 1 618 ? 133.026 127.114 175.978 1.00 41.92 ?  618 LEU B CG    1 
ATOM   10515 C  CD1   . LEU B 1 618 ? 131.537 127.314 176.196 1.00 39.41 ?  618 LEU B CD1   1 
ATOM   10516 C  CD2   . LEU B 1 618 ? 133.280 126.257 174.749 1.00 40.34 ?  618 LEU B CD2   1 
ATOM   10517 N  N     . ALA B 1 619 ? 133.477 128.128 179.119 1.00 45.10 ?  619 ALA B N     1 
ATOM   10518 C  CA    . ALA B 1 619 ? 133.917 127.433 180.321 1.00 46.02 ?  619 ALA B CA    1 
ATOM   10519 C  C     . ALA B 1 619 ? 132.783 126.532 180.788 1.00 48.01 ?  619 ALA B C     1 
ATOM   10520 O  O     . ALA B 1 619 ? 131.698 126.511 180.202 1.00 52.82 ?  619 ALA B O     1 
ATOM   10521 C  CB    . ALA B 1 619 ? 134.340 128.422 181.410 1.00 42.56 ?  619 ALA B CB    1 
ATOM   10522 N  N     . SER B 1 620 ? 133.046 125.778 181.856 1.00 54.00 ?  620 SER B N     1 
ATOM   10523 C  CA    . SER B 1 620 ? 132.027 124.883 182.395 1.00 52.81 ?  620 SER B CA    1 
ATOM   10524 C  C     . SER B 1 620 ? 130.836 125.662 182.941 1.00 53.26 ?  620 SER B C     1 
ATOM   10525 O  O     . SER B 1 620 ? 129.683 125.261 182.750 1.00 56.76 ?  620 SER B O     1 
ATOM   10526 C  CB    . SER B 1 620 ? 132.632 123.997 183.483 1.00 57.04 ?  620 SER B CB    1 
ATOM   10527 O  OG    . SER B 1 620 ? 133.802 123.347 183.020 1.00 60.56 ?  620 SER B OG    1 
ATOM   10528 N  N     . ASN B 1 621 ? 131.096 126.780 183.623 1.00 51.23 ?  621 ASN B N     1 
ATOM   10529 C  CA    . ASN B 1 621 ? 130.022 127.514 184.282 1.00 51.61 ?  621 ASN B CA    1 
ATOM   10530 C  C     . ASN B 1 621 ? 129.154 128.299 183.306 1.00 52.06 ?  621 ASN B C     1 
ATOM   10531 O  O     . ASN B 1 621 ? 128.012 128.627 183.644 1.00 52.13 ?  621 ASN B O     1 
ATOM   10532 C  CB    . ASN B 1 621 ? 130.601 128.455 185.340 1.00 52.24 ?  621 ASN B CB    1 
ATOM   10533 C  CG    . ASN B 1 621 ? 131.325 129.641 184.733 1.00 54.17 ?  621 ASN B CG    1 
ATOM   10534 O  OD1   . ASN B 1 621 ? 131.730 129.611 183.572 1.00 55.70 ?  621 ASN B OD1   1 
ATOM   10535 N  ND2   . ASN B 1 621 ? 131.491 130.696 185.522 1.00 52.17 ?  621 ASN B ND2   1 
ATOM   10536 N  N     . ASN B 1 622 ? 129.660 128.610 182.112 1.00 44.50 ?  622 ASN B N     1 
ATOM   10537 C  CA    . ASN B 1 622 ? 128.886 129.322 181.103 1.00 45.09 ?  622 ASN B CA    1 
ATOM   10538 C  C     . ASN B 1 622 ? 128.608 128.463 179.875 1.00 47.58 ?  622 ASN B C     1 
ATOM   10539 O  O     . ASN B 1 622 ? 128.276 128.993 178.811 1.00 51.27 ?  622 ASN B O     1 
ATOM   10540 C  CB    . ASN B 1 622 ? 129.589 130.622 180.704 1.00 46.48 ?  622 ASN B CB    1 
ATOM   10541 C  CG    . ASN B 1 622 ? 130.919 130.387 180.006 1.00 47.00 ?  622 ASN B CG    1 
ATOM   10542 O  OD1   . ASN B 1 622 ? 131.216 129.284 179.552 1.00 49.62 ?  622 ASN B OD1   1 
ATOM   10543 N  ND2   . ASN B 1 622 ? 131.727 131.436 179.920 1.00 43.26 ?  622 ASN B ND2   1 
ATOM   10544 N  N     . TRP B 1 623 ? 128.740 127.141 180.002 1.00 41.05 ?  623 TRP B N     1 
ATOM   10545 C  CA    . TRP B 1 623 ? 128.479 126.256 178.872 1.00 41.27 ?  623 TRP B CA    1 
ATOM   10546 C  C     . TRP B 1 623 ? 127.031 126.361 178.412 1.00 42.36 ?  623 TRP B C     1 
ATOM   10547 O  O     . TRP B 1 623 ? 126.755 126.397 177.207 1.00 37.88 ?  623 TRP B O     1 
ATOM   10548 C  CB    . TRP B 1 623 ? 128.818 124.815 179.254 1.00 41.92 ?  623 TRP B CB    1 
ATOM   10549 C  CG    . TRP B 1 623 ? 128.624 123.826 178.150 1.00 40.24 ?  623 TRP B CG    1 
ATOM   10550 C  CD1   . TRP B 1 623 ? 127.471 123.176 177.824 1.00 39.53 ?  623 TRP B CD1   1 
ATOM   10551 C  CD2   . TRP B 1 623 ? 129.618 123.363 177.229 1.00 43.01 ?  623 TRP B CD2   1 
ATOM   10552 N  NE1   . TRP B 1 623 ? 127.682 122.343 176.755 1.00 37.62 ?  623 TRP B NE1   1 
ATOM   10553 C  CE2   . TRP B 1 623 ? 128.994 122.438 176.371 1.00 39.39 ?  623 TRP B CE2   1 
ATOM   10554 C  CE3   . TRP B 1 623 ? 130.976 123.644 177.044 1.00 41.30 ?  623 TRP B CE3   1 
ATOM   10555 C  CZ2   . TRP B 1 623 ? 129.679 121.792 175.345 1.00 40.26 ?  623 TRP B CZ2   1 
ATOM   10556 C  CZ3   . TRP B 1 623 ? 131.653 123.001 176.025 1.00 42.18 ?  623 TRP B CZ3   1 
ATOM   10557 C  CH2   . TRP B 1 623 ? 131.005 122.086 175.189 1.00 41.89 ?  623 TRP B CH2   1 
ATOM   10558 N  N     . PHE B 1 624 ? 126.091 126.410 179.357 1.00 47.83 ?  624 PHE B N     1 
ATOM   10559 C  CA    . PHE B 1 624 ? 124.677 126.444 178.997 1.00 45.81 ?  624 PHE B CA    1 
ATOM   10560 C  C     . PHE B 1 624 ? 124.307 127.739 178.286 1.00 44.60 ?  624 PHE B C     1 
ATOM   10561 O  O     . PHE B 1 624 ? 123.476 127.725 177.372 1.00 46.49 ?  624 PHE B O     1 
ATOM   10562 C  CB    . PHE B 1 624 ? 123.822 126.245 180.250 1.00 45.65 ?  624 PHE B CB    1 
ATOM   10563 C  CG    . PHE B 1 624 ? 122.459 126.874 180.170 1.00 48.58 ?  624 PHE B CG    1 
ATOM   10564 C  CD1   . PHE B 1 624 ? 121.396 126.178 179.618 1.00 49.31 ?  624 PHE B CD1   1 
ATOM   10565 C  CD2   . PHE B 1 624 ? 122.235 128.146 180.665 1.00 48.63 ?  624 PHE B CD2   1 
ATOM   10566 C  CE1   . PHE B 1 624 ? 120.138 126.747 179.549 1.00 47.90 ?  624 PHE B CE1   1 
ATOM   10567 C  CE2   . PHE B 1 624 ? 120.979 128.721 180.597 1.00 47.43 ?  624 PHE B CE2   1 
ATOM   10568 C  CZ    . PHE B 1 624 ? 119.931 128.020 180.038 1.00 46.39 ?  624 PHE B CZ    1 
ATOM   10569 N  N     . PHE B 1 625 ? 124.908 128.862 178.684 1.00 38.94 ?  625 PHE B N     1 
ATOM   10570 C  CA    . PHE B 1 625 ? 124.620 130.136 178.038 1.00 38.69 ?  625 PHE B CA    1 
ATOM   10571 C  C     . PHE B 1 625 ? 125.244 130.252 176.655 1.00 35.29 ?  625 PHE B C     1 
ATOM   10572 O  O     . PHE B 1 625 ? 124.797 131.083 175.858 1.00 38.56 ?  625 PHE B O     1 
ATOM   10573 C  CB    . PHE B 1 625 ? 125.093 131.294 178.918 1.00 35.61 ?  625 PHE B CB    1 
ATOM   10574 C  CG    . PHE B 1 625 ? 124.367 131.394 180.226 1.00 37.86 ?  625 PHE B CG    1 
ATOM   10575 C  CD1   . PHE B 1 625 ? 123.035 131.765 180.266 1.00 38.23 ?  625 PHE B CD1   1 
ATOM   10576 C  CD2   . PHE B 1 625 ? 125.014 131.114 181.417 1.00 37.04 ?  625 PHE B CD2   1 
ATOM   10577 C  CE1   . PHE B 1 625 ? 122.361 131.856 181.468 1.00 37.30 ?  625 PHE B CE1   1 
ATOM   10578 C  CE2   . PHE B 1 625 ? 124.346 131.204 182.622 1.00 36.47 ?  625 PHE B CE2   1 
ATOM   10579 C  CZ    . PHE B 1 625 ? 123.018 131.576 182.647 1.00 37.50 ?  625 PHE B CZ    1 
ATOM   10580 N  N     . TYR B 1 626 ? 126.257 129.449 176.348 1.00 33.35 ?  626 TYR B N     1 
ATOM   10581 C  CA    . TYR B 1 626 ? 126.826 129.415 175.002 1.00 32.87 ?  626 TYR B CA    1 
ATOM   10582 C  C     . TYR B 1 626 ? 126.044 128.467 174.102 1.00 33.99 ?  626 TYR B C     1 
ATOM   10583 O  O     . TYR B 1 626 ? 126.597 127.592 173.438 1.00 39.93 ?  626 TYR B O     1 
ATOM   10584 C  CB    . TYR B 1 626 ? 128.297 129.027 175.067 1.00 33.32 ?  626 TYR B CB    1 
ATOM   10585 C  CG    . TYR B 1 626 ? 129.230 130.214 175.108 1.00 34.82 ?  626 TYR B CG    1 
ATOM   10586 C  CD1   . TYR B 1 626 ? 129.409 131.015 173.989 1.00 36.36 ?  626 TYR B CD1   1 
ATOM   10587 C  CD2   . TYR B 1 626 ? 129.925 130.537 176.264 1.00 33.61 ?  626 TYR B CD2   1 
ATOM   10588 C  CE1   . TYR B 1 626 ? 130.258 132.101 174.019 1.00 34.23 ?  626 TYR B CE1   1 
ATOM   10589 C  CE2   . TYR B 1 626 ? 130.777 131.621 176.303 1.00 34.41 ?  626 TYR B CE2   1 
ATOM   10590 C  CZ    . TYR B 1 626 ? 130.939 132.399 175.178 1.00 34.99 ?  626 TYR B CZ    1 
ATOM   10591 O  OH    . TYR B 1 626 ? 131.783 133.483 175.208 1.00 38.39 ?  626 TYR B OH    1 
ATOM   10592 N  N     . LYS B 1 627 ? 124.730 128.658 174.070 1.00 35.65 ?  627 LYS B N     1 
ATOM   10593 C  CA    . LYS B 1 627 ? 123.860 127.810 173.273 1.00 34.10 ?  627 LYS B CA    1 
ATOM   10594 C  C     . LYS B 1 627 ? 124.128 128.024 171.789 1.00 35.17 ?  627 LYS B C     1 
ATOM   10595 O  O     . LYS B 1 627 ? 124.301 129.156 171.331 1.00 38.30 ?  627 LYS B O     1 
ATOM   10596 C  CB    . LYS B 1 627 ? 122.399 128.106 173.604 1.00 35.18 ?  627 LYS B CB    1 
ATOM   10597 C  CG    . LYS B 1 627 ? 121.391 127.228 172.894 1.00 33.73 ?  627 LYS B CG    1 
ATOM   10598 C  CD    . LYS B 1 627 ? 120.002 127.445 173.465 1.00 34.68 ?  627 LYS B CD    1 
ATOM   10599 C  CE    . LYS B 1 627 ? 118.960 126.632 172.724 1.00 41.48 ?  627 LYS B CE    1 
ATOM   10600 N  NZ    . LYS B 1 627 ? 117.592 126.897 173.244 1.00 40.15 1  627 LYS B NZ    1 
ATOM   10601 N  N     . GLU B 1 628 ? 124.175 126.929 171.039 1.00 40.55 ?  628 GLU B N     1 
ATOM   10602 C  CA    . GLU B 1 628 ? 124.446 127.019 169.613 1.00 38.37 ?  628 GLU B CA    1 
ATOM   10603 C  C     . GLU B 1 628 ? 123.239 127.581 168.869 1.00 39.30 ?  628 GLU B C     1 
ATOM   10604 O  O     . GLU B 1 628 ? 122.089 127.408 169.279 1.00 37.34 ?  628 GLU B O     1 
ATOM   10605 C  CB    . GLU B 1 628 ? 124.829 125.650 169.055 1.00 36.19 ?  628 GLU B CB    1 
ATOM   10606 C  CG    . GLU B 1 628 ? 126.325 125.388 169.068 1.00 40.59 ?  628 GLU B CG    1 
ATOM   10607 C  CD    . GLU B 1 628 ? 126.666 123.912 169.075 1.00 47.63 ?  628 GLU B CD    1 
ATOM   10608 O  OE1   . GLU B 1 628 ? 126.302 123.213 168.106 1.00 42.69 ?  628 GLU B OE1   1 
ATOM   10609 O  OE2   . GLU B 1 628 ? 127.301 123.451 170.046 1.00 44.14 -1 628 GLU B OE2   1 
ATOM   10610 N  N     . ALA B 1 629 ? 123.518 128.264 167.756 1.00 37.06 ?  629 ALA B N     1 
ATOM   10611 C  CA    . ALA B 1 629 ? 122.461 128.944 167.017 1.00 32.34 ?  629 ALA B CA    1 
ATOM   10612 C  C     . ALA B 1 629 ? 121.444 127.958 166.458 1.00 34.71 ?  629 ALA B C     1 
ATOM   10613 O  O     . ALA B 1 629 ? 120.239 128.232 166.456 1.00 40.09 ?  629 ALA B O     1 
ATOM   10614 C  CB    . ALA B 1 629 ? 123.066 129.786 165.894 1.00 31.60 ?  629 ALA B CB    1 
ATOM   10615 N  N     . TYR B 1 630 ? 121.910 126.807 165.970 1.00 43.03 ?  630 TYR B N     1 
ATOM   10616 C  CA    . TYR B 1 630 ? 120.997 125.835 165.379 1.00 36.11 ?  630 TYR B CA    1 
ATOM   10617 C  C     . TYR B 1 630 ? 120.000 125.287 166.390 1.00 39.06 ?  630 TYR B C     1 
ATOM   10618 O  O     . TYR B 1 630 ? 118.933 124.807 165.992 1.00 44.21 ?  630 TYR B O     1 
ATOM   10619 C  CB    . TYR B 1 630 ? 121.789 124.693 164.747 1.00 37.22 ?  630 TYR B CB    1 
ATOM   10620 C  CG    . TYR B 1 630 ? 122.696 125.143 163.627 1.00 38.40 ?  630 TYR B CG    1 
ATOM   10621 C  CD1   . TYR B 1 630 ? 122.181 125.486 162.387 1.00 37.47 ?  630 TYR B CD1   1 
ATOM   10622 C  CD2   . TYR B 1 630 ? 124.069 125.233 163.815 1.00 40.17 ?  630 TYR B CD2   1 
ATOM   10623 C  CE1   . TYR B 1 630 ? 123.006 125.902 161.363 1.00 39.22 ?  630 TYR B CE1   1 
ATOM   10624 C  CE2   . TYR B 1 630 ? 124.901 125.647 162.796 1.00 41.29 ?  630 TYR B CE2   1 
ATOM   10625 C  CZ    . TYR B 1 630 ? 124.364 125.979 161.573 1.00 43.58 ?  630 TYR B CZ    1 
ATOM   10626 O  OH    . TYR B 1 630 ? 125.191 126.391 160.555 1.00 49.19 ?  630 TYR B OH    1 
ATOM   10627 N  N     . ASP B 1 631 ? 120.319 125.345 167.681 1.00 40.43 ?  631 ASP B N     1 
ATOM   10628 C  CA    . ASP B 1 631 ? 119.405 124.891 168.718 1.00 38.00 ?  631 ASP B CA    1 
ATOM   10629 C  C     . ASP B 1 631 ? 118.473 125.986 169.219 1.00 40.61 ?  631 ASP B C     1 
ATOM   10630 O  O     . ASP B 1 631 ? 117.542 125.685 169.972 1.00 43.57 ?  631 ASP B O     1 
ATOM   10631 C  CB    . ASP B 1 631 ? 120.194 124.315 169.899 1.00 40.27 ?  631 ASP B CB    1 
ATOM   10632 C  CG    . ASP B 1 631 ? 120.912 123.028 169.545 1.00 47.12 ?  631 ASP B CG    1 
ATOM   10633 O  OD1   . ASP B 1 631 ? 120.331 122.209 168.801 1.00 46.94 ?  631 ASP B OD1   1 
ATOM   10634 O  OD2   . ASP B 1 631 ? 122.056 122.836 170.006 1.00 48.16 -1 631 ASP B OD2   1 
ATOM   10635 N  N     . MET B 1 632 ? 118.693 127.237 168.824 1.00 38.93 ?  632 MET B N     1 
ATOM   10636 C  CA    . MET B 1 632 ? 117.832 128.321 169.264 1.00 37.33 ?  632 MET B CA    1 
ATOM   10637 C  C     . MET B 1 632 ? 116.569 128.397 168.415 1.00 37.51 ?  632 MET B C     1 
ATOM   10638 O  O     . MET B 1 632 ? 116.505 127.891 167.291 1.00 37.13 ?  632 MET B O     1 
ATOM   10639 C  CB    . MET B 1 632 ? 118.557 129.667 169.203 1.00 35.31 ?  632 MET B CB    1 
ATOM   10640 C  CG    . MET B 1 632 ? 120.022 129.640 169.575 1.00 38.12 ?  632 MET B CG    1 
ATOM   10641 S  SD    . MET B 1 632 ? 120.440 131.105 170.537 1.00 43.25 ?  632 MET B SD    1 
ATOM   10642 C  CE    . MET B 1 632 ? 122.209 130.925 170.696 1.00 35.56 ?  632 MET B CE    1 
ATOM   10643 N  N     . ASP B 1 633 ? 115.554 129.049 168.975 1.00 31.55 ?  633 ASP B N     1 
ATOM   10644 C  CA    . ASP B 1 633 ? 114.341 129.367 168.237 1.00 30.10 ?  633 ASP B CA    1 
ATOM   10645 C  C     . ASP B 1 633 ? 114.616 130.551 167.319 1.00 33.88 ?  633 ASP B C     1 
ATOM   10646 O  O     . ASP B 1 633 ? 114.911 131.654 167.791 1.00 34.42 ?  633 ASP B O     1 
ATOM   10647 C  CB    . ASP B 1 633 ? 113.203 129.686 169.205 1.00 25.12 ?  633 ASP B CB    1 
ATOM   10648 C  CG    . ASP B 1 633 ? 111.876 129.888 168.502 1.00 34.63 ?  633 ASP B CG    1 
ATOM   10649 O  OD1   . ASP B 1 633 ? 111.832 129.782 167.260 1.00 39.73 ?  633 ASP B OD1   1 
ATOM   10650 O  OD2   . ASP B 1 633 ? 110.875 130.155 169.197 1.00 36.61 -1 633 ASP B OD2   1 
ATOM   10651 N  N     . MET B 1 634 ? 114.524 130.326 166.007 1.00 28.04 ?  634 MET B N     1 
ATOM   10652 C  CA    . MET B 1 634 ? 114.765 131.408 165.061 1.00 24.62 ?  634 MET B CA    1 
ATOM   10653 C  C     . MET B 1 634 ? 113.809 132.574 165.266 1.00 26.36 ?  634 MET B C     1 
ATOM   10654 O  O     . MET B 1 634 ? 114.134 133.699 164.875 1.00 27.24 ?  634 MET B O     1 
ATOM   10655 C  CB    . MET B 1 634 ? 114.667 130.892 163.626 1.00 28.12 ?  634 MET B CB    1 
ATOM   10656 C  CG    . MET B 1 634 ? 115.873 130.088 163.167 1.00 30.97 ?  634 MET B CG    1 
ATOM   10657 S  SD    . MET B 1 634 ? 117.428 130.979 163.390 1.00 47.17 ?  634 MET B SD    1 
ATOM   10658 C  CE    . MET B 1 634 ? 117.888 130.477 165.046 1.00 32.98 ?  634 MET B CE    1 
ATOM   10659 N  N     . PHE B 1 635 ? 112.641 132.338 165.864 1.00 26.72 ?  635 PHE B N     1 
ATOM   10660 C  CA    . PHE B 1 635 ? 111.756 133.448 166.197 1.00 25.15 ?  635 PHE B CA    1 
ATOM   10661 C  C     . PHE B 1 635 ? 112.381 134.348 167.255 1.00 26.26 ?  635 PHE B C     1 
ATOM   10662 O  O     . PHE B 1 635 ? 112.274 135.577 167.175 1.00 29.51 ?  635 PHE B O     1 
ATOM   10663 C  CB    . PHE B 1 635 ? 110.401 132.919 166.668 1.00 24.83 ?  635 PHE B CB    1 
ATOM   10664 C  CG    . PHE B 1 635 ? 109.448 132.620 165.549 1.00 30.69 ?  635 PHE B CG    1 
ATOM   10665 C  CD1   . PHE B 1 635 ? 109.878 131.956 164.413 1.00 29.13 ?  635 PHE B CD1   1 
ATOM   10666 C  CD2   . PHE B 1 635 ? 108.121 132.999 165.631 1.00 29.09 ?  635 PHE B CD2   1 
ATOM   10667 C  CE1   . PHE B 1 635 ? 109.005 131.678 163.382 1.00 26.04 ?  635 PHE B CE1   1 
ATOM   10668 C  CE2   . PHE B 1 635 ? 107.242 132.724 164.603 1.00 27.26 ?  635 PHE B CE2   1 
ATOM   10669 C  CZ    . PHE B 1 635 ? 107.685 132.062 163.477 1.00 23.89 ?  635 PHE B CZ    1 
ATOM   10670 N  N     . LYS B 1 636 ? 113.048 133.759 168.248 1.00 27.28 ?  636 LYS B N     1 
ATOM   10671 C  CA    . LYS B 1 636 ? 113.734 134.565 169.252 1.00 27.64 ?  636 LYS B CA    1 
ATOM   10672 C  C     . LYS B 1 636 ? 114.932 135.299 168.662 1.00 22.14 ?  636 LYS B C     1 
ATOM   10673 O  O     . LYS B 1 636 ? 115.215 136.438 169.050 1.00 30.50 ?  636 LYS B O     1 
ATOM   10674 C  CB    . LYS B 1 636 ? 114.165 133.684 170.422 1.00 28.82 ?  636 LYS B CB    1 
ATOM   10675 C  CG    . LYS B 1 636 ? 113.011 132.974 171.105 1.00 28.85 ?  636 LYS B CG    1 
ATOM   10676 C  CD    . LYS B 1 636 ? 112.061 133.973 171.743 1.00 31.55 ?  636 LYS B CD    1 
ATOM   10677 C  CE    . LYS B 1 636 ? 111.182 133.310 172.787 1.00 31.36 ?  636 LYS B CE    1 
ATOM   10678 N  NZ    . LYS B 1 636 ? 109.839 133.949 172.861 1.00 32.27 1  636 LYS B NZ    1 
ATOM   10679 N  N     . VAL B 1 637 ? 115.646 134.671 167.725 1.00 20.90 ?  637 VAL B N     1 
ATOM   10680 C  CA    . VAL B 1 637 ? 116.738 135.359 167.046 1.00 18.67 ?  637 VAL B CA    1 
ATOM   10681 C  C     . VAL B 1 637 ? 116.200 136.525 166.229 1.00 25.02 ?  637 VAL B C     1 
ATOM   10682 O  O     . VAL B 1 637 ? 116.813 137.598 166.166 1.00 29.21 ?  637 VAL B O     1 
ATOM   10683 C  CB    . VAL B 1 637 ? 117.532 134.369 166.174 1.00 23.17 ?  637 VAL B CB    1 
ATOM   10684 C  CG1   . VAL B 1 637 ? 118.711 135.067 165.516 1.00 23.85 ?  637 VAL B CG1   1 
ATOM   10685 C  CG2   . VAL B 1 637 ? 117.997 133.186 167.008 1.00 23.94 ?  637 VAL B CG2   1 
ATOM   10686 N  N     . VAL B 1 638 ? 115.045 136.334 165.588 1.00 25.79 ?  638 VAL B N     1 
ATOM   10687 C  CA    . VAL B 1 638 ? 114.408 137.421 164.853 1.00 22.29 ?  638 VAL B CA    1 
ATOM   10688 C  C     . VAL B 1 638 ? 114.009 138.539 165.804 1.00 17.41 ?  638 VAL B C     1 
ATOM   10689 O  O     . VAL B 1 638 ? 114.148 139.723 165.484 1.00 27.40 ?  638 VAL B O     1 
ATOM   10690 C  CB    . VAL B 1 638 ? 113.197 136.897 164.059 1.00 22.52 ?  638 VAL B CB    1 
ATOM   10691 C  CG1   . VAL B 1 638 ? 112.332 138.052 163.590 1.00 15.31 ?  638 VAL B CG1   1 
ATOM   10692 C  CG2   . VAL B 1 638 ? 113.657 136.056 162.882 1.00 22.52 ?  638 VAL B CG2   1 
ATOM   10693 N  N     . ASP B 1 639 ? 113.499 138.183 166.982 1.00 17.93 ?  639 ASP B N     1 
ATOM   10694 C  CA    . ASP B 1 639 ? 113.151 139.196 167.975 1.00 20.95 ?  639 ASP B CA    1 
ATOM   10695 C  C     . ASP B 1 639 ? 114.378 139.996 168.394 1.00 26.09 ?  639 ASP B C     1 
ATOM   10696 O  O     . ASP B 1 639 ? 114.324 141.226 168.504 1.00 30.13 ?  639 ASP B O     1 
ATOM   10697 C  CB    . ASP B 1 639 ? 112.503 138.535 169.190 1.00 20.34 ?  639 ASP B CB    1 
ATOM   10698 C  CG    . ASP B 1 639 ? 111.059 138.159 168.946 1.00 29.42 ?  639 ASP B CG    1 
ATOM   10699 O  OD1   . ASP B 1 639 ? 110.362 138.909 168.231 1.00 31.81 ?  639 ASP B OD1   1 
ATOM   10700 O  OD2   . ASP B 1 639 ? 110.620 137.112 169.465 1.00 34.59 -1 639 ASP B OD2   1 
ATOM   10701 N  N     . MET B 1 640 ? 115.498 139.310 168.624 1.00 22.94 ?  640 MET B N     1 
ATOM   10702 C  CA    . MET B 1 640 ? 116.735 139.997 168.980 1.00 20.96 ?  640 MET B CA    1 
ATOM   10703 C  C     . MET B 1 640 ? 117.183 140.937 167.868 1.00 22.74 ?  640 MET B C     1 
ATOM   10704 O  O     . MET B 1 640 ? 117.513 142.104 168.115 1.00 30.55 ?  640 MET B O     1 
ATOM   10705 C  CB    . MET B 1 640 ? 117.824 138.969 169.287 1.00 22.71 ?  640 MET B CB    1 
ATOM   10706 C  CG    . MET B 1 640 ? 119.166 139.572 169.655 1.00 27.19 ?  640 MET B CG    1 
ATOM   10707 S  SD    . MET B 1 640 ? 119.034 140.865 170.898 1.00 34.39 ?  640 MET B SD    1 
ATOM   10708 C  CE    . MET B 1 640 ? 120.040 140.158 172.195 1.00 25.24 ?  640 MET B CE    1 
ATOM   10709 N  N     . ILE B 1 641 ? 117.202 140.442 166.629 1.00 17.21 ?  641 ILE B N     1 
ATOM   10710 C  CA    . ILE B 1 641 ? 117.672 141.257 165.514 1.00 17.72 ?  641 ILE B CA    1 
ATOM   10711 C  C     . ILE B 1 641 ? 116.747 142.444 165.282 1.00 21.72 ?  641 ILE B C     1 
ATOM   10712 O  O     . ILE B 1 641 ? 117.203 143.529 164.906 1.00 28.09 ?  641 ILE B O     1 
ATOM   10713 C  CB    . ILE B 1 641 ? 117.818 140.395 164.248 1.00 24.79 ?  641 ILE B CB    1 
ATOM   10714 C  CG1   . ILE B 1 641 ? 118.802 139.249 164.498 1.00 21.23 ?  641 ILE B CG1   1 
ATOM   10715 C  CG2   . ILE B 1 641 ? 118.272 141.245 163.076 1.00 10.32 ?  641 ILE B CG2   1 
ATOM   10716 C  CD1   . ILE B 1 641 ? 120.041 139.664 165.255 1.00 16.62 ?  641 ILE B CD1   1 
ATOM   10717 N  N     . ALA B 1 642 ? 115.442 142.266 165.498 1.00 18.90 ?  642 ALA B N     1 
ATOM   10718 C  CA    . ALA B 1 642 ? 114.510 143.376 165.348 1.00 19.67 ?  642 ALA B CA    1 
ATOM   10719 C  C     . ALA B 1 642 ? 114.698 144.400 166.457 1.00 17.81 ?  642 ALA B C     1 
ATOM   10720 O  O     . ALA B 1 642 ? 114.585 145.608 166.219 1.00 26.10 ?  642 ALA B O     1 
ATOM   10721 C  CB    . ALA B 1 642 ? 113.074 142.855 165.334 1.00 15.09 ?  642 ALA B CB    1 
ATOM   10722 N  N     . THR B 1 643 ? 114.985 143.938 167.676 1.00 16.79 ?  643 THR B N     1 
ATOM   10723 C  CA    . THR B 1 643 ? 115.310 144.868 168.750 1.00 18.30 ?  643 THR B CA    1 
ATOM   10724 C  C     . THR B 1 643 ? 116.554 145.677 168.408 1.00 21.13 ?  643 THR B C     1 
ATOM   10725 O  O     . THR B 1 643 ? 116.598 146.892 168.638 1.00 21.57 ?  643 THR B O     1 
ATOM   10726 C  CB    . THR B 1 643 ? 115.505 144.111 170.064 1.00 17.52 ?  643 THR B CB    1 
ATOM   10727 O  OG1   . THR B 1 643 ? 114.268 143.507 170.459 1.00 28.55 ?  643 THR B OG1   1 
ATOM   10728 C  CG2   . THR B 1 643 ? 115.969 145.055 171.156 1.00 16.71 ?  643 THR B CG2   1 
ATOM   10729 N  N     . ILE B 1 644 ? 117.574 145.021 167.854 1.00 15.63 ?  644 ILE B N     1 
ATOM   10730 C  CA    . ILE B 1 644 ? 118.781 145.737 167.455 1.00 14.44 ?  644 ILE B CA    1 
ATOM   10731 C  C     . ILE B 1 644 ? 118.505 146.629 166.252 1.00 14.28 ?  644 ILE B C     1 
ATOM   10732 O  O     . ILE B 1 644 ? 118.950 147.781 166.201 1.00 16.38 ?  644 ILE B O     1 
ATOM   10733 C  CB    . ILE B 1 644 ? 119.923 144.744 167.172 1.00 19.50 ?  644 ILE B CB    1 
ATOM   10734 C  CG1   . ILE B 1 644 ? 120.236 143.918 168.420 1.00 14.69 ?  644 ILE B CG1   1 
ATOM   10735 C  CG2   . ILE B 1 644 ? 121.159 145.480 166.679 1.00 8.25  ?  644 ILE B CG2   1 
ATOM   10736 C  CD1   . ILE B 1 644 ? 121.103 142.717 168.146 1.00 16.97 ?  644 ILE B CD1   1 
ATOM   10737 N  N     . GLN B 1 645 ? 117.762 146.116 165.268 1.00 14.63 ?  645 GLN B N     1 
ATOM   10738 C  CA    . GLN B 1 645 ? 117.567 146.838 164.017 1.00 12.96 ?  645 GLN B CA    1 
ATOM   10739 C  C     . GLN B 1 645 ? 116.830 148.157 164.201 1.00 19.07 ?  645 GLN B C     1 
ATOM   10740 O  O     . GLN B 1 645 ? 116.968 149.049 163.358 1.00 20.99 ?  645 GLN B O     1 
ATOM   10741 C  CB    . GLN B 1 645 ? 116.813 145.962 163.016 1.00 10.51 ?  645 GLN B CB    1 
ATOM   10742 C  CG    . GLN B 1 645 ? 116.571 146.634 161.677 1.00 4.60  ?  645 GLN B CG    1 
ATOM   10743 C  CD    . GLN B 1 645 ? 117.814 146.671 160.813 1.00 10.57 ?  645 GLN B CD    1 
ATOM   10744 O  OE1   . GLN B 1 645 ? 118.204 145.664 160.225 1.00 16.66 ?  645 GLN B OE1   1 
ATOM   10745 N  NE2   . GLN B 1 645 ? 118.445 147.835 160.734 1.00 10.79 ?  645 GLN B NE2   1 
ATOM   10746 N  N     . GLN B 1 646 ? 116.056 148.309 165.274 1.00 21.32 ?  646 GLN B N     1 
ATOM   10747 C  CA    . GLN B 1 646 ? 115.339 149.559 165.485 1.00 17.28 ?  646 GLN B CA    1 
ATOM   10748 C  C     . GLN B 1 646 ? 116.267 150.720 165.814 1.00 12.89 ?  646 GLN B C     1 
ATOM   10749 O  O     . GLN B 1 646 ? 115.814 151.869 165.814 1.00 20.93 ?  646 GLN B O     1 
ATOM   10750 C  CB    . GLN B 1 646 ? 114.300 149.386 166.593 1.00 19.06 ?  646 GLN B CB    1 
ATOM   10751 C  CG    . GLN B 1 646 ? 114.875 149.360 167.992 1.00 20.29 ?  646 GLN B CG    1 
ATOM   10752 C  CD    . GLN B 1 646 ? 113.813 149.138 169.046 1.00 29.54 ?  646 GLN B CD    1 
ATOM   10753 O  OE1   . GLN B 1 646 ? 112.938 149.979 169.248 1.00 32.67 ?  646 GLN B OE1   1 
ATOM   10754 N  NE2   . GLN B 1 646 ? 113.884 148.001 169.727 1.00 23.57 ?  646 GLN B NE2   1 
ATOM   10755 N  N     . HIS B 1 647 ? 117.543 150.454 166.089 1.00 22.06 ?  647 HIS B N     1 
ATOM   10756 C  CA    . HIS B 1 647 ? 118.518 151.500 166.362 1.00 14.27 ?  647 HIS B CA    1 
ATOM   10757 C  C     . HIS B 1 647 ? 119.615 151.577 165.312 1.00 10.77 ?  647 HIS B C     1 
ATOM   10758 O  O     . HIS B 1 647 ? 120.541 152.380 165.465 1.00 26.29 ?  647 HIS B O     1 
ATOM   10759 C  CB    . HIS B 1 647 ? 119.148 151.293 167.746 1.00 12.82 ?  647 HIS B CB    1 
ATOM   10760 C  CG    . HIS B 1 647 ? 118.147 151.099 168.841 1.00 13.80 ?  647 HIS B CG    1 
ATOM   10761 N  ND1   . HIS B 1 647 ? 117.222 152.062 169.181 1.00 18.26 ?  647 HIS B ND1   1 
ATOM   10762 C  CD2   . HIS B 1 647 ? 117.924 150.054 169.670 1.00 11.62 ?  647 HIS B CD2   1 
ATOM   10763 C  CE1   . HIS B 1 647 ? 116.472 151.618 170.174 1.00 17.47 ?  647 HIS B CE1   1 
ATOM   10764 N  NE2   . HIS B 1 647 ? 116.879 150.401 170.490 1.00 17.45 ?  647 HIS B NE2   1 
ATOM   10765 N  N     . ILE B 1 648 ? 119.541 150.772 164.258 1.00 10.38 ?  648 ILE B N     1 
ATOM   10766 C  CA    . ILE B 1 648 ? 120.509 150.782 163.168 1.00 14.01 ?  648 ILE B CA    1 
ATOM   10767 C  C     . ILE B 1 648 ? 119.850 151.436 161.963 1.00 13.88 ?  648 ILE B C     1 
ATOM   10768 O  O     . ILE B 1 648 ? 118.764 151.021 161.543 1.00 25.64 ?  648 ILE B O     1 
ATOM   10769 C  CB    . ILE B 1 648 ? 120.989 149.359 162.831 1.00 14.38 ?  648 ILE B CB    1 
ATOM   10770 C  CG1   . ILE B 1 648 ? 121.479 148.642 164.092 1.00 12.21 ?  648 ILE B CG1   1 
ATOM   10771 C  CG2   . ILE B 1 648 ? 122.078 149.393 161.768 1.00 1.05  ?  648 ILE B CG2   1 
ATOM   10772 C  CD1   . ILE B 1 648 ? 122.657 149.310 164.758 1.00 4.99  ?  648 ILE B CD1   1 
ATOM   10773 N  N     . ASP B 1 649 ? 120.498 152.464 161.412 1.00 11.72 ?  649 ASP B N     1 
ATOM   10774 C  CA    . ASP B 1 649 ? 119.934 153.131 160.243 1.00 4.81  ?  649 ASP B CA    1 
ATOM   10775 C  C     . ASP B 1 649 ? 120.077 152.279 158.990 1.00 12.21 ?  649 ASP B C     1 
ATOM   10776 O  O     . ASP B 1 649 ? 119.210 152.320 158.111 1.00 32.78 ?  649 ASP B O     1 
ATOM   10777 C  CB    . ASP B 1 649 ? 120.591 154.498 160.043 1.00 19.29 ?  649 ASP B CB    1 
ATOM   10778 C  CG    . ASP B 1 649 ? 122.094 154.457 160.226 1.00 16.57 ?  649 ASP B CG    1 
ATOM   10779 O  OD1   . ASP B 1 649 ? 122.578 153.569 160.955 1.00 23.29 ?  649 ASP B OD1   1 
ATOM   10780 O  OD2   . ASP B 1 649 ? 122.790 155.309 159.641 1.00 17.59 -1 649 ASP B OD2   1 
ATOM   10781 N  N     . GLN B 1 650 ? 121.162 151.521 158.885 1.00 12.81 ?  650 GLN B N     1 
ATOM   10782 C  CA    . GLN B 1 650 ? 121.336 150.541 157.826 1.00 6.04  ?  650 GLN B CA    1 
ATOM   10783 C  C     . GLN B 1 650 ? 120.841 149.180 158.311 1.00 11.69 ?  650 GLN B C     1 
ATOM   10784 O  O     . GLN B 1 650 ? 120.154 149.069 159.329 1.00 21.12 ?  650 GLN B O     1 
ATOM   10785 C  CB    . GLN B 1 650 ? 122.790 150.507 157.370 1.00 8.18  ?  650 GLN B CB    1 
ATOM   10786 C  CG    . GLN B 1 650 ? 123.199 151.718 156.556 1.00 6.23  ?  650 GLN B CG    1 
ATOM   10787 C  CD    . GLN B 1 650 ? 124.627 151.634 156.075 1.00 12.62 ?  650 GLN B CD    1 
ATOM   10788 O  OE1   . GLN B 1 650 ? 124.924 150.941 155.105 1.00 20.40 ?  650 GLN B OE1   1 
ATOM   10789 N  NE2   . GLN B 1 650 ? 125.523 152.343 156.750 1.00 2.98  ?  650 GLN B NE2   1 
ATOM   10790 N  N     . GLY B 1 651 ? 121.168 148.126 157.571 1.00 3.14  ?  651 GLY B N     1 
ATOM   10791 C  CA    . GLY B 1 651 ? 120.696 146.803 157.913 1.00 7.19  ?  651 GLY B CA    1 
ATOM   10792 C  C     . GLY B 1 651 ? 121.637 146.030 158.823 1.00 12.88 ?  651 GLY B C     1 
ATOM   10793 O  O     . GLY B 1 651 ? 122.741 146.459 159.146 1.00 9.14  ?  651 GLY B O     1 
ATOM   10794 N  N     . ILE B 1 652 ? 121.156 144.866 159.249 1.00 19.38 ?  652 ILE B N     1 
ATOM   10795 C  CA    . ILE B 1 652 ? 121.919 143.918 160.049 1.00 8.24  ?  652 ILE B CA    1 
ATOM   10796 C  C     . ILE B 1 652 ? 122.034 142.628 159.254 1.00 9.72  ?  652 ILE B C     1 
ATOM   10797 O  O     . ILE B 1 652 ? 121.023 142.089 158.791 1.00 25.81 ?  652 ILE B O     1 
ATOM   10798 C  CB    . ILE B 1 652 ? 121.258 143.656 161.415 1.00 6.05  ?  652 ILE B CB    1 
ATOM   10799 C  CG1   . ILE B 1 652 ? 121.017 144.971 162.159 1.00 2.68  ?  652 ILE B CG1   1 
ATOM   10800 C  CG2   . ILE B 1 652 ? 122.102 142.699 162.241 1.00 11.56 ?  652 ILE B CG2   1 
ATOM   10801 C  CD1   . ILE B 1 652 ? 120.247 144.809 163.444 1.00 11.61 ?  652 ILE B CD1   1 
ATOM   10802 N  N     . SER B 1 653 ? 123.258 142.139 159.089 1.00 7.44  ?  653 SER B N     1 
ATOM   10803 C  CA    . SER B 1 653 ? 123.488 140.913 158.330 1.00 14.49 ?  653 SER B CA    1 
ATOM   10804 C  C     . SER B 1 653 ? 122.958 139.740 159.146 1.00 15.71 ?  653 SER B C     1 
ATOM   10805 O  O     . SER B 1 653 ? 123.595 139.287 160.099 1.00 24.68 ?  653 SER B O     1 
ATOM   10806 C  CB    . SER B 1 653 ? 124.970 140.758 158.012 1.00 14.21 ?  653 SER B CB    1 
ATOM   10807 O  OG    . SER B 1 653 ? 125.240 139.499 157.430 1.00 24.33 ?  653 SER B OG    1 
ATOM   10808 N  N     . PHE B 1 654 ? 121.783 139.244 158.769 1.00 23.37 ?  654 PHE B N     1 
ATOM   10809 C  CA    . PHE B 1 654 ? 121.019 138.291 159.566 1.00 14.71 ?  654 PHE B CA    1 
ATOM   10810 C  C     . PHE B 1 654 ? 121.060 136.930 158.883 1.00 16.20 ?  654 PHE B C     1 
ATOM   10811 O  O     . PHE B 1 654 ? 120.437 136.736 157.834 1.00 20.84 ?  654 PHE B O     1 
ATOM   10812 C  CB    . PHE B 1 654 ? 119.584 138.782 159.743 1.00 16.57 ?  654 PHE B CB    1 
ATOM   10813 C  CG    . PHE B 1 654 ? 118.748 137.926 160.650 1.00 19.78 ?  654 PHE B CG    1 
ATOM   10814 C  CD1   . PHE B 1 654 ? 119.329 136.958 161.450 1.00 18.26 ?  654 PHE B CD1   1 
ATOM   10815 C  CD2   . PHE B 1 654 ? 117.377 138.100 160.709 1.00 21.61 ?  654 PHE B CD2   1 
ATOM   10816 C  CE1   . PHE B 1 654 ? 118.560 136.176 162.283 1.00 16.99 ?  654 PHE B CE1   1 
ATOM   10817 C  CE2   . PHE B 1 654 ? 116.602 137.321 161.543 1.00 21.82 ?  654 PHE B CE2   1 
ATOM   10818 C  CZ    . PHE B 1 654 ? 117.194 136.357 162.332 1.00 17.92 ?  654 PHE B CZ    1 
ATOM   10819 N  N     . THR B 1 655 ? 121.792 135.994 159.478 1.00 19.89 ?  655 THR B N     1 
ATOM   10820 C  CA    . THR B 1 655 ? 121.857 134.620 159.002 1.00 25.70 ?  655 THR B CA    1 
ATOM   10821 C  C     . THR B 1 655 ? 120.844 133.770 159.758 1.00 25.03 ?  655 THR B C     1 
ATOM   10822 O  O     . THR B 1 655 ? 120.717 133.888 160.980 1.00 27.08 ?  655 THR B O     1 
ATOM   10823 C  CB    . THR B 1 655 ? 123.261 134.042 159.183 1.00 28.46 ?  655 THR B CB    1 
ATOM   10824 O  OG1   . THR B 1 655 ? 124.168 134.690 158.284 1.00 35.08 ?  655 THR B OG1   1 
ATOM   10825 C  CG2   . THR B 1 655 ? 123.263 132.547 158.907 1.00 26.29 ?  655 THR B CG2   1 
ATOM   10826 N  N     . LEU B 1 656 ? 120.122 132.926 159.029 1.00 31.89 ?  656 LEU B N     1 
ATOM   10827 C  CA    . LEU B 1 656 ? 119.199 131.968 159.622 1.00 33.03 ?  656 LEU B CA    1 
ATOM   10828 C  C     . LEU B 1 656 ? 119.892 130.620 159.759 1.00 30.07 ?  656 LEU B C     1 
ATOM   10829 O  O     . LEU B 1 656 ? 120.488 130.120 158.799 1.00 27.19 ?  656 LEU B O     1 
ATOM   10830 C  CB    . LEU B 1 656 ? 117.928 131.829 158.782 1.00 28.69 ?  656 LEU B CB    1 
ATOM   10831 C  CG    . LEU B 1 656 ? 117.250 133.123 158.335 1.00 31.82 ?  656 LEU B CG    1 
ATOM   10832 C  CD1   . LEU B 1 656 ? 116.055 132.820 157.449 1.00 31.07 ?  656 LEU B CD1   1 
ATOM   10833 C  CD2   . LEU B 1 656 ? 116.831 133.950 159.540 1.00 29.14 ?  656 LEU B CD2   1 
ATOM   10834 N  N     . PHE B 1 657 ? 119.813 130.039 160.950 1.00 30.53 ?  657 PHE B N     1 
ATOM   10835 C  CA    . PHE B 1 657 ? 120.442 128.760 161.255 1.00 32.61 ?  657 PHE B CA    1 
ATOM   10836 C  C     . PHE B 1 657 ? 119.345 127.710 161.368 1.00 37.30 ?  657 PHE B C     1 
ATOM   10837 O  O     . PHE B 1 657 ? 118.575 127.710 162.335 1.00 39.71 ?  657 PHE B O     1 
ATOM   10838 C  CB    . PHE B 1 657 ? 121.265 128.858 162.538 1.00 31.21 ?  657 PHE B CB    1 
ATOM   10839 C  CG    . PHE B 1 657 ? 122.244 129.995 162.534 1.00 36.49 ?  657 PHE B CG    1 
ATOM   10840 C  CD1   . PHE B 1 657 ? 123.488 129.853 161.947 1.00 35.34 ?  657 PHE B CD1   1 
ATOM   10841 C  CD2   . PHE B 1 657 ? 121.913 131.212 163.106 1.00 35.48 ?  657 PHE B CD2   1 
ATOM   10842 C  CE1   . PHE B 1 657 ? 124.386 130.899 161.936 1.00 36.47 ?  657 PHE B CE1   1 
ATOM   10843 C  CE2   . PHE B 1 657 ? 122.808 132.261 163.099 1.00 31.97 ?  657 PHE B CE2   1 
ATOM   10844 C  CZ    . PHE B 1 657 ? 124.046 132.105 162.513 1.00 35.90 ?  657 PHE B CZ    1 
ATOM   10845 N  N     . LEU B 1 658 ? 119.280 126.818 160.386 1.00 39.59 ?  658 LEU B N     1 
ATOM   10846 C  CA    . LEU B 1 658 ? 118.186 125.869 160.252 1.00 40.20 ?  658 LEU B CA    1 
ATOM   10847 C  C     . LEU B 1 658 ? 118.672 124.450 160.506 1.00 41.79 ?  658 LEU B C     1 
ATOM   10848 O  O     . LEU B 1 658 ? 119.780 124.080 160.107 1.00 42.26 ?  658 LEU B O     1 
ATOM   10849 C  CB    . LEU B 1 658 ? 117.564 125.953 158.857 1.00 40.83 ?  658 LEU B CB    1 
ATOM   10850 C  CG    . LEU B 1 658 ? 117.379 127.357 158.284 1.00 37.69 ?  658 LEU B CG    1 
ATOM   10851 C  CD1   . LEU B 1 658 ? 117.041 127.287 156.806 1.00 40.23 ?  658 LEU B CD1   1 
ATOM   10852 C  CD2   . LEU B 1 658 ? 116.302 128.101 159.049 1.00 37.22 ?  658 LEU B CD2   1 
ATOM   10853 N  N     . LYS B 1 659 ? 117.838 123.663 161.178 1.00 51.50 ?  659 LYS B N     1 
ATOM   10854 C  CA    . LYS B 1 659 ? 118.075 122.234 161.297 1.00 50.52 ?  659 LYS B CA    1 
ATOM   10855 C  C     . LYS B 1 659 ? 117.601 121.522 160.036 1.00 51.93 ?  659 LYS B C     1 
ATOM   10856 O  O     . LYS B 1 659 ? 116.696 121.987 159.338 1.00 53.11 ?  659 LYS B O     1 
ATOM   10857 C  CB    . LYS B 1 659 ? 117.361 121.670 162.524 1.00 51.46 ?  659 LYS B CB    1 
ATOM   10858 C  CG    . LYS B 1 659 ? 117.928 122.159 163.846 1.00 51.93 ?  659 LYS B CG    1 
ATOM   10859 C  CD    . LYS B 1 659 ? 117.384 121.356 165.016 1.00 52.36 ?  659 LYS B CD    1 
ATOM   10860 C  CE    . LYS B 1 659 ? 118.043 121.770 166.322 1.00 51.66 ?  659 LYS B CE    1 
ATOM   10861 N  NZ    . LYS B 1 659 ? 117.789 120.786 167.411 1.00 53.66 1  659 LYS B NZ    1 
ATOM   10862 N  N     . ASP B 1 660 ? 118.228 120.382 159.743 1.00 58.94 ?  660 ASP B N     1 
ATOM   10863 C  CA    . ASP B 1 660 ? 117.879 119.638 158.539 1.00 58.85 ?  660 ASP B CA    1 
ATOM   10864 C  C     . ASP B 1 660 ? 116.448 119.119 158.570 1.00 56.88 ?  660 ASP B C     1 
ATOM   10865 O  O     . ASP B 1 660 ? 115.870 118.870 157.507 1.00 55.28 ?  660 ASP B O     1 
ATOM   10866 C  CB    . ASP B 1 660 ? 118.851 118.475 158.334 1.00 58.84 ?  660 ASP B CB    1 
ATOM   10867 C  CG    . ASP B 1 660 ? 118.743 117.426 159.424 1.00 60.24 ?  660 ASP B CG    1 
ATOM   10868 O  OD1   . ASP B 1 660 ? 118.615 117.805 160.607 1.00 60.14 ?  660 ASP B OD1   1 
ATOM   10869 O  OD2   . ASP B 1 660 ? 118.785 116.222 159.095 1.00 59.40 -1 660 ASP B OD2   1 
ATOM   10870 N  N     . THR B 1 661 ? 115.865 118.950 159.758 1.00 53.33 ?  661 THR B N     1 
ATOM   10871 C  CA    . THR B 1 661 ? 114.492 118.473 159.852 1.00 55.16 ?  661 THR B CA    1 
ATOM   10872 C  C     . THR B 1 661 ? 113.477 119.539 159.463 1.00 56.84 ?  661 THR B C     1 
ATOM   10873 O  O     . THR B 1 661 ? 112.339 119.198 159.123 1.00 58.24 ?  661 THR B O     1 
ATOM   10874 C  CB    . THR B 1 661 ? 114.198 117.981 161.270 1.00 57.48 ?  661 THR B CB    1 
ATOM   10875 O  OG1   . THR B 1 661 ? 114.543 119.003 162.213 1.00 56.19 ?  661 THR B OG1   1 
ATOM   10876 C  CG2   . THR B 1 661 ? 115.004 116.727 161.575 1.00 58.13 ?  661 THR B CG2   1 
ATOM   10877 N  N     . MET B 1 662 ? 113.856 120.812 159.506 1.00 55.54 ?  662 MET B N     1 
ATOM   10878 C  CA    . MET B 1 662 ? 112.924 121.881 159.184 1.00 52.24 ?  662 MET B CA    1 
ATOM   10879 C  C     . MET B 1 662 ? 112.523 121.824 157.715 1.00 53.85 ?  662 MET B C     1 
ATOM   10880 O  O     . MET B 1 662 ? 113.366 121.653 156.830 1.00 54.64 ?  662 MET B O     1 
ATOM   10881 C  CB    . MET B 1 662 ? 113.543 123.240 159.507 1.00 51.99 ?  662 MET B CB    1 
ATOM   10882 C  CG    . MET B 1 662 ? 113.825 123.459 160.983 1.00 52.79 ?  662 MET B CG    1 
ATOM   10883 S  SD    . MET B 1 662 ? 113.821 125.205 161.428 1.00 58.42 ?  662 MET B SD    1 
ATOM   10884 C  CE    . MET B 1 662 ? 113.792 125.961 159.806 1.00 53.45 ?  662 MET B CE    1 
ATOM   10885 N  N     . THR B 1 663 ? 111.226 121.969 157.462 1.00 47.28 ?  663 THR B N     1 
ATOM   10886 C  CA    . THR B 1 663 ? 110.701 121.970 156.107 1.00 43.39 ?  663 THR B CA    1 
ATOM   10887 C  C     . THR B 1 663 ? 110.811 123.368 155.502 1.00 43.35 ?  663 THR B C     1 
ATOM   10888 O  O     . THR B 1 663 ? 111.240 124.325 156.151 1.00 46.72 ?  663 THR B O     1 
ATOM   10889 C  CB    . THR B 1 663 ? 109.252 121.487 156.099 1.00 39.57 ?  663 THR B CB    1 
ATOM   10890 O  OG1   . THR B 1 663 ? 108.421 122.456 156.746 1.00 43.13 ?  663 THR B OG1   1 
ATOM   10891 C  CG2   . THR B 1 663 ? 109.131 120.160 156.832 1.00 45.54 ?  663 THR B CG2   1 
ATOM   10892 N  N     . THR B 1 664 ? 110.421 123.490 154.231 1.00 38.91 ?  664 THR B N     1 
ATOM   10893 C  CA    . THR B 1 664 ? 110.370 124.809 153.611 1.00 41.37 ?  664 THR B CA    1 
ATOM   10894 C  C     . THR B 1 664 ? 109.309 125.684 154.264 1.00 39.62 ?  664 THR B C     1 
ATOM   10895 O  O     . THR B 1 664 ? 109.423 126.915 154.247 1.00 44.36 ?  664 THR B O     1 
ATOM   10896 C  CB    . THR B 1 664 ? 110.100 124.687 152.111 1.00 41.23 ?  664 THR B CB    1 
ATOM   10897 O  OG1   . THR B 1 664 ? 108.903 123.930 151.900 1.00 43.25 ?  664 THR B OG1   1 
ATOM   10898 C  CG2   . THR B 1 664 ? 111.262 123.994 151.416 1.00 38.84 ?  664 THR B CG2   1 
ATOM   10899 N  N     . ARG B 1 665 ? 108.276 125.069 154.842 1.00 36.49 ?  665 ARG B N     1 
ATOM   10900 C  CA    . ARG B 1 665 ? 107.246 125.838 155.530 1.00 36.86 ?  665 ARG B CA    1 
ATOM   10901 C  C     . ARG B 1 665 ? 107.816 126.559 156.744 1.00 39.76 ?  665 ARG B C     1 
ATOM   10902 O  O     . ARG B 1 665 ? 107.446 127.703 157.023 1.00 41.27 ?  665 ARG B O     1 
ATOM   10903 C  CB    . ARG B 1 665 ? 106.092 124.925 155.939 1.00 38.10 ?  665 ARG B CB    1 
ATOM   10904 C  CG    . ARG B 1 665 ? 104.766 125.646 156.100 1.00 36.53 ?  665 ARG B CG    1 
ATOM   10905 C  CD    . ARG B 1 665 ? 104.437 125.867 157.564 1.00 38.49 ?  665 ARG B CD    1 
ATOM   10906 N  NE    . ARG B 1 665 ? 103.001 125.834 157.812 1.00 42.07 ?  665 ARG B NE    1 
ATOM   10907 C  CZ    . ARG B 1 665 ? 102.449 125.835 159.017 1.00 45.10 ?  665 ARG B CZ    1 
ATOM   10908 N  NH1   . ARG B 1 665 ? 103.186 125.863 160.116 1.00 42.39 1  665 ARG B NH1   1 
ATOM   10909 N  NH2   . ARG B 1 665 ? 101.124 125.813 159.124 1.00 43.33 ?  665 ARG B NH2   1 
ATOM   10910 N  N     . ASP B 1 666 ? 108.711 125.904 157.486 1.00 36.65 ?  666 ASP B N     1 
ATOM   10911 C  CA    . ASP B 1 666 ? 109.330 126.553 158.637 1.00 34.59 ?  666 ASP B CA    1 
ATOM   10912 C  C     . ASP B 1 666 ? 110.187 127.738 158.208 1.00 40.74 ?  666 ASP B C     1 
ATOM   10913 O  O     . ASP B 1 666 ? 110.170 128.793 158.852 1.00 43.95 ?  666 ASP B O     1 
ATOM   10914 C  CB    . ASP B 1 666 ? 110.163 125.541 159.421 1.00 40.89 ?  666 ASP B CB    1 
ATOM   10915 C  CG    . ASP B 1 666 ? 109.349 124.351 159.883 1.00 47.71 ?  666 ASP B CG    1 
ATOM   10916 O  OD1   . ASP B 1 666 ? 108.273 124.562 160.479 1.00 46.44 ?  666 ASP B OD1   1 
ATOM   10917 O  OD2   . ASP B 1 666 ? 109.784 123.204 159.647 1.00 50.11 -1 666 ASP B OD2   1 
ATOM   10918 N  N     . LEU B 1 667 ? 110.945 127.581 157.123 1.00 34.79 ?  667 LEU B N     1 
ATOM   10919 C  CA    . LEU B 1 667 ? 111.738 128.692 156.608 1.00 27.67 ?  667 LEU B CA    1 
ATOM   10920 C  C     . LEU B 1 667 ? 110.842 129.843 156.165 1.00 30.07 ?  667 LEU B C     1 
ATOM   10921 O  O     . LEU B 1 667 ? 111.143 131.013 156.426 1.00 36.06 ?  667 LEU B O     1 
ATOM   10922 C  CB    . LEU B 1 667 ? 112.614 128.213 155.451 1.00 34.82 ?  667 LEU B CB    1 
ATOM   10923 C  CG    . LEU B 1 667 ? 114.003 128.839 155.315 1.00 35.69 ?  667 LEU B CG    1 
ATOM   10924 C  CD1   . LEU B 1 667 ? 114.758 128.200 154.165 1.00 32.35 ?  667 LEU B CD1   1 
ATOM   10925 C  CD2   . LEU B 1 667 ? 113.906 130.344 155.128 1.00 36.05 ?  667 LEU B CD2   1 
ATOM   10926 N  N     . ASN B 1 668 ? 109.734 129.527 155.489 1.00 29.55 ?  668 ASN B N     1 
ATOM   10927 C  CA    . ASN B 1 668 ? 108.799 130.568 155.078 1.00 27.67 ?  668 ASN B CA    1 
ATOM   10928 C  C     . ASN B 1 668 ? 108.195 131.273 156.285 1.00 26.38 ?  668 ASN B C     1 
ATOM   10929 O  O     . ASN B 1 668 ? 108.010 132.493 156.272 1.00 30.16 ?  668 ASN B O     1 
ATOM   10930 C  CB    . ASN B 1 668 ? 107.700 129.974 154.200 1.00 27.01 ?  668 ASN B CB    1 
ATOM   10931 C  CG    . ASN B 1 668 ? 108.149 129.759 152.771 1.00 31.94 ?  668 ASN B CG    1 
ATOM   10932 O  OD1   . ASN B 1 668 ? 108.821 130.607 152.186 1.00 33.09 ?  668 ASN B OD1   1 
ATOM   10933 N  ND2   . ASN B 1 668 ? 107.779 128.619 152.201 1.00 34.99 ?  668 ASN B ND2   1 
ATOM   10934 N  N     . ARG B 1 669 ? 107.861 130.517 157.332 1.00 29.63 ?  669 ARG B N     1 
ATOM   10935 C  CA    . ARG B 1 669 ? 107.314 131.125 158.539 1.00 33.48 ?  669 ARG B CA    1 
ATOM   10936 C  C     . ARG B 1 669 ? 108.330 132.046 159.196 1.00 25.82 ?  669 ARG B C     1 
ATOM   10937 O  O     . ARG B 1 669 ? 107.979 133.129 159.673 1.00 23.67 ?  669 ARG B O     1 
ATOM   10938 C  CB    . ARG B 1 669 ? 106.861 130.042 159.517 1.00 28.94 ?  669 ARG B CB    1 
ATOM   10939 C  CG    . ARG B 1 669 ? 105.761 129.146 158.987 1.00 27.53 ?  669 ARG B CG    1 
ATOM   10940 C  CD    . ARG B 1 669 ? 104.599 129.069 159.960 1.00 33.60 ?  669 ARG B CD    1 
ATOM   10941 N  NE    . ARG B 1 669 ? 105.048 128.972 161.343 1.00 35.05 ?  669 ARG B NE    1 
ATOM   10942 C  CZ    . ARG B 1 669 ? 104.649 129.778 162.318 1.00 34.11 ?  669 ARG B CZ    1 
ATOM   10943 N  NH1   . ARG B 1 669 ? 103.783 130.753 162.098 1.00 27.69 1  669 ARG B NH1   1 
ATOM   10944 N  NH2   . ARG B 1 669 ? 105.129 129.598 163.545 1.00 32.94 ?  669 ARG B NH2   1 
ATOM   10945 N  N     . ILE B 1 670 ? 109.596 131.628 159.239 1.00 23.92 ?  670 ILE B N     1 
ATOM   10946 C  CA    . ILE B 1 670 ? 110.637 132.488 159.792 1.00 25.25 ?  670 ILE B CA    1 
ATOM   10947 C  C     . ILE B 1 670 ? 110.760 133.766 158.973 1.00 24.69 ?  670 ILE B C     1 
ATOM   10948 O  O     . ILE B 1 670 ? 110.870 134.868 159.525 1.00 24.23 ?  670 ILE B O     1 
ATOM   10949 C  CB    . ILE B 1 670 ? 111.975 131.732 159.867 1.00 28.75 ?  670 ILE B CB    1 
ATOM   10950 C  CG1   . ILE B 1 670 ? 111.868 130.555 160.835 1.00 28.38 ?  670 ILE B CG1   1 
ATOM   10951 C  CG2   . ILE B 1 670 ? 113.093 132.669 160.297 1.00 29.69 ?  670 ILE B CG2   1 
ATOM   10952 C  CD1   . ILE B 1 670 ? 112.911 129.486 160.613 1.00 28.15 ?  670 ILE B CD1   1 
ATOM   10953 N  N     . ASP B 1 671 ? 110.742 133.642 157.645 1.00 26.09 ?  671 ASP B N     1 
ATOM   10954 C  CA    . ASP B 1 671 ? 110.824 134.822 156.789 1.00 20.91 ?  671 ASP B CA    1 
ATOM   10955 C  C     . ASP B 1 671 ? 109.642 135.756 157.021 1.00 22.37 ?  671 ASP B C     1 
ATOM   10956 O  O     . ASP B 1 671 ? 109.810 136.978 157.099 1.00 30.15 ?  671 ASP B O     1 
ATOM   10957 C  CB    . ASP B 1 671 ? 110.888 134.401 155.320 1.00 22.69 ?  671 ASP B CB    1 
ATOM   10958 C  CG    . ASP B 1 671 ? 112.202 133.742 154.958 1.00 33.81 ?  671 ASP B CG    1 
ATOM   10959 O  OD1   . ASP B 1 671 ? 113.260 134.230 155.404 1.00 35.02 ?  671 ASP B OD1   1 
ATOM   10960 O  OD2   . ASP B 1 671 ? 112.177 132.731 154.223 1.00 34.28 -1 671 ASP B OD2   1 
ATOM   10961 N  N     . LEU B 1 672 ? 108.437 135.195 157.134 1.00 14.50 ?  672 LEU B N     1 
ATOM   10962 C  CA    . LEU B 1 672 ? 107.246 136.019 157.313 1.00 16.65 ?  672 LEU B CA    1 
ATOM   10963 C  C     . LEU B 1 672 ? 107.240 136.691 158.677 1.00 19.98 ?  672 LEU B C     1 
ATOM   10964 O  O     . LEU B 1 672 ? 106.782 137.829 158.810 1.00 20.47 ?  672 LEU B O     1 
ATOM   10965 C  CB    . LEU B 1 672 ? 105.989 135.171 157.125 1.00 25.91 ?  672 LEU B CB    1 
ATOM   10966 C  CG    . LEU B 1 672 ? 105.770 134.578 155.732 1.00 21.16 ?  672 LEU B CG    1 
ATOM   10967 C  CD1   . LEU B 1 672 ? 104.639 133.565 155.750 1.00 20.27 ?  672 LEU B CD1   1 
ATOM   10968 C  CD2   . LEU B 1 672 ? 105.500 135.676 154.718 1.00 21.64 ?  672 LEU B CD2   1 
ATOM   10969 N  N     . TYR B 1 673 ? 107.729 135.997 159.706 1.00 21.86 ?  673 TYR B N     1 
ATOM   10970 C  CA    . TYR B 1 673 ? 107.840 136.611 161.025 1.00 17.60 ?  673 TYR B CA    1 
ATOM   10971 C  C     . TYR B 1 673 ? 108.877 137.727 161.024 1.00 18.92 ?  673 TYR B C     1 
ATOM   10972 O  O     . TYR B 1 673 ? 108.663 138.779 161.636 1.00 20.89 ?  673 TYR B O     1 
ATOM   10973 C  CB    . TYR B 1 673 ? 108.183 135.549 162.068 1.00 13.97 ?  673 TYR B CB    1 
ATOM   10974 C  CG    . TYR B 1 673 ? 108.272 136.081 163.478 1.00 20.24 ?  673 TYR B CG    1 
ATOM   10975 C  CD1   . TYR B 1 673 ? 107.143 136.546 164.136 1.00 20.26 ?  673 TYR B CD1   1 
ATOM   10976 C  CD2   . TYR B 1 673 ? 109.483 136.111 164.155 1.00 19.23 ?  673 TYR B CD2   1 
ATOM   10977 C  CE1   . TYR B 1 673 ? 107.218 137.032 165.424 1.00 21.48 ?  673 TYR B CE1   1 
ATOM   10978 C  CE2   . TYR B 1 673 ? 109.568 136.596 165.441 1.00 20.05 ?  673 TYR B CE2   1 
ATOM   10979 C  CZ    . TYR B 1 673 ? 108.433 137.054 166.073 1.00 23.89 ?  673 TYR B CZ    1 
ATOM   10980 O  OH    . TYR B 1 673 ? 108.513 137.536 167.357 1.00 23.91 ?  673 TYR B OH    1 
ATOM   10981 N  N     . ALA B 1 674 ? 110.005 137.517 160.342 1.00 18.45 ?  674 ALA B N     1 
ATOM   10982 C  CA    . ALA B 1 674 ? 111.004 138.573 160.229 1.00 12.94 ?  674 ALA B CA    1 
ATOM   10983 C  C     . ALA B 1 674 ? 110.436 139.790 159.513 1.00 15.69 ?  674 ALA B C     1 
ATOM   10984 O  O     . ALA B 1 674 ? 110.671 140.930 159.928 1.00 20.66 ?  674 ALA B O     1 
ATOM   10985 C  CB    . ALA B 1 674 ? 112.242 138.051 159.501 1.00 12.35 ?  674 ALA B CB    1 
ATOM   10986 N  N     . HIS B 1 675 ? 109.682 139.570 158.435 1.00 19.67 ?  675 HIS B N     1 
ATOM   10987 C  CA    . HIS B 1 675 ? 109.028 140.683 157.755 1.00 17.65 ?  675 HIS B CA    1 
ATOM   10988 C  C     . HIS B 1 675 ? 108.025 141.369 158.675 1.00 19.95 ?  675 HIS B C     1 
ATOM   10989 O  O     . HIS B 1 675 ? 107.909 142.598 158.676 1.00 21.60 ?  675 HIS B O     1 
ATOM   10990 C  CB    . HIS B 1 675 ? 108.343 140.194 156.480 1.00 17.03 ?  675 HIS B CB    1 
ATOM   10991 C  CG    . HIS B 1 675 ? 107.468 141.221 155.834 1.00 20.94 ?  675 HIS B CG    1 
ATOM   10992 N  ND1   . HIS B 1 675 ? 106.116 141.311 156.086 1.00 22.19 ?  675 HIS B ND1   1 
ATOM   10993 C  CD2   . HIS B 1 675 ? 107.752 142.207 154.951 1.00 15.69 ?  675 HIS B CD2   1 
ATOM   10994 C  CE1   . HIS B 1 675 ? 105.605 142.307 155.386 1.00 22.65 ?  675 HIS B CE1   1 
ATOM   10995 N  NE2   . HIS B 1 675 ? 106.576 142.865 154.687 1.00 27.17 ?  675 HIS B NE2   1 
ATOM   10996 N  N     . HIS B 1 676 ? 107.287 140.582 159.460 1.00 23.41 ?  676 HIS B N     1 
ATOM   10997 C  CA    . HIS B 1 676 ? 106.341 141.141 160.418 1.00 17.85 ?  676 HIS B CA    1 
ATOM   10998 C  C     . HIS B 1 676 ? 107.055 141.929 161.508 1.00 26.76 ?  676 HIS B C     1 
ATOM   10999 O  O     . HIS B 1 676 ? 106.569 142.978 161.948 1.00 25.74 ?  676 HIS B O     1 
ATOM   11000 C  CB    . HIS B 1 676 ? 105.502 140.015 161.025 1.00 23.55 ?  676 HIS B CB    1 
ATOM   11001 C  CG    . HIS B 1 676 ? 104.624 140.451 162.155 1.00 28.61 ?  676 HIS B CG    1 
ATOM   11002 N  ND1   . HIS B 1 676 ? 103.496 141.220 161.968 1.00 29.08 ?  676 HIS B ND1   1 
ATOM   11003 C  CD2   . HIS B 1 676 ? 104.705 140.220 163.487 1.00 25.73 ?  676 HIS B CD2   1 
ATOM   11004 C  CE1   . HIS B 1 676 ? 102.921 141.446 163.135 1.00 29.78 ?  676 HIS B CE1   1 
ATOM   11005 N  NE2   . HIS B 1 676 ? 103.636 140.851 164.073 1.00 29.10 ?  676 HIS B NE2   1 
ATOM   11006 N  N     . ARG B 1 677 ? 108.209 141.442 161.954 1.00 21.28 ?  677 ARG B N     1 
ATOM   11007 C  CA    . ARG B 1 677 ? 108.938 142.047 163.060 1.00 17.45 ?  677 ARG B CA    1 
ATOM   11008 C  C     . ARG B 1 677 ? 109.825 143.206 162.629 1.00 20.71 ?  677 ARG B C     1 
ATOM   11009 O  O     . ARG B 1 677 ? 110.594 143.715 163.450 1.00 27.99 ?  677 ARG B O     1 
ATOM   11010 C  CB    . ARG B 1 677 ? 109.785 140.989 163.770 1.00 20.81 ?  677 ARG B CB    1 
ATOM   11011 C  CG    . ARG B 1 677 ? 109.013 140.146 164.767 1.00 20.08 ?  677 ARG B CG    1 
ATOM   11012 C  CD    . ARG B 1 677 ? 108.419 140.993 165.877 1.00 20.24 ?  677 ARG B CD    1 
ATOM   11013 N  NE    . ARG B 1 677 ? 109.318 141.099 167.020 1.00 26.81 ?  677 ARG B NE    1 
ATOM   11014 C  CZ    . ARG B 1 677 ? 109.962 142.205 167.368 1.00 34.13 ?  677 ARG B CZ    1 
ATOM   11015 N  NH1   . ARG B 1 677 ? 109.813 143.332 166.692 1.00 27.67 1  677 ARG B NH1   1 
ATOM   11016 N  NH2   . ARG B 1 677 ? 110.773 142.179 168.421 1.00 25.83 ?  677 ARG B NH2   1 
ATOM   11017 N  N     . GLY B 1 678 ? 109.741 143.634 161.373 1.00 20.97 ?  678 GLY B N     1 
ATOM   11018 C  CA    . GLY B 1 678 ? 110.524 144.752 160.897 1.00 15.51 ?  678 GLY B CA    1 
ATOM   11019 C  C     . GLY B 1 678 ? 111.920 144.419 160.426 1.00 13.12 ?  678 GLY B C     1 
ATOM   11020 O  O     . GLY B 1 678 ? 112.718 145.341 160.216 1.00 23.68 ?  678 GLY B O     1 
ATOM   11021 N  N     . ILE B 1 679 ? 112.248 143.137 160.256 1.00 7.70  ?  679 ILE B N     1 
ATOM   11022 C  CA    . ILE B 1 679 ? 113.552 142.776 159.718 1.00 12.73 ?  679 ILE B CA    1 
ATOM   11023 C  C     . ILE B 1 679 ? 113.693 143.353 158.318 1.00 12.39 ?  679 ILE B C     1 
ATOM   11024 O  O     . ILE B 1 679 ? 112.735 143.386 157.536 1.00 23.72 ?  679 ILE B O     1 
ATOM   11025 C  CB    . ILE B 1 679 ? 113.730 141.248 159.718 1.00 12.96 ?  679 ILE B CB    1 
ATOM   11026 C  CG1   . ILE B 1 679 ? 113.741 140.713 161.152 1.00 10.32 ?  679 ILE B CG1   1 
ATOM   11027 C  CG2   . ILE B 1 679 ? 115.002 140.856 158.986 1.00 9.27  ?  679 ILE B CG2   1 
ATOM   11028 C  CD1   . ILE B 1 679 ? 114.852 141.271 162.003 1.00 13.78 ?  679 ILE B CD1   1 
ATOM   11029 N  N     . LYS B 1 680 ? 114.896 143.826 157.997 1.00 12.39 ?  680 LYS B N     1 
ATOM   11030 C  CA    . LYS B 1 680 ? 115.137 144.464 156.710 1.00 5.56  ?  680 LYS B CA    1 
ATOM   11031 C  C     . LYS B 1 680 ? 115.705 143.490 155.684 1.00 11.19 ?  680 LYS B C     1 
ATOM   11032 O  O     . LYS B 1 680 ? 115.236 143.446 154.543 1.00 19.20 ?  680 LYS B O     1 
ATOM   11033 C  CB    . LYS B 1 680 ? 116.081 145.656 156.884 1.00 8.90  ?  680 LYS B CB    1 
ATOM   11034 C  CG    . LYS B 1 680 ? 115.465 146.829 157.615 1.00 0.00  ?  680 LYS B CG    1 
ATOM   11035 C  CD    . LYS B 1 680 ? 116.453 147.969 157.742 1.00 6.04  ?  680 LYS B CD    1 
ATOM   11036 C  CE    . LYS B 1 680 ? 115.919 149.067 158.641 1.00 8.83  ?  680 LYS B CE    1 
ATOM   11037 N  NZ    . LYS B 1 680 ? 116.860 150.214 158.712 1.00 12.65 1  680 LYS B NZ    1 
ATOM   11038 N  N     . THR B 1 681 ? 116.711 142.711 156.068 1.00 7.31  ?  681 THR B N     1 
ATOM   11039 C  CA    . THR B 1 681 ? 117.333 141.754 155.167 1.00 5.82  ?  681 THR B CA    1 
ATOM   11040 C  C     . THR B 1 681 ? 117.599 140.458 155.915 1.00 13.90 ?  681 THR B C     1 
ATOM   11041 O  O     . THR B 1 681 ? 117.805 140.454 157.131 1.00 22.74 ?  681 THR B O     1 
ATOM   11042 C  CB    . THR B 1 681 ? 118.644 142.295 154.573 1.00 15.14 ?  681 THR B CB    1 
ATOM   11043 O  OG1   . THR B 1 681 ? 119.510 142.726 155.630 1.00 24.15 ?  681 THR B OG1   1 
ATOM   11044 C  CG2   . THR B 1 681 ? 118.370 143.467 153.644 1.00 10.68 ?  681 THR B CG2   1 
ATOM   11045 N  N     . ILE B 1 682 ? 117.578 139.353 155.177 1.00 13.87 ?  682 ILE B N     1 
ATOM   11046 C  CA    . ILE B 1 682 ? 117.973 138.048 155.690 1.00 8.57  ?  682 ILE B CA    1 
ATOM   11047 C  C     . ILE B 1 682 ? 119.153 137.577 154.855 1.00 12.89 ?  682 ILE B C     1 
ATOM   11048 O  O     . ILE B 1 682 ? 119.059 137.505 153.624 1.00 20.77 ?  682 ILE B O     1 
ATOM   11049 C  CB    . ILE B 1 682 ? 116.816 137.039 155.648 1.00 16.24 ?  682 ILE B CB    1 
ATOM   11050 C  CG1   . ILE B 1 682 ? 115.581 137.629 156.330 1.00 18.29 ?  682 ILE B CG1   1 
ATOM   11051 C  CG2   . ILE B 1 682 ? 117.216 135.756 156.343 1.00 20.74 ?  682 ILE B CG2   1 
ATOM   11052 C  CD1   . ILE B 1 682 ? 114.381 136.722 156.313 1.00 20.86 ?  682 ILE B CD1   1 
ATOM   11053 N  N     . TYR B 1 683 ? 120.265 137.265 155.521 1.00 21.02 ?  683 TYR B N     1 
ATOM   11054 C  CA    . TYR B 1 683 ? 121.514 137.040 154.801 1.00 15.81 ?  683 TYR B CA    1 
ATOM   11055 C  C     . TYR B 1 683 ? 121.601 135.625 154.241 1.00 21.89 ?  683 TYR B C     1 
ATOM   11056 O  O     . TYR B 1 683 ? 121.634 135.429 153.022 1.00 36.09 ?  683 TYR B O     1 
ATOM   11057 C  CB    . TYR B 1 683 ? 122.700 137.321 155.727 1.00 19.49 ?  683 TYR B CB    1 
ATOM   11058 C  CG    . TYR B 1 683 ? 124.044 137.282 155.041 1.00 16.47 ?  683 TYR B CG    1 
ATOM   11059 C  CD1   . TYR B 1 683 ? 124.144 137.408 153.662 1.00 14.04 ?  683 TYR B CD1   1 
ATOM   11060 C  CD2   . TYR B 1 683 ? 125.215 137.127 155.770 1.00 10.09 ?  683 TYR B CD2   1 
ATOM   11061 C  CE1   . TYR B 1 683 ? 125.366 137.377 153.032 1.00 14.84 ?  683 TYR B CE1   1 
ATOM   11062 C  CE2   . TYR B 1 683 ? 126.445 137.097 155.146 1.00 17.39 ?  683 TYR B CE2   1 
ATOM   11063 C  CZ    . TYR B 1 683 ? 126.514 137.223 153.776 1.00 21.24 ?  683 TYR B CZ    1 
ATOM   11064 O  OH    . TYR B 1 683 ? 127.736 137.193 153.146 1.00 27.63 ?  683 TYR B OH    1 
ATOM   11065 N  N     . TYR B 1 684 ? 121.623 134.626 155.112 1.00 32.48 ?  684 TYR B N     1 
ATOM   11066 C  CA    . TYR B 1 684 ? 121.869 133.260 154.682 1.00 26.42 ?  684 TYR B CA    1 
ATOM   11067 C  C     . TYR B 1 684 ? 120.926 132.320 155.410 1.00 33.42 ?  684 TYR B C     1 
ATOM   11068 O  O     . TYR B 1 684 ? 120.513 132.580 156.544 1.00 34.45 ?  684 TYR B O     1 
ATOM   11069 C  CB    . TYR B 1 684 ? 123.321 132.837 154.937 1.00 27.97 ?  684 TYR B CB    1 
ATOM   11070 C  CG    . TYR B 1 684 ? 124.226 132.983 153.738 1.00 26.02 ?  684 TYR B CG    1 
ATOM   11071 C  CD1   . TYR B 1 684 ? 123.922 132.367 152.533 1.00 32.79 ?  684 TYR B CD1   1 
ATOM   11072 C  CD2   . TYR B 1 684 ? 125.388 133.739 153.812 1.00 29.91 ?  684 TYR B CD2   1 
ATOM   11073 C  CE1   . TYR B 1 684 ? 124.750 132.499 151.433 1.00 34.28 ?  684 TYR B CE1   1 
ATOM   11074 C  CE2   . TYR B 1 684 ? 126.220 133.878 152.721 1.00 26.35 ?  684 TYR B CE2   1 
ATOM   11075 C  CZ    . TYR B 1 684 ? 125.898 133.258 151.533 1.00 34.79 ?  684 TYR B CZ    1 
ATOM   11076 O  OH    . TYR B 1 684 ? 126.725 133.393 150.444 1.00 38.30 ?  684 TYR B OH    1 
ATOM   11077 N  N     . ALA B 1 685 ? 120.589 131.226 154.741 1.00 35.80 ?  685 ALA B N     1 
ATOM   11078 C  CA    . ALA B 1 685 ? 119.857 130.121 155.344 1.00 32.35 ?  685 ALA B CA    1 
ATOM   11079 C  C     . ALA B 1 685 ? 120.865 128.991 155.527 1.00 36.52 ?  685 ALA B C     1 
ATOM   11080 O  O     . ALA B 1 685 ? 121.122 128.212 154.608 1.00 43.17 ?  685 ALA B O     1 
ATOM   11081 C  CB    . ALA B 1 685 ? 118.676 129.702 154.479 1.00 30.46 ?  685 ALA B CB    1 
ATOM   11082 N  N     . ARG B 1 686 ? 121.443 128.912 156.722 1.00 33.83 ?  686 ARG B N     1 
ATOM   11083 C  CA    . ARG B 1 686 ? 122.408 127.871 157.047 1.00 35.87 ?  686 ARG B CA    1 
ATOM   11084 C  C     . ARG B 1 686 ? 121.688 126.693 157.685 1.00 40.57 ?  686 ARG B C     1 
ATOM   11085 O  O     . ARG B 1 686 ? 120.923 126.866 158.640 1.00 40.64 ?  686 ARG B O     1 
ATOM   11086 C  CB    . ARG B 1 686 ? 123.486 128.404 157.991 1.00 39.59 ?  686 ARG B CB    1 
ATOM   11087 C  CG    . ARG B 1 686 ? 124.631 129.114 157.299 1.00 40.79 ?  686 ARG B CG    1 
ATOM   11088 C  CD    . ARG B 1 686 ? 125.734 129.456 158.285 1.00 40.96 ?  686 ARG B CD    1 
ATOM   11089 N  NE    . ARG B 1 686 ? 127.040 129.000 157.828 1.00 43.95 ?  686 ARG B NE    1 
ATOM   11090 C  CZ    . ARG B 1 686 ? 127.623 127.878 158.227 1.00 45.05 ?  686 ARG B CZ    1 
ATOM   11091 N  NH1   . ARG B 1 686 ? 127.044 127.069 159.098 1.00 42.85 1  686 ARG B NH1   1 
ATOM   11092 N  NH2   . ARG B 1 686 ? 128.819 127.560 157.738 1.00 45.28 ?  686 ARG B NH2   1 
ATOM   11093 N  N     . THR B 1 687 ? 121.933 125.499 157.158 1.00 46.65 ?  687 THR B N     1 
ATOM   11094 C  CA    . THR B 1 687 ? 121.316 124.280 157.653 1.00 46.49 ?  687 THR B CA    1 
ATOM   11095 C  C     . THR B 1 687 ? 122.368 123.386 158.293 1.00 43.91 ?  687 THR B C     1 
ATOM   11096 O  O     . THR B 1 687 ? 123.512 123.319 157.835 1.00 44.81 ?  687 THR B O     1 
ATOM   11097 C  CB    . THR B 1 687 ? 120.602 123.523 156.528 1.00 43.74 ?  687 THR B CB    1 
ATOM   11098 O  OG1   . THR B 1 687 ? 119.620 124.373 155.923 1.00 46.02 ?  687 THR B OG1   1 
ATOM   11099 C  CG2   . THR B 1 687 ? 119.916 122.283 157.073 1.00 44.19 ?  687 THR B CG2   1 
ATOM   11100 N  N     . LYS B 1 688 ? 121.971 122.705 159.360 1.00 49.71 ?  688 LYS B N     1 
ATOM   11101 C  CA    . LYS B 1 688 ? 122.882 121.835 160.091 1.00 51.70 ?  688 LYS B CA    1 
ATOM   11102 C  C     . LYS B 1 688 ? 122.637 120.371 159.740 1.00 53.44 ?  688 LYS B C     1 
ATOM   11103 O  O     . LYS B 1 688 ? 121.495 119.944 159.583 1.00 55.31 ?  688 LYS B O     1 
ATOM   11104 C  CB    . LYS B 1 688 ? 122.731 122.051 161.598 1.00 49.78 ?  688 LYS B CB    1 
ATOM   11105 C  CG    . LYS B 1 688 ? 123.659 121.201 162.446 1.00 49.27 ?  688 LYS B CG    1 
ATOM   11106 C  CD    . LYS B 1 688 ? 123.537 121.559 163.916 1.00 50.46 ?  688 LYS B CD    1 
ATOM   11107 C  CE    . LYS B 1 688 ? 124.425 120.678 164.775 1.00 53.02 ?  688 LYS B CE    1 
ATOM   11108 N  NZ    . LYS B 1 688 ? 124.288 120.999 166.221 1.00 54.24 ?  688 LYS B NZ    1 
ATOM   11109 N  N     . ASP C 2 37  ? 133.273 83.957  113.176 1.00 45.99 ?  16  ASP C N     1 
ATOM   11110 C  CA    . ASP C 2 37  ? 133.376 84.556  111.842 1.00 45.47 ?  16  ASP C CA    1 
ATOM   11111 C  C     . ASP C 2 37  ? 132.760 85.950  111.723 1.00 44.13 ?  16  ASP C C     1 
ATOM   11112 O  O     . ASP C 2 37  ? 132.873 86.588  110.675 1.00 44.46 ?  16  ASP C O     1 
ATOM   11113 C  CB    . ASP C 2 37  ? 132.729 83.630  110.809 1.00 45.90 ?  16  ASP C CB    1 
ATOM   11114 C  CG    . ASP C 2 37  ? 133.212 82.205  110.928 1.00 47.25 ?  16  ASP C CG    1 
ATOM   11115 O  OD1   . ASP C 2 37  ? 134.418 82.002  111.184 1.00 47.99 ?  16  ASP C OD1   1 
ATOM   11116 O  OD2   . ASP C 2 37  ? 132.380 81.289  110.769 1.00 49.50 -1 16  ASP C OD2   1 
ATOM   11117 N  N     . PHE C 2 38  ? 132.115 86.424  112.786 1.00 42.17 ?  17  PHE C N     1 
ATOM   11118 C  CA    . PHE C 2 38  ? 131.301 87.641  112.686 1.00 40.67 ?  17  PHE C CA    1 
ATOM   11119 C  C     . PHE C 2 38  ? 131.477 88.700  113.781 1.00 39.46 ?  17  PHE C C     1 
ATOM   11120 O  O     . PHE C 2 38  ? 131.186 89.875  113.546 1.00 39.17 ?  17  PHE C O     1 
ATOM   11121 C  CB    . PHE C 2 38  ? 129.814 87.273  112.541 1.00 40.24 ?  17  PHE C CB    1 
ATOM   11122 C  CG    . PHE C 2 38  ? 129.292 86.371  113.635 1.00 39.58 ?  17  PHE C CG    1 
ATOM   11123 C  CD1   . PHE C 2 38  ? 128.808 86.906  114.829 1.00 38.78 ?  17  PHE C CD1   1 
ATOM   11124 C  CD2   . PHE C 2 38  ? 129.270 84.986  113.465 1.00 39.43 ?  17  PHE C CD2   1 
ATOM   11125 C  CE1   . PHE C 2 38  ? 128.315 86.080  115.839 1.00 38.07 ?  17  PHE C CE1   1 
ATOM   11126 C  CE2   . PHE C 2 38  ? 128.778 84.148  114.472 1.00 39.10 ?  17  PHE C CE2   1 
ATOM   11127 C  CZ    . PHE C 2 38  ? 128.301 84.699  115.662 1.00 38.63 ?  17  PHE C CZ    1 
ATOM   11128 N  N     . THR C 2 39  ? 131.937 88.296  114.966 1.00 38.22 ?  18  THR C N     1 
ATOM   11129 C  CA    . THR C 2 39  ? 131.995 89.217  116.114 1.00 37.09 ?  18  THR C CA    1 
ATOM   11130 C  C     . THR C 2 39  ? 132.817 90.485  115.826 1.00 36.84 ?  18  THR C C     1 
ATOM   11131 O  O     . THR C 2 39  ? 132.371 91.601  116.138 1.00 36.13 ?  18  THR C O     1 
ATOM   11132 C  CB    . THR C 2 39  ? 132.428 88.516  117.434 1.00 36.59 ?  18  THR C CB    1 
ATOM   11133 O  OG1   . THR C 2 39  ? 131.341 87.720  117.917 1.00 36.50 ?  18  THR C OG1   1 
ATOM   11134 C  CG2   . THR C 2 39  ? 132.766 89.530  118.509 1.00 36.06 ?  18  THR C CG2   1 
ATOM   11135 N  N     . GLN C 2 40  ? 133.994 90.313  115.217 1.00 37.01 ?  19  GLN C N     1 
ATOM   11136 C  CA    . GLN C 2 40  ? 134.873 91.451  114.907 1.00 37.33 ?  19  GLN C CA    1 
ATOM   11137 C  C     . GLN C 2 40  ? 134.210 92.495  114.025 1.00 36.63 ?  19  GLN C C     1 
ATOM   11138 O  O     . GLN C 2 40  ? 134.343 93.693  114.274 1.00 36.10 ?  19  GLN C O     1 
ATOM   11139 C  CB    . GLN C 2 40  ? 136.195 91.003  114.285 1.00 38.24 ?  19  GLN C CB    1 
ATOM   11140 C  CG    . GLN C 2 40  ? 137.212 90.570  115.317 1.00 41.33 ?  19  GLN C CG    1 
ATOM   11141 C  CD    . GLN C 2 40  ? 138.635 90.934  114.942 1.00 45.15 ?  19  GLN C CD    1 
ATOM   11142 O  OE1   . GLN C 2 40  ? 139.005 90.936  113.761 1.00 47.33 ?  19  GLN C OE1   1 
ATOM   11143 N  NE2   . GLN C 2 40  ? 139.448 91.244  115.950 1.00 46.51 ?  19  GLN C NE2   1 
ATOM   11144 N  N     . MET C 2 41  ? 133.486 92.040  113.006 1.00 36.23 ?  20  MET C N     1 
ATOM   11145 C  CA    . MET C 2 41  ? 132.781 92.963  112.128 1.00 36.40 ?  20  MET C CA    1 
ATOM   11146 C  C     . MET C 2 41  ? 131.590 93.636  112.836 1.00 34.93 ?  20  MET C C     1 
ATOM   11147 O  O     . MET C 2 41  ? 131.308 94.805  112.585 1.00 34.20 ?  20  MET C O     1 
ATOM   11148 C  CB    . MET C 2 41  ? 132.431 92.316  110.770 1.00 37.35 ?  20  MET C CB    1 
ATOM   11149 C  CG    . MET C 2 41  ? 131.129 91.544  110.670 1.00 40.49 ?  20  MET C CG    1 
ATOM   11150 S  SD    . MET C 2 41  ? 130.802 91.061  108.945 1.00 48.68 ?  20  MET C SD    1 
ATOM   11151 C  CE    . MET C 2 41  ? 131.701 89.508  108.832 1.00 47.17 ?  20  MET C CE    1 
ATOM   11152 N  N     . PHE C 2 42  ? 130.933 92.919  113.751 1.00 33.75 ?  21  PHE C N     1 
ATOM   11153 C  CA    . PHE C 2 42  ? 129.896 93.539  114.589 1.00 32.62 ?  21  PHE C CA    1 
ATOM   11154 C  C     . PHE C 2 42  ? 130.481 94.529  115.589 1.00 32.59 ?  21  PHE C C     1 
ATOM   11155 O  O     . PHE C 2 42  ? 129.901 95.593  115.828 1.00 32.23 ?  21  PHE C O     1 
ATOM   11156 C  CB    . PHE C 2 42  ? 129.032 92.490  115.289 1.00 32.12 ?  21  PHE C CB    1 
ATOM   11157 C  CG    . PHE C 2 42  ? 127.944 91.934  114.419 1.00 31.04 ?  21  PHE C CG    1 
ATOM   11158 C  CD1   . PHE C 2 42  ? 126.662 92.482  114.448 1.00 30.75 ?  21  PHE C CD1   1 
ATOM   11159 C  CD2   . PHE C 2 42  ? 128.197 90.868  113.563 1.00 30.99 ?  21  PHE C CD2   1 
ATOM   11160 C  CE1   . PHE C 2 42  ? 125.645 91.970  113.634 1.00 30.30 ?  21  PHE C CE1   1 
ATOM   11161 C  CE2   . PHE C 2 42  ? 127.186 90.345  112.740 1.00 30.74 ?  21  PHE C CE2   1 
ATOM   11162 C  CZ    . PHE C 2 42  ? 125.910 90.898  112.778 1.00 30.48 ?  21  PHE C CZ    1 
ATOM   11163 N  N     . TYR C 2 43  ? 131.633 94.182  116.161 1.00 32.33 ?  22  TYR C N     1 
ATOM   11164 C  CA    . TYR C 2 43  ? 132.350 95.100  117.042 1.00 32.50 ?  22  TYR C CA    1 
ATOM   11165 C  C     . TYR C 2 43  ? 132.632 96.417  116.321 1.00 33.01 ?  22  TYR C C     1 
ATOM   11166 O  O     . TYR C 2 43  ? 132.317 97.492  116.838 1.00 32.50 ?  22  TYR C O     1 
ATOM   11167 C  CB    . TYR C 2 43  ? 133.652 94.481  117.584 1.00 32.53 ?  22  TYR C CB    1 
ATOM   11168 C  CG    . TYR C 2 43  ? 134.523 95.503  118.295 1.00 33.27 ?  22  TYR C CG    1 
ATOM   11169 C  CD1   . TYR C 2 43  ? 134.265 95.870  119.619 1.00 32.34 ?  22  TYR C CD1   1 
ATOM   11170 C  CD2   . TYR C 2 43  ? 135.576 96.131  117.628 1.00 33.71 ?  22  TYR C CD2   1 
ATOM   11171 C  CE1   . TYR C 2 43  ? 135.049 96.824  120.267 1.00 33.58 ?  22  TYR C CE1   1 
ATOM   11172 C  CE2   . TYR C 2 43  ? 136.364 97.094  118.262 1.00 35.12 ?  22  TYR C CE2   1 
ATOM   11173 C  CZ    . TYR C 2 43  ? 136.097 97.431  119.583 1.00 35.30 ?  22  TYR C CZ    1 
ATOM   11174 O  OH    . TYR C 2 43  ? 136.878 98.379  120.208 1.00 36.54 ?  22  TYR C OH    1 
ATOM   11175 N  N     . ASN C 2 44  ? 133.211 96.320  115.121 1.00 33.80 ?  23  ASN C N     1 
ATOM   11176 C  CA    . ASN C 2 44  ? 133.556 97.495  114.332 1.00 34.80 ?  23  ASN C CA    1 
ATOM   11177 C  C     . ASN C 2 44  ? 132.323 98.305  113.938 1.00 34.40 ?  23  ASN C C     1 
ATOM   11178 O  O     . ASN C 2 44  ? 132.336 99.529  114.017 1.00 33.99 ?  23  ASN C O     1 
ATOM   11179 C  CB    . ASN C 2 44  ? 134.375 97.108  113.090 1.00 35.46 ?  23  ASN C CB    1 
ATOM   11180 C  CG    . ASN C 2 44  ? 135.730 96.472  113.438 1.00 38.28 ?  23  ASN C CG    1 
ATOM   11181 O  OD1   . ASN C 2 44  ? 136.285 96.680  114.528 1.00 41.01 ?  23  ASN C OD1   1 
ATOM   11182 N  ND2   . ASN C 2 44  ? 136.270 95.697  112.499 1.00 39.13 ?  23  ASN C ND2   1 
ATOM   11183 N  N     . GLN C 2 45  ? 131.255 97.615  113.533 1.00 34.49 ?  24  GLN C N     1 
ATOM   11184 C  CA    . GLN C 2 45  ? 130.011 98.277  113.157 1.00 34.81 ?  24  GLN C CA    1 
ATOM   11185 C  C     . GLN C 2 45  ? 129.366 98.991  114.351 1.00 34.68 ?  24  GLN C C     1 
ATOM   11186 O  O     . GLN C 2 45  ? 128.937 100.141 114.233 1.00 34.59 ?  24  GLN C O     1 
ATOM   11187 C  CB    . GLN C 2 45  ? 129.039 97.285  112.511 1.00 34.83 ?  24  GLN C CB    1 
ATOM   11188 C  CG    . GLN C 2 45  ? 127.881 97.932  111.747 1.00 36.14 ?  24  GLN C CG    1 
ATOM   11189 C  CD    . GLN C 2 45  ? 128.334 98.807  110.574 1.00 38.04 ?  24  GLN C CD    1 
ATOM   11190 O  OE1   . GLN C 2 45  ? 129.382 98.573  109.966 1.00 38.57 ?  24  GLN C OE1   1 
ATOM   11191 N  NE2   . GLN C 2 45  ? 127.536 99.828  110.259 1.00 38.67 ?  24  GLN C NE2   1 
ATOM   11192 N  N     . ASN C 2 46  ? 129.316 98.323  115.500 1.00 34.71 ?  25  ASN C N     1 
ATOM   11193 C  CA    . ASN C 2 46  ? 128.735 98.931  116.697 1.00 34.99 ?  25  ASN C CA    1 
