data_9BYC
# 
_entry.id   9BYC 
# 
_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   9BYC         pdb_00009byc 10.2210/pdb9byc/pdb 
WWPDB D_1000284376 ?            ?                   
EMDB  EMD-45026    ?            ?                   
# 
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                        9BYC 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-23 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
EMDB .                                                                                            EMD-45018 'consensus EM volume'  
EMDB 'Class 12 model for product condition of Bacillus subtilis ribonucleotide reductase complex' EMD-45026 'associated EM volume' 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              nozomi.ando@cornell.edu 
_pdbx_contact_author.name_first         Nozomi 
_pdbx_contact_author.name_last          Ando 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7062-1644 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Xu, D.'       1 0000-0002-3879-039X 
'Thomas, W.C.' 2 0000-0001-5490-4900 
'Burnim, A.A.' 3 0000-0002-9962-1397 
'Ando, N.'     4 0000-0001-7062-1644 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                2458 
_citation.page_last                 2458 
_citation.title                     
'Conformational landscapes of a class I ribonucleotide reductase complex during turnover reveal intrinsic dynamics and asymmetry.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-57735-4 
_citation.pdbx_database_id_PubMed   40075098 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Xu, D.'       1 ? 
primary 'Thomas, W.C.' 2 ? 
primary 'Burnim, A.A.' 3 ? 
primary 'Ando, N.'     4 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Ribonucleoside-diphosphate reductase subunit alpha' 80791.469 2 1.17.4.1 ? ? ? 
2 polymer     man 'Ribonucleoside-diphosphate reductase subunit beta'  40720.992 2 1.17.4.1 ? ? ? 
3 non-polymer syn "THYMIDINE-5'-TRIPHOSPHATE"                          482.168   2 ?        ? ? ? 
4 non-polymer syn 'MAGNESIUM ION'                                      24.305    2 ?        ? ? ? 
5 non-polymer syn "ADENOSINE-5'-TRIPHOSPHATE"                          507.181   2 ?        ? ? ? 
6 non-polymer syn "2'-DEOXYGUANOSINE-5'-DIPHOSPHATE"                   427.201   2 ?        ? ? ? 
7 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 "2'-DEOXYGUANOSINE-5'-DIPHOSPHATE" DGI 
7 '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 
DGI 'DNA linking'       n "2'-DEOXYGUANOSINE-5'-DIPHOSPHATE" ? 'C10 H15 N5 O10 P2' 427.201 
GLN 'L-peptide linking' y GLUTAMINE                          ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                    ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                            ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                          ? 'C6 H10 N3 O2 1'    156.162 
ILE 'L-peptide linking' y ISOLEUCINE                         ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                            ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                             ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                         ? 'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION'                    ? 'Mg 2'              24.305  
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 330 309 309 LYS LYS C . n 
C 2 331 ALA 331 310 310 ALA ALA C . n 
C 2 332 THR 332 311 311 THR THR C . n 
C 2 333 VAL 333 312 312 VAL VAL C . n 
C 2 334 GLU 334 313 313 GLU GLU C . n 
C 2 335 PRO 335 314 314 PRO PRO C . n 
C 2 336 LEU 336 315 315 LEU LEU C . n 
C 2 337 LYS 337 316 316 LYS LYS C . n 
C 2 338 ASP 338 317 317 ASP ASP C . n 
C 2 339 ASP 339 318 318 ASP ASP C . n 
C 2 340 ASP 340 319 319 ASP ASP C . n 
C 2 341 PHE 341 320 320 PHE PHE C . n 
C 2 342 TYR 342 321 321 TYR TYR C . n 
C 2 343 PHE 343 322 322 PHE PHE C . n 
C 2 344 GLU 344 323 ?   ?   ?   C . n 
C 2 345 ASP 345 324 ?   ?   ?   C . n 
C 2 346 GLU 346 325 ?   ?   ?   C . n 
C 2 347 LYS 347 326 ?   ?   ?   C . n 
C 2 348 GLU 348 327 ?   