ATOM   11194 C  C     . ASN C 2 46  ? 129.478 100.190 117.143 1.00 35.69 ?  25  ASN C C     1 
ATOM   11195 O  O     . ASN C 2 46  ? 128.859 101.230 117.390 1.00 35.41 ?  25  ASN C O     1 
ATOM   11196 C  CB    . ASN C 2 46  ? 128.619 97.917  117.843 1.00 34.64 ?  25  ASN C CB    1 
ATOM   11197 C  CG    . ASN C 2 46  ? 127.392 97.041  117.715 1.00 34.71 ?  25  ASN C CG    1 
ATOM   11198 O  OD1   . ASN C 2 46  ? 126.344 97.357  118.270 1.00 35.68 ?  25  ASN C OD1   1 
ATOM   11199 N  ND2   . ASN C 2 46  ? 127.502 95.950  116.950 1.00 34.71 ?  25  ASN C ND2   1 
ATOM   11200 N  N     . VAL C 2 47  ? 130.803 100.110 117.218 1.00 36.69 ?  26  VAL C N     1 
ATOM   11201 C  CA    . VAL C 2 47  ? 131.583 101.262 117.676 1.00 38.00 ?  26  VAL C CA    1 
ATOM   11202 C  C     . VAL C 2 47  ? 131.587 102.420 116.669 1.00 38.90 ?  26  VAL C C     1 
ATOM   11203 O  O     . VAL C 2 47  ? 131.658 103.578 117.069 1.00 39.46 ?  26  VAL C O     1 
ATOM   11204 C  CB    . VAL C 2 47  ? 133.022 100.890 118.125 1.00 38.16 ?  26  VAL C CB    1 
ATOM   11205 C  CG1   . VAL C 2 47  ? 132.971 99.863  119.241 1.00 37.75 ?  26  VAL C CG1   1 
ATOM   11206 C  CG2   . VAL C 2 47  ? 133.868 100.395 116.954 1.00 38.81 ?  26  VAL C CG2   1 
ATOM   11207 N  N     . LYS C 2 48  ? 131.474 102.110 115.377 1.00 39.67 ?  27  LYS C N     1 
ATOM   11208 C  CA    . LYS C 2 48  ? 131.418 103.158 114.354 1.00 40.50 ?  27  LYS C CA    1 
ATOM   11209 C  C     . LYS C 2 48  ? 130.034 103.815 114.285 1.00 40.02 ?  27  LYS C C     1 
ATOM   11210 O  O     . LYS C 2 48  ? 129.870 104.883 113.691 1.00 40.55 ?  27  LYS C O     1 
ATOM   11211 C  CB    . LYS C 2 48  ? 131.852 102.623 112.975 1.00 41.23 ?  27  LYS C CB    1 
ATOM   11212 C  CG    . LYS C 2 48  ? 130.751 101.925 112.178 1.00 42.50 ?  27  LYS C CG    1 
ATOM   11213 C  CD    . LYS C 2 48  ? 131.224 101.474 110.788 1.00 44.92 ?  27  LYS C CD    1 
ATOM   11214 C  CE    . LYS C 2 48  ? 131.229 102.621 109.779 1.00 46.66 ?  27  LYS C CE    1 
ATOM   11215 N  NZ    . LYS C 2 48  ? 129.871 103.208 109.586 1.00 47.26 1  27  LYS C NZ    1 
ATOM   11216 N  N     . GLN C 2 49  ? 129.039 103.171 114.884 1.00 39.10 ?  28  GLN C N     1 
ATOM   11217 C  CA    . GLN C 2 49  ? 127.703 103.728 114.924 1.00 38.22 ?  28  GLN C CA    1 
ATOM   11218 C  C     . GLN C 2 49  ? 127.477 104.573 116.177 1.00 37.23 ?  28  GLN C C     1 
ATOM   11219 O  O     . GLN C 2 49  ? 126.393 105.127 116.344 1.00 37.40 ?  28  GLN C O     1 
ATOM   11220 C  CB    . GLN C 2 49  ? 126.637 102.626 114.796 1.00 38.69 ?  28  GLN C CB    1 
ATOM   11221 C  CG    . GLN C 2 49  ? 126.505 102.045 113.379 1.00 39.57 ?  28  GLN C CG    1 
ATOM   11222 C  CD    . GLN C 2 49  ? 125.322 101.096 113.209 1.00 41.20 ?  28  GLN C CD    1 
ATOM   11223 O  OE1   . GLN C 2 49  ? 125.149 100.503 112.144 1.00 42.94 ?  28  GLN C OE1   1 
ATOM   11224 N  NE2   . GLN C 2 49  ? 124.502 100.950 114.254 1.00 41.23 ?  28  GLN C NE2   1 
ATOM   11225 N  N     . PHE C 2 50  ? 128.495 104.690 117.036 1.00 35.83 ?  29  PHE C N     1 
ATOM   11226 C  CA    . PHE C 2 50  ? 128.342 105.414 118.306 1.00 34.51 ?  29  PHE C CA    1 
ATOM   11227 C  C     . PHE C 2 50  ? 127.822 106.843 118.126 1.00 33.81 ?  29  PHE C C     1 
ATOM   11228 O  O     . PHE C 2 50  ? 128.304 107.579 117.265 1.00 33.66 ?  29  PHE C O     1 
ATOM   11229 C  CB    . PHE C 2 50  ? 129.631 105.423 119.133 1.00 34.59 ?  29  PHE C CB    1 
ATOM   11230 C  CG    . PHE C 2 50  ? 129.490 106.135 120.467 1.00 34.59 ?  29  PHE C CG    1 
ATOM   11231 C  CD1   . PHE C 2 50  ? 128.764 105.556 121.514 1.00 34.34 ?  29  PHE C CD1   1 
ATOM   11232 C  CD2   . PHE C 2 50  ? 130.063 107.390 120.667 1.00 35.49 ?  29  PHE C CD2   1 
ATOM   11233 C  CE1   . PHE C 2 50  ? 128.624 106.213 122.747 1.00 33.88 ?  29  PHE C CE1   1 
ATOM   11234 C  CE2   . PHE C 2 50  ? 129.928 108.062 121.896 1.00 34.12 ?  29  PHE C CE2   1 
ATOM   11235 C  CZ    . PHE C 2 50  ? 129.209 107.473 122.935 1.00 33.87 ?  29  PHE C CZ    1 
ATOM   11236 N  N     . TRP C 2 51  ? 126.843 107.216 118.953 1.00 32.24 ?  30  TRP C N     1 
ATOM   11237 C  CA    . TRP C 2 51  ? 126.221 108.537 118.898 1.00 31.28 ?  30  TRP C CA    1 
ATOM   11238 C  C     . TRP C 2 51  ? 125.657 108.956 120.257 1.00 31.12 ?  30  TRP C C     1 
ATOM   11239 O  O     . TRP C 2 51  ? 125.503 108.118 121.154 1.00 30.71 ?  30  TRP C O     1 
ATOM   11240 C  CB    . TRP C 2 51  ? 125.122 108.570 117.825 1.00 30.85 ?  30  TRP C CB    1 
ATOM   11241 C  CG    . TRP C 2 51  ? 123.979 107.619 118.082 1.00 29.31 ?  30  TRP C CG    1 
ATOM   11242 C  CD1   . TRP C 2 51  ? 123.937 106.283 117.790 1.00 29.07 ?  30  TRP C CD1   1 
ATOM   11243 C  CD2   . TRP C 2 51  ? 122.728 107.931 118.703 1.00 28.33 ?  30  TRP C CD2   1 
ATOM   11244 N  NE1   . TRP C 2 51  ? 122.735 105.748 118.181 1.00 28.01 ?  30  TRP C NE1   1 
ATOM   11245 C  CE2   . TRP C 2 51  ? 121.972 106.737 118.744 1.00 27.67 ?  30  TRP C CE2   1 
ATOM   11246 C  CE3   . TRP C 2 51  ? 122.172 109.104 119.233 1.00 27.27 ?  30  TRP C CE3   1 
ATOM   11247 C  CZ2   . TRP C 2 51  ? 120.691 106.682 119.291 1.00 26.54 ?  30  TRP C CZ2   1 
ATOM   11248 C  CZ3   . TRP C 2 51  ? 120.892 109.051 119.769 1.00 27.07 ?  30  TRP C CZ3   1 
ATOM   11249 C  CH2   . TRP C 2 51  ? 120.169 107.844 119.801 1.00 26.52 ?  30  TRP C CH2   1 
ATOM   11250 N  N     . LEU C 2 52  ? 125.359 110.251 120.398 1.00 30.65 ?  31  LEU C N     1 
ATOM   11251 C  CA    . LEU C 2 52  ? 124.684 110.803 121.575 1.00 30.38 ?  31  LEU C CA    1 
ATOM   11252 C  C     . LEU C 2 52  ? 123.531 111.698 121.131 1.00 30.51 ?  31  LEU C C     1 
ATOM   11253 O  O     . LEU C 2 52  ? 123.668 112.414 120.137 1.00 30.77 ?  31  LEU C O     1 
ATOM   11254 C  CB    . LEU C 2 52  ? 125.666 111.610 122.440 1.00 30.45 ?  31  LEU C CB    1 
ATOM   11255 C  CG    . LEU C 2 52  ? 126.803 110.809 123.082 1.00 30.29 ?  31  LEU C CG    1 
ATOM   11256 C  CD1   . LEU C 2 52  ? 127.971 111.705 123.517 1.00 30.69 ?  31  LEU C CD1   1 
ATOM   11257 C  CD2   . LEU C 2 52  ? 126.286 109.949 124.246 1.00 29.91 ?  31  LEU C CD2   1 
ATOM   11258 N  N     . PRO C 2 53  ? 122.394 111.674 121.863 1.00 30.73 ?  32  PRO C N     1 
ATOM   11259 C  CA    . PRO C 2 53  ? 121.229 112.484 121.468 1.00 31.17 ?  32  PRO C CA    1 
ATOM   11260 C  C     . PRO C 2 53  ? 121.530 113.977 121.359 1.00 32.18 ?  32  PRO C C     1 
ATOM   11261 O  O     . PRO C 2 53  ? 120.915 114.668 120.531 1.00 32.66 ?  32  PRO C O     1 
ATOM   11262 C  CB    . PRO C 2 53  ? 120.215 112.230 122.590 1.00 30.99 ?  32  PRO C CB    1 
ATOM   11263 C  CG    . PRO C 2 53  ? 121.012 111.631 123.725 1.00 30.50 ?  32  PRO C CG    1 
ATOM   11264 C  CD    . PRO C 2 53  ? 122.111 110.868 123.067 1.00 30.46 ?  32  PRO C CD    1 
ATOM   11265 N  N     . GLU C 2 54  ? 122.475 114.459 122.170 1.00 32.62 ?  33  GLU C N     1 
ATOM   11266 C  CA    . GLU C 2 54  ? 122.876 115.876 122.164 1.00 33.44 ?  33  GLU C CA    1 
ATOM   11267 C  C     . GLU C 2 54  ? 123.467 116.343 120.829 1.00 33.59 ?  33  GLU C C     1 
ATOM   11268 O  O     . GLU C 2 54  ? 123.566 117.544 120.588 1.00 34.05 ?  33  GLU C O     1 
ATOM   11269 C  CB    . GLU C 2 54  ? 123.859 116.188 123.307 1.00 33.72 ?  33  GLU C CB    1 
ATOM   11270 C  CG    . GLU C 2 54  ? 123.236 116.197 124.717 1.00 34.53 ?  33  GLU C CG    1 
ATOM   11271 C  CD    . GLU C 2 54  ? 122.938 114.796 125.252 1.00 35.09 ?  33  GLU C CD    1 
ATOM   11272 O  OE1   . GLU C 2 54  ? 123.566 113.815 124.778 1.00 34.38 ?  33  GLU C OE1   1 
ATOM   11273 O  OE2   . GLU C 2 54  ? 122.071 114.678 126.148 1.00 35.53 -1 33  GLU C OE2   1 
ATOM   11274 N  N     . GLU C 2 55  ? 123.859 115.398 119.971 1.00 33.82 ?  34  GLU C N     1 
ATOM   11275 C  CA    . GLU C 2 55  ? 124.344 115.715 118.625 1.00 34.19 ?  34  GLU C CA    1 
ATOM   11276 C  C     . GLU C 2 55  ? 123.226 116.287 117.741 1.00 33.83 ?  34  GLU C C     1 
ATOM   11277 O  O     . GLU C 2 55  ? 123.499 116.954 116.744 1.00 33.93 ?  34  GLU C O     1 
ATOM   11278 C  CB    . GLU C 2 55  ? 124.943 114.475 117.938 1.00 34.52 ?  34  GLU C CB    1 
ATOM   11279 C  CG    . GLU C 2 55  ? 126.170 113.863 118.609 1.00 36.50 ?  34  GLU C CG    1 
ATOM   11280 C  CD    . GLU C 2 55  ? 126.856 112.824 117.727 1.00 40.03 ?  34  GLU C CD    1 
ATOM   11281 O  OE1   . GLU C 2 55  ? 127.685 113.208 116.872 1.00 42.43 ?  34  GLU C OE1   1 
ATOM   11282 O  OE2   . GLU C 2 55  ? 126.576 111.621 117.889 1.00 39.35 -1 34  GLU C OE2   1 
ATOM   11283 N  N     . ILE C 2 56  ? 121.979 115.988 118.105 1.00 33.31 ?  35  ILE C N     1 
ATOM   11284 C  CA    . ILE C 2 56  ? 120.788 116.400 117.359 1.00 33.14 ?  35  ILE C CA    1 
ATOM   11285 C  C     . ILE C 2 56  ? 120.062 117.499 118.142 1.00 32.58 ?  35  ILE C C     1 
ATOM   11286 O  O     . ILE C 2 56  ? 119.606 117.262 119.255 1.00 32.12 ?  35  ILE C O     1 
ATOM   11287 C  CB    . ILE C 2 56  ? 119.808 115.194 117.150 1.00 33.03 ?  35  ILE C CB    1 
ATOM   11288 C  CG1   . ILE C 2 56  ? 120.523 113.963 116.554 1.00 34.76 ?  35  ILE C CG1   1 
ATOM   11289 C  CG2   . ILE C 2 56  ? 118.581 115.600 116.323 1.00 33.61 ?  35  ILE C CG2   1 
ATOM   11290 C  CD1   . ILE C 2 56  ? 121.019 114.114 115.113 1.00 36.75 ?  35  ILE C CD1   1 
ATOM   11291 N  N     . ALA C 2 57  ? 119.967 118.697 117.569 1.00 32.36 ?  36  ALA C N     1 
ATOM   11292 C  CA    . ALA C 2 57  ? 119.213 119.786 118.196 1.00 32.17 ?  36  ALA C CA    1 
ATOM   11293 C  C     . ALA C 2 57  ? 117.711 119.577 117.975 1.00 31.76 ?  36  ALA C C     1 
ATOM   11294 O  O     . ALA C 2 57  ? 117.274 119.311 116.854 1.00 31.95 ?  36  ALA C O     1 
ATOM   11295 C  CB    . ALA C 2 57  ? 119.656 121.129 117.637 1.00 33.01 ?  36  ALA C CB    1 
ATOM   11296 N  N     . LEU C 2 58  ? 116.924 119.698 119.040 1.00 30.68 ?  37  LEU C N     1 
ATOM   11297 C  CA    . LEU C 2 58  ? 115.524 119.280 118.991 1.00 30.14 ?  37  LEU C CA    1 
ATOM   11298 C  C     . LEU C 2 58  ? 114.512 120.417 118.909 1.00 30.21 ?  37  LEU C C     1 
ATOM   11299 O  O     . LEU C 2 58  ? 113.328 120.177 118.639 1.00 29.91 ?  37  LEU C O     1 
ATOM   11300 C  CB    . LEU C 2 58  ? 115.202 118.359 120.174 1.00 29.46 ?  37  LEU C CB    1 
ATOM   11301 C  CG    . LEU C 2 58  ? 115.894 116.989 120.156 1.00 29.08 ?  37  LEU C CG    1 
ATOM   11302 C  CD1   . LEU C 2 58  ? 115.647 116.242 121.454 1.00 29.23 ?  37  LEU C CD1   1 
ATOM   11303 C  CD2   . LEU C 2 58  ? 115.438 116.149 118.963 1.00 28.84 ?  37  LEU C CD2   1 
ATOM   11304 N  N     . ASN C 2 59  ? 114.979 121.645 119.115 1.00 30.50 ?  38  ASN C N     1 
ATOM   11305 C  CA    . ASN C 2 59  ? 114.095 122.814 119.114 1.00 31.23 ?  38  ASN C CA    1 
ATOM   11306 C  C     . ASN C 2 59  ? 113.376 123.054 117.775 1.00 31.03 ?  38  ASN C C     1 
ATOM   11307 O  O     . ASN C 2 59  ? 112.347 123.722 117.735 1.00 30.82 ?  38  ASN C O     1 
ATOM   11308 C  CB    . ASN C 2 59  ? 114.831 124.074 119.609 1.00 31.98 ?  38  ASN C CB    1 
ATOM   11309 C  CG    . ASN C 2 59  ? 116.057 124.414 118.778 1.00 33.59 ?  38  ASN C CG    1 
ATOM   11310 O  OD1   . ASN C 2 59  ? 116.958 123.584 118.601 1.00 36.48 ?  38  ASN C OD1   1 
ATOM   11311 N  ND2   . ASN C 2 59  ? 116.107 125.644 118.274 1.00 34.77 ?  38  ASN C ND2   1 
ATOM   11312 N  N     . GLY C 2 60  ? 113.908 122.476 116.701 1.00 30.88 ?  39  GLY C N     1 
ATOM   11313 C  CA    . GLY C 2 60  ? 113.261 122.505 115.383 1.00 31.37 ?  39  GLY C CA    1 
ATOM   11314 C  C     . GLY C 2 60  ? 111.931 121.766 115.285 1.00 31.05 ?  39  GLY C C     1 
ATOM   11315 O  O     . GLY C 2 60  ? 111.106 122.115 114.453 1.00 31.21 ?  39  GLY C O     1 
ATOM   11316 N  N     . ASP C 2 61  ? 111.719 120.757 116.134 1.00 30.63 ?  40  ASP C N     1 
ATOM   11317 C  CA    . ASP C 2 61  ? 110.423 120.054 116.213 1.00 30.65 ?  40  ASP C CA    1 
ATOM   11318 C  C     . ASP C 2 61  ? 109.327 120.803 116.977 1.00 31.00 ?  40  ASP C C     1 
ATOM   11319 O  O     . ASP C 2 61  ? 108.175 120.366 116.968 1.00 30.91 ?  40  ASP C O     1 
ATOM   11320 C  CB    . ASP C 2 61  ? 110.582 118.676 116.868 1.00 30.00 ?  40  ASP C CB    1 
ATOM   11321 C  CG    . ASP C 2 61  ? 111.388 117.711 116.033 1.00 30.88 ?  40  ASP C CG    1 
ATOM   11322 O  OD1   . ASP C 2 61  ? 111.863 118.087 114.935 1.00 30.42 ?  40  ASP C OD1   1 
ATOM   11323 O  OD2   . ASP C 2 61  ? 111.552 116.560 116.494 1.00 31.17 -1 40  ASP C OD2   1 
ATOM   11324 N  N     . LEU C 2 62  ? 109.678 121.901 117.645 1.00 31.54 ?  41  LEU C N     1 
ATOM   11325 C  CA    . LEU C 2 62  ? 108.744 122.596 118.545 1.00 32.47 ?  41  LEU C CA    1 
ATOM   11326 C  C     . LEU C 2 62  ? 107.417 122.977 117.897 1.00 33.21 ?  41  LEU C C     1 
ATOM   11327 O  O     . LEU C 2 62  ? 106.355 122.825 118.509 1.00 32.84 ?  41  LEU C O     1 
ATOM   11328 C  CB    . LEU C 2 62  ? 109.388 123.835 119.170 1.00 33.14 ?  41  LEU C CB    1 
ATOM   11329 C  CG    . LEU C 2 62  ? 110.234 123.633 120.427 1.00 34.44 ?  41  LEU C CG    1 
ATOM   11330 C  CD1   . LEU C 2 62  ? 111.033 124.895 120.723 1.00 35.04 ?  41  LEU C CD1   1 
ATOM   11331 C  CD2   . LEU C 2 62  ? 109.350 123.248 121.621 1.00 35.52 ?  41  LEU C CD2   1 
ATOM   11332 N  N     . LEU C 2 63  ? 107.484 123.466 116.660 1.00 33.75 ?  42  LEU C N     1 
ATOM   11333 C  CA    . LEU C 2 63  ? 106.281 123.890 115.956 1.00 34.79 ?  42  LEU C CA    1 
ATOM   11334 C  C     . LEU C 2 63  ? 105.420 122.755 115.407 1.00 34.66 ?  42  LEU C C     1 
ATOM   11335 O  O     . LEU C 2 63  ? 104.205 122.785 115.592 1.00 34.67 ?  42  LEU C O     1 
ATOM   11336 C  CB    . LEU C 2 63  ? 106.599 124.922 114.871 1.00 35.27 ?  42  LEU C CB    1 
ATOM   11337 C  CG    . LEU C 2 63  ? 106.732 126.354 115.405 1.00 36.82 ?  42  LEU C CG    1 
ATOM   11338 C  CD1   . LEU C 2 63  ? 107.089 127.297 114.262 1.00 37.93 ?  42  LEU C CD1   1 
ATOM   11339 C  CD2   . LEU C 2 63  ? 105.457 126.830 116.099 1.00 37.85 ?  42  LEU C CD2   1 
ATOM   11340 N  N     . THR C 2 64  ? 106.020 121.766 114.739 1.00 34.70 ?  43  THR C N     1 
ATOM   11341 C  CA    . THR C 2 64  ? 105.225 120.623 114.257 1.00 35.10 ?  43  THR C CA    1 
ATOM   11342 C  C     . THR C 2 64  ? 104.595 119.833 115.416 1.00 34.78 ?  43  THR C C     1 
ATOM   11343 O  O     . THR C 2 64  ? 103.555 119.209 115.240 1.00 35.04 ?  43  THR C O     1 
ATOM   11344 C  CB    . THR C 2 64  ? 105.978 119.684 113.264 1.00 35.30 ?  43  THR C CB    1 
ATOM   11345 O  OG1   . THR C 2 64  ? 107.199 119.202 113.848 1.00 36.01 ?  43  THR C OG1   1 
ATOM   11346 C  CG2   . THR C 2 64  ? 106.279 120.404 111.950 1.00 35.96 ?  43  THR C CG2   1 
ATOM   11347 N  N     . TRP C 2 65  ? 105.210 119.892 116.599 1.00 34.63 ?  44  TRP C N     1 
ATOM   11348 C  CA    . TRP C 2 65  ? 104.647 119.268 117.804 1.00 34.37 ?  44  TRP C CA    1 
ATOM   11349 C  C     . TRP C 2 65  ? 103.435 120.044 118.316 1.00 35.13 ?  44  TRP C C     1 
ATOM   11350 O  O     . TRP C 2 65  ? 102.371 119.467 118.579 1.00 34.98 ?  44  TRP C O     1 
ATOM   11351 C  CB    . TRP C 2 65  ? 105.705 119.173 118.903 1.00 33.95 ?  44  TRP C CB    1 
ATOM   11352 C  CG    . TRP C 2 65  ? 105.165 118.747 120.230 1.00 33.26 ?  44  TRP C CG    1 
ATOM   11353 C  CD1   . TRP C 2 65  ? 104.923 119.543 121.315 1.00 32.51 ?  44  TRP C CD1   1 
ATOM   11354 C  CD2   . TRP C 2 65  ? 104.803 117.415 120.619 1.00 30.93 ?  44  TRP C CD2   1 
ATOM   11355 N  NE1   . TRP C 2 65  ? 104.436 118.787 122.360 1.00 31.66 ?  44  TRP C NE1   1 
ATOM   11356 C  CE2   . TRP C 2 65  ? 104.352 117.478 121.959 1.00 30.39 ?  44  TRP C CE2   1 
ATOM   11357 C  CE3   . TRP C 2 65  ? 104.821 116.174 119.968 1.00 30.36 ?  44  TRP C CE3   1 
ATOM   11358 C  CZ2   . TRP C 2 65  ? 103.914 116.350 122.656 1.00 29.16 ?  44  TRP C CZ2   1 
ATOM   11359 C  CZ3   . TRP C 2 65  ? 104.386 115.045 120.665 1.00 28.84 ?  44  TRP C CZ3   1 
ATOM   11360 C  CH2   . TRP C 2 65  ? 103.946 115.143 121.996 1.00 29.34 ?  44  TRP C CH2   1 
ATOM   11361 N  N     . LYS C 2 66  ? 103.618 121.354 118.469 1.00 35.69 ?  45  LYS C N     1 
ATOM   11362 C  CA    . LYS C 2 66  ? 102.554 122.264 118.866 1.00 36.38 ?  45  LYS C CA    1 
ATOM   11363 C  C     . LYS C 2 66  ? 101.290 122.085 118.018 1.00 36.24 ?  45  LYS C C     1 
ATOM   11364 O  O     . LYS C 2 66  ? 100.187 122.230 118.531 1.00 36.78 ?  45  LYS C O     1 
ATOM   11365 C  CB    . LYS C 2 66  ? 103.064 123.702 118.754 1.00 37.14 ?  45  LYS C CB    1 
ATOM   11366 C  CG    . LYS C 2 66  ? 102.082 124.780 119.181 1.00 38.91 ?  45  LYS C CG    1 
ATOM   11367 C  CD    . LYS C 2 66  ? 102.605 126.162 118.787 1.00 41.12 ?  45  LYS C CD    1 
ATOM   11368 C  CE    . LYS C 2 66  ? 101.834 127.264 119.496 1.00 43.00 ?  45  LYS C CE    1 
ATOM   11369 N  NZ    . LYS C 2 66  ? 101.735 127.005 120.964 1.00 44.38 1  45  LYS C NZ    1 
ATOM   11370 N  N     . TYR C 2 67  ? 101.474 121.732 116.742 1.00 36.03 ?  46  TYR C N     1 
ATOM   11371 C  CA    . TYR C 2 67  ? 100.398 121.650 115.740 1.00 36.03 ?  46  TYR C CA    1 
ATOM   11372 C  C     . TYR C 2 67  ? 99.613  120.332 115.726 1.00 35.25 ?  46  TYR C C     1 
ATOM   11373 O  O     . TYR C 2 67  ? 98.570  120.231 115.072 1.00 35.32 ?  46  TYR C O     1 
ATOM   11374 C  CB    . TYR C 2 67  ? 100.960 121.890 114.328 1.00 36.60 ?  46  TYR C CB    1 
ATOM   11375 C  CG    . TYR C 2 67  ? 101.585 123.259 114.090 1.00 37.85 ?  46  TYR C CG    1 
ATOM   11376 C  CD1   . TYR C 2 67  ? 101.372 124.313 114.978 1.00 38.97 ?  46  TYR C CD1   1 
ATOM   11377 C  CD2   . TYR C 2 67  ? 102.379 123.499 112.960 1.00 40.06 ?  46  TYR C CD2   1 
ATOM   11378 C  CE1   . TYR C 2 67  ? 101.948 125.566 114.770 1.00 40.36 ?  46  TYR C CE1   1 
ATOM   11379 C  CE2   . TYR C 2 67  ? 102.960 124.757 112.736 1.00 40.53 ?  46  TYR C CE2   1 
ATOM   11380 C  CZ    . TYR C 2 67  ? 102.733 125.786 113.650 1.00 41.43 ?  46  TYR C CZ    1 
ATOM   11381 O  OH    . TYR C 2 67  ? 103.282 127.041 113.457 1.00 41.48 ?  46  TYR C OH    1 
ATOM   11382 N  N     . LEU C 2 68  ? 100.125 119.319 116.420 1.00 33.80 ?  47  LEU C N     1 
ATOM   11383 C  CA    . LEU C 2 68  ? 99.443  118.031 116.492 1.00 32.77 ?  47  LEU C CA    1 
ATOM   11384 C  C     . LEU C 2 68  ? 98.237  118.124 117.417 1.00 31.84 ?  47  LEU C C     1 
ATOM   11385 O  O     . LEU C 2 68  ? 98.242  118.894 118.374 1.00 31.90 ?  47  LEU C O     1 
ATOM   11386 C  CB    . LEU C 2 68  ? 100.390 116.942 117.000 1.00 32.39 ?  47  LEU C CB    1 
ATOM   11387 C  CG    . LEU C 2 68  ? 101.625 116.521 116.201 1.00 32.68 ?  47  LEU C CG    1 
ATOM   11388 C  CD1   . LEU C 2 68  ? 102.372 115.432 116.966 1.00 33.03 ?  47  LEU C CD1   1 
ATOM   11389 C  CD2   . LEU C 2 68  ? 101.274 116.042 114.788 1.00 32.78 ?  47  LEU C CD2   1 
ATOM   11390 N  N     . GLY C 2 69  ? 97.215  117.322 117.141 1.00 30.99 ?  48  GLY C N     1 
ATOM   11391 C  CA    . GLY C 2 69  ? 96.068  117.212 118.041 1.00 30.58 ?  48  GLY C CA    1 
ATOM   11392 C  C     . GLY C 2 69  ? 96.444  116.616 119.391 1.00 29.87 ?  48  GLY C C     1 
ATOM   11393 O  O     . GLY C 2 69  ? 97.489  115.981 119.529 1.00 28.79 ?  48  GLY C O     1 
ATOM   11394 N  N     . LYS C 2 70  ? 95.596  116.829 120.392 1.00 29.89 ?  49  LYS C N     1 
ATOM   11395 C  CA    . LYS C 2 70  ? 95.840  116.282 121.726 1.00 29.49 ?  49  LYS C CA    1 
ATOM   11396 C  C     . LYS C 2 70  ? 95.950  114.746 121.711 1.00 28.74 ?  49  LYS C C     1 
ATOM   11397 O  O     . LYS C 2 70  ? 96.803  114.178 122.406 1.00 27.27 ?  49  LYS C O     1 
ATOM   11398 C  CB    . LYS C 2 70  ? 94.782  116.772 122.720 1.00 30.67 ?  49  LYS C CB    1 
ATOM   11399 C  CG    . LYS C 2 70  ? 95.047  118.213 123.222 1.00 33.73 ?  49  LYS C CG    1 
ATOM   11400 C  CD    . LYS C 2 70  ? 93.813  118.862 123.874 1.00 38.93 ?  49  LYS C CD    1 
ATOM   11401 C  CE    . LYS C 2 70  ? 93.566  118.388 125.312 1.00 41.04 ?  49  LYS C CE    1 
ATOM   11402 N  NZ    . LYS C 2 70  ? 94.554  118.926 126.294 1.00 42.21 1  49  LYS C NZ    1 
ATOM   11403 N  N     . ASN C 2 71  ? 95.102  114.097 120.906 1.00 27.54 ?  50  ASN C N     1 
ATOM   11404 C  CA    . ASN C 2 71  ? 95.155  112.646 120.713 1.00 27.00 ?  50  ASN C CA    1 
ATOM   11405 C  C     . ASN C 2 71  ? 96.501  112.175 120.160 1.00 26.19 ?  50  ASN C C     1 
ATOM   11406 O  O     . ASN C 2 71  ? 97.057  111.154 120.615 1.00 25.38 ?  50  ASN C O     1 
ATOM   11407 C  CB    . ASN C 2 71  ? 94.007  112.163 119.799 1.00 27.08 ?  50  ASN C CB    1 
ATOM   11408 C  CG    . ASN C 2 71  ? 94.035  112.794 118.386 1.00 28.69 ?  50  ASN C CG    1 
ATOM   11409 O  OD1   . ASN C 2 71  ? 94.249  114.009 118.214 1.00 30.45 ?  50  ASN C OD1   1 
ATOM   11410 N  ND2   . ASN C 2 71  ? 93.786  111.958 117.366 1.00 29.42 ?  50  ASN C ND2   1 
ATOM   11411 N  N     . GLU C 2 72  ? 97.015  112.922 119.185 1.00 24.91 ?  51  GLU C N     1 
ATOM   11412 C  CA    . GLU C 2 72  ? 98.276  112.583 118.536 1.00 24.97 ?  51  GLU C CA    1 
ATOM   11413 C  C     . GLU C 2 72  ? 99.459  112.729 119.500 1.00 24.45 ?  51  GLU C C     1 
ATOM   11414 O  O     . GLU C 2 72  ? 100.332 111.849 119.566 1.00 23.90 ?  51  GLU C O     1 
ATOM   11415 C  CB    . GLU C 2 72  ? 98.483  113.446 117.291 1.00 25.27 ?  51  GLU C CB    1 
ATOM   11416 C  CG    . GLU C 2 72  ? 97.472  113.182 116.177 1.00 26.16 ?  51  GLU C CG    1 
ATOM   11417 C  CD    . GLU C 2 72  ? 97.689  114.101 114.982 1.00 28.70 ?  51  GLU C CD    1 
ATOM   11418 O  OE1   . GLU C 2 72  ? 97.307  115.286 115.066 1.00 28.70 ?  51  GLU C OE1   1 
ATOM   11419 O  OE2   . GLU C 2 72  ? 98.241  113.639 113.958 1.00 28.92 -1 51  GLU C OE2   1 
ATOM   11420 N  N     . GLN C 2 73  ? 99.464  113.825 120.258 1.00 23.75 ?  52  GLN C N     1 
ATOM   11421 C  CA    . GLN C 2 73  ? 100.515 114.071 121.243 1.00 23.94 ?  52  GLN C CA    1 
ATOM   11422 C  C     . GLN C 2 73  ? 100.496 113.011 122.346 1.00 23.36 ?  52  GLN C C     1 
ATOM   11423 O  O     . GLN C 2 73  ? 101.546 112.572 122.799 1.00 22.95 ?  52  GLN C O     1 
ATOM   11424 C  CB    . GLN C 2 73  ? 100.367 115.465 121.871 1.00 24.28 ?  52  GLN C CB    1 
ATOM   11425 C  CG    . GLN C 2 73  ? 100.745 116.645 120.955 1.00 25.22 ?  52  GLN C CG    1 
ATOM   11426 C  CD    . GLN C 2 73  ? 100.671 118.004 121.662 1.00 29.02 ?  52  GLN C CD    1 
ATOM   11427 O  OE1   . GLN C 2 73  ? 100.326 118.086 122.839 1.00 32.08 ?  52  GLN C OE1   1 
ATOM   11428 N  NE2   . GLN C 2 73  ? 100.999 119.068 120.939 1.00 29.13 ?  52  GLN C NE2   1 
ATOM   11429 N  N     . ASP C 2 74  ? 99.294  112.633 122.786 1.00 23.02 ?  53  ASP C N     1 
ATOM   11430 C  CA    . ASP C 2 74  ? 99.123  111.624 123.822 1.00 23.44 ?  53  ASP C CA    1 
ATOM   11431 C  C     . ASP C 2 74  ? 99.704  110.279 123.368 1.00 23.00 ?  53  ASP C C     1 
ATOM   11432 O  O     . ASP C 2 74  ? 100.475 109.661 124.097 1.00 22.96 ?  53  ASP C O     1 
ATOM   11433 C  CB    . ASP C 2 74  ? 97.639  111.461 124.181 1.00 23.31 ?  53  ASP C CB    1 
ATOM   11434 C  CG    . ASP C 2 74  ? 97.423  110.551 125.372 1.00 25.80 ?  53  ASP C CG    1 
ATOM   11435 O  OD1   . ASP C 2 74  ? 97.926  110.867 126.482 1.00 27.95 ?  53  ASP C OD1   1 
ATOM   11436 O  OD2   . ASP C 2 74  ? 96.741  109.521 125.202 1.00 26.30 -1 53  ASP C OD2   1 
ATOM   11437 N  N     . THR C 2 75  ? 99.316  109.837 122.175 1.00 22.20 ?  54  THR C N     1 
ATOM   11438 C  CA    . THR C 2 75  ? 99.809  108.584 121.618 1.00 21.84 ?  54  THR C CA    1 
ATOM   11439 C  C     . THR C 2 75  ? 101.324 108.634 121.454 1.00 22.09 ?  54  THR C C     1 
ATOM   11440 O  O     . THR C 2 75  ? 102.017 107.689 121.816 1.00 21.88 ?  54  THR C O     1 
ATOM   11441 C  CB    . THR C 2 75  ? 99.110  108.228 120.276 1.00 21.74 ?  54  THR C CB    1 
ATOM   11442 O  OG1   . THR C 2 75  ? 97.728  107.974 120.534 1.00 22.09 ?  54  THR C OG1   1 
ATOM   11443 C  CG2   . THR C 2 75  ? 99.715  106.963 119.653 1.00 19.76 ?  54  THR C CG2   1 
ATOM   11444 N  N     . TYR C 2 76  ? 101.832 109.742 120.923 1.00 22.38 ?  55  TYR C N     1 
ATOM   11445 C  CA    . TYR C 2 76  ? 103.271 109.908 120.741 1.00 22.85 ?  55  TYR C CA    1 
ATOM   11446 C  C     . TYR C 2 76  ? 104.061 109.785 122.056 1.00 22.56 ?  55  TYR C C     1 
ATOM   11447 O  O     . TYR C 2 76  ? 105.058 109.070 122.100 1.00 21.97 ?  55  TYR C O     1 
ATOM   11448 C  CB    . TYR C 2 76  ? 103.568 111.240 120.064 1.00 23.57 ?  55  TYR C CB    1 
ATOM   11449 C  CG    . TYR C 2 76  ? 104.956 111.359 119.470 1.00 25.59 ?  55  TYR C CG    1 
ATOM   11450 C  CD1   . TYR C 2 76  ? 105.199 111.009 118.137 1.00 27.49 ?  55  TYR C CD1   1 
ATOM   11451 C  CD2   . TYR C 2 76  ? 106.017 111.855 120.227 1.00 27.70 ?  55  TYR C CD2   1 
ATOM   11452 C  CE1   . TYR C 2 76  ? 106.475 111.144 117.578 1.00 30.28 ?  55  TYR C CE1   1 
ATOM   11453 C  CE2   . TYR C 2 76  ? 107.301 111.988 119.680 1.00 30.38 ?  55  TYR C CE2   1 
ATOM   11454 C  CZ    . TYR C 2 76  ? 107.520 111.628 118.355 1.00 31.39 ?  55  TYR C CZ    1 
ATOM   11455 O  OH    . TYR C 2 76  ? 108.783 111.772 117.811 1.00 32.67 ?  55  TYR C OH    1 
ATOM   11456 N  N     . MET C 2 77  ? 103.621 110.483 123.105 1.00 23.14 ?  56  MET C N     1 
ATOM   11457 C  CA    . MET C 2 77  ? 104.287 110.434 124.420 1.00 23.90 ?  56  MET C CA    1 
ATOM   11458 C  C     . MET C 2 77  ? 104.305 109.013 124.967 1.00 23.24 ?  56  MET C C     1 
ATOM   11459 O  O     . MET C 2 77  ? 105.312 108.544 125.512 1.00 22.47 ?  56  MET C O     1 
ATOM   11460 C  CB    . MET C 2 77  ? 103.567 111.323 125.441 1.00 24.38 ?  56  MET C CB    1 
ATOM   11461 C  CG    . MET C 2 77  ? 103.583 112.818 125.158 1.00 28.52 ?  56  MET C CG    1 
ATOM   11462 S  SD    . MET C 2 77  ? 105.163 113.575 125.512 1.00 34.32 ?  56  MET C SD    1 
ATOM   11463 C  CE    . MET C 2 77  ? 105.273 113.382 127.294 1.00 33.84 ?  56  MET C CE    1 
ATOM   11464 N  N     . LYS C 2 78  ? 103.168 108.336 124.825 1.00 23.25 ?  57  LYS C N     1 
ATOM   11465 C  CA    . LYS C 2 78  ? 102.983 107.024 125.431 1.00 22.98 ?  57  LYS C CA    1 
ATOM   11466 C  C     . LYS C 2 78  ? 103.827 105.989 124.701 1.00 22.77 ?  57  LYS C C     1 
ATOM   11467 O  O     . LYS C 2 78  ? 104.476 105.158 125.329 1.00 22.56 ?  57  LYS C O     1 
ATOM   11468 C  CB    . LYS C 2 78  ? 101.495 106.657 125.467 1.00 22.99 ?  57  LYS C CB    1 
ATOM   11469 C  CG    . LYS C 2 78  ? 100.732 107.401 126.566 1.00 24.86 ?  57  LYS C CG    1 
ATOM   11470 C  CD    . LYS C 2 78  ? 99.221  107.186 126.481 1.00 27.37 ?  57  LYS C CD    1 
ATOM   11471 C  CE    . LYS C 2 78  ? 98.518  107.737 127.727 1.00 28.99 ?  57  LYS C CE    1 
ATOM   11472 N  NZ    . LYS C 2 78  ? 97.038  107.697 127.533 1.00 29.82 1  57  LYS C NZ    1 
ATOM   11473 N  N     . VAL C 2 79  ? 103.820 106.077 123.373 1.00 22.70 ?  58  VAL C N     1 
ATOM   11474 C  CA    . VAL C 2 79  ? 104.641 105.251 122.491 1.00 23.48 ?  58  VAL C CA    1 
ATOM   11475 C  C     . VAL C 2 79  ? 106.137 105.320 122.882 1.00 23.04 ?  58  VAL C C     1 
ATOM   11476 O  O     . VAL C 2 79  ? 106.789 104.277 123.089 1.00 22.83 ?  58  VAL C O     1 
ATOM   11477 C  CB    . VAL C 2 79  ? 104.351 105.667 121.014 1.00 24.24 ?  58  VAL C CB    1 
ATOM   11478 C  CG1   . VAL C 2 79  ? 105.580 105.614 120.124 1.00 25.71 ?  58  VAL C CG1   1 
ATOM   11479 C  CG2   . VAL C 2 79  ? 103.165 104.851 120.454 1.00 25.04 ?  58  VAL C CG2   1 
ATOM   11480 N  N     . LEU C 2 80  ? 106.660 106.533 123.033 1.00 22.84 ?  59  LEU C N     1 
ATOM   11481 C  CA    . LEU C 2 80  ? 108.065 106.714 123.403 1.00 23.35 ?  59  LEU C CA    1 
ATOM   11482 C  C     . LEU C 2 80  ? 108.336 106.243 124.837 1.00 22.75 ?  59  LEU C C     1 
ATOM   11483 O  O     . LEU C 2 80  ? 109.416 105.729 125.120 1.00 22.75 ?  59  LEU C O     1 
ATOM   11484 C  CB    . LEU C 2 80  ? 108.523 108.168 123.224 1.00 23.91 ?  59  LEU C CB    1 
ATOM   11485 C  CG    . LEU C 2 80  ? 108.636 108.838 121.841 1.00 26.63 ?  59  LEU C CG    1 
ATOM   11486 C  CD1   . LEU C 2 80  ? 109.513 110.077 121.933 1.00 26.99 ?  59  LEU C CD1   1 
ATOM   11487 C  CD2   . LEU C 2 80  ? 109.177 107.910 120.766 1.00 27.23 ?  59  LEU C CD2   1 
ATOM   11488 N  N     . ALA C 2 81  ? 107.349 106.395 125.723 1.00 22.28 ?  60  ALA C N     1 
ATOM   11489 C  CA    . ALA C 2 81  ? 107.464 105.918 127.104 1.00 22.21 ?  60  ALA C CA    1 
ATOM   11490 C  C     . ALA C 2 81  ? 107.565 104.390 127.162 1.00 22.07 ?  60  ALA C C     1 
ATOM   11491 O  O     . ALA C 2 81  ? 108.370 103.862 127.922 1.00 21.97 ?  60  ALA C O     1 
ATOM   11492 C  CB    . ALA C 2 81  ? 106.297 106.443 127.968 1.00 22.38 ?  60  ALA C CB    1 
ATOM   11493 N  N     . GLY C 2 82  ? 106.779 103.702 126.325 1.00 21.67 ?  61  GLY C N     1 
ATOM   11494 C  CA    . GLY C 2 82  ? 106.839 102.250 126.177 1.00 21.74 ?  61  GLY C CA    1 
ATOM   11495 C  C     . GLY C 2 82  ? 108.192 101.788 125.666 1.00 21.79 ?  61  GLY C C     1 
ATOM   11496 O  O     . GLY C 2 82  ? 108.730 100.764 126.115 1.00 21.93 ?  61  GLY C O     1 
ATOM   11497 N  N     . LEU C 2 83  ? 108.752 102.561 124.737 1.00 21.54 ?  62  LEU C N     1 
ATOM   11498 C  CA    . LEU C 2 83  ? 110.098 102.314 124.223 1.00 21.12 ?  62  LEU C CA    1 
ATOM   11499 C  C     . LEU C 2 83  ? 111.143 102.516 125.311 1.00 20.89 ?  62  LEU C C     1 
ATOM   11500 O  O     . LEU C 2 83  ? 112.071 101.714 125.428 1.00 20.84 ?  62  LEU C O     1 
ATOM   11501 C  CB    . LEU C 2 83  ? 110.418 103.219 123.028 1.00 21.23 ?  62  LEU C CB    1 
ATOM   11502 C  CG    . LEU C 2 83  ? 109.628 103.047 121.724 1.00 21.98 ?  62  LEU C CG    1 
ATOM   11503 C  CD1   . LEU C 2 83  ? 109.979 104.145 120.716 1.00 24.12 ?  62  LEU C CD1   1 
ATOM   11504 C  CD2   . LEU C 2 83  ? 109.850 101.683 121.100 1.00 22.03 ?  62  LEU C CD2   1 
ATOM   11505 N  N     . THR C 2 84  ? 110.988 103.587 126.093 1.00 19.93 ?  63  THR C N     1 
ATOM   11506 C  CA    . THR C 2 84  ? 111.913 103.889 127.182 1.00 19.71 ?  63  THR C CA    1 
ATOM   11507 C  C     . THR C 2 84  ? 111.979 102.736 128.171 1.00 19.63 ?  63  THR C C     1 
ATOM   11508 O  O     . THR C 2 84  ? 113.065 102.375 128.633 1.00 19.62 ?  63  THR C O     1 
ATOM   11509 C  CB    . THR C 2 84  ? 111.517 105.187 127.929 1.00 20.22 ?  63  THR C CB    1 
ATOM   11510 O  OG1   . THR C 2 84  ? 111.322 106.252 126.982 1.00 19.37 ?  63  THR C OG1   1 
ATOM   11511 C  CG2   . THR C 2 84  ? 112.581 105.568 128.930 1.00 19.45 ?  63  THR C CG2   1 
ATOM   11512 N  N     . LEU C 2 85  ? 110.821 102.169 128.497 1.00 19.66 ?  64  LEU C N     1 
ATOM   11513 C  CA    . LEU C 2 85  ? 110.747 101.051 129.434 1.00 20.51 ?  64  LEU C CA    1 
ATOM   11514 C  C     . LEU C 2 85  ? 111.520 99.839  128.904 1.00 20.84 ?  64  LEU C C     1 
ATOM   11515 O  O     . LEU C 2 85  ? 112.354 99.271  129.612 1.00 21.30 ?  64  LEU C O     1 
ATOM   11516 C  CB    . LEU C 2 85  ? 109.290 100.683 129.765 1.00 20.03 ?  64  LEU C CB    1 
ATOM   11517 C  CG    . LEU C 2 85  ? 109.144 99.482  130.727 1.00 21.43 ?  64  LEU C CG    1 
ATOM   11518 C  CD1   . LEU C 2 85  ? 109.701 99.789  132.137 1.00 21.61 ?  64  LEU C CD1   1 
ATOM   11519 C  CD2   . LEU C 2 85  ? 107.704 98.985  130.828 1.00 20.99 ?  64  LEU C CD2   1 
ATOM   11520 N  N     . LEU C 2 86  ? 111.250 99.467  127.658 1.00 21.37 ?  65  LEU C N     1 
ATOM   11521 C  CA    . LEU C 2 86  ? 111.951 98.363  126.999 1.00 21.92 ?  65  LEU C CA    1 
ATOM   11522 C  C     . LEU C 2 86  ? 113.479 98.536  127.007 1.00 21.76 ?  65  LEU C C     1 
ATOM   11523 O  O     . LEU C 2 86  ? 114.202 97.606  127.362 1.00 21.72 ?  65  LEU C O     1 
ATOM   11524 C  CB    . LEU C 2 86  ? 111.446 98.177  125.560 1.00 22.42 ?  65  LEU C CB    1 
ATOM   11525 C  CG    . LEU C 2 86  ? 110.018 97.664  125.280 1.00 24.26 ?  65  LEU C CG    1 
ATOM   11526 C  CD1   . LEU C 2 86  ? 109.741 97.706  123.778 1.00 24.67 ?  65  LEU C CD1   1 
ATOM   11527 C  CD2   . LEU C 2 86  ? 109.813 96.256  125.812 1.00 25.60 ?  65  LEU C CD2   1 
ATOM   11528 N  N     . ASP C 2 87  ? 113.962 99.717  126.615 1.00 21.75 ?  66  ASP C N     1 
ATOM   11529 C  CA    . ASP C 2 87  ? 115.407 100.015 126.633 1.00 21.99 ?  66  ASP C CA    1 
ATOM   11530 C  C     . ASP C 2 87  ? 116.019 100.059 128.038 1.00 21.76 ?  66  ASP C C     1 
ATOM   11531 O  O     . ASP C 2 87  ? 117.187 99.690  128.228 1.00 21.65 ?  66  ASP C O     1 
ATOM   11532 C  CB    . ASP C 2 87  ? 115.702 101.345 125.934 1.00 22.23 ?  66  ASP C CB    1 
ATOM   11533 C  CG    . ASP C 2 87  ? 116.059 101.172 124.484 1.00 24.59 ?  66  ASP C CG    1 
ATOM   11534 O  OD1   . ASP C 2 87  ? 116.831 100.242 124.156 1.00 27.46 ?  66  ASP C OD1   1 
ATOM   11535 O  OD2   . ASP C 2 87  ? 115.570 101.981 123.669 1.00 27.98 -1 66  ASP C OD2   1 
ATOM   11536 N  N     . THR C 2 88  ? 115.242 100.544 129.004 1.00 21.50 ?  67  THR C N     1 
ATOM   11537 C  CA    . THR C 2 88  ? 115.657 100.524 130.402 1.00 21.80 ?  67  THR C CA    1 
ATOM   11538 C  C     . THR C 2 88  ? 116.000 99.088  130.844 1.00 22.04 ?  67  THR C C     1 
ATOM   11539 O  O     . THR C 2 88  ? 117.065 98.846  131.429 1.00 22.21 ?  67  THR C O     1 
ATOM   11540 C  CB    . THR C 2 88  ? 114.581 101.146 131.309 1.00 22.15 ?  67  THR C CB    1 
ATOM   11541 O  OG1   . THR C 2 88  ? 114.363 102.501 130.909 1.00 22.23 ?  67  THR C OG1   1 
ATOM   11542 C  CG2   . THR C 2 88  ? 115.003 101.129 132.781 1.00 21.19 ?  67  THR C CG2   1 
ATOM   11543 N  N     . GLU C 2 89  ? 115.115 98.145  130.533 1.00 21.55 ?  68  GLU C N     1 
ATOM   11544 C  CA    . GLU C 2 89  ? 115.312 96.764  130.953 1.00 21.81 ?  68  GLU C CA    1 
ATOM   11545 C  C     . GLU C 2 89  ? 116.340 96.030  130.078 1.00 21.35 ?  68  GLU C C     1 
ATOM   11546 O  O     . GLU C 2 89  ? 117.099 95.200  130.573 1.00 21.34 ?  68  GLU C O     1 
ATOM   11547 C  CB    . GLU C 2 89  ? 113.972 96.026  131.045 1.00 22.25 ?  68  GLU C CB    1 
ATOM   11548 C  CG    . GLU C 2 89  ? 113.190 96.356  132.349 1.00 24.02 ?  68  GLU C CG    1 
ATOM   11549 C  CD    . GLU C 2 89  ? 114.030 96.147  133.611 1.00 25.78 ?  68  GLU C CD    1 
ATOM   11550 O  OE1   . GLU C 2 89  ? 114.708 95.104  133.725 1.00 26.69 ?  68  GLU C OE1   1 
ATOM   11551 O  OE2   . GLU C 2 89  ? 114.013 97.029  134.502 1.00 28.98 -1 68  GLU C OE2   1 
ATOM   11552 N  N     . GLN C 2 90  ? 116.397 96.378  128.794 1.00 20.82 ?  69  GLN C N     1 
ATOM   11553 C  CA    . GLN C 2 90  ? 117.397 95.810  127.896 1.00 21.28 ?  69  GLN C CA    1 
ATOM   11554 C  C     . GLN C 2 90  ? 118.809 96.232  128.314 1.00 21.24 ?  69  GLN C C     1 
ATOM   11555 O  O     . GLN C 2 90  ? 119.747 95.434  128.234 1.00 20.99 ?  69  GLN C O     1 
ATOM   11556 C  CB    . GLN C 2 90  ? 117.109 96.192  126.433 1.00 21.86 ?  69  GLN C CB    1 
ATOM   11557 C  CG    . GLN C 2 90  ? 117.895 95.355  125.399 1.00 24.29 ?  69  GLN C CG    1 
ATOM   11558 C  CD    . GLN C 2 90  ? 117.429 93.897  125.327 1.00 27.14 ?  69  GLN C CD    1 
ATOM   11559 O  OE1   . GLN C 2 90  ? 116.817 93.381  126.267 1.00 27.13 ?  69  GLN C OE1   1 
ATOM   11560 N  NE2   . GLN C 2 90  ? 117.736 93.226  124.214 1.00 27.69 ?  69  GLN C NE2   1 
ATOM   11561 N  N     . GLY C 2 91  ? 118.941 97.473  128.790 1.00 20.62 ?  70  GLY C N     1 
ATOM   11562 C  CA    . GLY C 2 91  ? 120.229 98.008  129.242 1.00 22.00 ?  70  GLY C CA    1 
ATOM   11563 C  C     . GLY C 2 91  ? 120.607 97.577  130.645 1.00 22.45 ?  70  GLY C C     1 
ATOM   11564 O  O     . GLY C 2 91  ? 121.755 97.205  130.877 1.00 23.53 ?  70  GLY C O     1 
ATOM   11565 N  N     . ASN C 2 92  ? 119.649 97.627  131.572 1.00 22.79 ?  71  ASN C N     1 
ATOM   11566 C  CA    . ASN C 2 92  ? 119.888 97.266  132.979 1.00 23.85 ?  71  ASN C CA    1 
ATOM   11567 C  C     . ASN C 2 92  ? 120.087 95.767  133.175 1.00 24.33 ?  71  ASN C C     1 
ATOM   11568 O  O     . ASN C 2 92  ? 120.874 95.348  134.032 1.00 24.17 ?  71  ASN C O     1 
ATOM   11569 C  CB    . ASN C 2 92  ? 118.713 97.690  133.869 1.00 23.74 ?  71  ASN C CB    1 
ATOM   11570 C  CG    . ASN C 2 92  ? 118.585 99.195  134.028 1.00 24.38 ?  71  ASN C CG    1 
ATOM   11571 O  OD1   . ASN C 2 92  ? 119.348 99.981  133.452 1.00 25.16 ?  71  ASN C OD1   1 
ATOM   11572 N  ND2   . ASN C 2 92  ? 117.602 99.604  134.812 1.00 24.07 ?  71  ASN C ND2   1 
ATOM   11573 N  N     . THR C 2 93  ? 119.376 94.967  132.378 1.00 23.97 ?  72  THR C N     1 
ATOM   11574 C  CA    . THR C 2 93  ? 119.200 93.542  132.695 1.00 24.97 ?  72  THR C CA    1 
ATOM   11575 C  C     . THR C 2 93  ? 119.567 92.632  131.532 1.00 24.52 ?  72  THR C C     1 
ATOM   11576 O  O     . THR C 2 93  ? 120.451 91.794  131.664 1.00 25.39 ?  72  THR C O     1 
ATOM   11577 C  CB    . THR C 2 93  ? 117.747 93.237  133.147 1.00 24.54 ?  72  THR C CB    1 
ATOM   11578 O  OG1   . THR C 2 93  ? 117.386 94.103  134.231 1.00 26.43 ?  72  THR C OG1   1 
ATOM   11579 C  CG2   . THR C 2 93  ? 117.605 91.794  133.603 1.00 26.83 ?  72  THR C CG2   1 
ATOM   11580 N  N     . GLY C 2 94  ? 118.889 92.812  130.408 1.00 24.37 ?  73  GLY C N     1 
ATOM   11581 C  CA    . GLY C 2 94  ? 118.973 91.893  129.262 1.00 24.24 ?  73  GLY C CA    1 
ATOM   11582 C  C     . GLY C 2 94  ? 120.363 91.742  128.681 1.00 24.94 ?  73  GLY C C     1 
ATOM   11583 O  O     . GLY C 2 94  ? 120.924 90.641  128.667 1.00 25.86 ?  73  GLY C O     1 
ATOM   11584 N  N     . MET C 2 95  ? 120.924 92.845  128.197 1.00 24.07 ?  74  MET C N     1 
ATOM   11585 C  CA    . MET C 2 95  ? 122.254 92.791  127.604 1.00 24.35 ?  74  MET C CA    1 
ATOM   11586 C  C     . MET C 2 95  ? 123.383 92.409  128.580 1.00 23.52 ?  74  MET C C     1 
ATOM   11587 O  O     . MET C 2 95  ? 124.211 91.581  128.212 1.00 23.40 ?  74  MET C O     1 
ATOM   11588 C  CB    . MET C 2 95  ? 122.571 94.064  126.820 1.00 24.38 ?  74  MET C CB    1 
ATOM   11589 C  CG    . MET C 2 95  ? 121.772 94.210  125.524 1.00 27.47 ?  74  MET C CG    1 
ATOM   11590 S  SD    . MET C 2 95  ? 122.155 92.863  124.372 1.00 32.54 ?  74  MET C SD    1 
ATOM   11591 C  CE    . MET C 2 95  ? 123.784 93.307  123.881 1.00 34.32 ?  74  MET C CE    1 
ATOM   11592 N  N     . PRO C 2 96  ? 123.420 92.993  129.811 1.00 23.36 ?  75  PRO C N     1 
ATOM   11593 C  CA    . PRO C 2 96  ? 124.441 92.577  130.797 1.00 23.27 ?  75  PRO C CA    1 
ATOM   11594 C  C     . PRO C 2 96  ? 124.377 91.103  131.183 1.00 23.77 ?  75  PRO C C     1 
ATOM   11595 O  O     . PRO C 2 96  ? 125.421 90.463  131.308 1.00 23.46 ?  75  PRO C O     1 
ATOM   11596 C  CB    . PRO C 2 96  ? 124.120 93.432  132.034 1.00 23.55 ?  75  PRO C CB    1 
ATOM   11597 C  CG    . PRO C 2 96  ? 123.452 94.647  131.488 1.00 23.85 ?  75  PRO C CG    1 
ATOM   11598 C  CD    . PRO C 2 96  ? 122.632 94.138  130.313 1.00 22.76 ?  75  PRO C CD    1 
ATOM   11599 N  N     . ILE C 2 97  ? 123.170 90.571  131.393 1.00 23.81 ?  76  ILE C N     1 
ATOM   11600 C  CA    . ILE C 2 97  ? 123.020 89.161  131.761 1.00 24.52 ?  76  ILE C CA    1 
ATOM   11601 C  C     . ILE C 2 97  ? 123.439 88.192  130.634 1.00 23.92 ?  76  ILE C C     1 
ATOM   11602 O  O     . ILE C 2 97  ? 124.117 87.186  130.887 1.00 23.99 ?  76  ILE C O     1 
ATOM   11603 C  CB    . ILE C 2 97  ? 121.600 88.850  132.316 1.00 24.49 ?  76  ILE C CB    1 
ATOM   11604 C  CG1   . ILE C 2 97  ? 121.628 87.596  133.187 1.00 27.08 ?  76  ILE C CG1   1 
ATOM   11605 C  CG2   . ILE C 2 97  ? 120.554 88.703  131.191 1.00 26.06 ?  76  ILE C CG2   1 
ATOM   11606 C  CD1   . ILE C 2 97  ? 120.503 87.562  134.211 1.00 31.37 ?  76  ILE C CD1   1 
ATOM   11607 N  N     . VAL C 2 98  ? 123.068 88.509  129.398 1.00 23.97 ?  77  VAL C N     1 
ATOM   11608 C  CA    . VAL C 2 98  ? 123.534 87.727  128.244 1.00 24.01 ?  77  VAL C CA    1 
ATOM   11609 C  C     . VAL C 2 98  ? 125.070 87.832  128.123 1.00 25.23 ?  77  VAL C C     1 
ATOM   11610 O  O     . VAL C 2 98  ? 125.751 86.823  127.918 1.00 25.77 ?  77  VAL C O     1 
ATOM   11611 C  CB    . VAL C 2 98  ? 122.817 88.152  126.937 1.00 23.98 ?  77  VAL C CB    1 
ATOM   11612 C  CG1   . VAL C 2 98  ? 123.494 87.544  125.711 1.00 23.17 ?  77  VAL C CG1   1 
ATOM   11613 C  CG2   . VAL C 2 98  ? 121.341 87.739  126.995 1.00 22.55 ?  77  VAL C CG2   1 
ATOM   11614 N  N     . ALA C 2 99  ? 125.611 89.037  128.309 1.00 25.42 ?  78  ALA C N     1 
ATOM   11615 C  CA    . ALA C 2 99  ? 127.073 89.223  128.299 1.00 26.72 ?  78  ALA C CA    1 
ATOM   11616 C  C     . ALA C 2 99  ? 127.759 88.312  129.322 1.00 27.46 ?  78  ALA C C     1 
ATOM   11617 O  O     . ALA C 2 99  ? 128.786 87.703  129.024 1.00 28.07 ?  78  ALA C O     1 
ATOM   11618 C  CB    . ALA C 2 99  ? 127.441 90.673  128.551 1.00 26.52 ?  78  ALA C CB    1 
ATOM   11619 N  N     . GLU C 2 100 ? 127.162 88.194  130.507 1.00 28.33 ?  79  GLU C N     1 
ATOM   11620 C  CA    . GLU C 2 100 ? 127.726 87.377  131.585 1.00 29.60 ?  79  GLU C CA    1 
ATOM   11621 C  C     . GLU C 2 100 ? 127.861 85.903  131.194 1.00 29.64 ?  79  GLU C C     1 
ATOM   11622 O  O     . GLU C 2 100 ? 128.836 85.238  131.562 1.00 29.72 ?  79  GLU C O     1 
ATOM   11623 C  CB    . GLU C 2 100 ? 126.892 87.520  132.859 1.00 29.70 ?  79  GLU C CB    1 
ATOM   11624 C  CG    . GLU C 2 100 ? 127.455 86.762  134.061 1.00 33.58 ?  79  GLU C CG    1 
ATOM   11625 C  CD    . GLU C 2 100 ? 126.559 86.804  135.282 1.00 37.83 ?  79  GLU C CD    1 
ATOM   11626 O  OE1   . GLU C 2 100 ? 125.551 87.553  135.293 1.00 40.64 ?  79  GLU C OE1   1 
ATOM   11627 O  OE2   . GLU C 2 100 ? 126.863 86.068  136.246 1.00 41.40 -1 79  GLU C OE2   1 
ATOM   11628 N  N     . HIS C 2 101 ? 126.893 85.401  130.430 1.00 29.43 ?  80  HIS C N     1 
ATOM   11629 C  CA    . HIS C 2 101 ? 126.824 83.975  130.142 1.00 29.74 ?  80  HIS C CA    1 
ATOM   11630 C  C     . HIS C 2 101 ? 127.464 83.549  128.818 1.00 30.18 ?  80  HIS C C     1 
ATOM   11631 O  O     . HIS C 2 101 ? 127.733 82.372  128.615 1.00 30.30 ?  80  HIS C O     1 
ATOM   11632 C  CB    . HIS C 2 101 ? 125.378 83.472  130.284 1.00 29.21 ?  80  HIS C CB    1 
ATOM   11633 C  CG    . HIS C 2 101 ? 124.898 83.461  131.703 1.00 29.60 ?  80  HIS C CG    1 
ATOM   11634 N  ND1   . HIS C 2 101 ? 124.247 84.531  132.280 1.00 30.06 ?  80  HIS C ND1   1 
ATOM   11635 C  CD2   . HIS C 2 101 ? 125.016 82.525  132.674 1.00 29.49 ?  80  HIS C CD2   1 
ATOM   11636 C  CE1   . HIS C 2 101 ? 123.972 84.249  133.543 1.00 29.56 ?  80  HIS C CE1   1 
ATOM   11637 N  NE2   . HIS C 2 101 ? 124.427 83.038  133.806 1.00 30.20 ?  80  HIS C NE2   1 
ATOM   11638 N  N     . VAL C 2 102 ? 127.719 84.510  127.935 1.00 30.70 ?  81  VAL C N     1 
ATOM   11639 C  CA    . VAL C 2 102 ? 128.355 84.240  126.648 1.00 31.47 ?  81  VAL C CA    1 
ATOM   11640 C  C     . VAL C 2 102 ? 129.872 84.236  126.819 1.00 32.45 ?  81  VAL C C     1 
ATOM   11641 O  O     . VAL C 2 102 ? 130.431 85.162  127.419 1.00 32.50 ?  81  VAL C O     1 
ATOM   11642 C  CB    . VAL C 2 102 ? 127.942 85.274  125.568 1.00 31.18 ?  81  VAL C CB    1 
ATOM   11643 C  CG1   . VAL C 2 102 ? 128.771 85.105  124.293 1.00 31.20 ?  81  VAL C CG1   1 
ATOM   11644 C  CG2   . VAL C 2 102 ? 126.462 85.136  125.240 1.00 31.28 ?  81  VAL C CG2   1 
ATOM   11645 N  N     . ASP C 2 103 ? 130.524 83.202  126.282 1.00 33.38 ?  82  ASP C N     1 
ATOM   11646 C  CA    . ASP C 2 103 ? 131.977 83.040  126.391 1.00 34.82 ?  82  ASP C CA    1 
ATOM   11647 C  C     . ASP C 2 103 ? 132.748 83.776  125.302 1.00 34.74 ?  82  ASP C C     1 
ATOM   11648 O  O     . ASP C 2 103 ? 132.323 83.813  124.141 1.00 35.00 ?  82  ASP C O     1 
ATOM   11649 C  CB    . ASP C 2 103 ? 132.360 81.552  126.380 1.00 35.82 ?  82  ASP C CB    1 
ATOM   11650 C  CG    . ASP C 2 103 ? 132.010 80.842  127.685 1.00 38.29 ?  82  ASP C CG    1 
ATOM   11651 O  OD1   . ASP C 2 103 ? 132.054 81.481  128.764 1.00 41.49 ?  82  ASP C OD1   1 
ATOM   11652 O  OD2   . ASP C 2 103 ? 131.692 79.638  127.632 1.00 41.10 -1 82  ASP C OD2   1 
ATOM   11653 N  N     . GLY C 2 104 ? 133.885 84.352  125.689 1.00 34.89 ?  83  GLY C N     1 
ATOM   11654 C  CA    . GLY C 2 104 ? 134.789 85.028  124.752 1.00 35.11 ?  83  GLY C CA    1 
ATOM   11655 C  C     . GLY C 2 104 ? 134.824 86.532  124.948 1.00 34.96 ?  83  GLY C C     1 
ATOM   11656 O  O     . GLY C 2 104 ? 133.786 87.193  124.870 1.00 34.57 ?  83  GLY C O     1 
ATOM   11657 N  N     . HIS C 2 105 ? 136.022 87.070  125.186 1.00 35.02 ?  84  HIS C N     1 
ATOM   11658 C  CA    . HIS C 2 105 ? 136.199 88.494  125.506 1.00 34.83 ?  84  HIS C CA    1 
ATOM   11659 C  C     . HIS C 2 105 ? 135.679 89.445  124.436 1.00 33.77 ?  84  HIS C C     1 
ATOM   11660 O  O     . HIS C 2 105 ? 135.155 90.514  124.758 1.00 33.25 ?  84  HIS C O     1 
ATOM   11661 C  CB    . HIS C 2 105 ? 137.659 88.816  125.846 1.00 36.09 ?  84  HIS C CB    1 
ATOM   11662 C  CG    . HIS C 2 105 ? 138.074 88.347  127.207 1.00 39.17 ?  84  HIS C CG    1 
ATOM   11663 N  ND1   . HIS C 2 105 ? 139.352 87.909  127.488 1.00 43.00 ?  84  HIS C ND1   1 
ATOM   11664 C  CD2   . HIS C 2 105 ? 137.373 88.225  128.361 1.00 41.84 ?  84  HIS C CD2   1 
ATOM   11665 C  CE1   . HIS C 2 105 ? 139.422 87.549  128.759 1.00 43.47 ?  84  HIS C CE1   1 
ATOM   11666 N  NE2   . HIS C 2 105 ? 138.235 87.731  129.311 1.00 43.10 ?  84  HIS C NE2   1 
ATOM   11667 N  N     . GLN C 2 106 ? 135.805 89.056  123.173 1.00 32.84 ?  85  GLN C N     1 
ATOM   11668 C  CA    . GLN C 2 106 ? 135.304 89.894  122.087 1.00 32.29 ?  85  GLN C CA    1 
ATOM   11669 C  C     . GLN C 2 106 ? 133.773 89.879  122.002 1.00 30.88 ?  85  GLN C C     1 
ATOM   11670 O  O     . GLN C 2 106 ? 133.154 90.925  121.775 1.00 30.44 ?  85  GLN C O     1 
ATOM   11671 C  CB    . GLN C 2 106 ? 135.921 89.490  120.757 1.00 32.85 ?  85  GLN C CB    1 
ATOM   11672 C  CG    . GLN C 2 106 ? 137.423 89.734  120.684 1.00 35.55 ?  85  GLN C CG    1 
ATOM   11673 C  CD    . GLN C 2 106 ? 138.017 89.224  119.397 1.00 38.12 ?  85  GLN C CD    1 
ATOM   11674 O  OE1   . GLN C 2 106 ? 137.401 89.322  118.336 1.00 39.96 ?  85  GLN C OE1   1 
ATOM   11675 N  NE2   . GLN C 2 106 ? 139.227 88.675  119.480 1.00 40.39 ?  85  GLN C NE2   1 
ATOM   11676 N  N     . ARG C 2 107 ? 133.172 88.703  122.176 1.00 29.75 ?  86  ARG C N     1 
ATOM   11677 C  CA    . ARG C 2 107 ? 131.709 88.596  122.216 1.00 28.87 ?  86  ARG C CA    1 
ATOM   11678 C  C     . ARG C 2 107 ? 131.170 89.411  123.383 1.00 28.16 ?  86  ARG C C     1 
ATOM   11679 O  O     . ARG C 2 107 ? 130.176 90.120  123.238 1.00 27.55 ?  86  ARG C O     1 
ATOM   11680 C  CB    . ARG C 2 107 ? 131.257 87.141  122.335 1.00 28.48 ?  86  ARG C CB    1 
ATOM   11681 C  CG    . ARG C 2 107 ? 131.463 86.342  121.061 1.00 29.86 ?  86  ARG C CG    1 
ATOM   11682 C  CD    . ARG C 2 107 ? 131.040 84.890  121.218 1.00 30.23 ?  86  ARG C CD    1 
ATOM   11683 N  NE    . ARG C 2 107 ? 130.829 84.314  119.896 1.00 33.04 ?  86  ARG C NE    1 
ATOM   11684 C  CZ    . ARG C 2 107 ? 130.132 83.218  119.648 1.00 31.54 ?  86  ARG C CZ    1 
ATOM   11685 N  NH1   . ARG C 2 107 ? 129.575 82.537  120.640 1.00 31.85 1  86  ARG C NH1   1 
ATOM   11686 N  NH2   . ARG C 2 107 ? 130.004 82.804  118.399 1.00 34.74 ?  86  ARG C NH2   1 
ATOM   11687 N  N     . LYS C 2 108 ? 131.839 89.318  124.531 1.00 27.65 ?  87  LYS C N     1 
ATOM   11688 C  CA    . LYS C 2 108 ? 131.448 90.102  125.707 1.00 27.96 ?  87  LYS C CA    1 
ATOM   11689 C  C     . LYS C 2 108 ? 131.587 91.602  125.490 1.00 27.75 ?  87  LYS C C     1 
ATOM   11690 O  O     . LYS C 2 108 ? 130.756 92.371  125.972 1.00 28.29 ?  87  LYS C O     1 
ATOM   11691 C  CB    . LYS C 2 108 ? 132.232 89.686  126.952 1.00 27.80 ?  87  LYS C CB    1 
ATOM   11692 C  CG    . LYS C 2 108 ? 131.876 88.306  127.464 1.00 29.04 ?  87  LYS C CG    1 
ATOM   11693 C  CD    . LYS C 2 108 ? 132.681 87.994  128.717 1.00 31.15 ?  87  LYS C CD    1 
ATOM   11694 C  CE    . LYS C 2 108 ? 132.516 86.545  129.136 1.00 32.05 ?  87  LYS C CE    1 
ATOM   11695 N  NZ    . LYS C 2 108 ? 131.214 86.336  129.815 1.00 30.88 1  87  LYS C NZ    1 
ATOM   11696 N  N     . ALA C 2 109 ? 132.627 92.017  124.766 1.00 27.69 ?  88  ALA C N     1 
ATOM   11697 C  CA    . ALA C 2 109 ? 132.827 93.439  124.458 1.00 27.46 ?  88  ALA C CA    1 
ATOM   11698 C  C     . ALA C 2 109 ? 131.707 94.017  123.587 1.00 26.87 ?  88  ALA C C     1 
ATOM   11699 O  O     . ALA C 2 109 ? 131.280 95.152  123.795 1.00 26.47 ?  88  ALA C O     1 
ATOM   11700 C  CB    . ALA C 2 109 ? 134.172 93.659  123.796 1.00 27.98 ?  88  ALA C CB    1 
ATOM   11701 N  N     . VAL C 2 110 ? 131.252 93.240  122.607 1.00 25.98 ?  89  VAL C N     1 
ATOM   11702 C  CA    . VAL C 2 110 ? 130.136 93.643  121.748 1.00 25.46 ?  89  VAL C CA    1 
ATOM   11703 C  C     . VAL C 2 110 ? 128.855 93.762  122.581 1.00 24.57 ?  89  VAL C C     1 
ATOM   11704 O  O     . VAL C 2 110 ? 128.164 94.784  122.531 1.00 23.62 ?  89  VAL C O     1 
ATOM   11705 C  CB    . VAL C 2 110 ? 129.939 92.657  120.571 1.00 25.80 ?  89  VAL C CB    1 
ATOM   11706 C  CG1   . VAL C 2 110 ? 128.631 92.935  119.816 1.00 25.44 ?  89  VAL C CG1   1 
ATOM   11707 C  CG2   . VAL C 2 110 ? 131.133 92.722  119.619 1.00 26.23 ?  89  VAL C CG2   1 
ATOM   11708 N  N     . LEU C 2 111 ? 128.567 92.731  123.372 1.00 24.33 ?  90  LEU C N     1 
ATOM   11709 C  CA    . LEU C 2 111 ? 127.362 92.733  124.203 1.00 23.93 ?  90  LEU C CA    1 
ATOM   11710 C  C     . LEU C 2 111 ? 127.366 93.839  125.259 1.00 23.77 ?  90  LEU C C     1 
ATOM   11711 O  O     . LEU C 2 111 ? 126.324 94.441  125.521 1.00 23.04 ?  90  LEU C O     1 
ATOM   11712 C  CB    . LEU C 2 111 ? 127.116 91.361  124.837 1.00 23.73 ?  90  LEU C CB    1 
ATOM   11713 C  CG    . LEU C 2 111 ? 126.837 90.234  123.839 1.00 24.50 ?  90  LEU C CG    1 
ATOM   11714 C  CD1   . LEU C 2 111 ? 127.072 88.873  124.474 1.00 24.02 ?  90  LEU C CD1   1 
ATOM   11715 C  CD2   . LEU C 2 111 ? 125.424 90.331  123.258 1.00 25.38 ?  90  LEU C CD2   1 
ATOM   11716 N  N     . ASN C 2 112 ? 128.529 94.096  125.867 1.00 24.24 ?  91  ASN C N     1 
ATOM   11717 C  CA    . ASN C 2 112 ? 128.682 95.230  126.791 1.00 24.95 ?  91  ASN C CA    1 
ATOM   11718 C  C     . ASN C 2 112 ? 128.447 96.584  126.127 1.00 24.25 ?  91  ASN C C     1 
ATOM   11719 O  O     . ASN C 2 112 ? 127.834 97.469  126.723 1.00 23.99 ?  91  ASN C O     1 
ATOM   11720 C  CB    . ASN C 2 112 ? 130.066 95.235  127.447 1.00 25.81 ?  91  ASN C CB    1 
ATOM   11721 C  CG    . ASN C 2 112 ? 130.119 94.375  128.680 1.00 29.96 ?  91  ASN C CG    1 
ATOM   11722 O  OD1   . ASN C 2 112 ? 129.879 94.857  129.789 1.00 35.44 ?  91  ASN C OD1   1 
ATOM   11723 N  ND2   . ASN C 2 112 ? 130.431 93.091  128.506 1.00 32.37 ?  91  ASN C ND2   1 
ATOM   11724 N  N     . PHE C 2 113 ? 128.969 96.750  124.913 1.00 23.60 ?  92  PHE C N     1 
ATOM   11725 C  CA    . PHE C 2 113 ? 128.744 97.972  124.148 1.00 23.32 ?  92  PHE C CA    1 
ATOM   11726 C  C     . PHE C 2 113 ? 127.253 98.168  123.836 1.00 22.63 ?  92  PHE C C     1 
ATOM   11727 O  O     . PHE C 2 113 ? 126.726 99.270  123.996 1.00 21.94 ?  92  PHE C O     1 
ATOM   11728 C  CB    . PHE C 2 113 ? 129.531 97.962  122.830 1.00 23.27 ?  92  PHE C CB    1 
ATOM   11729 C  CG    . PHE C 2 113 ? 129.532 99.292  122.127 1.00 24.66 ?  92  PHE C CG    1 
ATOM   11730 C  CD1   . PHE C 2 113 ? 130.523 100.244 122.409 1.00 25.72 ?  92  PHE C CD1   1 
ATOM   11731 C  CD2   . PHE C 2 113 ? 128.536 99.610  121.207 1.00 25.36 ?  92  PHE C CD2   1 
ATOM   11732 C  CE1   . PHE C 2 113 ? 130.518 101.487 121.775 1.00 25.92 ?  92  PHE C CE1   1 
ATOM   11733 C  CE2   . PHE C 2 113 ? 128.521 100.855 120.566 1.00 25.82 ?  92  PHE C CE2   1 
ATOM   11734 C  CZ    . PHE C 2 113 ? 129.511 101.796 120.855 1.00 25.80 ?  92  PHE C CZ    1 
ATOM   11735 N  N     . MET C 2 114 ? 126.599 97.101  123.371 1.00 22.03 ?  93  MET C N     1 
ATOM   11736 C  CA    . MET C 2 114 ? 125.154 97.129  123.103 1.00 22.14 ?  93  MET C CA    1 
ATOM   11737 C  C     . MET C 2 114 ? 124.339 97.490  124.357 1.00 21.64 ?  93  MET C C     1 
ATOM   11738 O  O     . MET C 2 114 ? 123.409 98.300  124.279 1.00 21.59 ?  93  MET C O     1 
ATOM   11739 C  CB    . MET C 2 114 ? 124.689 95.797  122.525 1.00 22.46 ?  93  MET C CB    1 
ATOM   11740 C  CG    . MET C 2 114 ? 125.213 95.521  121.125 1.00 23.80 ?  93  MET C CG    1 
ATOM   11741 S  SD    . MET C 2 114 ? 124.799 93.858  120.555 1.00 28.07 ?  93  MET C SD    1 
ATOM   11742 C  CE    . MET C 2 114 ? 125.246 94.022  118.806 1.00 26.42 ?  93  MET C CE    1 
ATOM   11743 N  N     . ALA C 2 115 ? 124.712 96.917  125.507 1.00 20.98 ?  94  ALA C N     1 
ATOM   11744 C  CA    . ALA C 2 115 ? 124.093 97.258  126.801 1.00 20.58 ?  94  ALA C CA    1 
ATOM   11745 C  C     . ALA C 2 115 ? 124.202 98.743  127.142 1.00 21.01 ?  94  ALA C C     1 
ATOM   11746 O  O     . ALA C 2 115 ? 123.236 99.366  127.619 1.00 21.06 ?  94  ALA C O     1 
ATOM   11747 C  CB    . ALA C 2 115 ? 124.711 96.401  127.932 1.00 20.83 ?  94  ALA C CB    1 
ATOM   11748 N  N     . MET C 2 116 ? 125.392 99.304  126.934 1.00 20.36 ?  95  MET C N     1 
ATOM   11749 C  CA    . MET C 2 116 ? 125.618 100.718 127.173 1.00 20.83 ?  95  MET C CA    1 
ATOM   11750 C  C     . MET C 2 116 ? 124.698 101.567 126.280 1.00 20.55 ?  95  MET C C     1 
ATOM   11751 O  O     . MET C 2 116 ? 124.069 102.513 126.750 1.00 20.70 ?  95  MET C O     1 
ATOM   11752 C  CB    . MET C 2 116 ? 127.098 101.056 126.948 1.00 20.64 ?  95  MET C CB    1 
ATOM   11753 C  CG    . MET C 2 116 ? 127.451 102.540 127.045 1.00 21.42 ?  95  MET C CG    1 
ATOM   11754 S  SD    . MET C 2 116 ? 127.051 103.440 125.533 1.00 22.51 ?  95  MET C SD    1 
ATOM   11755 C  CE    . MET C 2 116 ? 128.075 102.594 124.327 1.00 20.66 ?  95  MET C CE    1 
ATOM   11756 N  N     . MET C 2 117 ? 124.610 101.206 125.004 1.00 20.50 ?  96  MET C N     1 
ATOM   11757 C  CA    . MET C 2 117 ? 123.750 101.924 124.073 1.00 21.22 ?  96  MET C CA    1 
ATOM   11758 C  C     . MET C 2 117 ? 122.300 101.941 124.554 1.00 21.11 ?  96  MET C C     1 
ATOM   11759 O  O     . MET C 2 117 ? 121.651 102.989 124.510 1.00 20.71 ?  96  MET C O     1 
ATOM   11760 C  CB    . MET C 2 117 ? 123.857 101.346 122.656 1.00 21.35 ?  96  MET C CB    1 
ATOM   11761 C  CG    . MET C 2 117 ? 125.195 101.657 121.913 1.00 22.54 ?  96  MET C CG    1 
ATOM   11762 S  SD    . MET C 2 117 ? 125.647 103.403 121.799 1.00 24.89 ?  96  MET C SD    1 
ATOM   11763 C  CE    . MET C 2 117 ? 124.514 103.976 120.533 1.00 24.95 ?  96  MET C CE    1 
ATOM   11764 N  N     . GLU C 2 118 ? 121.814 100.794 125.029 1.00 21.18 ?  97  GLU C N     1 
ATOM   11765 C  CA    . GLU C 2 118 ? 120.434 100.664 125.509 1.00 21.99 ?  97  GLU C CA    1 
ATOM   11766 C  C     . GLU C 2 118 ? 120.081 101.697 126.581 1.00 22.10 ?  97  GLU C C     1 
ATOM   11767 O  O     . GLU C 2 118 ? 119.114 102.447 126.428 1.00 22.22 ?  97  GLU C O     1 
ATOM   11768 C  CB    . GLU C 2 118 ? 120.137 99.251  126.038 1.00 22.01 ?  97  GLU C CB    1 
ATOM   11769 C  CG    . GLU C 2 118 ? 120.446 98.073  125.106 1.00 24.38 ?  97  GLU C CG    1 
ATOM   11770 C  CD    . GLU C 2 118 ? 119.684 98.076  123.774 1.00 26.32 ?  97  GLU C CD    1 
ATOM   11771 O  OE1   . GLU C 2 118 ? 119.374 99.146  123.233 1.00 29.86 ?  97  GLU C OE1   1 
ATOM   11772 O  OE2   . GLU C 2 118 ? 119.438 96.984  123.234 1.00 29.19 -1 97  GLU C OE2   1 
ATOM   11773 N  N     . ASN C 2 119 ? 120.855 101.740 127.663 1.00 22.26 ?  98  ASN C N     1 
ATOM   11774 C  CA    . ASN C 2 119 ? 120.483 102.609 128.781 1.00 21.91 ?  98  ASN C CA    1 
ATOM   11775 C  C     . ASN C 2 119 ? 121.186 103.971 128.866 1.00 22.41 ?  98  ASN C C     1 
ATOM   11776 O  O     . ASN C 2 119 ? 120.612 104.928 129.384 1.00 23.07 ?  98  ASN C O     1 
ATOM   11777 C  CB    . ASN C 2 119 ? 120.429 101.854 130.127 1.00 21.93 ?  98  ASN C CB    1 
ATOM   11778 C  CG    . ASN C 2 119 ? 121.768 101.297 130.560 1.00 21.31 ?  98  ASN C CG    1 
ATOM   11779 O  OD1   . ASN C 2 119 ? 122.775 101.422 129.860 1.00 21.88 ?  98  ASN C OD1   1 
ATOM   11780 N  ND2   . ASN C 2 119 ? 121.788 100.681 131.740 1.00 21.73 ?  98  ASN C ND2   1 
ATOM   11781 N  N     . ALA C 2 120 ? 122.419 104.054 128.374 1.00 22.75 ?  99  ALA C N     1 
ATOM   11782 C  CA    . ALA C 2 120 ? 123.166 105.312 128.385 1.00 23.12 ?  99  ALA C CA    1 
ATOM   11783 C  C     . ALA C 2 120 ? 122.877 106.181 127.178 1.00 23.60 ?  99  ALA C C     1 
ATOM   11784 O  O     . ALA C 2 120 ? 123.060 107.401 127.248 1.00 24.14 ?  99  ALA C O     1 
ATOM   11785 C  CB    . ALA C 2 120 ? 124.683 105.067 128.527 1.00 23.28 ?  99  ALA C CB    1 
ATOM   11786 N  N     . VAL C 2 121 ? 122.422 105.573 126.077 1.00 23.23 ?  100 VAL C N     1 
ATOM   11787 C  CA    . VAL C 2 121 ? 122.124 106.352 124.860 1.00 23.74 ?  100 VAL C CA    1 
ATOM   11788 C  C     . VAL C 2 121 ? 120.645 106.346 124.472 1.00 23.62 ?  100 VAL C C     1 
ATOM   11789 O  O     . VAL C 2 121 ? 120.034 107.407 124.391 1.00 24.51 ?  100 VAL C O     1 
ATOM   11790 C  CB    . VAL C 2 121 ? 123.000 105.932 123.660 1.00 23.19 ?  100 VAL C CB    1 
ATOM   11791 C  CG1   . VAL C 2 121 ? 122.623 106.733 122.400 1.00 24.10 ?  100 VAL C CG1   1 
ATOM   11792 C  CG2   . VAL C 2 121 ? 124.487 106.126 123.996 1.00 23.48 ?  100 VAL C CG2   1 
ATOM   11793 N  N     . HIS C 2 122 ? 120.081 105.161 124.246 1.00 23.45 ?  101 HIS C N     1 
ATOM   11794 C  CA    . HIS C 2 122 ? 118.703 105.044 123.763 1.00 23.81 ?  101 HIS C CA    1 
ATOM   11795 C  C     . HIS C 2 122 ? 117.672 105.514 124.767 1.00 24.33 ?  101 HIS C C     1 
ATOM   11796 O  O     . HIS C 2 122 ? 116.871 106.400 124.452 1.00 24.80 ?  101 HIS C O     1 
ATOM   11797 C  CB    . HIS C 2 122 ? 118.367 103.616 123.344 1.00 23.30 ?  101 HIS C CB    1 
ATOM   11798 C  CG    . HIS C 2 122 ? 119.193 103.104 122.208 1.00 22.96 ?  101 HIS C CG    1 
ATOM   11799 N  ND1   . HIS C 2 122 ? 119.125 101.796 121.773 1.00 22.78 ?  101 HIS C ND1   1 
ATOM   11800 C  CD2   . HIS C 2 122 ? 120.128 103.711 121.441 1.00 23.25 ?  101 HIS C CD2   1 
ATOM   11801 C  CE1   . HIS C 2 122 ? 119.973 101.627 120.776 1.00 22.57 ?  101 HIS C CE1   1 
ATOM   11802 N  NE2   . HIS C 2 122 ? 120.593 102.772 120.554 1.00 21.75 ?  101 HIS C NE2   1 
ATOM   11803 N  N     . ALA C 2 123 ? 117.668 104.903 125.955 1.00 24.40 ?  102 ALA C N     1 
ATOM   11804 C  CA    . ALA C 2 123 ? 116.683 105.249 126.982 1.00 24.00 ?  102 ALA C CA    1 
ATOM   11805 C  C     . ALA C 2 123 ? 116.758 106.740 127.317 1.00 24.05 ?  102 ALA C C     1 
ATOM   11806 O  O     . ALA C 2 123 ? 115.729 107.388 127.491 1.00 23.89 ?  102 ALA C O     1 
ATOM   11807 C  CB    . ALA C 2 123 ? 116.868 104.392 128.233 1.00 23.73 ?  102 ALA C CB    1 
ATOM   11808 N  N     . LYS C 2 124 ? 117.975 107.280 127.384 1.00 24.36 ?  103 LYS C N     1 
ATOM   11809 C  CA    . LYS C 2 124 ? 118.182 108.699 127.693 1.00 24.31 ?  103 LYS C CA    1 
ATOM   11810 C  C     . LYS C 2 124 ? 117.684 109.659 126.606 1.00 23.84 ?  103 LYS C C     1 
ATOM   11811 O  O     . LYS C 2 124 ? 117.125 110.716 126.924 1.00 24.21 ?  103 LYS C O     1 
ATOM   11812 C  CB    . LYS C 2 124 ? 119.640 108.994 128.058 1.00 24.93 ?  103 LYS C CB    1 
ATOM   11813 C  CG    . LYS C 2 124 ? 119.848 110.415 128.602 1.00 26.37 ?  103 LYS C CG    1 
ATOM   11814 C  CD    . LYS C 2 124 ? 121.257 110.630 129.128 1.00 29.42 ?  103 LYS C CD    1 
ATOM   11815 C  CE    . LYS C 2 124 ? 121.480 112.099 129.500 1.00 31.51 ?  103 LYS C CE    1 
ATOM   11816 N  NZ    . LYS C 2 124 ? 121.414 113.001 128.311 1.00 32.37 1  103 LYS C NZ    1 
ATOM   11817 N  N     . SER C 2 125 ? 117.871 109.289 125.337 1.00 23.52 ?  104 SER C N     1 
ATOM   11818 C  CA    . SER C 2 125 ? 117.400 110.092 124.204 0.50 23.23 ?  104 SER C CA    1 
ATOM   11819 C  C     . SER C 2 125 ? 115.908 110.410 124.302 1.00 22.91 ?  104 SER C C     1 
ATOM   11820 O  O     . SER C 2 125 ? 115.468 111.484 123.914 1.00 22.33 ?  104 SER C O     1 
ATOM   11821 C  CB    . SER C 2 125 ? 117.676 109.377 122.876 0.50 23.25 ?  104 SER C CB    1 
ATOM   11822 O  OG    . SER C 2 125 ? 119.059 109.138 122.692 0.50 24.57 ?  104 SER C OG    1 
ATOM   11823 N  N     . TYR C 2 126 ? 115.121 109.462 124.807 1.00 22.72 ?  105 TYR C N     1 
ATOM   11824 C  CA    . TYR C 2 126 ? 113.683 109.698 124.934 1.00 23.34 ?  105 TYR C CA    1 
ATOM   11825 C  C     . TYR C 2 126 ? 113.387 110.817 125.905 1.00 23.32 ?  105 TYR C C     1 
ATOM   11826 O  O     . TYR C 2 126 ? 112.455 111.576 125.681 1.00 23.17 ?  105 TYR C O     1 
ATOM   11827 C  CB    . TYR C 2 126 ? 112.908 108.444 125.345 1.00 23.45 ?  105 TYR C CB    1 
ATOM   11828 C  CG    . TYR C 2 126 ? 113.099 107.267 124.418 1.00 25.16 ?  105 TYR C CG    1 
ATOM   11829 C  CD1   . TYR C 2 126 ? 112.719 107.333 123.080 1.00 26.75 ?  105 TYR C CD1   1 
ATOM   11830 C  CD2   . TYR C 2 126 ? 113.665 106.082 124.888 1.00 26.36 ?  105 TYR C CD2   1 
ATOM   11831 C  CE1   . TYR C 2 126 ? 112.914 106.242 122.225 1.00 28.22 ?  105 TYR C CE1   1 
ATOM   11832 C  CE2   . TYR C 2 126 ? 113.863 104.997 124.050 1.00 27.17 ?  105 TYR C CE2   1 
ATOM   11833 C  CZ    . TYR C 2 126 ? 113.474 105.077 122.726 1.00 29.26 ?  105 TYR C CZ    1 
ATOM   11834 O  OH    . TYR C 2 126 ? 113.659 103.988 121.896 1.00 30.76 ?  105 TYR C OH    1 
ATOM   11835 N  N     . SER C 2 127 ? 114.182 110.910 126.974 1.00 23.61 ?  106 SER C N     1 
ATOM   11836 C  CA    . SER C 2 127 ? 114.051 112.003 127.930 1.00 24.40 ?  106 SER C CA    1 
ATOM   11837 C  C     . SER C 2 127 ? 114.436 113.336 127.305 1.00 24.55 ?  106 SER C C     1 
ATOM   11838 O  O     . SER C 2 127 ? 113.860 114.355 127.655 1.00 24.74 ?  106 SER C O     1 
ATOM   11839 C  CB    . SER C 2 127 ? 114.865 111.754 129.200 1.00 24.54 ?  106 SER C CB    1 
ATOM   11840 O  OG    . SER C 2 127 ? 114.207 110.820 130.049 1.00 24.69 ?  106 SER C OG    1 
ATOM   11841 N  N     . ASN C 2 128 ? 115.411 113.328 126.396 1.00 25.28 ?  107 ASN C N     1 
ATOM   11842 C  CA    . ASN C 2 128 ? 115.774 114.543 125.659 1.00 25.88 ?  107 ASN C CA    1 
ATOM   11843 C  C     . ASN C 2 128 ? 114.587 115.014 124.829 1.00 25.48 ?  107 ASN C C     1 
ATOM   11844 O  O     . ASN C 2 128 ? 114.263 116.200 124.808 1.00 25.23 ?  107 ASN C O     1 
ATOM   11845 C  CB    . ASN C 2 128 ? 116.992 114.318 124.755 1.00 26.40 ?  107 ASN C CB    1 
ATOM   11846 C  CG    . ASN C 2 128 ? 118.310 114.299 125.520 1.00 27.90 ?  107 ASN C CG    1 
ATOM   11847 O  OD1   . ASN C 2 128 ? 118.369 113.891 126.681 1.00 30.62 ?  107 ASN C OD1   1 
ATOM   11848 N  ND2   . ASN C 2 128 ? 119.378 114.729 124.856 1.00 27.91 ?  107 ASN C ND2   1 
ATOM   11849 N  N     . ILE C 2 129 ? 113.937 114.072 124.155 1.00 25.44 ?  108 ILE C N     1 
ATOM   11850 C  CA    . ILE C 2 129 ? 112.734 114.392 123.385 1.00 25.48 ?  108 ILE C CA    1 
ATOM   11851 C  C     . ILE C 2 129 ? 111.624 114.917 124.310 1.00 25.93 ?  108 ILE C C     1 
ATOM   11852 O  O     . ILE C 2 129 ? 111.073 115.993 124.055 1.00 25.54 ?  108 ILE C O     1 
ATOM   11853 C  CB    . ILE C 2 129 ? 112.268 113.212 122.494 1.00 25.21 ?  108 ILE C CB    1 
ATOM   11854 C  CG1   . ILE C 2 129 ? 113.362 112.871 121.468 1.00 25.96 ?  108 ILE C CG1   1 
ATOM   11855 C  CG2   . ILE C 2 129 ? 110.934 113.550 121.793 1.00 24.43 ?  108 ILE C CG2   1 
ATOM   11856 C  CD1   . ILE C 2 129 ? 113.163 111.559 120.711 1.00 26.11 ?  108 ILE C CD1   1 
ATOM   11857 N  N     . PHE C 2 130 ? 111.317 114.181 125.383 1.00 26.04 ?  109 PHE C N     1 
ATOM   11858 C  CA    . PHE C 2 130 ? 110.285 114.605 126.347 1.00 26.66 ?  109 PHE C CA    1 
ATOM   11859 C  C     . PHE C 2 130 ? 110.550 116.004 126.912 1.00 27.38 ?  109 PHE C C     1 
ATOM   11860 O  O     . PHE C 2 130 ? 109.632 116.835 126.999 1.00 27.22 ?  109 PHE C O     1 
ATOM   11861 C  CB    . PHE C 2 130 ? 110.174 113.617 127.530 1.00 26.98 ?  109 PHE C CB    1 
ATOM   11862 C  CG    . PHE C 2 130 ? 109.566 112.281 127.182 1.00 27.46 ?  109 PHE C CG    1 
ATOM   11863 C  CD1   . PHE C 2 130 ? 108.642 112.152 126.151 1.00 28.57 ?  109 PHE C CD1   1 
ATOM   11864 C  CD2   . PHE C 2 130 ? 109.911 111.145 127.914 1.00 28.51 ?  109 PHE C CD2   1 
ATOM   11865 C  CE1   . PHE C 2 130 ? 108.086 110.912 125.841 1.00 29.17 ?  109 PHE C CE1   1 
ATOM   11866 C  CE2   . PHE C 2 130 ? 109.353 109.894 127.616 1.00 29.27 ?  109 PHE C CE2   1 
ATOM   11867 C  CZ    . PHE C 2 130 ? 108.437 109.775 126.583 1.00 28.83 ?  109 PHE C CZ    1 
ATOM   11868 N  N     . MET C 2 131 ? 111.800 116.267 127.295 1.00 27.52 ?  110 MET C N     1 
ATOM   11869 C  CA    . MET C 2 131 ? 112.148 117.536 127.945 1.00 29.07 ?  110 MET C CA    1 
ATOM   11870 C  C     . MET C 2 131 ? 112.035 118.735 127.018 1.00 29.58 ?  110 MET C C     1 
ATOM   11871 O  O     . MET C 2 131 ? 111.810 119.855 127.475 1.00 30.07 ?  110 MET C O     1 
ATOM   11872 C  CB    . MET C 2 131 ? 113.539 117.485 128.571 1.00 28.96 ?  110 MET C CB    1 
ATOM   11873 C  CG    . MET C 2 131 ? 113.562 116.780 129.911 1.00 31.09 ?  110 MET C CG    1 
ATOM   11874 S  SD    . MET C 2 131 ? 115.209 116.662 130.648 1.00 35.43 ?  110 MET C SD    1 
ATOM   11875 C  CE    . MET C 2 131 ? 116.059 115.576 129.507 1.00 33.13 ?  110 MET C CE    1 
ATOM   11876 N  N     . THR C 2 132 ? 112.187 118.486 125.723 1.00 30.25 ?  111 THR C N     1 
ATOM   11877 C  CA    . THR C 2 132 ? 112.017 119.514 124.700 1.00 30.97 ?  111 THR C CA    1 
ATOM   11878 C  C     . THR C 2 132 ? 110.537 119.820 124.448 1.00 31.36 ?  111 THR C C     1 
ATOM   11879 O  O     . THR C 2 132 ? 110.111 120.982 124.499 1.00 31.60 ?  111 THR C O     1 
ATOM   11880 C  CB    . THR C 2 132 ? 112.715 119.081 123.380 1.00 30.88 ?  111 THR C CB    1 
ATOM   11881 O  OG1   . THR C 2 132 ? 114.120 118.940 123.619 1.00 29.86 ?  111 THR C OG1   1 
ATOM   11882 C  CG2   . THR C 2 132 ? 112.502 120.107 122.256 1.00 31.44 ?  111 THR C CG2   1 
ATOM   11883 N  N     . LEU C 2 133 ? 109.759 118.773 124.190 1.00 31.34 ?  112 LEU C N     1 
ATOM   11884 C  CA    . LEU C 2 133 ? 108.380 118.927 123.722 1.00 31.68 ?  112 LEU C CA    1 
ATOM   11885 C  C     . LEU C 2 133 ? 107.316 119.124 124.806 1.00 31.96 ?  112 LEU C C     1 
ATOM   11886 O  O     . LEU C 2 133 ? 106.310 119.792 124.573 1.00 31.69 ?  112 LEU C O     1 
ATOM   11887 C  CB    . LEU C 2 133 ? 107.992 117.738 122.849 1.00 31.35 ?  112 LEU C CB    1 
ATOM   11888 C  CG    . LEU C 2 133 ? 108.917 117.394 121.676 1.00 32.14 ?  112 LEU C CG    1 
ATOM   11889 C  CD1   . LEU C 2 133 ? 108.402 116.154 120.985 1.00 32.15 ?  112 LEU C CD1   1 
ATOM   11890 C  CD2   . LEU C 2 133 ? 109.034 118.561 120.698 1.00 32.39 ?  112 LEU C CD2   1 
ATOM   11891 N  N     . ALA C 2 134 ? 107.535 118.542 125.981 1.00 32.12 ?  113 ALA C N     1 
ATOM   11892 C  CA    . ALA C 2 134 ? 106.480 118.446 126.980 1.00 32.53 ?  113 ALA C CA    1 
ATOM   11893 C  C     . ALA C 2 134 ? 106.814 119.145 128.292 1.00 33.15 ?  113 ALA C C     1 
ATOM   11894 O  O     . ALA C 2 134 ? 107.974 119.178 128.697 1.00 32.47 ?  113 ALA C O     1 
ATOM   11895 C  CB    . ALA C 2 134 ? 106.126 116.976 127.234 1.00 32.20 ?  113 ALA C CB    1 
ATOM   11896 N  N     . PRO C 2 135 ? 105.785 119.692 128.968 1.00 34.27 ?  114 PRO C N     1 
ATOM   11897 C  CA    . PRO C 2 135 ? 105.975 120.239 130.306 1.00 35.35 ?  114 PRO C CA    1 
ATOM   11898 C  C     . PRO C 2 135 ? 106.155 119.115 131.321 1.00 36.17 ?  114 PRO C C     1 
ATOM   11899 O  O     . PRO C 2 135 ? 105.707 117.990 131.086 1.00 35.92 ?  114 PRO C O     1 
ATOM   11900 C  CB    . PRO C 2 135 ? 104.682 121.022 130.563 1.00 35.48 ?  114 PRO C CB    1 
ATOM   11901 C  CG    . PRO C 2 135 ? 103.668 120.418 129.672 1.00 34.94 ?  114 PRO C CG    1 
ATOM   11902 C  CD    . PRO C 2 135 ? 104.388 119.810 128.505 1.00 34.50 ?  114 PRO C CD    1 
ATOM   11903 N  N     . THR C 2 136 ? 106.818 119.425 132.430 1.00 37.30 ?  115 THR C N     1 
ATOM   11904 C  CA    . THR C 2 136 ? 107.171 118.435 133.454 1.00 38.49 ?  115 THR C CA    1 
ATOM   11905 C  C     . THR C 2 136 ? 106.011 117.547 133.927 1.00 38.48 ?  115 THR C C     1 
ATOM   11906 O  O     . THR C 2 136 ? 106.210 116.350 134.162 1.00 38.74 ?  115 THR C O     1 
ATOM   11907 C  CB    . THR C 2 136 ? 107.826 119.121 134.671 1.00 38.95 ?  115 THR C CB    1 
ATOM   11908 O  OG1   . THR C 2 136 ? 108.901 119.946 134.216 1.00 40.08 ?  115 THR C OG1   1 
ATOM   11909 C  CG2   . THR C 2 136 ? 108.368 118.094 135.667 1.00 39.82 ?  115 THR C CG2   1 
ATOM   11910 N  N     . GLU C 2 137 ? 104.818 118.129 134.058 1.00 38.89 ?  116 GLU C N     1 
ATOM   11911 C  CA    . GLU C 2 137 ? 103.644 117.401 134.561 1.00 38.65 ?  116 GLU C CA    1 
ATOM   11912 C  C     . GLU C 2 137 ? 103.198 116.307 133.597 1.00 37.38 ?  116 GLU C C     1 
ATOM   11913 O  O     . GLU C 2 137 ? 102.796 115.225 134.022 1.00 37.22 ?  116 GLU C O     1 
ATOM   11914 C  CB    . GLU C 2 137 ? 102.471 118.345 134.905 1.00 39.52 ?  116 GLU C CB    1 
ATOM   11915 C  CG    . GLU C 2 137 ? 101.755 119.019 133.712 1.00 41.90 ?  116 GLU C CG    1 
ATOM   11916 C  CD    . GLU C 2 137 ? 101.805 120.556 133.737 1.00 46.43 ?  116 GLU C CD    1 
ATOM   11917 O  OE1   . GLU C 2 137 ? 102.575 121.138 134.538 1.00 47.84 ?  116 GLU C OE1   1 
ATOM   11918 O  OE2   . GLU C 2 137 ? 101.064 121.186 132.943 1.00 47.52 -1 116 GLU C OE2   1 
ATOM   11919 N  N     . THR C 2 138 ? 103.285 116.599 132.302 1.00 36.05 ?  117 THR C N     1 
ATOM   11920 C  CA    . THR C 2 138 ? 102.950 115.635 131.265 1.00 34.88 ?  117 THR C CA    1 
ATOM   11921 C  C     . THR C 2 138 ? 103.993 114.523 131.237 1.00 33.58 ?  117 THR C C     1 
ATOM   11922 O  O     . THR C 2 138 ? 103.650 113.355 131.034 1.00 33.61 ?  117 THR C O     1 
ATOM   11923 C  CB    . THR C 2 138 ? 102.843 116.309 129.891 1.00 34.85 ?  117 THR C CB    1 
ATOM   11924 O  OG1   . THR C 2 138 ? 101.961 117.433 129.990 1.00 35.98 ?  117 THR C OG1   1 
ATOM   11925 C  CG2   . THR C 2 138 ? 102.303 115.340 128.849 1.00 34.92 ?  117 THR C CG2   1 
ATOM   11926 N  N     . ILE C 2 139 ? 105.256 114.892 131.446 1.00 32.29 ?  118 ILE C N     1 
ATOM   11927 C  CA    . ILE C 2 139 ? 106.338 113.915 131.555 1.00 31.19 ?  118 ILE C CA    1 
ATOM   11928 C  C     . ILE C 2 139 ? 106.124 113.003 132.777 1.00 30.85 ?  118 ILE C C     1 
ATOM   11929 O  O     . ILE C 2 139 ? 106.185 111.780 132.652 1.00 29.77 ?  118 ILE C O     1 
ATOM   11930 C  CB    . ILE C 2 139 ? 107.748 114.578 131.583 1.00 31.25 ?  118 ILE C CB    1 
ATOM   11931 C  CG1   . ILE C 2 139 ? 107.990 115.425 130.322 1.00 30.12 ?  118 ILE C CG1   1 
ATOM   11932 C  CG2   . ILE C 2 139 ? 108.852 113.518 131.725 1.00 30.21 ?  118 ILE C CG2   1 
ATOM   11933 C  CD1   . ILE C 2 139 ? 109.304 116.229 130.352 1.00 29.41 ?  118 ILE C CD1   1 
ATOM   11934 N  N     . ASN C 2 140 ? 105.855 113.602 133.943 1.00 31.17 ?  119 ASN C N     1 
ATOM   11935 C  CA    . ASN C 2 140 ? 105.568 112.839 135.169 1.00 31.76 ?  119 ASN C CA    1 
ATOM   11936 C  C     . ASN C 2 140 ? 104.399 111.865 134.981 1.00 31.25 ?  119 ASN C C     1 
ATOM   11937 O  O     . ASN C 2 140 ? 104.488 110.701 135.374 1.00 31.47 ?  119 ASN C O     1 
ATOM   11938 C  CB    . ASN C 2 140 ? 105.265 113.764 136.357 1.00 32.65 ?  119 ASN C CB    1 
ATOM   11939 C  CG    . ASN C 2 140 ? 106.493 114.505 136.876 1.00 35.14 ?  119 ASN C CG    1 
ATOM   11940 O  OD1   . ASN C 2 140 ? 107.633 114.046 136.743 1.00 36.75 ?  119 ASN C OD1   1 
ATOM   11941 N  ND2   . ASN C 2 140 ? 106.252 115.660 137.503 1.00 38.05 ?  119 ASN C ND2   1 
ATOM   11942 N  N     . GLU C 2 141 ? 103.321 112.355 134.371 1.00 30.96 ?  120 GLU C N     1 
ATOM   11943 C  CA    . GLU C 2 141 ? 102.122 111.562 134.109 1.00 30.36 ?  120 GLU C CA    1 
ATOM   11944 C  C     . GLU C 2 141 ? 102.394 110.363 133.197 1.00 28.60 ?  120 GLU C C     1 
ATOM   11945 O  O     . GLU C 2 141 ? 101.894 109.271 133.453 1.00 27.94 ?  120 GLU C O     1 
ATOM   11946 C  CB    . GLU C 2 141 ? 101.018 112.433 133.501 1.00 30.86 ?  120 GLU C CB    1 
ATOM   11947 C  CG    . GLU C 2 141 ? 100.292 113.328 134.499 1.00 34.89 ?  120 GLU C CG    1 
ATOM   11948 C  CD    . GLU C 2 141 ? 99.348  114.313 133.823 1.00 39.82 ?  120 GLU C CD    1 
ATOM   11949 O  OE1   . GLU C 2 141 ? 99.041  114.135 132.618 1.00 41.95 ?  120 GLU C OE1   1 
ATOM   11950 O  OE2   . GLU C 2 141 ? 98.905  115.266 134.496 1.00 41.94 -1 120 GLU C OE2   1 
ATOM   11951 N  N     . VAL C 2 142 ? 103.178 110.557 132.139 1.00 27.29 ?  121 VAL C N     1 
ATOM   11952 C  CA    . VAL C 2 142 ? 103.446 109.431 131.219 1.00 25.89 ?  121 VAL C CA    1 
ATOM   11953 C  C     . VAL C 2 142 ? 104.307 108.338 131.862 1.00 25.11 ?  121 VAL C C     1 
ATOM   11954 O  O     . VAL C 2 142 ? 104.125 107.154 131.581 1.00 24.23 ?  121 VAL C O     1 
ATOM   11955 C  CB    . VAL C 2 142 ? 103.976 109.878 129.813 1.00 25.99 ?  121 VAL C CB    1 
ATOM   11956 C  CG1   . VAL C 2 142 ? 105.494 110.077 129.795 1.00 25.21 ?  121 VAL C CG1   1 
ATOM   11957 C  CG2   . VAL C 2 142 ? 103.580 108.863 128.753 1.00 25.78 ?  121 VAL C CG2   1 
ATOM   11958 N  N     . PHE C 2 143 ? 105.233 108.722 132.736 1.00 24.69 ?  122 PHE C N     1 
ATOM   11959 C  CA    . PHE C 2 143 ? 106.027 107.716 133.458 1.00 24.77 ?  122 PHE C CA    1 
ATOM   11960 C  C     . PHE C 2 143 ? 105.183 106.977 134.511 1.00 24.99 ?  122 PHE C C     1 
ATOM   11961 O  O     . PHE C 2 143 ? 105.378 105.785 134.753 1.00 24.73 ?  122 PHE C O     1 
ATOM   11962 C  CB    . PHE C 2 143 ? 107.313 108.317 134.037 1.00 24.83 ?  122 PHE C CB    1 
ATOM   11963 C  CG    . PHE C 2 143 ? 108.402 108.501 133.002 1.00 25.12 ?  122 PHE C CG    1 
ATOM   11964 C  CD1   . PHE C 2 143 ? 109.093 107.403 132.494 1.00 26.58 ?  122 PHE C CD1   1 
ATOM   11965 C  CD2   . PHE C 2 143 ? 108.718 109.763 132.521 1.00 24.49 ?  122 PHE C CD2   1 
ATOM   11966 C  CE1   . PHE C 2 143 ? 110.090 107.569 131.524 1.00 26.96 ?  122 PHE C CE1   1 
ATOM   11967 C  CE2   . PHE C 2 143 ? 109.705 109.939 131.563 1.00 25.79 ?  122 PHE C CE2   1 
ATOM   11968 C  CZ    . PHE C 2 143 ? 110.395 108.841 131.057 1.00 26.45 ?  122 PHE C CZ    1 
ATOM   11969 N  N     . GLU C 2 144 ? 104.230 107.683 135.116 1.00 25.22 ?  123 GLU C N     1 
ATOM   11970 C  CA    . GLU C 2 144 ? 103.243 107.030 135.982 1.00 25.72 ?  123 GLU C CA    1 
ATOM   11971 C  C     . GLU C 2 144 ? 102.370 106.068 135.177 1.00 25.08 ?  123 GLU C C     1 
ATOM   11972 O  O     . GLU C 2 144 ? 102.063 104.966 135.633 1.00 24.67 ?  123 GLU C O     1 
ATOM   11973 C  CB    . GLU C 2 144 ? 102.394 108.060 136.722 1.00 26.23 ?  123 GLU C CB    1 
ATOM   11974 C  CG    . GLU C 2 144 ? 103.169 108.782 137.811 1.00 29.96 ?  123 GLU C CG    1 
ATOM   11975 C  CD    . GLU C 2 144 ? 103.837 107.818 138.777 1.00 33.82 ?  123 GLU C CD    1 
ATOM   11976 O  OE1   . GLU C 2 144 ? 103.108 107.100 139.494 1.00 36.54 ?  123 GLU C OE1   1 
ATOM   11977 O  OE2   . GLU C 2 144 ? 105.085 107.762 138.806 1.00 35.84 -1 123 GLU C OE2   1 
ATOM   11978 N  N     . TRP C 2 145 ? 102.002 106.485 133.968 1.00 24.21 ?  124 TRP C N     1 
ATOM   11979 C  CA    . TRP C 2 145 ? 101.215 105.651 133.061 1.00 23.99 ?  124 TRP C CA    1 
ATOM   11980 C  C     . TRP C 2 145 ? 101.915 104.345 132.662 1.00 23.95 ?  124 TRP C C     1 
ATOM   11981 O  O     . TRP C 2 145 ? 101.250 103.297 132.556 1.00 23.31 ?  124 TRP C O     1 
ATOM   11982 C  CB    . TRP C 2 145 ? 100.798 106.448 131.814 1.00 24.13 ?  124 TRP C CB    1 
ATOM   11983 C  CG    . TRP C 2 145 ? 100.240 105.585 130.705 1.00 24.37 ?  124 TRP C CG    1 
ATOM   11984 C  CD1   . TRP C 2 145 ? 98.931  105.209 130.522 1.00 24.76 ?  124 TRP C CD1   1 
ATOM   11985 C  CD2   . TRP C 2 145 ? 100.983 104.998 129.628 1.00 23.31 ?  124 TRP C CD2   1 
ATOM   11986 N  NE1   . TRP C 2 145 ? 98.823  104.415 129.395 1.00 24.97 ?  124 TRP C NE1   1 
ATOM   11987 C  CE2   . TRP C 2 145 ? 100.063 104.273 128.829 1.00 24.20 ?  124 TRP C CE2   1 
ATOM   11988 C  CE3   . TRP C 2 145 ? 102.336 105.005 129.264 1.00 23.76 ?  124 TRP C CE3   1 
ATOM   11989 C  CZ2   . TRP C 2 145 ? 100.459 103.566 127.685 1.00 23.41 ?  124 TRP C CZ2   1 
ATOM   11990 C  CZ3   . TRP C 2 145 ? 102.730 104.298 128.129 1.00 23.29 ?  124 TRP C CZ3   1 
ATOM   11991 C  CH2   . TRP C 2 145 ? 101.789 103.594 127.350 1.00 22.93 ?  124 TRP C CH2   1 
ATOM   11992 N  N     . VAL C 2 146 ? 103.232 104.376 132.431 1.00 23.35 ?  125 VAL C N     1 
ATOM   11993 C  CA    . VAL C 2 146 ? 103.926 103.094 132.143 1.00 23.53 ?  125 VAL C CA    1 
ATOM   11994 C  C     . VAL C 2 146 ? 103.818 102.099 133.306 1.00 23.73 ?  125 VAL C C     1 
ATOM   11995 O  O     . VAL C 2 146 ? 103.588 100.921 133.073 1.00 23.03 ?  125 VAL C O     1 
ATOM   11996 C  CB    . VAL C 2 146 ? 105.391 103.198 131.508 1.00 23.63 ?  125 VAL C CB    1 
ATOM   11997 C  CG1   . VAL C 2 146 ? 105.819 104.603 131.182 1.00 24.40 ?  125 VAL C CG1   1 
ATOM   11998 C  CG2   . VAL C 2 146 ? 106.468 102.418 132.286 1.00 22.97 ?  125 VAL C CG2   1 
ATOM   11999 N  N     . LYS C 2 147 ? 103.925 102.592 134.542 1.00 24.06 ?  126 LYS C N     1 
ATOM   12000 C  CA    . LYS C 2 147 ? 103.866 101.723 135.730 1.00 25.41 ?  126 LYS C CA    1 
ATOM   12001 C  C     . LYS C 2 147 ? 102.539 100.975 135.875 1.00 25.82 ?  126 LYS C C     1 
ATOM   12002 O  O     . LYS C 2 147 ? 102.517 99.850  136.381 1.00 26.08 ?  126 LYS C O     1 
ATOM   12003 C  CB    . LYS C 2 147 ? 104.120 102.525 137.009 1.00 25.49 ?  126 LYS C CB    1 
ATOM   12004 C  CG    . LYS C 2 147 ? 105.528 103.063 137.165 1.00 27.52 ?  126 LYS C CG    1 
ATOM   12005 C  CD    . LYS C 2 147 ? 105.604 103.908 138.431 1.00 30.43 ?  126 LYS C CD    1 
ATOM   12006 C  CE    . LYS C 2 147 ? 106.862 104.750 138.469 1.00 33.10 ?  126 LYS C CE    1 
ATOM   12007 N  NZ    . LYS C 2 147 ? 106.842 105.648 139.657 1.00 34.86 1  126 LYS C NZ    1 
ATOM   12008 N  N     . GLN C 2 148 ? 101.446 101.598 135.436 1.00 26.45 ?  127 GLN C N     1 
ATOM   12009 C  CA    . GLN C 2 148 ? 100.104 101.045 135.633 1.00 26.85 ?  127 GLN C CA    1 
ATOM   12010 C  C     . GLN C 2 148 ? 99.481  100.423 134.381 1.00 26.01 ?  127 GLN C C     1 
ATOM   12011 O  O     . GLN C 2 148 ? 98.401  99.833  134.462 1.00 26.12 ?  127 GLN C O     1 
ATOM   12012 C  CB    . GLN C 2 148 ? 99.156  102.097 136.240 1.00 28.08 ?  127 GLN C CB    1 
ATOM   12013 C  CG    . GLN C 2 148 ? 98.907  103.334 135.372 1.00 30.69 ?  127 GLN C CG    1 
ATOM   12014 C  CD    . GLN C 2 148 ? 97.966  103.071 134.199 1.00 34.64 ?  127 GLN C CD    1 
ATOM   12015 O  OE1   . GLN C 2 148 ? 98.371  103.148 133.026 1.00 33.80 ?  127 GLN C OE1   1 
ATOM   12016 N  NE2   . GLN C 2 148 ? 96.704  102.746 134.508 1.00 36.24 ?  127 GLN C NE2   1 
ATOM   12017 N  N     . ASN C 2 149 ? 100.147 100.559 133.232 1.00 24.97 ?  128 ASN C N     1 
ATOM   12018 C  CA    . ASN C 2 149 ? 99.640  99.996  131.984 1.00 24.03 ?  128 ASN C CA    1 
ATOM   12019 C  C     . ASN C 2 149 ? 99.847  98.490  131.951 1.00 24.13 ?  128 ASN C C     1 
ATOM   12020 O  O     . ASN C 2 149 ? 100.991 98.032  132.015 1.00 22.93 ?  128 ASN C O     1 
ATOM   12021 C  CB    . ASN C 2 149 ? 100.350 100.616 130.791 1.00 23.97 ?  128 ASN C CB    1 
ATOM   12022 C  CG    . ASN C 2 149 ? 99.762  100.165 129.476 1.00 23.94 ?  128 ASN C CG    1 
ATOM   12023 O  OD1   . ASN C 2 149 ? 100.179 99.155  128.911 1.00 24.85 ?  128 ASN C OD1   1 
ATOM   12024 N  ND2   . ASN C 2 149 ? 98.752  100.883 129.003 1.00 24.76 ?  128 ASN C ND2   1 
ATOM   12025 N  N     . LYS C 2 150 ? 98.758  97.729  131.820 1.00 24.32 ?  129 LYS C N     1 
ATOM   12026 C  CA    . LYS C 2 150 ? 98.825  96.263  131.981 1.00 24.77 ?  129 LYS C CA    1 
ATOM   12027 C  C     . LYS C 2 150 ? 99.573  95.514  130.875 1.00 24.54 ?  129 LYS C C     1 
ATOM   12028 O  O     . LYS C 2 150 ? 100.196 94.485  131.141 1.00 24.17 ?  129 LYS C O     1 
ATOM   12029 C  CB    . LYS C 2 150 ? 97.438  95.654  132.225 1.00 25.27 ?  129 LYS C CB    1 
ATOM   12030 C  CG    . LYS C 2 150 ? 96.435  95.828  131.103 1.00 28.72 ?  129 LYS C CG    1 
ATOM   12031 C  CD    . LYS C 2 150 ? 95.244  94.894  131.325 1.00 33.40 ?  129 LYS C CD    1 
ATOM   12032 C  CE    . LYS C 2 150 ? 94.017  95.375  130.576 1.00 36.77 ?  129 LYS C CE    1 
ATOM   12033 N  NZ    . LYS C 2 150 ? 92.819  94.576  130.977 1.00 39.66 1  129 LYS C NZ    1 
ATOM   12034 N  N     . TYR C 2 151 ? 99.505  96.027  129.642 1.00 23.92 ?  130 TYR C N     1 
ATOM   12035 C  CA    . TYR C 2 151 ? 100.202 95.406  128.508 1.00 24.12 ?  130 TYR C CA    1 
ATOM   12036 C  C     . TYR C 2 151 ? 101.706 95.616  128.569 1.00 23.54 ?  130 TYR C C     1 
ATOM   12037 O  O     . TYR C 2 151 ? 102.488 94.708  128.249 1.00 23.32 ?  130 TYR C O     1 
ATOM   12038 C  CB    . TYR C 2 151 ? 99.624  95.920  127.175 1.00 24.53 ?  130 TYR C CB    1 
ATOM   12039 C  CG    . TYR C 2 151 ? 98.111  95.959  127.184 1.00 25.83 ?  130 TYR C CG    1 
ATOM   12040 C  CD1   . TYR C 2 151 ? 97.369  94.782  127.298 1.00 26.57 ?  130 TYR C CD1   1 
ATOM   12041 C  CD2   . TYR C 2 151 ? 97.423  97.176  127.123 1.00 27.87 ?  130 TYR C CD2   1 
ATOM   12042 C  CE1   . TYR C 2 151 ? 95.979  94.806  127.328 1.00 29.65 ?  130 TYR C CE1   1 
ATOM   12043 C  CE2   . TYR C 2 151 ? 96.024  97.212  127.157 1.00 29.91 ?  130 TYR C CE2   1 
ATOM   12044 C  CZ    . TYR C 2 151 ? 95.314  96.024  127.261 1.00 31.19 ?  130 TYR C CZ    1 
ATOM   12045 O  OH    . TYR C 2 151 ? 93.934  96.039  127.295 1.00 34.44 ?  130 TYR C OH    1 
ATOM   12046 N  N     . LEU C 2 152 ? 102.106 96.813  128.982 1.00 23.38 ?  131 LEU C N     1 
ATOM   12047 C  CA    . LEU C 2 152 ? 103.511 97.148  129.131 1.00 23.43 ?  131 LEU C CA    1 
ATOM   12048 C  C     . LEU C 2 152 ? 104.109 96.376  130.312 1.00 23.37 ?  131 LEU C C     1 
ATOM   12049 O  O     . LEU C 2 152 ? 105.222 95.850  130.210 1.00 23.05 ?  131 LEU C O     1 
ATOM   12050 C  CB    . LEU C 2 152 ? 103.646 98.658  129.324 1.00 23.73 ?  131 LEU C CB    1 
ATOM   12051 C  CG    . LEU C 2 152 ? 104.667 99.539  128.613 1.00 24.71 ?  131 LEU C CG    1 
ATOM   12052 C  CD1   . LEU C 2 152 ? 105.284 98.936  127.340 1.00 21.63 ?  131 LEU C CD1   1 
ATOM   12053 C  CD2   . LEU C 2 152 ? 104.024 100.873 128.313 1.00 26.87 ?  131 LEU C CD2   1 
ATOM   12054 N  N     . GLN C 2 153 ? 103.380 96.305  131.430 1.00 22.80 ?  132 GLN C N     1 
ATOM   12055 C  CA    . GLN C 2 153 ? 103.823 95.458  132.549 1.00 22.70 ?  132 GLN C CA    1 
ATOM   12056 C  C     . GLN C 2 153 ? 103.912 93.973  132.186 1.00 22.54 ?  132 GLN C C     1 
ATOM   12057 O  O     . GLN C 2 153 ? 104.896 93.308  132.540 1.00 21.73 ?  132 GLN C O     1 
ATOM   12058 C  CB    . GLN C 2 153 ? 102.982 95.679  133.809 1.00 23.07 ?  132 GLN C CB    1 
ATOM   12059 C  CG    . GLN C 2 153 ? 103.113 97.096  134.369 1.00 21.83 ?  132 GLN C CG    1 
ATOM   12060 C  CD    . GLN C 2 153 ? 104.553 97.479  134.719 1.00 22.34 ?  132 GLN C CD    1 
ATOM   12061 O  OE1   . GLN C 2 153 ? 105.272 96.724  135.378 1.00 24.07 ?  132 GLN C OE1   1 
ATOM   12062 N  NE2   . GLN C 2 153 ? 104.969 98.664  134.290 1.00 22.26 ?  132 GLN C NE2   1 
ATOM   12063 N  N     . LYS C 2 154 ? 102.904 93.458  131.476 1.00 22.53 ?  133 LYS C N     1 
ATOM   12064 C  CA    . LYS C 2 154 ? 102.946 92.063  131.039 1.00 22.84 ?  133 LYS C CA    1 
ATOM   12065 C  C     . LYS C 2 154 ? 104.161 91.771  130.156 1.00 22.42 ?  133 LYS C C     1 
ATOM   12066 O  O     . LYS C 2 154 ? 104.835 90.769  130.368 1.00 21.90 ?  133 LYS C O     1 
ATOM   12067 C  CB    . LYS C 2 154 ? 101.635 91.607  130.356 1.00 22.96 ?  133 LYS C CB    1 
ATOM   12068 C  CG    . LYS C 2 154 ? 101.630 90.110  129.917 1.00 23.45 ?  133 LYS C CG    1 
ATOM   12069 C  CD    . LYS C 2 154 ? 101.712 89.122  131.101 1.00 26.74 ?  133 LYS C CD    1 
ATOM   12070 C  CE    . LYS C 2 154 ? 101.659 87.664  130.623 1.00 27.93 ?  133 LYS C CE    1 
ATOM   12071 N  NZ    . LYS C 2 154 ? 101.939 86.677  131.701 1.00 27.86 1  133 LYS C NZ    1 
ATOM   12072 N  N     . LYS C 2 155 ? 104.460 92.642  129.188 1.00 22.77 ?  134 LYS C N     1 
ATOM   12073 C  CA    . LYS C 2 155 ? 105.563 92.348  128.268 1.00 22.87 ?  134 LYS C CA    1 
ATOM   12074 C  C     . LYS C 2 155 ? 106.916 92.414  128.970 1.00 22.30 ?  134 LYS C C     1 
ATOM   12075 O  O     . LYS C 2 155 ? 107.774 91.545  128.738 1.00 21.89 ?  134 LYS C O     1 
ATOM   12076 C  CB    . LYS C 2 155 ? 105.508 93.173  126.961 1.00 23.33 ?  134 LYS C CB    1 
ATOM   12077 C  CG    . LYS C 2 155 ? 105.932 94.618  127.035 1.00 24.25 ?  134 LYS C CG    1 
ATOM   12078 C  CD    . LYS C 2 155 ? 105.836 95.297  125.658 1.00 26.87 ?  134 LYS C CD    1 
ATOM   12079 C  CE    . LYS C 2 155 ? 104.426 95.815  125.393 1.00 28.26 ?  134 LYS C CE    1 
ATOM   12080 N  NZ    . LYS C 2 155 ? 104.424 96.737  124.216 1.00 28.97 1  134 LYS C NZ    1 
ATOM   12081 N  N     . ALA C 2 156 ? 107.081 93.400  129.852 1.00 21.96 ?  135 ALA C N     1 
ATOM   12082 C  CA    . ALA C 2 156 ? 108.259 93.471  130.738 1.00 22.43 ?  135 ALA C CA    1 
ATOM   12083 C  C     . ALA C 2 156 ? 108.387 92.252  131.652 1.00 22.02 ?  135 ALA C C     1 
ATOM   12084 O  O     . ALA C 2 156 ? 109.481 91.719  131.816 1.00 22.60 ?  135 ALA C O     1 
ATOM   12085 C  CB    . ALA C 2 156 ? 108.245 94.760  131.587 1.00 22.05 ?  135 ALA C CB    1 
ATOM   12086 N  N     . GLN C 2 157 ? 107.280 91.826  132.261 1.00 21.97 ?  136 GLN C N     1 
ATOM   12087 C  CA    . GLN C 2 157 ? 107.287 90.641  133.129 1.00 22.10 ?  136 GLN C CA    1 
ATOM   12088 C  C     . GLN C 2 157 ? 107.797 89.423  132.387 1.00 21.87 ?  136 GLN C C     1 
ATOM   12089 O  O     . GLN C 2 157 ? 108.605 88.665  132.921 1.00 21.75 ?  136 GLN C O     1 
ATOM   12090 C  CB    . GLN C 2 157 ? 105.887 90.316  133.649 1.00 22.50 ?  136 GLN C CB    1 
ATOM   12091 C  CG    . GLN C 2 157 ? 105.425 91.159  134.828 1.00 23.55 ?  136 GLN C CG    1 
ATOM   12092 C  CD    . GLN C 2 157 ? 103.916 91.086  134.985 1.00 26.93 ?  136 GLN C CD    1 
ATOM   12093 O  OE1   . GLN C 2 157 ? 103.292 90.125  134.541 1.00 26.36 ?  136 GLN C OE1   1 
ATOM   12094 N  NE2   . GLN C 2 157 ? 103.323 92.110  135.588 1.00 28.09 ?  136 GLN C NE2   1 
ATOM   12095 N  N     . MET C 2 158 ? 107.303 89.240  131.164 1.00 21.38 ?  137 MET C N     1 
ATOM   12096 C  CA    . MET C 2 158 ? 107.627 88.069  130.363 1.00 22.08 ?  137 MET C CA    1 
ATOM   12097 C  C     . MET C 2 158 ? 109.077 88.073  129.893 1.00 21.70 ?  137 MET C C     1 
ATOM   12098 O  O     . MET C 2 158 ? 109.762 87.048  129.935 1.00 21.83 ?  137 MET C O     1 
ATOM   12099 C  CB    . MET C 2 158 ? 106.717 87.994  129.141 1.00 22.05 ?  137 MET C CB    1 
ATOM   12100 C  CG    . MET C 2 158 ? 105.283 87.540  129.444 1.00 23.93 ?  137 MET C CG    1 
ATOM   12101 S  SD    . MET C 2 158 ? 104.259 87.708  127.969 1.00 27.75 ?  137 MET C SD    1 
ATOM   12102 C  CE    . MET C 2 158 ? 104.972 86.405  126.954 1.00 26.00 ?  137 MET C CE    1 
ATOM   12103 N  N     . ILE C 2 159 ? 109.529 89.220  129.407 1.00 20.90 ?  138 ILE C N     1 
ATOM   12104 C  CA    . ILE C 2 159 ? 110.870 89.310  128.853 1.00 20.60 ?  138 ILE C CA    1 
ATOM   12105 C  C     . ILE C 2 159 ? 111.913 89.228  129.971 1.00 20.36 ?  138 ILE C C     1 
ATOM   12106 O  O     . ILE C 2 159 ? 112.847 88.428  129.886 1.00 19.65 ?  138 ILE C O     1 
ATOM   12107 C  CB    . ILE C 2 159 ? 111.046 90.583  127.974 1.00 20.17 ?  138 ILE C CB    1 
ATOM   12108 C  CG1   . ILE C 2 159 ? 110.165 90.501  126.714 1.00 20.66 ?  138 ILE C CG1   1 
ATOM   12109 C  CG2   . ILE C 2 159 ? 112.531 90.845  127.670 1.00 20.62 ?  138 ILE C CG2   1 
ATOM   12110 C  CD1   . ILE C 2 159 ? 110.492 89.391  125.709 1.00 22.17 ?  138 ILE C CD1   1 
ATOM   12111 N  N     . VAL C 2 160 ? 111.736 90.032  131.020 1.00 19.58 ?  139 VAL C N     1 
ATOM   12112 C  CA    . VAL C 2 160 ? 112.687 90.080  132.135 1.00 19.88 ?  139 VAL C CA    1 
ATOM   12113 C  C     . VAL C 2 160 ? 112.683 88.756  132.904 1.00 19.44 ?  139 VAL C C     1 
ATOM   12114 O  O     . VAL C 2 160 ? 113.704 88.342  133.441 1.00 19.88 ?  139 VAL C O     1 
ATOM   12115 C  CB    . VAL C 2 160 ? 112.412 91.278  133.115 1.00 19.52 ?  139 VAL C CB    1 
ATOM   12116 C  CG1   . VAL C 2 160 ? 113.372 91.239  134.318 1.00 20.75 ?  139 VAL C CG1   1 
ATOM   12117 C  CG2   . VAL C 2 160 ? 112.572 92.612  132.396 1.00 20.03 ?  139 VAL C CG2   1 
ATOM   12118 N  N     . GLY C 2 161 ? 111.533 88.091  132.950 1.00 19.13 ?  140 GLY C N     1 
ATOM   12119 C  CA    . GLY C 2 161 ? 111.450 86.804  133.621 1.00 18.05 ?  140 GLY C CA    1 
ATOM   12120 C  C     . GLY C 2 161 ? 112.378 85.809  132.973 1.00 17.86 ?  140 GLY C C     1 
ATOM   12121 O  O     . GLY C 2 161 ? 113.102 85.074  133.653 1.00 17.47 ?  140 GLY C O     1 
ATOM   12122 N  N     . LEU C 2 162 ? 112.349 85.774  131.645 1.00 17.92 ?  141 LEU C N     1 
ATOM   12123 C  CA    . LEU C 2 162 ? 113.240 84.898  130.892 1.00 18.32 ?  141 LEU C CA    1 
ATOM   12124 C  C     . LEU C 2 162 ? 114.731 85.256  131.079 1.00 18.55 ?  141 LEU C C     1 
ATOM   12125 O  O     . LEU C 2 162 ? 115.562 84.362  131.237 1.00 18.49 ?  141 LEU C O     1 
ATOM   12126 C  CB    . LEU C 2 162 ? 112.845 84.898  129.410 1.00 18.50 ?  141 LEU C CB    1 
ATOM   12127 C  CG    . LEU C 2 162 ? 111.521 84.185  129.121 1.00 19.32 ?  141 LEU C CG    1 
ATOM   12128 C  CD1   . LEU C 2 162 ? 111.006 84.553  127.733 1.00 20.38 ?  141 LEU C CD1   1 
ATOM   12129 C  CD2   . LEU C 2 162 ? 111.667 82.668  129.274 1.00 19.94 ?  141 LEU C CD2   1 
ATOM   12130 N  N     . TYR C 2 163 ? 115.063 86.544  131.097 1.00 19.16 ?  142 TYR C N     1 
ATOM   12131 C  CA    . TYR C 2 163 ? 116.443 86.972  131.404 1.00 20.16 ?  142 TYR C CA    1 
ATOM   12132 C  C     . TYR C 2 163 ? 116.910 86.468  132.758 1.00 20.78 ?  142 TYR C C     1 
ATOM   12133 O  O     . TYR C 2 163 ? 118.042 86.001  132.909 1.00 20.36 ?  142 TYR C O     1 
ATOM   12134 C  CB    . TYR C 2 163 ? 116.583 88.504  131.392 1.00 20.34 ?  142 TYR C CB    1 
ATOM   12135 C  CG    . TYR C 2 163 ? 116.365 89.163  130.038 1.00 22.46 ?  142 TYR C CG    1 
ATOM   12136 C  CD1   . TYR C 2 163 ? 116.545 88.459  128.852 1.00 23.88 ?  142 TYR C CD1   1 
ATOM   12137 C  CD2   . TYR C 2 163 ? 115.987 90.498  129.953 1.00 22.41 ?  142 TYR C CD2   1 
ATOM   12138 C  CE1   . TYR C 2 163 ? 116.338 89.077  127.604 1.00 25.93 ?  142 TYR C CE1   1 
ATOM   12139 C  CE2   . TYR C 2 163 ? 115.785 91.118  128.722 1.00 22.07 ?  142 TYR C CE2   1 
ATOM   12140 C  CZ    . TYR C 2 163 ? 115.970 90.409  127.559 1.00 25.19 ?  142 TYR C CZ    1 
ATOM   12141 O  OH    . TYR C 2 163 ? 115.761 91.048  126.354 1.00 27.43 ?  142 TYR C OH    1 
ATOM   12142 N  N     . LYS C 2 164 ? 116.031 86.561  133.748 1.00 21.39 ?  143 LYS C N     1 
ATOM   12143 C  CA    . LYS C 2 164 ? 116.423 86.212  135.104 1.00 22.49 ?  143 LYS C CA    1 
ATOM   12144 C  C     . LYS C 2 164 ? 116.369 84.710  135.367 1.00 22.49 ?  143 LYS C C     1 
ATOM   12145 O  O     . LYS C 2 164 ? 116.886 84.242  136.375 1.00 22.45 ?  143 LYS C O     1 
ATOM   12146 C  CB    . LYS C 2 164 ? 115.643 87.032  136.129 1.00 23.16 ?  143 LYS C CB    1 
ATOM   12147 C  CG    . LYS C 2 164 ? 116.030 88.509  136.071 1.00 26.08 ?  143 LYS C CG    1 
ATOM   12148 C  CD    . LYS C 2 164 ? 115.721 89.231  137.350 1.00 30.38 ?  143 LYS C CD    1 
ATOM   12149 C  CE    . LYS C 2 164 ? 116.288 90.630  137.326 1.00 32.69 ?  143 LYS C CE    1 
ATOM   12150 N  NZ    . LYS C 2 164 ? 115.932 91.352  138.579 1.00 35.60 1  143 LYS C NZ    1 
ATOM   12151 N  N     . ALA C 2 165 ? 115.812 83.956  134.417 1.00 22.02 ?  144 ALA C N     1 
ATOM   12152 C  CA    . ALA C 2 165 ? 115.785 82.509  134.523 1.00 22.69 ?  144 ALA C CA    1 
ATOM   12153 C  C     . ALA C 2 165 ? 117.056 81.839  133.974 1.00 23.20 ?  144 ALA C C     1 
ATOM   12154 O  O     . ALA C 2 165 ? 117.231 80.637  134.128 1.00 23.80 ?  144 ALA C O     1 
ATOM   12155 C  CB    . ALA C 2 165 ? 114.516 81.938  133.845 1.00 21.79 ?  144 ALA C CB    1 
ATOM   12156 N  N     . ILE C 2 166 ? 117.945 82.604  133.336 1.00 23.97 ?  145 ILE C N     1 
ATOM   12157 C  CA    . ILE C 2 166 ? 119.188 82.027  132.810 1.00 24.29 ?  145 ILE C CA    1 
ATOM   12158 C  C     . ILE C 2 166 ? 119.988 81.367  133.936 1.00 25.49 ?  145 ILE C C     1 
ATOM   12159 O  O     . ILE C 2 166 ? 120.169 81.950  135.001 1.00 25.82 ?  145 ILE C O     1 
ATOM   12160 C  CB    . ILE C 2 166 ? 120.082 83.071  132.080 1.00 24.22 ?  145 ILE C CB    1 
ATOM   12161 C  CG1   . ILE C 2 166 ? 119.350 83.685  130.890 1.00 23.45 ?  145 ILE C CG1   1 
ATOM   12162 C  CG2   . ILE C 2 166 ? 121.384 82.425  131.604 1.00 23.42 ?  145 ILE C CG2   1 
ATOM   12163 C  CD1   . ILE C 2 166 ? 120.047 84.946  130.316 1.00 21.99 ?  145 ILE C CD1   1 
ATOM   12164 N  N     . GLN C 2 167 ? 120.412 80.132  133.705 1.00 26.83 ?  146 GLN C N     1 
ATOM   12165 C  CA    . GLN C 2 167 ? 121.222 79.405  134.672 1.00 28.85 ?  146 GLN C CA    1 
ATOM   12166 C  C     . GLN C 2 167 ? 122.621 79.264  134.104 1.00 29.77 ?  146 GLN C C     1 
ATOM   12167 O  O     . GLN C 2 167 ? 122.788 78.975  132.914 1.00 29.74 ?  146 GLN C O     1 
ATOM   12168 C  CB    . GLN C 2 167 ? 120.629 78.020  134.971 1.00 28.99 ?  146 GLN C CB    1 
ATOM   12169 C  CG    . GLN C 2 167 ? 119.345 78.040  135.802 1.00 30.30 ?  146 GLN C CG    1 
ATOM   12170 C  CD    . GLN C 2 167 ? 119.580 78.447  137.251 1.00 33.32 ?  146 GLN C CD    1 
ATOM   12171 O  OE1   . GLN C 2 167 ? 120.722 78.536  137.705 1.00 34.63 ?  146 GLN C OE1   1 
ATOM   12172 N  NE2   . GLN C 2 167 ? 118.496 78.672  137.989 1.00 32.32 ?  146 GLN C NE2   1 
ATOM   12173 N  N     . LYS C 2 168 ? 123.620 79.475  134.952 1.00 31.29 ?  147 LYS C N     1 
ATOM   12174 C  CA    . LYS C 2 168 ? 125.019 79.357  134.542 1.00 33.14 ?  147 LYS C CA    1 
ATOM   12175 C  C     . LYS C 2 168 ? 125.247 77.993  133.906 1.00 33.79 ?  147 LYS C C     1 
ATOM   12176 O  O     . LYS C 2 168 ? 124.686 76.986  134.352 1.00 34.06 ?  147 LYS C O     1 
ATOM   12177 C  CB    . LYS C 2 168 ? 125.945 79.570  135.736 1.00 33.44 ?  147 LYS C CB    1 
ATOM   12178 C  CG    . LYS C 2 168 ? 127.378 79.971  135.392 1.00 35.61 ?  147 LYS C CG    1 
ATOM   12179 C  CD    . LYS C 2 168 ? 128.171 80.195  136.676 1.00 38.40 ?  147 LYS C CD    1 
ATOM   12180 C  CE    . LYS C 2 168 ? 129.511 80.867  136.428 1.00 40.48 ?  147 LYS C CE    1 
ATOM   12181 N  NZ    . LYS C 2 168 ? 130.603 79.859  136.363 1.00 41.56 1  147 LYS C NZ    1 
ATOM   12182 N  N     . ASP C 2 169 ? 126.031 77.980  132.832 1.00 35.10 ?  148 ASP C N     1 
ATOM   12183 C  CA    . ASP C 2 169 ? 126.362 76.750  132.095 1.00 36.27 ?  148 ASP C CA    1 
ATOM   12184 C  C     . ASP C 2 169 ? 125.162 75.975  131.548 1.00 36.29 ?  148 ASP C C     1 
ATOM   12185 O  O     . ASP C 2 169 ? 125.287 74.806  131.179 1.00 36.95 ?  148 ASP C O     1 
ATOM   12186 C  CB    . ASP C 2 169 ? 127.221 75.822  132.960 1.00 37.15 ?  148 ASP C CB    1 
ATOM   12187 C  CG    . ASP C 2 169 ? 128.611 76.356  133.182 1.00 38.94 ?  148 ASP C CG    1 
ATOM   12188 O  OD1   . ASP C 2 169 ? 129.071 77.198  132.376 1.00 41.71 ?  148 ASP C OD1   1 
ATOM   12189 O  OD2   . ASP C 2 169 ? 129.244 75.932  134.170 1.00 41.64 -1 148 ASP C OD2   1 
ATOM   12190 N  N     . ASP C 2 170 ? 124.000 76.616  131.498 1.00 35.87 ?  149 ASP C N     1 
ATOM   12191 C  CA    . ASP C 2 170 ? 122.814 75.973  130.948 1.00 35.24 ?  149 ASP C CA    1 
ATOM   12192 C  C     . ASP C 2 170 ? 122.424 76.726  129.683 1.00 34.12 ?  149 ASP C C     1 
ATOM   12193 O  O     . ASP C 2 170 ? 121.819 77.815  129.733 1.00 33.52 ?  149 ASP C O     1 
ATOM   12194 C  CB    . ASP C 2 170 ? 121.685 75.924  131.984 1.00 36.09 ?  149 ASP C CB    1 
ATOM   12195 C  CG    . ASP C 2 170 ? 120.357 75.436  131.406 1.00 38.39 ?  149 ASP C CG    1 
ATOM   12196 O  OD1   . ASP C 2 170 ? 120.322 74.863  130.291 1.00 42.06 ?  149 ASP C OD1   1 
ATOM   12197 O  OD2   . ASP C 2 170 ? 119.330 75.620  132.088 1.00 42.21 -1 149 ASP C OD2   1 
ATOM   12198 N  N     . GLU C 2 171 ? 122.802 76.133  128.555 1.00 32.48 ?  150 GLU C N     1 
ATOM   12199 C  CA    . GLU C 2 171 ? 122.669 76.765  127.254 1.00 30.93 ?  150 GLU C CA    1 
ATOM   12200 C  C     . GLU C 2 171 ? 121.209 76.921  126.818 1.00 29.37 ?  150 GLU C C     1 
ATOM   12201 O  O     . GLU C 2 171 ? 120.886 77.839  126.064 1.00 28.99 ?  150 GLU C O     1 
ATOM   12202 C  CB    . GLU C 2 171 ? 123.505 76.021  126.195 1.00 31.30 ?  150 GLU C CB    1 
ATOM   12203 C  CG    . GLU C 2 171 ? 122.986 74.630  125.758 1.00 33.64 ?  150 GLU C CG    1 
ATOM   12204 C  CD    . GLU C 2 171 ? 124.010 73.807  124.937 1.00 36.40 ?  150 GLU C CD    1 
ATOM   12205 O  OE1   . GLU C 2 171 ? 125.122 74.306  124.658 1.00 38.62 ?  150 GLU C OE1   1 
ATOM   12206 O  OE2   . GLU C 2 171 ? 123.700 72.651  124.570 1.00 37.42 -1 150 GLU C OE2   1 
ATOM   12207 N  N     . ILE C 2 172 ? 120.337 76.029  127.289 1.00 27.68 ?  151 ILE C N     1 
ATOM   12208 C  CA    . ILE C 2 172 ? 118.919 76.093  126.925 1.00 26.26 ?  151 ILE C CA    1 
ATOM   12209 C  C     . ILE C 2 172 ? 118.240 77.314  127.551 1.00 24.85 ?  151 ILE C C     1 
ATOM   12210 O  O     . ILE C 2 172 ? 117.494 78.012  126.867 1.00 23.53 ?  151 ILE C O     1 
ATOM   12211 C  CB    . ILE C 2 172 ? 118.158 74.782  127.260 1.00 26.53 ?  151 ILE C CB    1 
ATOM   12212 C  CG1   . ILE C 2 172 ? 118.749 73.595  126.481 1.00 27.59 ?  151 ILE C CG1   1 
ATOM   12213 C  CG2   . ILE C 2 172 ? 116.644 74.929  127.015 1.00 26.51 ?  151 ILE C CG2   1 
ATOM   12214 C  CD1   . ILE C 2 172 ? 118.562 73.645  124.958 1.00 26.91 ?  151 ILE C CD1   1 
ATOM   12215 N  N     . SER C 2 173 ? 118.505 77.584  128.833 1.00 23.58 ?  152 SER C N     1 
ATOM   12216 C  CA    . SER C 2 173 ? 117.928 78.772  129.457 1.00 22.36 ?  152 SER C CA    1 
ATOM   12217 C  C     . SER C 2 173 ? 118.466 80.040  128.792 1.00 21.79 ?  152 SER C C     1 
ATOM   12218 O  O     . SER C 2 173 ? 117.747 81.039  128.666 1.00 20.91 ?  152 SER C O     1 
ATOM   12219 C  CB    . SER C 2 173 ? 118.142 78.790  130.976 1.00 22.43 ?  152 SER C CB    1 
ATOM   12220 O  OG    . SER C 2 173 ? 119.520 78.799  131.313 1.00 24.02 ?  152 SER C OG    1 
ATOM   12221 N  N     . LEU C 2 174 ? 119.730 79.990  128.370 1.00 21.65 ?  153 LEU C N     1 
ATOM   12222 C  CA    . LEU C 2 174 ? 120.357 81.110  127.671 1.00 21.86 ?  153 LEU C CA    1 
ATOM   12223 C  C     . LEU C 2 174 ? 119.698 81.344  126.309 1.00 21.98 ?  153 LEU C C     1 
ATOM   12224 O  O     . LEU C 2 174 ? 119.379 82.487  125.976 1.00 21.64 ?  153 LEU C O     1 
ATOM   12225 C  CB    . LEU C 2 174 ? 121.882 80.923  127.539 1.00 21.71 ?  153 LEU C CB    1 
ATOM   12226 C  CG    . LEU C 2 174 ? 122.702 82.009  126.814 1.00 22.04 ?  153 LEU C CG    1 
ATOM   12227 C  CD1   . LEU C 2 174 ? 122.442 83.411  127.363 1.00 21.99 ?  153 LEU C CD1   1 
ATOM   12228 C  CD2   . LEU C 2 174 ? 124.195 81.672  126.888 1.00 23.37 ?  153 LEU C CD2   1 
ATOM   12229 N  N     . PHE C 2 175 ? 119.491 80.268  125.542 1.00 22.17 ?  154 PHE C N     1 
ATOM   12230 C  CA    . PHE C 2 175 ? 118.777 80.339  124.247 1.00 22.02 ?  154 PHE C CA    1 
ATOM   12231 C  C     . PHE C 2 175 ? 117.412 81.002  124.384 1.00 21.86 ?  154 PHE C C     1 
ATOM   12232 O  O     . PHE C 2 175 ? 117.024 81.836  123.556 1.00 21.62 ?  154 PHE C O     1 
ATOM   12233 C  CB    . PHE C 2 175 ? 118.580 78.935  123.652 1.00 22.08 ?  154 PHE C CB    1 
ATOM   12234 C  CG    . PHE C 2 175 ? 117.709 78.910  122.411 1.00 21.99 ?  154 PHE C CG    1 
ATOM   12235 C  CD1   . PHE C 2 175 ? 118.251 79.199  121.155 1.00 20.87 ?  154 PHE C CD1   1 
ATOM   12236 C  CD2   . PHE C 2 175 ? 116.342 78.613  122.504 1.00 20.82 ?  154 PHE C CD2   1 
ATOM   12237 C  CE1   . PHE C 2 175 ? 117.451 79.206  120.011 1.00 20.27 ?  154 PHE C CE1   1 
ATOM   12238 C  CE2   . PHE C 2 175 ? 115.528 78.605  121.368 1.00 20.19 ?  154 PHE C CE2   1 
ATOM   12239 C  CZ    . PHE C 2 175 ? 116.085 78.897  120.110 1.00 20.93 ?  154 PHE C CZ    1 
ATOM   12240 N  N     . LYS C 2 176 ? 116.669 80.592  125.413 1.00 21.98 ?  155 LYS C N     1 
ATOM   12241 C  CA    . LYS C 2 176 ? 115.325 81.126  125.650 1.00 21.79 ?  155 LYS C CA    1 
ATOM   12242 C  C     . LYS C 2 176 ? 115.360 82.638  125.897 1.00 21.70 ?  155 LYS C C     1 
ATOM   12243 O  O     . LYS C 2 176 ? 114.533 83.383  125.352 1.00 21.10 ?  155 LYS C O     1 
ATOM   12244 C  CB    . LYS C 2 176 ? 114.647 80.380  126.807 1.00 22.00 ?  155 LYS C CB    1 
ATOM   12245 C  CG    . LYS C 2 176 ? 114.342 78.918  126.506 1.00 21.93 ?  155 LYS C CG    1 
ATOM   12246 C  CD    . LYS C 2 176 ? 113.736 78.211  127.706 1.00 23.06 ?  155 LYS C CD    1 
ATOM   12247 C  CE    . LYS C 2 176 ? 113.375 76.776  127.380 1.00 24.91 ?  155 LYS C CE    1 
ATOM   12248 N  NZ    . LYS C 2 176 ? 113.090 75.987  128.625 1.00 25.16 1  155 LYS C NZ    1 
ATOM   12249 N  N     . ALA C 2 177 ? 116.320 83.085  126.712 1.00 21.49 ?  156 ALA C N     1 
ATOM   12250 C  CA    . ALA C 2 177 ? 116.518 84.515  126.935 1.00 20.60 ?  156 ALA C CA    1 
ATOM   12251 C  C     . ALA C 2 177 ? 116.963 85.273  125.665 1.00 20.37 ?  156 ALA C C     1 
ATOM   12252 O  O     . ALA C 2 177 ? 116.549 86.405  125.451 1.00 19.61 ?  156 ALA C O     1 
ATOM   12253 C  CB    . ALA C 2 177 ? 117.495 84.761  128.080 1.00 20.88 ?  156 ALA C CB    1 
ATOM   12254 N  N     . MET C 2 178 ? 117.788 84.644  124.828 1.00 20.70 ?  157 MET C N     1 
ATOM   12255 C  CA    . MET C 2 178 ? 118.212 85.258  123.558 1.00 21.06 ?  157 MET C CA    1 
ATOM   12256 C  C     . MET C 2 178 ? 117.060 85.385  122.581 1.00 20.83 ?  157 MET C C     1 
ATOM   12257 O  O     . MET C 2 178 ? 117.022 86.332  121.788 1.00 21.28 ?  157 MET C O     1 
ATOM   12258 C  CB    . MET C 2 178 ? 119.350 84.466  122.888 1.00 20.68 ?  157 MET C CB    1 
ATOM   12259 C  CG    . MET C 2 178 ? 120.699 84.502  123.605 1.00 21.61 ?  157 MET C CG    1 
ATOM   12260 S  SD    . MET C 2 178 ? 121.853 83.335  122.846 1.00 24.32 ?  157 MET C SD    1 
ATOM   12261 C  CE    . MET C 2 178 ? 123.403 83.851  123.613 1.00 23.64 ?  157 MET C CE    1 
ATOM   12262 N  N     . VAL C 2 179 ? 116.141 84.420  122.599 1.00 20.76 ?  158 VAL C N     1 
ATOM   12263 C  CA    . VAL C 2 179 ? 114.930 84.510  121.773 1.00 20.14 ?  158 VAL C CA    1 
ATOM   12264 C  C     . VAL C 2 179 ? 114.096 85.705  122.248 1.00 20.35 ?  158 VAL C C     1 
ATOM   12265 O  O     . VAL C 2 179 ? 113.615 86.505  121.442 1.00 19.82 ?  158 VAL C O     1 
ATOM   12266 C  CB    . VAL C 2 179 ? 114.072 83.219  121.848 1.00 20.07 ?  158 VAL C CB    1 
ATOM   12267 C  CG1   . VAL C 2 179 ? 112.707 83.439  121.190 1.00 20.07 ?  158 VAL C CG1   1 
ATOM   12268 C  CG2   . VAL C 2 179 ? 114.797 82.054  121.182 1.00 20.57 ?  158 VAL C CG2   1 
ATOM   12269 N  N     . ALA C 2 180 ? 113.942 85.810  123.564 1.00 19.89 ?  159 ALA C N     1 
ATOM   12270 C  CA    . ALA C 2 180 ? 113.221 86.924  124.181 1.00 20.50 ?  159 ALA C CA    1 
ATOM   12271 C  C     . ALA C 2 180 ? 113.855 88.268  123.780 1.00 20.67 ?  159 ALA C C     1 
ATOM   12272 O  O     . ALA C 2 180 ? 113.146 89.203  123.405 1.00 21.27 ?  159 ALA C O     1 
ATOM   12273 C  CB    . ALA C 2 180 ? 113.228 86.768  125.686 1.00 20.03 ?  159 ALA C CB    1 
ATOM   12274 N  N     . SER C 2 181 ? 115.183 88.344  123.848 1.00 20.78 ?  160 SER C N     1 
ATOM   12275 C  CA    . SER C 2 181 ? 115.927 89.543  123.445 1.00 21.26 ?  160 SER C CA    1 
ATOM   12276 C  C     . SER C 2 181 ? 115.741 89.875  121.957 1.00 21.19 ?  160 SER C C     1 
ATOM   12277 O  O     . SER C 2 181 ? 115.487 91.023  121.611 1.00 20.89 ?  160 SER C O     1 
ATOM   12278 C  CB    . SER C 2 181 ? 117.418 89.406  123.791 1.00 21.42 ?  160 SER C CB    1 
ATOM   12279 O  OG    . SER C 2 181 ? 118.127 90.598  123.485 1.00 23.69 ?  160 SER C OG    1 
ATOM   12280 N  N     . VAL C 2 182 ? 115.867 88.879  121.074 1.00 20.99 ?  161 VAL C N     1 
ATOM   12281 C  CA    . VAL C 2 182 ? 115.573 89.126  119.658 1.00 21.18 ?  161 VAL C CA    1 
ATOM   12282 C  C     . VAL C 2 182 ? 114.134 89.641  119.476 1.00 21.15 ?  161 VAL C C     1 
ATOM   12283 O  O     . VAL C 2 182 ? 113.903 90.597  118.717 1.00 21.18 ?  161 VAL C O     1 
ATOM   12284 C  CB    . VAL C 2 182 ? 115.844 87.879  118.757 1.00 21.11 ?  161 VAL C CB    1 
ATOM   12285 C  CG1   . VAL C 2 182 ? 115.331 88.117  117.339 1.00 21.75 ?  161 VAL C CG1   1 
ATOM   12286 C  CG2   . VAL C 2 182 ? 117.336 87.552  118.734 1.00 20.98 ?  161 VAL C CG2   1 
ATOM   12287 N  N     . TYR C 2 183 ? 113.165 89.033  120.174 1.00 21.10 ?  162 TYR C N     1 
ATOM   12288 C  CA    . TYR C 2 183 ? 111.774 89.502  120.083 1.00 21.21 ?  162 TYR C CA    1 
ATOM   12289 C  C     . TYR C 2 183 ? 111.594 90.935  120.582 1.00 21.38 ?  162 TYR C C     1 
ATOM   12290 O  O     . TYR C 2 183 ? 110.768 91.673  120.057 1.00 20.97 ?  162 TYR C O     1 
ATOM   12291 C  CB    . TYR C 2 183 ? 110.781 88.567  120.804 1.00 21.50 ?  162 TYR C CB    1 
ATOM   12292 C  CG    . TYR C 2 183 ? 110.561 87.250  120.110 1.00 22.20 ?  162 TYR C CG    1 
ATOM   12293 C  CD1   . TYR C 2 183 ? 110.852 87.096  118.756 1.00 23.80 ?  162 TYR C CD1   1 
ATOM   12294 C  CD2   . TYR C 2 183 ? 110.039 86.153  120.805 1.00 23.71 ?  162 TYR C CD2   1 
ATOM   12295 C  CE1   . TYR C 2 183 ? 110.648 85.872  118.108 1.00 25.52 ?  162 TYR C CE1   1 
ATOM   12296 C  CE2   . TYR C 2 183 ? 109.829 84.938  120.172 1.00 24.01 ?  162 TYR C CE2   1 
ATOM   12297 C  CZ    . TYR C 2 183 ? 110.143 84.798  118.830 1.00 25.47 ?  162 TYR C CZ    1 
ATOM   12298 O  OH    . TYR C 2 183 ? 109.952 83.587  118.199 1.00 25.37 ?  162 TYR C OH    1 
ATOM   12299 N  N     . LEU C 2 184 ? 112.355 91.312  121.599 1.00 22.12 ?  163 LEU C N     1 
ATOM   12300 C  CA    . LEU C 2 184 ? 112.361 92.710  122.071 1.00 23.80 ?  163 LEU C CA    1 
ATOM   12301 C  C     . LEU C 2 184 ? 112.993 93.629  121.017 1.00 24.21 ?  163 LEU C C     1 
ATOM   12302 O  O     . LEU C 2 184 ? 112.429 94.656  120.700 1.00 24.72 ?  163 LEU C O     1 
ATOM   12303 C  CB    . LEU C 2 184 ? 113.090 92.834  123.413 1.00 23.52 ?  163 LEU C CB    1 
ATOM   12304 C  CG    . LEU C 2 184 ? 113.139 94.188  124.150 1.00 24.91 ?  163 LEU C CG    1 
ATOM   12305 C  CD1   . LEU C 2 184 ? 113.129 93.956  125.640 1.00 24.81 ?  163 LEU C CD1   1 
ATOM   12306 C  CD2   . LEU C 2 184 ? 114.344 95.053  123.754 1.00 26.39 ?  163 LEU C CD2   1 
ATOM   12307 N  N     . GLU C 2 185 ? 114.150 93.237  120.466 1.00 25.17 ?  164 GLU C N     1 
ATOM   12308 C  CA    . GLU C 2 185 ? 114.898 94.084  119.524 1.00 25.30 ?  164 GLU C CA    1 
ATOM   12309 C  C     . GLU C 2 185 ? 114.176 94.294  118.182 1.00 25.07 ?  164 GLU C C     1 
ATOM   12310 O  O     . GLU C 2 185 ? 114.137 95.411  117.639 1.00 24.49 ?  164 GLU C O     1 
ATOM   12311 C  CB    . GLU C 2 185 ? 116.294 93.485  119.231 1.00 26.17 ?  164 GLU C CB    1 
ATOM   12312 C  CG    . GLU C 2 185 ? 117.260 93.453  120.435 1.00 27.05 ?  164 GLU C CG    1 
ATOM   12313 C  CD    . GLU C 2 185 ? 117.888 94.817  120.745 1.00 29.23 ?  164 GLU C CD    1 
ATOM   12314 O  OE1   . GLU C 2 185 ? 117.587 95.827  120.047 1.00 28.79 ?  164 GLU C OE1   1 
ATOM   12315 O  OE2   . GLU C 2 185 ? 118.725 94.888  121.675 1.00 28.65 -1 164 GLU C OE2   1 
ATOM   12316 N  N     . SER C 2 186 ? 113.633 93.203  117.657 1.00 24.23 ?  165 SER C N     1 
ATOM   12317 C  CA    . SER C 2 186 ? 113.234 93.114  116.258 1.00 24.71 ?  165 SER C CA    1 
ATOM   12318 C  C     . SER C 2 186 ? 111.724 93.049  116.053 1.00 24.51 ?  165 SER C C     1 
ATOM   12319 O  O     . SER C 2 186 ? 111.256 93.127  114.919 1.00 24.87 ?  165 SER C O     1 
ATOM   12320 C  CB    . SER C 2 186 ? 113.882 91.881  115.615 1.00 25.06 ?  165 SER C CB    1 
ATOM   12321 O  OG    . SER C 2 186 ? 115.294 91.928  115.709 1.00 26.29 ?  165 SER C OG    1 
ATOM   12322 N  N     . PHE C 2 187 ? 110.975 92.892  117.142 1.00 24.71 ?  166 PHE C N     1 
ATOM   12323 C  CA    . PHE C 2 187 ? 109.516 92.809  117.085 1.00 25.69 ?  166 PHE C CA    1 
ATOM   12324 C  C     . PHE C 2 187 ? 108.836 93.837  118.004 1.00 25.87 ?  166 PHE C C     1 
ATOM   12325 O  O     . PHE C 2 187 ? 108.102 94.695  117.511 1.00 26.03 ?  166 PHE C O     1 
ATOM   12326 C  CB    . PHE C 2 187 ? 109.027 91.382  117.398 1.00 25.54 ?  166 PHE C CB    1 
ATOM   12327 C  CG    . PHE C 2 187 ? 107.533 91.272  117.622 1.00 26.64 ?  166 PHE C CG    1 
ATOM   12328 C  CD1   . PHE C 2 187 ? 106.626 91.606  116.608 1.00 25.90 ?  166 PHE C CD1   1 
ATOM   12329 C  CD2   . PHE C 2 187 ? 107.032 90.821  118.847 1.00 27.45 ?  166 PHE C CD2   1 
ATOM   12330 C  CE1   . PHE C 2 187 ? 105.237 91.508  116.816 1.00 25.64 ?  166 PHE C CE1   1 
ATOM   12331 C  CE2   . PHE C 2 187 ? 105.638 90.714  119.069 1.00 26.52 ?  166 PHE C CE2   1 
ATOM   12332 C  CZ    . PHE C 2 187 ? 104.746 91.057  118.050 1.00 27.18 ?  166 PHE C CZ    1 
ATOM   12333 N  N     . LEU C 2 188 ? 109.096 93.750  119.310 1.00 26.13 ?  167 LEU C N     1 
ATOM   12334 C  CA    . LEU C 2 188 ? 108.381 94.557  120.334 1.00 27.13 ?  167 LEU C CA    1 
ATOM   12335 C  C     . LEU C 2 188 ? 108.566 96.083  120.245 1.00 27.22 ?  167 LEU C C     1 
ATOM   12336 O  O     . LEU C 2 188 ? 107.661 96.842  120.617 1.00 28.03 ?  167 LEU C O     1 
ATOM   12337 C  CB    . LEU C 2 188 ? 108.753 94.104  121.755 1.00 26.89 ?  167 LEU C CB    1 
ATOM   12338 C  CG    . LEU C 2 188 ? 108.382 92.716  122.300 1.00 28.64 ?  167 LEU C CG    1 
ATOM   12339 C  CD1   . LEU C 2 188 ? 108.924 92.545  123.717 1.00 28.34 ?  167 LEU C CD1   1 
ATOM   12340 C  CD2   . LEU C 2 188 ? 106.884 92.464  122.281 1.00 27.90 ?  167 LEU C CD2   1 
ATOM   12341 N  N     . PHE C 2 189 ? 109.736 96.528  119.802 1.00 26.79 ?  168 PHE C N     1 
ATOM   12342 C  CA    . PHE C 2 189 ? 109.990 97.960  119.657 1.00 26.90 ?  168 PHE C CA    1 
ATOM   12343 C  C     . PHE C 2 189 ? 109.097 98.578  118.575 1.00 26.52 ?  168 PHE C C     1 
ATOM   12344 O  O     . PHE C 2 189 ? 108.877 99.797  118.560 1.00 26.02 ?  168 PHE C O     1 
ATOM   12345 C  CB    . PHE C 2 189 ? 111.461 98.235  119.284 1.00 27.03 ?  168 PHE C CB    1 
ATOM   12346 C  CG    . PHE C 2 189 ? 112.415 98.340  120.470 1.00 28.09 ?  168 PHE C CG    1 
ATOM   12347 C  CD1   . PHE C 2 189 ? 112.192 99.249  121.506 1.00 28.69 ?  168 PHE C CD1   1 
ATOM   12348 C  CD2   . PHE C 2 189 ? 113.578 97.579  120.505 1.00 29.15 ?  168 PHE C CD2   1 
ATOM   12349 C  CE1   . PHE C 2 189 ? 113.082 99.360  122.586 1.00 28.50 ?  168 PHE C CE1   1 
ATOM   12350 C  CE2   . PHE C 2 189 ? 114.482 97.678  121.579 1.00 30.19 ?  168 PHE C CE2   1 
ATOM   12351 C  CZ    . PHE C 2 189 ? 114.225 98.579  122.629 1.00 29.81 ?  168 PHE C CZ    1 
ATOM   12352 N  N     . TYR C 2 190 ? 108.599 97.749  117.657 1.00 26.18 ?  169 TYR C N     1 
ATOM   12353 C  CA    . TYR C 2 190 ? 108.052 98.290  116.418 1.00 26.24 ?  169 TYR C CA    1 
ATOM   12354 C  C     . TYR C 2 190 ? 106.646 98.904  116.500 1.00 25.94 ?  169 TYR C C     1 
ATOM   12355 O  O     . TYR C 2 190 ? 106.297 99.771  115.697 1.00 25.71 ?  169 TYR C O     1 
ATOM   12356 C  CB    . TYR C 2 190 ? 108.259 97.307  115.264 1.00 27.13 ?  169 TYR C CB    1 
ATOM   12357 C  CG    . TYR C 2 190 ? 109.705 97.350  114.818 1.00 28.07 ?  169 TYR C CG    1 
ATOM   12358 C  CD1   . TYR C 2 190 ? 110.683 96.590  115.470 1.00 29.54 ?  169 TYR C CD1   1 
ATOM   12359 C  CD2   . TYR C 2 190 ? 110.110 98.204  113.792 1.00 29.31 ?  169 TYR C CD2   1 
ATOM   12360 C  CE1   . TYR C 2 190 ? 112.024 96.653  115.081 1.00 30.44 ?  169 TYR C CE1   1 
ATOM   12361 C  CE2   . TYR C 2 190 ? 111.454 98.273  113.392 1.00 30.64 ?  169 TYR C CE2   1 
ATOM   12362 C  CZ    . TYR C 2 190 ? 112.403 97.498  114.046 1.00 30.40 ?  169 TYR C CZ    1 
ATOM   12363 O  OH    . TYR C 2 190 ? 113.723 97.569  113.665 1.00 28.85 ?  169 TYR C OH    1 
ATOM   12364 N  N     . SER C 2 191 ? 105.872 98.499  117.503 1.00 25.17 ?  170 SER C N     1 
ATOM   12365 C  CA    . SER C 2 191 ? 104.584 99.132  117.772 1.00 25.10 ?  170 SER C CA    1 
ATOM   12366 C  C     . SER C 2 191 ? 104.829 100.586 118.194 1.00 25.16 ?  170 SER C C     1 
ATOM   12367 O  O     . SER C 2 191 ? 103.991 101.460 117.947 1.00 25.30 ?  170 SER C O     1 
ATOM   12368 C  CB    . SER C 2 191 ? 103.810 98.366  118.846 1.00 24.56 ?  170 SER C CB    1 
ATOM   12369 O  OG    . SER C 2 191 ? 104.481 98.407  120.090 1.00 24.98 ?  170 SER C OG    1 
ATOM   12370 N  N     . GLY C 2 192 ? 105.990 100.814 118.819 1.00 24.32 ?  171 GLY C N     1 
ATOM   12371 C  CA    . GLY C 2 192 ? 106.462 102.135 119.210 1.00 23.97 ?  171 GLY C CA    1 
ATOM   12372 C  C     . GLY C 2 192 ? 107.104 102.915 118.075 1.00 23.85 ?  171 GLY C C     1 
ATOM   12373 O  O     . GLY C 2 192 ? 106.728 104.064 117.843 1.00 23.99 ?  171 GLY C O     1 
ATOM   12374 N  N     . PHE C 2 193 ? 108.046 102.295 117.362 1.00 23.28 ?  172 PHE C N     1 
ATOM   12375 C  CA    . PHE C 2 193 ? 108.743 102.945 116.237 1.00 23.85 ?  172 PHE C CA    1 
ATOM   12376 C  C     . PHE C 2 193 ? 107.817 103.448 115.129 1.00 23.72 ?  172 PHE C C     1 
ATOM   12377 O  O     . PHE C 2 193 ? 108.159 104.401 114.431 1.00 23.92 ?  172 PHE C O     1 
ATOM   12378 C  CB    . PHE C 2 193 ? 109.774 102.015 115.584 1.00 23.47 ?  172 PHE C CB    1 
ATOM   12379 C  CG    . PHE C 2 193 ? 111.029 101.799 116.401 1.00 24.32 ?  172 PHE C CG    1 
ATOM   12380 C  CD1   . PHE C 2 193 ? 111.442 102.731 117.354 1.00 22.28 ?  172 PHE C CD1   1 
ATOM   12381 C  CD2   . PHE C 2 193 ? 111.812 100.663 116.188 1.00 23.82 ?  172 PHE C CD2   1 
ATOM   12382 C  CE1   . PHE C 2 193 ? 112.605 102.529 118.109 1.00 23.41 ?  172 PHE C CE1   1 
ATOM   12383 C  CE2   . PHE C 2 193 ? 112.984 100.443 116.934 1.00 24.70 ?  172 PHE C CE2   1 
ATOM   12384 C  CZ    . PHE C 2 193 ? 113.384 101.384 117.896 1.00 24.87 ?  172 PHE C CZ    1 
ATOM   12385 N  N     . TYR C 2 194 ? 106.669 102.791 114.951 1.00 23.31 ?  173 TYR C N     1 
ATOM   12386 C  CA    . TYR C 2 194 ? 105.748 103.127 113.862 1.00 23.26 ?  173 TYR C CA    1 
ATOM   12387 C  C     . TYR C 2 194 ? 105.457 104.629 113.804 1.00 23.04 ?  173 TYR C C     1 
ATOM   12388 O  O     . TYR C 2 194 ? 105.509 105.240 112.733 1.00 23.47 ?  173 TYR C O     1 
ATOM   12389 C  CB    . TYR C 2 194 ? 104.422 102.355 113.973 1.00 23.13 ?  173 TYR C CB    1 
ATOM   12390 C  CG    . TYR C 2 194 ? 103.482 102.599 112.799 1.00 24.10 ?  173 TYR C CG    1 
ATOM   12391 C  CD1   . TYR C 2 194 ? 103.473 101.736 111.703 1.00 25.72 ?  173 TYR C CD1   1 
ATOM   12392 C  CD2   . TYR C 2 194 ? 102.627 103.701 112.775 1.00 27.04 ?  173 TYR C CD2   1 
ATOM   12393 C  CE1   . TYR C 2 194 ? 102.616 101.954 110.616 1.00 28.94 ?  173 TYR C CE1   1 
ATOM   12394 C  CE2   . TYR C 2 194 ? 101.770 103.936 111.683 1.00 27.84 ?  173 TYR C CE2   1 
ATOM   12395 C  CZ    . TYR C 2 194 ? 101.776 103.056 110.613 1.00 29.97 ?  173 TYR C CZ    1 
ATOM   12396 O  OH    . TYR C 2 194 ? 100.948 103.272 109.526 1.00 34.34 ?  173 TYR C OH    1 
ATOM   12397 N  N     . TYR C 2 195 ? 105.146 105.209 114.953 1.00 22.51 ?  174 TYR C N     1 
ATOM   12398 C  CA    . TYR C 2 195 ? 104.583 106.554 114.990 1.00 22.60 ?  174 TYR C CA    1 
ATOM   12399 C  C     . TYR C 2 195 ? 105.610 107.659 114.680 1.00 22.64 ?  174 TYR C C     1 
ATOM   12400 O  O     . TYR C 2 195 ? 105.317 108.530 113.853 1.00 22.39 ?  174 TYR C O     1 
ATOM   12401 C  CB    . TYR C 2 195 ? 103.838 106.785 116.305 1.00 22.32 ?  174 TYR C CB    1 
ATOM   12402 C  CG    . TYR C 2 195 ? 102.665 107.741 116.213 1.00 23.39 ?  174 TYR C CG    1 
ATOM   12403 C  CD1   . TYR C 2 195 ? 101.890 107.840 115.045 1.00 22.84 ?  174 TYR C CD1   1 
ATOM   12404 C  CD2   . TYR C 2 195 ? 102.305 108.519 117.311 1.00 22.23 ?  174 TYR C CD2   1 
ATOM   12405 C  CE1   . TYR C 2 195 ? 100.802 108.718 114.976 1.00 24.05 ?  174 TYR C CE1   1 
ATOM   12406 C  CE2   . TYR C 2 195 ? 101.213 109.387 117.257 1.00 24.11 ?  174 TYR C CE2   1 
ATOM   12407 C  CZ    . TYR C 2 195 ? 100.469 109.479 116.093 1.00 23.92 ?  174 TYR C CZ    1 
ATOM   12408 O  OH    . TYR C 2 195 ? 99.416  110.352 116.049 1.00 25.00 ?  174 TYR C OH    1 
ATOM   12409 N  N     . PRO C 2 196 ? 106.816 107.619 115.318 1.00 22.25 ?  175 PRO C N     1 
ATOM   12410 C  CA    . PRO C 2 196 ? 107.865 108.561 114.893 1.00 22.45 ?  175 PRO C CA    1 
ATOM   12411 C  C     . PRO C 2 196 ? 108.214 108.433 113.410 1.00 22.59 ?  175 PRO C C     1 
ATOM   12412 O  O     . PRO C 2 196 ? 108.456 109.453 112.755 1.00 22.19 ?  175 PRO C O     1 
ATOM   12413 C  CB    . PRO C 2 196 ? 109.078 108.184 115.757 1.00 22.25 ?  175 PRO C CB    1 
ATOM   12414 C  CG    . PRO C 2 196 ? 108.524 107.454 116.935 1.00 22.22 ?  175 PRO C CG    1 
ATOM   12415 C  CD    . PRO C 2 196 ? 107.252 106.791 116.467 1.00 22.32 ?  175 PRO C CD    1 
ATOM   12416 N  N     . LEU C 2 197 ? 108.230 107.202 112.888 1.00 21.92 ?  176 LEU C N     1 
ATOM   12417 C  CA    . LEU C 2 197 ? 108.508 106.977 111.468 1.00 22.35 ?  176 LEU C CA    1 
ATOM   12418 C  C     . LEU C 2 197 ? 107.384 107.528 110.584 1.00 22.60 ?  176 LEU C C     1 
ATOM   12419 O  O     . LEU C 2 197 ? 107.634 108.092 109.515 1.00 22.41 ?  176 LEU C O     1 
ATOM   12420 C  CB    . LEU C 2 197 ? 108.709 105.493 111.166 1.00 22.69 ?  176 LEU C CB    1 
ATOM   12421 C  CG    . LEU C 2 197 ? 109.893 104.729 111.773 1.00 23.68 ?  176 LEU C CG    1 
ATOM   12422 C  CD1   . LEU C 2 197 ? 109.834 103.257 111.332 1.00 23.70 ?  176 LEU C CD1   1 
ATOM   12423 C  CD2   . LEU C 2 197 ? 111.221 105.360 111.369 1.00 23.09 ?  176 LEU C CD2   1 
ATOM   12424 N  N     . TYR C 2 198 ? 106.147 107.357 111.047 1.00 22.64 ?  177 TYR C N     1 
ATOM   12425 C  CA    . TYR C 2 198 ? 104.966 107.823 110.334 1.00 22.92 ?  177 TYR C CA    1 
ATOM   12426 C  C     . TYR C 2 198 ? 105.019 109.355 110.187 1.00 23.68 ?  177 TYR C C     1 
ATOM   12427 O  O     . TYR C 2 198 ? 104.746 109.896 109.113 1.00 23.81 ?  177 TYR C O     1 
ATOM   12428 C  CB    . TYR C 2 198 ? 103.729 107.358 111.095 1.00 22.73 ?  177 TYR C CB    1 
ATOM   12429 C  CG    . TYR C 2 198 ? 102.389 107.773 110.552 1.00 22.91 ?  177 TYR C CG    1 
ATOM   12430 C  CD1   . TYR C 2 198 ? 101.857 107.161 109.417 1.00 23.49 ?  177 TYR C CD1   1 
ATOM   12431 C  CD2   . TYR C 2 198 ? 101.621 108.732 111.213 1.00 21.97 ?  177 TYR C CD2   1 
ATOM   12432 C  CE1   . TYR C 2 198 ? 100.601 107.519 108.926 1.00 23.57 ?  177 TYR C CE1   1 
ATOM   12433 C  CE2   . TYR C 2 198 ? 100.352 109.099 110.732 1.00 22.54 ?  177 TYR C CE2   1 
ATOM   12434 C  CZ    . TYR C 2 198 ? 99.856  108.491 109.589 1.00 22.88 ?  177 TYR C CZ    1 
ATOM   12435 O  OH    . TYR C 2 198 ? 98.606  108.828 109.103 1.00 23.17 ?  177 TYR C OH    1 
ATOM   12436 N  N     . PHE C 2 199 ? 105.416 110.045 111.250 1.00 23.50 ?  178 PHE C N     1 
ATOM   12437 C  CA    . PHE C 2 199 ? 105.591 111.497 111.177 1.00 24.60 ?  178 PHE C CA    1 
ATOM   12438 C  C     . PHE C 2 199 ? 106.796 111.945 110.340 1.00 24.72 ?  178 PHE C C     1 
ATOM   12439 O  O     . PHE C 2 199 ? 106.681 112.847 109.511 1.00 24.19 ?  178 PHE C O     1 
ATOM   12440 C  CB    . PHE C 2 199 ? 105.642 112.107 112.581 1.00 24.35 ?  178 PHE C CB    1 
ATOM   12441 C  CG    . PHE C 2 199 ? 104.300 112.192 113.243 1.00 26.36 ?  178 PHE C CG    1 
ATOM   12442 C  CD1   . PHE C 2 199 ? 103.191 112.667 112.545 1.00 28.53 ?  178 PHE C CD1   1 
ATOM   12443 C  CD2   . PHE C 2 199 ? 104.140 111.818 114.570 1.00 28.23 ?  178 PHE C CD2   1 
ATOM   12444 C  CE1   . PHE C 2 199 ? 101.936 112.744 113.158 1.00 29.37 ?  178 PHE C CE1   1 
ATOM   12445 C  CE2   . PHE C 2 199 ? 102.883 111.905 115.194 1.00 28.69 ?  178 PHE C CE2   1 
ATOM   12446 C  CZ    . PHE C 2 199 ? 101.791 112.363 114.489 1.00 28.43 ?  178 PHE C CZ    1 
ATOM   12447 N  N     . TYR C 2 200 ? 107.942 111.305 110.560 1.00 25.36 ?  179 TYR C N     1 
ATOM   12448 C  CA    . TYR C 2 200 ? 109.167 111.582 109.798 1.00 26.02 ?  179 TYR C CA    1 
ATOM   12449 C  C     . TYR C 2 200 ? 108.877 111.527 108.297 1.00 26.57 ?  179 TYR C C     1 
ATOM   12450 O  O     . TYR C 2 200 ? 109.293 112.406 107.536 1.00 26.30 ?  179 TYR C O     1 
ATOM   12451 C  CB    . TYR C 2 200 ? 110.251 110.555 110.154 1.00 26.19 ?  179 TYR C CB    1 
ATOM   12452 C  CG    . TYR C 2 200 ? 111.622 110.865 109.596 1.00 27.82 ?  179 TYR C CG    1 
ATOM   12453 C  CD1   . TYR C 2 200 ? 112.096 110.209 108.456 1.00 30.77 ?  179 TYR C CD1   1 
ATOM   12454 C  CD2   . TYR C 2 200 ? 112.452 111.805 110.212 1.00 29.20 ?  179 TYR C CD2   1 
ATOM   12455 C  CE1   . TYR C 2 200 ? 113.357 110.486 107.940 1.00 31.82 ?  179 TYR C CE1   1 
ATOM   12456 C  CE2   . TYR C 2 200 ? 113.712 112.093 109.706 1.00 30.44 ?  179 TYR C CE2   1 
ATOM   12457 C  CZ    . TYR C 2 200 ? 114.158 111.428 108.568 1.00 32.74 ?  179 TYR C CZ    1 
ATOM   12458 O  OH    . TYR C 2 200 ? 115.398 111.704 108.048 1.00 34.58 ?  179 TYR C OH    1 
ATOM   12459 N  N     . GLY C 2 201 ? 108.136 110.497 107.893 1.00 26.71 ?  180 GLY C N     1 
ATOM   12460 C  CA    . GLY C 2 201 ? 107.777 110.292 106.497 1.00 27.38 ?  180 GLY C CA    1 
ATOM   12461 C  C     . GLY C 2 201 ? 106.878 111.364 105.903 1.00 27.62 ?  180 GLY C C     1 
ATOM   12462 O  O     . GLY C 2 201 ? 106.791 111.474 104.692 1.00 28.25 ?  180 GLY C O     1 
ATOM   12463 N  N     . GLN C 2 202 ? 106.216 112.147 106.755 1.00 27.60 ?  181 GLN C N     1 
ATOM   12464 C  CA    . GLN C 2 202 ? 105.364 113.266 106.317 1.00 28.24 ?  181 GLN C CA    1 
ATOM   12465 C  C     . GLN C 2 202 ? 106.066 114.605 106.484 1.00 28.30 ?  181 GLN C C     1 
ATOM   12466 O  O     . GLN C 2 202 ? 105.446 115.653 106.286 1.00 27.98 ?  181 GLN C O     1 
ATOM   12467 C  CB    . GLN C 2 202 ? 104.080 113.340 107.147 1.00 27.90 ?  181 GLN C CB    1 
ATOM   12468 C  CG    . GLN C 2 202 ? 103.177 112.151 107.067 1.00 29.54 ?  181 GLN C CG    1 
ATOM   12469 C  CD    . GLN C 2 202 ? 102.009 112.277 108.018 1.00 31.54 ?  181 GLN C CD    1 
ATOM   12470 O  OE1   . GLN C 2 202 ? 101.115 113.104 107.819 1.00 32.11 ?  181 GLN C OE1   1 
ATOM   12471 N  NE2   . GLN C 2 202 ? 102.010 111.464 109.067 1.00 31.29 ?  181 GLN C NE2   1 
ATOM   12472 N  N     . GLY C 2 203 ? 107.333 114.566 106.894 1.00 28.14 ?  182 GLY C N     1 
ATOM   12473 C  CA    . GLY C 2 203 ? 108.113 115.769 107.141 1.00 28.38 ?  182 GLY C CA    1 
ATOM   12474 C  C     . GLY C 2 203 ? 107.757 116.449 108.446 1.00 28.71 ?  182 GLY C C     1 
ATOM   12475 O  O     . GLY C 2 203 ? 107.862 117.667 108.557 1.00 28.80 ?  182 GLY C O     1 
ATOM   12476 N  N     . LYS C 2 204 ? 107.322 115.660 109.428 1.00 28.24 ?  183 LYS C N     1 
ATOM   12477 C  CA    . LYS C 2 204 ? 106.930 116.183 110.727 1.00 28.48 ?  183 LYS C CA    1 
ATOM   12478 C  C     . LYS C 2 204 ? 107.773 115.550 111.829 1.00 27.82 ?  183 LYS C C     1 
ATOM   12479 O  O     . LYS C 2 204 ? 108.117 114.361 111.758 1.00 26.73 ?  183 LYS C O     1 
ATOM   12480 C  CB    . LYS C 2 204 ? 105.445 115.933 110.991 1.00 29.13 ?  183 LYS C CB    1 
ATOM   12481 C  CG    . LYS C 2 204 ? 104.506 116.685 110.047 1.00 30.41 ?  183 LYS C CG    1 
ATOM   12482 C  CD    . LYS C 2 204 ? 103.149 116.002 109.973 1.00 33.74 ?  183 LYS C CD    1 
ATOM   12483 C  CE    . LYS C 2 204 ? 102.177 116.799 109.088 1.00 36.26 ?  183 LYS C CE    1 
ATOM   12484 N  NZ    . LYS C 2 204 ? 100.841 116.137 109.050 1.00 39.17 1  183 LYS C NZ    1 
ATOM   12485 N  N     . LEU C 2 205 ? 108.096 116.352 112.842 1.00 27.77 ?  184 LEU C N     1 
ATOM   12486 C  CA    . LEU C 2 205 ? 108.925 115.915 113.973 1.00 27.79 ?  184 LEU C CA    1 
ATOM   12487 C  C     . LEU C 2 205 ? 110.214 115.240 113.496 1.00 27.85 ?  184 LEU C C     1 
ATOM   12488 O  O     . LEU C 2 205 ? 110.572 114.134 113.923 1.00 27.07 ?  184 LEU C O     1 
ATOM   12489 C  CB    . LEU C 2 205 ? 108.122 114.998 114.918 1.00 27.76 ?  184 LEU C CB    1 
ATOM   12490 C  CG    . LEU C 2 205 ? 106.820 115.589 115.473 1.00 28.62 ?  184 LEU C CG    1 
ATOM   12491 C  CD1   . LEU C 2 205 ? 106.055 114.558 116.279 1.00 29.18 ?  184 LEU C CD1   1 
ATOM   12492 C  CD2   . LEU C 2 205 ? 107.091 116.825 116.320 1.00 28.43 ?  184 LEU C CD2   1 
ATOM   12493 N  N     . MET C 2 206 ? 110.926 115.924 112.612 1.00 28.15 ?  185 MET C N     1 
ATOM   12494 C  CA    . MET C 2 206 ? 112.030 115.289 111.931 1.00 28.80 ?  185 MET C CA    1 
ATOM   12495 C  C     . MET C 2 206 ? 113.308 115.168 112.751 1.00 28.77 ?  185 MET C C     1 
ATOM   12496 O  O     . MET C 2 206 ? 114.121 114.287 112.482 1.00 28.79 ?  185 MET C O     1 
ATOM   12497 C  CB    . MET C 2 206 ? 112.263 115.956 110.588 1.00 29.96 ?  185 MET C CB    1 
ATOM   12498 C  CG    . MET C 2 206 ? 111.096 115.696 109.631 1.00 31.23 ?  185 MET C CG    1 
ATOM   12499 S  SD    . MET C 2 206 ? 111.588 116.012 107.957 1.00 40.10 ?  185 MET C SD    1 
ATOM   12500 C  CE    . MET C 2 206 ? 112.653 114.624 107.618 1.00 35.10 ?  185 MET C CE    1 
ATOM   12501 N  N     . GLN C 2 207 ? 113.474 116.019 113.758 1.00 28.62 ?  186 GLN C N     1 
ATOM   12502 C  CA    . GLN C 2 207 ? 114.648 115.932 114.632 1.00 29.10 ?  186 GLN C CA    1 
ATOM   12503 C  C     . GLN C 2 207 ? 114.516 114.754 115.602 1.00 28.52 ?  186 GLN C C     1 
ATOM   12504 O  O     . GLN C 2 207 ? 115.443 113.956 115.725 1.00 28.28 ?  186 GLN C O     1 
ATOM   12505 C  CB    . GLN C 2 207 ? 114.901 117.243 115.383 1.00 29.21 ?  186 GLN C CB    1 
ATOM   12506 C  CG    . GLN C 2 207 ? 115.234 118.429 114.475 1.00 31.41 ?  186 GLN C CG    1 
ATOM   12507 C  CD    . GLN C 2 207 ? 116.540 118.241 113.730 1.00 34.70 ?  186 GLN C CD    1 
ATOM   12508 O  OE1   . GLN C 2 207 ? 116.558 117.730 112.613 1.00 37.69 ?  186 GLN C OE1   1 
ATOM   12509 N  NE2   . GLN C 2 207 ? 117.645 118.627 114.357 1.00 34.75 ?  186 GLN C NE2   1 
ATOM   12510 N  N     . SER C 2 208 ? 113.361 114.656 116.272 1.00 28.38 ?  187 SER C N     1 
ATOM   12511 C  CA    . SER C 2 208 ? 113.001 113.481 117.076 1.00 28.25 ?  187 SER C CA    1 
ATOM   12512 C  C     . SER C 2 208 ? 113.088 112.225 116.216 1.00 28.00 ?  187 SER C C     1 
ATOM   12513 O  O     . SER C 2 208 ? 113.584 111.193 116.669 1.00 27.90 ?  187 SER C O     1 
ATOM   12514 C  CB    . SER C 2 208 ? 111.570 113.599 117.603 1.00 27.88 ?  187 SER C CB    1 
ATOM   12515 O  OG    . SER C 2 208 ? 111.415 114.716 118.452 1.00 30.27 ?  187 SER C OG    1 
ATOM   12516 N  N     . GLY C 2 209 ? 112.587 112.330 114.981 1.00 27.31 ?  188 GLY C N     1 
ATOM   12517 C  CA    . GLY C 2 209 ? 112.612 111.230 114.020 1.00 27.86 ?  188 GLY C CA    1 
ATOM   12518 C  C     . GLY C 2 209 ? 114.013 110.776 113.658 1.00 27.96 ?  188 GLY C C     1 
ATOM   12519 O  O     . GLY C 2 209 ? 114.249 109.580 113.445 1.00 27.84 ?  188 GLY C O     1 
ATOM   12520 N  N     . GLU C 2 210 ? 114.943 111.729 113.583 1.00 28.21 ?  189 GLU C N     1 
ATOM   12521 C  CA    . GLU C 2 210 ? 116.347 111.422 113.327 1.00 29.15 ?  189 GLU C CA    1 
ATOM   12522 C  C     . GLU C 2 210 ? 116.943 110.582 114.474 1.00 28.02 ?  189 GLU C C     1 
ATOM   12523 O  O     . GLU C 2 210 ? 117.665 109.610 114.242 1.00 27.15 ?  189 GLU C O     1 
ATOM   12524 C  CB    . GLU C 2 210 ? 117.140 112.717 113.129 1.00 30.17 ?  189 GLU C CB    1 
ATOM   12525 C  CG    . GLU C 2 210 ? 118.006 112.736 111.880 1.00 35.68 ?  189 GLU C CG    1 
ATOM   12526 C  CD    . GLU C 2 210 ? 117.208 113.017 110.604 1.00 40.25 ?  189 GLU C CD    1 
ATOM   12527 O  OE1   . GLU C 2 210 ? 116.603 114.108 110.474 1.00 42.98 ?  189 GLU C OE1   1 
ATOM   12528 O  OE2   . GLU C 2 210 ? 117.193 112.145 109.715 1.00 43.59 -1 189 GLU C OE2   1 
ATOM   12529 N  N     . ILE C 2 211 ? 116.631 110.963 115.711 1.00 27.57 ?  190 ILE C N     1 
ATOM   12530 C  CA    . ILE C 2 211 ? 117.032 110.181 116.885 1.00 27.47 ?  190 ILE C CA    1 
ATOM   12531 C  C     . ILE C 2 211 ? 116.493 108.748 116.811 1.00 26.69 ?  190 ILE C C     1 
ATOM   12532 O  O     . ILE C 2 211 ? 117.239 107.772 116.963 1.00 26.56 ?  190 ILE C O     1 
ATOM   12533 C  CB    . ILE C 2 211 ? 116.596 110.882 118.206 1.00 27.84 ?  190 ILE C CB    1 
ATOM   12534 C  CG1   . ILE C 2 211 ? 117.452 112.138 118.433 1.00 28.56 ?  190 ILE C CG1   1 
ATOM   12535 C  CG2   . ILE C 2 211 ? 116.680 109.903 119.400 1.00 27.27 ?  190 ILE C CG2   1 
ATOM   12536 C  CD1   . ILE C 2 211 ? 117.151 112.884 119.728 1.00 30.09 ?  190 ILE C CD1   1 
ATOM   12537 N  N     . ILE C 2 212 ? 115.200 108.630 116.534 1.00 26.33 ?  191 ILE C N     1 
ATOM   12538 C  CA    . ILE C 2 212 ? 114.534 107.335 116.442 1.00 25.96 ?  191 ILE C CA    1 
ATOM   12539 C  C     . ILE C 2 212 ? 115.150 106.442 115.355 1.00 25.46 ?  191 ILE C C     1 
ATOM   12540 O  O     . ILE C 2 212 ? 115.321 105.245 115.574 1.00 24.84 ?  191 ILE C O     1 
ATOM   12541 C  CB    . ILE C 2 212 ? 112.995 107.500 116.250 1.00 26.00 ?  191 ILE C CB    1 
ATOM   12542 C  CG1   . ILE C 2 212 ? 112.364 108.151 117.492 1.00 27.16 ?  191 ILE C CG1   1 
ATOM   12543 C  CG2   . ILE C 2 212 ? 112.315 106.173 115.940 1.00 26.87 ?  191 ILE C CG2   1 
ATOM   12544 C  CD1   . ILE C 2 212 ? 112.468 107.335 118.767 1.00 29.84 ?  191 ILE C CD1   1 
ATOM   12545 N  N     . ASN C 2 213 ? 115.481 107.021 114.198 1.00 25.35 ?  192 ASN C N     1 
ATOM   12546 C  CA    . ASN C 2 213 ? 116.144 106.275 113.123 1.00 25.60 ?  192 ASN C CA    1 
ATOM   12547 C  C     . ASN C 2 213 ? 117.515 105.747 113.532 1.00 25.14 ?  192 ASN C C     1 
ATOM   12548 O  O     . ASN C 2 213 ? 117.913 104.638 113.143 1.00 25.61 ?  192 ASN C O     1 
ATOM   12549 C  CB    . ASN C 2 213 ? 116.273 107.119 111.848 1.00 26.55 ?  192 ASN C CB    1 
ATOM   12550 C  CG    . ASN C 2 213 ? 115.048 107.029 110.966 1.00 28.10 ?  192 ASN C CG    1 
ATOM   12551 O  OD1   . ASN C 2 213 ? 114.702 105.956 110.461 1.00 31.67 ?  192 ASN C OD1   1 
ATOM   12552 N  ND2   . ASN C 2 213 ? 114.389 108.156 110.764 1.00 30.36 ?  192 ASN C ND2   1 
ATOM   12553 N  N     . LEU C 2 214 ? 118.236 106.536 114.320 1.00 24.54 ?  193 LEU C N     1 
ATOM   12554 C  CA    . LEU C 2 214 ? 119.524 106.087 114.855 1.00 24.40 ?  193 LEU C CA    1 
ATOM   12555 C  C     . LEU C 2 214 ? 119.338 104.928 115.836 1.00 23.55 ?  193 LEU C C     1 
ATOM   12556 O  O     . LEU C 2 214 ? 120.068 103.935 115.770 1.00 23.09 ?  193 LEU C O     1 
ATOM   12557 C  CB    . LEU C 2 214 ? 120.295 107.248 115.476 1.00 24.00 ?  193 LEU C CB    1 
ATOM   12558 C  CG    . LEU C 2 214 ? 120.876 108.272 114.476 1.00 25.69 ?  193 LEU C CG    1 
ATOM   12559 C  CD1   . LEU C 2 214 ? 121.369 109.534 115.185 1.00 26.28 ?  193 LEU C CD1   1 
ATOM   12560 C  CD2   . LEU C 2 214 ? 122.013 107.674 113.644 1.00 26.05 ?  193 LEU C CD2   1 
ATOM   12561 N  N     . ILE C 2 215 ? 118.354 105.051 116.730 1.00 23.19 ?  194 ILE C N     1 
ATOM   12562 C  CA    . ILE C 2 215 ? 117.984 103.964 117.643 1.00 22.88 ?  194 ILE C CA    1 
ATOM   12563 C  C     . ILE C 2 215 ? 117.613 102.712 116.831 1.00 23.81 ?  194 ILE C C     1 
ATOM   12564 O  O     . ILE C 2 215 ? 118.105 101.619 117.113 1.00 23.83 ?  194 ILE C O     1 
ATOM   12565 C  CB    . ILE C 2 215 ? 116.822 104.368 118.594 1.00 22.92 ?  194 ILE C CB    1 
ATOM   12566 C  CG1   . ILE C 2 215 ? 117.229 105.556 119.469 1.00 21.11 ?  194 ILE C CG1   1 
ATOM   12567 C  CG2   . ILE C 2 215 ? 116.363 103.186 119.463 1.00 21.89 ?  194 ILE C CG2   1 
ATOM   12568 C  CD1   . ILE C 2 215 ? 116.144 106.035 120.412 1.00 22.26 ?  194 ILE C CD1   1 
ATOM   12569 N  N     . LEU C 2 216 ? 116.785 102.878 115.800 1.00 24.23 ?  195 LEU C N     1 
ATOM   12570 C  CA    . LEU C 2 216 ? 116.329 101.738 114.995 1.00 25.41 ?  195 LEU C CA    1 
ATOM   12571 C  C     . LEU C 2 216 ? 117.486 101.056 114.263 1.00 25.63 ?  195 LEU C C     1 
ATOM   12572 O  O     . LEU C 2 216 ? 117.560 99.819  114.216 1.00 25.46 ?  195 LEU C O     1 
ATOM   12573 C  CB    . LEU C 2 216 ? 115.229 102.170 114.006 1.00 26.03 ?  195 LEU C CB    1 
ATOM   12574 C  CG    . LEU C 2 216 ? 114.554 101.141 113.089 1.00 28.00 ?  195 LEU C CG    1 
ATOM   12575 C  CD1   . LEU C 2 216 ? 113.212 101.691 112.636 1.00 31.45 ?  195 LEU C CD1   1 
ATOM   12576 C  CD2   . LEU C 2 216 ? 115.423 100.776 111.879 1.00 29.83 ?  195 LEU C CD2   1 
ATOM   12577 N  N     . ARG C 2 217 ? 118.382 101.863 113.703 1.00 25.98 ?  196 ARG C N     1 
ATOM   12578 C  CA    . ARG C 2 217 ? 119.591 101.359 113.058 1.00 26.73 ?  196 ARG C CA    1 
ATOM   12579 C  C     . ARG C 2 217 ? 120.408 100.473 114.032 1.00 25.95 ?  196 ARG C C     1 
ATOM   12580 O  O     . ARG C 2 217 ? 120.868 99.396  113.637 1.00 25.75 ?  196 ARG C O     1 
ATOM   12581 C  CB    . ARG C 2 217 ? 120.433 102.528 112.539 1.00 27.29 ?  196 ARG C CB    1 
ATOM   12582 C  CG    . ARG C 2 217 ? 121.589 102.148 111.603 1.00 30.12 ?  196 ARG C CG    1 
ATOM   12583 C  CD    . ARG C 2 217 ? 122.720 103.147 111.764 1.00 35.40 ?  196 ARG C CD    1 
ATOM   12584 N  NE    . ARG C 2 217 ? 122.932 103.385 113.192 1.00 39.87 ?  196 ARG C NE    1 
ATOM   12585 C  CZ    . ARG C 2 217 ? 123.670 104.352 113.722 1.00 40.55 ?  196 ARG C CZ    1 
ATOM   12586 N  NH1   . ARG C 2 217 ? 124.319 105.223 112.950 1.00 40.77 1  196 ARG C NH1   1 
ATOM   12587 N  NH2   . ARG C 2 217 ? 123.748 104.440 115.044 1.00 41.10 ?  196 ARG C NH2   1 
ATOM   12588 N  N     . ASP C 2 218 ? 120.565 100.922 115.283 1.00 24.70 ?  197 ASP C N     1 
ATOM   12589 C  CA    . ASP C 2 218 ? 121.222 100.124 116.337 1.00 24.55 ?  197 ASP C CA    1 
ATOM   12590 C  C     . ASP C 2 218 ? 120.462 98.813  116.627 1.00 24.23 ?  197 ASP C C     1 
ATOM   12591 O  O     . ASP C 2 218 ? 121.067 97.737  116.628 1.00 23.69 ?  197 ASP C O     1 
ATOM   12592 C  CB    . ASP C 2 218 ? 121.390 100.906 117.656 1.00 24.50 ?  197 ASP C CB    1 
ATOM   12593 C  CG    . ASP C 2 218 ? 122.369 102.090 117.556 1.00 25.84 ?  197 ASP C CG    1 
ATOM   12594 O  OD1   . ASP C 2 218 ? 123.269 102.104 116.686 1.00 26.91 ?  197 ASP C OD1   1 
ATOM   12595 O  OD2   . ASP C 2 218 ? 122.245 103.014 118.383 1.00 25.72 -1 197 ASP C OD2   1 
ATOM   12596 N  N     . GLU C 2 219 ? 119.146 98.896  116.846 1.00 23.92 ?  198 GLU C N     1 
ATOM   12597 C  CA    . GLU C 2 219 ? 118.391 97.693  117.236 1.00 24.20 ?  198 GLU C CA    1 
ATOM   12598 C  C     . GLU C 2 219 ? 118.426 96.633  116.151 1.00 24.02 ?  198 GLU C C     1 
ATOM   12599 O  O     . GLU C 2 219 ? 118.461 95.449  116.465 1.00 24.24 ?  198 GLU C O     1 
ATOM   12600 C  CB    . GLU C 2 219 ? 116.936 97.981  117.616 1.00 24.05 ?  198 GLU C CB    1 
ATOM   12601 C  CG    . GLU C 2 219 ? 116.669 99.244  118.415 1.00 25.03 ?  198 GLU C CG    1 
ATOM   12602 C  CD    . GLU C 2 219 ? 117.143 99.238  119.881 1.00 26.31 ?  198 GLU C CD    1 
ATOM   12603 O  OE1   . GLU C 2 219 ? 118.083 98.487  120.277 1.00 27.65 ?  198 GLU C OE1   1 
ATOM   12604 O  OE2   . GLU C 2 219 ? 116.559 100.051 120.649 1.00 26.87 -1 198 GLU C OE2   1 
ATOM   12605 N  N     . ALA C 2 220 ? 118.416 97.054  114.884 1.00 24.00 ?  199 ALA C N     1 
ATOM   12606 C  CA    . ALA C 2 220 ? 118.495 96.114  113.772 1.00 24.72 ?  199 ALA C CA    1 
ATOM   12607 C  C     . ALA C 2 220 ? 119.760 95.242  113.843 1.00 24.80 ?  199 ALA C C     1 
ATOM   12608 O  O     . ALA C 2 220 ? 119.682 94.022  113.672 1.00 25.04 ?  199 ALA C O     1 
ATOM   12609 C  CB    . ALA C 2 220 ? 118.400 96.843  112.408 1.00 24.66 ?  199 ALA C CB    1 
ATOM   12610 N  N     . ILE C 2 221 ? 120.909 95.861  114.105 1.00 24.85 ?  200 ILE C N     1 
ATOM   12611 C  CA    . ILE C 2 221 ? 122.165 95.101  114.242 1.00 25.07 ?  200 ILE C CA    1 
ATOM   12612 C  C     . ILE C 2 221 ? 122.231 94.314  115.559 1.00 23.86 ?  200 ILE C C     1 
ATOM   12613 O  O     . ILE C 2 221 ? 122.806 93.222  115.593 1.00 23.72 ?  200 ILE C O     1 
ATOM   12614 C  CB    . ILE C 2 221 ? 123.461 95.961  114.016 1.00 25.71 ?  200 ILE C CB    1 
ATOM   12615 C  CG1   . ILE C 2 221 ? 123.734 96.899  115.196 1.00 27.10 ?  200 ILE C CG1   1 
ATOM   12616 C  CG2   . ILE C 2 221 ? 123.395 96.707  112.668 1.00 27.18 ?  200 ILE C CG2   1 
ATOM   12617 C  CD1   . ILE C 2 221 ? 125.080 97.632  115.144 1.00 29.63 ?  200 ILE C CD1   1 
ATOM   12618 N  N     . HIS C 2 222 ? 121.635 94.853  116.623 1.00 22.79 ?  201 HIS C N     1 
ATOM   12619 C  CA    . HIS C 2 222 ? 121.536 94.124  117.908 1.00 22.48 ?  201 HIS C CA    1 
ATOM   12620 C  C     . HIS C 2 222 ? 120.725 92.839  117.756 1.00 22.04 ?  201 HIS C C     1 
ATOM   12621 O  O     . HIS C 2 222 ? 121.107 91.805  118.291 1.00 22.06 ?  201 HIS C O     1 
ATOM   12622 C  CB    . HIS C 2 222 ? 120.856 94.958  118.995 1.00 21.77 ?  201 HIS C CB    1 
ATOM   12623 C  CG    . HIS C 2 222 ? 121.619 96.168  119.421 1.00 21.76 ?  201 HIS C CG    1 
ATOM   12624 N  ND1   . HIS C 2 222 ? 121.201 96.970  120.460 1.00 20.70 ?  201 HIS C ND1   1 
ATOM   12625 C  CD2   . HIS C 2 222 ? 122.769 96.715  118.963 1.00 22.07 ?  201 HIS C CD2   1 
ATOM   12626 C  CE1   . HIS C 2 222 ? 122.053 97.965  120.617 1.00 22.26 ?  201 HIS C CE1   1 
ATOM   12627 N  NE2   . HIS C 2 222 ? 123.008 97.838  119.717 1.00 22.52 ?  201 HIS C NE2   1 
ATOM   12628 N  N     . GLY C 2 223 ? 119.589 92.926  117.062 1.00 22.35 ?  202 GLY C N     1 
ATOM   12629 C  CA    . GLY C 2 223 ? 118.727 91.764  116.794 1.00 22.01 ?  202 GLY C CA    1 
ATOM   12630 C  C     . GLY C 2 223 ? 119.400 90.694  115.938 1.00 22.73 ?  202 GLY C C     1 
ATOM   12631 O  O     . GLY C 2 223 ? 119.244 89.488  116.193 1.00 21.99 ?  202 GLY C O     1 
ATOM   12632 N  N     . VAL C 2 224 ? 120.155 91.126  114.925 1.00 22.45 ?  203 VAL C N     1 
ATOM   12633 C  CA    . VAL C 2 224 ? 120.909 90.185  114.094 1.00 22.54 ?  203 VAL C CA    1 
ATOM   12634 C  C     . VAL C 2 224 ? 121.980 89.469  114.921 1.00 22.28 ?  203 VAL C C     1 
ATOM   12635 O  O     . VAL C 2 224 ? 122.063 88.243  114.901 1.00 22.44 ?  203 VAL C O     1 
ATOM   12636 C  CB    . VAL C 2 224 ? 121.558 90.868  112.842 1.00 23.00 ?  203 VAL C CB    1 
ATOM   12637 C  CG1   . VAL C 2 224 ? 122.512 89.895  112.127 1.00 23.10 ?  203 VAL C CG1   1 
ATOM   12638 C  CG2   . VAL C 2 224 ? 120.470 91.367  111.853 1.00 23.14 ?  203 VAL C CG2   1 
ATOM   12639 N  N     . TYR C 2 225 ? 122.768 90.237  115.670 1.00 22.41 ?  204 TYR C N     1 
ATOM   12640 C  CA    . TYR C 2 225 ? 123.854 89.676  116.472 1.00 22.03 ?  204 TYR C CA    1 
ATOM   12641 C  C     . TYR C 2 225 ? 123.365 88.654  117.498 1.00 21.66 ?  204 TYR C C     1 
ATOM   12642 O  O     . TYR C 2 225 ? 123.858 87.518  117.532 1.00 21.72 ?  204 TYR C O     1 
ATOM   12643 C  CB    . TYR C 2 225 ? 124.680 90.776  117.157 1.00 22.22 ?  204 TYR C CB    1 
ATOM   12644 C  CG    . TYR C 2 225 ? 125.938 90.239  117.809 1.00 21.92 ?  204 TYR C CG    1 
ATOM   12645 C  CD1   . TYR C 2 225 ? 126.990 89.748  117.034 1.00 22.36 ?  204 TYR C CD1   1 
ATOM   12646 C  CD2   . TYR C 2 225 ? 126.069 90.213  119.198 1.00 21.43 ?  204 TYR C CD2   1 
ATOM   12647 C  CE1   . TYR C 2 225 ? 128.143 89.237  117.629 1.00 23.82 ?  204 TYR C CE1   1 
ATOM   12648 C  CE2   . TYR C 2 225 ? 127.223 89.711  119.809 1.00 21.49 ?  204 TYR C CE2   1 
ATOM   12649 C  CZ    . TYR C 2 225 ? 128.249 89.229  119.019 1.00 23.58 ?  204 TYR C CZ    1 
ATOM   12650 O  OH    . TYR C 2 225 ? 129.379 88.737  119.615 1.00 25.42 ?  204 TYR C OH    1 
ATOM   12651 N  N     . VAL C 2 226 ? 122.396 89.049  118.327 1.00 20.95 ?  205 VAL C N     1 
ATOM   12652 C  CA    . VAL C 2 226 ? 121.823 88.126  119.315 1.00 20.49 ?  205 VAL C CA    1 
ATOM   12653 C  C     . VAL C 2 226 ? 121.180 86.911  118.622 1.00 20.84 ?  205 VAL C C     1 
ATOM   12654 O  O     . VAL C 2 226 ? 121.320 85.771  119.086 1.00 21.10 ?  205 VAL C O     1 
ATOM   12655 C  CB    . VAL C 2 226 ? 120.854 88.836  120.300 1.00 20.57 ?  205 VAL C CB    1 
ATOM   12656 C  CG1   . VAL C 2 226 ? 120.249 87.830  121.280 1.00 20.35 ?  205 VAL C CG1   1 
ATOM   12657 C  CG2   . VAL C 2 226 ? 121.607 89.930  121.071 1.00 19.60 ?  205 VAL C CG2   1 
ATOM   12658 N  N     . GLY C 2 227 ? 120.525 87.148  117.490 1.00 21.08 ?  206 GLY C N     1 
ATOM   12659 C  CA    . GLY C 2 227 ? 120.003 86.051  116.660 1.00 21.43 ?  206 GLY C CA    1 
ATOM   12660 C  C     . GLY C 2 227 ? 121.053 85.022  116.264 1.00 21.95 ?  206 GLY C C     1 
ATOM   12661 O  O     . GLY C 2 227 ? 120.807 83.805  116.330 1.00 21.84 ?  206 GLY C O     1 
ATOM   12662 N  N     . LEU C 2 228 ? 122.230 85.497  115.856 1.00 22.09 ?  207 LEU C N     1 
ATOM   12663 C  CA    . LEU C 2 228 ? 123.322 84.589  115.491 1.00 22.96 ?  207 LEU C CA    1 
ATOM   12664 C  C     . LEU C 2 228 ? 123.819 83.764  116.688 1.00 22.60 ?  207 LEU C C     1 
ATOM   12665 O  O     . LEU C 2 228 ? 124.108 82.572  116.548 1.00 22.04 ?  207 LEU C O     1 
ATOM   12666 C  CB    . LEU C 2 228 ? 124.473 85.338  114.807 1.00 23.39 ?  207 LEU C CB    1 
ATOM   12667 C  CG    . LEU C 2 228 ? 124.198 85.963  113.427 1.00 24.35 ?  207 LEU C CG    1 
ATOM   12668 C  CD1   . LEU C 2 228 ? 125.275 87.006  113.099 1.00 25.01 ?  207 LEU C CD1   1 
ATOM   12669 C  CD2   . LEU C 2 228 ? 124.121 84.917  112.320 1.00 25.11 ?  207 LEU C CD2   1 
ATOM   12670 N  N     . LEU C 2 229 ? 123.889 84.384  117.864 1.00 22.37 ?  208 LEU C N     1 
ATOM   12671 C  CA    . LEU C 2 229 ? 124.259 83.651  119.090 1.00 22.62 ?  208 LEU C CA    1 
ATOM   12672 C  C     . LEU C 2 229 ? 123.225 82.585  119.469 1.00 22.77 ?  208 LEU C C     1 
ATOM   12673 O  O     . LEU C 2 229 ? 123.587 81.464  119.867 1.00 22.57 ?  208 LEU C O     1 
ATOM   12674 C  CB    . LEU C 2 229 ? 124.516 84.610  120.256 1.00 22.44 ?  208 LEU C CB    1 
ATOM   12675 C  CG    . LEU C 2 229 ? 125.599 85.675  120.026 1.00 23.54 ?  208 LEU C CG    1 
ATOM   12676 C  CD1   . LEU C 2 229 ? 125.683 86.622  121.220 1.00 23.37 ?  208 LEU C CD1   1 
ATOM   12677 C  CD2   . LEU C 2 229 ? 126.970 85.038  119.735 1.00 23.91 ?  208 LEU C CD2   1 
ATOM   12678 N  N     . ALA C 2 230 ? 121.945 82.931  119.334 1.00 22.42 ?  209 ALA C N     1 
ATOM   12679 C  CA    . ALA C 2 230 ? 120.858 81.983  119.575 1.00 22.02 ?  209 ALA C CA    1 
ATOM   12680 C  C     . ALA C 2 230 ? 120.943 80.783  118.626 1.00 22.58 ?  209 ALA C C     1 
ATOM   12681 O  O     . ALA C 2 230 ? 120.815 79.644  119.056 1.00 22.14 ?  209 ALA C O     1 
ATOM   12682 C  CB    . ALA C 2 230 ? 119.518 82.668  119.440 1.00 22.04 ?  209 ALA C CB    1 
ATOM   12683 N  N     . GLN C 2 231 ? 121.178 81.052  117.344 1.00 22.96 ?  210 GLN C N     1 
ATOM   12684 C  CA    . GLN C 2 231 ? 121.340 79.978  116.347 1.00 24.30 ?  210 GLN C CA    1 
ATOM   12685 C  C     . GLN C 2 231 ? 122.494 79.042  116.658 1.00 25.11 ?  210 GLN C C     1 
ATOM   12686 O  O     . GLN C 2 231 ? 122.405 77.838  116.395 1.00 24.97 ?  210 GLN C O     1 
ATOM   12687 C  CB    . GLN C 2 231 ? 121.508 80.558  114.947 1.00 24.38 ?  210 GLN C CB    1 
ATOM   12688 C  CG    . GLN C 2 231 ? 120.231 81.235  114.420 1.00 25.12 ?  210 GLN C CG    1 
ATOM   12689 C  CD    . GLN C 2 231 ? 120.414 81.804  113.029 1.00 28.08 ?  210 GLN C CD    1 
ATOM   12690 O  OE1   . GLN C 2 231 ? 120.807 81.090  112.106 1.00 27.83 ?  210 GLN C OE1   1 
ATOM   12691 N  NE2   . GLN C 2 231 ? 120.146 83.102  112.873 1.00 26.38 ?  210 GLN C NE2   1 
ATOM   12692 N  N     . GLU C 2 232 ? 123.578 79.591  117.212 1.00 25.80 ?  211 GLU C N     1 
ATOM   12693 C  CA    . GLU C 2 232 ? 124.710 78.766  117.646 1.00 27.16 ?  211 GLU C CA    1 
ATOM   12694 C  C     . GLU C 2 232 ? 124.264 77.698  118.639 1.00 26.47 ?  211 GLU C C     1 
ATOM   12695 O  O     . GLU C 2 232 ? 124.654 76.530  118.528 1.00 26.10 ?  211 GLU C O     1 
ATOM   12696 C  CB    . GLU C 2 232 ? 125.779 79.617  118.320 1.00 27.59 ?  211 GLU C CB    1 
ATOM   12697 C  CG    . GLU C 2 232 ? 126.833 80.150  117.398 1.00 32.55 ?  211 GLU C CG    1 
ATOM   12698 C  CD    . GLU C 2 232 ? 128.187 80.276  118.086 1.00 36.72 ?  211 GLU C CD    1 
ATOM   12699 O  OE1   . GLU C 2 232 ? 128.276 80.034  119.313 1.00 38.32 ?  211 GLU C OE1   1 
ATOM   12700 O  OE2   . GLU C 2 232 ? 129.165 80.613  117.389 1.00 40.62 -1 211 GLU C OE2   1 
ATOM   12701 N  N     . ILE C 2 233 ? 123.461 78.110  119.619 1.00 25.55 ?  212 ILE C N     1 
ATOM   12702 C  CA    . ILE C 2 233 ? 122.991 77.195  120.659 1.00 25.32 ?  212 ILE C CA    1 
ATOM   12703 C  C     . ILE C 2 233 ? 121.991 76.189  120.101 1.00 25.48 ?  212 ILE C C     1 
ATOM   12704 O  O     . ILE C 2 233 ? 122.117 74.985  120.336 1.00 25.82 ?  212 ILE C O     1 
ATOM   12705 C  CB    . ILE C 2 233 ? 122.392 77.949  121.867 1.00 25.39 ?  212 ILE C CB    1 
ATOM   12706 C  CG1   . ILE C 2 233 ? 123.498 78.725  122.586 1.00 24.37 ?  212 ILE C CG1   1 
ATOM   12707 C  CG2   . ILE C 2 233 ? 121.688 76.972  122.815 1.00 24.86 ?  212 ILE C CG2   1 
ATOM   12708 C  CD1   . ILE C 2 233 ? 122.978 79.808  123.518 1.00 25.10 ?  212 ILE C CD1   1 
ATOM   12709 N  N     . TYR C 2 234 ? 121.018 76.686  119.343 1.00 25.27 ?  213 TYR C N     1 
ATOM   12710 C  CA    . TYR C 2 234 ? 120.040 75.842  118.653 1.00 25.77 ?  213 TYR C CA    1 
ATOM   12711 C  C     . TYR C 2 234 ? 120.711 74.755  117.794 1.00 26.44 ?  213 TYR C C     1 
ATOM   12712 O  O     . TYR C 2 234 ? 120.279 73.600  117.788 1.00 26.29 ?  213 TYR C O     1 
ATOM   12713 C  CB    . TYR C 2 234 ? 119.130 76.730  117.789 1.00 25.67 ?  213 TYR C CB    1 
ATOM   12714 C  CG    . TYR C 2 234 ? 118.086 76.026  116.946 1.00 25.65 ?  213 TYR C CG    1 
ATOM   12715 C  CD1   . TYR C 2 234 ? 116.794 75.818  117.435 1.00 25.02 ?  213 TYR C CD1   1 
ATOM   12716 C  CD2   . TYR C 2 234 ? 118.374 75.620  115.633 1.00 26.59 ?  213 TYR C CD2   1 
ATOM   12717 C  CE1   . TYR C 2 234 ? 115.823 75.197  116.657 1.00 26.52 ?  213 TYR C CE1   1 
ATOM   12718 C  CE2   . TYR C 2 234 ? 117.410 74.990  114.844 1.00 27.00 ?  213 TYR C CE2   1 
ATOM   12719 C  CZ    . TYR C 2 234 ? 116.140 74.782  115.368 1.00 27.79 ?  213 TYR C CZ    1 
ATOM   12720 O  OH    . TYR C 2 234 ? 115.184 74.181  114.598 1.00 29.00 ?  213 TYR C OH    1 
ATOM   12721 N  N     . ASN C 2 235 ? 121.764 75.125  117.070 1.00 26.96 ?  214 ASN C N     1 
ATOM   12722 C  CA    . ASN C 2 235 ? 122.423 74.181  116.169 1.00 28.05 ?  214 ASN C CA    1 
ATOM   12723 C  C     . ASN C 2 235 ? 123.174 73.050  116.865 1.00 28.24 ?  214 ASN C C     1 
ATOM   12724 O  O     . ASN C 2 235 ? 123.514 72.058  116.227 1.00 28.63 ?  214 ASN C O     1 
ATOM   12725 C  CB    . ASN C 2 235 ? 123.315 74.906  115.149 1.00 28.38 ?  214 ASN C CB    1 
ATOM   12726 C  CG    . ASN C 2 235 ? 122.507 75.738  114.158 1.00 31.14 ?  214 ASN C CG    1 
ATOM   12727 O  OD1   . ASN C 2 235 ? 121.378 75.388  113.804 1.00 34.16 ?  214 ASN C OD1   1 
ATOM   12728 N  ND2   . ASN C 2 235 ? 123.084 76.847  113.711 1.00 32.42 ?  214 ASN C ND2   1 
ATOM   12729 N  N     . LYS C 2 236 ? 123.408 73.191  118.169 1.00 27.91 ?  215 LYS C N     1 
ATOM   12730 C  CA    . LYS C 2 236 ? 124.041 72.142  118.973 1.00 28.49 ?  215 LYS C CA    1 
ATOM   12731 C  C     . LYS C 2 236 ? 123.074 71.031  119.397 1.00 28.50 ?  215 LYS C C     1 
ATOM   12732 O  O     . LYS C 2 236 ? 123.501 69.973  119.866 1.00 28.98 ?  215 LYS C O     1 
ATOM   12733 C  CB    . LYS C 2 236 ? 124.697 72.741  120.221 1.00 28.10 ?  215 LYS C CB    1 
ATOM   12734 C  CG    . LYS C 2 236 ? 125.851 73.690  119.930 1.00 29.25 ?  215 LYS C CG    1 
ATOM   12735 C  CD    . LYS C 2 236 ? 126.467 74.228  121.211 1.00 30.19 ?  215 LYS C CD    1 
ATOM   12736 C  CE    . LYS C 2 236 ? 127.383 75.387  120.897 1.00 32.63 ?  215 LYS C CE    1 
ATOM   12737 N  NZ    . LYS C 2 236 ? 127.996 75.943  122.126 1.00 35.39 1  215 LYS C NZ    1 
ATOM   12738 N  N     . GLN C 2 237 ? 121.777 71.257  119.219 1.00 28.25 ?  216 GLN C N     1 
ATOM   12739 C  CA    . GLN C 2 237 ? 120.775 70.351  119.783 1.00 28.34 ?  216 GLN C CA    1 
ATOM   12740 C  C     . GLN C 2 237 ? 120.435 69.153  118.879 1.00 28.92 ?  216 GLN C C     1 
ATOM   12741 O  O     . GLN C 2 237 ? 120.677 69.185  117.672 1.00 28.53 ?  216 GLN C O     1 
ATOM   12742 C  CB    . GLN C 2 237 ? 119.512 71.139  120.160 1.00 27.68 ?  216 GLN C CB    1 
ATOM   12743 C  CG    . GLN C 2 237 ? 119.779 72.395  121.024 1.00 26.67 ?  216 GLN C CG    1 
ATOM   12744 C  CD    . GLN C 2 237 ? 120.644 72.127  122.252 1.00 25.32 ?  216 GLN C CD    1 
ATOM   12745 O  OE1   . GLN C 2 237 ? 120.447 71.143  122.968 1.00 25.49 ?  216 GLN C OE1   1 
ATOM   12746 N  NE2   . GLN C 2 237 ? 121.607 73.010  122.503 1.00 23.63 ?  216 GLN C NE2   1 
ATOM   12747 N  N     . THR C 2 238 ? 119.871 68.103  119.477 1.00 29.53 ?  217 THR C N     1 
ATOM   12748 C  CA    . THR C 2 238 ? 119.267 67.009  118.711 1.00 30.73 ?  217 THR C CA    1 
ATOM   12749 C  C     . THR C 2 238 ? 118.060 67.547  117.933 1.00 31.13 ?  217 THR C C     1 
ATOM   12750 O  O     . THR C 2 238 ? 117.545 68.638  118.239 1.00 30.17 ?  217 THR C O     1 
ATOM   12751 C  CB    . THR C 2 238 ? 118.754 65.878  119.621 1.00 30.79 ?  217 THR C CB    1 
ATOM   12752 O  OG1   . THR C 2 238 ? 117.632 66.354  120.378 1.00 31.16 ?  217 THR C OG1   1 
ATOM   12753 C  CG2   . THR C 2 238 ? 119.848 65.381  120.572 1.00 31.22 ?  217 THR C CG2   1 
ATOM   12754 N  N     . GLU C 2 239 ? 117.592 66.773  116.951 1.00 31.67 ?  218 GLU C N     1 
ATOM   12755 C  CA    . GLU C 2 239 ? 116.405 67.163  116.188 1.00 32.25 ?  218 GLU C CA    1 
ATOM   12756 C  C     . GLU C 2 239 ? 115.164 67.287  117.080 1.00 31.86 ?  218 GLU C C     1 
ATOM   12757 O  O     . GLU C 2 239 ? 114.351 68.198  116.904 1.00 31.09 ?  218 GLU C O     1 
ATOM   12758 C  CB    . GLU C 2 239 ? 116.166 66.207  115.007 1.00 33.29 ?  218 GLU C CB    1 
ATOM   12759 C  CG    . GLU C 2 239 ? 117.237 66.317  113.905 1.00 35.65 ?  218 GLU C CG    1 
ATOM   12760 C  CD    . GLU C 2 239 ? 117.338 67.725  113.307 1.00 39.17 ?  218 GLU C CD    1 
ATOM   12761 O  OE1   . GLU C 2 239 ? 116.280 68.326  112.986 1.00 41.08 ?  218 GLU C OE1   1 
ATOM   12762 O  OE2   . GLU C 2 239 ? 118.475 68.238  113.161 1.00 39.64 -1 218 GLU C OE2   1 
ATOM   12763 N  N     . GLU C 2 240 ? 115.053 66.386  118.057 1.00 31.72 ?  219 GLU C N     1 
ATOM   12764 C  CA    . GLU C 2 240 ? 113.957 66.396  119.016 1.00 31.76 ?  219 GLU C CA    1 
ATOM   12765 C  C     . GLU C 2 240 ? 113.971 67.674  119.868 1.00 30.21 ?  219 GLU C C     1 
ATOM   12766 O  O     . GLU C 2 240 ? 112.928 68.315  120.065 1.00 29.63 ?  219 GLU C O     1 
ATOM   12767 C  CB    . GLU C 2 240 ? 114.031 65.144  119.893 1.00 32.58 ?  219 GLU C CB    1 
ATOM   12768 C  CG    . GLU C 2 240 ? 112.818 64.910  120.779 1.00 36.93 ?  219 GLU C CG    1 
ATOM   12769 C  CD    . GLU C 2 240 ? 112.764 63.488  121.326 1.00 42.06 ?  219 GLU C CD    1 
ATOM   12770 O  OE1   . GLU C 2 240 ? 112.902 63.312  122.558 1.00 44.09 ?  219 GLU C OE1   1 
ATOM   12771 O  OE2   . GLU C 2 240 ? 112.590 62.542  120.523 1.00 44.45 -1 219 GLU C OE2   1 
ATOM   12772 N  N     . LYS C 2 241 ? 115.156 68.041  120.353 1.00 28.91 ?  220 LYS C N     1 
ATOM   12773 C  CA    . LYS C 2 241 ? 115.332 69.251  121.144 1.00 28.14 ?  220 LYS C CA    1 
ATOM   12774 C  C     . LYS C 2 241 ? 115.045 70.517  120.334 1.00 27.03 ?  220 LYS C C     1 
ATOM   12775 O  O     . LYS C 2 241 ? 114.407 71.446  120.838 1.00 26.72 ?  220 LYS C O     1 
ATOM   12776 C  CB    . LYS C 2 241 ? 116.737 69.312  121.751 1.00 27.83 ?  220 LYS C CB    1 
ATOM   12777 C  CG    . LYS C 2 241 ? 116.950 70.506  122.693 1.00 29.68 ?  220 LYS C CG    1 
ATOM   12778 C  CD    . LYS C 2 241 ? 116.778 70.124  124.157 1.00 33.58 ?  220 LYS C CD    1 
ATOM   12779 C  CE    . LYS C 2 241 ? 115.336 70.125  124.578 1.00 33.71 ?  220 LYS C CE    1 
ATOM   12780 N  NZ    . LYS C 2 241 ? 115.146 69.593  125.967 1.00 34.69 1  220 LYS C NZ    1 
ATOM   12781 N  N     . LYS C 2 242 ? 115.527 70.542  119.090 1.00 26.38 ?  221 LYS C N     1 
ATOM   12782 C  CA    . LYS C 2 242 ? 115.254 71.629  118.146 1.00 25.87 ?  221 LYS C CA    1 
ATOM   12783 C  C     . LYS C 2 242 ? 113.766 71.847  117.943 1.00 25.72 ?  221 LYS C C     1 
ATOM   12784 O  O     . LYS C 2 242 ? 113.299 72.995  117.941 1.00 24.52 ?  221 LYS C O     1 
ATOM   12785 C  CB    . LYS C 2 242 ? 115.909 71.365  116.788 1.00 25.83 ?  221 LYS C CB    1 
ATOM   12786 C  CG    . LYS C 2 242 ? 117.403 71.593  116.744 1.00 26.76 ?  221 LYS C CG    1 
ATOM   12787 C  CD    . LYS C 2 242 ? 117.909 71.430  115.315 1.00 28.40 ?  221 LYS C CD    1 
ATOM   12788 C  CE    . LYS C 2 242 ? 119.410 71.420  115.253 1.00 29.84 ?  221 LYS C CE    1 
ATOM   12789 N  NZ    . LYS C 2 242 ? 119.874 71.040  113.898 1.00 30.96 1  221 LYS C NZ    1 
ATOM   12790 N  N     . ALA C 2 243 ? 113.034 70.744  117.762 1.00 25.97 ?  222 ALA C N     1 
ATOM   12791 C  CA    . ALA C 2 243 ? 111.576 70.795  117.621 1.00 25.79 ?  222 ALA C CA    1 
ATOM   12792 C  C     . ALA C 2 243 ? 110.914 71.456  118.831 1.00 25.24 ?  222 ALA C C     1 
ATOM   12793 O  O     . ALA C 2 243 ? 109.987 72.263  118.670 1.00 25.37 ?  222 ALA C O     1 
ATOM   12794 C  CB    . ALA C 2 243 ? 111.006 69.398  117.370 1.00 26.17 ?  222 ALA C CB    1 
ATOM   12795 N  N     . GLU C 2 244 ? 111.399 71.147  120.031 1.00 25.02 ?  223 GLU C N     1 
ATOM   12796 C  CA    . GLU C 2 244 ? 110.897 71.795  121.253 1.00 25.08 ?  223 GLU C CA    1 
ATOM   12797 C  C     . GLU C 2 244 ? 111.251 73.292  121.314 1.00 24.70 ?  223 GLU C C     1 
ATOM   12798 O  O     . GLU C 2 244 ? 110.437 74.119  121.751 1.00 24.20 ?  223 GLU C O     1 
ATOM   12799 C  CB    . GLU C 2 244 ? 111.399 71.077  122.510 1.00 25.35 ?  223 GLU C CB    1 
ATOM   12800 C  CG    . GLU C 2 244 ? 110.852 71.683  123.813 1.00 26.67 ?  223 GLU C CG    1 
ATOM   12801 C  CD    . GLU C 2 244 ? 111.559 71.170  125.055 1.00 28.29 ?  223 GLU C CD    1 
ATOM   12802 O  OE1   . GLU C 2 244 ? 112.138 70.068  125.016 1.00 29.51 ?  223 GLU C OE1   1 
ATOM   12803 O  OE2   . GLU C 2 244 ? 111.535 71.880  126.077 1.00 29.09 -1 223 GLU C OE2   1 
ATOM   12804 N  N     . LEU C 2 245 ? 112.463 73.633  120.888 1.00 24.27 ?  224 LEU C N     1 
ATOM   12805 C  CA    . LEU C 2 245 ? 112.900 75.031  120.886 1.00 24.54 ?  224 LEU C CA    1 
ATOM   12806 C  C     . LEU C 2 245 ? 112.098 75.903  119.909 1.00 24.42 ?  224 LEU C C     1 
ATOM   12807 O  O     . LEU C 2 245 ? 111.789 77.057  120.216 1.00 24.10 ?  224 LEU C O     1 
ATOM   12808 C  CB    . LEU C 2 245 ? 114.417 75.134  120.639 1.00 23.86 ?  224 LEU C CB    1 
ATOM   12809 C  CG    . LEU C 2 245 ? 115.310 74.576  121.755 1.00 24.78 ?  224 LEU C CG    1 
ATOM   12810 C  CD1   . LEU C 2 245 ? 116.792 74.785  121.427 1.00 25.54 ?  224 LEU C CD1   1 
ATOM   12811 C  CD2   . LEU C 2 245 ? 114.978 75.182  123.126 1.00 25.29 ?  224 LEU C CD2   1 
ATOM   12812 N  N     . ARG C 2 246 ? 111.753 75.342  118.751 1.00 25.26 ?  225 ARG C N     1 
ATOM   12813 C  CA    . ARG C 2 246 ? 110.872 76.018  117.788 1.00 25.97 ?  225 ARG C CA    1 
ATOM   12814 C  C     . ARG C 2 246 ? 109.494 76.234  118.399 1.00 25.85 ?  225 ARG C C     1 
ATOM   12815 O  O     . ARG C 2 246 ? 108.910 77.308  118.246 1.00 25.01 ?  225 ARG C O     1 
ATOM   12816 C  CB    . ARG C 2 246 ? 110.761 75.238  116.461 1.00 26.65 ?  225 ARG C CB    1 
ATOM   12817 C  CG    . ARG C 2 246 ? 112.064 75.185  115.665 1.00 28.90 ?  225 ARG C CG    1 
ATOM   12818 C  CD    . ARG C 2 246 ? 111.866 74.757  114.191 1.00 31.26 ?  225 ARG C CD    1 
ATOM   12819 N  NE    . ARG C 2 246 ? 111.258 73.431  114.056 1.00 34.01 ?  225 ARG C NE    1 
ATOM   12820 C  CZ    . ARG C 2 246 ? 111.898 72.274  114.233 1.00 35.64 ?  225 ARG C CZ    1 
ATOM   12821 N  NH1   . ARG C 2 246 ? 113.183 72.252  114.562 1.00 36.11 1  225 ARG C NH1   1 
ATOM   12822 N  NH2   . ARG C 2 246 ? 111.242 71.129  114.081 1.00 37.05 ?  225 ARG C NH2   1 
ATOM   12823 N  N     . GLU C 2 247 ? 108.982 75.217  119.099 1.00 26.01 ?  226 GLU C N     1 
ATOM   12824 C  CA    . GLU C 2 247 ? 107.713 75.339  119.824 1.00 26.48 ?  226 GLU C CA    1 
ATOM   12825 C  C     . GLU C 2 247 ? 107.776 76.472  120.848 1.00 25.72 ?  226 GLU C C     1 
ATOM   12826 O  O     . GLU C 2 247 ? 106.861 77.306  120.918 1.00 25.16 ?  226 GLU C O     1 
ATOM   12827 C  CB    . GLU C 2 247 ? 107.338 74.036  120.535 1.00 27.18 ?  226 GLU C CB    1 
ATOM   12828 C  CG    . GLU C 2 247 ? 105.867 73.978  120.932 1.00 30.38 ?  226 GLU C CG    1 
ATOM   12829 C  CD    . GLU C 2 247 ? 105.603 73.287  122.256 1.00 35.77 ?  226 GLU C CD    1 
ATOM   12830 O  OE1   . GLU C 2 247 ? 106.373 72.388  122.658 1.00 38.02 ?  226 GLU C OE1   1 
ATOM   12831 O  OE2   . GLU C 2 247 ? 104.599 73.648  122.906 1.00 40.39 -1 226 GLU C OE2   1 
ATOM   12832 N  N     . PHE C 2 248 ? 108.854 76.499  121.634 1.00 24.71 ?  227 PHE C N     1 
ATOM   12833 C  CA    . PHE C 2 248 ? 109.056 77.571  122.608 1.00 23.71 ?  227 PHE C CA    1 
ATOM   12834 C  C     . PHE C 2 248 ? 109.020 78.935  121.917 1.00 23.14 ?  227 PHE C C     1 
ATOM   12835 O  O     . PHE C 2 248 ? 108.315 79.839  122.368 1.00 22.40 ?  227 PHE C O     1 
ATOM   12836 C  CB    . PHE C 2 248 ? 110.374 77.413  123.386 1.00 23.85 ?  227 PHE C CB    1 
ATOM   12837 C  CG    . PHE C 2 248 ? 110.774 78.661  124.133 1.00 23.64 ?  227 PHE C CG    1 
ATOM   12838 C  CD1   . PHE C 2 248 ? 110.222 78.941  125.385 1.00 23.07 ?  227 PHE C CD1   1 
ATOM   12839 C  CD2   . PHE C 2 248 ? 111.648 79.593  123.549 1.00 23.04 ?  227 PHE C CD2   1 
ATOM   12840 C  CE1   . PHE C 2 248 ? 110.562 80.105  126.073 1.00 22.73 ?  227 PHE C CE1   1 
ATOM   12841 C  CE2   . PHE C 2 248 ? 111.993 80.768  124.221 1.00 23.31 ?  227 PHE C CE2   1 
ATOM   12842 C  CZ    . PHE C 2 248 ? 111.451 81.026  125.491 1.00 21.51 ?  227 PHE C CZ    1 
ATOM   12843 N  N     . ALA C 2 249 ? 109.775 79.066  120.825 1.00 22.95 ?  228 ALA C N     1 
ATOM   12844 C  CA    . ALA C 2 249 ? 109.928 80.351  120.130 1.00 22.96 ?  228 ALA C CA    1 
ATOM   12845 C  C     . ALA C 2 249 ? 108.606 80.836  119.540 1.00 23.31 ?  228 ALA C C     1 
ATOM   12846 O  O     . ALA C 2 249 ? 108.263 82.015  119.647 1.00 22.63 ?  228 ALA C O     1 
ATOM   12847 C  CB    . ALA C 2 249 ? 110.995 80.251  119.041 1.00 22.40 ?  228 ALA C CB    1 
ATOM   12848 N  N     . ILE C 2 250 ? 107.874 79.915  118.923 1.00 23.66 ?  229 ILE C N     1 
ATOM   12849 C  CA    . ILE C 2 250 ? 106.587 80.233  118.303 1.00 25.00 ?  229 ILE C CA    1 
ATOM   12850 C  C     . ILE C 2 250 ? 105.496 80.506  119.347 1.00 24.64 ?  229 ILE C C     1 
ATOM   12851 O  O     . ILE C 2 250 ? 104.738 81.474  119.213 1.00 24.26 ?  229 ILE C O     1 
ATOM   12852 C  CB    . ILE C 2 250 ? 106.178 79.158  117.248 1.00 25.43 ?  229 ILE C CB    1 
ATOM   12853 C  CG1   . ILE C 2 250 ? 107.090 79.285  116.019 1.00 27.27 ?  229 ILE C CG1   1 
ATOM   12854 C  CG2   . ILE C 2 250 ? 104.707 79.358  116.792 1.00 27.62 ?  229 ILE C CG2   1 
ATOM   12855 C  CD1   . ILE C 2 250 ? 107.453 77.958  115.339 1.00 31.32 ?  229 ILE C CD1   1 
ATOM   12856 N  N     . ASP C 2 251 ? 105.435 79.686  120.397 1.00 24.78 ?  230 ASP C N     1 
ATOM   12857 C  CA    . ASP C 2 251 ? 104.507 79.949  121.513 1.00 25.20 ?  230 ASP C CA    1 
ATOM   12858 C  C     . ASP C 2 251 ? 104.767 81.306  122.167 1.00 24.08 ?  230 ASP C C     1 
ATOM   12859 O  O     . ASP C 2 251 ? 103.826 82.045  122.495 1.00 23.34 ?  230 ASP C O     1 
ATOM   12860 C  CB    . ASP C 2 251 ? 104.612 78.873  122.603 1.00 25.73 ?  230 ASP C CB    1 
ATOM   12861 C  CG    . ASP C 2 251 ? 103.945 77.573  122.218 1.00 28.78 ?  230 ASP C CG    1 
ATOM   12862 O  OD1   . ASP C 2 251 ? 103.297 77.503  121.148 1.00 29.99 ?  230 ASP C OD1   1 
ATOM   12863 O  OD2   . ASP C 2 251 ? 104.081 76.610  123.002 1.00 33.31 -1 230 ASP C OD2   1 
ATOM   12864 N  N     . LEU C 2 252 ? 106.043 81.624  122.369 1.00 22.98 ?  231 LEU C N     1 
ATOM   12865 C  CA    . LEU C 2 252 ? 106.406 82.902  122.984 1.00 21.63 ?  231 LEU C CA    1 
ATOM   12866 C  C     . LEU C 2 252 ? 106.029 84.058  122.065 1.00 21.66 ?  231 LEU C C     1 
ATOM   12867 O  O     . LEU C 2 252 ? 105.503 85.079  122.511 1.00 19.41 ?  231 LEU C O     1 
ATOM   12868 C  CB    . LEU C 2 252 ? 107.900 82.960  123.301 1.00 21.89 ?  231 LEU C CB    1 
ATOM   12869 C  CG    . LEU C 2 252 ? 108.449 84.281  123.871 1.00 21.33 ?  231 LEU C CG    1 
ATOM   12870 C  CD1   . LEU C 2 252 ? 107.738 84.681  125.181 1.00 20.89 ?  231 LEU C CD1   1 
ATOM   12871 C  CD2   . LEU C 2 252 ? 109.962 84.152  124.069 1.00 20.31 ?  231 LEU C CD2   1 
ATOM   12872 N  N     . LEU C 2 253 ? 106.311 83.893  120.776 1.00 22.28 ?  232 LEU C N     1 
ATOM   12873 C  CA    . LEU C 2 253 ? 105.993 84.941  119.812 1.00 23.05 ?  232 LEU C CA    1 
ATOM   12874 C  C     . LEU C 2 253 ? 104.494 85.221  119.792 1.00 23.36 ?  232 LEU C C     1 
ATOM   12875 O  O     . LEU C 2 253 ? 104.079 86.388  119.887 1.00 22.96 ?  232 LEU C O     1 
ATOM   12876 C  CB    . LEU C 2 253 ? 106.506 84.585  118.415 1.00 23.53 ?  232 LEU C CB    1 
ATOM   12877 C  CG    . LEU C 2 253 ? 106.212 85.653  117.354 1.00 25.63 ?  232 LEU C CG    1 
ATOM   12878 C  CD1   . LEU C 2 253 ? 106.939 86.964  117.654 1.00 25.88 ?  232 LEU C CD1   1 
ATOM   12879 C  CD2   . LEU C 2 253 ? 106.591 85.124  115.979 1.00 27.67 ?  232 LEU C CD2   1 
ATOM   12880 N  N     . ASN C 2 254 ? 103.691 84.157  119.687 1.00 23.55 ?  233 ASN C N     1 
ATOM   12881 C  CA    . ASN C 2 254 ? 102.223 84.289  119.717 1.00 24.61 ?  233 ASN C CA    1 
ATOM   12882 C  C     . ASN C 2 254 ? 101.692 84.949  120.993 1.00 23.57 ?  233 ASN C C     1 
ATOM   12883 O  O     . ASN C 2 254 ? 100.799 85.791  120.940 1.00 23.52 ?  233 ASN C O     1 
ATOM   12884 C  CB    . ASN C 2 254 ? 101.540 82.938  119.491 1.00 24.99 ?  233 ASN C CB    1 
ATOM   12885 C  CG    . ASN C 2 254 ? 101.391 82.597  118.014 1.00 28.92 ?  233 ASN C CG    1 
ATOM   12886 O  OD1   . ASN C 2 254 ? 100.788 83.345  117.242 1.00 33.75 ?  233 ASN C OD1   1 
ATOM   12887 N  ND2   . ASN C 2 254 ? 101.936 81.462  117.620 1.00 30.99 ?  233 ASN C ND2   1 
ATOM   12888 N  N     . GLN C 2 255 ? 102.248 84.568  122.139 1.00 23.22 ?  234 GLN C N     1 
ATOM   12889 C  CA    . GLN C 2 255 ? 101.841 85.170  123.401 1.00 22.54 ?  234 GLN C CA    1 
ATOM   12890 C  C     . GLN C 2 255 ? 102.172 86.676  123.446 1.00 22.00 ?  234 GLN C C     1 
ATOM   12891 O  O     . GLN C 2 255 ? 101.341 87.500  123.863 1.00 21.73 ?  234 GLN C O     1 
ATOM   12892 C  CB    . GLN C 2 255 ? 102.483 84.433  124.576 1.00 22.85 ?  234 GLN C CB    1 
ATOM   12893 C  CG    . GLN C 2 255 ? 101.878 84.797  125.915 1.00 23.87 ?  234 GLN C CG    1 
ATOM   12894 C  CD    . GLN C 2 255 ? 102.543 84.084  127.087 1.00 24.95 ?  234 GLN C CD    1 
ATOM   12895 O  OE1   . GLN C 2 255 ? 103.360 83.175  126.901 1.00 24.21 ?  234 GLN C OE1   1 
ATOM   12896 N  NE2   . GLN C 2 255 ? 102.212 84.517  128.305 1.00 25.97 ?  234 GLN C NE2   1 
ATOM   12897 N  N     . LEU C 2 256 ? 103.379 87.027  123.018 1.00 21.27 ?  235 LEU C N     1 
ATOM   12898 C  CA    . LEU C 2 256 ? 103.787 88.427  122.945 1.00 21.37 ?  235 LEU C CA    1 
ATOM   12899 C  C     . LEU C 2 256 ? 102.949 89.187  121.913 1.00 21.21 ?  235 LEU C C     1 
ATOM   12900 O  O     . LEU C 2 256 ? 102.559 90.332  122.136 1.00 20.75 ?  235 LEU C O     1 
ATOM   12901 C  CB    . LEU C 2 256 ? 105.275 88.523  122.583 1.00 20.93 ?  235 LEU C CB    1 
ATOM   12902 C  CG    . LEU C 2 256 ? 106.318 88.129  123.632 1.00 21.74 ?  235 LEU C CG    1 
ATOM   12903 C  CD1   . LEU C 2 256 ? 107.724 88.179  123.016 1.00 20.15 ?  235 LEU C CD1   1 
ATOM   12904 C  CD2   . LEU C 2 256 ? 106.244 89.010  124.879 1.00 20.90 ?  235 LEU C CD2   1 
ATOM   12905 N  N     . TYR C 2 257 ? 102.699 88.537  120.782 1.00 21.68 ?  236 TYR C N     1 
ATOM   12906 C  CA    . TYR C 2 257 ? 101.915 89.117  119.692 1.00 22.40 ?  236 TYR C CA    1 
ATOM   12907 C  C     . TYR C 2 257 ? 100.498 89.495  120.155 1.00 23.31 ?  236 TYR C C     1 
ATOM   12908 O  O     . TYR C 2 257 ? 100.056 90.642  119.947 1.00 22.99 ?  236 TYR C O     1 
ATOM   12909 C  CB    . TYR C 2 257 ? 101.878 88.156  118.500 1.00 22.81 ?  236 TYR C CB    1 
ATOM   12910 C  CG    . TYR C 2 257 ? 100.978 88.584  117.357 1.00 23.76 ?  236 TYR C CG    1 
ATOM   12911 C  CD1   . TYR C 2 257 ? 101.279 89.712  116.588 1.00 24.05 ?  236 TYR C CD1   1 
ATOM   12912 C  CD2   . TYR C 2 257 ? 99.821  87.870  117.056 1.00 24.04 ?  236 TYR C CD2   1 
ATOM   12913 C  CE1   . TYR C 2 257 ? 100.450 90.117  115.548 1.00 24.40 ?  236 TYR C CE1   1 
ATOM   12914 C  CE2   . TYR C 2 257 ? 98.987  88.266  116.013 1.00 26.30 ?  236 TYR C CE2   1 
ATOM   12915 C  CZ    . TYR C 2 257 ? 99.316  89.382  115.265 1.00 25.80 ?  236 TYR C CZ    1 
ATOM   12916 O  OH    . TYR C 2 257 ? 98.501  89.762  114.237 1.00 28.42 ?  236 TYR C OH    1 
ATOM   12917 N  N     . GLU C 2 258 ? 99.814  88.556  120.816 1.00 22.99 ?  237 GLU C N     1 
ATOM   12918 C  CA    . GLU C 2 258 ? 98.447  88.789  121.295 1.00 24.46 ?  237 GLU C CA    1 
ATOM   12919 C  C     . GLU C 2 258 ? 98.380  89.952  122.271 1.00 23.86 ?  237 GLU C C     1 
ATOM   12920 O  O     . GLU C 2 258 ? 97.466  90.772  122.203 1.00 24.01 ?  237 GLU C O     1 
ATOM   12921 C  CB    . GLU C 2 258 ? 97.832  87.516  121.903 1.00 25.21 ?  237 GLU C CB    1 
ATOM   12922 C  CG    . GLU C 2 258 ? 97.540  86.410  120.863 1.00 30.12 ?  237 GLU C CG    1 
ATOM   12923 C  CD    . GLU C 2 258 ? 96.451  86.803  119.859 1.00 35.29 ?  237 GLU C CD    1 
ATOM   12924 O  OE1   . GLU C 2 258 ? 95.553  87.602  120.210 1.00 37.71 ?  237 GLU C OE1   1 
ATOM   12925 O  OE2   . GLU C 2 258 ? 96.492  86.304  118.710 1.00 39.07 -1 237 GLU C OE2   1 
ATOM   12926 N  N     . ASN C 2 259 ? 99.369  90.040  123.160 1.00 23.25 ?  238 ASN C N     1 
ATOM   12927 C  CA    . ASN C 2 259 ? 99.480  91.176  124.072 1.00 23.10 ?  238 ASN C CA    1 
ATOM   12928 C  C     . ASN C 2 259 ? 99.761  92.488  123.315 1.00 22.68 ?  238 ASN C C     1 
ATOM   12929 O  O     . ASN C 2 259 ? 99.187  93.535  123.628 1.00 22.73 ?  238 ASN C O     1 
ATOM   12930 C  CB    . ASN C 2 259 ? 100.556 90.897  125.123 1.00 23.22 ?  238 ASN C CB    1 
ATOM   12931 C  CG    . ASN C 2 259 ? 100.696 92.022  126.127 1.00 24.46 ?  238 ASN C CG    1 
ATOM   12932 O  OD1   . ASN C 2 259 ? 99.814  92.242  126.963 1.00 26.28 ?  238 ASN C OD1   1 
ATOM   12933 N  ND2   . ASN C 2 259 ? 101.808 92.743  126.052 1.00 24.93 ?  238 ASN C ND2   1 
ATOM   12934 N  N     . GLU C 2 260 ? 100.624 92.423  122.303 1.00 22.64 ?  239 GLU C N     1 
ATOM   12935 C  CA    . GLU C 2 260 ? 100.986 93.614  121.532 1.00 23.18 ?  239 GLU C CA    1 
ATOM   12936 C  C     . GLU C 2 260 ? 99.792  94.168  120.737 1.00 23.40 ?  239 GLU C C     1 
ATOM   12937 O  O     . GLU C 2 260 ? 99.657  95.391  120.573 1.00 23.57 ?  239 GLU C O     1 
ATOM   12938 C  CB    . GLU C 2 260 ? 102.180 93.331  120.609 1.00 23.19 ?  239 GLU C CB    1 
ATOM   12939 C  CG    . GLU C 2 260 ? 103.036 94.579  120.285 1.00 24.33 ?  239 GLU C CG    1 
ATOM   12940 C  CD    . GLU C 2 260 ? 103.742 95.175  121.516 1.00 27.99 ?  239 GLU C CD    1 
ATOM   12941 O  OE1   . GLU C 2 260 ? 103.712 94.573  122.611 1.00 27.36 ?  239 GLU C OE1   1 
ATOM   12942 O  OE2   . GLU C 2 260 ? 104.330 96.272  121.389 1.00 28.98 -1 239 GLU C OE2   1 
ATOM   12943 N  N     . LEU C 2 261 ? 98.927  93.272  120.260 1.00 23.35 ?  240 LEU C N     1 
ATOM   12944 C  CA    . LEU C 2 261 ? 97.679  93.681  119.597 1.00 23.74 ?  240 LEU C CA    1 
ATOM   12945 C  C     . LEU C 2 261 ? 96.813  94.570  120.493 1.00 23.80 ?  240 LEU C C     1 
ATOM   12946 O  O     . LEU C 2 261 ? 96.337  95.634  120.065 1.00 23.33 ?  240 LEU C O     1 
ATOM   12947 C  CB    . LEU C 2 261 ? 96.871  92.463  119.141 1.00 24.09 ?  240 LEU C CB    1 
ATOM   12948 C  CG    . LEU C 2 261 ? 97.440  91.640  117.985 1.00 24.07 ?  240 LEU C CG    1 
ATOM   12949 C  CD1   . LEU C 2 261 ? 96.517  90.466  117.685 1.00 24.77 ?  240 LEU C CD1   1 
ATOM   12950 C  CD2   . LEU C 2 261 ? 97.650  92.513  116.731 1.00 24.38 ?  240 LEU C CD2   1 
ATOM   12951 N  N     . GLU C 2 262 ? 96.605  94.124  121.726 1.00 23.41 ?  241 GLU C N     1 
ATOM   12952 C  CA    . GLU C 2 262 ? 95.828  94.887  122.701 1.00 24.02 ?  241 GLU C CA    1 
ATOM   12953 C  C     . GLU C 2 262 ? 96.492  96.229  123.045 1.00 22.91 ?  241 GLU C C     1 
ATOM   12954 O  O     . GLU C 2 262 ? 95.814  97.243  123.150 1.00 22.94 ?  241 GLU C O     1 
ATOM   12955 C  CB    . GLU C 2 262 ? 95.618  94.053  123.966 1.00 24.92 ?  241 GLU C CB    1 
ATOM   12956 C  CG    . GLU C 2 262 ? 94.759  92.816  123.766 1.00 27.82 ?  241 GLU C CG    1 
ATOM   12957 C  CD    . GLU C 2 262 ? 94.556  92.040  125.055 1.00 33.08 ?  241 GLU C CD    1 
ATOM   12958 O  OE1   . GLU C 2 262 ? 95.450  91.256  125.445 1.00 36.94 ?  241 GLU C OE1   1 
ATOM   12959 O  OE2   . GLU C 2 262 ? 93.492  92.209  125.679 1.00 37.48 -1 241 GLU C OE2   1 
ATOM   12960 N  N     . TYR C 2 263 ? 97.814  96.215  123.228 1.00 21.84 ?  242 TYR C N     1 
ATOM   12961 C  CA    . TYR C 2 263 ? 98.609  97.422  123.448 1.00 21.66 ?  242 TYR C CA    1 
ATOM   12962 C  C     . TYR C 2 263 ? 98.468  98.388  122.279 1.00 21.28 ?  242 TYR C C     1 
ATOM   12963 O  O     . TYR C 2 263 ? 98.281  99.597  122.478 1.00 21.14 ?  242 TYR C O     1 
ATOM   12964 C  CB    . TYR C 2 263 ? 100.091 97.046  123.605 1.00 21.44 ?  242 TYR C CB    1 
ATOM   12965 C  CG    . TYR C 2 263 ? 101.052 98.197  123.866 1.00 21.89 ?  242 TYR C CG    1 
ATOM   12966 C  CD1   . TYR C 2 263 ? 101.048 98.875  125.086 1.00 22.52 ?  242 TYR C CD1   1 
ATOM   12967 C  CD2   . TYR C 2 263 ? 101.992 98.579  122.905 1.00 22.58 ?  242 TYR C CD2   1 
ATOM   12968 C  CE1   . TYR C 2 263 ? 101.945 99.914  125.336 1.00 22.67 ?  242 TYR C CE1   1 
ATOM   12969 C  CE2   . TYR C 2 263 ? 102.900 99.617  123.147 1.00 24.03 ?  242 TYR C CE2   1 
ATOM   12970 C  CZ    . TYR C 2 263 ? 102.871 100.271 124.374 1.00 23.75 ?  242 TYR C CZ    1 
ATOM   12971 O  OH    . TYR C 2 263 ? 103.753 101.302 124.632 1.00 26.82 ?  242 TYR C OH    1 
ATOM   12972 N  N     . THR C 2 264 ? 98.562  97.851  121.065 1.00 20.66 ?  243 THR C N     1 
ATOM   12973 C  CA    . THR C 2 264 ? 98.470  98.665  119.844 1.00 20.99 ?  243 THR C CA    1 
ATOM   12974 C  C     . THR C 2 264 ? 97.096  99.338  119.737 1.00 21.22 ?  243 THR C C     1 
ATOM   12975 O  O     . THR C 2 264 ? 97.010  100.546 119.471 1.00 20.95 ?  243 THR C O     1 
ATOM   12976 C  CB    . THR C 2 264 ? 98.771  97.816  118.578 1.00 20.58 ?  243 THR C CB    1 
ATOM   12977 O  OG1   . THR C 2 264 ? 100.135 97.387  118.618 1.00 20.84 ?  243 THR C OG1   1 
ATOM   12978 C  CG2   . THR C 2 264 ? 98.546  98.622  117.296 1.00 20.90 ?  243 THR C CG2   1 
ATOM   12979 N  N     . GLU C 2 265 ? 96.033  98.568  119.972 1.00 21.62 ?  244 GLU C N     1 
ATOM   12980 C  CA    . GLU C 2 265 ? 94.679  99.122  119.928 1.00 23.46 ?  244 GLU C CA    1 
ATOM   12981 C  C     . GLU C 2 265 ? 94.489  100.198 120.978 1.00 23.33 ?  244 GLU C C     1 
ATOM   12982 O  O     . GLU C 2 265 ? 93.914  101.254 120.711 1.00 22.86 ?  244 GLU C O     1 
ATOM   12983 C  CB    . GLU C 2 265 ? 93.618  98.034  120.097 1.00 24.31 ?  244 GLU C CB    1 
ATOM   12984 C  CG    . GLU C 2 265 ? 93.481  97.124  118.880 1.00 27.63 ?  244 GLU C CG    1 
ATOM   12985 C  CD    . GLU C 2 265 ? 92.410  96.053  119.067 1.00 33.27 ?  244 GLU C CD    1 
ATOM   12986 O  OE1   . GLU C 2 265 ? 91.427  96.302  119.801 1.00 35.56 ?  244 GLU C OE1   1 
ATOM   12987 O  OE2   . GLU C 2 265 ? 92.549  94.962  118.469 1.00 35.96 -1 244 GLU C OE2   1 
ATOM   12988 N  N     . ASP C 2 266 ? 94.986  99.926  122.175 1.00 23.36 ?  245 ASP C N     1 
ATOM   12989 C  CA    . ASP C 2 266 ? 94.895  100.875 123.273 1.00 24.18 ?  245 ASP C CA    1 
ATOM   12990 C  C     . ASP C 2 266 ? 95.544  102.230 122.931 1.00 23.96 ?  245 ASP C C     1 
ATOM   12991 O  O     . ASP C 2 266 ? 95.003  103.283 123.259 1.00 24.19 ?  245 ASP C O     1 
ATOM   12992 C  CB    . ASP C 2 266 ? 95.545  100.271 124.514 1.00 25.14 ?  245 ASP C CB    1 
ATOM   12993 C  CG    . ASP C 2 266 ? 95.277  101.075 125.749 1.00 27.35 ?  245 ASP C CG    1 
ATOM   12994 O  OD1   . ASP C 2 266 ? 94.090  101.305 126.062 1.00 28.45 ?  245 ASP C OD1   1 
ATOM   12995 O  OD2   . ASP C 2 266 ? 96.262  101.479 126.405 1.00 31.99 -1 245 ASP C OD2   1 
ATOM   12996 N  N     . LEU C 2 267 ? 96.688  102.197 122.257 1.00 23.34 ?  246 LEU C N     1 
ATOM   12997 C  CA    . LEU C 2 267 ? 97.404  103.429 121.909 1.00 23.53 ?  246 LEU C CA    1 
ATOM   12998 C  C     . LEU C 2 267 ? 96.920  104.108 120.638 1.00 22.94 ?  246 LEU C C     1 
ATOM   12999 O  O     . LEU C 2 267 ? 96.818  105.335 120.588 1.00 23.14 ?  246 LEU C O     1 
ATOM   13000 C  CB    . LEU C 2 267 ? 98.899  103.150 121.779 1.00 23.37 ?  246 LEU C CB    1 
ATOM   13001 C  CG    . LEU C 2 267 ? 99.676  102.872 123.067 1.00 26.17 ?  246 LEU C CG    1 
ATOM   13002 C  CD1   . LEU C 2 267 ? 101.128 102.648 122.710 1.00 27.31 ?  246 LEU C CD1   1 
ATOM   13003 C  CD2   . LEU C 2 267 ? 99.549  104.039 124.041 1.00 28.08 ?  246 LEU C CD2   1 
ATOM   13004 N  N     . TYR C 2 268 ? 96.649  103.312 119.607 1.00 22.46 ?  247 TYR C N     1 
ATOM   13005 C  CA    . TYR C 2 268 ? 96.414  103.857 118.273 1.00 22.00 ?  247 TYR C CA    1 
ATOM   13006 C  C     . TYR C 2 268 ? 94.974  104.084 117.843 1.00 22.26 ?  247 TYR C C     1 
ATOM   13007 O  O     . TYR C 2 268 ? 94.754  104.794 116.861 1.00 22.17 ?  247 TYR C O     1 
ATOM   13008 C  CB    . TYR C 2 268 ? 97.137  103.015 117.214 1.00 21.73 ?  247 TYR C CB    1 
ATOM   13009 C  CG    . TYR C 2 268 ? 98.638  103.172 117.244 1.00 21.49 ?  247 TYR C CG    1 
ATOM   13010 C  CD1   . TYR C 2 268 ? 99.446  102.210 117.859 1.00 19.45 ?  247 TYR C CD1   1 
ATOM   13011 C  CD2   . TYR C 2 268 ? 99.252  104.291 116.671 1.00 22.71 ?  247 TYR C CD2   1 
ATOM   13012 C  CE1   . TYR C 2 268 ? 100.836 102.358 117.897 1.00 20.30 ?  247 TYR C CE1   1 
ATOM   13013 C  CE2   . TYR C 2 268 ? 100.647 104.451 116.696 1.00 21.69 ?  247 TYR C CE2   1 
ATOM   13014 C  CZ    . TYR C 2 268 ? 101.425 103.474 117.298 1.00 21.40 ?  247 TYR C CZ    1 
ATOM   13015 O  OH    . TYR C 2 268 ? 102.788 103.626 117.316 1.00 22.11 ?  247 TYR C OH    1 
ATOM   13016 N  N     . ASP C 2 269 ? 93.998  103.480 118.529 1.00 22.40 ?  248 ASP C N     1 
ATOM   13017 C  CA    . ASP C 2 269 ? 92.589  103.703 118.158 1.00 22.75 ?  248 ASP C CA    1 
ATOM   13018 C  C     . ASP C 2 269 ? 92.228  105.190 118.154 1.00 22.55 ?  248 ASP C C     1 
ATOM   13019 O  O     . ASP C 2 269 ? 91.486  105.645 117.275 1.00 22.22 ?  248 ASP C O     1 
ATOM   13020 C  CB    . ASP C 2 269 ? 91.610  102.912 119.047 1.00 23.03 ?  248 ASP C CB    1 
ATOM   13021 C  CG    . ASP C 2 269 ? 91.469  101.459 118.626 1.00 25.02 ?  248 ASP C CG    1 
ATOM   13022 O  OD1   . ASP C 2 269 ? 91.955  101.077 117.540 1.00 26.85 ?  248 ASP C OD1   1 
ATOM   13023 O  OD2   . ASP C 2 269 ? 90.857  100.685 119.390 1.00 28.74 -1 248 ASP C OD2   1 
ATOM   13024 N  N     . GLN C 2 270 ? 92.761  105.943 119.120 1.00 22.21 ?  249 GLN C N     1 
ATOM   13025 C  CA    . GLN C 2 270 ? 92.458  107.390 119.211 1.00 22.39 ?  249 GLN C CA    1 
ATOM   13026 C  C     . GLN C 2 270 ? 93.061  108.240 118.084 1.00 21.65 ?  249 GLN C C     1 
ATOM   13027 O  O     . GLN C 2 270 ? 92.686  109.402 117.924 1.00 21.70 ?  249 GLN C O     1 
ATOM   13028 C  CB    . GLN C 2 270 ? 92.830  107.968 120.585 1.00 22.53 ?  249 GLN C CB    1 
ATOM   13029 C  CG    . GLN C 2 270 ? 94.331  107.895 120.966 1.00 22.73 ?  249 GLN C CG    1 
ATOM   13030 C  CD    . GLN C 2 270 ? 94.593  108.491 122.334 1.00 25.39 ?  249 GLN C CD    1 
ATOM   13031 O  OE1   . GLN C 2 270 ? 93.666  108.683 123.123 1.00 27.88 ?  249 GLN C OE1   1 
ATOM   13032 N  NE2   . GLN C 2 270 ? 95.854  108.799 122.624 1.00 24.88 ?  249 GLN C NE2   1 
ATOM   13033 N  N     . VAL C 2 271 ? 93.987  107.663 117.317 1.00 20.91 ?  250 VAL C N     1 
ATOM   13034 C  CA    . VAL C 2 271 ? 94.589  108.356 116.154 1.00 20.62 ?  250 VAL C CA    1 
ATOM   13035 C  C     . VAL C 2 271 ? 94.267  107.643 114.827 1.00 20.53 ?  250 VAL C C     1 
ATOM   13036 O  O     . VAL C 2 271 ? 94.714  108.069 113.750 1.00 20.05 ?  250 VAL C O     1 
ATOM   13037 C  CB    . VAL C 2 271 ? 96.133  108.617 116.321 1.00 20.32 ?  250 VAL C CB    1 
ATOM   13038 C  CG1   . VAL C 2 271 ? 96.401  109.571 117.480 1.00 20.35 ?  250 VAL C CG1   1 
ATOM   13039 C  CG2   . VAL C 2 271 ? 96.924  107.316 116.520 1.00 19.32 ?  250 VAL C CG2   1 
ATOM   13040 N  N     . GLY C 2 272 ? 93.481  106.568 114.921 1.00 20.29 ?  251 GLY C N     1 
ATOM   13041 C  CA    . GLY C 2 272 ? 92.929  105.887 113.748 1.00 20.51 ?  251 GLY C CA    1 
ATOM   13042 C  C     . GLY C 2 272 ? 93.876  104.963 112.999 1.00 20.99 ?  251 GLY C C     1 
ATOM   13043 O  O     . GLY C 2 272 ? 93.649  104.662 111.816 1.00 20.22 ?  251 GLY C O     1 
ATOM   13044 N  N     . LEU C 2 273 ? 94.937  104.508 113.673 1.00 20.76 ?  252 LEU C N     1 
ATOM   13045 C  CA    . LEU C 2 273 ? 96.022  103.814 112.973 1.00 21.38 ?  252 LEU C CA    1 
ATOM   13046 C  C     . LEU C 2 273 ? 96.263  102.361 113.373 1.00 21.86 ?  252 LEU C C     1 
ATOM   13047 O  O     . LEU C 2 273 ? 97.217  101.744 112.902 1.00 22.45 ?  252 LEU C O     1 
ATOM   13048 C  CB    . LEU C 2 273 ? 97.331  104.617 113.070 1.00 21.44 ?  252 LEU C CB    1 
ATOM   13049 C  CG    . LEU C 2 273 ? 97.358  106.050 112.535 1.00 22.02 ?  252 LEU C CG    1 
ATOM   13050 C  CD1   . LEU C 2 273 ? 98.724  106.670 112.806 1.00 22.86 ?  252 LEU C CD1   1 
ATOM   13051 C  CD2   . LEU C 2 273 ? 97.016  106.093 111.030 1.00 23.88 ?  252 LEU C CD2   1 
ATOM   13052 N  N     . SER C 2 274 ? 95.397  101.802 114.216 1.00 22.19 ?  253 SER C N     1 
ATOM   13053 C  CA    . SER C 2 274 ? 95.672  100.504 114.829 1.00 22.47 ?  253 SER C CA    1 
ATOM   13054 C  C     . SER C 2 274 ? 95.903  99.387  113.810 1.00 22.94 ?  253 SER C C     1 
ATOM   13055 O  O     . SER C 2 274 ? 96.845  98.613  113.941 1.00 22.07 ?  253 SER C O     1 
ATOM   13056 C  CB    . SER C 2 274 ? 94.550  100.119 115.797 1.00 22.91 ?  253 SER C CB    1 
ATOM   13057 O  OG    . SER C 2 274 ? 94.568  100.984 116.915 1.00 24.25 ?  253 SER C OG    1 
ATOM   13058 N  N     . HIS C 2 275 ? 95.062  99.336  112.780 1.00 24.59 ?  254 HIS C N     1 
ATOM   13059 C  CA    . HIS C 2 275 ? 95.167  98.295  111.751 1.00 25.66 ?  254 HIS C CA    1 
ATOM   13060 C  C     . HIS C 2 275 ? 96.491  98.384  110.976 1.00 26.01 ?  254 HIS C C     1 
ATOM   13061 O  O     . HIS C 2 275 ? 97.122  97.359  110.665 1.00 26.23 ?  254 HIS C O     1 
ATOM   13062 C  CB    . HIS C 2 275 ? 93.971  98.374  110.792 1.00 26.89 ?  254 HIS C CB    1 
ATOM   13063 C  CG    . HIS C 2 275 ? 93.946  97.282  109.768 1.00 29.10 ?  254 HIS C CG    1 
ATOM   13064 N  ND1   . HIS C 2 275 ? 94.002  95.945  110.103 1.00 32.70 ?  254 HIS C ND1   1 
ATOM   13065 C  CD2   . HIS C 2 275 ? 93.869  97.328  108.418 1.00 31.68 ?  254 HIS C CD2   1 
ATOM   13066 C  CE1   . HIS C 2 275 ? 93.963  95.216  109.002 1.00 33.55 ?  254 HIS C CE1   1 
ATOM   13067 N  NE2   . HIS C 2 275 ? 93.867  96.029  107.967 1.00 33.71 ?  254 HIS C NE2   1 
ATOM   13068 N  N     . ASP C 2 276 ? 96.899  99.610  110.669 1.00 25.93 ?  255 ASP C N     1 
ATOM   13069 C  CA    . ASP C 2 276 ? 98.162  99.868  109.983 1.00 26.65 ?  255 ASP C CA    1 
ATOM   13070 C  C     . ASP C 2 276 ? 99.370  99.424  110.808 1.00 25.61 ?  255 ASP C C     1 
ATOM   13071 O  O     . ASP C 2 276 ? 100.277 98.768  110.279 1.00 25.34 ?  255 ASP C O     1 
ATOM   13072 C  CB    . ASP C 2 276 ? 98.283  101.350 109.623 1.00 27.44 ?  255 ASP C CB    1 
ATOM   13073 C  CG    . ASP C 2 276 ? 98.243  101.586 108.129 1.00 32.09 ?  255 ASP C CG    1 
ATOM   13074 O  OD1   . ASP C 2 276 ? 98.922  100.832 107.390 1.00 36.67 ?  255 ASP C OD1   1 
ATOM   13075 O  OD2   . ASP C 2 276 ? 97.526  102.514 107.687 1.00 36.30 -1 255 ASP C OD2   1 
ATOM   13076 N  N     . VAL C 2 277 ? 99.371  99.784  112.096 1.00 24.17 ?  256 VAL C N     1 
ATOM   13077 C  CA    . VAL C 2 277 ? 100.446 99.392  113.017 1.00 23.71 ?  256 VAL C CA    1 
ATOM   13078 C  C     . VAL C 2 277 ? 100.521 97.868  113.149 1.00 23.48 ?  256 VAL C C     1 
ATOM   13079 O  O     . VAL C 2 277 ? 101.613 97.297  113.166 1.00 23.08 ?  256 VAL C O     1 
ATOM   13080 C  CB    . VAL C 2 277 ? 100.283 100.025 114.427 1.00 23.27 ?  256 VAL C CB    1 
ATOM   13081 C  CG1   . VAL C 2 277 ? 101.423 99.595  115.355 1.00 24.02 ?  256 VAL C CG1   1 
ATOM   13082 C  CG2   . VAL C 2 277 ? 100.223 101.544 114.340 1.00 23.35 ?  256 VAL C CG2   1 
ATOM   13083 N  N     . LYS C 2 278 ? 99.365  97.217  113.240 1.00 23.36 ?  257 LYS C N     1 
ATOM   13084 C  CA    . LYS C 2 278 ? 99.304  95.757  113.318 1.00 24.12 ?  257 LYS C CA    1 
ATOM   13085 C  C     . LYS C 2 278 ? 99.996  95.074  112.141 1.00 24.30 ?  257 LYS C C     1 
ATOM   13086 O  O     . LYS C 2 278 ? 100.707 94.075  112.321 1.00 24.37 ?  257 LYS C O     1 
ATOM   13087 C  CB    . LYS C 2 278 ? 97.860  95.271  113.436 1.00 24.22 ?  257 LYS C CB    1 
ATOM   13088 C  CG    . LYS C 2 278 ? 97.240  95.505  114.803 1.00 24.96 ?  257 LYS C CG    1 
ATOM   13089 C  CD    . LYS C 2 278 ? 95.766  95.122  114.766 1.00 26.34 ?  257 LYS C CD    1 
ATOM   13090 C  CE    . LYS C 2 278 ? 95.095  95.377  116.088 1.00 27.16 ?  257 LYS C CE    1 
ATOM   13091 N  NZ    . LYS C 2 278 ? 93.660  94.973  115.987 1.00 29.60 1  257 LYS C NZ    1 
ATOM   13092 N  N     . LYS C 2 279 ? 99.797  95.611  110.938 1.00 24.55 ?  258 LYS C N     1 
ATOM   13093 C  CA    . LYS C 2 279 ? 100.484 95.092  109.760 1.00 24.85 ?  258 LYS C CA    1 
ATOM   13094 C  C     . LYS C 2 279 ? 101.996 95.249  109.912 1.00 24.57 ?  258 LYS C C     1 
ATOM   13095 O  O     . LYS C 2 279 ? 102.752 94.345  109.557 1.00 24.07 ?  258 LYS C O     1 
ATOM   13096 C  CB    . LYS C 2 279 ? 100.007 95.806  108.495 1.00 25.30 ?  258 LYS C CB    1 
ATOM   13097 C  CG    . LYS C 2 279 ? 98.534  95.629  108.206 1.00 26.63 ?  258 LYS C CG    1 
ATOM   13098 C  CD    . LYS C 2 279 ? 98.171  96.385  106.933 1.00 29.30 ?  258 LYS C CD    1 
ATOM   13099 C  CE    . LYS C 2 279 ? 96.755  96.103  106.532 1.00 31.79 ?  258 LYS C CE    1 
ATOM   13100 N  NZ    . LYS C 2 279 ? 96.323  97.097  105.518 1.00 33.80 1  258 LYS C NZ    1 
ATOM   13101 N  N     . PHE C 2 280 ? 102.418 96.386  110.467 1.00 24.29 ?  259 PHE C N     1 
ATOM   13102 C  CA    . PHE C 2 280 ? 103.840 96.692  110.669 1.00 24.90 ?  259 PHE C CA    1 
ATOM   13103 C  C     . PHE C 2 280 ? 104.507 95.735  111.673 1.00 24.86 ?  259 PHE C C     1 
ATOM   13104 O  O     . PHE C 2 280 ? 105.623 95.257  111.441 1.00 24.68 ?  259 PHE C O     1 
ATOM   13105 C  CB    . PHE C 2 280 ? 103.988 98.159  111.099 1.00 24.70 ?  259 PHE C CB    1 
ATOM   13106 C  CG    . PHE C 2 280 ? 105.408 98.676  111.112 1.00 25.70 ?  259 PHE C CG    1 
ATOM   13107 C  CD1   . PHE C 2 280 ? 106.190 98.662  109.956 1.00 26.86 ?  259 PHE C CD1   1 
ATOM   13108 C  CD2   . PHE C 2 280 ? 105.949 99.223  112.282 1.00 26.19 ?  259 PHE C CD2   1 
ATOM   13109 C  CE1   . PHE C 2 280 ? 107.499 99.165  109.964 1.00 26.66 ?  259 PHE C CE1   1 
ATOM   13110 C  CE2   . PHE C 2 280 ? 107.251 99.734  112.298 1.00 26.52 ?  259 PHE C CE2   1 
ATOM   13111 C  CZ    . PHE C 2 280 ? 108.030 99.699  111.134 1.00 26.23 ?  259 PHE C CZ    1 
ATOM   13112 N  N     . ILE C 2 281 ? 103.820 95.449  112.780 1.00 25.53 ?  260 ILE C N     1 
ATOM   13113 C  CA    . ILE C 2 281 ? 104.378 94.551  113.793 1.00 26.21 ?  260 ILE C CA    1 
ATOM   13114 C  C     . ILE C 2 281 ? 104.471 93.102  113.293 1.00 26.47 ?  260 ILE C C     1 
ATOM   13115 O  O     . ILE C 2 281 ? 105.407 92.392  113.643 1.00 26.52 ?  260 ILE C O     1 
ATOM   13116 C  CB    . ILE C 2 281 ? 103.682 94.669  115.193 1.00 26.27 ?  260 ILE C CB    1 
ATOM   13117 C  CG1   . ILE C 2 281 ? 102.341 93.933  115.232 1.00 27.37 ?  260 ILE C CG1   1 
ATOM   13118 C  CG2   . ILE C 2 281 ? 103.557 96.151  115.612 1.00 26.92 ?  260 ILE C CG2   1 
ATOM   13119 C  CD1   . ILE C 2 281 ? 101.650 93.955  116.596 1.00 29.51 ?  260 ILE C CD1   1 
ATOM   13120 N  N     . ARG C 2 282 ? 103.527 92.689  112.445 1.00 26.57 ?  261 ARG C N     1 
ATOM   13121 C  CA    . ARG C 2 282 ? 103.586 91.360  111.829 1.00 26.84 ?  261 ARG C CA    1 
ATOM   13122 C  C     . ARG C 2 282 ? 104.780 91.250  110.881 1.00 27.34 ?  261 ARG C C     1 
ATOM   13123 O  O     . ARG C 2 282 ? 105.500 90.256  110.898 1.00 27.54 ?  261 ARG C O     1 
ATOM   13124 C  CB    . ARG C 2 282 ? 102.281 91.011  111.109 1.00 26.98 ?  261 ARG C CB    1 
ATOM   13125 C  CG    . ARG C 2 282 ? 101.163 90.555  112.026 1.00 26.53 ?  261 ARG C CG    1 
ATOM   13126 C  CD    . ARG C 2 282 ? 99.987  89.949  111.234 1.00 27.77 ?  261 ARG C CD    1 
ATOM   13127 N  NE    . ARG C 2 282 ? 99.246  90.947  110.468 1.00 28.67 ?  261 ARG C NE    1 
ATOM   13128 C  CZ    . ARG C 2 282 ? 98.254  91.694  110.956 1.00 29.68 ?  261 ARG C CZ    1 
ATOM   13129 N  NH1   . ARG C 2 282 ? 97.865  91.568  112.224 1.00 28.31 1  261 ARG C NH1   1 
ATOM   13130 N  NH2   . ARG C 2 282 ? 97.641  92.567  110.172 1.00 29.15 ?  261 ARG C NH2   1 
ATOM   13131 N  N     . TYR C 2 283 ? 104.980 92.288  110.072 1.00 27.78 ?  262 TYR C N     1 
ATOM   13132 C  CA    . TYR C 2 283 ? 106.149 92.415  109.204 1.00 28.18 ?  262 TYR C CA    1 
ATOM   13133 C  C     . TYR C 2 283 ? 107.455 92.231  109.998 1.00 27.08 ?  262 TYR C C     1 
ATOM   13134 O  O     . TYR C 2 283 ? 108.334 91.438  109.624 1.00 26.51 ?  262 TYR C O     1 
ATOM   13135 C  CB    . TYR C 2 283 ? 106.128 93.790  108.524 1.00 29.11 ?  262 TYR C CB    1 
ATOM   13136 C  CG    . TYR C 2 283 ? 107.275 94.049  107.579 1.00 32.56 ?  262 TYR C CG    1 
ATOM   13137 C  CD1   . TYR C 2 283 ? 107.305 93.458  106.314 1.00 36.59 ?  262 TYR C CD1   1 
ATOM   13138 C  CD2   . TYR C 2 283 ? 108.326 94.899  107.939 1.00 36.34 ?  262 TYR C CD2   1 
ATOM   13139 C  CE1   . TYR C 2 283 ? 108.361 93.696  105.428 1.00 39.47 ?  262 TYR C CE1   1 
ATOM   13140 C  CE2   . TYR C 2 283 ? 109.390 95.149  107.052 1.00 39.23 ?  262 TYR C CE2   1 
ATOM   13141 C  CZ    . TYR C 2 283 ? 109.396 94.540  105.802 1.00 40.48 ?  262 TYR C CZ    1 
ATOM   13142 O  OH    . TYR C 2 283 ? 110.430 94.767  104.921 1.00 44.00 ?  262 TYR C OH    1 
ATOM   13143 N  N     . ASN C 2 284 ? 107.562 92.946  111.110 1.00 26.08 ?  263 ASN C N     1 
ATOM   13144 C  CA    . ASN C 2 284 ? 108.753 92.865  111.942 1.00 25.73 ?  263 ASN C CA    1 
ATOM   13145 C  C     . ASN C 2 284 ? 108.887 91.572  112.749 1.00 25.24 ?  263 ASN C C     1 
ATOM   13146 O  O     . ASN C 2 284 ? 110.011 91.105  112.979 1.00 25.56 ?  263 ASN C O     1 
ATOM   13147 C  CB    . ASN C 2 284 ? 108.884 94.121  112.804 1.00 25.69 ?  263 ASN C CB    1 
ATOM   13148 C  CG    . ASN C 2 284 ? 109.340 95.315  111.996 1.00 26.39 ?  263 ASN C CG    1 
ATOM   13149 O  OD1   . ASN C 2 284 ? 110.517 95.425  111.642 1.00 26.91 ?  263 ASN C OD1   1 
ATOM   13150 N  ND2   . ASN C 2 284 ? 108.415 96.212  111.690 1.00 27.56 ?  263 ASN C ND2   1 
ATOM   13151 N  N     . ALA C 2 285 ? 107.762 90.975  113.152 1.00 24.51 ?  264 ALA C N     1 
ATOM   13152 C  CA    . ALA C 2 285 ? 107.785 89.617  113.728 1.00 24.19 ?  264 ALA C CA    1 
ATOM   13153 C  C     . ALA C 2 285 ? 108.487 88.606  112.799 1.00 24.63 ?  264 ALA C C     1 
ATOM   13154 O  O     . ALA C 2 285 ? 109.284 87.787  113.254 1.00 24.01 ?  264 ALA C O     1 
ATOM   13155 C  CB    . ALA C 2 285 ? 106.384 89.136  114.057 1.00 23.63 ?  264 ALA C CB    1 
ATOM   13156 N  N     . ASN C 2 286 ? 108.186 88.673  111.503 1.00 24.66 ?  265 ASN C N     1 
ATOM   13157 C  CA    . ASN C 2 286 ? 108.859 87.835  110.510 1.00 25.24 ?  265 ASN C CA    1 
ATOM   13158 C  C     . ASN C 2 286 ? 110.367 88.053  110.435 1.00 25.09 ?  265 ASN C C     1 
ATOM   13159 O  O     . ASN C 2 286 ? 111.120 87.088  110.223 1.00 24.14 ?  265 ASN C O     1 
ATOM   13160 C  CB    . ASN C 2 286 ? 108.234 88.011  109.114 1.00 25.62 ?  265 ASN C CB    1 
ATOM   13161 C  CG    . ASN C 2 286 ? 106.884 87.324  108.991 1.00 26.46 ?  265 ASN C CG    1 
ATOM   13162 O  OD1   . ASN C 2 286 ? 106.493 86.531  109.851 1.00 27.14 ?  265 ASN C OD1   1 
ATOM   13163 N  ND2   . ASN C 2 286 ? 106.151 87.642  107.921 1.00 27.89 ?  265 ASN C ND2   1 
ATOM   13164 N  N     . LYS C 2 287 ? 110.789 89.311  110.589 1.00 24.99 ?  266 LYS C N     1 
ATOM   13165 C  CA    . LYS C 2 287 ? 112.207 89.676  110.628 1.00 25.91 ?  266 LYS C CA    1 
ATOM   13166 C  C     . LYS C 2 287 ? 112.882 89.115  111.876 1.00 25.23 ?  266 LYS C C     1 
ATOM   13167 O  O     . LYS C 2 287 ? 114.024 88.655  111.810 1.00 25.34 ?  266 LYS C O     1 
ATOM   13168 C  CB    . LYS C 2 287 ? 112.396 91.193  110.612 1.00 25.96 ?  266 LYS C CB    1 
ATOM   13169 C  CG    . LYS C 2 287 ? 112.165 91.876  109.274 1.00 29.60 ?  266 LYS C CG    1 
ATOM   13170 C  CD    . LYS C 2 287 ? 112.651 93.328  109.370 1.00 34.20 ?  266 LYS C CD    1 
ATOM   13171 C  CE    . LYS C 2 287 ? 112.552 94.059  108.055 1.00 37.67 ?  266 LYS C CE    1 
ATOM   13172 N  NZ    . LYS C 2 287 ? 113.169 95.421  108.178 1.00 39.48 1  266 LYS C NZ    1 
ATOM   13173 N  N     . ALA C 2 288 ? 112.185 89.169  113.008 1.00 24.87 ?  267 ALA C N     1 
ATOM   13174 C  CA    . ALA C 2 288 ? 112.685 88.553  114.251 1.00 24.23 ?  267 ALA C CA    1 
ATOM   13175 C  C     . ALA C 2 288 ? 112.868 87.038  114.091 1.00 24.24 ?  267 ALA C C     1 
ATOM   13176 O  O     . ALA C 2 288 ? 113.907 86.490  114.464 1.00 23.96 ?  267 ALA C O     1 
ATOM   13177 C  CB    . ALA C 2 288 ? 111.757 88.858  115.412 1.00 24.23 ?  267 ALA C CB    1 
ATOM   13178 N  N     . LEU C 2 289 ? 111.864 86.364  113.531 1.00 24.63 ?  268 LEU C N     1 
ATOM   13179 C  CA    . LEU C 2 289 ? 111.975 84.929  113.258 1.00 25.14 ?  268 LEU C CA    1 
ATOM   13180 C  C     . LEU C 2 289 ? 113.161 84.647  112.350 1.00 25.58 ?  268 LEU C C     1 
ATOM   13181 O  O     . LEU C 2 289 ? 113.931 83.727  112.602 1.00 25.42 ?  268 LEU C O     1 
ATOM   13182 C  CB    . LEU C 2 289 ? 110.684 84.359  112.650 1.00 25.28 ?  268 LEU C CB    1 
ATOM   13183 C  CG    . LEU C 2 289 ? 109.515 84.201  113.626 1.00 25.93 ?  268 LEU C CG    1 
ATOM   13184 C  CD1   . LEU C 2 289 ? 108.201 84.076  112.880 1.00 26.50 ?  268 LEU C CD1   1 
ATOM   13185 C  CD2   . LEU C 2 289 ? 109.718 83.029  114.604 1.00 25.20 ?  268 LEU C CD2   1 
ATOM   13186 N  N     . MET C 2 290 ? 113.321 85.455  111.301 1.00 26.32 ?  269 MET C N     1 
ATOM   13187 C  CA    . MET C 2 290 ? 114.444 85.264  110.388 1.00 27.41 ?  269 MET C CA    1 
ATOM   13188 C  C     . MET C 2 290 ? 115.800 85.459  111.064 1.00 26.66 ?  269 MET C C     1 
ATOM   13189 O  O     . MET C 2 290 ? 116.741 84.714  110.782 1.00 26.69 ?  269 MET C O     1 
ATOM   13190 C  CB    . MET C 2 290 ? 114.295 86.126  109.139 1.00 28.28 ?  269 MET C CB    1 
ATOM   13191 C  CG    . MET C 2 290 ? 113.550 85.382  108.032 1.00 32.91 ?  269 MET C CG    1 
ATOM   13192 S  SD    . MET C 2 290 ? 113.051 86.450  106.678 1.00 42.49 ?  269 MET C SD    1 
ATOM   13193 C  CE    . MET C 2 290 ? 111.286 86.571  106.968 1.00 38.74 ?  269 MET C CE    1 
ATOM   13194 N  N     . ASN C 2 291 ? 115.884 86.430  111.975 1.00 25.48 ?  270 ASN C N     1 
ATOM   13195 C  CA    . ASN C 2 291 ? 117.097 86.651  112.778 1.00 25.39 ?  270 ASN C CA    1 
ATOM   13196 C  C     . ASN C 2 291 ? 117.464 85.422  113.626 1.00 25.18 ?  270 ASN C C     1 
ATOM   13197 O  O     . ASN C 2 291 ? 118.640 85.202  113.952 1.00 24.73 ?  270 ASN C O     1 
ATOM   13198 C  CB    . ASN C 2 291 ? 116.941 87.890  113.671 1.00 24.83 ?  270 ASN C CB    1 
ATOM   13199 C  CG    . ASN C 2 291 ? 117.056 89.203  112.889 1.00 25.58 ?  270 ASN C CG    1 
ATOM   13200 O  OD1   . ASN C 2 291 ? 117.485 89.224  111.740 1.00 25.58 ?  270 ASN C OD1   1 
ATOM   13201 N  ND2   . ASN C 2 291 ? 116.670 90.300  113.522 1.00 24.32 ?  270 ASN C ND2   1 
ATOM   13202 N  N     . LEU C 2 292 ? 116.443 84.622  113.945 1.00 25.09 ?  271 LEU C N     1 
ATOM   13203 C  CA    . LEU C 2 292 ? 116.586 83.361  114.685 1.00 25.46 ?  271 LEU C CA    1 
ATOM   13204 C  C     . LEU C 2 292 ? 116.763 82.120  113.795 1.00 26.18 ?  271 LEU C C     1 
ATOM   13205 O  O     . LEU C 2 292 ? 116.868 80.985  114.295 1.00 26.06 ?  271 LEU C O     1 
ATOM   13206 C  CB    . LEU C 2 292 ? 115.392 83.181  115.631 1.00 25.19 ?  271 LEU C CB    1 
ATOM   13207 C  CG    . LEU C 2 292 ? 115.289 84.209  116.771 1.00 25.03 ?  271 LEU C CG    1 
ATOM   13208 C  CD1   . LEU C 2 292 ? 113.938 84.123  117.444 1.00 24.50 ?  271 LEU C CD1   1 
ATOM   13209 C  CD2   . LEU C 2 292 ? 116.423 83.998  117.788 1.00 25.64 ?  271 LEU C CD2   1 
ATOM   13210 N  N     . GLY C 2 293 ? 116.801 82.334  112.480 1.00 26.71 ?  272 GLY C N     1 
ATOM   13211 C  CA    . GLY C 2 293 ? 116.948 81.238  111.514 1.00 28.06 ?  272 GLY C CA    1 
ATOM   13212 C  C     . GLY C 2 293 ? 115.678 80.446  111.241 1.00 29.34 ?  272 GLY C C     1 
ATOM   13213 O  O     . GLY C 2 293 ? 115.741 79.294  110.787 1.00 29.73 ?  272 GLY C O     1 
ATOM   13214 N  N     . PHE C 2 294 ? 114.527 81.057  111.515 1.00 29.88 ?  273 PHE C N     1 
ATOM   13215 C  CA    . PHE C 2 294 ? 113.231 80.415  111.310 1.00 31.24 ?  273 PHE C CA    1 
ATOM   13216 C  C     . PHE C 2 294 ? 112.485 81.037  110.121 1.00 32.42 ?  273 PHE C C     1 
ATOM   13217 O  O     . PHE C 2 294 ? 112.756 82.181  109.730 1.00 32.30 ?  273 PHE C O     1 
ATOM   13218 C  CB    . PHE C 2 294 ? 112.373 80.496  112.580 1.00 30.82 ?  273 PHE C CB    1 
ATOM   13219 C  CG    . PHE C 2 294 ? 112.983 79.812  113.785 1.00 30.93 ?  273 PHE C CG    1 
ATOM   13220 C  CD1   . PHE C 2 294 ? 113.496 78.518  113.698 1.00 30.85 ?  273 PHE C CD1   1 
ATOM   13221 C  CD2   . PHE C 2 294 ? 113.031 80.461  115.010 1.00 30.30 ?  273 PHE C CD2   1 
ATOM   13222 C  CE1   . PHE C 2 294 ? 114.061 77.895  114.809 1.00 30.75 ?  273 PHE C CE1   1 
ATOM   13223 C  CE2   . PHE C 2 294 ? 113.581 79.842  116.135 1.00 30.41 ?  273 PHE C CE2   1 
ATOM   13224 C  CZ    . PHE C 2 294 ? 114.092 78.555  116.036 1.00 30.88 ?  273 PHE C CZ    1 
ATOM   13225 N  N     . ASP C 2 295 ? 111.564 80.268  109.546 1.00 33.81 ?  274 ASP C N     1 
ATOM   13226 C  CA    . ASP C 2 295 ? 110.717 80.736  108.444 1.00 35.32 ?  274 ASP C CA    1 
ATOM   13227 C  C     . ASP C 2 295 ? 109.718 81.809  108.912 1.00 35.36 ?  274 ASP C C     1 
ATOM   13228 O  O     . ASP C 2 295 ? 109.273 81.774  110.056 1.00 34.78 ?  274 ASP C O     1 
ATOM   13229 C  CB    . ASP C 2 295 ? 109.938 79.559  107.840 1.00 35.95 ?  274 ASP C CB    1 
ATOM   13230 C  CG    . ASP C 2 295 ? 110.842 78.509  107.200 1.00 37.98 ?  274 ASP C CG    1 
ATOM   13231 O  OD1   . ASP C 2 295 ? 111.957 78.844  106.745 1.00 39.83 ?  274 ASP C OD1   1 
ATOM   13232 O  OD2   . ASP C 2 295 ? 110.422 77.332  107.152 1.00 40.03 -1 274 ASP C OD2   1 
ATOM   13233 N  N     . PRO C 2 296 ? 109.356 82.756  108.025 1.00 36.33 ?  275 PRO C N     1 
ATOM   13234 C  CA    . PRO C 2 296 ? 108.305 83.743  108.358 1.00 36.92 ?  275 PRO C CA    1 
ATOM   13235 C  C     . PRO C 2 296 ? 106.977 83.082  108.761 1.00 37.68 ?  275 PRO C C     1 
ATOM   13236 O  O     . PRO C 2 296 ? 106.616 82.037  108.214 1.00 38.07 ?  275 PRO C O     1 
ATOM   13237 C  CB    . PRO C 2 296 ? 108.138 84.542  107.056 1.00 36.82 ?  275 PRO C CB    1 
ATOM   13238 C  CG    . PRO C 2 296 ? 108.860 83.736  105.985 1.00 37.42 ?  275 PRO C CG    1 
ATOM   13239 C  CD    . PRO C 2 296 ? 109.953 83.015  106.702 1.00 36.41 ?  275 PRO C CD    1 
ATOM   13240 N  N     . TYR C 2 297 ? 106.267 83.691  109.711 1.00 38.10 ?  276 TYR C N     1 
ATOM   13241 C  CA    . TYR C 2 297 ? 105.047 83.110  110.291 1.00 38.96 ?  276 TYR C CA    1 
ATOM   13242 C  C     . TYR C 2 297 ? 103.769 83.819  109.824 1.00 39.71 ?  276 TYR C C     1 
ATOM   13243 O  O     . TYR C 2 297 ? 102.697 83.208  109.767 1.00 40.18 ?  276 TYR C O     1 
ATOM   13244 C  CB    . TYR C 2 297 ? 105.143 83.161  111.819 1.00 38.94 ?  276 TYR C CB    1 
ATOM   13245 C  CG    . TYR C 2 297 ? 104.028 82.512  112.611 1.00 39.64 ?  276 TYR C CG    1 
ATOM   13246 C  CD1   . TYR C 2 297 ? 104.014 81.135  112.845 1.00 40.43 ?  276 TYR C CD1   1 
ATOM   13247 C  CD2   . TYR C 2 297 ? 103.019 83.282  113.181 1.00 41.04 ?  276 TYR C CD2   1 
ATOM   13248 C  CE1   . TYR C 2 297 ? 102.996 80.540  113.592 1.00 41.69 ?  276 TYR C CE1   1 
ATOM   13249 C  CE2   . TYR C 2 297 ? 101.995 82.700  113.928 1.00 41.60 ?  276 TYR C CE2   1 
ATOM   13250 C  CZ    . TYR C 2 297 ? 101.992 81.331  114.134 1.00 41.92 ?  276 TYR C CZ    1 
ATOM   13251 O  OH    . TYR C 2 297 ? 100.984 80.762  114.882 1.00 42.52 ?  276 TYR C OH    1 
ATOM   13252 N  N     . PHE C 2 298 ? 103.879 85.104  109.507 1.00 39.85 ?  277 PHE C N     1 
ATOM   13253 C  CA    . PHE C 2 298 ? 102.725 85.878  109.066 1.00 40.77 ?  277 PHE C CA    1 
ATOM   13254 C  C     . PHE C 2 298 ? 102.788 86.130  107.568 1.00 41.95 ?  277 PHE C C     1 
ATOM   13255 O  O     . PHE C 2 298 ? 103.876 86.235  107.003 1.00 41.91 ?  277 PHE C O     1 
ATOM   13256 C  CB    . PHE C 2 298 ? 102.651 87.208  109.824 1.00 39.94 ?  277 PHE C CB    1 
ATOM   13257 C  CG    . PHE C 2 298 ? 102.446 87.057  111.307 1.00 39.09 ?  277 PHE C CG    1 
ATOM   13258 C  CD1   . PHE C 2 298 ? 103.488 87.300  112.193 1.00 37.84 ?  277 PHE C CD1   1 
ATOM   13259 C  CD2   . PHE C 2 298 ? 101.205 86.686  111.819 1.00 38.97 ?  277 PHE C CD2   1 
ATOM   13260 C  CE1   . PHE C 2 298 ? 103.307 87.169  113.567 1.00 37.46 ?  277 PHE C CE1   1 
ATOM   13261 C  CE2   . PHE C 2 298 ? 101.010 86.551  113.188 1.00 38.20 ?  277 PHE C CE2   1 
ATOM   13262 C  CZ    . PHE C 2 298 ? 102.064 86.794  114.067 1.00 37.91 ?  277 PHE C CZ    1 
ATOM   13263 N  N     . GLU C 2 299 ? 101.628 86.223  106.917 1.00 43.74 ?  278 GLU C N     1 
ATOM   13264 C  CA    . GLU C 2 299 ? 101.598 86.513  105.480 1.00 45.61 ?  278 GLU C CA    1 
ATOM   13265 C  C     . GLU C 2 299 ? 101.969 87.973  105.218 1.00 46.04 ?  278 GLU C C     1 
ATOM   13266 O  O     . GLU C 2 299 ? 101.715 88.847  106.047 1.00 45.88 ?  278 GLU C O     1 
ATOM   13267 C  CB    . GLU C 2 299 ? 100.234 86.190  104.861 1.00 46.43 ?  278 GLU C CB    1 
ATOM   13268 C  CG    . GLU C 2 299 ? 100.322 85.755  103.388 1.00 48.82 ?  278 GLU C CG    1 
ATOM   13269 C  CD    . GLU C 2 299 ? 99.013  85.911  102.629 1.00 51.86 ?  278 GLU C CD    1 
ATOM   13270 O  OE1   . GLU C 2 299 ? 98.994  85.597  101.417 1.00 53.35 ?  278 GLU C OE1   1 
ATOM   13271 O  OE2   . GLU C 2 299 ? 98.004  86.350  103.230 1.00 53.10 -1 278 GLU C OE2   1 
ATOM   13272 N  N     . GLU C 2 300 ? 102.585 88.222  104.063 1.00 47.16 ?  279 GLU C N     1 
ATOM   13273 C  CA    . GLU C 2 300 ? 102.989 89.571  103.654 1.00 47.75 ?  279 GLU C CA    1 
ATOM   13274 C  C     . GLU C 2 300 ? 101.789 90.500  103.414 1.00 47.71 ?  279 GLU C C     1 
ATOM   13275 O  O     . GLU C 2 300 ? 100.760 90.073  102.879 1.00 47.77 ?  279 GLU C O     1 
ATOM   13276 C  CB    . GLU C 2 300 ? 103.892 89.505  102.409 1.00 48.42 ?  279 GLU C CB    1 
ATOM   13277 C  CG    . GLU C 2 300 ? 103.333 88.666  101.254 1.00 50.63 ?  279 GLU C CG    1 
ATOM   13278 C  CD    . GLU C 2 300 ? 104.415 88.158  100.301 1.00 53.06 ?  279 GLU C CD    1 
ATOM   13279 O  OE1   . GLU C 2 300 ? 105.208 88.984  99.788  1.00 54.35 ?  279 GLU C OE1   1 
ATOM   13280 O  OE2   . GLU C 2 300 ? 104.463 86.931  100.056 1.00 53.32 -1 279 GLU C OE2   1 
ATOM   13281 N  N     . GLU C 2 301 ? 101.932 91.757  103.836 1.00 47.40 ?  280 GLU C N     1 
ATOM   13282 C  CA    . GLU C 2 301 ? 100.904 92.791  103.659 1.00 47.46 ?  280 GLU C CA    1 
ATOM   13283 C  C     . GLU C 2 301 ? 101.545 94.121  103.243 1.00 47.31 ?  280 GLU C C     1 
ATOM   13284 O  O     . GLU C 2 301 ? 102.728 94.352  103.509 1.00 47.21 ?  280 GLU C O     1 
ATOM   13285 C  CB    . GLU C 2 301 ? 100.109 92.999  104.956 1.00 47.19 ?  280 GLU C CB    1 
ATOM   13286 C  CG    . GLU C 2 301 ? 99.343  91.780  105.474 1.00 47.14 ?  280 GLU C CG    1 
ATOM   13287 C  CD    . GLU C 2 301 ? 99.020  91.885  106.961 1.00 47.21 ?  280 GLU C CD    1 
ATOM   13288 O  OE1   . GLU C 2 301 ? 97.841  92.119  107.296 1.00 46.97 ?  280 GLU C OE1   1 
ATOM   13289 O  OE2   . GLU C 2 301 ? 99.947  91.745  107.795 1.00 46.13 -1 280 GLU C OE2   1 
ATOM   13290 N  N     . ASP C 2 302 ? 100.765 94.990  102.600 1.00 47.15 ?  281 ASP C N     1 
ATOM   13291 C  CA    . ASP C 2 302 ? 101.251 96.318  102.209 1.00 47.04 ?  281 ASP C CA    1 
ATOM   13292 C  C     . ASP C 2 302 ? 101.336 97.244  103.427 1.00 46.05 ?  281 ASP C C     1 
ATOM   13293 O  O     . ASP C 2 302 ? 100.323 97.518  104.080 1.00 46.10 ?  281 ASP C O     1 
ATOM   13294 C  CB    . ASP C 2 302 ? 100.352 96.950  101.131 1.00 47.66 ?  281 ASP C CB    1 
ATOM   13295 C  CG    . ASP C 2 302 ? 100.521 96.305  99.752  1.00 49.53 ?  281 ASP C CG    1 
ATOM   13296 O  OD1   . ASP C 2 302 ? 101.647 95.884  99.404  1.00 50.58 ?  281 ASP C OD1   1 
ATOM   13297 O  OD2   . ASP C 2 302 ? 99.517  96.244  99.000  1.00 51.14 -1 281 ASP C OD2   1 
ATOM   13298 N  N     . ILE C 2 303 ? 102.547 97.706  103.730 1.00 44.96 ?  282 ILE C N     1 
ATOM   13299 C  CA    . ILE C 2 303 ? 102.785 98.658  104.820 1.00 43.99 ?  282 ILE C CA    1 
ATOM   13300 C  C     . ILE C 2 303 ? 102.560 100.087 104.314 1.00 43.53 ?  282 ILE C C     1 
ATOM   13301 O  O     . ILE C 2 303 ? 102.830 100.378 103.148 1.00 43.52 ?  282 ILE C O     1 
ATOM   13302 C  CB    . ILE C 2 303 ? 104.227 98.517  105.391 1.00 43.84 ?  282 ILE C CB    1 
ATOM   13303 C  CG1   . ILE C 2 303 ? 104.518 97.069  105.827 1.00 43.91 ?  282 ILE C CG1   1 
ATOM   13304 C  CG2   . ILE C 2 303 ? 104.487 99.522  106.527 1.00 43.55 ?  282 ILE C CG2   1 
ATOM   13305 C  CD1   . ILE C 2 303 ? 103.577 96.504  106.895 1.00 42.76 ?  282 ILE C CD1   1 
ATOM   13306 N  N     . ASN C 2 304 ? 102.057 100.963 105.185 1.00 42.51 ?  283 ASN C N     1 
ATOM   13307 C  CA    . ASN C 2 304 ? 101.852 102.370 104.840 1.00 41.93 ?  283 ASN C CA    1 
ATOM   13308 C  C     . ASN C 2 304 ? 103.122 102.959 104.207 1.00 41.78 ?  283 ASN C C     1 
ATOM   13309 O  O     . ASN C 2 304 ? 104.189 102.941 104.836 1.00 41.13 ?  283 ASN C O     1 
ATOM   13310 C  CB    . ASN C 2 304 ? 101.448 103.171 106.087 1.00 41.83 ?  283 ASN C CB    1 
ATOM   13311 C  CG    . ASN C 2 304 ? 100.752 104.491 105.754 1.00 41.27 ?  283 ASN C CG    1 
ATOM   13312 O  OD1   . ASN C 2 304 ? 101.185 105.242 104.883 1.00 41.28 ?  283 ASN C OD1   1 
ATOM   13313 N  ND2   . ASN C 2 304 ? 99.670  104.776 106.462 1.00 40.67 ?  283 ASN C ND2   1 
ATOM   13314 N  N     . PRO C 2 305 ? 103.019 103.464 102.953 1.00 41.74 ?  284 PRO C N     1 
ATOM   13315 C  CA    . PRO C 2 305 ? 104.210 103.974 102.254 1.00 41.82 ?  284 PRO C CA    1 
ATOM   13316 C  C     . PRO C 2 305 ? 104.849 105.179 102.954 1.00 41.56 ?  284 PRO C C     1 
ATOM   13317 O  O     . PRO C 2 305 ? 106.037 105.443 102.759 1.00 41.46 ?  284 PRO C O     1 
ATOM   13318 C  CB    . PRO C 2 305 ? 103.681 104.355 100.858 1.00 42.14 ?  284 PRO C CB    1 
ATOM   13319 C  CG    . PRO C 2 305 ? 102.215 104.517 101.023 1.00 42.59 ?  284 PRO C CG    1 
ATOM   13320 C  CD    . PRO C 2 305 ? 101.810 103.552 102.111 1.00 42.05 ?  284 PRO C CD    1 
ATOM   13321 N  N     . ILE C 2 306 ? 104.066 105.883 103.768 1.00 41.19 ?  285 ILE C N     1 
ATOM   13322 C  CA    . ILE C 2 306 ? 104.572 106.983 104.590 1.00 41.47 ?  285 ILE C CA    1 
ATOM   13323 C  C     . ILE C 2 306 ? 105.653 106.474 105.553 1.00 41.71 ?  285 ILE C C     1 
ATOM   13324 O  O     . ILE C 2 306 ? 106.717 107.078 105.678 1.00 41.38 ?  285 ILE C O     1 
ATOM   13325 C  CB    . ILE C 2 306 ? 103.433 107.660 105.397 1.00 41.22 ?  285 ILE C CB    1 
ATOM   13326 C  CG1   . ILE C 2 306 ? 102.392 108.278 104.454 1.00 41.27 ?  285 ILE C CG1   1 
ATOM   13327 C  CG2   . ILE C 2 306 ? 103.992 108.701 106.364 1.00 40.37 ?  285 ILE C CG2   1 
ATOM   13328 C  CD1   . ILE C 2 306 ? 101.075 108.624 105.136 1.00 41.85 ?  285 ILE C CD1   1 
ATOM   13329 N  N     . VAL C 2 307 ? 105.361 105.358 106.221 1.00 42.33 ?  286 VAL C N     1 
ATOM   13330 C  CA    . VAL C 2 307 ? 106.297 104.722 107.154 1.00 43.36 ?  286 VAL C CA    1 
ATOM   13331 C  C     . VAL C 2 307 ? 107.564 104.222 106.447 1.00 44.51 ?  286 VAL C C     1 
ATOM   13332 O  O     . VAL C 2 307 ? 108.652 104.279 107.016 1.00 44.57 ?  286 VAL C O     1 
ATOM   13333 C  CB    . VAL C 2 307 ? 105.601 103.598 107.959 1.00 42.97 ?  286 VAL C CB    1 
ATOM   13334 C  CG1   . VAL C 2 307 ? 106.620 102.693 108.671 1.00 42.86 ?  286 VAL C CG1   1 
ATOM   13335 C  CG2   . VAL C 2 307 ? 104.641 104.216 108.958 1.00 41.93 ?  286 VAL C CG2   1 
ATOM   13336 N  N     . LEU C 2 308 ? 107.407 103.760 105.207 1.00 46.21 ?  287 LEU C N     1 
ATOM   13337 C  CA    . LEU C 2 308 ? 108.527 103.322 104.362 1.00 47.66 ?  287 LEU C CA    1 
ATOM   13338 C  C     . LEU C 2 308 ? 109.423 104.485 103.939 1.00 48.82 ?  287 LEU C C     1 
ATOM   13339 O  O     . LEU C 2 308 ? 110.646 104.325 103.825 1.00 49.02 ?  287 LEU C O     1 
ATOM   13340 C  CB    . LEU C 2 308 ? 108.011 102.560 103.133 1.00 47.95 ?  287 LEU C CB    1 
ATOM   13341 C  CG    . LEU C 2 308 ? 107.843 101.034 103.231 1.00 48.23 ?  287 LEU C CG    1 
ATOM   13342 C  CD1   . LEU C 2 308 ? 107.603 100.524 104.660 1.00 48.10 ?  287 LEU C CD1   1 
ATOM   13343 C  CD2   . LEU C 2 308 ? 106.755 100.537 102.283 1.00 48.81 ?  287 LEU C CD2   1 
ATOM   13344 N  N     . ASN C 2 309 ? 108.810 105.646 103.705 1.00 49.80 ?  288 ASN C N     1 
ATOM   13345 C  CA    . ASN C 2 309 ? 109.549 106.892 103.519 1.00 51.09 ?  288 ASN C CA    1 
ATOM   13346 C  C     . ASN C 2 309 ? 110.194 107.393 104.815 1.00 51.08 ?  288 ASN C C     1 
ATOM   13347 O  O     . ASN C 2 309 ? 111.187 108.120 104.775 1.00 51.41 ?  288 ASN C O     1 
ATOM   13348 C  CB    . ASN C 2 309 ? 108.662 107.974 102.898 1.00 51.37 ?  288 ASN C CB    1 
ATOM   13349 C  CG    . ASN C 2 309 ? 108.532 107.826 101.395 1.00 53.22 ?  288 ASN C CG    1 
ATOM   13350 O  OD1   . ASN C 2 309 ? 108.295 106.728 100.880 1.00 54.39 ?  288 ASN C OD1   1 
ATOM   13351 N  ND2   . ASN C 2 309 ? 108.688 108.935 100.679 1.00 54.70 ?  288 ASN C ND2   1 
ATOM   13352 N  N     . GLY C 2 310 ? 109.625 107.000 105.954 1.00 51.25 ?  289 GLY C N     1 
ATOM   13353 C  CA    . GLY C 2 310 ? 110.210 107.280 107.267 1.00 51.35 ?  289 GLY C CA    1 
ATOM   13354 C  C     . GLY C 2 310 ? 111.536 106.566 107.501 1.00 51.86 ?  289 GLY C C     1 
ATOM   13355 O  O     . GLY C 2 310 ? 112.330 106.982 108.353 1.00 51.49 ?  289 GLY C O     1 
ATOM   13356 N  N     . LEU C 2 311 ? 111.773 105.491 106.749 1.00 52.45 ?  290 LEU C N     1 
ATOM   13357 C  CA    . LEU C 2 311 ? 113.029 104.741 106.820 1.00 52.99 ?  290 LEU C CA    1 
ATOM   13358 C  C     . LEU C 2 311 ? 114.086 105.329 105.882 1.00 53.65 ?  290 LEU C C     1 
ATOM   13359 O  O     . LEU C 2 311 ? 113.984 105.225 104.653 1.00 54.22 ?  290 LEU C O     1 
ATOM   13360 C  CB    . LEU C 2 311 ? 112.797 103.261 106.497 1.00 53.08 ?  290 LEU C CB    1 
ATOM   13361 C  CG    . LEU C 2 311 ? 112.078 102.376 107.520 1.00 53.33 ?  290 LEU C CG    1 
ATOM   13362 C  CD1   . LEU C 2 311 ? 111.619 101.080 106.867 1.00 53.79 ?  290 LEU C CD1   1 
ATOM   13363 C  CD2   . LEU C 2 311 ? 112.964 102.086 108.733 1.00 53.22 ?  290 LEU C CD2   1 
ATOM   13364 N  N     . THR C 2 332 ? 144.003 111.060 110.758 1.00 29.75 ?  311 THR C N     1 
ATOM   13365 C  CA    . THR C 2 332 ? 145.144 110.450 111.429 1.00 33.42 ?  311 THR C CA    1 
ATOM   13366 C  C     . THR C 2 332 ? 146.239 111.479 111.686 1.00 31.78 ?  311 THR C C     1 
ATOM   13367 O  O     . THR C 2 332 ? 146.203 112.583 111.146 1.00 34.05 ?  311 THR C O     1 
ATOM   13368 C  CB    . THR C 2 332 ? 145.726 109.285 110.607 1.00 34.98 ?  311 THR C CB    1 
ATOM   13369 O  OG1   . THR C 2 332 ? 146.701 108.584 111.388 1.00 33.22 ?  311 THR C OG1   1 
ATOM   13370 C  CG2   . THR C 2 332 ? 146.378 109.804 109.335 1.00 32.63 ?  311 THR C CG2   1 
ATOM   13371 N  N     . VAL C 2 333 ? 147.211 111.110 112.516 1.00 31.80 ?  312 VAL C N     1 
ATOM   13372 C  CA    . VAL C 2 333 ? 148.304 111.996 112.898 1.00 32.03 ?  312 VAL C CA    1 
ATOM   13373 C  C     . VAL C 2 333 ? 149.619 111.331 112.515 1.00 31.05 ?  312 VAL C C     1 
ATOM   13374 O  O     . VAL C 2 333 ? 149.914 110.223 112.978 1.00 37.64 ?  312 VAL C O     1 
ATOM   13375 C  CB    . VAL C 2 333 ? 148.285 112.320 114.401 1.00 31.94 ?  312 VAL C CB    1 
ATOM   13376 C  CG1   . VAL C 2 333 ? 149.421 113.266 114.755 1.00 35.19 ?  312 VAL C CG1   1 
ATOM   13377 C  CG2   . VAL C 2 333 ? 146.945 112.916 114.799 1.00 31.89 ?  312 VAL C CG2   1 
ATOM   13378 N  N     . GLU C 2 334 ? 150.400 112.001 111.676 1.00 30.63 ?  313 GLU C N     1 
ATOM   13379 C  CA    . GLU C 2 334 ? 151.751 111.568 111.363 1.00 36.82 ?  313 GLU C CA    1 
ATOM   13380 C  C     . GLU C 2 334 ? 152.705 112.744 111.490 1.00 38.18 ?  313 GLU C C     1 
ATOM   13381 O  O     . GLU C 2 334 ? 152.320 113.893 111.250 1.00 39.00 ?  313 GLU C O     1 
ATOM   13382 C  CB    . GLU C 2 334 ? 151.847 110.975 109.950 1.00 35.32 ?  313 GLU C CB    1 
ATOM   13383 C  CG    . GLU C 2 334 ? 150.884 111.569 108.943 1.00 37.19 ?  313 GLU C CG    1 
ATOM   13384 C  CD    . GLU C 2 334 ? 151.264 111.231 107.513 1.00 41.54 ?  313 GLU C CD    1 
ATOM   13385 O  OE1   . GLU C 2 334 ? 152.325 110.602 107.314 1.00 35.42 ?  313 GLU C OE1   1 
ATOM   13386 O  OE2   . GLU C 2 334 ? 150.503 111.589 106.590 1.00 41.02 -1 313 GLU C OE2   1 
ATOM   13387 N  N     . PRO C 2 335 ? 153.954 112.489 111.864 1.00 33.28 ?  314 PRO C N     1 
ATOM   13388 C  CA    . PRO C 2 335 ? 154.895 113.584 112.103 1.00 35.79 ?  314 PRO C CA    1 
ATOM   13389 C  C     . PRO C 2 335 ? 155.369 114.227 110.807 1.00 35.44 ?  314 PRO C C     1 
ATOM   13390 O  O     . PRO C 2 335 ? 155.281 113.656 109.719 1.00 35.41 ?  314 PRO C O     1 
ATOM   13391 C  CB    . PRO C 2 335 ? 156.055 112.896 112.829 1.00 36.88 ?  314 PRO C CB    1 
ATOM   13392 C  CG    . PRO C 2 335 ? 156.028 111.499 112.316 1.00 35.05 ?  314 PRO C CG    1 
ATOM   13393 C  CD    . PRO C 2 335 ? 154.583 111.167 112.033 1.00 33.26 ?  314 PRO C CD    1 
ATOM   13394 N  N     . LEU C 2 336 ? 155.878 115.446 110.950 1.00 32.52 ?  315 LEU C N     1 
ATOM   13395 C  CA    . LEU C 2 336 ? 156.453 116.189 109.837 1.00 31.09 ?  315 LEU C CA    1 
ATOM   13396 C  C     . LEU C 2 336 ? 157.928 115.832 109.711 1.00 32.85 ?  315 LEU C C     1 
ATOM   13397 O  O     . LEU C 2 336 ? 158.689 115.970 110.674 1.00 34.34 ?  315 LEU C O     1 
ATOM   13398 C  CB    . LEU C 2 336 ? 156.285 117.693 110.047 1.00 25.46 ?  315 LEU C CB    1 
ATOM   13399 C  CG    . LEU C 2 336 ? 154.997 118.340 109.535 1.00 31.53 ?  315 LEU C CG    1 
ATOM   13400 C  CD1   . LEU C 2 336 ? 154.854 119.739 110.104 1.00 29.56 ?  315 LEU C CD1   1 
ATOM   13401 C  CD2   . LEU C 2 336 ? 154.979 118.374 108.016 1.00 25.47 ?  315 LEU C CD2   1 
ATOM   13402 N  N     . LYS C 2 337 ? 158.328 115.374 108.530 1.00 30.29 ?  316 LYS C N     1 
ATOM   13403 C  CA    . LYS C 2 337 ? 159.728 115.094 108.262 1.00 29.27 ?  316 LYS C CA    1 
ATOM   13404 C  C     . LYS C 2 337 ? 160.415 116.330 107.687 1.00 24.34 ?  316 LYS C C     1 
ATOM   13405 O  O     . LYS C 2 337 ? 159.775 117.309 107.299 1.00 31.89 ?  316 LYS C O     1 
ATOM   13406 C  CB    . LYS C 2 337 ? 159.866 113.902 107.315 1.00 27.34 ?  316 LYS C CB    1 
ATOM   13407 C  CG    . LYS C 2 337 ? 158.753 113.778 106.292 1.00 30.14 ?  316 LYS C CG    1 
ATOM   13408 C  CD    . LYS C 2 337 ? 158.549 112.326 105.890 1.00 33.94 ?  316 LYS C CD    1 
ATOM   13409 C  CE    . LYS C 2 337 ? 158.016 111.502 107.051 1.00 30.61 ?  316 LYS C CE    1 
ATOM   13410 N  NZ    . LYS C 2 337 ? 156.610 111.852 107.395 1.00 36.38 1  316 LYS C NZ    1 
ATOM   13411 N  N     . ASP C 2 338 ? 161.747 116.276 107.639 1.00 30.40 ?  317 ASP C N     1 
ATOM   13412 C  CA    . ASP C 2 338 ? 162.514 117.432 107.189 1.00 32.51 ?  317 ASP C CA    1 
ATOM   13413 C  C     . ASP C 2 338 ? 162.149 117.817 105.761 1.00 28.90 ?  317 ASP C C     1 
ATOM   13414 O  O     . ASP C 2 338 ? 162.063 119.006 105.434 1.00 22.50 ?  317 ASP C O     1 
ATOM   13415 C  CB    . ASP C 2 338 ? 164.011 117.145 107.304 1.00 27.18 ?  317 ASP C CB    1 
ATOM   13416 C  CG    . ASP C 2 338 ? 164.438 116.842 108.726 1.00 32.70 ?  317 ASP C CG    1 
ATOM   13417 O  OD1   . ASP C 2 338 ? 163.555 116.611 109.578 1.00 34.97 ?  317 ASP C OD1   1 
ATOM   13418 O  OD2   . ASP C 2 338 ? 165.659 116.837 108.992 1.00 35.21 -1 317 ASP C OD2   1 
ATOM   13419 N  N     . ASP C 2 339 ? 161.934 116.826 104.895 1.00 31.41 ?  318 ASP C N     1 
ATOM   13420 C  CA    . ASP C 2 339 ? 161.593 117.105 103.505 1.00 32.31 ?  318 ASP C CA    1 
ATOM   13421 C  C     . ASP C 2 339 ? 160.232 117.768 103.349 1.00 28.21 ?  318 ASP C C     1 
ATOM   13422 O  O     . ASP C 2 339 ? 159.951 118.315 102.277 1.00 28.94 ?  318 ASP C O     1 
ATOM   13423 C  CB    . ASP C 2 339 ? 161.636 115.814 102.686 1.00 27.80 ?  318 ASP C CB    1 
ATOM   13424 C  CG    . ASP C 2 339 ? 163.018 115.515 102.147 1.00 37.08 ?  318 ASP C CG    1 
ATOM   13425 O  OD1   . ASP C 2 339 ? 163.829 116.460 102.034 1.00 36.40 ?  318 ASP C OD1   1 
ATOM   13426 O  OD2   . ASP C 2 339 ? 163.296 114.337 101.837 1.00 36.58 -1 318 ASP C OD2   1 
ATOM   13427 N  N     . ASP C 2 340 ? 159.384 117.734 104.379 1.00 28.83 ?  319 ASP C N     1 
ATOM   13428 C  CA    . ASP C 2 340 ? 158.082 118.384 104.300 1.00 20.00 ?  319 ASP C CA    1 
ATOM   13429 C  C     . ASP C 2 340 ? 158.179 119.902 104.309 1.00 14.54 ?  319 ASP C C     1 
ATOM   13430 O  O     . ASP C 2 340 ? 157.175 120.571 104.046 1.00 28.61 ?  319 ASP C O     1 
ATOM   13431 C  CB    . ASP C 2 340 ? 157.194 117.922 105.456 1.00 23.12 ?  319 ASP C CB    1 
ATOM   13432 C  CG    . ASP C 2 340 ? 156.760 116.479 105.316 1.00 31.13 ?  319 ASP C CG    1 
ATOM   13433 O  OD1   . ASP C 2 340 ? 156.983 115.893 104.236 1.00 30.52 ?  319 ASP C OD1   1 
ATOM   13434 O  OD2   . ASP C 2 340 ? 156.196 115.929 106.284 1.00 37.33 -1 319 ASP C OD2   1 
ATOM   13435 N  N     . PHE C 2 341 ? 159.352 120.460 104.603 1.00 20.85 ?  320 PHE C N     1 
ATOM   13436 C  CA    . PHE C 2 341 ? 159.552 121.900 104.650 1.00 15.27 ?  320 PHE C CA    1 
ATOM   13437 C  C     . PHE C 2 341 ? 160.217 122.441 103.393 1.00 13.98 ?  320 PHE C C     1 
ATOM   13438 O  O     . PHE C 2 341 ? 160.590 123.617 103.357 1.00 17.66 ?  320 PHE C O     1 
ATOM   13439 C  CB    . PHE C 2 341 ? 160.379 122.275 105.880 1.00 14.81 ?  320 PHE C CB    1 
ATOM   13440 C  CG    . PHE C 2 341 ? 159.687 121.998 107.180 1.00 17.09 ?  320 PHE C CG    1 
ATOM   13441 C  CD1   . PHE C 2 341 ? 159.731 120.736 107.747 1.00 10.37 ?  320 PHE C CD1   1 
ATOM   13442 C  CD2   . PHE C 2 341 ? 158.986 122.996 107.834 1.00 10.45 ?  320 PHE C CD2   1 
ATOM   13443 C  CE1   . PHE C 2 341 ? 159.091 120.476 108.940 1.00 7.03  ?  320 PHE C CE1   1 
ATOM   13444 C  CE2   . PHE C 2 341 ? 158.345 122.741 109.029 1.00 13.32 ?  320 PHE C CE2   1 
ATOM   13445 C  CZ    . PHE C 2 341 ? 158.397 121.478 109.583 1.00 3.64  ?  320 PHE C CZ    1 
ATOM   13446 N  N     . TYR C 2 342 ? 160.376 121.612 102.366 1.00 16.46 ?  321 TYR C N     1 
ATOM   13447 C  CA    . TYR C 2 342 ? 161.015 122.017 101.124 1.00 16.25 ?  321 TYR C CA    1 
ATOM   13448 C  C     . TYR C 2 342 ? 160.152 121.585 99.950  1.00 21.99 ?  321 TYR C C     1 
ATOM   13449 O  O     . TYR C 2 342 ? 159.507 120.533 99.984  1.00 17.96 ?  321 TYR C O     1 
ATOM   13450 C  CB    . TYR C 2 342 ? 162.420 121.419 100.997 1.00 19.82 ?  321 TYR C CB    1 
ATOM   13451 C  CG    . TYR C 2 342 ? 163.328 121.765 102.154 1.00 16.70 ?  321 TYR C CG    1 
ATOM   13452 C  CD1   . TYR C 2 342 ? 163.385 120.958 103.282 1.00 20.67 ?  321 TYR C CD1   1 
ATOM   13453 C  CD2   . TYR C 2 342 ? 164.123 122.902 102.122 1.00 16.00 ?  321 TYR C CD2   1 
ATOM   13454 C  CE1   . TYR C 2 342 ? 164.211 121.270 104.343 1.00 14.93 ?  321 TYR C CE1   1 
ATOM   13455 C  CE2   . TYR C 2 342 ? 164.951 123.224 103.178 1.00 19.30 ?  321 TYR C CE2   1 
ATOM   13456 C  CZ    . TYR C 2 342 ? 164.992 122.405 104.286 1.00 24.01 ?  321 TYR C CZ    1 
ATOM   13457 O  OH    . TYR C 2 342 ? 165.818 122.724 105.339 1.00 25.58 ?  321 TYR C OH    1 
ATOM   13458 N  N     . PHE C 2 343 ? 160.143 122.412 98.909  1.00 18.10 ?  322 PHE C N     1 
ATOM   13459 C  CA    . PHE C 2 343 ? 159.300 122.165 97.747  1.00 25.12 ?  322 PHE C CA    1 
ATOM   13460 C  C     . PHE C 2 343 ? 160.048 122.469 96.454  1.00 30.04 ?  322 PHE C C     1 
ATOM   13461 O  O     . PHE C 2 343 ? 160.832 123.415 96.378  1.00 30.76 ?  322 PHE C O     1 
ATOM   13462 C  CB    . PHE C 2 343 ? 158.022 123.005 97.829  1.00 19.42 ?  322 PHE C CB    1 
ATOM   13463 C  CG    . PHE C 2 343 ? 157.397 123.028 99.195  1.00 15.10 ?  322 PHE C CG    1 
ATOM   13464 C  CD1   . PHE C 2 343 ? 157.765 123.985 100.125 1.00 13.48 ?  322 PHE C CD1   1 
ATOM   13465 C  CD2   . PHE C 2 343 ? 156.445 122.089 99.550  1.00 18.02 ?  322 PHE C CD2   1 
ATOM   13466 C  CE1   . PHE C 2 343 ? 157.194 124.006 101.380 1.00 13.10 ?  322 PHE C CE1   1 
ATOM   13467 C  CE2   . PHE C 2 343 ? 155.871 122.104 100.804 1.00 14.11 ?  322 PHE C CE2   1 
ATOM   13468 C  CZ    . PHE C 2 343 ? 156.246 123.065 101.720 1.00 10.84 ?  322 PHE C CZ    1 
ATOM   13469 N  N     . ASP D 2 37  ? 122.825 113.544 143.669 1.00 32.44 ?  16  ASP D N     1 
ATOM   13470 C  CA    . ASP D 2 37  ? 123.424 114.867 143.465 1.00 32.83 ?  16  ASP D CA    1 
ATOM   13471 C  C     . ASP D 2 37  ? 124.514 114.897 142.396 1.00 31.65 ?  16  ASP D C     1 
ATOM   13472 O  O     . ASP D 2 37  ? 125.010 115.976 142.060 1.00 32.65 ?  16  ASP D O     1 
ATOM   13473 C  CB    . ASP D 2 37  ? 124.042 115.390 144.771 1.00 33.73 ?  16  ASP D CB    1 
ATOM   13474 C  CG    . ASP D 2 37  ? 123.012 115.651 145.860 1.00 36.81 ?  16  ASP D CG    1 
ATOM   13475 O  OD1   . ASP D 2 37  ? 123.426 115.725 147.042 1.00 39.69 ?  16  ASP D OD1   1 
ATOM   13476 O  OD2   . ASP D 2 37  ? 121.805 115.777 145.550 1.00 39.67 -1 16  ASP D OD2   1 
ATOM   13477 N  N     . PHE D 2 38  ? 124.897 113.738 141.864 1.00 29.55 ?  17  PHE D N     1 
ATOM   13478 C  CA    . PHE D 2 38  ? 126.146 113.664 141.106 1.00 27.75 ?  17  PHE D CA    1 
ATOM   13479 C  C     . PHE D 2 38  ? 126.149 112.817 139.823 1.00 26.21 ?  17  PHE D C     1 
ATOM   13480 O  O     . PHE D 2 38  ? 127.024 112.991 138.981 1.00 25.93 ?  17  PHE D O     1 
ATOM   13481 C  CB    . PHE D 2 38  ? 127.290 113.220 142.045 1.00 27.37 ?  17  PHE D CB    1 
ATOM   13482 C  CG    . PHE D 2 38  ? 127.062 111.875 142.681 1.00 27.32 ?  17  PHE D CG    1 
ATOM   13483 C  CD1   . PHE D 2 38  ? 127.402 110.706 142.007 1.00 27.01 ?  17  PHE D CD1   1 
ATOM   13484 C  CD2   . PHE D 2 38  ? 126.507 111.773 143.951 1.00 28.02 ?  17  PHE D CD2   1 
ATOM   13485 C  CE1   . PHE D 2 38  ? 127.186 109.458 142.587 1.00 27.66 ?  17  PHE D CE1   1 
ATOM   13486 C  CE2   . PHE D 2 38  ? 126.284 110.532 144.533 1.00 27.68 ?  17  PHE D CE2   1 
ATOM   13487 C  CZ    . PHE D 2 38  ? 126.626 109.370 143.847 1.00 27.47 ?  17  PHE D CZ    1 
ATOM   13488 N  N     . THR D 2 39  ? 125.189 111.911 139.672 1.00 24.88 ?  18  THR D N     1 
ATOM   13489 C  CA    . THR D 2 39  ? 125.220 110.938 138.567 1.00 23.81 ?  18  THR D CA    1 
ATOM   13490 C  C     . THR D 2 39  ? 125.118 111.566 137.165 1.00 23.56 ?  18  THR D C     1 
ATOM   13491 O  O     . THR D 2 39  ? 125.835 111.170 136.245 1.00 23.02 ?  18  THR D O     1 
ATOM   13492 C  CB    . THR D 2 39  ? 124.199 109.794 138.782 1.00 23.40 ?  18  THR D CB    1 
ATOM   13493 O  OG1   . THR D 2 39  ? 124.731 108.868 139.737 1.00 23.77 ?  18  THR D OG1   1 
ATOM   13494 C  CG2   . THR D 2 39  ? 123.924 109.037 137.494 1.00 22.31 ?  18  THR D CG2   1 
ATOM   13495 N  N     . GLN D 2 40  ? 124.248 112.553 136.997 1.00 23.78 ?  19  GLN D N     1 
ATOM   13496 C  CA    . GLN D 2 40  ? 124.144 113.205 135.689 1.00 23.88 ?  19  GLN D CA    1 
ATOM   13497 C  C     . GLN D 2 40  ? 125.423 113.962 135.317 1.00 24.09 ?  19  GLN D C     1 
ATOM   13498 O  O     . GLN D 2 40  ? 125.873 113.899 134.181 1.00 23.15 ?  19  GLN D O     1 
ATOM   13499 C  CB    . GLN D 2 40  ? 122.907 114.101 135.605 1.00 24.53 ?  19  GLN D CB    1 
ATOM   13500 C  CG    . GLN D 2 40  ? 121.617 113.296 135.624 1.00 24.06 ?  19  GLN D CG    1 
ATOM   13501 C  CD    . GLN D 2 40  ? 120.424 114.060 135.100 1.00 25.83 ?  19  GLN D CD    1 
ATOM   13502 O  OE1   . GLN D 2 40  ? 120.572 115.122 134.498 1.00 25.90 ?  19  GLN D OE1   1 
ATOM   13503 N  NE2   . GLN D 2 40  ? 119.228 113.509 135.308 1.00 23.56 ?  19  GLN D NE2   1 
ATOM   13504 N  N     . MET D 2 41  ? 126.028 114.636 136.287 1.00 24.07 ?  20  MET D N     1 
ATOM   13505 C  CA    . MET D 2 41  ? 127.326 115.274 136.065 1.00 25.53 ?  20  MET D CA    1 
ATOM   13506 C  C     . MET D 2 41  ? 128.414 114.269 135.633 1.00 24.24 ?  20  MET D C     1 
ATOM   13507 O  O     . MET D 2 41  ? 129.183 114.541 134.707 1.00 23.16 ?  20  MET D O     1 
ATOM   13508 C  CB    . MET D 2 41  ? 127.754 116.041 137.320 1.00 26.79 ?  20  MET D CB    1 
ATOM   13509 C  CG    . MET D 2 41  ? 129.104 116.724 137.221 1.00 32.62 ?  20  MET D CG    1 
ATOM   13510 S  SD    . MET D 2 41  ? 129.630 117.295 138.854 1.00 44.01 ?  20  MET D SD    1 
ATOM   13511 C  CE    . MET D 2 41  ? 131.413 117.338 138.649 1.00 41.93 ?  20  MET D CE    1 
ATOM   13512 N  N     . PHE D 2 42  ? 128.468 113.109 136.290 1.00 23.31 ?  21  PHE D N     1 
ATOM   13513 C  CA    . PHE D 2 42  ? 129.452 112.091 135.918 1.00 23.44 ?  21  PHE D CA    1 
ATOM   13514 C  C     . PHE D 2 42  ? 129.132 111.447 134.584 1.00 23.55 ?  21  PHE D C     1 
ATOM   13515 O  O     . PHE D 2 42  ? 130.037 111.098 133.835 1.00 23.74 ?  21  PHE D O     1 
ATOM   13516 C  CB    . PHE D 2 42  ? 129.617 111.035 137.013 1.00 22.97 ?  21  PHE D CB    1 
ATOM   13517 C  CG    . PHE D 2 42  ? 130.601 111.434 138.057 1.00 23.86 ?  21  PHE D CG    1 
ATOM   13518 C  CD1   . PHE D 2 42  ? 131.926 111.015 137.977 1.00 24.55 ?  21  PHE D CD1   1 
ATOM   13519 C  CD2   . PHE D 2 42  ? 130.222 112.263 139.095 1.00 24.06 ?  21  PHE D CD2   1 
ATOM   13520 C  CE1   . PHE D 2 42  ? 132.856 111.405 138.943 1.00 25.78 ?  21  PHE D CE1   1 
ATOM   13521 C  CE2   . PHE D 2 42  ? 131.146 112.659 140.067 1.00 25.25 ?  21  PHE D CE2   1 
ATOM   13522 C  CZ    . PHE D 2 42  ? 132.457 112.236 139.989 1.00 25.79 ?  21  PHE D CZ    1 
ATOM   13523 N  N     . TYR D 2 43  ? 127.840 111.313 134.290 1.00 24.08 ?  22  TYR D N     1 
ATOM   13524 C  CA    . TYR D 2 43  ? 127.405 110.850 132.982 1.00 24.74 ?  22  TYR D CA    1 
ATOM   13525 C  C     . TYR D 2 43  ? 128.030 111.730 131.897 1.00 25.72 ?  22  TYR D C     1 
ATOM   13526 O  O     . TYR D 2 43  ? 128.634 111.226 130.946 1.00 25.56 ?  22  TYR D O     1 
ATOM   13527 C  CB    . TYR D 2 43  ? 125.873 110.850 132.854 1.00 24.90 ?  22  TYR D CB    1 
ATOM   13528 C  CG    . TYR D 2 43  ? 125.424 110.532 131.435 1.00 24.38 ?  22  TYR D CG    1 
ATOM   13529 C  CD1   . TYR D 2 43  ? 125.205 109.219 131.035 1.00 23.96 ?  22  TYR D CD1   1 
ATOM   13530 C  CD2   . TYR D 2 43  ? 125.278 111.545 130.483 1.00 24.73 ?  22  TYR D CD2   1 
ATOM   13531 C  CE1   . TYR D 2 43  ? 124.828 108.919 129.724 1.00 23.42 ?  22  TYR D CE1   1 
ATOM   13532 C  CE2   . TYR D 2 43  ? 124.888 111.262 129.172 1.00 26.65 ?  22  TYR D CE2   1 
ATOM   13533 C  CZ    . TYR D 2 43  ? 124.670 109.945 128.804 1.00 25.68 ?  22  TYR D CZ    1 
ATOM   13534 O  OH    . TYR D 2 43  ? 124.289 109.660 127.513 1.00 26.57 ?  22  TYR D OH    1 
ATOM   13535 N  N     . ASN D 2 44  ? 127.869 113.042 132.054 1.00 26.77 ?  23  ASN D N     1 
ATOM   13536 C  CA    . ASN D 2 44  ? 128.385 114.013 131.096 1.00 28.57 ?  23  ASN D CA    1 
ATOM   13537 C  C     . ASN D 2 44  ? 129.887 113.902 130.910 1.00 28.70 ?  23  ASN D C     1 
ATOM   13538 O  O     . ASN D 2 44  ? 130.363 113.779 129.778 1.00 28.99 ?  23  ASN D O     1 
ATOM   13539 C  CB    . ASN D 2 44  ? 127.973 115.433 131.496 1.00 29.62 ?  23  ASN D CB    1 
ATOM   13540 C  CG    . ASN D 2 44  ? 126.478 115.670 131.322 1.00 32.44 ?  23  ASN D CG    1 
ATOM   13541 O  OD1   . ASN D 2 44  ? 125.810 114.968 130.552 1.00 34.30 ?  23  ASN D OD1   1 
ATOM   13542 N  ND2   . ASN D 2 44  ? 125.944 116.657 132.037 1.00 35.17 ?  23  ASN D ND2   1 
ATOM   13543 N  N     . GLN D 2 45  ? 130.620 113.899 132.020 1.00 28.97 ?  24  GLN D N     1 
ATOM   13544 C  CA    . GLN D 2 45  ? 132.075 113.810 131.974 1.00 29.99 ?  24  GLN D CA    1 
ATOM   13545 C  C     . GLN D 2 45  ? 132.561 112.493 131.349 1.00 29.69 ?  24  GLN D C     1 
ATOM   13546 O  O     . GLN D 2 45  ? 133.521 112.489 130.580 1.00 30.01 ?  24  GLN D O     1 
ATOM   13547 C  CB    . GLN D 2 45  ? 132.684 114.018 133.366 1.00 30.27 ?  24  GLN D CB    1 
ATOM   13548 C  CG    . GLN D 2 45  ? 134.221 114.171 133.359 1.00 32.29 ?  24  GLN D CG    1 
ATOM   13549 C  CD    . GLN D 2 45  ? 134.700 115.396 132.590 1.00 35.95 ?  24  GLN D CD    1 
ATOM   13550 O  OE1   . GLN D 2 45  ? 133.991 116.401 132.486 1.00 36.72 ?  24  GLN D OE1   1 
ATOM   13551 N  NE2   . GLN D 2 45  ? 135.912 115.318 132.049 1.00 37.05 ?  24  GLN D NE2   1 
ATOM   13552 N  N     . ASN D 2 46  ? 131.882 111.390 131.660 1.00 28.93 ?  25  ASN D N     1 
ATOM   13553 C  CA    . ASN D 2 46  ? 132.220 110.100 131.082 1.00 28.70 ?  25  ASN D CA    1 
ATOM   13554 C  C     . ASN D 2 46  ? 132.047 110.044 129.570 1.00 29.05 ?  25  ASN D C     1 
ATOM   13555 O  O     . ASN D 2 46  ? 132.975 109.652 128.856 1.00 28.51 ?  25  ASN D O     1 
ATOM   13556 C  CB    . ASN D 2 46  ? 131.431 108.966 131.751 1.00 28.36 ?  25  ASN D CB    1 
ATOM   13557 C  CG    . ASN D 2 46  ? 132.128 108.427 132.981 1.00 28.45 ?  25  ASN D CG    1 
ATOM   13558 O  OD1   . ASN D 2 46  ? 132.831 107.421 132.903 1.00 28.03 ?  25  ASN D OD1   1 
ATOM   13559 N  ND2   . ASN D 2 46  ? 131.965 109.106 134.115 1.00 26.53 ?  25  ASN D ND2   1 
ATOM   13560 N  N     . VAL D 2 47  ? 130.877 110.456 129.082 1.00 29.66 ?  26  VAL D N     1 
ATOM   13561 C  CA    . VAL D 2 47  ? 130.577 110.332 127.655 1.00 31.15 ?  26  VAL D CA    1 
ATOM   13562 C  C     . VAL D 2 47  ? 131.388 111.318 126.820 1.00 32.39 ?  26  VAL D C     1 
ATOM   13563 O  O     . VAL D 2 47  ? 131.726 111.030 125.673 1.00 32.80 ?  26  VAL D O     1 
ATOM   13564 C  CB    . VAL D 2 47  ? 129.050 110.412 127.321 1.00 31.08 ?  26  VAL D CB    1 
ATOM   13565 C  CG1   . VAL D 2 47  ? 128.270 109.363 128.105 1.00 31.09 ?  26  VAL D CG1   1 
ATOM   13566 C  CG2   . VAL D 2 47  ? 128.482 111.819 127.557 1.00 30.81 ?  26  VAL D CG2   1 
ATOM   13567 N  N     . LYS D 2 48  ? 131.731 112.466 127.393 1.00 33.28 ?  27  LYS D N     1 
ATOM   13568 C  CA    . LYS D 2 48  ? 132.544 113.412 126.646 1.00 34.87 ?  27  LYS D CA    1 
ATOM   13569 C  C     . LYS D 2 48  ? 134.034 113.019 126.577 1.00 34.91 ?  27  LYS D C     1 
ATOM   13570 O  O     . LYS D 2 48  ? 134.788 113.584 125.789 1.00 34.92 ?  27  LYS D O     1 
ATOM   13571 C  CB    . LYS D 2 48  ? 132.319 114.853 127.130 1.00 35.45 ?  27  LYS D CB    1 
ATOM   13572 C  CG    . LYS D 2 48  ? 133.149 115.304 128.309 1.00 37.41 ?  27  LYS D CG    1 
ATOM   13573 C  CD    . LYS D 2 48  ? 133.106 116.837 128.417 1.00 40.91 ?  27  LYS D CD    1 
ATOM   13574 C  CE    . LYS D 2 48  ? 134.226 117.358 129.323 1.00 42.46 ?  27  LYS D CE    1 
ATOM   13575 N  NZ    . LYS D 2 48  ? 134.319 118.848 129.333 1.00 45.13 1  27  LYS D NZ    1 
ATOM   13576 N  N     . GLN D 2 49  ? 134.432 112.037 127.389 1.00 34.66 ?  28  GLN D N     1 
ATOM   13577 C  CA    . GLN D 2 49  ? 135.787 111.492 127.380 1.00 34.64 ?  28  GLN D CA    1 
ATOM   13578 C  C     . GLN D 2 49  ? 135.899 110.269 126.470 1.00 34.20 ?  28  GLN D C     1 
ATOM   13579 O  O     . GLN D 2 49  ? 136.934 109.600 126.469 1.00 34.53 ?  28  GLN D O     1 
ATOM   13580 C  CB    . GLN D 2 49  ? 136.231 111.102 128.804 1.00 34.89 ?  28  GLN D CB    1 
ATOM   13581 C  CG    . GLN D 2 49  ? 136.867 112.230 129.614 1.00 36.47 ?  28  GLN D CG    1 
ATOM   13582 C  CD    . GLN D 2 49  ? 137.114 111.864 131.080 1.00 38.37 ?  28  GLN D CD    1 
ATOM   13583 O  OE1   . GLN D 2 49  ? 137.058 112.729 131.954 1.00 40.68 ?  28  GLN D OE1   1 
ATOM   13584 N  NE2   . GLN D 2 49  ? 137.386 110.588 131.352 1.00 38.57 ?  28  GLN D NE2   1 
ATOM   13585 N  N     . PHE D 2 50  ? 134.848 109.968 125.707 1.00 33.42 ?  29  PHE D N     1 
ATOM   13586 C  CA    . PHE D 2 50  ? 134.845 108.767 124.873 1.00 32.57 ?  29  PHE D CA    1 
ATOM   13587 C  C     . PHE D 2 50  ? 135.962 108.839 123.831 1.00 32.60 ?  29  PHE D C     1 
ATOM   13588 O  O     . PHE D 2 50  ? 136.211 109.894 123.241 1.00 32.39 ?  29  PHE D O     1 
ATOM   13589 C  CB    . PHE D 2 50  ? 133.479 108.533 124.207 1.00 32.77 ?  29  PHE D CB    1 
ATOM   13590 C  CG    . PHE D 2 50  ? 133.417 107.279 123.358 1.00 32.24 ?  29  PHE D CG    1 
ATOM   13591 C  CD1   . PHE D 2 50  ? 133.328 106.022 123.949 1.00 31.50 ?  29  PHE D CD1   1 
ATOM   13592 C  CD2   . PHE D 2 50  ? 133.450 107.360 121.971 1.00 33.60 ?  29  PHE D CD2   1 
ATOM   13593 C  CE1   . PHE D 2 50  ? 133.273 104.871 123.178 1.00 33.02 ?  29  PHE D CE1   1 
ATOM   13594 C  CE2   . PHE D 2 50  ? 133.400 106.209 121.182 1.00 33.78 ?  29  PHE D CE2   1 
ATOM   13595 C  CZ    . PHE D 2 50  ? 133.304 104.965 121.785 1.00 33.13 ?  29  PHE D CZ    1 
ATOM   13596 N  N     . TRP D 2 51  ? 136.632 107.712 123.625 1.00 31.95 ?  30  TRP D N     1 
ATOM   13597 C  CA    . TRP D 2 51  ? 137.735 107.615 122.670 1.00 32.03 ?  30  TRP D CA    1 
ATOM   13598 C  C     . TRP D 2 51  ? 137.855 106.177 122.183 1.00 33.03 ?  30  TRP D C     1 
ATOM   13599 O  O     . TRP D 2 51  ? 137.242 105.268 122.747 1.00 32.54 ?  30  TRP D O     1 
ATOM   13600 C  CB    . TRP D 2 51  ? 139.054 108.103 123.290 1.00 31.19 ?  30  TRP D CB    1 
ATOM   13601 C  CG    . TRP D 2 51  ? 139.502 107.304 124.497 1.00 28.11 ?  30  TRP D CG    1 
ATOM   13602 C  CD1   . TRP D 2 51  ? 139.031 107.416 125.768 1.00 26.51 ?  30  TRP D CD1   1 
ATOM   13603 C  CD2   . TRP D 2 51  ? 140.502 106.273 124.528 1.00 25.93 ?  30  TRP D CD2   1 
ATOM   13604 N  NE1   . TRP D 2 51  ? 139.679 106.522 126.597 1.00 24.52 ?  30  TRP D NE1   1 
ATOM   13605 C  CE2   . TRP D 2 51  ? 140.583 105.808 125.862 1.00 24.42 ?  30  TRP D CE2   1 
ATOM   13606 C  CE3   . TRP D 2 51  ? 141.342 105.701 123.561 1.00 25.37 ?  30  TRP D CE3   1 
ATOM   13607 C  CZ2   . TRP D 2 51  ? 141.474 104.800 126.255 1.00 24.00 ?  30  TRP D CZ2   1 
ATOM   13608 C  CZ3   . TRP D 2 51  ? 142.223 104.692 123.952 1.00 24.99 ?  30  TRP D CZ3   1 
ATOM   13609 C  CH2   . TRP D 2 51  ? 142.280 104.253 125.287 1.00 23.72 ?  30  TRP D CH2   1 
ATOM   13610 N  N     . LEU D 2 52  ? 138.634 105.988 121.122 1.00 34.81 ?  31  LEU D N     1 
ATOM   13611 C  CA    . LEU D 2 52  ? 138.840 104.681 120.516 1.00 36.58 ?  31  LEU D CA    1 
ATOM   13612 C  C     . LEU D 2 52  ? 140.327 104.450 120.265 1.00 37.80 ?  31  LEU D C     1 
ATOM   13613 O  O     . LEU D 2 52  ? 141.054 105.398 119.981 1.00 37.92 ?  31  LEU D O     1 
ATOM   13614 C  CB    . LEU D 2 52  ? 138.045 104.565 119.205 1.00 36.95 ?  31  LEU D CB    1 
ATOM   13615 C  CG    . LEU D 2 52  ? 136.550 104.234 119.269 1.00 38.15 ?  31  LEU D CG    1 
ATOM   13616 C  CD1   . LEU D 2 52  ? 136.043 103.824 117.891 1.00 39.50 ?  31  LEU D CD1   1 
ATOM   13617 C  CD2   . LEU D 2 52  ? 136.252 103.126 120.273 1.00 37.94 ?  31  LEU D CD2   1 
ATOM   13618 N  N     . PRO D 2 53  ? 140.787 103.187 120.363 1.00 39.26 ?  32  PRO D N     1 
ATOM   13619 C  CA    . PRO D 2 53  ? 142.206 102.842 120.162 1.00 40.41 ?  32  PRO D CA    1 
ATOM   13620 C  C     . PRO D 2 53  ? 142.774 103.328 118.821 1.00 41.91 ?  32  PRO D C     1 
ATOM   13621 O  O     . PRO D 2 53  ? 143.878 103.883 118.779 1.00 42.52 ?  32  PRO D O     1 
ATOM   13622 C  CB    . PRO D 2 53  ? 142.203 101.310 120.193 1.00 40.42 ?  32  PRO D CB    1 
ATOM   13623 C  CG    . PRO D 2 53  ? 140.965 100.938 120.905 1.00 40.01 ?  32  PRO D CG    1 
ATOM   13624 C  CD    . PRO D 2 53  ? 139.959 101.991 120.601 1.00 39.30 ?  32  PRO D CD    1 
ATOM   13625 N  N     . GLU D 2 54  ? 142.011 103.137 117.749 1.00 43.27 ?  33  GLU D N     1 
ATOM   13626 C  CA    . GLU D 2 54  ? 142.412 103.501 116.380 1.00 45.17 ?  33  GLU D CA    1 
ATOM   13627 C  C     . GLU D 2 54  ? 142.869 104.957 116.194 1.00 45.57 ?  33  GLU D C     1 
ATOM   13628 O  O     . GLU D 2 54  ? 143.581 105.268 115.234 1.00 46.08 ?  33  GLU D O     1 
ATOM   13629 C  CB    . GLU D 2 54  ? 141.267 103.195 115.402 1.00 45.55 ?  33  GLU D CB    1 
ATOM   13630 C  CG    . GLU D 2 54  ? 141.170 101.733 114.960 1.00 48.19 ?  33  GLU D CG    1 
ATOM   13631 C  CD    . GLU D 2 54  ? 140.864 100.768 116.098 1.00 50.61 ?  33  GLU D CD    1 
ATOM   13632 O  OE1   . GLU D 2 54  ? 139.931 101.044 116.889 1.00 51.10 ?  33  GLU D OE1   1 
ATOM   13633 O  OE2   . GLU D 2 54  ? 141.565 99.733  116.199 1.00 52.64 -1 33  GLU D OE2   1 
ATOM   13634 N  N     . GLU D 2 55  ? 142.460 105.836 117.109 1.00 45.74 ?  34  GLU D N     1 
ATOM   13635 C  CA    . GLU D 2 55  ? 142.772 107.268 117.020 1.00 46.28 ?  34  GLU D CA    1 
ATOM   13636 C  C     . GLU D 2 55  ? 144.267 107.574 117.174 1.00 46.49 ?  34  GLU D C     1 
ATOM   13637 O  O     . GLU D 2 55  ? 144.768 108.551 116.609 1.00 46.73 ?  34  GLU D O     1 
ATOM   13638 C  CB    . GLU D 2 55  ? 141.962 108.067 118.046 1.00 46.17 ?  34  GLU D CB    1 
ATOM   13639 C  CG    . GLU D 2 55  ? 140.445 108.025 117.845 1.00 47.10 ?  34  GLU D CG    1 
ATOM   13640 C  CD    . GLU D 2 55  ? 139.699 108.886 118.862 1.00 48.43 ?  34  GLU D CD    1 
ATOM   13641 O  OE1   . GLU D 2 55  ? 139.893 110.122 118.859 1.00 49.62 ?  34  GLU D OE1   1 
ATOM   13642 O  OE2   . GLU D 2 55  ? 138.918 108.330 119.663 1.00 47.11 -1 34  GLU D OE2   1 
ATOM   13643 N  N     . ILE D 2 56  ? 144.970 106.742 117.942 1.00 46.23 ?  35  ILE D N     1 
ATOM   13644 C  CA    . ILE D 2 56  ? 146.408 106.901 118.143 1.00 46.25 ?  35  ILE D CA    1 
ATOM   13645 C  C     . ILE D 2 56  ? 147.158 105.880 117.288 1.00 46.30 ?  35  ILE D C     1 
ATOM   13646 O  O     . ILE D 2 56  ? 146.966 104.671 117.445 1.00 46.36 ?  35  ILE D O     1 
ATOM   13647 C  CB    . ILE D 2 56  ? 146.815 106.728 119.648 1.00 45.84 ?  35  ILE D CB    1 
ATOM   13648 C  CG1   . ILE D 2 56  ? 145.829 107.427 120.606 1.00 46.15 ?  35  ILE D CG1   1 
ATOM   13649 C  CG2   . ILE D 2 56  ? 148.277 107.160 119.885 1.00 45.72 ?  35  ILE D CG2   1 
ATOM   13650 C  CD1   . ILE D 2 56  ? 145.730 108.943 120.472 1.00 47.27 ?  35  ILE D CD1   1 
ATOM   13651 N  N     . ALA D 2 57  ? 147.999 106.366 116.380 1.00 46.51 ?  36  ALA D N     1 
ATOM   13652 C  CA    . ALA D 2 57  ? 148.869 105.492 115.589 1.00 46.56 ?  36  ALA D CA    1 
ATOM   13653 C  C     . ALA D 2 57  ? 150.043 105.030 116.458 1.00 46.08 ?  36  ALA D C     1 
ATOM   13654 O  O     . ALA D 2 57  ? 150.746 105.858 117.035 1.00 45.70 ?  36  ALA D O     1 
ATOM   13655 C  CB    . ALA D 2 57  ? 149.371 106.216 114.343 1.00 47.10 ?  36  ALA D CB    1 
ATOM   13656 N  N     . LEU D 2 58  ? 150.254 103.717 116.536 1.00 45.66 ?  37  LEU D N     1 
ATOM   13657 C  CA    . LEU D 2 58  ? 151.250 103.154 117.460 1.00 45.27 ?  37  LEU D CA    1 
ATOM   13658 C  C     . LEU D 2 58  ? 152.634 102.867 116.881 1.00 45.25 ?  37  LEU D C     1 
ATOM   13659 O  O     . LEU D 2 58  ? 153.613 102.775 117.630 1.00 44.82 ?  37  LEU D O     1 
ATOM   13660 C  CB    . LEU D 2 58  ? 150.706 101.890 118.125 1.00 45.05 ?  37  LEU D CB    1 
ATOM   13661 C  CG    . LEU D 2 58  ? 149.729 102.141 119.272 1.00 45.41 ?  37  LEU D CG    1 
ATOM   13662 C  CD1   . LEU D 2 58  ? 149.208 100.820 119.804 1.00 45.40 ?  37  LEU D CD1   1 
ATOM   13663 C  CD2   . LEU D 2 58  ? 150.391 102.952 120.384 1.00 44.70 ?  37  LEU D CD2   1 
ATOM   13664 N  N     . ASN D 2 59  ? 152.722 102.741 115.560 1.00 45.33 ?  38  ASN D N     1 
ATOM   13665 C  CA    . ASN D 2 59  ? 153.943 102.239 114.922 1.00 45.22 ?  38  ASN D CA    1 
ATOM   13666 C  C     . ASN D 2 59  ? 155.218 103.049 115.196 1.00 44.39 ?  38  ASN D C     1 
ATOM   13667 O  O     . ASN D 2 59  ? 156.311 102.477 115.272 1.00 44.33 ?  38  ASN D O     1 
ATOM   13668 C  CB    . ASN D 2 59  ? 153.725 102.060 113.422 1.00 46.22 ?  38  ASN D CB    1 
ATOM   13669 C  CG    . ASN D 2 59  ? 154.470 100.859 112.867 1.00 47.90 ?  38  ASN D CG    1 
ATOM   13670 O  OD1   . ASN D 2 59  ? 155.347 100.998 112.014 1.00 49.28 ?  38  ASN D OD1   1 
ATOM   13671 N  ND2   . ASN D 2 59  ? 154.121 99.665  113.350 1.00 49.18 ?  38  ASN D ND2   1 
ATOM   13672 N  N     . GLY D 2 60  ? 155.070 104.365 115.365 1.00 43.45 ?  39  GLY D N     1 
ATOM   13673 C  CA    . GLY D 2 60  ? 156.196 105.260 115.649 1.00 42.42 ?  39  GLY D CA    1 
ATOM   13674 C  C     . GLY D 2 60  ? 156.892 105.057 116.992 1.00 41.55 ?  39  GLY D C     1 
ATOM   13675 O  O     . GLY D 2 60  ? 157.934 105.665 117.258 1.00 41.29 ?  39  GLY D O     1 
ATOM   13676 N  N     . ASP D 2 61  ? 156.319 104.212 117.847 1.00 40.35 ?  40  ASP D N     1 
ATOM   13677 C  CA    . ASP D 2 61  ? 156.960 103.850 119.117 1.00 39.53 ?  40  ASP D CA    1 
ATOM   13678 C  C     . ASP D 2 61  ? 158.178 102.954 118.938 1.00 39.38 ?  40  ASP D C     1 
ATOM   13679 O  O     . ASP D 2 61  ? 159.057 102.914 119.796 1.00 38.90 ?  40  ASP D O     1 
ATOM   13680 C  CB    . ASP D 2 61  ? 155.966 103.161 120.039 1.00 38.93 ?  40  ASP D CB    1 
ATOM   13681 C  CG    . ASP D 2 61  ? 155.152 104.135 120.842 1.00 38.21 ?  40  ASP D CG    1 
ATOM   13682 O  OD1   . ASP D 2 61  ? 155.362 105.361 120.712 1.00 38.79 ?  40  ASP D OD1   1 
ATOM   13683 O  OD2   . ASP D 2 61  ? 154.302 103.668 121.617 1.00 38.02 -1 40  ASP D OD2   1 
ATOM   13684 N  N     . LEU D 2 62  ? 158.220 102.237 117.820 1.00 39.82 ?  41  LEU D N     1 
ATOM   13685 C  CA    . LEU D 2 62  ? 159.317 101.324 117.522 1.00 40.22 ?  41  LEU D CA    1 
ATOM   13686 C  C     . LEU D 2 62  ? 160.646 102.065 117.375 1.00 40.40 ?  41  LEU D C     1 
ATOM   13687 O  O     . LEU D 2 62  ? 161.713 101.464 117.514 1.00 40.91 ?  41  LEU D O     1 
ATOM   13688 C  CB    . LEU D 2 62  ? 158.997 100.506 116.268 1.00 40.52 ?  41  LEU D CB    1 
ATOM   13689 C  CG    . LEU D 2 62  ? 157.815 99.536  116.380 1.00 41.03 ?  41  LEU D CG    1 
ATOM   13690 C  CD1   . LEU D 2 62  ? 157.544 98.862  115.042 1.00 42.53 ?  41  LEU D CD1   1 
ATOM   13691 C  CD2   . LEU D 2 62  ? 158.043 98.494  117.484 1.00 41.89 ?  41  LEU D CD2   1 
ATOM   13692 N  N     . LEU D 2 63  ? 160.563 103.374 117.120 1.00 40.20 ?  42  LEU D N     1 
ATOM   13693 C  CA    . LEU D 2 63  ? 161.725 104.249 116.970 1.00 39.85 ?  42  LEU D CA    1 
ATOM   13694 C  C     . LEU D 2 63  ? 162.391 104.615 118.310 1.00 38.90 ?  42  LEU D C     1 
ATOM   13695 O  O     . LEU D 2 63  ? 163.528 105.102 118.334 1.00 39.48 ?  42  LEU D O     1 
ATOM   13696 C  CB    . LEU D 2 63  ? 161.314 105.515 116.202 1.00 40.50 ?  42  LEU D CB    1 
ATOM   13697 C  CG    . LEU D 2 63  ? 162.277 106.246 115.252 1.00 41.98 ?  42  LEU D CG    1 
ATOM   13698 C  CD1   . LEU D 2 63  ? 162.835 105.329 114.169 1.00 43.07 ?  42  LEU D CD1   1 
ATOM   13699 C  CD2   . LEU D 2 63  ? 161.556 107.413 114.600 1.00 43.17 ?  42  LEU D CD2   1 
ATOM   13700 N  N     . THR D 2 64  ? 161.694 104.399 119.423 1.00 37.28 ?  43  THR D N     1 
ATOM   13701 C  CA    . THR D 2 64  ? 162.320 104.567 120.743 1.00 35.53 ?  43  THR D CA    1 
ATOM   13702 C  C     . THR D 2 64  ? 162.443 103.245 121.491 1.00 34.57 ?  43  THR D C     1 
ATOM   13703 O  O     . THR D 2 64  ? 163.356 103.066 122.300 1.00 34.23 ?  43  THR D O     1 
ATOM   13704 C  CB    . THR D 2 64  ? 161.619 105.621 121.629 1.00 35.18 ?  43  THR D CB    1 
ATOM   13705 O  OG1   . THR D 2 64  ? 160.205 105.400 121.642 1.00 34.59 ?  43  THR D OG1   1 
ATOM   13706 C  CG2   . THR D 2 64  ? 161.903 107.007 121.122 1.00 35.48 ?  43  THR D CG2   1 
ATOM   13707 N  N     . TRP D 2 65  ? 161.522 102.325 121.203 1.00 33.62 ?  44  TRP D N     1 
ATOM   13708 C  CA    . TRP D 2 65  ? 161.512 100.983 121.807 1.00 32.87 ?  44  TRP D CA    1 
ATOM   13709 C  C     . TRP D 2 65  ? 162.824 100.230 121.550 1.00 33.46 ?  44  TRP D C     1 
ATOM   13710 O  O     . TRP D 2 65  ? 163.378 99.609  122.458 1.00 32.58 ?  44  TRP D O     1 
ATOM   13711 C  CB    . TRP D 2 65  ? 160.317 100.179 121.269 1.00 32.09 ?  44  TRP D CB    1 
ATOM   13712 C  CG    . TRP D 2 65  ? 160.233 98.761  121.763 1.00 30.42 ?  44  TRP D CG    1 
ATOM   13713 C  CD1   . TRP D 2 65  ? 160.515 97.630  121.049 1.00 29.35 ?  44  TRP D CD1   1 
ATOM   13714 C  CD2   . TRP D 2 65  ? 159.835 98.322  123.071 1.00 28.04 ?  44  TRP D CD2   1 
ATOM   13715 N  NE1   . TRP D 2 65  ? 160.317 96.515  121.829 1.00 28.44 ?  44  TRP D NE1   1 
ATOM   13716 C  CE2   . TRP D 2 65  ? 159.904 96.911  123.075 1.00 28.14 ?  44  TRP D CE2   1 
ATOM   13717 C  CE3   . TRP D 2 65  ? 159.435 98.983  124.241 1.00 27.11 ?  44  TRP D CE3   1 
ATOM   13718 C  CZ2   . TRP D 2 65  ? 159.579 96.143  124.202 1.00 27.21 ?  44  TRP D CZ2   1 
ATOM   13719 C  CZ3   . TRP D 2 65  ? 159.104 98.217  125.362 1.00 27.45 ?  44  TRP D CZ3   1 
ATOM   13720 C  CH2   . TRP D 2 65  ? 159.175 96.810  125.328 1.00 27.25 ?  44  TRP D CH2   1 
ATOM   13721 N  N     . LYS D 2 66  ? 163.305 100.306 120.310 1.00 34.52 ?  45  LYS D N     1 
ATOM   13722 C  CA    . LYS D 2 66  ? 164.551 99.669  119.897 1.00 36.41 ?  45  LYS D CA    1 
ATOM   13723 C  C     . LYS D 2 66  ? 165.782 100.159 120.659 1.00 36.26 ?  45  LYS D C     1 
ATOM   13724 O  O     . LYS D 2 66  ? 166.795 99.463  120.703 1.00 36.52 ?  45  LYS D O     1 
ATOM   13725 C  CB    . LYS D 2 66  ? 164.769 99.838  118.388 1.00 36.98 ?  45  LYS D CB    1 
ATOM   13726 C  CG    . LYS D 2 66  ? 164.432 98.595  117.568 1.00 40.03 ?  45  LYS D CG    1 
ATOM   13727 C  CD    . LYS D 2 66  ? 162.926 98.312  117.519 1.00 43.70 ?  45  LYS D CD    1 
ATOM   13728 C  CE    . LYS D 2 66  ? 162.615 97.094  116.644 1.00 45.57 ?  45  LYS D CE    1 
ATOM   13729 N  NZ    . LYS D 2 66  ? 163.026 97.281  115.222 1.00 46.59 1  45  LYS D NZ    1 
ATOM   13730 N  N     . TYR D 2 67  ? 165.683 101.340 121.265 1.00 36.26 ?  46  TYR D N     1 
ATOM   13731 C  CA    . TYR D 2 67  ? 166.816 101.909 122.001 1.00 36.90 ?  46  TYR D CA    1 
ATOM   13732 C  C     . TYR D 2 67  ? 166.811 101.640 123.508 1.00 36.28 ?  46  TYR D C     1 
ATOM   13733 O  O     . TYR D 2 67  ? 167.731 102.056 124.205 1.00 36.44 ?  46  TYR D O     1 
ATOM   13734 C  CB    . TYR D 2 67  ? 166.966 103.409 121.720 1.00 37.15 ?  46  TYR D CB    1 
ATOM   13735 C  CG    . TYR D 2 67  ? 167.132 103.736 120.255 1.00 39.40 ?  46  TYR D CG    1 
ATOM   13736 C  CD1   . TYR D 2 67  ? 167.976 102.976 119.440 1.00 41.26 ?  46  TYR D CD1   1 
ATOM   13737 C  CD2   . TYR D 2 67  ? 166.467 104.818 119.686 1.00 41.06 ?  46  TYR D CD2   1 
ATOM   13738 C  CE1   . TYR D 2 67  ? 168.131 103.272 118.086 1.00 43.03 ?  46  TYR D CE1   1 
ATOM   13739 C  CE2   . TYR D 2 67  ? 166.621 105.128 118.333 1.00 43.05 ?  46  TYR D CE2   1 
ATOM   13740 C  CZ    . TYR D 2 67  ? 167.453 104.354 117.540 1.00 43.80 ?  46  TYR D CZ    1 
ATOM   13741 O  OH    . TYR D 2 67  ? 167.600 104.661 116.199 1.00 45.18 ?  46  TYR D OH    1 
ATOM   13742 N  N     . LEU D 2 68  ? 165.782 100.961 124.011 1.00 35.71 ?  47  LEU D N     1 
ATOM   13743 C  CA    . LEU D 2 68  ? 165.744 100.599 125.429 1.00 34.92 ?  47  LEU D CA    1 
ATOM   13744 C  C     . LEU D 2 68  ? 166.564 99.332  125.688 1.00 34.32 ?  47  LEU D C     1 
ATOM   13745 O  O     . LEU D 2 68  ? 166.647 98.449  124.830 1.00 34.50 ?  47  LEU D O     1 
ATOM   13746 C  CB    . LEU D 2 68  ? 164.302 100.413 125.924 1.00 35.00 ?  47  LEU D CB    1 
ATOM   13747 C  CG    . LEU D 2 68  ? 163.264 101.520 125.674 1.00 35.82 ?  47  LEU D CG    1 
ATOM   13748 C  CD1   . LEU D 2 68  ? 161.918 101.113 126.254 1.00 35.95 ?  47  LEU D CD1   1 
ATOM   13749 C  CD2   . LEU D 2 68  ? 163.696 102.877 126.230 1.00 35.97 ?  47  LEU D CD2   1 
ATOM   13750 N  N     . GLY D 2 69  ? 167.166 99.253  126.873 1.00 33.50 ?  48  GLY D N     1 
ATOM   13751 C  CA    . GLY D 2 69  ? 167.841 98.040  127.329 1.00 32.41 ?  48  GLY D CA    1 
ATOM   13752 C  C     . GLY D 2 69  ? 166.876 96.890  127.577 1.00 32.15 ?  48  GLY D C     1 
ATOM   13753 O  O     . GLY D 2 69  ? 165.655 97.085  127.633 1.00 30.98 ?  48  GLY D O     1 
ATOM   13754 N  N     . LYS D 2 70  ? 167.429 95.690  127.737 1.00 32.14 ?  49  LYS D N     1 
ATOM   13755 C  CA    . LYS D 2 70  ? 166.632 94.494  127.993 1.00 32.25 ?  49  LYS D CA    1 
ATOM   13756 C  C     . LYS D 2 70  ? 165.807 94.603  129.274 1.00 31.24 ?  49  LYS D C     1 
ATOM   13757 O  O     . LYS D 2 70  ? 164.642 94.214  129.276 1.00 31.34 ?  49  LYS D O     1 
ATOM   13758 C  CB    . LYS D 2 70  ? 167.514 93.245  128.036 1.00 33.07 ?  49  LYS D CB    1 
ATOM   13759 C  CG    . LYS D 2 70  ? 168.234 92.953  126.729 1.00 35.74 ?  49  LYS D CG    1 
ATOM   13760 C  CD    . LYS D 2 70  ? 169.300 91.882  126.940 1.00 39.67 ?  49  LYS D CD    1 
ATOM   13761 C  CE    . LYS D 2 70  ? 170.246 91.799  125.752 1.00 40.96 ?  49  LYS D CE    1 
ATOM   13762 N  NZ    . LYS D 2 70  ? 171.432 90.979  126.103 1.00 42.55 1  49  LYS D NZ    1 
ATOM   13763 N  N     . ASN D 2 71  ? 166.404 95.135  130.346 1.00 29.92 ?  50  ASN D N     1 
ATOM   13764 C  CA    . ASN D 2 71  ? 165.694 95.303  131.620 1.00 29.37 ?  50  ASN D CA    1 
ATOM   13765 C  C     . ASN D 2 71  ? 164.526 96.276  131.496 1.00 28.35 ?  50  ASN D C     1 
ATOM   13766 O  O     . ASN D 2 71  ? 163.457 96.035  132.071 1.00 27.64 ?  50  ASN D O     1 
ATOM   13767 C  CB    . ASN D 2 71  ? 166.628 95.747  132.762 1.00 29.38 ?  50  ASN D CB    1 
ATOM   13768 C  CG    . ASN D 2 71  ? 167.502 94.614  133.295 1.00 31.22 ?  50  ASN D CG    1 
ATOM   13769 O  OD1   . ASN D 2 71  ? 167.116 93.443  133.283 1.00 33.03 ?  50  ASN D OD1   1 
ATOM   13770 N  ND2   . ASN D 2 71  ? 168.689 94.966  133.779 1.00 31.97 ?  50  ASN D ND2   1 
ATOM   13771 N  N     . GLU D 2 72  ? 164.730 97.357  130.740 1.00 27.72 ?  51  GLU D N     1 
ATOM   13772 C  CA    . GLU D 2 72  ? 163.664 98.341  130.498 1.00 27.70 ?  51  GLU D CA    1 
ATOM   13773 C  C     . GLU D 2 72  ? 162.507 97.732  129.702 1.00 27.62 ?  51  GLU D C     1 
ATOM   13774 O  O     . GLU D 2 72  ? 161.334 97.963  130.013 1.00 27.56 ?  51  GLU D O     1 
ATOM   13775 C  CB    . GLU D 2 72  ? 164.197 99.576  129.763 1.00 27.55 ?  51  GLU D CB    1 
ATOM   13776 C  CG    . GLU D 2 72  ? 165.309 100.337 130.495 1.00 28.77 ?  51  GLU D CG    1 
ATOM   13777 C  CD    . GLU D 2 72  ? 165.692 101.610 129.762 1.00 31.18 ?  51  GLU D CD    1 
ATOM   13778 O  OE1   . GLU D 2 72  ? 166.331 101.515 128.693 1.00 33.17 ?  51  GLU D OE1   1 
ATOM   13779 O  OE2   . GLU D 2 72  ? 165.345 102.703 130.250 1.00 31.66 -1 51  GLU D OE2   1 
ATOM   13780 N  N     . GLN D 2 73  ? 162.846 96.954  128.678 1.00 27.32 ?  52  GLN D N     1 
ATOM   13781 C  CA    . GLN D 2 73  ? 161.844 96.303  127.840 1.00 27.33 ?  52  GLN D CA    1 
ATOM   13782 C  C     . GLN D 2 73  ? 161.090 95.241  128.644 1.00 26.85 ?  52  GLN D C     1 
ATOM   13783 O  O     . GLN D 2 73  ? 159.864 95.131  128.542 1.00 26.24 ?  52  GLN D O     1 
ATOM   13784 C  CB    . GLN D 2 73  ? 162.488 95.695  126.600 1.00 27.65 ?  52  GLN D CB    1 
ATOM   13785 C  CG    . GLN D 2 73  ? 162.931 96.717  125.535 1.00 29.66 ?  52  GLN D CG    1 
ATOM   13786 C  CD    . GLN D 2 73  ? 163.391 96.062  124.233 1.00 32.60 ?  52  GLN D CD    1 
ATOM   13787 O  OE1   . GLN D 2 73  ? 163.746 94.887  124.206 1.00 34.76 ?  52  GLN D OE1   1 
ATOM   13788 N  NE2   . GLN D 2 73  ? 163.402 96.831  123.154 1.00 33.42 ?  52  GLN D NE2   1 
ATOM   13789 N  N     . ASP D 2 74  ? 161.830 94.498  129.465 1.00 26.26 ?  53  ASP D N     1 
ATOM   13790 C  CA    . ASP D 2 74  ? 161.272 93.465  130.345 1.00 26.50 ?  53  ASP D CA    1 
ATOM   13791 C  C     . ASP D 2 74  ? 160.313 94.064  131.364 1.00 25.81 ?  53  ASP D C     1 
ATOM   13792 O  O     . ASP D 2 74  ? 159.205 93.564  131.540 1.00 26.12 ?  53  ASP D O     1 
ATOM   13793 C  CB    . ASP D 2 74  ? 162.408 92.730  131.070 1.00 26.84 ?  53  ASP D CB    1 
ATOM   13794 C  CG    . ASP D 2 74  ? 161.928 91.536  131.894 1.00 29.50 ?  53  ASP D CG    1 
ATOM   13795 O  OD1   . ASP D 2 74  ? 161.400 90.562  131.317 1.00 32.08 ?  53  ASP D OD1   1 
ATOM   13796 O  OD2   . ASP D 2 74  ? 162.124 91.554  133.126 1.00 33.52 -1 53  ASP D OD2   1 
ATOM   13797 N  N     . THR D 2 75  ? 160.734 95.135  132.034 1.00 25.10 ?  54  THR D N     1 
ATOM   13798 C  CA    . THR D 2 75  ? 159.877 95.787  133.029 1.00 24.11 ?  54  THR D CA    1 
ATOM   13799 C  C     . THR D 2 75  ? 158.599 96.315  132.371 1.00 23.82 ?  54  THR D C     1 
ATOM   13800 O  O     . THR D 2 75  ? 157.498 96.081  132.870 1.00 23.81 ?  54  THR D O     1 
ATOM   13801 C  CB    . THR D 2 75  ? 160.622 96.905  133.784 1.00 23.80 ?  54  THR D CB    1 
ATOM   13802 O  OG1   . THR D 2 75  ? 161.713 96.328  134.514 1.00 24.62 ?  54  THR D OG1   1 
ATOM   13803 C  CG2   . THR D 2 75  ? 159.683 97.626  134.767 1.00 23.25 ?  54  THR D CG2   1 
ATOM   13804 N  N     . TYR D 2 76  ? 158.757 97.033  131.268 1.00 24.06 ?  55  TYR D N     1 
ATOM   13805 C  CA    . TYR D 2 76  ? 157.617 97.554  130.519 1.00 24.76 ?  55  TYR D CA    1 
ATOM   13806 C  C     . TYR D 2 76  ? 156.603 96.463  130.144 1.00 24.85 ?  55  TYR D C     1 
ATOM   13807 O  O     . TYR D 2 76  ? 155.402 96.627  130.376 1.00 24.83 ?  55  TYR D O     1 
ATOM   13808 C  CB    . TYR D 2 76  ? 158.080 98.291  129.262 1.00 24.78 ?  55  TYR D CB    1 
ATOM   13809 C  CG    . TYR D 2 76  ? 157.042 99.254  128.724 1.00 26.19 ?  55  TYR D CG    1 
ATOM   13810 C  CD1   . TYR D 2 76  ? 157.027 100.585 129.145 1.00 27.81 ?  55  TYR D CD1   1 
ATOM   13811 C  CD2   . TYR D 2 76  ? 156.068 98.839  127.810 1.00 28.03 ?  55  TYR D CD2   1 
ATOM   13812 C  CE1   . TYR D 2 76  ? 156.084 101.483 128.664 1.00 29.32 ?  55  TYR D CE1   1 
ATOM   13813 C  CE2   . TYR D 2 76  ? 155.108 99.737  127.320 1.00 29.01 ?  55  TYR D CE2   1 
ATOM   13814 C  CZ    . TYR D 2 76  ? 155.129 101.057 127.758 1.00 30.76 ?  55  TYR D CZ    1 
ATOM   13815 O  OH    . TYR D 2 76  ? 154.210 101.970 127.295 1.00 34.50 ?  55  TYR D OH    1 
ATOM   13816 N  N     . MET D 2 77  ? 157.090 95.366  129.566 1.00 25.76 ?  56  MET D N     1 
ATOM   13817 C  CA    . MET D 2 77  ? 156.230 94.234  129.203 1.00 26.81 ?  56  MET D CA    1 
ATOM   13818 C  C     . MET D 2 77  ? 155.463 93.690  130.412 1.00 26.23 ?  56  MET D C     1 
ATOM   13819 O  O     . MET D 2 77  ? 154.255 93.457  130.339 1.00 25.00 ?  56  MET D O     1 
ATOM   13820 C  CB    . MET D 2 77  ? 157.047 93.114  128.563 1.00 28.11 ?  56  MET D CB    1 
ATOM   13821 C  CG    . MET D 2 77  ? 157.606 93.427  127.170 1.00 32.52 ?  56  MET D CG    1 
ATOM   13822 S  SD    . MET D 2 77  ? 156.364 93.444  125.867 1.00 42.68 ?  56  MET D SD    1 
ATOM   13823 C  CE    . MET D 2 77  ? 155.745 95.124  125.939 1.00 38.97 ?  56  MET D CE    1 
ATOM   13824 N  N     . LYS D 2 78  ? 156.183 93.487  131.516 1.00 26.01 ?  57  LYS D N     1 
ATOM   13825 C  CA    . LYS D 2 78  ? 155.594 92.925  132.735 1.00 26.07 ?  57  LYS D CA    1 
ATOM   13826 C  C     . LYS D 2 78  ? 154.555 93.854  133.360 1.00 25.69 ?  57  LYS D C     1 
ATOM   13827 O  O     . LYS D 2 78  ? 153.508 93.400  133.835 1.00 25.58 ?  57  LYS D O     1 
ATOM   13828 C  CB    . LYS D 2 78  ? 156.681 92.568  133.759 1.00 26.08 ?  57  LYS D CB    1 
ATOM   13829 C  CG    . LYS D 2 78  ? 157.552 91.374  133.344 1.00 27.64 ?  57  LYS D CG    1 
ATOM   13830 C  CD    . LYS D 2 78  ? 158.718 91.173  134.305 1.00 29.47 ?  57  LYS D CD    1 
ATOM   13831 C  CE    . LYS D 2 78  ? 159.441 89.869  134.004 1.00 31.69 ?  57  LYS D CE    1 
ATOM   13832 N  NZ    . LYS D 2 78  ? 160.574 89.625  134.937 1.00 33.36 1  57  LYS D NZ    1 
ATOM   13833 N  N     . VAL D 2 79  ? 154.854 95.151  133.359 1.00 25.32 ?  58  VAL D N     1 
ATOM   13834 C  CA    . VAL D 2 79  ? 153.940 96.169  133.889 1.00 25.47 ?  58  VAL D CA    1 
ATOM   13835 C  C     . VAL D 2 79  ? 152.676 96.198  133.038 1.00 25.09 ?  58  VAL D C     1 
ATOM   13836 O  O     . VAL D 2 79  ? 151.556 96.181  133.557 1.00 24.46 ?  58  VAL D O     1 
ATOM   13837 C  CB    . VAL D 2 79  ? 154.632 97.561  133.904 1.00 25.83 ?  58  VAL D CB    1 
ATOM   13838 C  CG1   . VAL D 2 79  ? 153.627 98.685  133.799 1.00 27.35 ?  58  VAL D CG1   1 
ATOM   13839 C  CG2   . VAL D 2 79  ? 155.514 97.696  135.145 1.00 26.42 ?  58  VAL D CG2   1 
ATOM   13840 N  N     . LEU D 2 80  ? 152.874 96.192  131.721 1.00 25.27 ?  59  LEU D N     1 
ATOM   13841 C  CA    . LEU D 2 80  ? 151.780 96.259  130.779 1.00 25.55 ?  59  LEU D CA    1 
ATOM   13842 C  C     . LEU D 2 80  ? 150.845 95.064  130.962 1.00 24.94 ?  59  LEU D C     1 
ATOM   13843 O  O     . LEU D 2 80  ? 149.628 95.231  130.974 1.00 24.82 ?  59  LEU D O     1 
ATOM   13844 C  CB    . LEU D 2 80  ? 152.321 96.297  129.348 1.00 25.80 ?  59  LEU D CB    1 
ATOM   13845 C  CG    . LEU D 2 80  ? 151.982 97.438  128.381 1.00 28.76 ?  59  LEU D CG    1 
ATOM   13846 C  CD1   . LEU D 2 80  ? 151.963 96.871  126.962 1.00 30.25 ?  59  LEU D CD1   1 
ATOM   13847 C  CD2   . LEU D 2 80  ? 150.675 98.153  128.682 1.00 27.79 ?  59  LEU D CD2   1 
ATOM   13848 N  N     . ALA D 2 81  ? 151.424 93.872  131.109 1.00 24.86 ?  60  ALA D N     1 
ATOM   13849 C  CA    . ALA D 2 81  ? 150.641 92.643  131.303 1.00 24.60 ?  60  ALA D CA    1 
ATOM   13850 C  C     . ALA D 2 81  ? 149.886 92.688  132.628 1.00 23.80 ?  60  ALA D C     1 
ATOM   13851 O  O     . ALA D 2 81  ? 148.747 92.243  132.717 1.00 24.07 ?  60  ALA D O     1 
ATOM   13852 C  CB    . ALA D 2 81  ? 151.546 91.413  131.245 1.00 24.48 ?  60  ALA D CB    1 
ATOM   13853 N  N     . GLY D 2 82  ? 150.527 93.238  133.652 1.00 23.54 ?  61  GLY D N     1 
ATOM   13854 C  CA    . GLY D 2 82  ? 149.889 93.438  134.949 1.00 22.53 ?  61  GLY D CA    1 
ATOM   13855 C  C     . GLY D 2 82  ? 148.647 94.297  134.831 1.00 22.23 ?  61  GLY D C     1 
ATOM   13856 O  O     . GLY D 2 82  ? 147.582 93.933  135.328 1.00 21.27 ?  61  GLY D O     1 
ATOM   13857 N  N     . LEU D 2 83  ? 148.781 95.443  134.164 1.00 22.36 ?  62  LEU D N     1 
ATOM   13858 C  CA    . LEU D 2 83  ? 147.641 96.343  133.952 1.00 22.42 ?  62  LEU D CA    1 
ATOM   13859 C  C     . LEU D 2 83  ? 146.542 95.663  133.147 1.00 22.91 ?  62  LEU D C     1 
ATOM   13860 O  O     . LEU D 2 83  ? 145.356 95.778  133.483 1.00 22.99 ?  62  LEU D O     1 
ATOM   13861 C  CB    . LEU D 2 83  ? 148.076 97.632  133.243 1.00 22.19 ?  62  LEU D CB    1 
ATOM   13862 C  CG    . LEU D 2 83  ? 149.025 98.561  134.017 1.00 22.17 ?  62  LEU D CG    1 
ATOM   13863 C  CD1   . LEU D 2 83  ? 149.631 99.599  133.063 1.00 21.55 ?  62  LEU D CD1   1 
ATOM   13864 C  CD2   . LEU D 2 83  ? 148.274 99.236  135.151 1.00 22.42 ?  62  LEU D CD2   1 
ATOM   13865 N  N     . THR D 2 84  ? 146.941 94.941  132.104 1.00 23.39 ?  63  THR D N     1 
ATOM   13866 C  CA    . THR D 2 84  ? 145.985 94.266  131.230 1.00 24.42 ?  63  THR D CA    1 
ATOM   13867 C  C     . THR D 2 84  ? 145.146 93.253  132.012 1.00 24.55 ?  63  THR D C     1 
ATOM   13868 O  O     . THR D 2 84  ? 143.915 93.252  131.926 1.00 23.68 ?  63  THR D O     1 
ATOM   13869 C  CB    . THR D 2 84  ? 146.689 93.556  130.045 1.00 24.70 ?  63  THR D CB    1 
ATOM   13870 O  OG1   . THR D 2 84  ? 147.421 94.521  129.278 1.00 25.57 ?  63  THR D OG1   1 
ATOM   13871 C  CG2   . THR D 2 84  ? 145.663 92.897  129.138 1.00 25.36 ?  63  THR D CG2   1 
ATOM   13872 N  N     . LEU D 2 85  ? 145.834 92.406  132.771 1.00 25.38 ?  64  LEU D N     1 
ATOM   13873 C  CA    . LEU D 2 85  ? 145.184 91.367  133.558 1.00 26.44 ?  64  LEU D CA    1 
ATOM   13874 C  C     . LEU D 2 85  ? 144.226 91.945  134.605 1.00 25.96 ?  64  LEU D C     1 
ATOM   13875 O  O     . LEU D 2 85  ? 143.079 91.487  134.703 1.00 25.83 ?  64  LEU D O     1 
ATOM   13876 C  CB    . LEU D 2 85  ? 146.218 90.402  134.159 1.00 26.65 ?  64  LEU D CB    1 
ATOM   13877 C  CG    . LEU D 2 85  ? 146.779 89.414  133.117 1.00 29.62 ?  64  LEU D CG    1 
ATOM   13878 C  CD1   . LEU D 2 85  ? 148.137 88.871  133.520 1.00 31.57 ?  64  LEU D CD1   1 
ATOM   13879 C  CD2   . LEU D 2 85  ? 145.807 88.252  132.841 1.00 30.96 ?  64  LEU D CD2   1 
ATOM   13880 N  N     . LEU D 2 86  ? 144.662 92.969  135.342 1.00 25.63 ?  65  LEU D N     1 
ATOM   13881 C  CA    . LEU D 2 86  ? 143.775 93.611  136.316 1.00 25.59 ?  65  LEU D CA    1 
ATOM   13882 C  C     . LEU D 2 86  ? 142.568 94.296  135.678 1.00 25.60 ?  65  LEU D C     1 
ATOM   13883 O  O     . LEU D 2 86  ? 141.463 94.263  136.227 1.00 25.47 ?  65  LEU D O     1 
ATOM   13884 C  CB    . LEU D 2 86  ? 144.532 94.593  137.231 1.00 25.76 ?  65  LEU D CB    1 
ATOM   13885 C  CG    . LEU D 2 86  ? 145.512 93.967  138.231 1.00 26.71 ?  65  LEU D CG    1 
ATOM   13886 C  CD1   . LEU D 2 86  ? 146.432 95.017  138.848 1.00 28.01 ?  65  LEU D CD1   1 
ATOM   13887 C  CD2   . LEU D 2 86  ? 144.784 93.214  139.321 1.00 28.01 ?  65  LEU D CD2   1 
ATOM   13888 N  N     . ASP D 2 87  ? 142.774 94.925  134.527 1.00 25.49 ?  66  ASP D N     1 
ATOM   13889 C  CA    . ASP D 2 87  ? 141.698 95.659  133.881 1.00 25.83 ?  66  ASP D CA    1 
ATOM   13890 C  C     . ASP D 2 87  ? 140.622 94.726  133.308 1.00 26.20 ?  66  ASP D C     1 
ATOM   13891 O  O     . ASP D 2 87  ? 139.450 95.081  133.260 1.00 25.99 ?  66  ASP D O     1 
ATOM   13892 C  CB    . ASP D 2 87  ? 142.249 96.585  132.805 1.00 25.50 ?  66  ASP D CB    1 
ATOM   13893 C  CG    . ASP D 2 87  ? 141.425 97.832  132.655 1.00 25.76 ?  66  ASP D CG    1 
ATOM   13894 O  OD1   . ASP D 2 87  ? 140.792 98.247  133.655 1.00 26.91 ?  66  ASP D OD1   1 
ATOM   13895 O  OD2   . ASP D 2 87  ? 141.403 98.404  131.548 1.00 23.11 -1 66  ASP D OD2   1 
ATOM   13896 N  N     . THR D 2 88  ? 141.034 93.528  132.901 1.00 27.12 ?  67  THR D N     1 
ATOM   13897 C  CA    . THR D 2 88  ? 140.117 92.497  132.435 1.00 28.40 ?  67  THR D CA    1 
ATOM   13898 C  C     . THR D 2 88  ? 139.177 92.050  133.542 1.00 28.28 ?  67  THR D C     1 
ATOM   13899 O  O     . THR D 2 88  ? 137.984 91.868  133.306 1.00 28.10 ?  67  THR D O     1 
ATOM   13900 C  CB    . THR D 2 88  ? 140.874 91.282  131.864 1.00 29.04 ?  67  THR D CB    1 
ATOM   13901 O  OG1   . THR D 2 88  ? 141.693 91.716  130.776 1.00 31.00 ?  67  THR D OG1   1 
ATOM   13902 C  CG2   . THR D 2 88  ? 139.896 90.230  131.348 1.00 30.16 ?  67  THR D CG2   1 
ATOM   13903 N  N     . GLU D 2 89  ? 139.707 91.875  134.751 1.00 28.28 ?  68  GLU D N     1 
ATOM   13904 C  CA    . GLU D 2 89  ? 138.858 91.548  135.892 1.00 29.16 ?  68  GLU D CA    1 
ATOM   13905 C  C     . GLU D 2 89  ? 137.825 92.652  136.107 1.00 28.65 ?  68  GLU D C     1 
ATOM   13906 O  O     . GLU D 2 89  ? 136.664 92.370  136.370 1.00 28.44 ?  68  GLU D O     1 
ATOM   13907 C  CB    . GLU D 2 89  ? 139.680 91.338  137.172 1.00 29.32 ?  68  GLU D CB    1 
ATOM   13908 C  CG    . GLU D 2 89  ? 140.706 90.199  137.095 1.00 31.95 ?  68  GLU D CG    1 
ATOM   13909 C  CD    . GLU D 2 89  ? 140.084 88.817  136.913 1.00 35.19 ?  68  GLU D CD    1 
ATOM   13910 O  OE1   . GLU D 2 89  ? 138.867 88.641  137.145 1.00 35.47 ?  68  GLU D OE1   1 
ATOM   13911 O  OE2   . GLU D 2 89  ? 140.832 87.894  136.528 1.00 38.06 -1 68  GLU D OE2   1 
ATOM   13912 N  N     . GLN D 2 90  ? 138.250 93.905  135.974 1.00 28.45 ?  69  GLN D N     1 
ATOM   13913 C  CA    . GLN D 2 90  ? 137.345 95.036  136.181 1.00 28.47 ?  69  GLN D CA    1 
ATOM   13914 C  C     . GLN D 2 90  ? 136.236 95.087  135.121 1.00 28.97 ?  69  GLN D C     1 
ATOM   13915 O  O     . GLN D 2 90  ? 135.088 95.391  135.438 1.00 28.84 ?  69  GLN D O     1 
ATOM   13916 C  CB    . GLN D 2 90  ? 138.125 96.353  136.247 1.00 28.21 ?  69  GLN D CB    1 
ATOM   13917 C  CG    . GLN D 2 90  ? 137.355 97.518  136.868 1.00 27.75 ?  69  GLN D CG    1 
ATOM   13918 C  CD    . GLN D 2 90  ? 137.153 97.397  138.374 1.00 28.91 ?  69  GLN D CD    1 
ATOM   13919 O  OE1   . GLN D 2 90  ? 137.215 96.301  138.950 1.00 27.62 ?  69  GLN D OE1   1 
ATOM   13920 N  NE2   . GLN D 2 90  ? 136.885 98.532  139.020 1.00 28.23 ?  69  GLN D NE2   1 
ATOM   13921 N  N     . GLY D 2 91  ? 136.581 94.762  133.874 1.00 29.62 ?  70  GLY D N     1 
ATOM   13922 C  CA    . GLY D 2 91  ? 135.604 94.717  132.784 1.00 30.43 ?  70  GLY D CA    1 
ATOM   13923 C  C     . GLY D 2 91  ? 134.638 93.539  132.835 1.00 31.11 ?  70  GLY D C     1 
ATOM   13924 O  O     . GLY D 2 91  ? 133.443 93.684  132.555 1.00 30.77 ?  70  GLY D O     1 
ATOM   13925 N  N     . ASN D 2 92  ? 135.149 92.367  133.180 1.00 31.69 ?  71  ASN D N     1 
ATOM   13926 C  CA    . ASN D 2 92  ? 134.305 91.178  133.222 1.00 32.72 ?  71  ASN D CA    1 
ATOM   13927 C  C     . ASN D 2 92  ? 133.491 91.006  134.496 1.00 32.60 ?  71  ASN D C     1 
ATOM   13928 O  O     . ASN D 2 92  ? 132.405 90.423  134.453 1.00 33.12 ?  71  ASN D O     1 
ATOM   13929 C  CB    . ASN D 2 92  ? 135.129 89.927  132.947 1.00 33.68 ?  71  ASN D CB    1 
ATOM   13930 C  CG    . ASN D 2 92  ? 135.558 89.828  131.498 1.00 35.15 ?  71  ASN D CG    1 
ATOM   13931 O  OD1   . ASN D 2 92  ? 136.573 89.214  131.194 1.00 40.21 ?  71  ASN D OD1   1 
ATOM   13932 N  ND2   . ASN D 2 92  ? 134.790 90.444  130.597 1.00 36.91 ?  71  ASN D ND2   1 
ATOM   13933 N  N     . THR D 2 93  ? 134.002 91.530  135.611 1.00 31.76 ?  72  THR D N     1 
ATOM   13934 C  CA    . THR D 2 93  ? 133.379 91.317  136.912 1.00 31.47 ?  72  THR D CA    1 
ATOM   13935 C  C     . THR D 2 93  ? 133.122 92.604  137.694 1.00 30.62 ?  72  THR D C     1 
ATOM   13936 O  O     . THR D 2 93  ? 131.980 92.894  138.039 1.00 30.71 ?  72  THR D O     1 
ATOM   13937 C  CB    . THR D 2 93  ? 134.213 90.361  137.761 1.00 31.60 ?  72  THR D CB    1 
ATOM   13938 O  OG1   . THR D 2 93  ? 134.404 89.140  137.034 1.00 33.14 ?  72  THR D OG1   1 
ATOM   13939 C  CG2   . THR D 2 93  ? 133.516 90.064  139.079 1.00 31.89 ?  72  THR D CG2   1 
ATOM   13940 N  N     . GLY D 2 94  ? 134.181 93.365  137.961 1.00 29.61 ?  73  GLY D N     1 
ATOM   13941 C  CA    . GLY D 2 94  ? 134.104 94.541  138.830 1.00 28.47 ?  73  GLY D CA    1 
ATOM   13942 C  C     . GLY D 2 94  ? 133.016 95.541  138.495 1.00 27.90 ?  73  GLY D C     1 
ATOM   13943 O  O     . GLY D 2 94  ? 132.183 95.884  139.346 1.00 28.27 ?  73  GLY D O     1 
ATOM   13944 N  N     . MET D 2 95  ? 133.021 96.044  137.269 1.00 26.67 ?  74  MET D N     1 
ATOM   13945 C  CA    . MET D 2 95  ? 132.001 97.026  136.907 1.00 26.00 ?  74  MET D CA    1 
ATOM   13946 C  C     . MET D 2 95  ? 130.634 96.382  136.714 1.00 25.25 ?  74  MET D C     1 
ATOM   13947 O  O     . MET D 2 95  ? 129.645 96.931  137.183 1.00 24.97 ?  74  MET D O     1 
ATOM   13948 C  CB    . MET D 2 95  ? 132.395 97.869  135.687 1.00 26.00 ?  74  MET D CB    1 
ATOM   13949 C  CG    . MET D 2 95  ? 133.360 98.986  136.002 1.00 26.40 ?  74  MET D CG    1 
ATOM   13950 S  SD    . MET D 2 95  ? 132.719 100.206 137.177 1.00 28.10 ?  74  MET D SD    1 
ATOM   13951 C  CE    . MET D 2 95  ? 134.197 101.187 137.402 1.00 28.95 ?  74  MET D CE    1 
ATOM   13952 N  N     . PRO D 2 96  ? 130.566 95.230  136.019 1.00 24.98 ?  75  PRO D N     1 
ATOM   13953 C  CA    . PRO D 2 96  ? 129.214 94.671  135.845 1.00 24.59 ?  75  PRO D CA    1 
ATOM   13954 C  C     . PRO D 2 96  ? 128.550 94.216  137.143 1.00 23.90 ?  75  PRO D C     1 
ATOM   13955 O  O     . PRO D 2 96  ? 127.332 94.298  137.246 1.00 23.45 ?  75  PRO D O     1 
ATOM   13956 C  CB    . PRO D 2 96  ? 129.436 93.466  134.921 1.00 24.80 ?  75  PRO D CB    1 
ATOM   13957 C  CG    . PRO D 2 96  ? 130.705 93.796  134.169 1.00 25.75 ?  75  PRO D CG    1 
ATOM   13958 C  CD    . PRO D 2 96  ? 131.557 94.553  135.154 1.00 25.07 ?  75  PRO D CD    1 
ATOM   13959 N  N     . ILE D 2 97  ? 129.331 93.736  138.114 1.00 23.36 ?  76  ILE D N     1 
ATOM   13960 C  CA    . ILE D 2 97  ? 128.744 93.261  139.363 1.00 23.48 ?  76  ILE D CA    1 
ATOM   13961 C  C     . ILE D 2 97  ? 128.210 94.424  140.183 1.00 23.30 ?  76  ILE D C     1 
ATOM   13962 O  O     . ILE D 2 97  ? 127.163 94.304  140.815 1.00 23.45 ?  76  ILE D O     1 
ATOM   13963 C  CB    . ILE D 2 97  ? 129.713 92.368  140.189 1.00 23.96 ?  76  ILE D CB    1 
ATOM   13964 C  CG1   . ILE D 2 97  ? 128.934 91.417  141.090 1.00 24.71 ?  76  ILE D CG1   1 
ATOM   13965 C  CG2   . ILE D 2 97  ? 130.730 93.204  141.004 1.00 24.02 ?  76  ILE D CG2   1 
ATOM   13966 C  CD1   . ILE D 2 97  ? 129.651 90.058  141.277 1.00 29.17 ?  76  ILE D CD1   1 
ATOM   13967 N  N     . VAL D 2 98  ? 128.921 95.550  140.160 1.00 22.71 ?  77  VAL D N     1 
ATOM   13968 C  CA    . VAL D 2 98  ? 128.466 96.755  140.873 1.00 22.78 ?  77  VAL D CA    1 
ATOM   13969 C  C     . VAL D 2 98  ? 127.217 97.329  140.202 1.00 22.89 ?  77  VAL D C     1 
ATOM   13970 O  O     . VAL D 2 98  ? 126.258 97.704  140.877 1.00 23.72 ?  77  VAL D O     1 
ATOM   13971 C  CB    . VAL D 2 98  ? 129.604 97.805  141.009 1.00 22.49 ?  77  VAL D CB    1 
ATOM   13972 C  CG1   . VAL D 2 98  ? 129.077 99.150  141.543 1.00 21.91 ?  77  VAL D CG1   1 
ATOM   13973 C  CG2   . VAL D 2 98  ? 130.684 97.271  141.935 1.00 23.02 ?  77  VAL D CG2   1 
ATOM   13974 N  N     . ALA D 2 99  ? 127.213 97.363  138.870 1.00 23.19 ?  78  ALA D N     1 
ATOM   13975 C  CA    . ALA D 2 99  ? 126.034 97.822  138.121 1.00 23.05 ?  78  ALA D CA    1 
ATOM   13976 C  C     . ALA D 2 99  ? 124.806 96.970  138.454 1.00 23.52 ?  78  ALA D C     1 
ATOM   13977 O  O     . ALA D 2 99  ? 123.684 97.477  138.560 1.00 23.68 ?  78  ALA D O     1 
ATOM   13978 C  CB    . ALA D 2 99  ? 126.317 97.808  136.628 1.00 22.81 ?  78  ALA D CB    1 
ATOM   13979 N  N     . GLU D 2 100 ? 125.020 95.669  138.627 1.00 23.68 ?  79  GLU D N     1 
ATOM   13980 C  CA    . GLU D 2 100 ? 123.934 94.756  138.976 1.00 24.14 ?  79  GLU D CA    1 
ATOM   13981 C  C     . GLU D 2 100 ? 123.281 95.047  140.337 1.00 23.66 ?  79  GLU D C     1 
ATOM   13982 O  O     . GLU D 2 100 ? 122.054 94.998  140.468 1.00 22.94 ?  79  GLU D O     1 
ATOM   13983 C  CB    . GLU D 2 100 ? 124.442 93.315  138.930 1.00 24.47 ?  79  GLU D CB    1 
ATOM   13984 C  CG    . GLU D 2 100 ? 123.347 92.271  139.042 1.00 27.90 ?  79  GLU D CG    1 
ATOM   13985 C  CD    . GLU D 2 100 ? 123.896 90.862  139.173 1.00 32.30 ?  79  GLU D CD    1 
ATOM   13986 O  OE1   . GLU D 2 100 ? 125.027 90.605  138.700 1.00 32.88 ?  79  GLU D OE1   1 
ATOM   13987 O  OE2   . GLU D 2 100 ? 123.191 90.013  139.756 1.00 34.74 -1 79  GLU D OE2   1 
ATOM   13988 N  N     . HIS D 2 101 ? 124.097 95.337  141.349 1.00 23.62 ?  80  HIS D N     1 
ATOM   13989 C  CA    . HIS D 2 101 ? 123.584 95.526  142.719 1.00 23.99 ?  80  HIS D CA    1 
ATOM   13990 C  C     . HIS D 2 101 ? 123.190 96.957  143.108 1.00 24.35 ?  80  HIS D C     1 
ATOM   13991 O  O     . HIS D 2 101 ? 122.464 97.151  144.083 1.00 24.21 ?  80  HIS D O     1 
ATOM   13992 C  CB    . HIS D 2 101 ? 124.562 94.929  143.742 1.00 24.13 ?  80  HIS D CB    1 
ATOM   13993 C  CG    . HIS D 2 101 ? 124.690 93.438  143.641 1.00 24.76 ?  80  HIS D CG    1 
ATOM   13994 N  ND1   . HIS D 2 101 ? 123.935 92.572  144.404 1.00 25.68 ?  80  HIS D ND1   1 
ATOM   13995 C  CD2   . HIS D 2 101 ? 125.467 92.662  142.850 1.00 25.75 ?  80  HIS D CD2   1 
ATOM   13996 C  CE1   . HIS D 2 101 ? 124.247 91.326  144.089 1.00 26.21 ?  80  HIS D CE1   1 
ATOM   13997 N  NE2   . HIS D 2 101 ? 125.174 91.352  143.150 1.00 25.35 ?  80  HIS D NE2   1 
ATOM   13998 N  N     . VAL D 2 102 ? 123.671 97.954  142.366 1.00 24.50 ?  81  VAL D N     1 
ATOM   13999 C  CA    . VAL D 2 102 ? 123.307 99.346  142.624 1.00 25.50 ?  81  VAL D CA    1 
ATOM   14000 C  C     . VAL D 2 102 ? 121.886 99.626  142.110 1.00 26.14 ?  81  VAL D C     1 
ATOM   14001 O  O     . VAL D 2 102 ? 121.545 99.232  140.998 1.00 26.96 ?  81  VAL D O     1 
ATOM   14002 C  CB    . VAL D 2 102 ? 124.324 100.326 141.967 1.00 25.30 ?  81  VAL D CB    1 
ATOM   14003 C  CG1   . VAL D 2 102 ? 123.809 101.745 141.992 1.00 27.08 ?  81  VAL D CG1   1 
ATOM   14004 C  CG2   . VAL D 2 102 ? 125.660 100.259 142.688 1.00 25.41 ?  81  VAL D CG2   1 
ATOM   14005 N  N     . ASP D 2 103 ? 121.067 100.284 142.928 1.00 26.45 ?  82  ASP D N     1 
ATOM   14006 C  CA    . ASP D 2 103 ? 119.727 100.705 142.513 1.00 27.15 ?  82  ASP D CA    1 
ATOM   14007 C  C     . ASP D 2 103 ? 119.770 102.095 141.895 1.00 26.39 ?  82  ASP D C     1 
ATOM   14008 O  O     . ASP D 2 103 ? 120.504 102.975 142.363 1.00 26.40 ?  82  ASP D O     1 
ATOM   14009 C  CB    . ASP D 2 103 ? 118.753 100.705 143.696 1.00 27.72 ?  82  ASP D CB    1 
ATOM   14010 C  CG    . ASP D 2 103 ? 118.548 99.322  144.303 1.00 31.46 ?  82  ASP D CG    1 
ATOM   14011 O  OD1   . ASP D 2 103 ? 118.608 98.297  143.572 1.00 34.26 ?  82  ASP D OD1   1 
ATOM   14012 O  OD2   . ASP D 2 103 ? 118.313 99.259  145.532 1.00 35.52 -1 82  ASP D OD2   1 
ATOM   14013 N  N     . GLY D 2 104 ? 118.964 102.292 140.856 1.00 25.52 ?  83  GLY D N     1 
ATOM   14014 C  CA    . GLY D 2 104 ? 118.866 103.588 140.188 1.00 24.31 ?  83  GLY D CA    1 
ATOM   14015 C  C     . GLY D 2 104 ? 119.180 103.418 138.706 1.00 23.27 ?  83  GLY D C     1 
ATOM   14016 O  O     . GLY D 2 104 ? 120.241 102.912 138.343 1.00 22.38 ?  83  GLY D O     1 
ATOM   14017 N  N     . HIS D 2 105 ? 118.248 103.826 137.850 1.00 22.46 ?  84  HIS D N     1 
ATOM   14018 C  CA    . HIS D 2 105 ? 118.441 103.699 136.404 1.00 22.17 ?  84  HIS D CA    1 
ATOM   14019 C  C     . HIS D 2 105 ? 119.625 104.495 135.880 1.00 21.13 ?  84  HIS D C     1 
ATOM   14020 O  O     . HIS D 2 105 ? 120.351 104.020 135.009 1.00 20.91 ?  84  HIS D O     1 
ATOM   14021 C  CB    . HIS D 2 105 ? 117.163 104.094 135.650 1.00 22.07 ?  84  HIS D CB    1 
ATOM   14022 C  CG    . HIS D 2 105 ? 115.982 103.256 136.023 1.00 23.85 ?  84  HIS D CG    1 
ATOM   14023 N  ND1   . HIS D 2 105 ? 116.021 101.878 136.004 1.00 24.86 ?  84  HIS D ND1   1 
ATOM   14024 C  CD2   . HIS D 2 105 ? 114.747 103.593 136.459 1.00 25.19 ?  84  HIS D CD2   1 
ATOM   14025 C  CE1   . HIS D 2 105 ? 114.851 101.403 136.393 1.00 24.94 ?  84  HIS D CE1   1 
ATOM   14026 N  NE2   . HIS D 2 105 ? 114.064 102.423 136.679 1.00 26.41 ?  84  HIS D NE2   1 
ATOM   14027 N  N     . GLN D 2 106 ? 119.818 105.697 136.404 1.00 20.66 ?  85  GLN D N     1 
ATOM   14028 C  CA    . GLN D 2 106 ? 120.857 106.574 135.872 1.00 20.70 ?  85  GLN D CA    1 
ATOM   14029 C  C     . GLN D 2 106 ? 122.236 106.075 136.299 1.00 20.46 ?  85  GLN D C     1 
ATOM   14030 O  O     . GLN D 2 106 ? 123.179 106.112 135.509 1.00 20.72 ?  85  GLN D O     1 
ATOM   14031 C  CB    . GLN D 2 106 ? 120.591 108.044 136.237 1.00 20.60 ?  85  GLN D CB    1 
ATOM   14032 C  CG    . GLN D 2 106 ? 119.255 108.576 135.650 1.00 20.74 ?  85  GLN D CG    1 
ATOM   14033 C  CD    . GLN D 2 106 ? 118.854 109.969 136.152 1.00 22.11 ?  85  GLN D CD    1 
ATOM   14034 O  OE1   . GLN D 2 106 ? 119.701 110.788 136.494 1.00 22.88 ?  85  GLN D OE1   1 
ATOM   14035 N  NE2   . GLN D 2 106 ? 117.552 110.239 136.180 1.00 21.64 ?  85  GLN D NE2   1 
ATOM   14036 N  N     . ARG D 2 107 ? 122.332 105.563 137.528 1.00 20.17 ?  86  ARG D N     1 
ATOM   14037 C  CA    . ARG D 2 107 ? 123.578 104.975 138.024 1.00 20.29 ?  86  ARG D CA    1 
ATOM   14038 C  C     . ARG D 2 107 ? 123.940 103.731 137.231 1.00 20.07 ?  86  ARG D C     1 
ATOM   14039 O  O     . ARG D 2 107 ? 125.098 103.534 136.887 1.00 19.53 ?  86  ARG D O     1 
ATOM   14040 C  CB    . ARG D 2 107 ? 123.461 104.607 139.501 1.00 20.88 ?  86  ARG D CB    1 
ATOM   14041 C  CG    . ARG D 2 107 ? 123.129 105.775 140.370 1.00 22.56 ?  86  ARG D CG    1 
ATOM   14042 C  CD    . ARG D 2 107 ? 122.701 105.318 141.741 1.00 27.21 ?  86  ARG D CD    1 
ATOM   14043 N  NE    . ARG D 2 107 ? 122.901 106.442 142.636 1.00 31.70 ?  86  ARG D NE    1 
ATOM   14044 C  CZ    . ARG D 2 107 ? 123.022 106.360 143.945 1.00 32.23 ?  86  ARG D CZ    1 
ATOM   14045 N  NH1   . ARG D 2 107 ? 122.952 105.182 144.562 1.00 34.27 1  86  ARG D NH1   1 
ATOM   14046 N  NH2   . ARG D 2 107 ? 123.220 107.475 144.624 1.00 33.79 ?  86  ARG D NH2   1 
ATOM   14047 N  N     . LYS D 2 108 ? 122.946 102.883 136.957 1.00 19.61 ?  87  LYS D N     1 
ATOM   14048 C  CA    . LYS D 2 108 ? 123.189 101.690 136.148 1.00 19.92 ?  87  LYS D CA    1 
ATOM   14049 C  C     . LYS D 2 108 ? 123.704 102.049 134.750 1.00 20.08 ?  87  LYS D C     1 
ATOM   14050 O  O     . LYS D 2 108 ? 124.529 101.324 134.183 1.00 20.38 ?  87  LYS D O     1 
ATOM   14051 C  CB    . LYS D 2 108 ? 121.947 100.800 136.056 1.00 19.54 ?  87  LYS D CB    1 
ATOM   14052 C  CG    . LYS D 2 108 ? 121.539 100.161 137.370 1.00 20.55 ?  87  LYS D CG    1 
ATOM   14053 C  CD    . LYS D 2 108 ? 120.310 99.266  137.198 1.00 21.09 ?  87  LYS D CD    1 
ATOM   14054 C  CE    . LYS D 2 108 ? 119.911 98.581  138.500 1.00 22.98 ?  87  LYS D CE    1 
ATOM   14055 N  NZ    . LYS D 2 108 ? 120.899 97.495  138.866 1.00 22.30 1  87  LYS D NZ    1 
ATOM   14056 N  N     . ALA D 2 109 ? 123.213 103.156 134.195 1.00 19.72 ?  88  ALA D N     1 
ATOM   14057 C  CA    . ALA D 2 109 ? 123.642 103.588 132.870 1.00 19.83 ?  88  ALA D CA    1 
ATOM   14058 C  C     . ALA D 2 109 ? 125.099 104.054 132.880 1.00 19.84 ?  88  ALA D C     1 
ATOM   14059 O  O     . ALA D 2 109 ? 125.886 103.670 132.008 1.00 19.96 ?  88  ALA D O     1 
ATOM   14060 C  CB    . ALA D 2 109 ? 122.709 104.681 132.320 1.00 19.65 ?  88  ALA D CB    1 
ATOM   14061 N  N     . VAL D 2 110 ? 125.462 104.857 133.878 1.00 19.33 ?  89  VAL D N     1 
ATOM   14062 C  CA    . VAL D 2 110 ? 126.846 105.333 134.014 1.00 19.22 ?  89  VAL D CA    1 
ATOM   14063 C  C     . VAL D 2 110 ? 127.776 104.122 134.219 1.00 19.45 ?  89  VAL D C     1 
ATOM   14064 O  O     . VAL D 2 110 ? 128.765 103.950 133.493 1.00 18.97 ?  89  VAL D O     1 
ATOM   14065 C  CB    . VAL D 2 110 ? 126.966 106.402 135.138 1.00 19.01 ?  89  VAL D CB    1 
ATOM   14066 C  CG1   . VAL D 2 110 ? 128.448 106.776 135.430 1.00 19.90 ?  89  VAL D CG1   1 
ATOM   14067 C  CG2   . VAL D 2 110 ? 126.200 107.643 134.735 1.00 19.69 ?  89  VAL D CG2   1 
ATOM   14068 N  N     . LEU D 2 111 ? 127.410 103.248 135.158 1.00 19.27 ?  90  LEU D N     1 
ATOM   14069 C  CA    . LEU D 2 111 ? 128.188 102.030 135.393 1.00 19.96 ?  90  LEU D CA    1 
ATOM   14070 C  C     . LEU D 2 111 ? 128.334 101.148 134.145 1.00 20.30 ?  90  LEU D C     1 
ATOM   14071 O  O     . LEU D 2 111 ? 129.422 100.629 133.882 1.00 19.88 ?  90  LEU D O     1 
ATOM   14072 C  CB    . LEU D 2 111 ? 127.647 101.244 136.595 1.00 19.87 ?  90  LEU D CB    1 
ATOM   14073 C  CG    . LEU D 2 111 ? 127.836 101.974 137.926 1.00 20.24 ?  90  LEU D CG    1 
ATOM   14074 C  CD1   . LEU D 2 111 ? 126.998 101.370 139.065 1.00 21.85 ?  90  LEU D CD1   1 
ATOM   14075 C  CD2   . LEU D 2 111 ? 129.326 102.053 138.309 1.00 20.29 ?  90  LEU D CD2   1 
ATOM   14076 N  N     . ASN D 2 112 ? 127.256 101.002 133.371 1.00 20.92 ?  91  ASN D N     1 
ATOM   14077 C  CA    . ASN D 2 112 ? 127.327 100.308 132.064 1.00 20.70 ?  91  ASN D CA    1 
ATOM   14078 C  C     . ASN D 2 112 ? 128.310 100.951 131.101 1.00 20.57 ?  91  ASN D C     1 
ATOM   14079 O  O     . ASN D 2 112 ? 128.996 100.255 130.335 1.00 20.45 ?  91  ASN D O     1 
ATOM   14080 C  CB    . ASN D 2 112 ? 125.969 100.302 131.361 1.00 21.16 ?  91  ASN D CB    1 
ATOM   14081 C  CG    . ASN D 2 112 ? 125.179 99.032  131.602 1.00 21.98 ?  91  ASN D CG    1 
ATOM   14082 O  OD1   . ASN D 2 112 ? 125.581 98.157  132.375 1.00 25.37 ?  91  ASN D OD1   1 
ATOM   14083 N  ND2   . ASN D 2 112 ? 124.033 98.936  130.954 1.00 21.12 ?  91  ASN D ND2   1 
ATOM   14084 N  N     . PHE D 2 113 ? 128.312 102.281 131.078 1.00 19.70 ?  92  PHE D N     1 
ATOM   14085 C  CA    . PHE D 2 113 ? 129.234 103.006 130.232 1.00 20.02 ?  92  PHE D CA    1 
ATOM   14086 C  C     . PHE D 2 113 ? 130.688 102.726 130.643 1.00 19.97 ?  92  PHE D C     1 
ATOM   14087 O  O     . PHE D 2 113 ? 131.546 102.473 129.790 1.00 19.22 ?  92  PHE D O     1 
ATOM   14088 C  CB    . PHE D 2 113 ? 128.944 104.516 130.215 1.00 20.09 ?  92  PHE D CB    1 
ATOM   14089 C  CG    . PHE D 2 113 ? 129.769 105.252 129.218 1.00 20.54 ?  92  PHE D CG    1 
ATOM   14090 C  CD1   . PHE D 2 113 ? 129.318 105.412 127.906 1.00 20.14 ?  92  PHE D CD1   1 
ATOM   14091 C  CD2   . PHE D 2 113 ? 131.032 105.732 129.568 1.00 20.77 ?  92  PHE D CD2   1 
ATOM   14092 C  CE1   . PHE D 2 113 ? 130.105 106.067 126.963 1.00 20.54 ?  92  PHE D CE1   1 
ATOM   14093 C  CE2   . PHE D 2 113 ? 131.829 106.382 128.627 1.00 21.23 ?  92  PHE D CE2   1 
ATOM   14094 C  CZ    . PHE D 2 113 ? 131.358 106.545 127.318 1.00 20.92 ?  92  PHE D CZ    1 
ATOM   14095 N  N     . MET D 2 114 ? 130.949 102.761 131.946 1.00 19.67 ?  93  MET D N     1 
ATOM   14096 C  CA    . MET D 2 114 ? 132.276 102.445 132.460 1.00 20.55 ?  93  MET D CA    1 
ATOM   14097 C  C     . MET D 2 114 ? 132.699 101.012 132.132 1.00 20.82 ?  93  MET D C     1 
ATOM   14098 O  O     . MET D 2 114 ? 133.839 100.806 131.737 1.00 20.43 ?  93  MET D O     1 
ATOM   14099 C  CB    . MET D 2 114 ? 132.357 102.702 133.960 1.00 20.24 ?  93  MET D CB    1 
ATOM   14100 C  CG    . MET D 2 114 ? 132.010 104.139 134.292 1.00 22.05 ?  93  MET D CG    1 
ATOM   14101 S  SD    . MET D 2 114 ? 131.888 104.484 136.032 1.00 25.85 ?  93  MET D SD    1 
ATOM   14102 C  CE    . MET D 2 114 ? 132.196 106.257 136.004 1.00 27.57 ?  93  MET D CE    1 
ATOM   14103 N  N     . ALA D 2 115 ? 131.786 100.043 132.291 1.00 21.19 ?  94  ALA D N     1 
ATOM   14104 C  CA    . ALA D 2 115 ? 132.070 98.641  131.926 1.00 21.53 ?  94  ALA D CA    1 
ATOM   14105 C  C     . ALA D 2 115 ? 132.402 98.524  130.440 1.00 21.75 ?  94  ALA D C     1 
ATOM   14106 O  O     . ALA D 2 115 ? 133.351 97.831  130.072 1.00 22.18 ?  94  ALA D O     1 
ATOM   14107 C  CB    . ALA D 2 115 ? 130.905 97.718  132.299 1.00 21.32 ?  94  ALA D CB    1 
ATOM   14108 N  N     . MET D 2 116 ? 131.640 99.224  129.597 1.00 21.47 ?  95  MET D N     1 
ATOM   14109 C  CA    . MET D 2 116 ? 131.915 99.278  128.165 1.00 21.83 ?  95  MET D CA    1 
ATOM   14110 C  C     . MET D 2 116 ? 133.350 99.760  127.875 1.00 22.15 ?  95  MET D C     1 
ATOM   14111 O  O     . MET D 2 116 ? 134.055 99.155  127.070 1.00 22.09 ?  95  MET D O     1 
ATOM   14112 C  CB    . MET D 2 116 ? 130.883 100.165 127.448 1.00 21.72 ?  95  MET D CB    1 
ATOM   14113 C  CG    . MET D 2 116 ? 131.137 100.376 125.946 1.00 22.57 ?  95  MET D CG    1 
ATOM   14114 S  SD    . MET D 2 116 ? 132.408 101.608 125.562 1.00 22.75 ?  95  MET D SD    1 
ATOM   14115 C  CE    . MET D 2 116 ? 131.631 103.121 126.131 1.00 22.96 ?  95  MET D CE    1 
ATOM   14116 N  N     . MET D 2 117 ? 133.770 100.843 128.533 1.00 22.04 ?  96  MET D N     1 
ATOM   14117 C  CA    . MET D 2 117 ? 135.122 101.393 128.337 1.00 22.45 ?  96  MET D CA    1 
ATOM   14118 C  C     . MET D 2 117 ? 136.211 100.365 128.690 1.00 22.39 ?  96  MET D C     1 
ATOM   14119 O  O     . MET D 2 117 ? 137.217 100.254 127.987 1.00 21.88 ?  96  MET D O     1 
ATOM   14120 C  CB    . MET D 2 117 ? 135.315 102.699 129.134 1.00 22.00 ?  96  MET D CB    1 
ATOM   14121 C  CG    . MET D 2 117 ? 134.534 103.907 128.553 1.00 23.25 ?  96  MET D CG    1 
ATOM   14122 S  SD    . MET D 2 117 ? 134.964 104.299 126.840 1.00 24.28 ?  96  MET D SD    1 
ATOM   14123 C  CE    . MET D 2 117 ? 136.590 105.021 127.032 1.00 24.59 ?  96  MET D CE    1 
ATOM   14124 N  N     . GLU D 2 118 ? 135.996 99.604  129.763 1.00 22.66 ?  97  GLU D N     1 
ATOM   14125 C  CA    . GLU D 2 118 ? 136.942 98.552  130.154 1.00 23.52 ?  97  GLU D CA    1 
ATOM   14126 C  C     . GLU D 2 118 ? 137.091 97.502  129.066 1.00 24.25 ?  97  GLU D C     1 
ATOM   14127 O  O     . GLU D 2 118 ? 138.213 97.185  128.665 1.00 25.05 ?  97  GLU D O     1 
ATOM   14128 C  CB    . GLU D 2 118 ? 136.544 97.861  131.480 1.00 23.11 ?  97  GLU D CB    1 
ATOM   14129 C  CG    . GLU D 2 118 ? 136.093 98.783  132.620 1.00 23.08 ?  97  GLU D CG    1 
ATOM   14130 C  CD    . GLU D 2 118 ? 137.201 99.640  133.212 1.00 24.08 ?  97  GLU D CD    1 
ATOM   14131 O  OE1   . GLU D 2 118 ? 138.260 99.779  132.581 1.00 26.39 ?  97  GLU D OE1   1 
ATOM   14132 O  OE2   . GLU D 2 118 ? 137.000 100.205 134.308 1.00 27.52 -1 97  GLU D OE2   1 
ATOM   14133 N  N     . ASN D 2 119 ? 135.961 96.990  128.584 1.00 25.47 ?  98  ASN D N     1 
ATOM   14134 C  CA    . ASN D 2 119 ? 135.922 95.828  127.674 1.00 26.32 ?  98  ASN D CA    1 
ATOM   14135 C  C     . ASN D 2 119 ? 136.129 96.150  126.197 1.00 26.22 ?  98  ASN D C     1 
ATOM   14136 O  O     . ASN D 2 119 ? 136.775 95.377  125.461 1.00 26.54 ?  98  ASN D O     1 
ATOM   14137 C  CB    . ASN D 2 119 ? 134.596 95.063  127.841 1.00 26.72 ?  98  ASN D CB    1 
ATOM   14138 C  CG    . ASN D 2 119 ? 134.459 94.426  129.224 1.00 29.12 ?  98  ASN D CG    1 
ATOM   14139 O  OD1   . ASN D 2 119 ? 135.338 93.679  129.668 1.00 32.07 ?  98  ASN D OD1   1 
ATOM   14140 N  ND2   . ASN D 2 119 ? 133.373 94.746  129.918 1.00 29.12 ?  98  ASN D ND2   1 
ATOM   14141 N  N     . ALA D 2 120 ? 135.562 97.273  125.769 1.00 25.46 ?  99  ALA D N     1 
ATOM   14142 C  CA    . ALA D 2 120 ? 135.566 97.653  124.357 1.00 25.77 ?  99  ALA D CA    1 
ATOM   14143 C  C     . ALA D 2 120 ? 136.714 98.585  123.983 1.00 25.51 ?  99  ALA D C     1 
ATOM   14144 O  O     . ALA D 2 120 ? 137.150 98.594  122.829 1.00 26.64 ?  99  ALA D O     1 
ATOM   14145 C  CB    . ALA D 2 120 ? 134.220 98.284  123.963 1.00 25.75 ?  99  ALA D CB    1 
ATOM   14146 N  N     . VAL D 2 121 ? 137.196 99.370  124.940 1.00 24.40 ?  100 VAL D N     1 
ATOM   14147 C  CA    . VAL D 2 121 ? 138.185 100.396 124.627 1.00 24.15 ?  100 VAL D CA    1 
ATOM   14148 C  C     . VAL D 2 121 ? 139.543 100.089 125.264 1.00 23.94 ?  100 VAL D C     1 
ATOM   14149 O  O     . VAL D 2 121 ? 140.543 99.932  124.558 1.00 23.75 ?  100 VAL D O     1 
ATOM   14150 C  CB    . VAL D 2 121 ? 137.680 101.821 125.007 1.00 23.68 ?  100 VAL D CB    1 
ATOM   14151 C  CG1   . VAL D 2 121 ? 138.715 102.881 124.633 1.00 23.76 ?  100 VAL D CG1   1 
ATOM   14152 C  CG2   . VAL D 2 121 ? 136.353 102.115 124.299 1.00 23.99 ?  100 VAL D CG2   1 
ATOM   14153 N  N     . HIS D 2 122 ? 139.568 99.999  126.593 1.00 23.68 ?  101 HIS D N     1 
ATOM   14154 C  CA    . HIS D 2 122 ? 140.810 99.731  127.321 1.00 24.02 ?  101 HIS D CA    1 
ATOM   14155 C  C     . HIS D 2 122 ? 141.449 98.407  126.937 1.00 24.39 ?  101 HIS D C     1 
ATOM   14156 O  O     . HIS D 2 122 ? 142.650 98.362  126.681 1.00 24.71 ?  101 HIS D O     1 
ATOM   14157 C  CB    . HIS D 2 122 ? 140.610 99.802  128.840 1.00 23.20 ?  101 HIS D CB    1 
ATOM   14158 C  CG    . HIS D 2 122 ? 140.217 101.159 129.337 1.00 22.82 ?  101 HIS D CG    1 
ATOM   14159 N  ND1   . HIS D 2 122 ? 139.932 101.408 130.661 1.00 20.48 ?  101 HIS D ND1   1 
ATOM   14160 C  CD2   . HIS D 2 122 ? 140.036 102.333 128.685 1.00 21.03 ?  101 HIS D CD2   1 
ATOM   14161 C  CE1   . HIS D 2 122 ? 139.607 102.679 130.807 1.00 19.88 ?  101 HIS D CE1   1 
ATOM   14162 N  NE2   . HIS D 2 122 ? 139.664 103.264 129.623 1.00 21.62 ?  101 HIS D NE2   1 
ATOM   14163 N  N     . ALA D 2 123 ? 140.657 97.336  126.886 1.00 25.30 ?  102 ALA D N     1 
ATOM   14164 C  CA    . ALA D 2 123 ? 141.209 96.004  126.601 1.00 25.77 ?  102 ALA D CA    1 
ATOM   14165 C  C     . ALA D 2 123 ? 141.820 95.916  125.199 1.00 26.37 ?  102 ALA D C     1 
ATOM   14166 O  O     . ALA D 2 123 ? 142.875 95.298  125.006 1.00 25.87 ?  102 ALA D O     1 
ATOM   14167 C  CB    . ALA D 2 123 ? 140.148 94.914  126.803 1.00 26.43 ?  102 ALA D CB    1 
ATOM   14168 N  N     . LYS D 2 124 ? 141.152 96.539  124.227 1.00 26.51 ?  103 LYS D N     1 
ATOM   14169 C  CA    . LYS D 2 124 ? 141.648 96.584  122.859 1.00 27.22 ?  103 LYS D CA    1 
ATOM   14170 C  C     . LYS D 2 124 ? 142.921 97.437  122.774 1.00 26.63 ?  103 LYS D C     1 
ATOM   14171 O  O     . LYS D 2 124 ? 143.835 97.113  122.015 1.00 26.07 ?  103 LYS D O     1 
ATOM   14172 C  CB    . LYS D 2 124 ? 140.559 97.112  121.903 1.00 27.51 ?  103 LYS D CB    1 
ATOM   14173 C  CG    . LYS D 2 124 ? 140.994 97.290  120.432 1.00 30.58 ?  103 LYS D CG    1 
ATOM   14174 C  CD    . LYS D 2 124 ? 141.287 95.961  119.751 1.00 35.72 ?  103 LYS D CD    1 
ATOM   14175 C  CE    . LYS D 2 124 ? 141.748 96.141  118.303 1.00 37.33 ?  103 LYS D CE    1 
ATOM   14176 N  NZ    . LYS D 2 124 ? 140.652 96.701  117.469 1.00 40.73 1  103 LYS D NZ    1 
ATOM   14177 N  N     . SER D 2 125 ? 142.974 98.508  123.572 1.00 26.02 ?  104 SER D N     1 
ATOM   14178 C  CA    . SER D 2 125 ? 144.119 99.421  123.601 1.00 26.16 ?  104 SER D CA    1 
ATOM   14179 C  C     . SER D 2 125 ? 145.385 98.746  124.129 1.00 26.18 ?  104 SER D C     1 
ATOM   14180 O  O     . SER D 2 125 ? 146.470 98.928  123.564 1.00 26.06 ?  104 SER D O     1 
ATOM   14181 C  CB    . SER D 2 125 ? 143.809 100.668 124.432 1.00 26.10 ?  104 SER D CB    1 
ATOM   14182 O  OG    . SER D 2 125 ? 142.786 101.428 123.812 1.00 26.58 ?  104 SER D OG    1 
ATOM   14183 N  N     . TYR D 2 126 ? 145.240 97.975  125.204 1.00 25.68 ?  105 TYR D N     1 
ATOM   14184 C  CA    . TYR D 2 126 ? 146.360 97.218  125.777 1.00 26.12 ?  105 TYR D CA    1 
ATOM   14185 C  C     . TYR D 2 126 ? 146.864 96.164  124.784 1.00 26.38 ?  105 TYR D C     1 
ATOM   14186 O  O     . TYR D 2 126 ? 148.071 96.004  124.590 1.00 26.83 ?  105 TYR D O     1 
ATOM   14187 C  CB    . TYR D 2 126 ? 145.963 96.539  127.101 1.00 25.35 ?  105 TYR D CB    1 
ATOM   14188 C  CG    . TYR D 2 126 ? 145.934 97.453  128.311 1.00 25.46 ?  105 TYR D CG    1 
ATOM   14189 C  CD1   . TYR D 2 126 ? 147.057 98.200  128.669 1.00 25.41 ?  105 TYR D CD1   1 
ATOM   14190 C  CD2   . TYR D 2 126 ? 144.793 97.547  129.123 1.00 24.77 ?  105 TYR D CD2   1 
ATOM   14191 C  CE1   . TYR D 2 126 ? 147.045 99.040  129.780 1.00 25.89 ?  105 TYR D CE1   1 
ATOM   14192 C  CE2   . TYR D 2 126 ? 144.771 98.391  130.244 1.00 23.11 ?  105 TYR D CE2   1 
ATOM   14193 C  CZ    . TYR D 2 126 ? 145.906 99.120  130.572 1.00 25.38 ?  105 TYR D CZ    1 
ATOM   14194 O  OH    . TYR D 2 126 ? 145.921 99.957  131.667 1.00 23.31 ?  105 TYR D OH    1 
ATOM   14195 N  N     . SER D 2 127 ? 145.931 95.467  124.144 1.00 27.16 ?  106 SER D N     1 
ATOM   14196 C  CA    . SER D 2 127 ? 146.268 94.464  123.129 1.00 27.83 ?  106 SER D CA    1 
ATOM   14197 C  C     . SER D 2 127 ? 147.055 95.092  121.969 1.00 28.21 ?  106 SER D C     1 
ATOM   14198 O  O     . SER D 2 127 ? 148.094 94.556  121.561 1.00 28.30 ?  106 SER D O     1 
ATOM   14199 C  CB    . SER D 2 127 ? 144.998 93.759  122.625 1.00 28.37 ?  106 SER D CB    1 
ATOM   14200 O  OG    . SER D 2 127 ? 145.288 92.857  121.559 1.00 29.33 ?  106 SER D OG    1 
ATOM   14201 N  N     . ASN D 2 128 ? 146.559 96.224  121.460 1.00 28.27 ?  107 ASN D N     1 
ATOM   14202 C  CA    . ASN D 2 128 ? 147.232 97.005  120.409 1.00 28.79 ?  107 ASN D CA    1 
ATOM   14203 C  C     . ASN D 2 128 ? 148.662 97.405  120.757 1.00 28.53 ?  107 ASN D C     1 
ATOM   14204 O  O     . ASN D 2 128 ? 149.561 97.282  119.918 1.00 28.03 ?  107 ASN D O     1 
ATOM   14205 C  CB    . ASN D 2 128 ? 146.431 98.267  120.041 1.00 29.05 ?  107 ASN D CB    1 
ATOM   14206 C  CG    . ASN D 2 128 ? 145.131 97.952  119.294 1.00 30.48 ?  107 ASN D CG    1 
ATOM   14207 O  OD1   . ASN D 2 128 ? 144.902 96.822  118.870 1.00 32.19 ?  107 ASN D OD1   1 
ATOM   14208 N  ND2   . ASN D 2 128 ? 144.272 98.956  119.151 1.00 31.59 ?  107 ASN D ND2   1 
ATOM   14209 N  N     . ILE D 2 129 ? 148.868 97.909  121.976 1.00 28.21 ?  108 ILE D N     1 
ATOM   14210 C  CA    . ILE D 2 129 ? 150.223 98.251  122.433 1.00 28.76 ?  108 ILE D CA    1 
ATOM   14211 C  C     . ILE D 2 129 ? 151.140 97.017  122.399 1.00 29.83 ?  108 ILE D C     1 
ATOM   14212 O  O     . ILE D 2 129 ? 152.256 97.075  121.865 1.00 29.99 ?  108 ILE D O     1 
ATOM   14213 C  CB    . ILE D 2 129 ? 150.234 98.920  123.845 1.00 28.28 ?  108 ILE D CB    1 
ATOM   14214 C  CG1   . ILE D 2 129 ? 149.487 100.262 123.821 1.00 27.94 ?  108 ILE D CG1   1 
ATOM   14215 C  CG2   . ILE D 2 129 ? 151.675 99.138  124.327 1.00 27.52 ?  108 ILE D CG2   1 
ATOM   14216 C  CD1   . ILE D 2 129 ? 149.131 100.803 125.201 1.00 27.98 ?  108 ILE D CD1   1 
ATOM   14217 N  N     . PHE D 2 130 ? 150.669 95.907  122.962 1.00 30.86 ?  109 PHE D N     1 
ATOM   14218 C  CA    . PHE D 2 130 ? 151.433 94.663  122.961 1.00 32.76 ?  109 PHE D CA    1 
ATOM   14219 C  C     . PHE D 2 130 ? 151.820 94.190  121.556 1.00 34.37 ?  109 PHE D C     1 
ATOM   14220 O  O     . PHE D 2 130 ? 152.993 93.937  121.290 1.00 34.61 ?  109 PHE D O     1 
ATOM   14221 C  CB    . PHE D 2 130 ? 150.674 93.554  123.685 1.00 32.81 ?  109 PHE D CB    1 
ATOM   14222 C  CG    . PHE D 2 130 ? 151.065 93.390  125.126 1.00 33.84 ?  109 PHE D CG    1 
ATOM   14223 C  CD1   . PHE D 2 130 ? 152.329 92.913  125.466 1.00 34.61 ?  109 PHE D CD1   1 
ATOM   14224 C  CD2   . PHE D 2 130 ? 150.160 93.678  126.140 1.00 35.74 ?  109 PHE D CD2   1 
ATOM   14225 C  CE1   . PHE D 2 130 ? 152.697 92.745  126.801 1.00 36.99 ?  109 PHE D CE1   1 
ATOM   14226 C  CE2   . PHE D 2 130 ? 150.514 93.514  127.485 1.00 36.96 ?  109 PHE D CE2   1 
ATOM   14227 C  CZ    . PHE D 2 130 ? 151.785 93.047  127.817 1.00 36.91 ?  109 PHE D CZ    1 
ATOM   14228 N  N     . MET D 2 131 ? 150.829 94.092  120.669 1.00 35.90 ?  110 MET D N     1 
ATOM   14229 C  CA    . MET D 2 131 ? 151.031 93.615  119.300 1.00 37.94 ?  110 MET D CA    1 
ATOM   14230 C  C     . MET D 2 131 ? 152.005 94.487  118.519 1.00 38.05 ?  110 MET D C     1 
ATOM   14231 O  O     . MET D 2 131 ? 152.677 94.001  117.616 1.00 38.20 ?  110 MET D O     1 
ATOM   14232 C  CB    . MET D 2 131 ? 149.697 93.514  118.542 1.00 38.63 ?  110 MET D CB    1 
ATOM   14233 C  CG    . MET D 2 131 ? 148.748 92.418  119.054 1.00 42.34 ?  110 MET D CG    1 
ATOM   14234 S  SD    . MET D 2 131 ? 147.172 92.294  118.146 1.00 50.15 ?  110 MET D SD    1 
ATOM   14235 C  CE    . MET D 2 131 ? 146.316 93.802  118.621 1.00 48.14 ?  110 MET D CE    1 
ATOM   14236 N  N     . THR D 2 132 ? 152.077 95.770  118.873 1.00 38.12 ?  111 THR D N     1 
ATOM   14237 C  CA    . THR D 2 132 ? 153.007 96.695  118.225 1.00 38.79 ?  111 THR D CA    1 
ATOM   14238 C  C     . THR D 2 132 ? 154.463 96.462  118.667 1.00 38.81 ?  111 THR D C     1 
ATOM   14239 O  O     . THR D 2 132 ? 155.375 96.480  117.833 1.00 39.26 ?  111 THR D O     1 
ATOM   14240 C  CB    . THR D 2 132 ? 152.597 98.162  118.467 1.00 38.78 ?  111 THR D CB    1 
ATOM   14241 O  OG1   . THR D 2 132 ? 151.259 98.364  117.997 1.00 39.32 ?  111 THR D OG1   1 
ATOM   14242 C  CG2   . THR D 2 132 ? 153.520 99.120  117.720 1.00 39.75 ?  111 THR D CG2   1 
ATOM   14243 N  N     . LEU D 2 133 ? 154.665 96.230  119.965 1.00 38.34 ?  112 LEU D N     1 
ATOM   14244 C  CA    . LEU D 2 133 ? 156.001 96.172  120.565 1.00 38.36 ?  112 LEU D CA    1 
ATOM   14245 C  C     . LEU D 2 133 ? 156.640 94.783  120.604 1.00 38.94 ?  112 LEU D C     1 
ATOM   14246 O  O     . LEU D 2 133 ? 157.863 94.663  120.535 1.00 39.14 ?  112 LEU D O     1 
ATOM   14247 C  CB    . LEU D 2 133 ? 155.978 96.753  121.988 1.00 37.62 ?  112 LEU D CB    1 
ATOM   14248 C  CG    . LEU D 2 133 ? 155.435 98.170  122.191 1.00 36.50 ?  112 LEU D CG    1 
ATOM   14249 C  CD1   . LEU D 2 133 ? 155.263 98.468  123.684 1.00 35.80 ?  112 LEU D CD1   1 
ATOM   14250 C  CD2   . LEU D 2 133 ? 156.304 99.221  121.522 1.00 35.32 ?  112 LEU D CD2   1 
ATOM   14251 N  N     . ALA D 2 134 ? 155.834 93.736  120.728 1.00 39.41 ?  113 ALA D N     1 
ATOM   14252 C  CA    . ALA D 2 134 ? 156.396 92.385  120.839 1.00 40.33 ?  113 ALA D CA    1 
ATOM   14253 C  C     . ALA D 2 134 ? 155.829 91.424  119.800 1.00 41.05 ?  113 ALA D C     1 
ATOM   14254 O  O     . ALA D 2 134 ? 154.688 91.585  119.380 1.00 40.81 ?  113 ALA D O     1 
ATOM   14255 C  CB    . ALA D 2 134 ? 156.180 91.843  122.240 1.00 40.15 ?  113 ALA D CB    1 
ATOM   14256 N  N     . PRO D 2 135 ? 156.630 90.425  119.369 1.00 42.21 ?  114 PRO D N     1 
ATOM   14257 C  CA    . PRO D 2 135 ? 156.060 89.373  118.518 1.00 43.27 ?  114 PRO D CA    1 
ATOM   14258 C  C     . PRO D 2 135 ? 155.144 88.442  119.325 1.00 43.89 ?  114 PRO D C     1 
ATOM   14259 O  O     . PRO D 2 135 ? 155.250 88.385  120.554 1.00 43.31 ?  114 PRO D O     1 
ATOM   14260 C  CB    . PRO D 2 135 ? 157.292 88.617  118.015 1.00 43.69 ?  114 PRO D CB    1 
ATOM   14261 C  CG    . PRO D 2 135 ? 158.319 88.839  119.059 1.00 43.01 ?  114 PRO D CG    1 
ATOM   14262 C  CD    . PRO D 2 135 ? 158.069 90.213  119.617 1.00 42.16 ?  114 PRO D CD    1 
ATOM   14263 N  N     . THR D 2 136 ? 154.268 87.719  118.628 1.00 45.26 ?  115 THR D N     1 
ATOM   14264 C  CA    . THR D 2 136 ? 153.238 86.877  119.260 1.00 46.11 ?  115 THR D CA    1 
ATOM   14265 C  C     . THR D 2 136 ? 153.789 85.957  120.354 1.00 46.35 ?  115 THR D C     1 
ATOM   14266 O  O     . THR D 2 136 ? 153.214 85.880  121.445 1.00 46.25 ?  115 THR D O     1 
ATOM   14267 C  CB    . THR D 2 136 ? 152.436 86.060  118.210 1.00 46.59 ?  115 THR D CB    1 
ATOM   14268 O  OG1   . THR D 2 136 ? 151.917 86.948  117.215 1.00 47.80 ?  115 THR D OG1   1 
ATOM   14269 C  CG2   . THR D 2 136 ? 151.258 85.328  118.851 1.00 46.94 ?  115 THR D CG2   1 
ATOM   14270 N  N     . GLU D 2 137 ? 154.905 85.285  120.071 1.00 46.92 ?  116 GLU D N     1 
ATOM   14271 C  CA    . GLU D 2 137 ? 155.503 84.352  121.025 1.00 47.37 ?  116 GLU D CA    1 
ATOM   14272 C  C     . GLU D 2 137 ? 155.957 85.027  122.322 1.00 46.64 ?  116 GLU D C     1 
ATOM   14273 O  O     . GLU D 2 137 ? 155.802 84.453  123.401 1.00 46.89 ?  116 GLU D O     1 
ATOM   14274 C  CB    . GLU D 2 137 ? 156.657 83.563  120.387 1.00 48.04 ?  116 GLU D CB    1 
ATOM   14275 C  CG    . GLU D 2 137 ? 157.263 82.466  121.283 1.00 49.86 ?  116 GLU D CG    1 
ATOM   14276 C  CD    . GLU D 2 137 ? 156.346 81.252  121.498 1.00 52.40 ?  116 GLU D CD    1 
ATOM   14277 O  OE1   . GLU D 2 137 ? 155.180 81.427  121.918 1.00 52.97 ?  116 GLU D OE1   1 
ATOM   14278 O  OE2   . GLU D 2 137 ? 156.807 80.110  121.268 1.00 54.12 -1 116 GLU D OE2   1 
ATOM   14279 N  N     . THR D 2 138 ? 156.507 86.235  122.208 1.00 46.09 ?  117 THR D N     1 
ATOM   14280 C  CA    . THR D 2 138 ? 156.934 87.024  123.374 1.00 45.30 ?  117 THR D CA    1 
ATOM   14281 C  C     . THR D 2 138 ? 155.744 87.460  124.239 1.00 44.63 ?  117 THR D C     1 
ATOM   14282 O  O     . THR D 2 138 ? 155.823 87.432  125.471 1.00 44.51 ?  117 THR D O     1 
ATOM   14283 C  CB    . THR D 2 138 ? 157.761 88.260  122.949 1.00 45.20 ?  117 THR D CB    1 
ATOM   14284 O  OG1   . THR D 2 138 ? 158.885 87.837  122.171 1.00 45.69 ?  117 THR D OG1   1 
ATOM   14285 C  CG2   . THR D 2 138 ? 158.268 89.038  124.163 1.00 44.67 ?  117 THR D CG2   1 
ATOM   14286 N  N     . ILE D 2 139 ? 154.647 87.854  123.593 1.00 44.24 ?  118 ILE D N     1 
ATOM   14287 C  CA    . ILE D 2 139 ? 153.425 88.237  124.305 1.00 43.65 ?  118 ILE D CA    1 
ATOM   14288 C  C     . ILE D 2 139 ? 152.887 87.059  125.131 1.00 43.87 ?  118 ILE D C     1 
ATOM   14289 O  O     . ILE D 2 139 ? 152.604 87.206  126.323 1.00 43.36 ?  118 ILE D O     1 
ATOM   14290 C  CB    . ILE D 2 139 ? 152.353 88.802  123.337 1.00 43.68 ?  118 ILE D CB    1 
ATOM   14291 C  CG1   . ILE D 2 139 ? 152.827 90.141  122.750 1.00 43.30 ?  118 ILE D CG1   1 
ATOM   14292 C  CG2   . ILE D 2 139 ? 150.995 88.968  124.044 1.00 43.11 ?  118 ILE D CG2   1 
ATOM   14293 C  CD1   . ILE D 2 139 ? 152.074 90.603  121.509 1.00 43.41 ?  118 ILE D CD1   1 
ATOM   14294 N  N     . ASN D 2 140 ? 152.779 85.891  124.498 1.00 44.52 ?  119 ASN D N     1 
ATOM   14295 C  CA    . ASN D 2 140 ? 152.311 84.676  125.174 1.00 45.00 ?  119 ASN D CA    1 
ATOM   14296 C  C     . ASN D 2 140 ? 153.164 84.299  126.403 1.00 44.99 ?  119 ASN D C     1 
ATOM   14297 O  O     . ASN D 2 140 ? 152.622 83.902  127.443 1.00 44.61 ?  119 ASN D O     1 
ATOM   14298 C  CB    . ASN D 2 140 ? 152.215 83.502  124.183 1.00 45.74 ?  119 ASN D CB    1 
ATOM   14299 C  CG    . ASN D 2 140 ? 151.223 83.760  123.043 1.00 46.40 ?  119 ASN D CG    1 
ATOM   14300 O  OD1   . ASN D 2 140 ? 150.392 84.673  123.105 1.00 46.85 ?  119 ASN D OD1   1 
ATOM   14301 N  ND2   . ASN D 2 140 ? 151.307 82.941  121.996 1.00 48.16 ?  119 ASN D ND2   1 
ATOM   14302 N  N     . GLU D 2 141 ? 154.485 84.454  126.290 1.00 45.09 ?  120 GLU D N     1 
ATOM   14303 C  CA    . GLU D 2 141 ? 155.404 84.141  127.389 1.00 45.27 ?  120 GLU D CA    1 
ATOM   14304 C  C     . GLU D 2 141 ? 155.310 85.122  128.566 1.00 44.75 ?  120 GLU D C     1 
ATOM   14305 O  O     . GLU D 2 141 ? 155.330 84.706  129.730 1.00 44.37 ?  120 GLU D O     1 
ATOM   14306 C  CB    . GLU D 2 141 ? 156.846 84.054  126.888 1.00 45.75 ?  120 GLU D CB    1 
ATOM   14307 C  CG    . GLU D 2 141 ? 157.119 82.854  125.980 1.00 48.17 ?  120 GLU D CG    1 
ATOM   14308 C  CD    . GLU D 2 141 ? 158.567 82.752  125.545 1.00 50.15 ?  120 GLU D CD    1 
ATOM   14309 O  OE1   . GLU D 2 141 ? 159.465 82.820  126.410 1.00 50.90 ?  120 GLU D OE1   1 
ATOM   14310 O  OE2   . GLU D 2 141 ? 158.808 82.597  124.330 1.00 52.25 -1 120 GLU D OE2   1 
ATOM   14311 N  N     . VAL D 2 142 ? 155.225 86.416  128.258 1.00 44.31 ?  121 VAL D N     1 
ATOM   14312 C  CA    . VAL D 2 142 ? 155.063 87.452  129.280 1.00 43.91 ?  121 VAL D CA    1 
ATOM   14313 C  C     . VAL D 2 142 ? 153.769 87.231  130.070 1.00 43.71 ?  121 VAL D C     1 
ATOM   14314 O  O     . VAL D 2 142 ? 153.761 87.335  131.296 1.00 43.44 ?  121 VAL D O     1 
ATOM   14315 C  CB    . VAL D 2 142 ? 155.093 88.881  128.671 1.00 43.65 ?  121 VAL D CB    1 
ATOM   14316 C  CG1   . VAL D 2 142 ? 154.791 89.935  129.736 1.00 43.40 ?  121 VAL D CG1   1 
ATOM   14317 C  CG2   . VAL D 2 142 ? 156.452 89.161  128.037 1.00 43.96 ?  121 VAL D CG2   1 
ATOM   14318 N  N     . PHE D 2 143 ? 152.686 86.912  129.366 1.00 44.03 ?  122 PHE D N     1 
ATOM   14319 C  CA    . PHE D 2 143 ? 151.413 86.650  130.027 1.00 44.42 ?  122 PHE D CA    1 
ATOM   14320 C  C     . PHE D 2 143 ? 151.425 85.369  130.853 1.00 45.38 ?  122 PHE D C     1 
ATOM   14321 O  O     . PHE D 2 143 ? 150.815 85.321  131.918 1.00 45.50 ?  122 PHE D O     1 
ATOM   14322 C  CB    . PHE D 2 143 ? 150.244 86.687  129.040 1.00 44.27 ?  122 PHE D CB    1 
ATOM   14323 C  CG    . PHE D 2 143 ? 149.691 88.066  128.839 1.00 43.28 ?  122 PHE D CG    1 
ATOM   14324 C  CD1   . PHE D 2 143 ? 148.784 88.603  129.750 1.00 42.17 ?  122 PHE D CD1   1 
ATOM   14325 C  CD2   . PHE D 2 143 ? 150.103 88.844  127.765 1.00 42.76 ?  122 PHE D CD2   1 
ATOM   14326 C  CE1   . PHE D 2 143 ? 148.280 89.887  129.584 1.00 42.16 ?  122 PHE D CE1   1 
ATOM   14327 C  CE2   . PHE D 2 143 ? 149.606 90.130  127.589 1.00 42.77 ?  122 PHE D CE2   1 
ATOM   14328 C  CZ    . PHE D 2 143 ? 148.691 90.655  128.501 1.00 42.28 ?  122 PHE D CZ    1 
ATOM   14329 N  N     . GLU D 2 144 ? 152.136 84.351  130.375 1.00 46.18 ?  123 GLU D N     1 
ATOM   14330 C  CA    . GLU D 2 144 ? 152.373 83.141  131.160 1.00 47.19 ?  123 GLU D CA    1 
ATOM   14331 C  C     . GLU D 2 144 ? 153.113 83.462  132.468 1.00 46.99 ?  123 GLU D C     1 
ATOM   14332 O  O     . GLU D 2 144 ? 152.726 82.965  133.530 1.00 46.94 ?  123 GLU D O     1 
ATOM   14333 C  CB    . GLU D 2 144 ? 153.153 82.109  130.334 1.00 47.80 ?  123 GLU D CB    1 
ATOM   14334 C  CG    . GLU D 2 144 ? 153.339 80.739  130.995 1.00 49.54 ?  123 GLU D CG    1 
ATOM   14335 C  CD    . GLU D 2 144 ? 154.223 79.795  130.175 1.00 52.37 ?  123 GLU D CD    1 
ATOM   14336 O  OE1   . GLU D 2 144 ? 155.297 80.226  129.693 1.00 52.92 ?  123 GLU D OE1   1 
ATOM   14337 O  OE2   . GLU D 2 144 ? 153.846 78.614  130.016 1.00 53.55 -1 123 GLU D OE2   1 
ATOM   14338 N  N     . TRP D 2 145 ? 154.161 84.290  132.380 1.00 47.02 ?  124 TRP D N     1 
ATOM   14339 C  CA    . TRP D 2 145 ? 154.969 84.697  133.544 1.00 46.93 ?  124 TRP D CA    1 
ATOM   14340 C  C     . TRP D 2 145 ? 154.148 85.509  134.536 1.00 46.55 ?  124 TRP D C     1 
ATOM   14341 O  O     . TRP D 2 145 ? 154.119 85.196  135.723 1.00 46.42 ?  124 TRP D O     1 
ATOM   14342 C  CB    . TRP D 2 145 ? 156.194 85.517  133.109 1.00 47.07 ?  124 TRP D CB    1 
ATOM   14343 C  CG    . TRP D 2 145 ? 157.206 85.814  134.220 1.00 47.82 ?  124 TRP D CG    1 
ATOM   14344 C  CD1   . TRP D 2 145 ? 158.317 85.078  134.536 1.00 48.78 ?  124 TRP D CD1   1 
ATOM   14345 C  CD2   . TRP D 2 145 ? 157.202 86.934  135.131 1.00 47.80 ?  124 TRP D CD2   1 
ATOM   14346 N  NE1   . TRP D 2 145 ? 158.997 85.658  135.584 1.00 49.06 ?  124 TRP D NE1   1 
ATOM   14347 C  CE2   . TRP D 2 145 ? 158.335 86.795  135.970 1.00 48.24 ?  124 TRP D CE2   1 
ATOM   14348 C  CE3   . TRP D 2 145 ? 156.351 88.031  135.324 1.00 47.65 ?  124 TRP D CE3   1 
ATOM   14349 C  CZ2   . TRP D 2 145 ? 158.637 87.715  136.988 1.00 47.74 ?  124 TRP D CZ2   1 
ATOM   14350 C  CZ3   . TRP D 2 145 ? 156.651 88.947  136.335 1.00 46.92 ?  124 TRP D CZ3   1 
ATOM   14351 C  CH2   . TRP D 2 145 ? 157.788 88.779  137.153 1.00 47.88 ?  124 TRP D CH2   1 
ATOM   14352 N  N     . VAL D 2 146 ? 153.486 86.552  134.044 1.00 46.09 ?  125 VAL D N     1 
ATOM   14353 C  CA    . VAL D 2 146 ? 152.723 87.447  134.905 1.00 45.36 ?  125 VAL D CA    1 
ATOM   14354 C  C     . VAL D 2 146 ? 151.511 86.715  135.505 1.00 45.28 ?  125 VAL D C     1 
ATOM   14355 O  O     . VAL D 2 146 ? 151.123 86.980  136.649 1.00 45.29 ?  125 VAL D O     1 
ATOM   14356 C  CB    . VAL D 2 146 ? 152.384 88.784  134.171 1.00 45.33 ?  125 VAL D CB    1 
ATOM   14357 C  CG1   . VAL D 2 146 ? 151.469 89.657  134.991 1.00 44.97 ?  125 VAL D CG1   1 
ATOM   14358 C  CG2   . VAL D 2 146 ? 153.671 89.556  133.871 1.00 44.52 ?  125 VAL D CG2   1 
ATOM   14359 N  N     . LYS D 2 147 ? 150.957 85.762  134.756 1.00 44.98 ?  126 LYS D N     1 
ATOM   14360 C  CA    . LYS D 2 147 ? 149.862 84.917  135.253 1.00 44.65 ?  126 LYS D CA    1 
ATOM   14361 C  C     . LYS D 2 147 ? 150.278 84.034  136.441 1.00 44.06 ?  126 LYS D C     1 
ATOM   14362 O  O     . LYS D 2 147 ? 149.452 83.702  137.293 1.00 44.65 ?  126 LYS D O     1 
ATOM   14363 C  CB    . LYS D 2 147 ? 149.294 84.035  134.137 1.00 45.31 ?  126 LYS D CB    1 
ATOM   14364 C  CG    . LYS D 2 147 ? 147.773 84.009  134.097 1.00 46.54 ?  126 LYS D CG    1 
ATOM   14365 C  CD    . LYS D 2 147 ? 147.211 82.607  133.853 1.00 49.06 ?  126 LYS D CD    1 
ATOM   14366 C  CE    . LYS D 2 147 ? 147.031 81.842  135.171 1.00 50.46 ?  126 LYS D CE    1 
ATOM   14367 N  NZ    . LYS D 2 147 ? 145.965 80.797  135.092 1.00 51.33 1  126 LYS D NZ    1 
ATOM   14368 N  N     . GLN D 2 148 ? 151.553 83.659  136.490 1.00 42.58 ?  127 GLN D N     1 
ATOM   14369 C  CA    . GLN D 2 148 ? 152.085 82.833  137.573 1.00 41.39 ?  127 GLN D CA    1 
ATOM   14370 C  C     . GLN D 2 148 ? 152.701 83.667  138.704 1.00 39.56 ?  127 GLN D C     1 
ATOM   14371 O  O     . GLN D 2 148 ? 152.928 83.154  139.799 1.00 39.77 ?  127 GLN D O     1 
ATOM   14372 C  CB    . GLN D 2 148 ? 153.091 81.813  137.003 1.00 42.11 ?  127 GLN D CB    1 
ATOM   14373 C  CG    . GLN D 2 148 ? 154.281 81.464  137.892 1.00 44.08 ?  127 GLN D CG    1 
ATOM   14374 C  CD    . GLN D 2 148 ? 155.551 82.244  137.545 1.00 46.12 ?  127 GLN D CD    1 
ATOM   14375 O  OE1   . GLN D 2 148 ? 155.512 83.451  137.271 1.00 46.47 ?  127 GLN D OE1   1 
ATOM   14376 N  NE2   . GLN D 2 148 ? 156.690 81.552  137.573 1.00 45.69 ?  127 GLN D NE2   1 
ATOM   14377 N  N     . ASN D 2 149 ? 152.954 84.951  138.434 1.00 36.99 ?  128 ASN D N     1 
ATOM   14378 C  CA    . ASN D 2 149 ? 153.598 85.845  139.396 1.00 34.54 ?  128 ASN D CA    1 
ATOM   14379 C  C     . ASN D 2 149 ? 152.835 86.003  140.714 1.00 33.13 ?  128 ASN D C     1 
ATOM   14380 O  O     . ASN D 2 149 ? 151.659 86.358  140.725 1.00 32.62 ?  128 ASN D O     1 
ATOM   14381 C  CB    . ASN D 2 149 ? 153.848 87.220  138.774 1.00 34.24 ?  128 ASN D CB    1 
ATOM   14382 C  CG    . ASN D 2 149 ? 154.619 88.138  139.701 1.00 33.83 ?  128 ASN D CG    1 
ATOM   14383 O  OD1   . ASN D 2 149 ? 154.040 88.999  140.365 1.00 32.21 ?  128 ASN D OD1   1 
ATOM   14384 N  ND2   . ASN D 2 149 ? 155.932 87.934  139.775 1.00 33.26 ?  128 ASN D ND2   1 
ATOM   14385 N  N     . LYS D 2 150 ? 153.535 85.767  141.820 1.00 31.49 ?  129 LYS D N     1 
ATOM   14386 C  CA    . LYS D 2 150 ? 152.939 85.747  143.154 1.00 30.68 ?  129 LYS D CA    1 
ATOM   14387 C  C     . LYS D 2 150 ? 152.286 87.083  143.584 1.00 28.95 ?  129 LYS D C     1 
ATOM   14388 O  O     . LYS D 2 150 ? 151.202 87.087  144.178 1.00 27.90 ?  129 LYS D O     1 
ATOM   14389 C  CB    . LYS D 2 150 ? 154.006 85.283  144.157 1.00 31.17 ?  129 LYS D CB    1 
ATOM   14390 C  CG    . LYS D 2 150 ? 153.730 85.517  145.628 1.00 33.66 ?  129 LYS D CG    1 
ATOM   14391 C  CD    . LYS D 2 150 ? 154.923 85.013  146.455 1.00 38.08 ?  129 LYS D CD    1 
ATOM   14392 C  CE    . LYS D 2 150 ? 155.039 85.734  147.804 1.00 40.20 ?  129 LYS D CE    1 
ATOM   14393 N  NZ    . LYS D 2 150 ? 154.317 85.023  148.893 1.00 42.60 1  129 LYS D NZ    1 
ATOM   14394 N  N     . TYR D 2 151 ? 152.943 88.203  143.288 1.00 27.36 ?  130 TYR D N     1 
ATOM   14395 C  CA    . TYR D 2 151 ? 152.465 89.517  143.755 1.00 26.56 ?  130 TYR D CA    1 
ATOM   14396 C  C     . TYR D 2 151 ? 151.305 90.039  142.922 1.00 25.66 ?  130 TYR D C     1 
ATOM   14397 O  O     . TYR D 2 151 ? 150.379 90.642  143.472 1.00 25.61 ?  130 TYR D O     1 
ATOM   14398 C  CB    . TYR D 2 151 ? 153.614 90.541  143.845 1.00 26.32 ?  130 TYR D CB    1 
ATOM   14399 C  CG    . TYR D 2 151 ? 154.842 89.954  144.513 1.00 27.20 ?  130 TYR D CG    1 
ATOM   14400 C  CD1   . TYR D 2 151 ? 154.839 89.666  145.878 1.00 27.31 ?  130 TYR D CD1   1 
ATOM   14401 C  CD2   . TYR D 2 151 ? 155.981 89.635  143.773 1.00 27.22 ?  130 TYR D CD2   1 
ATOM   14402 C  CE1   . TYR D 2 151 ? 155.949 89.096  146.497 1.00 29.65 ?  130 TYR D CE1   1 
ATOM   14403 C  CE2   . TYR D 2 151 ? 157.105 89.060  144.387 1.00 28.75 ?  130 TYR D CE2   1 
ATOM   14404 C  CZ    . TYR D 2 151 ? 157.071 88.805  145.761 1.00 29.17 ?  130 TYR D CZ    1 
ATOM   14405 O  OH    . TYR D 2 151 ? 158.150 88.243  146.406 1.00 30.61 ?  130 TYR D OH    1 
ATOM   14406 N  N     . LEU D 2 152 ? 151.357 89.805  141.609 1.00 24.87 ?  131 LEU D N     1 
ATOM   14407 C  CA    . LEU D 2 152 ? 150.232 90.135  140.739 1.00 24.37 ?  131 LEU D CA    1 
ATOM   14408 C  C     . LEU D 2 152 ? 149.005 89.296  141.117 1.00 24.18 ?  131 LEU D C     1 
ATOM   14409 O  O     . LEU D 2 152 ? 147.924 89.845  141.329 1.00 23.16 ?  131 LEU D O     1 
ATOM   14410 C  CB    . LEU D 2 152 ? 150.560 89.967  139.252 1.00 24.45 ?  131 LEU D CB    1 
ATOM   14411 C  CG    . LEU D 2 152 ? 149.293 90.401  138.491 1.00 26.33 ?  131 LEU D CG    1 
ATOM   14412 C  CD1   . LEU D 2 152 ? 149.136 91.927  138.513 1.00 25.00 ?  131 LEU D CD1   1 
ATOM   14413 C  CD2   . LEU D 2 152 ? 149.194 89.848  137.099 1.00 29.15 ?  131 LEU D CD2   1 
ATOM   14414 N  N     . GLN D 2 153 ? 149.186 87.979  141.233 1.00 24.07 ?  132 GLN D N     1 
ATOM   14415 C  CA    . GLN D 2 153 ? 148.082 87.092  141.657 1.00 24.99 ?  132 GLN D CA    1 
ATOM   14416 C  C     . GLN D 2 153 ? 147.493 87.454  143.017 1.00 24.24 ?  132 GLN D C     1 
ATOM   14417 O  O     . GLN D 2 153 ? 146.260 87.484  143.184 1.00 23.75 ?  132 GLN D O     1 
ATOM   14418 C  CB    . GLN D 2 153 ? 148.492 85.610  141.612 1.00 25.84 ?  132 GLN D CB    1 
ATOM   14419 C  CG    . GLN D 2 153 ? 148.659 85.055  140.172 1.00 28.48 ?  132 GLN D CG    1 
ATOM   14420 C  CD    . GLN D 2 153 ? 147.374 85.121  139.331 1.00 30.95 ?  132 GLN D CD    1 
ATOM   14421 O  OE1   . GLN D 2 153 ? 146.277 84.932  139.842 1.00 31.78 ?  132 GLN D OE1   1 
ATOM   14422 N  NE2   . GLN D 2 153 ? 147.522 85.377  138.029 1.00 32.81 ?  132 GLN D NE2   1 
ATOM   14423 N  N     . LYS D 2 154 ? 148.349 87.742  143.993 1.00 24.00 ?  133 LYS D N     1 
ATOM   14424 C  CA    . LYS D 2 154 ? 147.828 88.076  145.319 1.00 24.43 ?  133 LYS D CA    1 
ATOM   14425 C  C     . LYS D 2 154 ? 146.810 89.223  145.245 1.00 23.40 ?  133 LYS D C     1 
ATOM   14426 O  O     . LYS D 2 154 ? 145.682 89.090  145.726 1.00 22.68 ?  133 LYS D O     1 
ATOM   14427 C  CB    . LYS D 2 154 ? 148.932 88.425  146.323 1.00 24.64 ?  133 LYS D CB    1 
ATOM   14428 C  CG    . LYS D 2 154 ? 148.339 88.732  147.710 1.00 28.01 ?  133 LYS D CG    1 
ATOM   14429 C  CD    . LYS D 2 154 ? 149.370 88.915  148.799 1.00 32.56 ?  133 LYS D CD    1 
ATOM   14430 C  CE    . LYS D 2 154 ? 150.047 87.610  149.142 1.00 34.45 ?  133 LYS D CE    1 
ATOM   14431 N  NZ    . LYS D 2 154 ? 151.070 87.816  150.215 1.00 36.11 1  133 LYS D NZ    1 
ATOM   14432 N  N     . LYS D 2 155 ? 147.204 90.343  144.639 1.00 23.07 ?  134 LYS D N     1 
ATOM   14433 C  CA    . LYS D 2 155 ? 146.287 91.475  144.534 1.00 22.70 ?  134 LYS D CA    1 
ATOM   14434 C  C     . LYS D 2 155 ? 145.095 91.181  143.624 1.00 21.96 ?  134 LYS D C     1 
ATOM   14435 O  O     . LYS D 2 155 ? 143.971 91.523  143.975 1.00 22.25 ?  134 LYS D O     1 
ATOM   14436 C  CB    . LYS D 2 155 ? 147.004 92.784  144.154 1.00 22.70 ?  134 LYS D CB    1 
ATOM   14437 C  CG    . LYS D 2 155 ? 147.646 92.834  142.782 1.00 23.62 ?  134 LYS D CG    1 
ATOM   14438 C  CD    . LYS D 2 155 ? 148.235 94.225  142.556 1.00 25.32 ?  134 LYS D CD    1 
ATOM   14439 C  CE    . LYS D 2 155 ? 149.509 94.138  141.722 1.00 27.09 ?  134 LYS D CE    1 
ATOM   14440 N  NZ    . LYS D 2 155 ? 150.045 95.501  141.438 1.00 26.65 1  134 LYS D NZ    1 
ATOM   14441 N  N     . ALA D 2 156 ? 145.314 90.528  142.482 1.00 21.76 ?  135 ALA D N     1 
ATOM   14442 C  CA    . ALA D 2 156 ? 144.188 90.232  141.577 1.00 21.83 ?  135 ALA D CA    1 
ATOM   14443 C  C     . ALA D 2 156 ? 143.113 89.393  142.288 1.00 22.30 ?  135 ALA D C     1 
ATOM   14444 O  O     . ALA D 2 156 ? 141.921 89.708  142.217 1.00 21.92 ?  135 ALA D O     1 
ATOM   14445 C  CB    . ALA D 2 156 ? 144.668 89.527  140.296 1.00 22.30 ?  135 ALA D CB    1 
ATOM   14446 N  N     . GLN D 2 157 ? 143.538 88.345  142.995 1.00 22.15 ?  136 GLN D N     1 
ATOM   14447 C  CA    . GLN D 2 157 ? 142.585 87.461  143.676 1.00 22.38 ?  136 GLN D CA    1 
ATOM   14448 C  C     . GLN D 2 157 ? 141.933 88.089  144.915 1.00 21.59 ?  136 GLN D C     1 
ATOM   14449 O  O     . GLN D 2 157 ? 140.785 87.779  145.232 1.00 21.44 ?  136 GLN D O     1 
ATOM   14450 C  CB    . GLN D 2 157 ? 143.216 86.099  144.018 1.00 22.94 ?  136 GLN D CB    1 
ATOM   14451 C  CG    . GLN D 2 157 ? 143.766 85.317  142.815 1.00 25.31 ?  136 GLN D CG    1 
ATOM   14452 C  CD    . GLN D 2 157 ? 142.817 85.281  141.612 1.00 28.02 ?  136 GLN D CD    1 
ATOM   14453 O  OE1   . GLN D 2 157 ? 141.597 85.155  141.755 1.00 27.14 ?  136 GLN D OE1   1 
ATOM   14454 N  NE2   . GLN D 2 157 ? 143.391 85.384  140.415 1.00 29.47 ?  136 GLN D NE2   1 
ATOM   14455 N  N     . MET D 2 158 ? 142.655 88.956  145.616 1.00 21.52 ?  137 MET D N     1 
ATOM   14456 C  CA    . MET D 2 158 ? 142.063 89.696  146.745 1.00 22.20 ?  137 MET D CA    1 
ATOM   14457 C  C     . MET D 2 158 ? 140.873 90.556  146.302 1.00 21.84 ?  137 MET D C     1 
ATOM   14458 O  O     . MET D 2 158 ? 139.828 90.568  146.957 1.00 21.91 ?  137 MET D O     1 
ATOM   14459 C  CB    . MET D 2 158 ? 143.102 90.572  147.444 1.00 22.52 ?  137 MET D CB    1 
ATOM   14460 C  CG    . MET D 2 158 ? 144.050 89.794  148.368 1.00 25.81 ?  137 MET D CG    1 
ATOM   14461 S  SD    . MET D 2 158 ? 145.284 90.842  149.185 1.00 31.19 ?  137 MET D SD    1 
ATOM   14462 C  CE    . MET D 2 158 ? 144.182 91.850  150.142 1.00 23.91 ?  137 MET D CE    1 
ATOM   14463 N  N     . ILE D 2 159 ? 141.048 91.265  145.189 1.00 21.41 ?  138 ILE D N     1 
ATOM   14464 C  CA    . ILE D 2 159 ? 140.013 92.138  144.646 1.00 21.51 ?  138 ILE D CA    1 
ATOM   14465 C  C     . ILE D 2 159 ? 138.813 91.310  144.160 1.00 21.77 ?  138 ILE D C     1 
ATOM   14466 O  O     . ILE D 2 159 ? 137.660 91.604  144.515 1.00 21.44 ?  138 ILE D O     1 
ATOM   14467 C  CB    . ILE D 2 159 ? 140.606 93.066  143.516 1.00 21.49 ?  138 ILE D CB    1 
ATOM   14468 C  CG1   . ILE D 2 159 ? 141.697 93.994  144.072 1.00 21.16 ?  138 ILE D CG1   1 
ATOM   14469 C  CG2   . ILE D 2 159 ? 139.515 93.874  142.802 1.00 22.34 ?  138 ILE D CG2   1 
ATOM   14470 C  CD1   . ILE D 2 159 ? 141.222 94.988  145.153 1.00 23.85 ?  138 ILE D CD1   1 
ATOM   14471 N  N     . VAL D 2 160 ? 139.100 90.273  143.363 1.00 21.96 ?  139 VAL D N     1 
ATOM   14472 C  CA    . VAL D 2 160 ? 138.082 89.382  142.787 1.00 22.59 ?  139 VAL D CA    1 
ATOM   14473 C  C     . VAL D 2 160 ? 137.291 88.670  143.893 1.00 22.36 ?  139 VAL D C     1 
ATOM   14474 O  O     . VAL D 2 160 ? 136.076 88.481  143.770 1.00 21.64 ?  139 VAL D O     1 
ATOM   14475 C  CB    . VAL D 2 160 ? 138.723 88.351  141.796 1.00 23.08 ?  139 VAL D CB    1 
ATOM   14476 C  CG1   . VAL D 2 160 ? 137.777 87.179  141.475 1.00 24.33 ?  139 VAL D CG1   1 
ATOM   14477 C  CG2   . VAL D 2 160 ? 139.159 89.050  140.498 1.00 22.87 ?  139 VAL D CG2   1 
ATOM   14478 N  N     . GLY D 2 161 ? 137.985 88.288  144.969 1.00 22.21 ?  140 GLY D N     1 
ATOM   14479 C  CA    . GLY D 2 161 ? 137.341 87.668  146.126 1.00 22.50 ?  140 GLY D CA    1 
ATOM   14480 C  C     . GLY D 2 161 ? 136.236 88.540  146.713 1.00 22.88 ?  140 GLY D C     1 
ATOM   14481 O  O     . GLY D 2 161 ? 135.148 88.042  147.037 1.00 23.54 ?  140 GLY D O     1 
ATOM   14482 N  N     . LEU D 2 162 ? 136.501 89.840  146.841 1.00 22.25 ?  141 LEU D N     1 
ATOM   14483 C  CA    . LEU D 2 162 ? 135.494 90.769  147.360 1.00 22.48 ?  141 LEU D CA    1 
ATOM   14484 C  C     . LEU D 2 162 ? 134.315 90.976  146.406 1.00 22.27 ?  141 LEU D C     1 
ATOM   14485 O  O     . LEU D 2 162 ? 133.180 91.130  146.861 1.00 22.31 ?  141 LEU D O     1 
ATOM   14486 C  CB    . LEU D 2 162 ? 136.120 92.107  147.803 1.00 22.07 ?  141 LEU D CB    1 
ATOM   14487 C  CG    . LEU D 2 162 ? 136.902 92.024  149.132 1.00 22.81 ?  141 LEU D CG    1 
ATOM   14488 C  CD1   . LEU D 2 162 ? 137.906 93.165  149.283 1.00 21.65 ?  141 LEU D CD1   1 
ATOM   14489 C  CD2   . LEU D 2 162 ? 135.986 91.911  150.357 1.00 23.35 ?  141 LEU D CD2   1 
ATOM   14490 N  N     . TYR D 2 163 ? 134.572 90.980  145.096 1.00 22.63 ?  142 TYR D N     1 
ATOM   14491 C  CA    . TYR D 2 163 ? 133.478 91.033  144.104 1.00 23.30 ?  142 TYR D CA    1 
ATOM   14492 C  C     . TYR D 2 163 ? 132.595 89.793  144.165 1.00 23.40 ?  142 TYR D C     1 
ATOM   14493 O  O     . TYR D 2 163 ? 131.383 89.891  144.045 1.00 23.75 ?  142 TYR D O     1 
ATOM   14494 C  CB    . TYR D 2 163 ? 134.003 91.139  142.680 1.00 23.22 ?  142 TYR D CB    1 
ATOM   14495 C  CG    . TYR D 2 163 ? 134.816 92.363  142.361 1.00 24.01 ?  142 TYR D CG    1 
ATOM   14496 C  CD1   . TYR D 2 163 ? 134.693 93.525  143.111 1.00 24.47 ?  142 TYR D CD1   1 
ATOM   14497 C  CD2   . TYR D 2 163 ? 135.707 92.354  141.292 1.00 24.62 ?  142 TYR D CD2   1 
ATOM   14498 C  CE1   . TYR D 2 163 ? 135.439 94.647  142.813 1.00 26.33 ?  142 TYR D CE1   1 
ATOM   14499 C  CE2   . TYR D 2 163 ? 136.452 93.478  140.975 1.00 26.07 ?  142 TYR D CE2   1 
ATOM   14500 C  CZ    . TYR D 2 163 ? 136.305 94.624  141.745 1.00 26.65 ?  142 TYR D CZ    1 
ATOM   14501 O  OH    . TYR D 2 163 ? 137.044 95.748  141.456 1.00 31.13 ?  142 TYR D OH    1 
ATOM   14502 N  N     . LYS D 2 164 ? 133.208 88.630  144.340 1.00 23.70 ?  143 LYS D N     1 
ATOM   14503 C  CA    . LYS D 2 164 ? 132.455 87.369  144.435 1.00 24.47 ?  143 LYS D CA    1 
ATOM   14504 C  C     . LYS D 2 164 ? 131.637 87.236  145.730 1.00 24.55 ?  143 LYS D C     1 
ATOM   14505 O  O     . LYS D 2 164 ? 130.721 86.415  145.810 1.00 24.49 ?  143 LYS D O     1 
ATOM   14506 C  CB    . LYS D 2 164 ? 133.409 86.181  144.294 1.00 24.98 ?  143 LYS D CB    1 
ATOM   14507 C  CG    . LYS D 2 164 ? 133.900 85.919  142.862 1.00 27.10 ?  143 LYS D CG    1 
ATOM   14508 C  CD    . LYS D 2 164 ? 134.737 84.649  142.829 1.00 30.75 ?  143 LYS D CD    1 
ATOM   14509 C  CE    . LYS D 2 164 ? 135.176 84.266  141.416 1.00 32.81 ?  143 LYS D CE    1 
ATOM   14510 N  NZ    . LYS D 2 164 ? 136.097 83.060  141.415 1.00 33.68 1  143 LYS D NZ    1 
ATOM   14511 N  N     . ALA D 2 165 ? 131.976 88.032  146.740 1.00 24.18 ?  144 ALA D N     1 
ATOM   14512 C  CA    . ALA D 2 165 ? 131.317 87.949  148.046 1.00 25.04 ?  144 ALA D CA    1 
ATOM   14513 C  C     . ALA D 2 165 ? 130.103 88.876  148.209 1.00 25.00 ?  144 ALA D C     1 
ATOM   14514 O  O     . ALA D 2 165 ? 129.452 88.860  149.264 1.00 25.50 ?  144 ALA D O     1 
ATOM   14515 C  CB    . ALA D 2 165 ? 132.330 88.191  149.178 1.00 25.02 ?  144 ALA D CB    1 
ATOM   14516 N  N     . ILE D 2 166 ? 129.798 89.679  147.188 1.00 24.60 ?  145 ILE D N     1 
ATOM   14517 C  CA    . ILE D 2 166 ? 128.613 90.537  147.230 1.00 24.40 ?  145 ILE D CA    1 
ATOM   14518 C  C     . ILE D 2 166 ? 127.355 89.660  147.302 1.00 25.75 ?  145 ILE D C     1 
ATOM   14519 O  O     . ILE D 2 166 ? 127.217 88.690  146.550 1.00 25.84 ?  145 ILE D O     1 
ATOM   14520 C  CB    . ILE D 2 166 ? 128.497 91.485  146.002 1.00 24.15 ?  145 ILE D CB    1 
ATOM   14521 C  CG1   . ILE D 2 166 ? 129.798 92.253  145.773 1.00 23.15 ?  145 ILE D CG1   1 
ATOM   14522 C  CG2   . ILE D 2 166 ? 127.332 92.457  146.188 1.00 22.72 ?  145 ILE D CG2   1 
ATOM   14523 C  CD1   . ILE D 2 166 ? 129.837 93.015  144.465 1.00 21.70 ?  145 ILE D CD1   1 
ATOM   14524 N  N     . GLN D 2 167 ? 126.467 89.988  148.231 1.00 26.52 ?  146 GLN D N     1 
ATOM   14525 C  CA    . GLN D 2 167 ? 125.203 89.276  148.366 1.00 28.77 ?  146 GLN D CA    1 
ATOM   14526 C  C     . GLN D 2 167 ? 124.036 90.180  147.994 1.00 29.20 ?  146 GLN D C     1 
ATOM   14527 O  O     . GLN D 2 167 ? 124.035 91.377  148.317 1.00 28.89 ?  146 GLN D O     1 
ATOM   14528 C  CB    . GLN D 2 167 ? 125.035 88.761  149.793 1.00 29.04 ?  146 GLN D CB    1 
ATOM   14529 C  CG    . GLN D 2 167 ? 126.061 87.713  150.177 1.00 31.87 ?  146 GLN D CG    1 
ATOM   14530 C  CD    . GLN D 2 167 ? 126.615 87.943  151.558 1.00 35.35 ?  146 GLN D CD    1 
ATOM   14531 O  OE1   . GLN D 2 167 ? 125.908 87.790  152.557 1.00 36.91 ?  146 GLN D OE1   1 
ATOM   14532 N  NE2   . GLN D 2 167 ? 127.892 88.313  151.627 1.00 36.19 ?  146 GLN D NE2   1 
ATOM   14533 N  N     . LYS D 2 168 ? 123.045 89.604  147.318 1.00 30.29 ?  147 LYS D N     1 
ATOM   14534 C  CA    . LYS D 2 168 ? 121.836 90.340  146.954 1.00 31.24 ?  147 LYS D CA    1 
ATOM   14535 C  C     . LYS D 2 168 ? 121.231 91.048  148.166 1.00 31.73 ?  147 LYS D C     1 
ATOM   14536 O  O     . LYS D 2 168 ? 121.148 90.464  149.246 1.00 31.46 ?  147 LYS D O     1 
ATOM   14537 C  CB    . LYS D 2 168 ? 120.813 89.409  146.310 1.00 31.92 ?  147 LYS D CB    1 
ATOM   14538 C  CG    . LYS D 2 168 ? 119.560 90.124  145.826 1.00 33.23 ?  147 LYS D CG    1 
ATOM   14539 C  CD    . LYS D 2 168 ? 118.683 89.212  144.983 1.00 36.06 ?  147 LYS D CD    1 
ATOM   14540 C  CE    . LYS D 2 168 ? 117.405 89.911  144.568 1.00 35.46 ?  147 LYS D CE    1 
ATOM   14541 N  NZ    . LYS D 2 168 ? 117.648 90.973  143.555 1.00 38.24 1  147 LYS D NZ    1 
ATOM   14542 N  N     . ASP D 2 169 ? 120.835 92.310  147.978 1.00 32.28 ?  148 ASP D N     1 
ATOM   14543 C  CA    . ASP D 2 169 ? 120.227 93.135  149.035 1.00 33.45 ?  148 ASP D CA    1 
ATOM   14544 C  C     . ASP D 2 169 ? 121.058 93.301  150.307 1.00 33.30 ?  148 ASP D C     1 
ATOM   14545 O  O     . ASP D 2 169 ? 120.510 93.559  151.381 1.00 34.32 ?  148 ASP D O     1 
ATOM   14546 C  CB    . ASP D 2 169 ? 118.841 92.597  149.426 1.00 34.63 ?  148 ASP D CB    1 
ATOM   14547 C  CG    . ASP D 2 169 ? 117.784 92.857  148.374 1.00 36.09 ?  148 ASP D CG    1 
ATOM   14548 O  OD1   . ASP D 2 169 ? 118.015 93.656  147.442 1.00 37.80 ?  148 ASP D OD1   1 
ATOM   14549 O  OD2   . ASP D 2 169 ? 116.701 92.250  148.498 1.00 40.47 -1 148 ASP D OD2   1 
ATOM   14550 N  N     . ASP D 2 170 ? 122.368 93.133  150.209 1.00 32.58 ?  149 ASP D N     1 
ATOM   14551 C  CA    . ASP D 2 170 ? 123.232 93.395  151.358 1.00 32.01 ?  149 ASP D CA    1 
ATOM   14552 C  C     . ASP D 2 170 ? 124.202 94.514  150.999 1.00 30.59 ?  149 ASP D C     1 
ATOM   14553 O  O     . ASP D 2 170 ? 125.174 94.302  150.273 1.00 29.11 ?  149 ASP D O     1 
ATOM   14554 C  CB    . ASP D 2 170 ? 123.961 92.127  151.809 1.00 32.93 ?  149 ASP D CB    1 
ATOM   14555 C  CG    . ASP D 2 170 ? 125.051 92.400  152.836 1.00 35.05 ?  149 ASP D CG    1 
ATOM   14556 O  OD1   . ASP D 2 170 ? 124.954 93.370  153.620 1.00 39.25 ?  149 ASP D OD1   1 
ATOM   14557 O  OD2   . ASP D 2 170 ? 126.014 91.623  152.875 1.00 39.22 -1 149 ASP D OD2   1 
ATOM   14558 N  N     . GLU D 2 171 ? 123.908 95.706  151.511 1.00 29.34 ?  150 GLU D N     1 
ATOM   14559 C  CA    . GLU D 2 171 ? 124.675 96.904  151.185 1.00 28.51 ?  150 GLU D CA    1 
ATOM   14560 C  C     . GLU D 2 171 ? 126.074 96.926  151.816 1.00 27.27 ?  150 GLU D C     1 
ATOM   14561 O  O     . GLU D 2 171 ? 126.956 97.610  151.322 1.00 26.62 ?  150 GLU D O     1 
ATOM   14562 C  CB    . GLU D 2 171 ? 123.881 98.168  151.542 1.00 29.09 ?  150 GLU D CB    1 
ATOM   14563 C  CG    . GLU D 2 171 ? 123.691 98.424  153.036 1.00 30.68 ?  150 GLU D CG    1 
ATOM   14564 C  CD    . GLU D 2 171 ? 122.748 99.584  153.311 1.00 33.92 ?  150 GLU D CD    1 
ATOM   14565 O  OE1   . GLU D 2 171 ? 122.275 100.217 152.336 1.00 36.31 ?  150 GLU D OE1   1 
ATOM   14566 O  OE2   . GLU D 2 171 ? 122.477 99.876  154.497 1.00 34.02 -1 150 GLU D OE2   1 
ATOM   14567 N  N     . ILE D 2 172 ? 126.277 96.160  152.887 1.00 26.19 ?  151 ILE D N     1 
ATOM   14568 C  CA    . ILE D 2 172 ? 127.594 96.064  153.518 1.00 25.49 ?  151 ILE D CA    1 
ATOM   14569 C  C     . ILE D 2 172 ? 128.583 95.352  152.590 1.00 24.61 ?  151 ILE D C     1 
ATOM   14570 O  O     . ILE D 2 172 ? 129.698 95.841  152.366 1.00 24.09 ?  151 ILE D O     1 
ATOM   14571 C  CB    . ILE D 2 172 ? 127.527 95.380  154.912 1.00 25.98 ?  151 ILE D CB    1 
ATOM   14572 C  CG1   . ILE D 2 172 ? 126.690 96.211  155.886 1.00 26.86 ?  151 ILE D CG1   1 
ATOM   14573 C  CG2   . ILE D 2 172 ? 128.937 95.107  155.502 1.00 26.50 ?  151 ILE D CG2   1 
ATOM   14574 C  CD1   . ILE D 2 172 ? 127.227 97.612  156.140 1.00 27.81 ?  151 ILE D CD1   1 
ATOM   14575 N  N     . SER D 2 173 ? 128.161 94.219  152.038 1.00 23.71 ?  152 SER D N     1 
ATOM   14576 C  CA    . SER D 2 173 ? 128.994 93.461  151.105 1.00 23.38 ?  152 SER D CA    1 
ATOM   14577 C  C     . SER D 2 173 ? 129.221 94.249  149.802 1.00 22.41 ?  152 SER D C     1 
ATOM   14578 O  O     . SER D 2 173 ? 130.291 94.169  149.192 1.00 21.43 ?  152 SER D O     1 
ATOM   14579 C  CB    . SER D 2 173 ? 128.394 92.076  150.830 1.00 23.90 ?  152 SER D CB    1 
ATOM   14580 O  OG    . SER D 2 173 ? 127.200 92.123  150.050 1.00 23.74 ?  152 SER D OG    1 
ATOM   14581 N  N     . LEU D 2 174 ? 128.220 95.023  149.395 1.00 21.63 ?  153 LEU D N     1 
ATOM   14582 C  CA    . LEU D 2 174 ? 128.371 95.882  148.217 1.00 20.75 ?  153 LEU D CA    1 
ATOM   14583 C  C     . LEU D 2 174 ? 129.421 96.958  148.490 1.00 20.96 ?  153 LEU D C     1 
ATOM   14584 O  O     . LEU D 2 174 ? 130.282 97.216  147.650 1.00 20.41 ?  153 LEU D O     1 
ATOM   14585 C  CB    . LEU D 2 174 ? 127.028 96.520  147.811 1.00 20.62 ?  153 LEU D CB    1 
ATOM   14586 C  CG    . LEU D 2 174 ? 127.056 97.483  146.605 1.00 19.55 ?  153 LEU D CG    1 
ATOM   14587 C  CD1   . LEU D 2 174 ? 127.701 96.814  145.385 1.00 20.44 ?  153 LEU D CD1   1 
ATOM   14588 C  CD2   . LEU D 2 174 ? 125.635 97.968  146.286 1.00 20.99 ?  153 LEU D CD2   1 
ATOM   14589 N  N     . PHE D 2 175 ? 129.349 97.578  149.668 1.00 21.07 ?  154 PHE D N     1 
ATOM   14590 C  CA    . PHE D 2 175 ? 130.309 98.612  150.048 1.00 21.32 ?  154 PHE D CA    1 
ATOM   14591 C  C     . PHE D 2 175 ? 131.746 98.078  150.025 1.00 21.08 ?  154 PHE D C     1 
ATOM   14592 O  O     . PHE D 2 175 ? 132.653 98.731  149.505 1.00 20.85 ?  154 PHE D O     1 
ATOM   14593 C  CB    . PHE D 2 175 ? 129.976 99.170  151.436 1.00 21.20 ?  154 PHE D CB    1 
ATOM   14594 C  CG    . PHE D 2 175 ? 131.055 100.034 152.018 1.00 22.46 ?  154 PHE D CG    1 
ATOM   14595 C  CD1   . PHE D 2 175 ? 131.052 101.410 151.797 1.00 21.21 ?  154 PHE D CD1   1 
ATOM   14596 C  CD2   . PHE D 2 175 ? 132.075 99.480  152.796 1.00 22.53 ?  154 PHE D CD2   1 
ATOM   14597 C  CE1   . PHE D 2 175 ? 132.035 102.216 152.336 1.00 22.11 ?  154 PHE D CE1   1 
ATOM   14598 C  CE2   . PHE D 2 175 ? 133.080 100.282 153.329 1.00 23.26 ?  154 PHE D CE2   1 
ATOM   14599 C  CZ    . PHE D 2 175 ? 133.059 101.655 153.105 1.00 22.08 ?  154 PHE D CZ    1 
ATOM   14600 N  N     . LYS D 2 176 ? 131.946 96.898  150.602 1.00 21.14 ?  155 LYS D N     1 
ATOM   14601 C  CA    . LYS D 2 176 ? 133.268 96.265  150.629 1.00 20.93 ?  155 LYS D CA    1 
ATOM   14602 C  C     . LYS D 2 176 ? 133.831 96.044  149.227 1.00 20.61 ?  155 LYS D C     1 
ATOM   14603 O  O     . LYS D 2 176 ? 135.016 96.291  148.975 1.00 20.62 ?  155 LYS D O     1 
ATOM   14604 C  CB    . LYS D 2 176 ? 133.198 94.951  151.392 1.00 21.27 ?  155 LYS D CB    1 
ATOM   14605 C  CG    . LYS D 2 176 ? 133.059 95.169  152.874 1.00 22.04 ?  155 LYS D CG    1 
ATOM   14606 C  CD    . LYS D 2 176 ? 132.881 93.872  153.644 1.00 25.24 ?  155 LYS D CD    1 
ATOM   14607 C  CE    . LYS D 2 176 ? 132.815 94.177  155.119 1.00 25.83 ?  155 LYS D CE    1 
ATOM   14608 N  NZ    . LYS D 2 176 ? 132.659 92.955  155.960 1.00 26.64 1  155 LYS D NZ    1 
ATOM   14609 N  N     . ALA D 2 177 ? 132.970 95.607  148.315 1.00 20.02 ?  156 ALA D N     1 
ATOM   14610 C  CA    . ALA D 2 177 ? 133.350 95.455  146.912 1.00 19.86 ?  156 ALA D CA    1 
ATOM   14611 C  C     . ALA D 2 177 ? 133.670 96.803  146.250 1.00 19.61 ?  156 ALA D C     1 
ATOM   14612 O  O     . ALA D 2 177 ? 134.555 96.894  145.397 1.00 19.69 ?  156 ALA D O     1 
ATOM   14613 C  CB    . ALA D 2 177 ? 132.253 94.760  146.174 1.00 19.99 ?  156 ALA D CB    1 
ATOM   14614 N  N     . MET D 2 178 ? 132.941 97.847  146.637 1.00 19.75 ?  157 MET D N     1 
ATOM   14615 C  CA    . MET D 2 178 ? 133.171 99.193  146.071 1.00 18.89 ?  157 MET D CA    1 
ATOM   14616 C  C     . MET D 2 178 ? 134.519 99.731  146.526 1.00 18.62 ?  157 MET D C     1 
ATOM   14617 O  O     . MET D 2 178 ? 135.242 100.357 145.743 1.00 18.10 ?  157 MET D O     1 
ATOM   14618 C  CB    . MET D 2 178 ? 132.055 100.152 146.471 1.00 18.82 ?  157 MET D CB    1 
ATOM   14619 C  CG    . MET D 2 178 ? 130.757 99.912  145.717 1.00 20.20 ?  157 MET D CG    1 
ATOM   14620 S  SD    . MET D 2 178 ? 129.461 100.982 146.358 1.00 23.78 ?  157 MET D SD    1 
ATOM   14621 C  CE    . MET D 2 178 ? 128.177 100.672 145.148 1.00 22.62 ?  157 MET D CE    1 
ATOM   14622 N  N     . VAL D 2 179 ? 134.855 99.457  147.787 1.00 18.34 ?  158 VAL D N     1 
ATOM   14623 C  CA    . VAL D 2 179 ? 136.160 99.803  148.332 1.00 18.75 ?  158 VAL D CA    1 
ATOM   14624 C  C     . VAL D 2 179 ? 137.263 99.115  147.537 1.00 18.86 ?  158 VAL D C     1 
ATOM   14625 O  O     . VAL D 2 179 ? 138.254 99.766  147.160 1.00 18.79 ?  158 VAL D O     1 
ATOM   14626 C  CB    . VAL D 2 179 ? 136.294 99.447  149.836 1.00 19.02 ?  158 VAL D CB    1 
ATOM   14627 C  CG1   . VAL D 2 179 ? 137.750 99.621  150.294 1.00 19.10 ?  158 VAL D CG1   1 
ATOM   14628 C  CG2   . VAL D 2 179 ? 135.344 100.305 150.686 1.00 18.94 ?  158 VAL D CG2   1 
ATOM   14629 N  N     . ALA D 2 180 ? 137.093 97.808  147.300 1.00 18.96 ?  159 ALA D N     1 
ATOM   14630 C  CA    . ALA D 2 180 ? 138.017 97.043  146.461 1.00 19.05 ?  159 ALA D CA    1 
ATOM   14631 C  C     . ALA D 2 180 ? 138.140 97.663  145.068 1.00 18.67 ?  159 ALA D C     1 
ATOM   14632 O  O     . ALA D 2 180 ? 139.253 97.833  144.554 1.00 17.72 ?  159 ALA D O     1 
ATOM   14633 C  CB    . ALA D 2 180 ? 137.578 95.570  146.364 1.00 19.43 ?  159 ALA D CB    1 
ATOM   14634 N  N     . SER D 2 181 ? 136.997 98.029  144.479 1.00 18.49 ?  160 SER D N     1 
ATOM   14635 C  CA    . SER D 2 181 ? 136.989 98.648  143.153 1.00 18.51 ?  160 SER D CA    1 
ATOM   14636 C  C     . SER D 2 181 ? 137.729 99.986  143.126 1.00 18.23 ?  160 SER D C     1 
ATOM   14637 O  O     . SER D 2 181 ? 138.540 100.230 142.243 1.00 18.18 ?  160 SER D O     1 
ATOM   14638 C  CB    . SER D 2 181 ? 135.560 98.837  142.636 1.00 18.51 ?  160 SER D CB    1 
ATOM   14639 O  OG    . SER D 2 181 ? 135.604 99.275  141.292 1.00 19.42 ?  160 SER D OG    1 
ATOM   14640 N  N     . VAL D 2 182 ? 137.451 100.845 144.105 1.00 18.43 ?  161 VAL D N     1 
ATOM   14641 C  CA    . VAL D 2 182 ? 138.165 102.121 144.213 1.00 18.09 ?  161 VAL D CA    1 
ATOM   14642 C  C     . VAL D 2 182 ? 139.670 101.900 144.398 1.00 18.41 ?  161 VAL D C     1 
ATOM   14643 O  O     . VAL D 2 182 ? 140.482 102.585 143.772 1.00 18.52 ?  161 VAL D O     1 
ATOM   14644 C  CB    . VAL D 2 182 ? 137.591 103.007 145.326 1.00 17.71 ?  161 VAL D CB    1 
ATOM   14645 C  CG1   . VAL D 2 182 ? 138.488 104.246 145.563 1.00 16.02 ?  161 VAL D CG1   1 
ATOM   14646 C  CG2   . VAL D 2 182 ? 136.169 103.444 144.947 1.00 17.78 ?  161 VAL D CG2   1 
ATOM   14647 N  N     . TYR D 2 183 ? 140.038 100.914 145.219 1.00 19.06 ?  162 TYR D N     1 
ATOM   14648 C  CA    . TYR D 2 183 ? 141.453 100.609 145.405 1.00 19.73 ?  162 TYR D CA    1 
ATOM   14649 C  C     . TYR D 2 183 ? 142.106 100.164 144.103 1.00 19.90 ?  162 TYR D C     1 
ATOM   14650 O  O     . TYR D 2 183 ? 143.253 100.497 143.857 1.00 20.73 ?  162 TYR D O     1 
ATOM   14651 C  CB    . TYR D 2 183 ? 141.700 99.581  146.525 1.00 19.84 ?  162 TYR D CB    1 
ATOM   14652 C  CG    . TYR D 2 183 ? 141.496 100.121 147.926 1.00 20.24 ?  162 TYR D CG    1 
ATOM   14653 C  CD1   . TYR D 2 183 ? 141.377 101.489 148.160 1.00 21.51 ?  162 TYR D CD1   1 
ATOM   14654 C  CD2   . TYR D 2 183 ? 141.446 99.259  149.028 1.00 20.45 ?  162 TYR D CD2   1 
ATOM   14655 C  CE1   . TYR D 2 183 ? 141.196 101.987 149.457 1.00 21.68 ?  162 TYR D CE1   1 
ATOM   14656 C  CE2   . TYR D 2 183 ? 141.287 99.749  150.330 1.00 19.97 ?  162 TYR D CE2   1 
ATOM   14657 C  CZ    . TYR D 2 183 ? 141.158 101.113 150.533 1.00 21.83 ?  162 TYR D CZ    1 
ATOM   14658 O  OH    . TYR D 2 183 ? 140.990 101.609 151.811 1.00 21.96 ?  162 TYR D OH    1 
ATOM   14659 N  N     . LEU D 2 184 ? 141.382 99.438  143.263 1.00 20.22 ?  163 LEU D N     1 
ATOM   14660 C  CA    . LEU D 2 184 ? 141.945 99.033  141.978 1.00 20.89 ?  163 LEU D CA    1 
ATOM   14661 C  C     . LEU D 2 184 ? 142.084 100.250 141.052 1.00 20.72 ?  163 LEU D C     1 
ATOM   14662 O  O     . LEU D 2 184 ? 143.173 100.532 140.561 1.00 21.07 ?  163 LEU D O     1 
ATOM   14663 C  CB    . LEU D 2 184 ? 141.137 97.886  141.340 1.00 21.16 ?  163 LEU D CB    1 
ATOM   14664 C  CG    . LEU D 2 184 ? 141.555 97.351  139.955 1.00 22.77 ?  163 LEU D CG    1 
ATOM   14665 C  CD1   . LEU D 2 184 ? 143.052 96.976  139.883 1.00 22.44 ?  163 LEU D CD1   1 
ATOM   14666 C  CD2   . LEU D 2 184 ? 140.697 96.166  139.539 1.00 24.75 ?  163 LEU D CD2   1 
ATOM   14667 N  N     . GLU D 2 185 ? 140.989 100.983 140.859 1.00 20.65 ?  164 GLU D N     1 
ATOM   14668 C  CA    . GLU D 2 185 ? 140.951 102.143 139.956 1.00 20.69 ?  164 GLU D CA    1 
ATOM   14669 C  C     . GLU D 2 185 ? 141.912 103.271 140.332 1.00 20.64 ?  164 GLU D C     1 
ATOM   14670 O  O     . GLU D 2 185 ? 142.526 103.896 139.454 1.00 20.25 ?  164 GLU D O     1 
ATOM   14671 C  CB    . GLU D 2 185 ? 139.531 102.724 139.893 1.00 21.03 ?  164 GLU D CB    1 
ATOM   14672 C  CG    . GLU D 2 185 ? 138.452 101.744 139.421 1.00 22.19 ?  164 GLU D CG    1 
ATOM   14673 C  CD    . GLU D 2 185 ? 138.347 101.623 137.903 1.00 24.19 ?  164 GLU D CD    1 
ATOM   14674 O  OE1   . GLU D 2 185 ? 139.158 102.209 137.164 1.00 27.97 ?  164 GLU D OE1   1 
ATOM   14675 O  OE2   . GLU D 2 185 ? 137.427 100.952 137.434 1.00 25.47 -1 164 GLU D OE2   1 
ATOM   14676 N  N     . SER D 2 186 ? 142.012 103.550 141.627 1.00 20.42 ?  165 SER D N     1 
ATOM   14677 C  CA    . SER D 2 186 ? 142.691 104.754 142.104 1.00 20.70 ?  165 SER D CA    1 
ATOM   14678 C  C     . SER D 2 186 ? 144.029 104.487 142.793 1.00 20.88 ?  165 SER D C     1 
ATOM   14679 O  O     . SER D 2 186 ? 144.690 105.424 143.241 1.00 21.21 ?  165 SER D O     1 
ATOM   14680 C  CB    . SER D 2 186 ? 141.777 105.549 143.054 1.00 21.25 ?  165 SER D CB    1 
ATOM   14681 O  OG    . SER D 2 186 ? 140.505 105.804 142.475 1.00 20.97 ?  165 SER D OG    1 
ATOM   14682 N  N     . PHE D 2 187 ? 144.444 103.223 142.876 1.00 20.94 ?  166 PHE D N     1 
ATOM   14683 C  CA    . PHE D 2 187 ? 145.617 102.895 143.674 1.00 21.19 ?  166 PHE D CA    1 
ATOM   14684 C  C     . PHE D 2 187 ? 146.450 101.774 143.053 1.00 21.22 ?  166 PHE D C     1 
ATOM   14685 O  O     . PHE D 2 187 ? 147.602 102.017 142.678 1.00 21.10 ?  166 PHE D O     1 
ATOM   14686 C  CB    . PHE D 2 187 ? 145.201 102.650 145.151 1.00 21.63 ?  166 PHE D CB    1 
ATOM   14687 C  CG    . PHE D 2 187 ? 146.186 101.857 145.971 1.00 24.05 ?  166 PHE D CG    1 
ATOM   14688 C  CD1   . PHE D 2 187 ? 147.497 102.296 146.152 1.00 25.52 ?  166 PHE D CD1   1 
ATOM   14689 C  CD2   . PHE D 2 187 ? 145.782 100.687 146.609 1.00 27.03 ?  166 PHE D CD2   1 
ATOM   14690 C  CE1   . PHE D 2 187 ? 148.388 101.569 146.930 1.00 26.73 ?  166 PHE D CE1   1 
ATOM   14691 C  CE2   . PHE D 2 187 ? 146.683 99.945  147.386 1.00 27.36 ?  166 PHE D CE2   1 
ATOM   14692 C  CZ    . PHE D 2 187 ? 147.980 100.389 147.540 1.00 27.87 ?  166 PHE D CZ    1 
ATOM   14693 N  N     . LEU D 2 188 ? 145.867 100.589 142.895 1.00 20.78 ?  167 LEU D N     1 
ATOM   14694 C  CA    . LEU D 2 188 ? 146.621 99.410  142.419 1.00 21.78 ?  167 LEU D CA    1 
ATOM   14695 C  C     . LEU D 2 188 ? 147.187 99.530  140.999 1.00 21.91 ?  167 LEU D C     1 
ATOM   14696 O  O     . LEU D 2 188 ? 148.247 98.973  140.713 1.00 22.87 ?  167 LEU D O     1 
ATOM   14697 C  CB    . LEU D 2 188 ? 145.778 98.140  142.527 1.00 22.32 ?  167 LEU D CB    1 
ATOM   14698 C  CG    . LEU D 2 188 ? 145.379 97.592  143.897 1.00 23.33 ?  167 LEU D CG    1 
ATOM   14699 C  CD1   . LEU D 2 188 ? 144.532 96.348  143.695 1.00 22.43 ?  167 LEU D CD1   1 
ATOM   14700 C  CD2   . LEU D 2 188 ? 146.589 97.284  144.789 1.00 25.71 ?  167 LEU D CD2   1 
ATOM   14701 N  N     . PHE D 2 189 ? 146.478 100.231 140.112 1.00 21.56 ?  168 PHE D N     1 
ATOM   14702 C  CA    . PHE D 2 189 ? 146.960 100.471 138.749 1.00 21.86 ?  168 PHE D CA    1 
ATOM   14703 C  C     . PHE D 2 189 ? 148.252 101.314 138.713 1.00 21.87 ?  168 PHE D C     1 
ATOM   14704 O  O     . PHE D 2 189 ? 149.014 101.257 137.744 1.00 21.79 ?  168 PHE D O     1 
ATOM   14705 C  CB    . PHE D 2 189 ? 145.900 101.206 137.908 1.00 21.79 ?  168 PHE D CB    1 
ATOM   14706 C  CG    . PHE D 2 189 ? 144.798 100.322 137.370 1.00 21.88 ?  168 PHE D CG    1 
ATOM   14707 C  CD1   . PHE D 2 189 ? 145.062 99.033  136.903 1.00 21.44 ?  168 PHE D CD1   1 
ATOM   14708 C  CD2   . PHE D 2 189 ? 143.492 100.806 137.300 1.00 22.82 ?  168 PHE D CD2   1 
ATOM   14709 C  CE1   . PHE D 2 189 ? 144.032 98.226  136.400 1.00 22.35 ?  168 PHE D CE1   1 
ATOM   14710 C  CE2   . PHE D 2 189 ? 142.454 100.018 136.800 1.00 22.08 ?  168 PHE D CE2   1 
ATOM   14711 C  CZ    . PHE D 2 189 ? 142.722 98.719  136.358 1.00 22.60 ?  168 PHE D CZ    1 
ATOM   14712 N  N     . TYR D 2 190 ? 148.487 102.111 139.751 1.00 21.91 ?  169 TYR D N     1 
ATOM   14713 C  CA    . TYR D 2 190 ? 149.513 103.160 139.657 1.00 22.52 ?  169 TYR D CA    1 
ATOM   14714 C  C     . TYR D 2 190 ? 150.964 102.692 139.781 1.00 22.75 ?  169 TYR D C     1 
ATOM   14715 O  O     . TYR D 2 190 ? 151.849 103.344 139.242 1.00 21.93 ?  169 TYR D O     1 
ATOM   14716 C  CB    . TYR D 2 190 ? 149.191 104.347 140.569 1.00 22.67 ?  169 TYR D CB    1 
ATOM   14717 C  CG    . TYR D 2 190 ? 148.085 105.193 139.973 1.00 24.77 ?  169 TYR D CG    1 
ATOM   14718 C  CD1   . TYR D 2 190 ? 146.753 104.769 140.013 1.00 25.65 ?  169 TYR D CD1   1 
ATOM   14719 C  CD2   . TYR D 2 190 ? 148.375 106.392 139.327 1.00 25.94 ?  169 TYR D CD2   1 
ATOM   14720 C  CE1   . TYR D 2 190 ? 145.736 105.536 139.433 1.00 26.62 ?  169 TYR D CE1   1 
ATOM   14721 C  CE2   . TYR D 2 190 ? 147.368 107.171 138.761 1.00 26.91 ?  169 TYR D CE2   1 
ATOM   14722 C  CZ    . TYR D 2 190 ? 146.057 106.738 138.813 1.00 27.39 ?  169 TYR D CZ    1 
ATOM   14723 O  OH    . TYR D 2 190 ? 145.074 107.522 138.239 1.00 27.50 ?  169 TYR D OH    1 
ATOM   14724 N  N     . SER D 2 191 ? 151.203 101.559 140.450 1.00 22.74 ?  170 SER D N     1 
ATOM   14725 C  CA    . SER D 2 191 ? 152.534 100.942 140.413 1.00 23.43 ?  170 SER D CA    1 
ATOM   14726 C  C     . SER D 2 191 ? 152.873 100.566 138.970 1.00 23.08 ?  170 SER D C     1 
ATOM   14727 O  O     . SER D 2 191 ? 154.028 100.557 138.581 1.00 23.67 ?  170 SER D O     1 
ATOM   14728 C  CB    . SER D 2 191 ? 152.626 99.709  141.326 1.00 23.39 ?  170 SER D CB    1 
ATOM   14729 O  OG    . SER D 2 191 ? 151.714 98.695  140.927 1.00 24.10 ?  170 SER D OG    1 
ATOM   14730 N  N     . GLY D 2 192 ? 151.844 100.297 138.177 1.00 22.82 ?  171 GLY D N     1 
ATOM   14731 C  CA    . GLY D 2 192 ? 151.998 99.984  136.762 1.00 22.08 ?  171 GLY D CA    1 
ATOM   14732 C  C     . GLY D 2 192 ? 152.075 101.214 135.871 1.00 22.12 ?  171 GLY D C     1 
ATOM   14733 O  O     . GLY D 2 192 ? 152.986 101.324 135.049 1.00 22.86 ?  171 GLY D O     1 
ATOM   14734 N  N     . PHE D 2 193 ? 151.130 102.138 136.034 1.00 21.48 ?  172 PHE D N     1 
ATOM   14735 C  CA    . PHE D 2 193 ? 151.103 103.384 135.244 1.00 21.06 ?  172 PHE D CA    1 
ATOM   14736 C  C     . PHE D 2 193 ? 152.415 104.163 135.338 1.00 21.13 ?  172 PHE D C     1 
ATOM   14737 O  O     . PHE D 2 193 ? 152.776 104.877 134.401 1.00 21.18 ?  172 PHE D O     1 
ATOM   14738 C  CB    . PHE D 2 193 ? 149.967 104.300 135.698 1.00 21.33 ?  172 PHE D CB    1 
ATOM   14739 C  CG    . PHE D 2 193 ? 148.585 103.826 135.314 1.00 20.93 ?  172 PHE D CG    1 
ATOM   14740 C  CD1   . PHE D 2 193 ? 148.365 103.071 134.163 1.00 20.88 ?  172 PHE D CD1   1 
ATOM   14741 C  CD2   . PHE D 2 193 ? 147.492 104.189 136.091 1.00 19.83 ?  172 PHE D CD2   1 
ATOM   14742 C  CE1   . PHE D 2 193 ? 147.072 102.659 133.818 1.00 22.31 ?  172 PHE D CE1   1 
ATOM   14743 C  CE2   . PHE D 2 193 ? 146.195 103.793 135.746 1.00 20.67 ?  172 PHE D CE2   1 
ATOM   14744 C  CZ    . PHE D 2 193 ? 145.987 103.028 134.608 1.00 21.00 ?  172 PHE D CZ    1 
ATOM   14745 N  N     . TYR D 2 194 ? 153.125 104.014 136.458 1.00 20.48 ?  173 TYR D N     1 
ATOM   14746 C  CA    . TYR D 2 194 ? 154.366 104.749 136.691 1.00 20.76 ?  173 TYR D CA    1 
ATOM   14747 C  C     . TYR D 2 194 ? 155.310 104.684 135.485 1.00 20.53 ?  173 TYR D C     1 
ATOM   14748 O  O     . TYR D 2 194 ? 155.808 105.706 135.002 1.00 19.89 ?  173 TYR D O     1 
ATOM   14749 C  CB    . TYR D 2 194 ? 155.088 104.241 137.965 1.00 20.94 ?  173 TYR D CB    1 
ATOM   14750 C  CG    . TYR D 2 194 ? 156.254 105.128 138.365 1.00 21.56 ?  173 TYR D CG    1 
ATOM   14751 C  CD1   . TYR D 2 194 ? 156.115 106.084 139.375 1.00 22.23 ?  173 TYR D CD1   1 
ATOM   14752 C  CD2   . TYR D 2 194 ? 157.491 105.030 137.717 1.00 22.00 ?  173 TYR D CD2   1 
ATOM   14753 C  CE1   . TYR D 2 194 ? 157.176 106.916 139.728 1.00 21.58 ?  173 TYR D CE1   1 
ATOM   14754 C  CE2   . TYR D 2 194 ? 158.550 105.847 138.067 1.00 20.52 ?  173 TYR D CE2   1 
ATOM   14755 C  CZ    . TYR D 2 194 ? 158.387 106.788 139.070 1.00 21.66 ?  173 TYR D CZ    1 
ATOM   14756 O  OH    . TYR D 2 194 ? 159.433 107.617 139.398 1.00 21.37 ?  173 TYR D OH    1 
ATOM   14757 N  N     . TYR D 2 195 ? 155.529 103.482 134.980 1.00 20.77 ?  174 TYR D N     1 
ATOM   14758 C  CA    . TYR D 2 195 ? 156.566 103.289 133.982 1.00 21.12 ?  174 TYR D CA    1 
ATOM   14759 C  C     . TYR D 2 195 ? 156.241 103.948 132.629 1.00 21.49 ?  174 TYR D C     1 
ATOM   14760 O  O     . TYR D 2 195 ? 157.070 104.706 132.118 1.00 21.60 ?  174 TYR D O     1 
ATOM   14761 C  CB    . TYR D 2 195 ? 156.931 101.805 133.871 1.00 21.23 ?  174 TYR D CB    1 
ATOM   14762 C  CG    . TYR D 2 195 ? 158.362 101.528 133.470 1.00 21.77 ?  174 TYR D CG    1 
ATOM   14763 C  CD1   . TYR D 2 195 ? 159.418 102.313 133.946 1.00 23.28 ?  174 TYR D CD1   1 
ATOM   14764 C  CD2   . TYR D 2 195 ? 158.664 100.459 132.628 1.00 22.87 ?  174 TYR D CD2   1 
ATOM   14765 C  CE1   . TYR D 2 195 ? 160.742 102.040 133.570 1.00 23.81 ?  174 TYR D CE1   1 
ATOM   14766 C  CE2   . TYR D 2 195 ? 159.978 100.178 132.260 1.00 24.09 ?  174 TYR D CE2   1 
ATOM   14767 C  CZ    . TYR D 2 195 ? 161.005 100.971 132.727 1.00 23.51 ?  174 TYR D CZ    1 
ATOM   14768 O  OH    . TYR D 2 195 ? 162.305 100.693 132.349 1.00 25.36 ?  174 TYR D OH    1 
ATOM   14769 N  N     . PRO D 2 196 ? 155.041 103.680 132.051 1.00 21.86 ?  175 PRO D N     1 
ATOM   14770 C  CA    . PRO D 2 196 ? 154.657 104.394 130.824 1.00 22.03 ?  175 PRO D CA    1 
ATOM   14771 C  C     . PRO D 2 196 ? 154.675 105.913 130.987 1.00 22.18 ?  175 PRO D C     1 
ATOM   14772 O  O     . PRO D 2 196 ? 155.085 106.613 130.058 1.00 23.00 ?  175 PRO D O     1 
ATOM   14773 C  CB    . PRO D 2 196 ? 153.222 103.921 130.557 1.00 21.50 ?  175 PRO D CB    1 
ATOM   14774 C  CG    . PRO D 2 196 ? 153.085 102.664 131.262 1.00 22.47 ?  175 PRO D CG    1 
ATOM   14775 C  CD    . PRO D 2 196 ? 154.108 102.581 132.356 1.00 20.91 ?  175 PRO D CD    1 
ATOM   14776 N  N     . LEU D 2 197 ? 154.251 106.415 132.148 1.00 21.70 ?  176 LEU D N     1 
ATOM   14777 C  CA    . LEU D 2 197 ? 154.308 107.858 132.426 1.00 22.40 ?  176 LEU D CA    1 
ATOM   14778 C  C     . LEU D 2 197 ? 155.743 108.381 132.513 1.00 22.58 ?  176 LEU D C     1 
ATOM   14779 O  O     . LEU D 2 197 ? 156.033 109.499 132.068 1.00 22.15 ?  176 LEU D O     1 
ATOM   14780 C  CB    . LEU D 2 197 ? 153.576 108.198 133.718 1.00 22.15 ?  176 LEU D CB    1 
ATOM   14781 C  CG    . LEU D 2 197 ? 152.045 108.110 133.761 1.00 23.08 ?  176 LEU D CG    1 
ATOM   14782 C  CD1   . LEU D 2 197 ? 151.606 108.138 135.215 1.00 21.62 ?  176 LEU D CD1   1 
ATOM   14783 C  CD2   . LEU D 2 197 ? 151.398 109.257 132.958 1.00 21.94 ?  176 LEU D CD2   1 
ATOM   14784 N  N     . TYR D 2 198 ? 156.622 107.563 133.097 1.00 22.76 ?  177 TYR D N     1 
ATOM   14785 C  CA    . TYR D 2 198 ? 158.055 107.851 133.188 1.00 23.23 ?  177 TYR D CA    1 
ATOM   14786 C  C     . TYR D 2 198 ? 158.680 107.982 131.800 1.00 23.91 ?  177 TYR D C     1 
ATOM   14787 O  O     . TYR D 2 198 ? 159.416 108.945 131.535 1.00 24.20 ?  177 TYR D O     1 
ATOM   14788 C  CB    . TYR D 2 198 ? 158.760 106.771 134.027 1.00 23.19 ?  177 TYR D CB    1 
ATOM   14789 C  CG    . TYR D 2 198 ? 160.249 106.966 134.240 1.00 23.52 ?  177 TYR D CG    1 
ATOM   14790 C  CD1   . TYR D 2 198 ? 160.730 108.021 135.002 1.00 24.85 ?  177 TYR D CD1   1 
ATOM   14791 C  CD2   . TYR D 2 198 ? 161.175 106.058 133.711 1.00 25.30 ?  177 TYR D CD2   1 
ATOM   14792 C  CE1   . TYR D 2 198 ? 162.100 108.194 135.218 1.00 26.05 ?  177 TYR D CE1   1 
ATOM   14793 C  CE2   . TYR D 2 198 ? 162.554 106.219 133.926 1.00 26.38 ?  177 TYR D CE2   1 
ATOM   14794 C  CZ    . TYR D 2 198 ? 162.999 107.288 134.680 1.00 26.68 ?  177 TYR D CZ    1 
ATOM   14795 O  OH    . TYR D 2 198 ? 164.346 107.468 134.909 1.00 30.01 ?  177 TYR D OH    1 
ATOM   14796 N  N     . PHE D 2 199 ? 158.389 107.037 130.906 1.00 24.84 ?  178 PHE D N     1 
ATOM   14797 C  CA    . PHE D 2 199 ? 158.845 107.166 129.518 1.00 25.81 ?  178 PHE D CA    1 
ATOM   14798 C  C     . PHE D 2 199 ? 158.220 108.350 128.791 1.00 26.23 ?  178 PHE D C     1 
ATOM   14799 O  O     . PHE D 2 199 ? 158.917 109.102 128.109 1.00 26.58 ?  178 PHE D O     1 
ATOM   14800 C  CB    . PHE D 2 199 ? 158.614 105.880 128.735 1.00 26.08 ?  178 PHE D CB    1 
ATOM   14801 C  CG    . PHE D 2 199 ? 159.594 104.794 129.064 1.00 28.71 ?  178 PHE D CG    1 
ATOM   14802 C  CD1   . PHE D 2 199 ? 160.954 105.068 129.143 1.00 32.03 ?  178 PHE D CD1   1 
ATOM   14803 C  CD2   . PHE D 2 199 ? 159.165 103.499 129.300 1.00 31.77 ?  178 PHE D CD2   1 
ATOM   14804 C  CE1   . PHE D 2 199 ? 161.879 104.062 129.463 1.00 32.29 ?  178 PHE D CE1   1 
ATOM   14805 C  CE2   . PHE D 2 199 ? 160.083 102.490 129.610 1.00 32.72 ?  178 PHE D CE2   1 
ATOM   14806 C  CZ    . PHE D 2 199 ? 161.440 102.779 129.689 1.00 31.91 ?  178 PHE D CZ    1 
ATOM   14807 N  N     . TYR D 2 200 ? 156.908 108.496 128.950 1.00 26.46 ?  179 TYR D N     1 
ATOM   14808 C  CA    . TYR D 2 200 ? 156.117 109.566 128.322 1.00 27.43 ?  179 TYR D CA    1 
ATOM   14809 C  C     . TYR D 2 200 ? 156.662 110.939 128.699 1.00 27.68 ?  179 TYR D C     1 
ATOM   14810 O  O     . TYR D 2 200 ? 156.731 111.835 127.859 1.00 28.71 ?  179 TYR D O     1 
ATOM   14811 C  CB    . TYR D 2 200 ? 154.673 109.430 128.792 1.00 27.27 ?  179 TYR D CB    1 
ATOM   14812 C  CG    . TYR D 2 200 ? 153.608 110.148 127.999 1.00 28.90 ?  179 TYR D CG    1 
ATOM   14813 C  CD1   . TYR D 2 200 ? 153.554 110.064 126.615 1.00 29.00 ?  179 TYR D CD1   1 
ATOM   14814 C  CD2   . TYR D 2 200 ? 152.603 110.862 128.660 1.00 30.14 ?  179 TYR D CD2   1 
ATOM   14815 C  CE1   . TYR D 2 200 ? 152.548 110.705 125.895 1.00 31.26 ?  179 TYR D CE1   1 
ATOM   14816 C  CE2   . TYR D 2 200 ? 151.591 111.494 127.958 1.00 31.86 ?  179 TYR D CE2   1 
ATOM   14817 C  CZ    . TYR D 2 200 ? 151.570 111.418 126.576 1.00 32.51 ?  179 TYR D CZ    1 
ATOM   14818 O  OH    . TYR D 2 200 ? 150.569 112.049 125.879 1.00 33.77 ?  179 TYR D OH    1 
ATOM   14819 N  N     . GLY D 2 201 ? 157.051 111.096 129.963 1.00 27.68 ?  180 GLY D N     1 
ATOM   14820 C  CA    . GLY D 2 201 ? 157.648 112.337 130.444 1.00 28.02 ?  180 GLY D CA    1 
ATOM   14821 C  C     . GLY D 2 201 ? 159.055 112.622 129.925 1.00 28.60 ?  180 GLY D C     1 
ATOM   14822 O  O     . GLY D 2 201 ? 159.537 113.739 130.057 1.00 28.44 ?  180 GLY D O     1 
ATOM   14823 N  N     . GLN D 2 202 ? 159.706 111.604 129.355 1.00 29.34 ?  181 GLN D N     1 
ATOM   14824 C  CA    . GLN D 2 202 ? 161.061 111.704 128.786 1.00 30.39 ?  181 GLN D CA    1 
ATOM   14825 C  C     . GLN D 2 202 ? 161.076 111.794 127.259 1.00 30.55 ?  181 GLN D C     1 
ATOM   14826 O  O     . GLN D 2 202 ? 162.151 111.896 126.658 1.00 31.23 ?  181 GLN D O     1 
ATOM   14827 C  CB    . GLN D 2 202 ? 161.868 110.444 129.106 1.00 30.31 ?  181 GLN D CB    1 
ATOM   14828 C  CG    . GLN D 2 202 ? 162.248 110.198 130.517 1.00 32.40 ?  181 GLN D CG    1 
ATOM   14829 C  CD    . GLN D 2 202 ? 163.029 108.905 130.632 1.00 33.85 ?  181 GLN D CD    1 
ATOM   14830 O  OE1   . GLN D 2 202 ? 162.515 107.891 131.097 1.00 33.94 ?  181 GLN D OE1   1 
ATOM   14831 N  NE2   . GLN D 2 202 ? 164.265 108.924 130.162 1.00 34.92 ?  181 GLN D NE2   1 
ATOM   14832 N  N     . GLY D 2 203 ? 159.914 111.683 126.627 1.00 30.57 ?  182 GLY D N     1 
ATOM   14833 C  CA    . GLY D 2 203 ? 159.839 111.687 125.165 1.00 30.83 ?  182 GLY D CA    1 
ATOM   14834 C  C     . GLY D 2 203 ? 159.973 110.312 124.529 1.00 30.80 ?  182 GLY D C     1 
ATOM   14835 O  O     . GLY D 2 203 ? 160.129 110.201 123.309 1.00 30.86 ?  182 GLY D O     1 
ATOM   14836 N  N     . LYS D 2 204 ? 159.907 109.264 125.351 1.00 30.14 ?  183 LYS D N     1 
ATOM   14837 C  CA    . LYS D 2 204 ? 159.988 107.884 124.861 1.00 30.35 ?  183 LYS D CA    1 
ATOM   14838 C  C     . LYS D 2 204 ? 158.620 107.205 124.847 1.00 29.52 ?  183 LYS D C     1 
ATOM   14839 O  O     . LYS D 2 204 ? 157.785 107.478 125.707 1.00 28.60 ?  183 LYS D O     1 
ATOM   14840 C  CB    . LYS D 2 204 ? 160.970 107.075 125.706 1.00 30.76 ?  183 LYS D CB    1 
ATOM   14841 C  CG    . LYS D 2 204 ? 162.420 107.552 125.584 1.00 32.95 ?  183 LYS D CG    1 
ATOM   14842 C  CD    . LYS D 2 204 ? 163.269 106.902 126.650 1.00 36.37 ?  183 LYS D CD    1 
ATOM   14843 C  CE    . LYS D 2 204 ? 164.720 107.340 126.573 1.00 38.47 ?  183 LYS D CE    1 
ATOM   14844 N  NZ    . LYS D 2 204 ? 165.421 106.855 127.800 1.00 40.21 1  183 LYS D NZ    1 
ATOM   14845 N  N     . LEU D 2 205 ? 158.407 106.316 123.874 1.00 29.47 ?  184 LEU D N     1 
ATOM   14846 C  CA    . LEU D 2 205 ? 157.141 105.584 123.717 1.00 29.06 ?  184 LEU D CA    1 
ATOM   14847 C  C     . LEU D 2 205 ? 155.919 106.506 123.913 1.00 28.96 ?  184 LEU D C     1 
ATOM   14848 O  O     . LEU D 2 205 ? 155.034 106.247 124.737 1.00 27.68 ?  184 LEU D O     1 
ATOM   14849 C  CB    . LEU D 2 205 ? 157.084 104.369 124.655 1.00 28.63 ?  184 LEU D CB    1 
ATOM   14850 C  CG    . LEU D 2 205 ? 158.212 103.329 124.556 1.00 29.00 ?  184 LEU D CG    1 
ATOM   14851 C  CD1   . LEU D 2 205 ? 158.026 102.242 125.618 1.00 28.90 ?  184 LEU D CD1   1 
ATOM   14852 C  CD2   . LEU D 2 205 ? 158.275 102.704 123.169 1.00 28.67 ?  184 LEU D CD2   1 
ATOM   14853 N  N     . MET D 2 206 ? 155.905 107.580 123.128 1.00 29.02 ?  185 MET D N     1 
ATOM   14854 C  CA    . MET D 2 206 ? 154.902 108.631 123.205 1.00 29.72 ?  185 MET D CA    1 
ATOM   14855 C  C     . MET D 2 206 ? 153.496 108.231 122.768 1.00 29.54 ?  185 MET D C     1 
ATOM   14856 O  O     . MET D 2 206 ? 152.521 108.751 123.306 1.00 29.47 ?  185 MET D O     1 
ATOM   14857 C  CB    . MET D 2 206 ? 155.366 109.849 122.397 1.00 30.69 ?  185 MET D CB    1 
ATOM   14858 C  CG    . MET D 2 206 ? 156.695 110.409 122.881 1.00 32.03 ?  185 MET D CG    1 
ATOM   14859 S  SD    . MET D 2 206 ? 156.611 110.895 124.614 1.00 36.63 ?  185 MET D SD    1 
ATOM   14860 C  CE    . MET D 2 206 ? 155.938 112.540 124.459 1.00 33.80 ?  185 MET D CE    1 
ATOM   14861 N  N     . GLN D 2 207 ? 153.393 107.338 121.785 1.00 29.56 ?  186 GLN D N     1 
ATOM   14862 C  CA    . GLN D 2 207 ? 152.090 106.904 121.270 1.00 29.17 ?  186 GLN D CA    1 
ATOM   14863 C  C     . GLN D 2 207 ? 151.384 106.005 122.280 1.00 28.26 ?  186 GLN D C     1 
ATOM   14864 O  O     . GLN D 2 207 ? 150.210 106.209 122.577 1.00 27.98 ?  186 GLN D O     1 
ATOM   14865 C  CB    . GLN D 2 207 ? 152.229 106.189 119.916 1.00 29.80 ?  186 GLN D CB    1 
ATOM   14866 C  CG    . GLN D 2 207 ? 152.976 106.985 118.848 1.00 31.75 ?  186 GLN D CG    1 
ATOM   14867 C  CD    . GLN D 2 207 ? 152.413 108.382 118.678 1.00 34.93 ?  186 GLN D CD    1 
ATOM   14868 O  OE1   . GLN D 2 207 ? 151.309 108.569 118.150 1.00 36.91 ?  186 GLN D OE1   1 
ATOM   14869 N  NE2   . GLN D 2 207 ? 153.167 109.376 119.135 1.00 36.09 ?  186 GLN D NE2   1 
ATOM   14870 N  N     . SER D 2 208 ? 152.100 105.014 122.808 0.50 27.75 ?  187 SER D N     1 
ATOM   14871 C  CA    . SER D 2 208 ? 151.533 104.134 123.823 0.50 27.12 ?  187 SER D CA    1 
ATOM   14872 C  C     . SER D 2 208 ? 151.333 104.883 125.138 0.50 26.72 ?  187 SER D C     1 
ATOM   14873 O  O     . SER D 2 208 ? 150.397 104.585 125.878 0.50 26.30 ?  187 SER D O     1 
ATOM   14874 C  CB    . SER D 2 208 ? 152.403 102.894 124.033 0.50 26.88 ?  187 SER D CB    1 
ATOM   14875 O  OG    . SER D 2 208 ? 153.744 103.260 124.272 0.50 26.59 ?  187 SER D OG    1 
ATOM   14876 N  N     . GLY D 2 209 ? 152.209 105.849 125.415 1.00 26.64 ?  188 GLY D N     1 
ATOM   14877 C  CA    . GLY D 2 209 ? 152.075 106.717 126.602 1.00 26.43 ?  188 GLY D CA    1 
ATOM   14878 C  C     . GLY D 2 209 ? 150.836 107.602 126.542 1.00 26.66 ?  188 GLY D C     1 
ATOM   14879 O  O     . GLY D 2 209 ? 150.194 107.862 127.560 1.00 26.57 ?  188 GLY D O     1 
ATOM   14880 N  N     . GLU D 2 210 ? 150.500 108.073 125.345 1.00 27.42 ?  189 GLU D N     1 
ATOM   14881 C  CA    . GLU D 2 210 ? 149.270 108.838 125.144 1.00 27.73 ?  189 GLU D CA    1 
ATOM   14882 C  C     . GLU D 2 210 ? 148.050 107.947 125.421 1.00 27.04 ?  189 GLU D C     1 
ATOM   14883 O  O     . GLU D 2 210 ? 147.126 108.350 126.127 1.00 26.57 ?  189 GLU D O     1 
ATOM   14884 C  CB    . GLU D 2 210 ? 149.215 109.442 123.729 1.00 28.28 ?  189 GLU D CB    1 
ATOM   14885 C  CG    . GLU D 2 210 ? 147.989 110.340 123.495 1.00 30.71 ?  189 GLU D CG    1 
ATOM   14886 C  CD    . GLU D 2 210 ? 148.044 111.155 122.205 1.00 35.43 ?  189 GLU D CD    1 
ATOM   14887 O  OE1   . GLU D 2 210 ? 148.954 110.940 121.366 1.00 36.89 ?  189 GLU D OE1   1 
ATOM   14888 O  OE2   . GLU D 2 210 ? 147.164 112.031 122.037 1.00 37.04 -1 189 GLU D OE2   1 
ATOM   14889 N  N     . ILE D 2 211 ? 148.064 106.736 124.873 1.00 26.80 ?  190 ILE D N     1 
ATOM   14890 C  CA    . ILE D 2 211 ? 147.015 105.760 125.150 1.00 26.92 ?  190 ILE D CA    1 
ATOM   14891 C  C     . ILE D 2 211 ? 146.885 105.503 126.645 1.00 26.45 ?  190 ILE D C     1 
ATOM   14892 O  O     . ILE D 2 211 ? 145.777 105.531 127.177 1.00 26.65 ?  190 ILE D O     1 
ATOM   14893 C  CB    . ILE D 2 211 ? 147.226 104.437 124.370 1.00 27.00 ?  190 ILE D CB    1 
ATOM   14894 C  CG1   . ILE D 2 211 ? 146.973 104.677 122.876 1.00 28.77 ?  190 ILE D CG1   1 
ATOM   14895 C  CG2   . ILE D 2 211 ? 146.290 103.336 124.897 1.00 26.82 ?  190 ILE D CG2   1 
ATOM   14896 C  CD1   . ILE D 2 211 ? 147.295 103.494 121.971 1.00 30.88 ?  190 ILE D CD1   1 
ATOM   14897 N  N     . ILE D 2 212 ? 148.010 105.282 127.331 1.00 26.49 ?  191 ILE D N     1 
ATOM   14898 C  CA    . ILE D 2 212 ? 147.974 104.980 128.762 1.00 25.73 ?  191 ILE D CA    1 
ATOM   14899 C  C     . ILE D 2 212 ? 147.395 106.156 129.552 1.00 25.48 ?  191 ILE D C     1 
ATOM   14900 O  O     . ILE D 2 212 ? 146.622 105.962 130.494 1.00 24.95 ?  191 ILE D O     1 
ATOM   14901 C  CB    . ILE D 2 212 ? 149.369 104.562 129.317 1.00 26.44 ?  191 ILE D CB    1 
ATOM   14902 C  CG1   . ILE D 2 212 ? 149.826 103.235 128.697 1.00 26.71 ?  191 ILE D CG1   1 
ATOM   14903 C  CG2   . ILE D 2 212 ? 149.353 104.473 130.859 1.00 26.01 ?  191 ILE D CG2   1 
ATOM   14904 C  CD1   . ILE D 2 212 ? 148.950 102.030 128.987 1.00 30.50 ?  191 ILE D CD1   1 
ATOM   14905 N  N     . ASN D 2 213 ? 147.753 107.370 129.144 1.00 24.79 ?  192 ASN D N     1 
ATOM   14906 C  CA    . ASN D 2 213 ? 147.237 108.570 129.788 1.00 24.80 ?  192 ASN D CA    1 
ATOM   14907 C  C     . ASN D 2 213 ? 145.706 108.702 129.654 1.00 24.44 ?  192 ASN D C     1 
ATOM   14908 O  O     . ASN D 2 213 ? 145.033 109.189 130.570 1.00 23.25 ?  192 ASN D O     1 
ATOM   14909 C  CB    . ASN D 2 213 ? 147.952 109.809 129.244 1.00 25.68 ?  192 ASN D CB    1 
ATOM   14910 C  CG    . ASN D 2 213 ? 148.205 110.854 130.313 1.00 27.89 ?  192 ASN D CG    1 
ATOM   14911 O  OD1   . ASN D 2 213 ? 148.386 110.537 131.485 1.00 31.05 ?  192 ASN D OD1   1 
ATOM   14912 N  ND2   . ASN D 2 213 ? 148.227 112.116 129.905 1.00 31.70 ?  192 ASN D ND2   1 
ATOM   14913 N  N     . LEU D 2 214 ? 145.163 108.255 128.521 1.00 23.60 ?  193 LEU D N     1 
ATOM   14914 C  CA    . LEU D 2 214 ? 143.716 108.291 128.306 1.00 23.84 ?  193 LEU D CA    1 
ATOM   14915 C  C     . LEU D 2 214 ? 143.032 107.247 129.169 1.00 23.48 ?  193 LEU D C     1 
ATOM   14916 O  O     . LEU D 2 214 ? 141.982 107.515 129.760 1.00 24.12 ?  193 LEU D O     1 
ATOM   14917 C  CB    . LEU D 2 214 ? 143.381 108.063 126.832 1.00 23.71 ?  193 LEU D CB    1 
ATOM   14918 C  CG    . LEU D 2 214 ? 143.687 109.239 125.895 1.00 25.29 ?  193 LEU D CG    1 
ATOM   14919 C  CD1   . LEU D 2 214 ? 143.451 108.838 124.438 1.00 25.41 ?  193 LEU D CD1   1 
ATOM   14920 C  CD2   . LEU D 2 214 ? 142.862 110.466 126.246 1.00 25.80 ?  193 LEU D CD2   1 
ATOM   14921 N  N     . ILE D 2 215 ? 143.640 106.063 129.245 1.00 22.89 ?  194 ILE D N     1 
ATOM   14922 C  CA    . ILE D 2 215 ? 143.144 104.987 130.089 1.00 22.25 ?  194 ILE D CA    1 
ATOM   14923 C  C     . ILE D 2 215 ? 143.139 105.454 131.541 1.00 22.55 ?  194 ILE D C     1 
ATOM   14924 O  O     . ILE D 2 215 ? 142.123 105.341 132.242 1.00 22.53 ?  194 ILE D O     1 
ATOM   14925 C  CB    . ILE D 2 215 ? 144.001 103.712 129.957 1.00 22.37 ?  194 ILE D CB    1 
ATOM   14926 C  CG1   . ILE D 2 215 ? 143.858 103.117 128.549 1.00 21.89 ?  194 ILE D CG1   1 
ATOM   14927 C  CG2   . ILE D 2 215 ? 143.628 102.692 131.051 1.00 20.25 ?  194 ILE D CG2   1 
ATOM   14928 C  CD1   . ILE D 2 215 ? 144.685 101.848 128.309 1.00 20.48 ?  194 ILE D CD1   1 
ATOM   14929 N  N     . LEU D 2 216 ? 144.271 105.993 131.983 1.00 22.35 ?  195 LEU D N     1 
ATOM   14930 C  CA    . LEU D 2 216 ? 144.425 106.437 133.365 1.00 22.51 ?  195 LEU D CA    1 
ATOM   14931 C  C     . LEU D 2 216 ? 143.373 107.495 133.708 1.00 22.30 ?  195 LEU D C     1 
ATOM   14932 O  O     . LEU D 2 216 ? 142.794 107.462 134.802 1.00 21.62 ?  195 LEU D O     1 
ATOM   14933 C  CB    . LEU D 2 216 ? 145.846 106.986 133.575 1.00 23.06 ?  195 LEU D CB    1 
ATOM   14934 C  CG    . LEU D 2 216 ? 146.319 107.649 134.877 1.00 23.98 ?  195 LEU D CG    1 
ATOM   14935 C  CD1   . LEU D 2 216 ? 147.824 107.698 134.858 1.00 24.44 ?  195 LEU D CD1   1 
ATOM   14936 C  CD2   . LEU D 2 216 ? 145.757 109.071 135.047 1.00 25.00 ?  195 LEU D CD2   1 
ATOM   14937 N  N     . ARG D 2 217 ? 143.137 108.426 132.777 1.00 21.64 ?  196 ARG D N     1 
ATOM   14938 C  CA    . ARG D 2 217 ? 142.119 109.467 132.960 1.00 22.49 ?  196 ARG D CA    1 
ATOM   14939 C  C     . ARG D 2 217 ? 140.707 108.860 133.148 1.00 21.56 ?  196 ARG D C     1 
ATOM   14940 O  O     . ARG D 2 217 ? 139.938 109.347 133.966 1.00 21.32 ?  196 ARG D O     1 
ATOM   14941 C  CB    . ARG D 2 217 ? 142.144 110.506 131.821 1.00 23.07 ?  196 ARG D CB    1 
ATOM   14942 C  CG    . ARG D 2 217 ? 141.216 111.718 132.053 1.00 25.64 ?  196 ARG D CG    1 
ATOM   14943 C  CD    . ARG D 2 217 ? 141.087 112.626 130.816 1.00 32.11 ?  196 ARG D CD    1 
ATOM   14944 N  NE    . ARG D 2 217 ? 140.566 111.906 129.645 1.00 35.06 ?  196 ARG D NE    1 
ATOM   14945 C  CZ    . ARG D 2 217 ? 140.156 112.483 128.521 1.00 37.65 ?  196 ARG D CZ    1 
ATOM   14946 N  NH1   . ARG D 2 217 ? 140.173 113.806 128.398 1.00 40.20 1  196 ARG D NH1   1 
ATOM   14947 N  NH2   . ARG D 2 217 ? 139.712 111.736 127.514 1.00 38.20 ?  196 ARG D NH2   1 
ATOM   14948 N  N     . ASP D 2 218 ? 140.380 107.804 132.401 1.00 21.34 ?  197 ASP D N     1 
ATOM   14949 C  CA    . ASP D 2 218 ? 139.138 107.052 132.633 1.00 21.09 ?  197 ASP D CA    1 
ATOM   14950 C  C     . ASP D 2 218 ? 139.121 106.382 134.023 1.00 20.65 ?  197 ASP D C     1 
ATOM   14951 O  O     . ASP D 2 218 ? 138.124 106.482 134.743 1.00 20.16 ?  197 ASP D O     1 
ATOM   14952 C  CB    . ASP D 2 218 ? 138.911 105.989 131.547 1.00 21.58 ?  197 ASP D CB    1 
ATOM   14953 C  CG    . ASP D 2 218 ? 138.638 106.589 130.168 1.00 22.60 ?  197 ASP D CG    1 
ATOM   14954 O  OD1   . ASP D 2 218 ? 138.187 107.754 130.073 1.00 24.72 ?  197 ASP D OD1   1 
ATOM   14955 O  OD2   . ASP D 2 218 ? 138.890 105.879 129.167 1.00 22.64 -1 197 ASP D OD2   1 
ATOM   14956 N  N     . GLU D 2 219 ? 140.204 105.703 134.405 1.00 20.59 ?  198 GLU D N     1 
ATOM   14957 C  CA    . GLU D 2 219 ? 140.221 105.007 135.711 1.00 20.66 ?  198 GLU D CA    1 
ATOM   14958 C  C     . GLU D 2 219 ? 140.070 105.987 136.878 1.00 20.45 ?  198 GLU D C     1 
ATOM   14959 O  O     . GLU D 2 219 ? 139.421 105.669 137.879 1.00 20.59 ?  198 GLU D O     1 
ATOM   14960 C  CB    . GLU D 2 219 ? 141.476 104.139 135.902 1.00 20.55 ?  198 GLU D CB    1 
ATOM   14961 C  CG    . GLU D 2 219 ? 141.934 103.305 134.665 1.00 21.99 ?  198 GLU D CG    1 
ATOM   14962 C  CD    . GLU D 2 219 ? 140.916 102.280 134.148 1.00 24.00 ?  198 GLU D CD    1 
ATOM   14963 O  OE1   . GLU D 2 219 ? 139.693 102.422 134.361 1.00 25.06 ?  198 GLU D OE1   1 
ATOM   14964 O  OE2   . GLU D 2 219 ? 141.345 101.322 133.484 1.00 24.49 -1 198 GLU D OE2   1 
ATOM   14965 N  N     . ALA D 2 220 ? 140.652 107.175 136.737 1.00 20.47 ?  199 ALA D N     1 
ATOM   14966 C  CA    . ALA D 2 220 ? 140.511 108.237 137.755 1.00 21.10 ?  199 ALA D CA    1 
ATOM   14967 C  C     . ALA D 2 220 ? 139.050 108.592 138.015 1.00 21.34 ?  199 ALA D C     1 
ATOM   14968 O  O     . ALA D 2 220 ? 138.600 108.542 139.159 1.00 21.19 ?  199 ALA D O     1 
ATOM   14969 C  CB    . ALA D 2 220 ? 141.319 109.481 137.378 1.00 21.09 ?  199 ALA D CB    1 
ATOM   14970 N  N     . ILE D 2 221 ? 138.306 108.918 136.956 1.00 21.31 ?  200 ILE D N     1 
ATOM   14971 C  CA    . ILE D 2 221 ? 136.878 109.188 137.102 1.00 21.80 ?  200 ILE D CA    1 
ATOM   14972 C  C     . ILE D 2 221 ? 136.062 107.961 137.563 1.00 20.90 ?  200 ILE D C     1 
ATOM   14973 O  O     . ILE D 2 221 ? 135.125 108.109 138.347 1.00 20.54 ?  200 ILE D O     1 
ATOM   14974 C  CB    . ILE D 2 221 ? 136.258 109.890 135.860 1.00 22.75 ?  200 ILE D CB    1 
ATOM   14975 C  CG1   . ILE D 2 221 ? 134.915 110.506 136.235 1.00 24.63 ?  200 ILE D CG1   1 
ATOM   14976 C  CG2   . ILE D 2 221 ? 136.069 108.919 134.696 1.00 23.38 ?  200 ILE D CG2   1 
ATOM   14977 C  CD1   . ILE D 2 221 ? 134.474 111.611 135.321 1.00 26.91 ?  200 ILE D CD1   1 
ATOM   14978 N  N     . HIS D 2 222 ? 136.437 106.756 137.119 1.00 20.31 ?  201 HIS D N     1 
ATOM   14979 C  CA    . HIS D 2 222 ? 135.779 105.543 137.611 1.00 20.25 ?  201 HIS D CA    1 
ATOM   14980 C  C     . HIS D 2 222 ? 135.926 105.438 139.127 1.00 20.51 ?  201 HIS D C     1 
ATOM   14981 O  O     . HIS D 2 222 ? 134.940 105.232 139.845 1.00 20.99 ?  201 HIS D O     1 
ATOM   14982 C  CB    . HIS D 2 222 ? 136.328 104.274 136.949 1.00 19.79 ?  201 HIS D CB    1 
ATOM   14983 C  CG    . HIS D 2 222 ? 136.131 104.207 135.466 1.00 19.25 ?  201 HIS D CG    1 
ATOM   14984 N  ND1   . HIS D 2 222 ? 136.700 103.216 134.695 1.00 18.35 ?  201 HIS D ND1   1 
ATOM   14985 C  CD2   . HIS D 2 222 ? 135.445 105.005 134.609 1.00 17.64 ?  201 HIS D CD2   1 
ATOM   14986 C  CE1   . HIS D 2 222 ? 136.364 103.394 133.429 1.00 18.28 ?  201 HIS D CE1   1 
ATOM   14987 N  NE2   . HIS D 2 222 ? 135.610 104.477 133.348 1.00 20.01 ?  201 HIS D NE2   1 
ATOM   14988 N  N     . GLY D 2 223 ? 137.159 105.605 139.611 1.00 20.33 ?  202 GLY D N     1 
ATOM   14989 C  CA    . GLY D 2 223 ? 137.450 105.578 141.051 1.00 19.94 ?  202 GLY D CA    1 
ATOM   14990 C  C     . GLY D 2 223 ? 136.676 106.619 141.851 1.00 19.80 ?  202 GLY D C     1 
ATOM   14991 O  O     . GLY D 2 223 ? 136.123 106.304 142.903 1.00 19.96 ?  202 GLY D O     1 
ATOM   14992 N  N     . VAL D 2 224 ? 136.608 107.852 141.344 1.00 19.49 ?  203 VAL D N     1 
ATOM   14993 C  CA    . VAL D 2 224 ? 135.852 108.920 142.021 1.00 18.88 ?  203 VAL D CA    1 
ATOM   14994 C  C     . VAL D 2 224 ? 134.354 108.595 142.101 1.00 18.55 ?  203 VAL D C     1 
ATOM   14995 O  O     . VAL D 2 224 ? 133.721 108.762 143.156 1.00 17.65 ?  203 VAL D O     1 
ATOM   14996 C  CB    . VAL D 2 224 ? 136.078 110.325 141.352 1.00 19.22 ?  203 VAL D CB    1 
ATOM   14997 C  CG1   . VAL D 2 224 ? 135.250 111.414 142.066 1.00 18.51 ?  203 VAL D CG1   1 
ATOM   14998 C  CG2   . VAL D 2 224 ? 137.573 110.705 141.366 1.00 19.69 ?  203 VAL D CG2   1 
ATOM   14999 N  N     . TYR D 2 225 ? 133.800 108.107 140.993 1.00 18.17 ?  204 TYR D N     1 
ATOM   15000 C  CA    . TYR D 2 225 ? 132.373 107.785 140.911 1.00 18.76 ?  204 TYR D CA    1 
ATOM   15001 C  C     . TYR D 2 225 ? 131.989 106.631 141.853 1.00 18.93 ?  204 TYR D C     1 
ATOM   15002 O  O     . TYR D 2 225 ? 131.063 106.755 142.666 1.00 18.77 ?  204 TYR D O     1 
ATOM   15003 C  CB    . TYR D 2 225 ? 131.956 107.465 139.462 1.00 18.96 ?  204 TYR D CB    1 
ATOM   15004 C  CG    . TYR D 2 225 ? 130.451 107.261 139.336 1.00 20.06 ?  204 TYR D CG    1 
ATOM   15005 C  CD1   . TYR D 2 225 ? 129.568 108.328 139.547 1.00 21.79 ?  204 TYR D CD1   1 
ATOM   15006 C  CD2   . TYR D 2 225 ? 129.912 106.005 139.042 1.00 19.51 ?  204 TYR D CD2   1 
ATOM   15007 C  CE1   . TYR D 2 225 ? 128.186 108.150 139.463 1.00 20.38 ?  204 TYR D CE1   1 
ATOM   15008 C  CE2   . TYR D 2 225 ? 128.514 105.817 138.950 1.00 19.38 ?  204 TYR D CE2   1 
ATOM   15009 C  CZ    . TYR D 2 225 ? 127.668 106.901 139.168 1.00 20.84 ?  204 TYR D CZ    1 
ATOM   15010 O  OH    . TYR D 2 225 ? 126.300 106.753 139.101 1.00 20.77 ?  204 TYR D OH    1 
ATOM   15011 N  N     . VAL D 2 226 ? 132.705 105.512 141.750 1.00 18.76 ?  205 VAL D N     1 
ATOM   15012 C  CA    . VAL D 2 226 ? 132.438 104.376 142.629 1.00 18.85 ?  205 VAL D CA    1 
ATOM   15013 C  C     . VAL D 2 226 ? 132.640 104.787 144.087 1.00 19.19 ?  205 VAL D C     1 
ATOM   15014 O  O     . VAL D 2 226 ? 131.890 104.345 144.960 1.00 19.87 ?  205 VAL D O     1 
ATOM   15015 C  CB    . VAL D 2 226 ? 133.287 103.153 142.260 1.00 19.28 ?  205 VAL D CB    1 
ATOM   15016 C  CG1   . VAL D 2 226 ? 133.034 101.983 143.248 1.00 18.22 ?  205 VAL D CG1   1 
ATOM   15017 C  CG2   . VAL D 2 226 ? 132.963 102.737 140.815 1.00 18.40 ?  205 VAL D CG2   1 
ATOM   15018 N  N     . GLY D 2 227 ? 133.627 105.650 144.333 1.00 18.53 ?  206 GLY D N     1 
ATOM   15019 C  CA    . GLY D 2 227 ? 133.850 106.224 145.674 1.00 18.74 ?  206 GLY D CA    1 
ATOM   15020 C  C     . GLY D 2 227 ? 132.645 106.949 146.249 1.00 19.17 ?  206 GLY D C     1 
ATOM   15021 O  O     . GLY D 2 227 ? 132.342 106.827 147.444 1.00 18.66 ?  206 GLY D O     1 
ATOM   15022 N  N     . LEU D 2 228 ? 131.964 107.722 145.406 1.00 19.00 ?  207 LEU D N     1 
ATOM   15023 C  CA    . LEU D 2 228 ? 130.761 108.436 145.841 1.00 19.73 ?  207 LEU D CA    1 
ATOM   15024 C  C     . LEU D 2 228 ? 129.623 107.457 146.158 1.00 19.76 ?  207 LEU D C     1 
ATOM   15025 O  O     . LEU D 2 228 ? 128.907 107.639 147.142 1.00 20.07 ?  207 LEU D O     1 
ATOM   15026 C  CB    . LEU D 2 228 ? 130.340 109.478 144.802 1.00 19.36 ?  207 LEU D CB    1 
ATOM   15027 C  CG    . LEU D 2 228 ? 131.280 110.687 144.663 1.00 20.50 ?  207 LEU D CG    1 
ATOM   15028 C  CD1   . LEU D 2 228 ? 130.918 111.506 143.438 1.00 19.87 ?  207 LEU D CD1   1 
ATOM   15029 C  CD2   . LEU D 2 228 ? 131.261 111.576 145.940 1.00 22.38 ?  207 LEU D CD2   1 
ATOM   15030 N  N     . LEU D 2 229 ? 129.488 106.401 145.356 1.00 19.27 ?  208 LEU D N     1 
ATOM   15031 C  CA    . LEU D 2 229 ? 128.503 105.341 145.640 1.00 19.47 ?  208 LEU D CA    1 
ATOM   15032 C  C     . LEU D 2 229 ? 128.786 104.603 146.955 1.00 19.67 ?  208 LEU D C     1 
ATOM   15033 O  O     . LEU D 2 229 ? 127.853 104.227 147.676 1.00 19.82 ?  208 LEU D O     1 
ATOM   15034 C  CB    . LEU D 2 229 ? 128.418 104.330 144.477 1.00 19.51 ?  208 LEU D CB    1 
ATOM   15035 C  CG    . LEU D 2 229 ? 127.992 104.816 143.082 1.00 19.48 ?  208 LEU D CG    1 
ATOM   15036 C  CD1   . LEU D 2 229 ? 128.132 103.676 142.056 1.00 20.14 ?  208 LEU D CD1   1 
ATOM   15037 C  CD2   . LEU D 2 229 ? 126.567 105.412 143.055 1.00 19.95 ?  208 LEU D CD2   1 
ATOM   15038 N  N     . ALA D 2 230 ? 130.065 104.387 147.264 1.00 19.43 ?  209 ALA D N     1 
ATOM   15039 C  CA    . ALA D 2 230 ? 130.464 103.782 148.541 1.00 20.29 ?  209 ALA D CA    1 
ATOM   15040 C  C     . ALA D 2 230 ? 130.163 104.694 149.732 1.00 21.17 ?  209 ALA D C     1 
ATOM   15041 O  O     . ALA D 2 230 ? 129.662 104.233 150.753 1.00 21.73 ?  209 ALA D O     1 
ATOM   15042 C  CB    . ALA D 2 230 ? 131.942 103.400 148.517 1.00 19.99 ?  209 ALA D CB    1 
ATOM   15043 N  N     . GLN D 2 231 ? 130.462 105.986 149.598 1.00 22.26 ?  210 GLN D N     1 
ATOM   15044 C  CA    . GLN D 2 231 ? 130.161 106.969 150.656 1.00 23.33 ?  210 GLN D CA    1 
ATOM   15045 C  C     . GLN D 2 231 ? 128.660 107.051 150.954 1.00 23.85 ?  210 GLN D C     1 
ATOM   15046 O  O     . GLN D 2 231 ? 128.264 107.212 152.105 1.00 24.91 ?  210 GLN D O     1 
ATOM   15047 C  CB    . GLN D 2 231 ? 130.681 108.361 150.286 1.00 23.49 ?  210 GLN D CB    1 
ATOM   15048 C  CG    . GLN D 2 231 ? 132.205 108.492 150.202 1.00 23.05 ?  210 GLN D CG    1 
ATOM   15049 C  CD    . GLN D 2 231 ? 132.635 109.902 149.802 1.00 24.65 ?  210 GLN D CD    1 
ATOM   15050 O  OE1   . GLN D 2 231 ? 132.198 110.880 150.408 1.00 25.85 ?  210 GLN D OE1   1 
ATOM   15051 N  NE2   . GLN D 2 231 ? 133.477 110.012 148.774 1.00 22.30 ?  210 GLN D NE2   1 
ATOM   15052 N  N     . GLU D 2 232 ? 127.835 106.960 149.915 1.00 24.36 ?  211 GLU D N     1 
ATOM   15053 C  CA    . GLU D 2 232 ? 126.385 106.897 150.085 1.00 24.83 ?  211 GLU D CA    1 
ATOM   15054 C  C     . GLU D 2 232 ? 125.966 105.747 151.007 1.00 24.34 ?  211 GLU D C     1 
ATOM   15055 O  O     . GLU D 2 232 ? 125.142 105.943 151.902 1.00 24.20 ?  211 GLU D O     1 
ATOM   15056 C  CB    . GLU D 2 232 ? 125.691 106.761 148.735 1.00 25.15 ?  211 GLU D CB    1 
ATOM   15057 C  CG    . GLU D 2 232 ? 124.198 106.952 148.792 1.00 28.55 ?  211 GLU D CG    1 
ATOM   15058 C  CD    . GLU D 2 232 ? 123.577 106.830 147.428 1.00 33.83 ?  211 GLU D CD    1 
ATOM   15059 O  OE1   . GLU D 2 232 ? 123.434 107.874 146.758 1.00 35.09 ?  211 GLU D OE1   1 
ATOM   15060 O  OE2   . GLU D 2 232 ? 123.274 105.691 147.009 1.00 35.51 -1 211 GLU D OE2   1 
ATOM   15061 N  N     . ILE D 2 233 ? 126.533 104.560 150.796 1.00 23.39 ?  212 ILE D N     1 
ATOM   15062 C  CA    . ILE D 2 233 ? 126.257 103.411 151.676 1.00 23.42 ?  212 ILE D CA    1 
ATOM   15063 C  C     . ILE D 2 233 ? 126.806 103.656 153.083 1.00 23.74 ?  212 ILE D C     1 
ATOM   15064 O  O     . ILE D 2 233 ? 126.099 103.476 154.074 1.00 24.61 ?  212 ILE D O     1 
ATOM   15065 C  CB    . ILE D 2 233 ? 126.797 102.076 151.095 1.00 22.81 ?  212 ILE D CB    1 
ATOM   15066 C  CG1   . ILE D 2 233 ? 126.042 101.709 149.808 1.00 22.94 ?  212 ILE D CG1   1 
ATOM   15067 C  CG2   . ILE D 2 233 ? 126.663 100.938 152.116 1.00 22.45 ?  212 ILE D CG2   1 
ATOM   15068 C  CD1   . ILE D 2 233 ? 126.726 100.605 148.972 1.00 22.21 ?  212 ILE D CD1   1 
ATOM   15069 N  N     . TYR D 2 234 ? 128.063 104.085 153.162 1.00 24.19 ?  213 TYR D N     1 
ATOM   15070 C  CA    . TYR D 2 234 ? 128.726 104.372 154.426 1.00 24.59 ?  213 TYR D CA    1 
ATOM   15071 C  C     . TYR D 2 234 ? 127.903 105.332 155.293 1.00 25.15 ?  213 TYR D C     1 
ATOM   15072 O  O     . TYR D 2 234 ? 127.775 105.119 156.501 1.00 24.94 ?  213 TYR D O     1 
ATOM   15073 C  CB    . TYR D 2 234 ? 130.112 104.965 154.158 1.00 24.41 ?  213 TYR D CB    1 
ATOM   15074 C  CG    . TYR D 2 234 ? 130.909 105.327 155.394 1.00 25.93 ?  213 TYR D CG    1 
ATOM   15075 C  CD1   . TYR D 2 234 ? 131.684 104.375 156.046 1.00 24.70 ?  213 TYR D CD1   1 
ATOM   15076 C  CD2   . TYR D 2 234 ? 130.892 106.633 155.903 1.00 26.11 ?  213 TYR D CD2   1 
ATOM   15077 C  CE1   . TYR D 2 234 ? 132.424 104.703 157.178 1.00 27.90 ?  213 TYR D CE1   1 
ATOM   15078 C  CE2   . TYR D 2 234 ? 131.632 106.969 157.029 1.00 27.70 ?  213 TYR D CE2   1 
ATOM   15079 C  CZ    . TYR D 2 234 ? 132.396 106.003 157.659 1.00 27.89 ?  213 TYR D CZ    1 
ATOM   15080 O  OH    . TYR D 2 234 ? 133.129 106.329 158.776 1.00 32.34 ?  213 TYR D OH    1 
ATOM   15081 N  N     . ASN D 2 235 ? 127.361 106.378 154.667 1.00 25.43 ?  214 ASN D N     1 
ATOM   15082 C  CA    . ASN D 2 235 ? 126.598 107.416 155.381 1.00 26.77 ?  214 ASN D CA    1 
ATOM   15083 C  C     . ASN D 2 235 ? 125.230 106.955 155.880 1.00 27.06 ?  214 ASN D C     1 
ATOM   15084 O  O     . ASN D 2 235 ? 124.593 107.638 156.676 1.00 27.42 ?  214 ASN D O     1 
ATOM   15085 C  CB    . ASN D 2 235 ? 126.412 108.662 154.511 1.00 26.80 ?  214 ASN D CB    1 
ATOM   15086 C  CG    . ASN D 2 235 ? 127.713 109.336 154.169 1.00 28.19 ?  214 ASN D CG    1 
ATOM   15087 O  OD1   . ASN D 2 235 ? 128.653 109.351 154.962 1.00 29.35 ?  214 ASN D OD1   1 
ATOM   15088 N  ND2   . ASN D 2 235 ? 127.773 109.912 152.980 1.00 30.84 ?  214 ASN D ND2   1 
ATOM   15089 N  N     . LYS D 2 236 ? 124.783 105.801 155.408 1.00 26.87 ?  215 LYS D N     1 
ATOM   15090 C  CA    . LYS D 2 236 ? 123.519 105.234 155.860 1.00 27.86 ?  215 LYS D CA    1 
ATOM   15091 C  C     . LYS D 2 236 ? 123.707 104.357 157.106 1.00 28.07 ?  215 LYS D C     1 
ATOM   15092 O  O     . LYS D 2 236 ? 122.737 103.837 157.655 1.00 28.22 ?  215 LYS D O     1 
ATOM   15093 C  CB    . LYS D 2 236 ? 122.859 104.434 154.736 1.00 27.52 ?  215 LYS D CB    1 
ATOM   15094 C  CG    . LYS D 2 236 ? 122.447 105.264 153.544 1.00 29.60 ?  215 LYS D CG    1 
ATOM   15095 C  CD    . LYS D 2 236 ? 121.303 104.620 152.777 1.00 34.24 ?  215 LYS D CD    1 
ATOM   15096 C  CE    . LYS D 2 236 ? 121.756 103.863 151.544 1.00 36.75 ?  215 LYS D CE    1 
ATOM   15097 N  NZ    . LYS D 2 236 ? 122.583 102.688 151.893 1.00 40.41 1  215 LYS D NZ    1 
ATOM   15098 N  N     . GLN D 2 237 ? 124.953 104.207 157.550 1.00 28.33 ?  216 GLN D N     1 
ATOM   15099 C  CA    . GLN D 2 237 ? 125.274 103.285 158.642 1.00 29.60 ?  216 GLN D CA    1 
ATOM   15100 C  C     . GLN D 2 237 ? 125.330 103.977 159.999 1.00 30.69 ?  216 GLN D C     1 
ATOM   15101 O  O     . GLN D 2 237 ? 125.515 105.196 160.078 1.00 30.85 ?  216 GLN D O     1 
ATOM   15102 C  CB    . GLN D 2 237 ? 126.611 102.560 158.381 1.00 29.08 ?  216 GLN D CB    1 
ATOM   15103 C  CG    . GLN D 2 237 ? 126.731 101.858 157.025 1.00 27.78 ?  216 GLN D CG    1 
ATOM   15104 C  CD    . GLN D 2 237 ? 125.546 100.961 156.702 1.00 28.38 ?  216 GLN D CD    1 
ATOM   15105 O  OE1   . GLN D 2 237 ? 125.150 100.120 157.507 1.00 29.30 ?  216 GLN D OE1   1 
ATOM   15106 N  NE2   . GLN D 2 237 ? 124.982 101.132 155.510 1.00 26.88 ?  216 GLN D NE2   1 
ATOM   15107 N  N     . THR D 2 238 ? 125.184 103.185 161.061 1.00 32.02 ?  217 THR D N     1 
ATOM   15108 C  CA    . THR D 2 238 ? 125.381 103.667 162.431 1.00 33.47 ?  217 THR D CA    1 
ATOM   15109 C  C     . THR D 2 238 ? 126.843 104.055 162.675 1.00 34.29 ?  217 THR D C     1 
ATOM   15110 O  O     . THR D 2 238 ? 127.728 103.766 161.852 1.00 33.78 ?  217 THR D O     1 
ATOM   15111 C  CB    . THR D 2 238 ? 124.964 102.594 163.476 1.00 34.00 ?  217 THR D CB    1 
ATOM   15112 O  OG1   . THR D 2 238 ? 125.841 101.461 163.382 1.00 34.33 ?  217 THR D OG1   1 
ATOM   15113 C  CG2   . THR D 2 238 ? 123.513 102.138 163.248 1.00 33.53 ?  217 THR D CG2   1 
ATOM   15114 N  N     . GLU D 2 239 ? 127.105 104.697 163.809 1.00 35.45 ?  218 GLU D N     1 
ATOM   15115 C  CA    . GLU D 2 239 ? 128.468 105.095 164.147 1.00 36.37 ?  218 GLU D CA    1 
ATOM   15116 C  C     . GLU D 2 239 ? 129.385 103.898 164.391 1.00 36.29 ?  218 GLU D C     1 
ATOM   15117 O  O     . GLU D 2 239 ? 130.545 103.910 163.969 1.00 36.18 ?  218 GLU D O     1 
ATOM   15118 C  CB    . GLU D 2 239 ? 128.488 106.067 165.330 1.00 37.27 ?  218 GLU D CB    1 
ATOM   15119 C  CG    . GLU D 2 239 ? 127.913 107.455 164.992 1.00 39.45 ?  218 GLU D CG    1 
ATOM   15120 C  CD    . GLU D 2 239 ? 128.611 108.128 163.812 1.00 41.22 ?  218 GLU D CD    1 
ATOM   15121 O  OE1   . GLU D 2 239 ? 129.861 108.136 163.768 1.00 42.62 ?  218 GLU D OE1   1 
ATOM   15122 O  OE2   . GLU D 2 239 ? 127.906 108.652 162.923 1.00 41.24 -1 218 GLU D OE2   1 
ATOM   15123 N  N     . GLU D 2 240 ? 128.862 102.865 165.049 1.00 36.66 ?  219 GLU D N     1 
ATOM   15124 C  CA    . GLU D 2 240 ? 129.639 101.648 165.297 1.00 37.01 ?  219 GLU D CA    1 
ATOM   15125 C  C     . GLU D 2 240 ? 129.941 100.915 163.990 1.00 35.85 ?  219 GLU D C     1 
ATOM   15126 O  O     . GLU D 2 240 ? 131.059 100.432 163.794 1.00 35.62 ?  219 GLU D O     1 
ATOM   15127 C  CB    . GLU D 2 240 ? 128.927 100.710 166.283 1.00 37.98 ?  219 GLU D CB    1 
ATOM   15128 C  CG    . GLU D 2 240 ? 129.761 99.472  166.648 1.00 40.87 ?  219 GLU D CG    1 
ATOM   15129 C  CD    . GLU D 2 240 ? 129.074 98.512  167.617 1.00 44.58 ?  219 GLU D CD    1 
ATOM   15130 O  OE1   . GLU D 2 240 ? 129.806 97.788  168.335 1.00 45.86 ?  219 GLU D OE1   1 
ATOM   15131 O  OE2   . GLU D 2 240 ? 127.820 98.472  167.662 1.00 45.75 -1 219 GLU D OE2   1 
ATOM   15132 N  N     . LYS D 2 241 ? 128.939 100.838 163.113 1.00 34.54 ?  220 LYS D N     1 
ATOM   15133 C  CA    . LYS D 2 241 ? 129.093 100.194 161.807 1.00 33.65 ?  220 LYS D CA    1 
ATOM   15134 C  C     . LYS D 2 241 ? 130.076 100.972 160.922 1.00 32.67 ?  220 LYS D C     1 
ATOM   15135 O  O     . LYS D 2 241 ? 130.864 100.364 160.203 1.00 32.05 ?  220 LYS D O     1 
ATOM   15136 C  CB    . LYS D 2 241 ? 127.737 100.026 161.113 1.00 33.30 ?  220 LYS D CB    1 
ATOM   15137 C  CG    . LYS D 2 241 ? 127.758 99.218  159.801 1.00 34.50 ?  220 LYS D CG    1 
ATOM   15138 C  CD    . LYS D 2 241 ? 128.255 97.779  159.989 1.00 36.30 ?  220 LYS D CD    1 
ATOM   15139 C  CE    . LYS D 2 241 ? 127.244 96.924  160.744 1.00 38.44 ?  220 LYS D CE    1 
ATOM   15140 N  NZ    . LYS D 2 241 ? 127.903 95.760  161.394 1.00 39.28 1  220 LYS D NZ    1 
ATOM   15141 N  N     . LYS D 2 242 ? 130.023 102.306 160.988 1.00 31.90 ?  221 LYS D N     1 
ATOM   15142 C  CA    . LYS D 2 242 ? 130.975 103.160 160.278 1.00 31.28 ?  221 LYS D CA    1 
ATOM   15143 C  C     . LYS D 2 242 ? 132.413 102.874 160.708 1.00 31.32 ?  221 LYS D C     1 
ATOM   15144 O  O     . LYS D 2 242 ? 133.275 102.671 159.863 1.00 30.72 ?  221 LYS D O     1 
ATOM   15145 C  CB    . LYS D 2 242 ? 130.659 104.649 160.482 1.00 31.38 ?  221 LYS D CB    1 
ATOM   15146 C  CG    . LYS D 2 242 ? 129.566 105.200 159.572 1.00 30.64 ?  221 LYS D CG    1 
ATOM   15147 C  CD    . LYS D 2 242 ? 129.341 106.685 159.853 1.00 32.51 ?  221 LYS D CD    1 
ATOM   15148 C  CE    . LYS D 2 242 ? 128.282 107.259 158.939 1.00 32.66 ?  221 LYS D CE    1 
ATOM   15149 N  NZ    . LYS D 2 242 ? 127.895 108.622 159.369 1.00 35.31 1  221 LYS D NZ    1 
ATOM   15150 N  N     . ALA D 2 243 ? 132.660 102.867 162.022 1.00 31.62 ?  222 ALA D N     1 
ATOM   15151 C  CA    . ALA D 2 243 ? 133.987 102.564 162.569 1.00 31.66 ?  222 ALA D CA    1 
ATOM   15152 C  C     . ALA D 2 243 ? 134.501 101.196 162.101 1.00 31.52 ?  222 ALA D C     1 
ATOM   15153 O  O     . ALA D 2 243 ? 135.696 101.020 161.849 1.00 31.41 ?  222 ALA D O     1 
ATOM   15154 C  CB    . ALA D 2 243 ? 133.968 102.647 164.099 1.00 31.89 ?  222 ALA D CB    1 
ATOM   15155 N  N     . GLU D 2 244 ? 133.576 100.249 161.971 1.00 31.35 ?  223 GLU D N     1 
ATOM   15156 C  CA    . GLU D 2 244 ? 133.860 98.897  161.520 1.00 31.54 ?  223 GLU D CA    1 
ATOM   15157 C  C     . GLU D 2 244 ? 134.214 98.858  160.016 1.00 30.63 ?  223 GLU D C     1 
ATOM   15158 O  O     . GLU D 2 244 ? 135.123 98.130  159.591 1.00 29.47 ?  223 GLU D O     1 
ATOM   15159 C  CB    . GLU D 2 244 ? 132.633 98.049  161.815 1.00 32.45 ?  223 GLU D CB    1 
ATOM   15160 C  CG    . GLU D 2 244 ? 132.797 96.563  161.720 1.00 35.31 ?  223 GLU D CG    1 
ATOM   15161 C  CD    . GLU D 2 244 ? 131.617 95.846  162.344 1.00 38.36 ?  223 GLU D CD    1 
ATOM   15162 O  OE1   . GLU D 2 244 ? 131.463 95.914  163.581 1.00 41.93 ?  223 GLU D OE1   1 
ATOM   15163 O  OE2   . GLU D 2 244 ? 130.833 95.223  161.601 1.00 39.37 -1 223 GLU D OE2   1 
ATOM   15164 N  N     . LEU D 2 245 ? 133.495 99.649  159.227 1.00 29.62 ?  224 LEU D N     1 
ATOM   15165 C  CA    . LEU D 2 245 ? 133.785 99.800  157.804 1.00 29.44 ?  224 LEU D CA    1 
ATOM   15166 C  C     . LEU D 2 245 ? 135.100 100.541 157.551 1.00 28.99 ?  224 LEU D C     1 
ATOM   15167 O  O     . LEU D 2 245 ? 135.807 100.221 156.600 1.00 28.63 ?  224 LEU D O     1 
ATOM   15168 C  CB    . LEU D 2 245 ? 132.622 100.494 157.086 1.00 29.06 ?  224 LEU D CB    1 
ATOM   15169 C  CG    . LEU D 2 245 ? 131.312 99.706  156.987 1.00 29.27 ?  224 LEU D CG    1 
ATOM   15170 C  CD1   . LEU D 2 245 ? 130.289 100.520 156.201 1.00 30.76 ?  224 LEU D CD1   1 
ATOM   15171 C  CD2   . LEU D 2 245 ? 131.512 98.343  156.332 1.00 28.11 ?  224 LEU D CD2   1 
ATOM   15172 N  N     . ARG D 2 246 ? 135.419 101.521 158.398 1.00 29.31 ?  225 ARG D N     1 
ATOM   15173 C  CA    . ARG D 2 246 ? 136.712 102.210 158.329 1.00 29.86 ?  225 ARG D CA    1 
ATOM   15174 C  C     . ARG D 2 246 ? 137.859 101.250 158.608 1.00 29.23 ?  225 ARG D C     1 
ATOM   15175 O  O     . ARG D 2 246 ? 138.864 101.265 157.910 1.00 28.95 ?  225 ARG D O     1 
ATOM   15176 C  CB    . ARG D 2 246 ? 136.799 103.376 159.321 1.00 30.56 ?  225 ARG D CB    1 
ATOM   15177 C  CG    . ARG D 2 246 ? 136.048 104.619 158.903 1.00 33.71 ?  225 ARG D CG    1 
ATOM   15178 C  CD    . ARG D 2 246 ? 136.581 105.886 159.598 1.00 37.42 ?  225 ARG D CD    1 
ATOM   15179 N  NE    . ARG D 2 246 ? 136.583 105.795 161.063 1.00 39.17 ?  225 ARG D NE    1 
ATOM   15180 C  CZ    . ARG D 2 246 ? 135.515 105.946 161.848 1.00 40.68 ?  225 ARG D CZ    1 
ATOM   15181 N  NH1   . ARG D 2 246 ? 134.313 106.188 161.332 1.00 40.28 1  225 ARG D NH1   1 
ATOM   15182 N  NH2   . ARG D 2 246 ? 135.651 105.842 163.166 1.00 41.65 ?  225 ARG D NH2   1 
ATOM   15183 N  N     . GLU D 2 247 ? 137.706 100.431 159.641 1.00 28.89 ?  226 GLU D N     1 
ATOM   15184 C  CA    . GLU D 2 247 ? 138.709 99.424  159.974 1.00 29.27 ?  226 GLU D CA    1 
ATOM   15185 C  C     . GLU D 2 247 ? 138.897 98.445  158.816 1.00 27.84 ?  226 GLU D C     1 
ATOM   15186 O  O     . GLU D 2 247 ? 140.036 98.106  158.482 1.00 27.37 ?  226 GLU D O     1 
ATOM   15187 C  CB    . GLU D 2 247 ? 138.355 98.687  161.277 1.00 30.21 ?  226 GLU D CB    1 
ATOM   15188 C  CG    . GLU D 2 247 ? 139.298 97.524  161.641 1.00 34.46 ?  226 GLU D CG    1 
ATOM   15189 C  CD    . GLU D 2 247 ? 140.751 97.963  161.812 1.00 40.77 ?  226 GLU D CD    1 
ATOM   15190 O  OE1   . GLU D 2 247 ? 141.024 98.772  162.730 1.00 44.03 ?  226 GLU D OE1   1 
ATOM   15191 O  OE2   . GLU D 2 247 ? 141.622 97.503  161.031 1.00 42.98 -1 226 GLU D OE2   1 
ATOM   15192 N  N     . PHE D 2 248 ? 137.792 98.009  158.205 1.00 26.73 ?  227 PHE D N     1 
ATOM   15193 C  CA    . PHE D 2 248 ? 137.850 97.156  157.011 1.00 26.15 ?  227 PHE D CA    1 
ATOM   15194 C  C     . PHE D 2 248 ? 138.685 97.797  155.899 1.00 25.33 ?  227 PHE D C     1 
ATOM   15195 O  O     . PHE D 2 248 ? 139.562 97.149  155.335 1.00 24.70 ?  227 PHE D O     1 
ATOM   15196 C  CB    . PHE D 2 248 ? 136.458 96.804  156.450 1.00 26.02 ?  227 PHE D CB    1 
ATOM   15197 C  CG    . PHE D 2 248 ? 136.501 96.254  155.024 1.00 25.61 ?  227 PHE D CG    1 
ATOM   15198 C  CD1   . PHE D 2 248 ? 136.715 94.899  154.792 1.00 26.51 ?  227 PHE D CD1   1 
ATOM   15199 C  CD2   . PHE D 2 248 ? 136.366 97.106  153.924 1.00 26.21 ?  227 PHE D CD2   1 
ATOM   15200 C  CE1   . PHE D 2 248 ? 136.781 94.390  153.495 1.00 26.16 ?  227 PHE D CE1   1 
ATOM   15201 C  CE2   . PHE D 2 248 ? 136.434 96.609  152.615 1.00 26.07 ?  227 PHE D CE2   1 
ATOM   15202 C  CZ    . PHE D 2 248 ? 136.645 95.243  152.405 1.00 25.82 ?  227 PHE D CZ    1 
ATOM   15203 N  N     . ALA D 2 249 ? 138.386 99.060  155.587 1.00 24.83 ?  228 ALA D N     1 
ATOM   15204 C  CA    . ALA D 2 249 ? 139.043 99.784  154.491 1.00 24.08 ?  228 ALA D CA    1 
ATOM   15205 C  C     . ALA D 2 249 ? 140.549 99.957  154.737 1.00 23.93 ?  228 ALA D C     1 
ATOM   15206 O  O     . ALA D 2 249 ? 141.359 99.764  153.829 1.00 22.51 ?  228 ALA D O     1 
ATOM   15207 C  CB    . ALA D 2 249 ? 138.379 101.152 154.294 1.00 24.18 ?  228 ALA D CB    1 
ATOM   15208 N  N     . ILE D 2 250 ? 140.910 100.327 155.966 1.00 24.20 ?  229 ILE D N     1 
ATOM   15209 C  CA    . ILE D 2 250 ? 142.314 100.529 156.329 1.00 24.86 ?  229 ILE D CA    1 
ATOM   15210 C  C     . ILE D 2 250 ? 143.073 99.197  156.340 1.00 24.68 ?  229 ILE D C     1 
ATOM   15211 O  O     . ILE D 2 250 ? 144.197 99.121  155.857 1.00 24.30 ?  229 ILE D O     1 
ATOM   15212 C  CB    . ILE D 2 250 ? 142.469 101.294 157.690 1.00 25.44 ?  229 ILE D CB    1 
ATOM   15213 C  CG1   . ILE D 2 250 ? 141.787 102.675 157.650 1.00 26.49 ?  229 ILE D CG1   1 
ATOM   15214 C  CG2   . ILE D 2 250 ? 143.943 101.432 158.098 1.00 27.13 ?  229 ILE D CG2   1 
ATOM   15215 C  CD1   . ILE D 2 250 ? 142.204 103.589 156.496 1.00 28.58 ?  229 ILE D CD1   1 
ATOM   15216 N  N     . ASP D 2 251 ? 142.451 98.153  156.889 1.00 24.90 ?  230 ASP D N     1 
ATOM   15217 C  CA    . ASP D 2 251 ? 143.042 96.819  156.912 1.00 25.04 ?  230 ASP D CA    1 
ATOM   15218 C  C     . ASP D 2 251 ? 143.294 96.305  155.483 1.00 24.25 ?  230 ASP D C     1 
ATOM   15219 O  O     . ASP D 2 251 ? 144.377 95.800  155.181 1.00 23.60 ?  230 ASP D O     1 
ATOM   15220 C  CB    . ASP D 2 251 ? 142.131 95.861  157.686 1.00 26.23 ?  230 ASP D CB    1 
ATOM   15221 C  CG    . ASP D 2 251 ? 142.610 94.426  157.645 1.00 28.91 ?  230 ASP D CG    1 
ATOM   15222 O  OD1   . ASP D 2 251 ? 143.664 94.116  158.238 1.00 32.03 ?  230 ASP D OD1   1 
ATOM   15223 O  OD2   . ASP D 2 251 ? 141.909 93.596  157.034 1.00 33.16 -1 230 ASP D OD2   1 
ATOM   15224 N  N     . LEU D 2 252 ? 142.289 96.433  154.620 1.00 23.43 ?  231 LEU D N     1 
ATOM   15225 C  CA    . LEU D 2 252 ? 142.435 96.062  153.215 1.00 22.79 ?  231 LEU D CA    1 
ATOM   15226 C  C     . LEU D 2 252 ? 143.553 96.866  152.544 1.00 22.71 ?  231 LEU D C     1 
ATOM   15227 O  O     . LEU D 2 252 ? 144.386 96.302  151.824 1.00 21.58 ?  231 LEU D O     1 
ATOM   15228 C  CB    . LEU D 2 252 ? 141.119 96.257  152.453 1.00 22.48 ?  231 LEU D CB    1 
ATOM   15229 C  CG    . LEU D 2 252 ? 141.157 95.891  150.957 1.00 21.05 ?  231 LEU D CG    1 
ATOM   15230 C  CD1   . LEU D 2 252 ? 141.580 94.423  150.733 1.00 22.94 ?  231 LEU D CD1   1 
ATOM   15231 C  CD2   . LEU D 2 252 ? 139.808 96.147  150.299 1.00 19.31 ?  231 LEU D CD2   1 
ATOM   15232 N  N     . LEU D 2 253 ? 143.562 98.179  152.779 1.00 22.90 ?  232 LEU D N     1 
ATOM   15233 C  CA    . LEU D 2 253 ? 144.603 99.040  152.198 1.00 23.78 ?  232 LEU D CA    1 
ATOM   15234 C  C     . LEU D 2 253 ? 146.001 98.569  152.614 1.00 23.75 ?  232 LEU D C     1 
ATOM   15235 O  O     . LEU D 2 253 ? 146.902 98.477  151.779 1.00 23.26 ?  232 LEU D O     1 
ATOM   15236 C  CB    . LEU D 2 253 ? 144.413 100.502 152.609 1.00 24.03 ?  232 LEU D CB    1 
ATOM   15237 C  CG    . LEU D 2 253 ? 145.585 101.428 152.239 1.00 26.46 ?  232 LEU D CG    1 
ATOM   15238 C  CD1   . LEU D 2 253 ? 145.610 101.664 150.748 1.00 26.52 ?  232 LEU D CD1   1 
ATOM   15239 C  CD2   . LEU D 2 253 ? 145.514 102.764 152.985 1.00 27.50 ?  232 LEU D CD2   1 
ATOM   15240 N  N     . ASN D 2 254 ? 146.170 98.301  153.910 1.00 24.63 ?  233 ASN D N     1 
ATOM   15241 C  CA    . ASN D 2 254 ? 147.431 97.779  154.443 1.00 25.49 ?  233 ASN D CA    1 
ATOM   15242 C  C     . ASN D 2 254 ? 147.900 96.483  153.767 1.00 24.94 ?  233 ASN D C     1 
ATOM   15243 O  O     . ASN D 2 254 ? 149.081 96.359  153.433 1.00 24.64 ?  233 ASN D O     1 
ATOM   15244 C  CB    . ASN D 2 254 ? 147.335 97.560  155.951 1.00 26.98 ?  233 ASN D CB    1 
ATOM   15245 C  CG    . ASN D 2 254 ? 147.648 98.811  156.741 1.00 29.94 ?  233 ASN D CG    1 
ATOM   15246 O  OD1   . ASN D 2 254 ? 148.565 99.570  156.402 1.00 34.55 ?  233 ASN D OD1   1 
ATOM   15247 N  ND2   . ASN D 2 254 ? 146.896 99.032  157.811 1.00 33.81 ?  233 ASN D ND2   1 
ATOM   15248 N  N     . GLN D 2 255 ? 146.986 95.530  153.582 1.00 24.08 ?  234 GLN D N     1 
ATOM   15249 C  CA    . GLN D 2 255 ? 147.331 94.260  152.938 1.00 24.35 ?  234 GLN D CA    1 
ATOM   15250 C  C     . GLN D 2 255 ? 147.797 94.507  151.515 1.00 23.26 ?  234 GLN D C     1 
ATOM   15251 O  O     . GLN D 2 255 ? 148.837 93.981  151.106 1.00 23.12 ?  234 GLN D O     1 
ATOM   15252 C  CB    . GLN D 2 255 ? 146.147 93.285  152.901 1.00 24.84 ?  234 GLN D CB    1 
ATOM   15253 C  CG    . GLN D 2 255 ? 145.763 92.660  154.224 1.00 27.45 ?  234 GLN D CG    1 
ATOM   15254 C  CD    . GLN D 2 255 ? 146.914 91.934  154.898 1.00 32.02 ?  234 GLN D CD    1 
ATOM   15255 O  OE1   . GLN D 2 255 ? 147.317 92.301  156.000 1.00 35.80 ?  234 GLN D OE1   1 
ATOM   15256 N  NE2   . GLN D 2 255 ? 147.446 90.899  154.244 1.00 32.12 ?  234 GLN D NE2   1 
ATOM   15257 N  N     . LEU D 2 256 ? 147.028 95.308  150.776 1.00 21.77 ?  235 LEU D N     1 
ATOM   15258 C  CA    . LEU D 2 256 ? 147.352 95.619  149.381 1.00 21.68 ?  235 LEU D CA    1 
ATOM   15259 C  C     . LEU D 2 256 ? 148.651 96.413  149.286 1.00 21.49 ?  235 LEU D C     1 
ATOM   15260 O  O     . LEU D 2 256 ? 149.470 96.158  148.409 1.00 20.89 ?  235 LEU D O     1 
ATOM   15261 C  CB    . LEU D 2 256 ? 146.213 96.395  148.691 1.00 20.49 ?  235 LEU D CB    1 
ATOM   15262 C  CG    . LEU D 2 256 ? 144.905 95.630  148.448 1.00 21.52 ?  235 LEU D CG    1 
ATOM   15263 C  CD1   . LEU D 2 256 ? 143.779 96.561  147.965 1.00 20.71 ?  235 LEU D CD1   1 
ATOM   15264 C  CD2   . LEU D 2 256 ? 145.095 94.489  147.458 1.00 20.74 ?  235 LEU D CD2   1 
ATOM   15265 N  N     . TYR D 2 257 ? 148.830 97.369  150.196 1.00 21.42 ?  236 TYR D N     1 
ATOM   15266 C  CA    . TYR D 2 257 ? 150.035 98.197  150.190 1.00 22.02 ?  236 TYR D CA    1 
ATOM   15267 C  C     . TYR D 2 257 ? 151.308 97.382  150.423 1.00 22.61 ?  236 TYR D C     1 
ATOM   15268 O  O     . TYR D 2 257 ? 152.311 97.583  149.737 1.00 22.19 ?  236 TYR D O     1 
ATOM   15269 C  CB    . TYR D 2 257 ? 149.926 99.336  151.199 1.00 22.06 ?  236 TYR D CB    1 
ATOM   15270 C  CG    . TYR D 2 257 ? 151.199 100.136 151.360 1.00 23.44 ?  236 TYR D CG    1 
ATOM   15271 C  CD1   . TYR D 2 257 ? 151.690 100.928 150.316 1.00 24.01 ?  236 TYR D CD1   1 
ATOM   15272 C  CD2   . TYR D 2 257 ? 151.906 100.108 152.560 1.00 25.22 ?  236 TYR D CD2   1 
ATOM   15273 C  CE1   . TYR D 2 257 ? 152.860 101.669 150.468 1.00 25.14 ?  236 TYR D CE1   1 
ATOM   15274 C  CE2   . TYR D 2 257 ? 153.082 100.836 152.720 1.00 26.71 ?  236 TYR D CE2   1 
ATOM   15275 C  CZ    . TYR D 2 257 ? 153.548 101.615 151.675 1.00 25.35 ?  236 TYR D CZ    1 
ATOM   15276 O  OH    . TYR D 2 257 ? 154.700 102.336 151.849 1.00 26.77 ?  236 TYR D OH    1 
ATOM   15277 N  N     . GLU D 2 258 ? 151.267 96.457  151.378 1.00 23.09 ?  237 GLU D N     1 
ATOM   15278 C  CA    . GLU D 2 258 ? 152.455 95.651  151.667 1.00 23.98 ?  237 GLU D CA    1 
ATOM   15279 C  C     . GLU D 2 258 ? 152.822 94.746  150.491 1.00 23.13 ?  237 GLU D C     1 
ATOM   15280 O  O     . GLU D 2 258 ? 153.998 94.577  150.182 1.00 23.02 ?  237 GLU D O     1 
ATOM   15281 C  CB    . GLU D 2 258 ? 152.299 94.862  152.976 1.00 25.20 ?  237 GLU D CB    1 
ATOM   15282 C  CG    . GLU D 2 258 ? 152.218 95.755  154.225 1.00 28.82 ?  237 GLU D CG    1 
ATOM   15283 C  CD    . GLU D 2 258 ? 153.537 96.450  154.592 1.00 34.48 ?  237 GLU D CD    1 
ATOM   15284 O  OE1   . GLU D 2 258 ? 154.634 95.907  154.294 1.00 37.75 ?  237 GLU D OE1   1 
ATOM   15285 O  OE2   . GLU D 2 258 ? 153.480 97.547  155.198 1.00 37.16 -1 237 GLU D OE2   1 
ATOM   15286 N  N     . ASN D 2 259 ? 151.814 94.201  149.822 1.00 22.12 ?  238 ASN D N     1 
ATOM   15287 C  CA    . ASN D 2 259 ? 152.029 93.450  148.584 1.00 22.35 ?  238 ASN D CA    1 
ATOM   15288 C  C     . ASN D 2 259 ? 152.527 94.330  147.406 1.00 22.11 ?  238 ASN D C     1 
ATOM   15289 O  O     . ASN D 2 259 ? 153.351 93.881  146.606 1.00 22.24 ?  238 ASN D O     1 
ATOM   15290 C  CB    . ASN D 2 259 ? 150.760 92.679  148.199 1.00 21.69 ?  238 ASN D CB    1 
ATOM   15291 C  CG    . ASN D 2 259 ? 150.944 91.843  146.946 1.00 23.38 ?  238 ASN D CG    1 
ATOM   15292 O  OD1   . ASN D 2 259 ? 151.627 90.807  146.963 1.00 23.95 ?  238 ASN D OD1   1 
ATOM   15293 N  ND2   . ASN D 2 259 ? 150.349 92.291  145.849 1.00 21.14 ?  238 ASN D ND2   1 
ATOM   15294 N  N     . GLU D 2 260 ? 152.032 95.570  147.312 1.00 21.95 ?  239 GLU D N     1 
ATOM   15295 C  CA    . GLU D 2 260 ? 152.510 96.536  146.302 1.00 22.50 ?  239 GLU D CA    1 
ATOM   15296 C  C     . GLU D 2 260 ? 154.000 96.842  146.450 1.00 22.03 ?  239 GLU D C     1 
ATOM   15297 O  O     . GLU D 2 260 ? 154.699 97.027  145.459 1.00 22.03 ?  239 GLU D O     1 
ATOM   15298 C  CB    . GLU D 2 260 ? 151.753 97.875  146.376 1.00 22.90 ?  239 GLU D CB    1 
ATOM   15299 C  CG    . GLU D 2 260 ? 150.406 97.937  145.636 1.00 25.84 ?  239 GLU D CG    1 
ATOM   15300 C  CD    . GLU D 2 260 ? 150.458 97.400  144.209 1.00 28.59 ?  239 GLU D CD    1 
ATOM   15301 O  OE1   . GLU D 2 260 ? 150.418 96.164  144.040 1.00 28.18 ?  239 GLU D OE1   1 
ATOM   15302 O  OE2   . GLU D 2 260 ? 150.498 98.214  143.257 1.00 30.32 -1 239 GLU D OE2   1 
ATOM   15303 N  N     . LEU D 2 261 ? 154.470 96.929  147.690 1.00 21.50 ?  240 LEU D N     1 
ATOM   15304 C  CA    . LEU D 2 261 ? 155.885 97.188  147.937 1.00 22.03 ?  240 LEU D CA    1 
ATOM   15305 C  C     . LEU D 2 261 ? 156.722 96.047  147.387 1.00 21.52 ?  240 LEU D C     1 
ATOM   15306 O  O     . LEU D 2 261 ? 157.740 96.286  146.736 1.00 21.44 ?  240 LEU D O     1 
ATOM   15307 C  CB    . LEU D 2 261 ? 156.173 97.391  149.422 1.00 21.57 ?  240 LEU D CB    1 
ATOM   15308 C  CG    . LEU D 2 261 ? 155.488 98.558  150.133 1.00 23.22 ?  240 LEU D CG    1 
ATOM   15309 C  CD1   . LEU D 2 261 ? 155.888 98.550  151.596 1.00 23.06 ?  240 LEU D CD1   1 
ATOM   15310 C  CD2   . LEU D 2 261 ? 155.845 99.894  149.480 1.00 23.52 ?  240 LEU D CD2   1 
ATOM   15311 N  N     . GLU D 2 262 ? 156.276 94.815  147.630 1.00 21.69 ?  241 GLU D N     1 
ATOM   15312 C  CA    . GLU D 2 262 ? 156.964 93.627  147.097 1.00 22.31 ?  241 GLU D CA    1 
ATOM   15313 C  C     . GLU D 2 262 ? 156.868 93.552  145.572 1.00 21.69 ?  241 GLU D C     1 
ATOM   15314 O  O     . GLU D 2 262 ? 157.852 93.249  144.892 1.00 21.75 ?  241 GLU D O     1 
ATOM   15315 C  CB    . GLU D 2 262 ? 156.401 92.341  147.709 1.00 22.46 ?  241 GLU D CB    1 
ATOM   15316 C  CG    . GLU D 2 262 ? 156.546 92.207  149.227 1.00 25.63 ?  241 GLU D CG    1 
ATOM   15317 C  CD    . GLU D 2 262 ? 156.044 90.853  149.711 1.00 29.83 ?  241 GLU D CD    1 
ATOM   15318 O  OE1   . GLU D 2 262 ? 154.814 90.679  149.841 1.00 33.22 ?  241 GLU D OE1   1 
ATOM   15319 O  OE2   . GLU D 2 262 ? 156.871 89.951  149.933 1.00 33.36 -1 241 GLU D OE2   1 
ATOM   15320 N  N     . TYR D 2 263 ? 155.674 93.809  145.040 1.00 21.42 ?  242 TYR D N     1 
ATOM   15321 C  CA    . TYR D 2 263 ? 155.441 93.861  143.592 1.00 21.04 ?  242 TYR D CA    1 
ATOM   15322 C  C     . TYR D 2 263 ? 156.393 94.876  142.943 1.00 21.15 ?  242 TYR D C     1 
ATOM   15323 O  O     . TYR D 2 263 ? 156.968 94.621  141.884 1.00 20.32 ?  242 TYR D O     1 
ATOM   15324 C  CB    . TYR D 2 263 ? 153.981 94.258  143.323 1.00 20.95 ?  242 TYR D CB    1 
ATOM   15325 C  CG    . TYR D 2 263 ? 153.609 94.453  141.865 1.00 21.86 ?  242 TYR D CG    1 
ATOM   15326 C  CD1   . TYR D 2 263 ? 153.325 93.359  141.047 1.00 23.53 ?  242 TYR D CD1   1 
ATOM   15327 C  CD2   . TYR D 2 263 ? 153.541 95.731  141.302 1.00 21.20 ?  242 TYR D CD2   1 
ATOM   15328 C  CE1   . TYR D 2 263 ? 152.982 93.531  139.714 1.00 23.34 ?  242 TYR D CE1   1 
ATOM   15329 C  CE2   . TYR D 2 263 ? 153.198 95.911  139.966 1.00 23.11 ?  242 TYR D CE2   1 
ATOM   15330 C  CZ    . TYR D 2 263 ? 152.926 94.805  139.179 1.00 23.27 ?  242 TYR D CZ    1 
ATOM   15331 O  OH    . TYR D 2 263 ? 152.585 94.978  137.854 1.00 27.07 ?  242 TYR D OH    1 
ATOM   15332 N  N     . THR D 2 264 ? 156.526 96.028  143.596 1.00 21.12 ?  243 THR D N     1 
ATOM   15333 C  CA    . THR D 2 264 ? 157.339 97.138  143.106 1.00 21.98 ?  243 THR D CA    1 
ATOM   15334 C  C     . THR D 2 264 ? 158.817 96.760  143.034 1.00 22.32 ?  243 THR D C     1 
ATOM   15335 O  O     . THR D 2 264 ? 159.445 96.931  141.992 1.00 21.78 ?  243 THR D O     1 
ATOM   15336 C  CB    . THR D 2 264 ? 157.119 98.404  143.964 1.00 21.68 ?  243 THR D CB    1 
ATOM   15337 O  OG1   . THR D 2 264 ? 155.771 98.850  143.793 1.00 23.29 ?  243 THR D OG1   1 
ATOM   15338 C  CG2   . THR D 2 264 ? 158.087 99.541  143.582 1.00 23.16 ?  243 THR D CG2   1 
ATOM   15339 N  N     . GLU D 2 265 ? 159.359 96.225  144.128 1.00 22.48 ?  244 GLU D N     1 
ATOM   15340 C  CA    . GLU D 2 265 ? 160.764 95.809  144.131 1.00 23.73 ?  244 GLU D CA    1 
ATOM   15341 C  C     . GLU D 2 265 ? 161.028 94.734  143.088 1.00 23.85 ?  244 GLU D C     1 
ATOM   15342 O  O     . GLU D 2 265 ? 162.044 94.780  142.407 1.00 24.40 ?  244 GLU D O     1 
ATOM   15343 C  CB    . GLU D 2 265 ? 161.189 95.325  145.509 1.00 23.19 ?  244 GLU D CB    1 
ATOM   15344 C  CG    . GLU D 2 265 ? 161.349 96.464  146.481 1.00 25.08 ?  244 GLU D CG    1 
ATOM   15345 C  CD    . GLU D 2 265 ? 161.601 96.002  147.901 1.00 27.30 ?  244 GLU D CD    1 
ATOM   15346 O  OE1   . GLU D 2 265 ? 161.859 94.802  148.115 1.00 27.77 ?  244 GLU D OE1   1 
ATOM   15347 O  OE2   . GLU D 2 265 ? 161.543 96.856  148.805 1.00 28.63 -1 244 GLU D OE2   1 
ATOM   15348 N  N     . ASP D 2 266 ? 160.088 93.798  142.951 1.00 24.13 ?  245 ASP D N     1 
ATOM   15349 C  CA    . ASP D 2 266 ? 160.193 92.692  141.994 1.00 25.22 ?  245 ASP D CA    1 
ATOM   15350 C  C     . ASP D 2 266 ? 160.349 93.178  140.536 1.00 24.84 ?  245 ASP D C     1 
ATOM   15351 O  O     . ASP D 2 266 ? 161.087 92.572  139.753 1.00 25.64 ?  245 ASP D O     1 
ATOM   15352 C  CB    . ASP D 2 266 ? 158.967 91.776  142.142 1.00 25.79 ?  245 ASP D CB    1 
ATOM   15353 C  CG    . ASP D 2 266 ? 159.050 90.520  141.286 1.00 27.71 ?  245 ASP D CG    1 
ATOM   15354 O  OD1   . ASP D 2 266 ? 160.034 89.776  141.417 1.00 31.57 ?  245 ASP D OD1   1 
ATOM   15355 O  OD2   . ASP D 2 266 ? 158.117 90.260  140.497 1.00 30.29 -1 245 ASP D OD2   1 
ATOM   15356 N  N     . LEU D 2 267 ? 159.677 94.272  140.190 1.00 24.07 ?  246 LEU D N     1 
ATOM   15357 C  CA    . LEU D 2 267 ? 159.685 94.797  138.822 1.00 23.98 ?  246 LEU D CA    1 
ATOM   15358 C  C     . LEU D 2 267 ? 160.695 95.919  138.575 1.00 22.83 ?  246 LEU D C     1 
ATOM   15359 O  O     . LEU D 2 267 ? 161.311 95.972  137.503 1.00 23.00 ?  246 LEU D O     1 
ATOM   15360 C  CB    . LEU D 2 267 ? 158.286 95.300  138.425 1.00 23.82 ?  246 LEU D CB    1 
ATOM   15361 C  CG    . LEU D 2 267 ? 157.200 94.232  138.234 1.00 26.05 ?  246 LEU D CG    1 
ATOM   15362 C  CD1   . LEU D 2 267 ? 155.976 94.831  137.598 1.00 26.74 ?  246 LEU D CD1   1 
ATOM   15363 C  CD2   . LEU D 2 267 ? 157.695 93.070  137.395 1.00 28.00 ?  246 LEU D CD2   1 
ATOM   15364 N  N     . TYR D 2 268 ? 160.852 96.805  139.560 1.00 21.68 ?  247 TYR D N     1 
ATOM   15365 C  CA    . TYR D 2 268 ? 161.579 98.062  139.360 1.00 20.95 ?  247 TYR D CA    1 
ATOM   15366 C  C     . TYR D 2 268 ? 163.016 98.128  139.894 1.00 21.43 ?  247 TYR D C     1 
ATOM   15367 O  O     . TYR D 2 268 ? 163.759 99.027  139.503 1.00 20.73 ?  247 TYR D O     1 
ATOM   15368 C  CB    . TYR D 2 268 ? 160.782 99.244  139.920 1.00 20.27 ?  247 TYR D CB    1 
ATOM   15369 C  CG    . TYR D 2 268 ? 159.538 99.601  139.126 1.00 19.54 ?  247 TYR D CG    1 
ATOM   15370 C  CD1   . TYR D 2 268 ? 158.276 99.211  139.562 1.00 18.52 ?  247 TYR D CD1   1 
ATOM   15371 C  CD2   . TYR D 2 268 ? 159.632 100.329 137.930 1.00 20.62 ?  247 TYR D CD2   1 
ATOM   15372 C  CE1   . TYR D 2 268 ? 157.107 99.552  138.832 1.00 18.33 ?  247 TYR D CE1   1 
ATOM   15373 C  CE2   . TYR D 2 268 ? 158.476 100.673 137.192 1.00 20.79 ?  247 TYR D CE2   1 
ATOM   15374 C  CZ    . TYR D 2 268 ? 157.227 100.287 137.658 1.00 20.23 ?  247 TYR D CZ    1 
ATOM   15375 O  OH    . TYR D 2 268 ? 156.106 100.628 136.927 1.00 20.50 ?  247 TYR D OH    1 
ATOM   15376 N  N     . ASP D 2 269 ? 163.409 97.215  140.789 1.00 21.65 ?  248 ASP D N     1 
ATOM   15377 C  CA    . ASP D 2 269 ? 164.812 97.187  141.218 1.00 22.30 ?  248 ASP D CA    1 
ATOM   15378 C  C     . ASP D 2 269 ? 165.797 97.051  140.033 1.00 22.54 ?  248 ASP D C     1 
ATOM   15379 O  O     . ASP D 2 269 ? 166.858 97.681  140.037 1.00 22.49 ?  248 ASP D O     1 
ATOM   15380 C  CB    . ASP D 2 269 ? 165.070 96.096  142.259 1.00 22.83 ?  248 ASP D CB    1 
ATOM   15381 C  CG    . ASP D 2 269 ? 164.666 96.518  143.668 1.00 23.55 ?  248 ASP D CG    1 
ATOM   15382 O  OD1   . ASP D 2 269 ? 164.331 97.702  143.874 1.00 24.95 ?  248 ASP D OD1   1 
ATOM   15383 O  OD2   . ASP D 2 269 ? 164.684 95.657  144.577 1.00 24.47 -1 248 ASP D OD2   1 
ATOM   15384 N  N     . GLN D 2 270 ? 165.441 96.246  139.029 1.00 22.79 ?  249 GLN D N     1 
ATOM   15385 C  CA    . GLN D 2 270 ? 166.321 96.018  137.876 1.00 23.41 ?  249 GLN D CA    1 
ATOM   15386 C  C     . GLN D 2 270 ? 166.527 97.259  137.002 1.00 22.83 ?  249 GLN D C     1 
ATOM   15387 O  O     . GLN D 2 270 ? 167.448 97.293  136.189 1.00 23.75 ?  249 GLN D O     1 
ATOM   15388 C  CB    . GLN D 2 270 ? 165.843 94.839  137.022 1.00 24.02 ?  249 GLN D CB    1 
ATOM   15389 C  CG    . GLN D 2 270 ? 164.540 95.090  136.243 1.00 25.40 ?  249 GLN D CG    1 
ATOM   15390 C  CD    . GLN D 2 270 ? 163.946 93.813  135.670 1.00 29.23 ?  249 GLN D CD    1 
ATOM   15391 O  OE1   . GLN D 2 270 ? 164.094 92.735  136.248 1.00 31.31 ?  249 GLN D OE1   1 
ATOM   15392 N  NE2   . GLN D 2 270 ? 163.259 93.931  134.537 1.00 30.04 ?  249 GLN D NE2   1 
ATOM   15393 N  N     . VAL D 2 271 ? 165.662 98.261  137.157 1.00 21.93 ?  250 VAL D N     1 
ATOM   15394 C  CA    . VAL D 2 271 ? 165.829 99.537  136.452 1.00 21.29 ?  250 VAL D CA    1 
ATOM   15395 C  C     . VAL D 2 271 ? 166.031 100.717 137.421 1.00 21.16 ?  250 VAL D C     1 
ATOM   15396 O  O     . VAL D 2 271 ? 165.971 101.881 137.013 1.00 21.54 ?  250 VAL D O     1 
ATOM   15397 C  CB    . VAL D 2 271 ? 164.654 99.797  135.455 1.00 21.62 ?  250 VAL D CB    1 
ATOM   15398 C  CG1   . VAL D 2 271 ? 164.654 98.747  134.345 1.00 21.36 ?  250 VAL D CG1   1 
ATOM   15399 C  CG2   . VAL D 2 271 ? 163.297 99.825  136.181 1.00 21.17 ?  250 VAL D CG2   1 
ATOM   15400 N  N     . GLY D 2 272 ? 166.247 100.407 138.705 1.00 20.92 ?  251 GLY D N     1 
ATOM   15401 C  CA    . GLY D 2 272 ? 166.640 101.398 139.727 1.00 20.61 ?  251 GLY D CA    1 
ATOM   15402 C  C     . GLY D 2 272 ? 165.613 102.446 140.148 1.00 20.77 ?  251 GLY D C     1 
ATOM   15403 O  O     . GLY D 2 272 ? 165.981 103.534 140.615 1.00 20.28 ?  251 GLY D O     1 
ATOM   15404 N  N     . LEU D 2 273 ? 164.330 102.121 140.013 1.00 19.85 ?  252 LEU D N     1 
ATOM   15405 C  CA    . LEU D 2 273 ? 163.286 103.128 140.208 1.00 20.09 ?  252 LEU D CA    1 
ATOM   15406 C  C     . LEU D 2 273 ? 162.395 102.953 141.441 1.00 19.88 ?  252 LEU D C     1 
ATOM   15407 O  O     . LEU D 2 273 ? 161.564 103.813 141.712 1.00 20.04 ?  252 LEU D O     1 
ATOM   15408 C  CB    . LEU D 2 273 ? 162.391 103.185 138.959 1.00 19.97 ?  252 LEU D CB    1 
ATOM   15409 C  CG    . LEU D 2 273 ? 163.070 103.520 137.639 1.00 20.26 ?  252 LEU D CG    1 
ATOM   15410 C  CD1   . LEU D 2 273 ? 161.998 103.630 136.577 1.00 18.98 ?  252 LEU D CD1   1 
ATOM   15411 C  CD2   . LEU D 2 273 ? 163.900 104.832 137.726 1.00 21.03 ?  252 LEU D CD2   1 
ATOM   15412 N  N     . SER D 2 274 ? 162.585 101.858 142.180 0.50 19.54 ?  253 SER D N     1 
ATOM   15413 C  CA    . SER D 2 274 ? 161.633 101.437 143.220 0.50 19.34 ?  253 SER D CA    1 
ATOM   15414 C  C     . SER D 2 274 ? 161.317 102.494 144.284 0.50 20.05 ?  253 SER D C     1 
ATOM   15415 O  O     . SER D 2 274 ? 160.161 102.647 144.675 0.50 20.31 ?  253 SER D O     1 
ATOM   15416 C  CB    . SER D 2 274 ? 162.080 100.126 143.880 0.50 18.97 ?  253 SER D CB    1 
ATOM   15417 O  OG    . SER D 2 274 ? 162.265 99.102  142.920 0.50 15.35 ?  253 SER D OG    1 
ATOM   15418 N  N     . HIS D 2 275 ? 162.340 103.208 144.754 1.00 20.77 ?  254 HIS D N     1 
ATOM   15419 C  CA    . HIS D 2 275 ? 162.148 104.289 145.743 1.00 21.18 ?  254 HIS D CA    1 
ATOM   15420 C  C     . HIS D 2 275 ? 161.090 105.310 145.289 1.00 21.50 ?  254 HIS D C     1 
ATOM   15421 O  O     . HIS D 2 275 ? 160.158 105.633 146.044 1.00 19.88 ?  254 HIS D O     1 
ATOM   15422 C  CB    . HIS D 2 275 ? 163.471 105.000 146.070 1.00 21.60 ?  254 HIS D CB    1 
ATOM   15423 C  CG    . HIS D 2 275 ? 163.305 106.187 146.971 1.00 22.43 ?  254 HIS D CG    1 
ATOM   15424 N  ND1   . HIS D 2 275 ? 163.330 106.091 148.348 1.00 22.77 ?  254 HIS D ND1   1 
ATOM   15425 C  CD2   . HIS D 2 275 ? 163.092 107.496 146.687 1.00 22.50 ?  254 HIS D CD2   1 
ATOM   15426 C  CE1   . HIS D 2 275 ? 163.146 107.291 148.871 1.00 24.05 ?  254 HIS D CE1   1 
ATOM   15427 N  NE2   . HIS D 2 275 ? 162.993 108.160 147.885 1.00 23.22 ?  254 HIS D NE2   1 
ATOM   15428 N  N     . ASP D 2 276 ? 161.233 105.795 144.055 1.00 22.34 ?  255 ASP D N     1 
ATOM   15429 C  CA    . ASP D 2 276 ? 160.304 106.780 143.508 1.00 23.19 ?  255 ASP D CA    1 
ATOM   15430 C  C     . ASP D 2 276 ? 158.930 106.192 143.222 1.00 22.17 ?  255 ASP D C     1 
ATOM   15431 O  O     . ASP D 2 276 ? 157.931 106.881 143.376 1.00 21.87 ?  255 ASP D O     1 
ATOM   15432 C  CB    . ASP D 2 276 ? 160.859 107.433 142.232 1.00 24.33 ?  255 ASP D CB    1 
ATOM   15433 C  CG    . ASP D 2 276 ? 161.736 108.655 142.516 1.00 27.58 ?  255 ASP D CG    1 
ATOM   15434 O  OD1   . ASP D 2 276 ? 161.585 109.295 143.581 1.00 31.10 ?  255 ASP D OD1   1 
ATOM   15435 O  OD2   . ASP D 2 276 ? 162.589 108.973 141.656 1.00 29.88 -1 255 ASP D OD2   1 
ATOM   15436 N  N     . VAL D 2 277 ? 158.883 104.939 142.771 1.00 21.21 ?  256 VAL D N     1 
ATOM   15437 C  CA    . VAL D 2 277 ? 157.599 104.267 142.544 1.00 20.51 ?  256 VAL D CA    1 
ATOM   15438 C  C     . VAL D 2 277 ? 156.804 104.135 143.848 1.00 20.32 ?  256 VAL D C     1 
ATOM   15439 O  O     . VAL D 2 277 ? 155.593 104.343 143.858 1.00 19.81 ?  256 VAL D O     1 
ATOM   15440 C  CB    . VAL D 2 277 ? 157.763 102.876 141.868 1.00 20.30 ?  256 VAL D CB    1 
ATOM   15441 C  CG1   . VAL D 2 277 ? 156.416 102.190 141.720 1.00 21.16 ?  256 VAL D CG1   1 
ATOM   15442 C  CG2   . VAL D 2 277 ? 158.419 103.024 140.506 1.00 19.06 ?  256 VAL D CG2   1 
ATOM   15443 N  N     . LYS D 2 278 ? 157.499 103.811 144.938 1.00 19.84 ?  257 LYS D N     1 
ATOM   15444 C  CA    . LYS D 2 278 ? 156.873 103.707 146.256 1.00 20.27 ?  257 LYS D CA    1 
ATOM   15445 C  C     . LYS D 2 278 ? 156.212 105.018 146.699 1.00 20.16 ?  257 LYS D C     1 
ATOM   15446 O  O     . LYS D 2 278 ? 155.107 104.988 147.235 1.00 19.88 ?  257 LYS D O     1 
ATOM   15447 C  CB    . LYS D 2 278 ? 157.864 103.196 147.305 1.00 20.20 ?  257 LYS D CB    1 
ATOM   15448 C  CG    . LYS D 2 278 ? 158.179 101.711 147.161 1.00 21.60 ?  257 LYS D CG    1 
ATOM   15449 C  CD    . LYS D 2 278 ? 159.360 101.294 148.029 1.00 21.53 ?  257 LYS D CD    1 
ATOM   15450 C  CE    . LYS D 2 278 ? 159.739 99.865  147.727 1.00 24.52 ?  257 LYS D CE    1 
ATOM   15451 N  NZ    . LYS D 2 278 ? 160.876 99.422  148.598 1.00 26.32 1  257 LYS D NZ    1 
ATOM   15452 N  N     . LYS D 2 279 ? 156.873 106.154 146.451 1.00 19.67 ?  258 LYS D N     1 
ATOM   15453 C  CA    . LYS D 2 279 ? 156.269 107.465 146.736 1.00 20.10 ?  258 LYS D CA    1 
ATOM   15454 C  C     . LYS D 2 279 ? 154.970 107.660 145.944 1.00 19.12 ?  258 LYS D C     1 
ATOM   15455 O  O     . LYS D 2 279 ? 153.990 108.179 146.482 1.00 18.59 ?  258 LYS D O     1 
ATOM   15456 C  CB    . LYS D 2 279 ? 157.244 108.623 146.448 1.00 20.54 ?  258 LYS D CB    1 
ATOM   15457 C  CG    . LYS D 2 279 ? 158.525 108.608 147.278 1.00 22.84 ?  258 LYS D CG    1 
ATOM   15458 C  CD    . LYS D 2 279 ? 159.170 110.010 147.393 1.00 24.16 ?  258 LYS D CD    1 
ATOM   15459 C  CE    . LYS D 2 279 ? 159.691 110.529 146.056 1.00 25.61 ?  258 LYS D CE    1 
ATOM   15460 N  NZ    . LYS D 2 279 ? 160.327 111.899 146.179 1.00 24.70 1  258 LYS D NZ    1 
ATOM   15461 N  N     . PHE D 2 280 ? 154.975 107.218 144.683 1.00 19.04 ?  259 PHE D N     1 
ATOM   15462 C  CA    . PHE D 2 280 ? 153.816 107.327 143.777 1.00 19.31 ?  259 PHE D CA    1 
ATOM   15463 C  C     . PHE D 2 280 ? 152.639 106.443 144.204 1.00 19.25 ?  259 PHE D C     1 
ATOM   15464 O  O     . PHE D 2 280 ? 151.474 106.847 144.100 1.00 19.71 ?  259 PHE D O     1 
ATOM   15465 C  CB    . PHE D 2 280 ? 154.240 106.969 142.352 1.00 19.04 ?  259 PHE D CB    1 
ATOM   15466 C  CG    . PHE D 2 280 ? 153.266 107.409 141.274 1.00 20.15 ?  259 PHE D CG    1 
ATOM   15467 C  CD1   . PHE D 2 280 ? 152.882 108.736 141.156 1.00 21.63 ?  259 PHE D CD1   1 
ATOM   15468 C  CD2   . PHE D 2 280 ? 152.784 106.484 140.346 1.00 19.95 ?  259 PHE D CD2   1 
ATOM   15469 C  CE1   . PHE D 2 280 ? 152.008 109.144 140.125 1.00 22.56 ?  259 PHE D CE1   1 
ATOM   15470 C  CE2   . PHE D 2 280 ? 151.920 106.869 139.322 1.00 20.29 ?  259 PHE D CE2   1 
ATOM   15471 C  CZ    . PHE D 2 280 ? 151.528 108.204 139.212 1.00 21.30 ?  259 PHE D CZ    1 
ATOM   15472 N  N     . ILE D 2 281 ? 152.939 105.234 144.667 1.00 19.36 ?  260 ILE D N     1 
ATOM   15473 C  CA    . ILE D 2 281 ? 151.925 104.357 145.260 1.00 19.45 ?  260 ILE D CA    1 
ATOM   15474 C  C     . ILE D 2 281 ? 151.218 105.006 146.469 1.00 19.61 ?  260 ILE D C     1 
ATOM   15475 O  O     . ILE D 2 281 ? 149.988 104.989 146.541 1.00 19.72 ?  260 ILE D O     1 
ATOM   15476 C  CB    . ILE D 2 281 ? 152.557 102.992 145.640 1.00 19.49 ?  260 ILE D CB    1 
ATOM   15477 C  CG1   . ILE D 2 281 ? 152.998 102.258 144.370 1.00 20.10 ?  260 ILE D CG1   1 
ATOM   15478 C  CG2   . ILE D 2 281 ? 151.621 102.131 146.516 1.00 20.53 ?  260 ILE D CG2   1 
ATOM   15479 C  CD1   . ILE D 2 281 ? 153.927 101.077 144.672 1.00 21.17 ?  260 ILE D CD1   1 
ATOM   15480 N  N     . ARG D 2 282 ? 151.989 105.581 147.395 1.00 19.75 ?  261 ARG D N     1 
ATOM   15481 C  CA    . ARG D 2 282 ? 151.417 106.182 148.616 1.00 20.34 ?  261 ARG D CA    1 
ATOM   15482 C  C     . ARG D 2 282 ? 150.560 107.403 148.301 1.00 21.18 ?  261 ARG D C     1 
ATOM   15483 O  O     . ARG D 2 282 ? 149.488 107.603 148.889 1.00 21.68 ?  261 ARG D O     1 
ATOM   15484 C  CB    . ARG D 2 282 ? 152.513 106.538 149.630 1.00 20.20 ?  261 ARG D CB    1 
ATOM   15485 C  CG    . ARG D 2 282 ? 153.157 105.331 150.288 1.00 20.57 ?  261 ARG D CG    1 
ATOM   15486 C  CD    . ARG D 2 282 ? 154.115 105.751 151.404 1.00 23.15 ?  261 ARG D CD    1 
ATOM   15487 N  NE    . ARG D 2 282 ? 155.371 106.325 150.914 1.00 23.46 ?  261 ARG D NE    1 
ATOM   15488 C  CZ    . ARG D 2 282 ? 156.463 105.619 150.623 1.00 22.84 ?  261 ARG D CZ    1 
ATOM   15489 N  NH1   . ARG D 2 282 ? 156.463 104.297 150.731 1.00 23.37 1  261 ARG D NH1   1 
ATOM   15490 N  NH2   . ARG D 2 282 ? 157.558 106.241 150.209 1.00 22.27 ?  261 ARG D NH2   1 
ATOM   15491 N  N     . TYR D 2 283 ? 151.056 108.224 147.382 1.00 21.46 ?  262 TYR D N     1 
ATOM   15492 C  CA    . TYR D 2 283 ? 150.332 109.401 146.906 1.00 22.97 ?  262 TYR D CA    1 
ATOM   15493 C  C     . TYR D 2 283 ? 148.973 108.987 146.299 1.00 22.12 ?  262 TYR D C     1 
ATOM   15494 O  O     . TYR D 2 283 ? 147.945 109.614 146.567 1.00 22.00 ?  262 TYR D O     1 
ATOM   15495 C  CB    . TYR D 2 283 ? 151.224 110.150 145.909 1.00 23.37 ?  262 TYR D CB    1 
ATOM   15496 C  CG    . TYR D 2 283 ? 150.551 111.191 145.045 1.00 27.31 ?  262 TYR D CG    1 
ATOM   15497 C  CD1   . TYR D 2 283 ? 150.405 112.506 145.490 1.00 30.79 ?  262 TYR D CD1   1 
ATOM   15498 C  CD2   . TYR D 2 283 ? 150.102 110.871 143.764 1.00 30.31 ?  262 TYR D CD2   1 
ATOM   15499 C  CE1   . TYR D 2 283 ? 149.788 113.477 144.685 1.00 33.18 ?  262 TYR D CE1   1 
ATOM   15500 C  CE2   . TYR D 2 283 ? 149.496 111.831 142.948 1.00 33.20 ?  262 TYR D CE2   1 
ATOM   15501 C  CZ    . TYR D 2 283 ? 149.349 113.132 143.416 1.00 34.74 ?  262 TYR D CZ    1 
ATOM   15502 O  OH    . TYR D 2 283 ? 148.756 114.080 142.604 1.00 37.63 ?  262 TYR D OH    1 
ATOM   15503 N  N     . ASN D 2 284 ? 148.960 107.903 145.528 1.00 21.63 ?  263 ASN D N     1 
ATOM   15504 C  CA    . ASN D 2 284 ? 147.716 107.430 144.925 1.00 21.41 ?  263 ASN D CA    1 
ATOM   15505 C  C     . ASN D 2 284 ? 146.807 106.681 145.904 1.00 20.86 ?  263 ASN D C     1 
ATOM   15506 O  O     . ASN D 2 284 ? 145.590 106.737 145.772 1.00 20.92 ?  263 ASN D O     1 
ATOM   15507 C  CB    . ASN D 2 284 ? 147.985 106.635 143.646 1.00 21.15 ?  263 ASN D CB    1 
ATOM   15508 C  CG    . ASN D 2 284 ? 148.370 107.538 142.482 1.00 22.59 ?  263 ASN D CG    1 
ATOM   15509 O  OD1   . ASN D 2 284 ? 147.530 108.261 141.940 1.00 22.35 ?  263 ASN D OD1   1 
ATOM   15510 N  ND2   . ASN D 2 284 ? 149.645 107.513 142.103 1.00 22.93 ?  263 ASN D ND2   1 
ATOM   15511 N  N     . ALA D 2 285 ? 147.398 105.995 146.882 1.00 20.92 ?  264 ALA D N     1 
ATOM   15512 C  CA    . ALA D 2 285 ? 146.634 105.428 148.006 1.00 20.77 ?  264 ALA D CA    1 
ATOM   15513 C  C     . ALA D 2 285 ? 145.830 106.504 148.744 1.00 21.13 ?  264 ALA D C     1 
ATOM   15514 O  O     . ALA D 2 285 ? 144.655 106.296 149.072 1.00 19.92 ?  264 ALA D O     1 
ATOM   15515 C  CB    . ALA D 2 285 ? 147.560 104.681 148.977 1.00 20.68 ?  264 ALA D CB    1 
ATOM   15516 N  N     . ASN D 2 286 ? 146.468 107.653 148.995 1.00 21.38 ?  265 ASN D N     1 
ATOM   15517 C  CA    . ASN D 2 286 ? 145.804 108.802 149.616 1.00 21.94 ?  265 ASN D CA    1 
ATOM   15518 C  C     . ASN D 2 286 ? 144.634 109.332 148.768 1.00 22.13 ?  265 ASN D C     1 
ATOM   15519 O  O     . ASN D 2 286 ? 143.598 109.702 149.306 1.00 21.95 ?  265 ASN D O     1 
ATOM   15520 C  CB    . ASN D 2 286 ? 146.800 109.933 149.881 1.00 22.22 ?  265 ASN D CB    1 
ATOM   15521 C  CG    . ASN D 2 286 ? 147.651 109.710 151.128 1.00 22.80 ?  265 ASN D CG    1 
ATOM   15522 O  OD1   . ASN D 2 286 ? 147.375 108.840 151.962 1.00 22.57 ?  265 ASN D OD1   1 
ATOM   15523 N  ND2   . ASN D 2 286 ? 148.705 110.509 151.251 1.00 23.91 ?  265 ASN D ND2   1 
ATOM   15524 N  N     . LYS D 2 287 ? 144.801 109.361 147.447 1.00 22.51 ?  266 LYS D N     1 
ATOM   15525 C  CA    . LYS D 2 287 ? 143.707 109.774 146.557 1.00 22.91 ?  266 LYS D CA    1 
ATOM   15526 C  C     . LYS D 2 287 ? 142.525 108.799 146.639 1.00 22.33 ?  266 LYS D C     1 
ATOM   15527 O  O     . LYS D 2 287 ? 141.378 109.226 146.686 1.00 22.24 ?  266 LYS D O     1 
ATOM   15528 C  CB    . LYS D 2 287 ? 144.188 109.916 145.106 1.00 23.65 ?  266 LYS D CB    1 
ATOM   15529 C  CG    . LYS D 2 287 ? 145.027 111.169 144.854 1.00 26.50 ?  266 LYS D CG    1 
ATOM   15530 C  CD    . LYS D 2 287 ? 145.458 111.248 143.378 1.00 31.30 ?  266 LYS D CD    1 
ATOM   15531 C  CE    . LYS D 2 287 ? 145.834 112.674 143.014 1.00 35.08 ?  266 LYS D CE    1 
ATOM   15532 N  NZ    . LYS D 2 287 ? 146.232 112.844 141.584 1.00 37.66 1  266 LYS D NZ    1 
ATOM   15533 N  N     . ALA D 2 288 ? 142.823 107.499 146.671 1.00 21.41 ?  267 ALA D N     1 
ATOM   15534 C  CA    . ALA D 2 288 ? 141.815 106.446 146.798 1.00 21.53 ?  267 ALA D CA    1 
ATOM   15535 C  C     . ALA D 2 288 ? 141.020 106.578 148.109 1.00 21.77 ?  267 ALA D C     1 
ATOM   15536 O  O     . ALA D 2 288 ? 139.782 106.474 148.124 1.00 21.59 ?  267 ALA D O     1 
ATOM   15537 C  CB    . ALA D 2 288 ? 142.471 105.063 146.691 1.00 21.33 ?  267 ALA D CB    1 
ATOM   15538 N  N     . LEU D 2 289 ? 141.731 106.829 149.200 1.00 21.71 ?  268 LEU D N     1 
ATOM   15539 C  CA    . LEU D 2 289 ? 141.079 107.082 150.480 1.00 22.36 ?  268 LEU D CA    1 
ATOM   15540 C  C     . LEU D 2 289 ? 140.193 108.318 150.410 1.00 23.01 ?  268 LEU D C     1 
ATOM   15541 O  O     . LEU D 2 289 ? 139.045 108.290 150.860 1.00 23.14 ?  268 LEU D O     1 
ATOM   15542 C  CB    . LEU D 2 289 ? 142.109 107.193 151.611 1.00 22.61 ?  268 LEU D CB    1 
ATOM   15543 C  CG    . LEU D 2 289 ? 142.814 105.874 151.997 1.00 21.22 ?  268 LEU D CG    1 
ATOM   15544 C  CD1   . LEU D 2 289 ? 144.018 106.143 152.887 1.00 20.77 ?  268 LEU D CD1   1 
ATOM   15545 C  CD2   . LEU D 2 289 ? 141.848 104.879 152.678 1.00 21.40 ?  268 LEU D CD2   1 
ATOM   15546 N  N     . MET D 2 290 ? 140.701 109.398 149.825 1.00 23.87 ?  269 MET D N     1 
ATOM   15547 C  CA    . MET D 2 290 ? 139.878 110.598 149.700 1.00 25.26 ?  269 MET D CA    1 
ATOM   15548 C  C     . MET D 2 290 ? 138.623 110.349 148.845 1.00 24.37 ?  269 MET D C     1 
ATOM   15549 O  O     . MET D 2 290 ? 137.555 110.848 149.183 1.00 23.97 ?  269 MET D O     1 
ATOM   15550 C  CB    . MET D 2 290 ? 140.706 111.798 149.253 1.00 25.94 ?  269 MET D CB    1 
ATOM   15551 C  CG    . MET D 2 290 ? 141.497 112.396 150.434 1.00 31.08 ?  269 MET D CG    1 
ATOM   15552 S  SD    . MET D 2 290 ? 142.537 113.809 150.002 1.00 41.28 ?  269 MET D SD    1 
ATOM   15553 C  CE    . MET D 2 290 ? 141.348 114.891 149.167 1.00 38.56 ?  269 MET D CE    1 
ATOM   15554 N  N     . ASN D 2 291 ? 138.742 109.540 147.787 1.00 23.66 ?  270 ASN D N     1 
ATOM   15555 C  CA    . ASN D 2 291 ? 137.561 109.102 147.007 1.00 23.17 ?  270 ASN D CA    1 
ATOM   15556 C  C     . ASN D 2 291 ? 136.481 108.402 147.838 1.00 23.22 ?  270 ASN D C     1 
ATOM   15557 O  O     . ASN D 2 291 ? 135.296 108.478 147.515 1.00 22.68 ?  270 ASN D O     1 
ATOM   15558 C  CB    . ASN D 2 291 ? 137.960 108.193 145.834 1.00 22.41 ?  270 ASN D CB    1 
ATOM   15559 C  CG    . ASN D 2 291 ? 138.702 108.936 144.748 1.00 21.93 ?  270 ASN D CG    1 
ATOM   15560 O  OD1   . ASN D 2 291 ? 138.722 110.171 144.722 1.00 20.94 ?  270 ASN D OD1   1 
ATOM   15561 N  ND2   . ASN D 2 291 ? 139.322 108.188 143.839 1.00 19.20 ?  270 ASN D ND2   1 
ATOM   15562 N  N     . LEU D 2 292 ? 136.911 107.722 148.900 1.00 23.53 ?  271 LEU D N     1 
ATOM   15563 C  CA    . LEU D 2 292 ? 136.009 107.016 149.813 1.00 24.21 ?  271 LEU D CA    1 
ATOM   15564 C  C     . LEU D 2 292 ? 135.611 107.880 151.013 1.00 25.14 ?  271 LEU D C     1 
ATOM   15565 O  O     . LEU D 2 292 ? 135.003 107.389 151.978 1.00 25.14 ?  271 LEU D O     1 
ATOM   15566 C  CB    . LEU D 2 292 ? 136.647 105.690 150.279 1.00 23.71 ?  271 LEU D CB    1 
ATOM   15567 C  CG    . LEU D 2 292 ? 136.917 104.618 149.212 1.00 23.37 ?  271 LEU D CG    1 
ATOM   15568 C  CD1   . LEU D 2 292 ? 137.894 103.561 149.734 1.00 23.28 ?  271 LEU D CD1   1 
ATOM   15569 C  CD2   . LEU D 2 292 ? 135.613 103.962 148.720 1.00 23.06 ?  271 LEU D CD2   1 
ATOM   15570 N  N     . GLY D 2 293 ? 135.948 109.170 150.944 1.00 25.82 ?  272 GLY D N     1 
ATOM   15571 C  CA    . GLY D 2 293 ? 135.628 110.120 152.003 1.00 27.13 ?  272 GLY D CA    1 
ATOM   15572 C  C     . GLY D 2 293 ? 136.436 109.942 153.272 1.00 27.99 ?  272 GLY D C     1 
ATOM   15573 O  O     . GLY D 2 293 ? 136.037 110.427 154.327 1.00 27.97 ?  272 GLY D O     1 
ATOM   15574 N  N     . PHE D 2 294 ? 137.572 109.246 153.172 1.00 28.02 ?  273 PHE D N     1 
ATOM   15575 C  CA    . PHE D 2 294 ? 138.455 109.010 154.322 1.00 28.75 ?  273 PHE D CA    1 
ATOM   15576 C  C     . PHE D 2 294 ? 139.681 109.933 154.317 1.00 29.00 ?  273 PHE D C     1 
ATOM   15577 O  O     . PHE D 2 294 ? 140.050 110.476 153.278 1.00 28.74 ?  273 PHE D O     1 
ATOM   15578 C  CB    . PHE D 2 294 ? 138.920 107.545 154.350 1.00 28.32 ?  273 PHE D CB    1 
ATOM   15579 C  CG    . PHE D 2 294 ? 137.810 106.555 154.571 1.00 28.66 ?  273 PHE D CG    1 
ATOM   15580 C  CD1   . PHE D 2 294 ? 136.804 106.805 155.504 1.00 30.23 ?  273 PHE D CD1   1 
ATOM   15581 C  CD2   . PHE D 2 294 ? 137.780 105.364 153.856 1.00 26.94 ?  273 PHE D CD2   1 
ATOM   15582 C  CE1   . PHE D 2 294 ? 135.772 105.883 155.710 1.00 31.04 ?  273 PHE D CE1   1 
ATOM   15583 C  CE2   . PHE D 2 294 ? 136.766 104.437 154.054 1.00 27.39 ?  273 PHE D CE2   1 
ATOM   15584 C  CZ    . PHE D 2 294 ? 135.760 104.688 154.979 1.00 29.80 ?  273 PHE D CZ    1 
ATOM   15585 N  N     . ASP D 2 295 ? 140.301 110.101 155.483 1.00 29.60 ?  274 ASP D N     1 
ATOM   15586 C  CA    . ASP D 2 295 ? 141.517 110.901 155.612 1.00 30.40 ?  274 ASP D CA    1 
ATOM   15587 C  C     . ASP D 2 295 ? 142.723 110.211 154.945 1.00 29.58 ?  274 ASP D C     1 
ATOM   15588 O  O     . ASP D 2 295 ? 142.767 108.983 154.861 1.00 28.68 ?  274 ASP D O     1 
ATOM   15589 C  CB    . ASP D 2 295 ? 141.833 111.175 157.088 1.00 31.44 ?  274 ASP D CB    1 
ATOM   15590 C  CG    . ASP D 2 295 ? 140.784 112.046 157.771 1.00 34.27 ?  274 ASP D CG    1 
ATOM   15591 O  OD1   . ASP D 2 295 ? 140.130 112.874 157.091 1.00 36.43 ?  274 ASP D OD1   1 
ATOM   15592 O  OD2   . ASP D 2 295 ? 140.623 111.898 159.001 1.00 38.03 -1 274 ASP D OD2   1 
ATOM   15593 N  N     . PRO D 2 296 ? 143.709 111.003 154.482 1.00 29.59 ?  275 PRO D N     1 
ATOM   15594 C  CA    . PRO D 2 296 ? 144.914 110.377 153.929 1.00 29.09 ?  275 PRO D CA    1 
ATOM   15595 C  C     . PRO D 2 296 ? 145.634 109.549 154.993 1.00 29.26 ?  275 PRO D C     1 
ATOM   15596 O  O     . PRO D 2 296 ? 145.631 109.908 156.170 1.00 29.36 ?  275 PRO D O     1 
ATOM   15597 C  CB    . PRO D 2 296 ? 145.779 111.571 153.502 1.00 29.49 ?  275 PRO D CB    1 
ATOM   15598 C  CG    . PRO D 2 296 ? 145.226 112.757 154.245 1.00 30.28 ?  275 PRO D CG    1 
ATOM   15599 C  CD    . PRO D 2 296 ? 143.768 112.477 154.433 1.00 29.63 ?  275 PRO D CD    1 
ATOM   15600 N  N     . TYR D 2 297 ? 146.226 108.439 154.578 1.00 28.97 ?  276 TYR D N     1 
ATOM   15601 C  CA    . TYR D 2 297 ? 146.906 107.538 155.501 1.00 29.63 ?  276 TYR D CA    1 
ATOM   15602 C  C     . TYR D 2 297 ? 148.405 107.861 155.598 1.00 29.55 ?  276 TYR D C     1 
ATOM   15603 O  O     . TYR D 2 297 ? 149.024 107.719 156.661 1.00 30.12 ?  276 TYR D O     1 
ATOM   15604 C  CB    . TYR D 2 297 ? 146.711 106.101 155.016 1.00 29.49 ?  276 TYR D CB    1 
ATOM   15605 C  CG    . TYR D 2 297 ? 147.074 105.030 156.009 1.00 31.19 ?  276 TYR D CG    1 
ATOM   15606 C  CD1   . TYR D 2 297 ? 146.387 104.918 157.223 1.00 31.93 ?  276 TYR D CD1   1 
ATOM   15607 C  CD2   . TYR D 2 297 ? 148.084 104.108 155.730 1.00 31.98 ?  276 TYR D CD2   1 
ATOM   15608 C  CE1   . TYR D 2 297 ? 146.708 103.928 158.141 1.00 33.86 ?  276 TYR D CE1   1 
ATOM   15609 C  CE2   . TYR D 2 297 ? 148.410 103.105 156.644 1.00 33.88 ?  276 TYR D CE2   1 
ATOM   15610 C  CZ    . TYR D 2 297 ? 147.711 103.024 157.843 1.00 34.42 ?  276 TYR D CZ    1 
ATOM   15611 O  OH    . TYR D 2 297 ? 148.021 102.051 158.758 1.00 37.63 ?  276 TYR D OH    1 
ATOM   15612 N  N     . PHE D 2 298 ? 148.970 108.292 154.475 1.00 29.10 ?  277 PHE D N     1 
ATOM   15613 C  CA    . PHE D 2 298 ? 150.405 108.514 154.331 1.00 28.97 ?  277 PHE D CA    1 
ATOM   15614 C  C     . PHE D 2 298 ? 150.728 110.012 154.329 1.00 29.77 ?  277 PHE D C     1 
ATOM   15615 O  O     . PHE D 2 298 ? 149.926 110.827 153.864 1.00 29.07 ?  277 PHE D O     1 
ATOM   15616 C  CB    . PHE D 2 298 ? 150.905 107.881 153.028 1.00 27.99 ?  277 PHE D CB    1 
ATOM   15617 C  CG    . PHE D 2 298 ? 150.705 106.386 152.952 1.00 27.61 ?  277 PHE D CG    1 
ATOM   15618 C  CD1   . PHE D 2 298 ? 149.741 105.841 152.115 1.00 25.91 ?  277 PHE D CD1   1 
ATOM   15619 C  CD2   . PHE D 2 298 ? 151.501 105.523 153.708 1.00 27.32 ?  277 PHE D CD2   1 
ATOM   15620 C  CE1   . PHE D 2 298 ? 149.564 104.470 152.038 1.00 26.65 ?  277 PHE D CE1   1 
ATOM   15621 C  CE2   . PHE D 2 298 ? 151.337 104.152 153.640 1.00 25.38 ?  277 PHE D CE2   1 
ATOM   15622 C  CZ    . PHE D 2 298 ? 150.366 103.618 152.815 1.00 26.20 ?  277 PHE D CZ    1 
ATOM   15623 N  N     . GLU D 2 299 ? 151.902 110.362 154.855 1.00 31.10 ?  278 GLU D N     1 
ATOM   15624 C  CA    . GLU D 2 299 ? 152.403 111.737 154.801 1.00 32.86 ?  278 GLU D CA    1 
ATOM   15625 C  C     . GLU D 2 299 ? 152.578 112.172 153.340 1.00 33.04 ?  278 GLU D C     1 
ATOM   15626 O  O     . GLU D 2 299 ? 152.842 111.343 152.464 1.00 32.23 ?  278 GLU D O     1 
ATOM   15627 C  CB    . GLU D 2 299 ? 153.730 111.865 155.570 1.00 33.45 ?  278 GLU D CB    1 
ATOM   15628 C  CG    . GLU D 2 299 ? 154.862 111.003 154.992 1.00 36.27 ?  278 GLU D CG    1 
ATOM   15629 C  CD    . GLU D 2 299 ? 156.218 111.215 155.649 1.00 40.47 ?  278 GLU D CD    1 
ATOM   15630 O  OE1   . GLU D 2 299 ? 156.289 111.353 156.892 1.00 41.72 ?  278 GLU D OE1   1 
ATOM   15631 O  OE2   . GLU D 2 299 ? 157.223 111.210 154.905 1.00 42.65 -1 278 GLU D OE2   1 
ATOM   15632 N  N     . GLU D 2 300 ? 152.421 113.471 153.095 1.00 34.09 ?  279 GLU D N     1 
ATOM   15633 C  CA    . GLU D 2 300 ? 152.580 114.049 151.767 1.00 35.06 ?  279 GLU D CA    1 
ATOM   15634 C  C     . GLU D 2 300 ? 154.038 113.948 151.316 1.00 34.97 ?  279 GLU D C     1 
ATOM   15635 O  O     . GLU D 2 300 ? 154.958 114.227 152.086 1.00 34.96 ?  279 GLU D O     1 
ATOM   15636 C  CB    . GLU D 2 300 ? 152.105 115.512 151.767 1.00 35.81 ?  279 GLU D CB    1 
ATOM   15637 C  CG    . GLU D 2 300 ? 152.051 116.157 150.380 1.00 38.58 ?  279 GLU D CG    1 
ATOM   15638 C  CD    . GLU D 2 300 ? 151.066 117.322 150.297 1.00 43.09 ?  279 GLU D CD    1 
ATOM   15639 O  OE1   . GLU D 2 300 ? 150.159 117.270 149.435 1.00 44.69 ?  279 GLU D OE1   1 
ATOM   15640 O  OE2   . GLU D 2 300 ? 151.191 118.280 151.094 1.00 44.94 -1 279 GLU D OE2   1 
ATOM   15641 N  N     . GLU D 2 301 ? 154.229 113.522 150.071 1.00 34.73 ?  280 GLU D N     1 
ATOM   15642 C  CA    . GLU D 2 301 ? 155.553 113.404 149.473 1.00 35.16 ?  280 GLU D CA    1 
ATOM   15643 C  C     . GLU D 2 301 ? 155.528 114.036 148.092 1.00 35.23 ?  280 GLU D C     1 
ATOM   15644 O  O     . GLU D 2 301 ? 154.481 114.080 147.439 1.00 34.92 ?  280 GLU D O     1 
ATOM   15645 C  CB    . GLU D 2 301 ? 155.958 111.929 149.350 1.00 35.10 ?  280 GLU D CB    1 
ATOM   15646 C  CG    . GLU D 2 301 ? 156.499 111.300 150.632 1.00 36.62 ?  280 GLU D CG    1 
ATOM   15647 C  CD    . GLU D 2 301 ? 156.631 109.780 150.539 1.00 37.59 ?  280 GLU D CD    1 
ATOM   15648 O  OE1   . GLU D 2 301 ? 155.621 109.100 150.261 1.00 38.10 ?  280 GLU D OE1   1 
ATOM   15649 O  OE2   . GLU D 2 301 ? 157.740 109.260 150.769 1.00 38.93 -1 280 GLU D OE2   1 
ATOM   15650 N  N     . ASP D 2 302 ? 156.677 114.527 147.643 1.00 35.60 ?  281 ASP D N     1 
ATOM   15651 C  CA    . ASP D 2 302 ? 156.784 115.044 146.284 1.00 35.96 ?  281 ASP D CA    1 
ATOM   15652 C  C     . ASP D 2 302 ? 156.944 113.867 145.331 1.00 35.01 ?  281 ASP D C     1 
ATOM   15653 O  O     . ASP D 2 302 ? 157.439 112.812 145.726 1.00 35.52 ?  281 ASP D O     1 
ATOM   15654 C  CB    . ASP D 2 302 ? 157.933 116.060 146.159 1.00 36.82 ?  281 ASP D CB    1 
ATOM   15655 C  CG    . ASP D 2 302 ? 159.322 115.450 146.425 1.00 39.01 ?  281 ASP D CG    1 
ATOM   15656 O  OD1   . ASP D 2 302 ? 159.438 114.384 147.080 1.00 40.83 ?  281 ASP D OD1   1 
ATOM   15657 O  OD2   . ASP D 2 302 ? 160.312 116.069 145.986 1.00 41.13 -1 281 ASP D OD2   1 
ATOM   15658 N  N     . ILE D 2 303 ? 156.494 114.025 144.093 1.00 33.94 ?  282 ILE D N     1 
ATOM   15659 C  CA    . ILE D 2 303 ? 156.589 112.948 143.111 1.00 33.00 ?  282 ILE D CA    1 
ATOM   15660 C  C     . ILE D 2 303 ? 157.682 113.212 142.067 1.00 31.59 ?  282 ILE D C     1 
ATOM   15661 O  O     . ILE D 2 303 ? 158.004 114.366 141.775 1.00 31.14 ?  282 ILE D O     1 
ATOM   15662 C  CB    . ILE D 2 303 ? 155.199 112.636 142.469 1.00 33.44 ?  282 ILE D CB    1 
ATOM   15663 C  CG1   . ILE D 2 303 ? 155.333 112.120 141.032 1.00 34.29 ?  282 ILE D CG1   1 
ATOM   15664 C  CG2   . ILE D 2 303 ? 154.290 113.853 142.539 1.00 35.47 ?  282 ILE D CG2   1 
ATOM   15665 C  CD1   . ILE D 2 303 ? 154.017 111.992 140.292 1.00 36.30 ?  282 ILE D CD1   1 
ATOM   15666 N  N     . ASN D 2 304 ? 158.262 112.137 141.533 1.00 29.53 ?  283 ASN D N     1 
ATOM   15667 C  CA    . ASN D 2 304 ? 159.252 112.238 140.465 1.00 28.49 ?  283 ASN D CA    1 
ATOM   15668 C  C     . ASN D 2 304 ? 158.797 113.216 139.361 1.00 27.87 ?  283 ASN D C     1 
ATOM   15669 O  O     . ASN D 2 304 ? 157.710 113.057 138.806 1.00 27.02 ?  283 ASN D O     1 
ATOM   15670 C  CB    . ASN D 2 304 ? 159.526 110.853 139.874 1.00 28.20 ?  283 ASN D CB    1 
ATOM   15671 C  CG    . ASN D 2 304 ? 160.609 110.879 138.828 1.00 28.17 ?  283 ASN D CG    1 
ATOM   15672 O  OD1   . ASN D 2 304 ? 160.345 111.149 137.661 1.00 29.01 ?  283 ASN D OD1   1 
ATOM   15673 N  ND2   . ASN D 2 304 ? 161.836 110.596 139.236 1.00 27.24 ?  283 ASN D ND2   1 
ATOM   15674 N  N     . PRO D 2 305 ? 159.622 114.239 139.053 1.00 28.00 ?  284 PRO D N     1 
ATOM   15675 C  CA    . PRO D 2 305 ? 159.208 115.280 138.099 1.00 27.58 ?  284 PRO D CA    1 
ATOM   15676 C  C     . PRO D 2 305 ? 159.026 114.791 136.660 1.00 27.01 ?  284 PRO D C     1 
ATOM   15677 O  O     . PRO D 2 305 ? 158.275 115.397 135.903 1.00 26.66 ?  284 PRO D O     1 
ATOM   15678 C  CB    . PRO D 2 305 ? 160.344 116.309 138.173 1.00 28.21 ?  284 PRO D CB    1 
ATOM   15679 C  CG    . PRO D 2 305 ? 161.491 115.595 138.739 1.00 28.80 ?  284 PRO D CG    1 
ATOM   15680 C  CD    . PRO D 2 305 ? 160.911 114.570 139.687 1.00 28.11 ?  284 PRO D CD    1 
ATOM   15681 N  N     . ILE D 2 306 ? 159.700 113.706 136.291 1.00 26.52 ?  285 ILE D N     1 
ATOM   15682 C  CA    . ILE D 2 306 ? 159.542 113.137 134.958 1.00 26.50 ?  285 ILE D CA    1 
ATOM   15683 C  C     . ILE D 2 306 ? 158.149 112.507 134.820 1.00 26.43 ?  285 ILE D C     1 
ATOM   15684 O  O     . ILE D 2 306 ? 157.425 112.761 133.846 1.00 26.00 ?  285 ILE D O     1 
ATOM   15685 C  CB    . ILE D 2 306 ? 160.675 112.137 134.619 1.00 26.88 ?  285 ILE D CB    1 
ATOM   15686 C  CG1   . ILE D 2 306 ? 162.035 112.856 134.664 1.00 26.98 ?  285 ILE D CG1   1 
ATOM   15687 C  CG2   . ILE D 2 306 ? 160.414 111.494 133.256 1.00 24.94 ?  285 ILE D CG2   1 
ATOM   15688 C  CD1   . ILE D 2 306 ? 163.236 111.960 134.537 1.00 26.65 ?  285 ILE D CD1   1 
ATOM   15689 N  N     . VAL D 2 307 ? 157.770 111.716 135.818 1.00 26.36 ?  286 VAL D N     1 
ATOM   15690 C  CA    . VAL D 2 307 ? 156.417 111.182 135.904 1.00 26.71 ?  286 VAL D CA    1 
ATOM   15691 C  C     . VAL D 2 307 ? 155.371 112.300 135.978 1.00 27.68 ?  286 VAL D C     1 
ATOM   15692 O  O     . VAL D 2 307 ? 154.344 112.215 135.304 1.00 27.92 ?  286 VAL D O     1 
ATOM   15693 C  CB    . VAL D 2 307 ? 156.276 110.161 137.065 1.00 26.37 ?  286 VAL D CB    1 
ATOM   15694 C  CG1   . VAL D 2 307 ? 154.806 109.789 137.317 1.00 25.48 ?  286 VAL D CG1   1 
ATOM   15695 C  CG2   . VAL D 2 307 ? 157.058 108.932 136.728 1.00 25.55 ?  286 VAL D CG2   1 
ATOM   15696 N  N     . LEU D 2 308 ? 155.639 113.358 136.750 1.00 28.80 ?  287 LEU D N     1 
ATOM   15697 C  CA    . LEU D 2 308 ? 154.737 114.521 136.766 1.00 30.07 ?  287 LEU D CA    1 
ATOM   15698 C  C     . LEU D 2 308 ? 154.559 115.147 135.379 1.00 30.38 ?  287 LEU D C     1 
ATOM   15699 O  O     . LEU D 2 308 ? 153.446 115.515 134.988 1.00 30.71 ?  287 LEU D O     1 
ATOM   15700 C  CB    . LEU D 2 308 ? 155.201 115.583 137.767 1.00 30.86 ?  287 LEU D CB    1 
ATOM   15701 C  CG    . LEU D 2 308 ? 154.762 115.369 139.219 1.00 32.62 ?  287 LEU D CG    1 
ATOM   15702 C  CD1   . LEU D 2 308 ? 155.448 116.356 140.137 1.00 33.97 ?  287 LEU D CD1   1 
ATOM   15703 C  CD2   . LEU D 2 308 ? 153.232 115.459 139.366 1.00 34.73 ?  287 LEU D CD2   1 
ATOM   15704 N  N     . ASN D 2 309 ? 155.652 115.258 134.631 1.00 30.81 ?  288 ASN D N     1 
ATOM   15705 C  CA    . ASN D 2 309 ? 155.584 115.794 133.276 1.00 31.25 ?  288 ASN D CA    1 
ATOM   15706 C  C     . ASN D 2 309 ? 154.756 114.897 132.354 1.00 31.83 ?  288 ASN D C     1 
ATOM   15707 O  O     . ASN D 2 309 ? 154.064 115.388 131.457 1.00 31.73 ?  288 ASN D O     1 
ATOM   15708 C  CB    . ASN D 2 309 ? 156.982 116.043 132.698 1.00 31.21 ?  288 ASN D CB    1 
ATOM   15709 C  CG    . ASN D 2 309 ? 156.934 116.784 131.372 1.00 31.41 ?  288 ASN D CG    1 
ATOM   15710 O  OD1   . ASN D 2 309 ? 156.187 117.758 131.221 1.00 31.88 ?  288 ASN D OD1   1 
ATOM   15711 N  ND2   . ASN D 2 309 ? 157.720 116.326 130.404 1.00 29.12 ?  288 ASN D ND2   1 
ATOM   15712 N  N     . GLY D 2 310 ? 154.829 113.586 132.587 1.00 32.04 ?  289 GLY D N     1 
ATOM   15713 C  CA    . GLY D 2 310 ? 153.980 112.624 131.894 1.00 33.04 ?  289 GLY D CA    1 
ATOM   15714 C  C     . GLY D 2 310 ? 152.513 112.812 132.257 1.00 33.85 ?  289 GLY D C     1 
ATOM   15715 O  O     . GLY D 2 310 ? 151.656 112.859 131.375 1.00 34.05 ?  289 GLY D O     1 
ATOM   15716 N  N     . LEU D 2 311 ? 152.231 112.923 133.554 1.00 34.33 ?  290 LEU D N     1 
ATOM   15717 C  CA    . LEU D 2 311 ? 150.865 113.086 134.061 1.00 35.77 ?  290 LEU D CA    1 
ATOM   15718 C  C     . LEU D 2 311 ? 150.187 114.361 133.569 1.00 37.01 ?  290 LEU D C     1 
ATOM   15719 O  O     . LEU D 2 311 ? 149.000 114.350 133.238 1.00 37.18 ?  290 LEU D O     1 
ATOM   15720 C  CB    . LEU D 2 311 ? 150.855 113.089 135.595 1.00 35.50 ?  290 LEU D CB    1 
ATOM   15721 C  CG    . LEU D 2 311 ? 150.688 111.802 136.397 1.00 35.45 ?  290 LEU D CG    1 
ATOM   15722 C  CD1   . LEU D 2 311 ? 150.911 112.104 137.887 1.00 35.28 ?  290 LEU D CD1   1 
ATOM   15723 C  CD2   . LEU D 2 311 ? 149.318 111.155 136.181 1.00 34.16 ?  290 LEU D CD2   1 
ATOM   15724 N  N     . THR D 2 332 ? 112.675 119.374 152.428 1.00 32.64 ?  311 THR D N     1 
ATOM   15725 C  CA    . THR D 2 332 ? 111.304 118.958 152.704 1.00 31.78 ?  311 THR D CA    1 
ATOM   15726 C  C     . THR D 2 332 ? 110.319 120.066 152.352 1.00 32.37 ?  311 THR D C     1 
ATOM   15727 O  O     . THR D 2 332 ? 110.071 120.967 153.152 1.00 35.72 ?  311 THR D O     1 
ATOM   15728 C  CB    . THR D 2 332 ? 111.118 118.568 154.180 1.00 33.94 ?  311 THR D CB    1 
ATOM   15729 O  OG1   . THR D 2 332 ? 112.252 117.812 154.624 1.00 36.69 ?  311 THR D OG1   1 
ATOM   15730 C  CG2   . THR D 2 332 ? 109.860 117.734 154.353 1.00 32.38 ?  311 THR D CG2   1 
ATOM   15731 N  N     . VAL D 2 333 ? 109.755 119.992 151.151 1.00 30.43 ?  312 VAL D N     1 
ATOM   15732 C  CA    . VAL D 2 333 ? 108.825 121.010 150.675 1.00 25.25 ?  312 VAL D CA    1 
ATOM   15733 C  C     . VAL D 2 333 ? 107.468 120.790 151.333 1.00 34.67 ?  312 VAL D C     1 
ATOM   15734 O  O     . VAL D 2 333 ? 106.891 119.702 151.244 1.00 39.77 ?  312 VAL D O     1 
ATOM   15735 C  CB    . VAL D 2 333 ? 108.706 120.978 149.146 1.00 28.81 ?  312 VAL D CB    1 
ATOM   15736 C  CG1   . VAL D 2 333 ? 107.786 122.087 148.663 1.00 33.67 ?  312 VAL D CG1   1 
ATOM   15737 C  CG2   . VAL D 2 333 ? 110.078 121.102 148.508 1.00 31.46 ?  312 VAL D CG2   1 
ATOM   15738 N  N     . GLU D 2 334 ? 106.958 121.827 151.996 1.00 38.13 ?  313 GLU D N     1 
ATOM   15739 C  CA    . GLU D 2 334 ? 105.623 121.810 152.566 1.00 32.68 ?  313 GLU D CA    1 
ATOM   15740 C  C     . GLU D 2 334 ? 104.944 123.143 152.279 1.00 42.07 ?  313 GLU D C     1 
ATOM   15741 O  O     . GLU D 2 334 ? 105.608 124.187 152.262 1.00 44.37 ?  313 GLU D O     1 
ATOM   15742 C  CB    . GLU D 2 334 ? 105.669 121.546 154.078 1.00 35.51 ?  313 GLU D CB    1 
ATOM   15743 C  CG    . GLU D 2 334 ? 104.452 122.030 154.844 1.00 40.09 ?  313 GLU D CG    1 
ATOM   15744 C  CD    . GLU D 2 334 ? 104.476 121.607 156.299 1.00 41.38 ?  313 GLU D CD    1 
ATOM   15745 O  OE1   . GLU D 2 334 ? 105.447 120.935 156.709 1.00 38.01 ?  313 GLU D OE1   1 
ATOM   15746 O  OE2   . GLU D 2 334 ? 103.525 121.944 157.035 1.00 41.10 -1 313 GLU D OE2   1 
ATOM   15747 N  N     . PRO D 2 335 ? 103.634 123.144 152.049 1.00 34.04 ?  314 PRO D N     1 
ATOM   15748 C  CA    . PRO D 2 335 ? 102.964 124.369 151.611 1.00 37.54 ?  314 PRO D CA    1 
ATOM   15749 C  C     . PRO D 2 335 ? 102.544 125.260 152.769 1.00 39.25 ?  314 PRO D C     1 
ATOM   15750 O  O     . PRO D 2 335 ? 102.258 124.801 153.877 1.00 37.42 ?  314 PRO D O     1 
ATOM   15751 C  CB    . PRO D 2 335 ? 101.737 123.849 150.849 1.00 35.55 ?  314 PRO D CB    1 
ATOM   15752 C  CG    . PRO D 2 335 ? 101.605 122.383 151.211 1.00 34.61 ?  314 PRO D CG    1 
ATOM   15753 C  CD    . PRO D 2 335 ? 102.699 122.016 152.167 1.00 38.99 ?  314 PRO D CD    1 
ATOM   15754 N  N     . LEU D 2 336 ? 102.511 126.561 152.487 1.00 37.68 ?  315 LEU D N     1 
ATOM   15755 C  CA    . LEU D 2 336 ? 102.001 127.532 153.442 1.00 31.18 ?  315 LEU D CA    1 
ATOM   15756 C  C     . LEU D 2 336 ? 100.497 127.342 153.618 1.00 34.09 ?  315 LEU D C     1 
ATOM   15757 O  O     . LEU D 2 336 ? 99.772  127.044 152.665 1.00 40.33 ?  315 LEU D O     1 
ATOM   15758 C  CB    . LEU D 2 336 ? 102.310 128.950 152.965 1.00 30.11 ?  315 LEU D CB    1 
ATOM   15759 C  CG    . LEU D 2 336 ? 103.767 129.407 153.103 1.00 28.46 ?  315 LEU D CG    1 
ATOM   15760 C  CD1   . LEU D 2 336 ? 104.008 130.674 152.300 1.00 27.43 ?  315 LEU D CD1   1 
ATOM   15761 C  CD2   . LEU D 2 336 ? 104.148 129.615 154.559 1.00 31.93 ?  315 LEU D CD2   1 
ATOM   15762 N  N     . LYS D 2 337 ? 100.023 127.522 154.852 1.00 34.15 ?  316 LYS D N     1 
ATOM   15763 C  CA    . LYS D 2 337 ? 98.673  127.109 155.224 1.00 38.53 ?  316 LYS D CA    1 
ATOM   15764 C  C     . LYS D 2 337 ? 97.816  128.303 155.655 1.00 43.06 ?  316 LYS D C     1 
ATOM   15765 O  O     . LYS D 2 337 ? 96.883  128.185 156.444 1.00 52.48 ?  316 LYS D O     1 
ATOM   15766 C  CB    . LYS D 2 337 ? 98.730  126.052 156.325 1.00 43.23 ?  316 LYS D CB    1 
ATOM   15767 C  CG    . LYS D 2 337 ? 98.976  124.642 155.812 1.00 44.18 ?  316 LYS D CG    1 
ATOM   15768 C  CD    . LYS D 2 337 ? 99.909  123.875 156.733 1.00 42.17 ?  316 LYS D CD    1 
ATOM   15769 C  CE    . LYS D 2 337 ? 99.153  123.267 157.903 1.00 45.82 ?  316 LYS D CE    1 
ATOM   15770 N  NZ    . LYS D 2 337 ? 98.614  124.305 158.823 1.00 42.77 1  316 LYS D NZ    1 
ATOM   15771 N  N     . ASP D 2 338 ? 98.141  129.485 155.132 1.00 30.41 ?  317 ASP D N     1 
ATOM   15772 C  CA    . ASP D 2 338 ? 97.299  130.665 155.307 1.00 36.21 ?  317 ASP D CA    1 
ATOM   15773 C  C     . ASP D 2 338 ? 97.301  131.176 156.744 1.00 38.96 ?  317 ASP D C     1 
ATOM   15774 O  O     . ASP D 2 338 ? 96.709  132.220 157.035 1.00 45.43 ?  317 ASP D O     1 
ATOM   15775 C  CB    . ASP D 2 338 ? 95.865  130.360 154.869 1.00 38.67 ?  317 ASP D CB    1 
ATOM   15776 C  CG    . ASP D 2 338 ? 95.279  131.451 153.995 1.00 42.65 ?  317 ASP D CG    1 
ATOM   15777 O  OD1   . ASP D 2 338 ? 94.628  131.118 152.983 1.00 43.60 ?  317 ASP D OD1   1 
ATOM   15778 O  OD2   . ASP D 2 338 ? 95.466  132.641 154.323 1.00 40.06 -1 317 ASP D OD2   1 
ATOM   15779 N  N     . ASP D 2 339 ? 97.966  130.457 157.645 1.00 37.70 ?  318 ASP D N     1 
ATOM   15780 C  CA    . ASP D 2 339 ? 98.160  130.937 159.006 1.00 37.72 ?  318 ASP D CA    1 
ATOM   15781 C  C     . ASP D 2 339 ? 99.600  131.334 159.277 1.00 36.27 ?  318 ASP D C     1 
ATOM   15782 O  O     . ASP D 2 339 ? 99.866  132.011 160.275 1.00 44.43 ?  318 ASP D O     1 
ATOM   15783 C  CB    . ASP D 2 339 ? 97.719  129.874 160.016 1.00 33.05 ?  318 ASP D CB    1 
ATOM   15784 C  CG    . ASP D 2 339 ? 96.250  129.980 160.369 1.00 43.22 ?  318 ASP D CG    1 
ATOM   15785 O  OD1   . ASP D 2 339 ? 95.421  130.112 159.444 1.00 43.86 ?  318 ASP D OD1   1 
ATOM   15786 O  OD2   . ASP D 2 339 ? 95.923  129.936 161.573 1.00 42.14 -1 318 ASP D OD2   1 
ATOM   15787 N  N     . ASP D 2 340 ? 100.529 130.928 158.411 1.00 28.22 ?  319 ASP D N     1 
ATOM   15788 C  CA    . ASP D 2 340 ? 101.920 131.330 158.545 1.00 24.24 ?  319 ASP D CA    1 
ATOM   15789 C  C     . ASP D 2 340 ? 102.101 132.821 158.303 1.00 29.87 ?  319 ASP D C     1 
ATOM   15790 O  O     . ASP D 2 340 ? 103.165 133.370 158.606 1.00 42.86 ?  319 ASP D O     1 
ATOM   15791 C  CB    . ASP D 2 340 ? 102.782 130.522 157.574 1.00 29.20 ?  319 ASP D CB    1 
ATOM   15792 C  CG    . ASP D 2 340 ? 102.470 129.040 157.624 1.00 35.23 ?  319 ASP D CG    1 
ATOM   15793 O  OD1   . ASP D 2 340 ? 101.797 128.611 158.583 1.00 33.87 ?  319 ASP D OD1   1 
ATOM   15794 O  OD2   . ASP D 2 340 ? 102.892 128.303 156.709 1.00 46.31 -1 319 ASP D OD2   1 
ATOM   15795 N  N     . PHE D 2 341 ? 101.082 133.484 157.761 1.00 24.46 ?  320 PHE D N     1 
ATOM   15796 C  CA    . PHE D 2 341 ? 101.126 134.908 157.467 1.00 16.71 ?  320 PHE D CA    1 
ATOM   15797 C  C     . PHE D 2 341 ? 100.581 135.762 158.606 1.00 20.53 ?  320 PHE D C     1 
ATOM   15798 O  O     . PHE D 2 341 ? 100.484 136.985 158.460 1.00 23.45 ?  320 PHE D O     1 
ATOM   15799 C  CB    . PHE D 2 341 ? 100.352 135.199 156.180 1.00 22.18 ?  320 PHE D CB    1 
ATOM   15800 C  CG    . PHE D 2 341 ? 100.944 134.558 154.959 1.00 18.10 ?  320 PHE D CG    1 
ATOM   15801 C  CD1   . PHE D 2 341 ? 101.876 135.232 154.191 1.00 16.07 ?  320 PHE D CD1   1 
ATOM   15802 C  CD2   . PHE D 2 341 ? 100.567 133.281 154.577 1.00 18.98 ?  320 PHE D CD2   1 
ATOM   15803 C  CE1   . PHE D 2 341 ? 102.422 134.646 153.068 1.00 11.21 ?  320 PHE D CE1   1 
ATOM   15804 C  CE2   . PHE D 2 341 ? 101.110 132.689 153.455 1.00 18.90 ?  320 PHE D CE2   1 
ATOM   15805 C  CZ    . PHE D 2 341 ? 102.038 133.373 152.700 1.00 14.14 ?  320 PHE D CZ    1 
ATOM   15806 N  N     . TYR D 2 342 ? 100.221 135.149 159.730 1.00 16.25 ?  321 TYR D N     1 
ATOM   15807 C  CA    . TYR D 2 342 ? 99.637  135.874 160.851 1.00 23.89 ?  321 TYR D CA    1 
ATOM   15808 C  C     . TYR D 2 342 ? 100.361 135.489 162.129 1.00 27.68 ?  321 TYR D C     1 
ATOM   15809 O  O     . TYR D 2 342 ? 100.682 134.316 162.336 1.00 27.93 ?  321 TYR D O     1 
ATOM   15810 C  CB    . TYR D 2 342 ? 98.138  135.582 160.975 1.00 18.45 ?  321 TYR D CB    1 
ATOM   15811 C  CG    . TYR D 2 342 ? 97.342  136.047 159.780 1.00 20.05 ?  321 TYR D CG    1 
ATOM   15812 C  CD1   . TYR D 2 342 ? 96.910  137.361 159.676 1.00 23.35 ?  321 TYR D CD1   1 
ATOM   15813 C  CD2   . TYR D 2 342 ? 97.031  135.172 158.748 1.00 22.69 ?  321 TYR D CD2   1 
ATOM   15814 C  CE1   . TYR D 2 342 ? 96.186  137.790 158.583 1.00 23.94 ?  321 TYR D CE1   1 
ATOM   15815 C  CE2   . TYR D 2 342 ? 96.306  135.591 157.651 1.00 21.84 ?  321 TYR D CE2   1 
ATOM   15816 C  CZ    . TYR D 2 342 ? 95.887  136.901 157.574 1.00 26.78 ?  321 TYR D CZ    1 
ATOM   15817 O  OH    . TYR D 2 342 ? 95.164  137.323 156.481 1.00 35.28 ?  321 TYR D OH    1 
ATOM   15818 N  N     . PHE D 2 343 ? 100.611 136.477 162.982 1.00 26.29 ?  322 PHE D N     1 
ATOM   15819 C  CA    . PHE D 2 343 ? 101.385 136.262 164.197 1.00 30.81 ?  322 PHE D CA    1 
ATOM   15820 C  C     . PHE D 2 343 ? 100.766 136.997 165.381 1.00 35.47 ?  322 PHE D C     1 
ATOM   15821 O  O     . PHE D 2 343 ? 100.405 138.170 165.281 1.00 34.40 ?  322 PHE D O     1 
ATOM   15822 C  CB    . PHE D 2 343 ? 102.829 136.720 163.984 1.00 21.57 ?  322 PHE D CB    1 
ATOM   15823 C  CG    . PHE D 2 343 ? 103.509 136.044 162.830 1.00 24.72 ?  322 PHE D CG    1 
ATOM   15824 C  CD1   . PHE D 2 343 ? 104.042 134.776 162.969 1.00 30.83 ?  322 PHE D CD1   1 
ATOM   15825 C  CD2   . PHE D 2 343 ? 103.597 136.672 161.600 1.00 17.69 ?  322 PHE D CD2   1 
ATOM   15826 C  CE1   . PHE D 2 343 ? 104.663 134.153 161.907 1.00 28.36 ?  322 PHE D CE1   1 
ATOM   15827 C  CE2   . PHE D 2 343 ? 104.215 136.053 160.535 1.00 15.64 ?  322 PHE D CE2   1 
ATOM   15828 C  CZ    . PHE D 2 343 ? 104.748 134.791 160.688 1.00 17.88 ?  322 PHE D CZ    1 
HETATM 15829 P  PA    . TTP E 3 .   ? 146.512 146.108 134.682 1.00 12.29 ?  801 TTP A PA    1 
HETATM 15830 O  O1A   . TTP E 3 .   ? 145.081 146.580 134.664 1.00 17.62 -1 801 TTP A O1A   1 
HETATM 15831 O  O2A   . TTP E 3 .   ? 147.332 146.856 133.661 1.00 21.44 ?  801 TTP A O2A   1 
HETATM 15832 O  O3A   . TTP E 3 .   ? 147.131 146.230 136.161 1.00 27.08 ?  801 TTP A O3A   1 
HETATM 15833 P  PB    . TTP E 3 .   ? 148.211 147.365 136.525 1.00 24.47 ?  801 TTP A PB    1 
HETATM 15834 O  O1B   . TTP E 3 .   ? 148.568 148.214 135.331 1.00 36.93 -1 801 TTP A O1B   1 
HETATM 15835 O  O2B   . TTP E 3 .   ? 147.707 148.223 137.657 1.00 28.79 ?  801 TTP A O2B   1 
HETATM 15836 O  O3B   . TTP E 3 .   ? 149.466 146.477 136.993 1.00 22.70 ?  801 TTP A O3B   1 
HETATM 15837 P  PG    . TTP E 3 .   ? 150.768 146.353 136.056 1.00 25.17 ?  801 TTP A PG    1 
HETATM 15838 O  O1G   . TTP E 3 .   ? 151.311 147.722 135.734 1.00 27.94 ?  801 TTP A O1G   1 
HETATM 15839 O  O2G   . TTP E 3 .   ? 151.824 145.537 136.757 1.00 34.66 -1 801 TTP A O2G   1 
HETATM 15840 O  O3G   . TTP E 3 .   ? 150.385 145.656 134.776 1.00 32.64 ?  801 TTP A O3G   1 
HETATM 15841 O  "O5'" . TTP E 3 .   ? 146.588 144.525 134.428 1.00 20.09 ?  801 TTP A "O5'" 1 
HETATM 15842 C  "C5'" . TTP E 3 .   ? 147.565 143.992 133.541 1.00 18.36 ?  801 TTP A "C5'" 1 
HETATM 15843 C  "C4'" . TTP E 3 .   ? 147.106 142.634 133.038 1.00 19.42 ?  801 TTP A "C4'" 1 
HETATM 15844 O  "O4'" . TTP E 3 .   ? 146.692 141.829 134.140 1.00 27.75 ?  801 TTP A "O4'" 1 
HETATM 15845 C  "C3'" . TTP E 3 .   ? 145.924 142.760 132.096 1.00 24.14 ?  801 TTP A "C3'" 1 
HETATM 15846 O  "O3'" . TTP E 3 .   ? 146.309 142.421 130.760 1.00 27.74 ?  801 TTP A "O3'" 1 
HETATM 15847 C  "C2'" . TTP E 3 .   ? 144.877 141.792 132.612 1.00 26.46 ?  801 TTP A "C2'" 1 
HETATM 15848 C  "C1'" . TTP E 3 .   ? 145.513 141.096 133.808 1.00 23.44 ?  801 TTP A "C1'" 1 
HETATM 15849 N  N1    . TTP E 3 .   ? 144.620 141.067 134.969 1.00 24.28 ?  801 TTP A N1    1 
HETATM 15850 C  C2    . TTP E 3 .   ? 144.075 139.839 135.410 1.00 23.58 ?  801 TTP A C2    1 
HETATM 15851 O  O2    . TTP E 3 .   ? 144.352 138.787 134.799 1.00 22.85 ?  801 TTP A O2    1 
HETATM 15852 N  N3    . TTP E 3 .   ? 143.261 139.778 136.471 1.00 24.45 ?  801 TTP A N3    1 
HETATM 15853 C  C4    . TTP E 3 .   ? 142.945 140.883 137.147 1.00 27.61 ?  801 TTP A C4    1 
HETATM 15854 O  O4    . TTP E 3 .   ? 142.186 140.817 138.136 1.00 32.39 ?  801 TTP A O4    1 
HETATM 15855 C  C5    . TTP E 3 .   ? 143.503 142.185 136.711 1.00 23.22 ?  801 TTP A C5    1 
HETATM 15856 C  C5M   . TTP E 3 .   ? 143.176 143.459 137.442 1.00 25.93 ?  801 TTP A C5M   1 
HETATM 15857 C  C6    . TTP E 3 .   ? 144.342 142.207 135.609 1.00 25.04 ?  801 TTP A C6    1 
HETATM 15858 MG MG    . MG  F 4 .   ? 149.109 148.306 133.492 1.00 28.90 ?  802 MG  A MG    1 
HETATM 15859 P  PG    . ATP G 5 .   ? 107.842 139.526 80.712  1.00 69.04 ?  803 ATP A PG    1 
HETATM 15860 O  O1G   . ATP G 5 .   ? 108.240 140.648 79.813  1.00 55.92 ?  803 ATP A O1G   1 
HETATM 15861 O  O2G   . ATP G 5 .   ? 108.869 138.390 80.770  1.00 57.63 -1 803 ATP A O2G   1 
HETATM 15862 O  O3G   . ATP G 5 .   ? 107.508 139.973 82.139  1.00 56.73 ?  803 ATP A O3G   1 
HETATM 15863 P  PB    . ATP G 5 .   ? 105.459 137.713 80.624  1.00 63.99 ?  803 ATP A PB    1 
HETATM 15864 O  O1B   . ATP G 5 .   ? 104.071 138.217 80.607  1.00 56.62 -1 803 ATP A O1B   1 
HETATM 15865 O  O2B   . ATP G 5 .   ? 105.728 136.479 79.761  1.00 55.81 ?  803 ATP A O2B   1 
HETATM 15866 O  O3B   . ATP G 5 .   ? 106.503 138.831 80.184  1.00 55.92 ?  803 ATP A O3B   1 
HETATM 15867 P  PA    . ATP G 5 .   ? 106.101 136.070 82.999  1.00 63.15 ?  803 ATP A PA    1 
HETATM 15868 O  O1A   . ATP G 5 .   ? 107.190 135.198 82.515  1.00 58.46 -1 803 ATP A O1A   1 
HETATM 15869 O  O2A   . ATP G 5 .   ? 104.724 135.408 83.067  1.00 53.96 ?  803 ATP A O2A   1 
HETATM 15870 O  O3A   . ATP G 5 .   ? 105.949 137.372 82.099  1.00 54.74 ?  803 ATP A O3A   1 
HETATM 15871 O  "O5'" . ATP G 5 .   ? 106.434 136.666 84.422  1.00 52.95 ?  803 ATP A "O5'" 1 
HETATM 15872 C  "C5'" . ATP G 5 .   ? 105.583 137.657 85.036  1.00 52.93 ?  803 ATP A "C5'" 1 
HETATM 15873 C  "C4'" . ATP G 5 .   ? 106.432 138.658 85.775  1.00 53.43 ?  803 ATP A "C4'" 1 
HETATM 15874 O  "O4'" . ATP G 5 .   ? 107.072 137.947 86.853  1.00 52.51 ?  803 ATP A "O4'" 1 
HETATM 15875 C  "C3'" . ATP G 5 .   ? 107.614 139.106 84.932  1.00 53.48 ?  803 ATP A "C3'" 1 
HETATM 15876 O  "O3'" . ATP G 5 .   ? 107.199 140.302 84.286  1.00 57.07 ?  803 ATP A "O3'" 1 
HETATM 15877 C  "C2'" . ATP G 5 .   ? 108.604 139.530 86.011  1.00 52.44 ?  803 ATP A "C2'" 1 
HETATM 15878 O  "O2'" . ATP G 5 .   ? 108.054 140.693 86.615  1.00 53.71 ?  803 ATP A "O2'" 1 
HETATM 15879 C  "C1'" . ATP G 5 .   ? 108.396 138.420 87.044  1.00 52.98 ?  803 ATP A "C1'" 1 
HETATM 15880 N  N9    . ATP G 5 .   ? 109.282 137.289 86.796  1.00 54.37 ?  803 ATP A N9    1 
HETATM 15881 C  C8    . ATP G 5 .   ? 108.971 136.111 86.169  1.00 53.38 ?  803 ATP A C8    1 
HETATM 15882 N  N7    . ATP G 5 .   ? 109.970 135.267 86.086  1.00 53.37 ?  803 ATP A N7    1 
HETATM 15883 C  C5    . ATP G 5 .   ? 111.016 135.937 86.703  1.00 54.75 ?  803 ATP A C5    1 
HETATM 15884 C  C6    . ATP G 5 .   ? 112.358 135.588 86.946  1.00 49.48 ?  803 ATP A C6    1 
HETATM 15885 N  N6    . ATP G 5 .   ? 112.901 134.422 86.581  1.00 49.97 ?  803 ATP A N6    1 
HETATM 15886 N  N1    . ATP G 5 .   ? 113.136 136.486 87.588  1.00 51.18 ?  803 ATP A N1    1 
HETATM 15887 C  C2    . ATP G 5 .   ? 112.601 137.654 87.954  1.00 50.78 ?  803 ATP A C2    1 
HETATM 15888 N  N3    . ATP G 5 .   ? 111.353 138.093 87.781  1.00 51.81 ?  803 ATP A N3    1 
HETATM 15889 C  C4    . ATP G 5 .   ? 110.606 137.185 87.145  1.00 53.82 ?  803 ATP A C4    1 
HETATM 15890 P  PA    . TTP H 3 .   ? 120.099 149.535 124.736 1.00 10.25 ?  801 TTP B PA    1 
HETATM 15891 O  O1A   . TTP H 3 .   ? 121.601 149.603 124.827 1.00 21.91 -1 801 TTP B O1A   1 
HETATM 15892 O  O2A   . TTP H 3 .   ? 119.458 150.616 125.570 1.00 20.55 ?  801 TTP B O2A   1 
HETATM 15893 O  O3A   . TTP H 3 .   ? 119.623 149.614 123.203 1.00 30.28 ?  801 TTP B O3A   1 
HETATM 15894 P  PB    . TTP H 3 .   ? 118.918 150.939 122.627 1.00 25.31 ?  801 TTP B PB    1 
HETATM 15895 O  O1B   . TTP H 3 .   ? 118.967 152.082 123.610 1.00 34.69 -1 801 TTP B O1B   1 
HETATM 15896 O  O2B   . TTP H 3 .   ? 119.543 151.340 121.316 1.00 29.70 ?  801 TTP B O2B   1 
HETATM 15897 O  O3B   . TTP H 3 .   ? 117.417 150.411 122.404 1.00 18.55 ?  801 TTP B O3B   1 
HETATM 15898 P  PG    . TTP H 3 .   ? 116.177 151.079 123.178 1.00 20.18 ?  801 TTP B PG    1 
HETATM 15899 O  O1G   . TTP H 3 .   ? 115.788 152.379 122.521 1.00 28.67 ?  801 TTP B O1G   1 
HETATM 15900 O  O2G   . TTP H 3 .   ? 115.008 150.129 123.140 1.00 23.97 -1 801 TTP B O2G   1 
HETATM 15901 O  O3G   . TTP H 3 .   ? 116.557 151.339 124.614 1.00 31.12 ?  801 TTP B O3G   1 
HETATM 15902 O  "O5'" . TTP H 3 .   ? 119.570 148.085 125.180 1.00 18.75 ?  801 TTP B "O5'" 1 
HETATM 15903 C  "C5'" . TTP H 3 .   ? 118.429 147.976 126.026 1.00 15.35 ?  801 TTP B "C5'" 1 
HETATM 15904 C  "C4'" . TTP H 3 .   ? 118.426 146.620 126.717 1.00 17.50 ?  801 TTP B "C4'" 1 
HETATM 15905 O  "O4'" . TTP H 3 .   ? 118.535 145.576 125.751 1.00 27.35 ?  801 TTP B "O4'" 1 
HETATM 15906 C  "C3'" . TTP H 3 .   ? 119.597 146.474 127.673 1.00 18.41 ?  801 TTP B "C3'" 1 
HETATM 15907 O  "O3'" . TTP H 3 .   ? 119.154 146.551 129.031 1.00 29.17 ?  801 TTP B "O3'" 1 
HETATM 15908 C  "C2'" . TTP H 3 .   ? 120.200 145.114 127.380 1.00 24.62 ?  801 TTP B "C2'" 1 
HETATM 15909 C  "C1'" . TTP H 3 .   ? 119.376 144.530 126.240 1.00 24.54 ?  801 TTP B "C1'" 1 
HETATM 15910 N  N1    . TTP H 3 .   ? 120.234 144.045 125.156 1.00 22.26 ?  801 TTP B N1    1 
HETATM 15911 C  C2    . TTP H 3 .   ? 120.421 142.657 124.968 1.00 23.20 ?  801 TTP B C2    1 
HETATM 15912 O  O2    . TTP H 3 .   ? 119.853 141.849 125.731 1.00 25.71 ?  801 TTP B O2    1 
HETATM 15913 N  N3    . TTP H 3 .   ? 121.197 142.186 123.986 1.00 25.31 ?  801 TTP B N3    1 
HETATM 15914 C  C4    . TTP H 3 .   ? 121.818 143.022 123.150 1.00 28.09 ?  801 TTP B C4    1 
HETATM 15915 O  O4    . TTP H 3 .   ? 122.539 142.576 122.235 1.00 34.85 ?  801 TTP B O4    1 
HETATM 15916 C  C5    . TTP H 3 .   ? 121.639 144.483 123.323 1.00 24.84 ?  801 TTP B C5    1 
HETATM 15917 C  C5M   . TTP H 3 .   ? 122.320 145.465 122.407 1.00 23.82 ?  801 TTP B C5M   1 
HETATM 15918 C  C6    . TTP H 3 .   ? 120.830 144.931 124.351 1.00 25.14 ?  801 TTP B C6    1 
HETATM 15919 MG MG    . MG  I 4 .   ? 118.334 152.143 125.921 1.00 30.79 ?  802 MG  B MG    1 
HETATM 15920 P  PG    . ATP J 5 .   ? 156.658 139.817 179.600 1.00 72.82 ?  803 ATP B PG    1 
HETATM 15921 O  O1G   . ATP J 5 .   ? 156.211 140.898 180.526 1.00 63.31 ?  803 ATP B O1G   1 
HETATM 15922 O  O2G   . ATP J 5 .   ? 155.524 138.887 179.153 1.00 63.47 -1 803 ATP B O2G   1 
HETATM 15923 O  O3G   . ATP J 5 .   ? 157.402 140.334 178.366 1.00 63.49 ?  803 ATP B O3G   1 
HETATM 15924 P  PB    . ATP J 5 .   ? 158.124 137.316 180.358 1.00 73.44 ?  803 ATP B PB    1 
HETATM 15925 O  O1B   . ATP J 5 .   ? 159.591 137.145 180.411 1.00 63.09 -1 803 ATP B O1B   1 
HETATM 15926 O  O2B   . ATP J 5 .   ? 157.334 136.656 181.487 1.00 62.66 ?  803 ATP B O2B   1 
HETATM 15927 O  O3B   . ATP J 5 .   ? 157.705 138.852 180.327 1.00 63.04 ?  803 ATP B O3B   1 
HETATM 15928 P  PA    . ATP J 5 .   ? 157.075 135.384 178.377 1.00 71.06 ?  803 ATP B PA    1 
HETATM 15929 O  O1A   . ATP J 5 .   ? 155.875 134.855 179.056 1.00 63.87 -1 803 ATP B O1A   1 
HETATM 15930 O  O2A   . ATP J 5 .   ? 158.299 134.470 178.421 1.00 62.40 ?  803 ATP B O2A   1 
HETATM 15931 O  O3A   . ATP J 5 .   ? 157.518 136.785 178.986 1.00 63.62 ?  803 ATP B O3A   1 
HETATM 15932 O  "O5'" . ATP J 5 .   ? 156.776 135.739 176.868 1.00 58.80 ?  803 ATP B "O5'" 1 
HETATM 15933 C  "C5'" . ATP J 5 .   ? 157.806 136.264 176.005 1.00 60.43 ?  803 ATP B "C5'" 1 
HETATM 15934 C  "C4'" . ATP J 5 .   ? 157.187 137.188 174.991 1.00 61.61 ?  803 ATP B "C4'" 1 
HETATM 15935 O  "O4'" . ATP J 5 .   ? 156.296 136.390 174.190 1.00 63.32 ?  803 ATP B "O4'" 1 
HETATM 15936 C  "C3'" . ATP J 5 .   ? 156.227 138.165 175.647 1.00 61.44 ?  803 ATP B "C3'" 1 
HETATM 15937 O  "O3'" . ATP J 5 .   ? 156.991 139.332 175.923 1.00 63.49 ?  803 ATP B "O3'" 1 
HETATM 15938 C  "C2'" . ATP J 5 .   ? 155.318 138.523 174.475 1.00 59.36 ?  803 ATP B "C2'" 1 
HETATM 15939 O  "O2'" . ATP J 5 .   ? 156.103 139.315 173.594 1.00 59.29 ?  803 ATP B "O2'" 1 
HETATM 15940 C  "C1'" . ATP J 5 .   ? 155.189 137.169 173.768 1.00 61.36 ?  803 ATP B "C1'" 1 
HETATM 15941 N  N9    . ATP J 5 .   ? 153.990 136.459 174.193 1.00 60.50 ?  803 ATP B N9    1 
HETATM 15942 C  C8    . ATP J 5 .   ? 153.917 135.382 175.038 1.00 59.47 ?  803 ATP B C8    1 
HETATM 15943 N  N7    . ATP J 5 .   ? 152.699 134.943 175.242 1.00 60.62 ?  803 ATP B N7    1 
HETATM 15944 C  C5    . ATP J 5 .   ? 151.913 135.790 174.475 1.00 61.83 ?  803 ATP B C5    1 
HETATM 15945 C  C6    . ATP J 5 .   ? 150.524 135.860 174.256 1.00 57.82 ?  803 ATP B C6    1 
HETATM 15946 N  N6    . ATP J 5 .   ? 149.639 135.026 174.812 1.00 58.95 ?  803 ATP B N6    1 
HETATM 15947 N  N1    . ATP J 5 .   ? 150.065 136.827 173.432 1.00 58.92 ?  803 ATP B N1    1 
HETATM 15948 C  C2    . ATP J 5 .   ? 150.942 137.666 172.873 1.00 57.54 ?  803 ATP B C2    1 
HETATM 15949 N  N3    . ATP J 5 .   ? 152.269 137.697 173.005 1.00 59.67 ?  803 ATP B N3    1 
HETATM 15950 C  C4    . ATP J 5 .   ? 152.695 136.729 173.823 1.00 61.73 ?  803 ATP B C4    1 
HETATM 15951 MN MN    . MN  K 6 .   ? 118.965 96.809  121.339 0.85 25.05 ?  401 MN  C MN    1 
HETATM 15952 MN MN    . MN  L 6 .   ? 117.766 100.199 122.355 0.85 26.37 ?  402 MN  C MN    1 
HETATM 15953 MN MN    . MN  M 6 .   ? 138.097 101.441 135.269 1.00 22.51 ?  401 MN  D MN    1 
HETATM 15954 MN MN    . MN  N 6 .   ? 140.212 100.040 132.292 1.00 24.72 ?  402 MN  D MN    1 
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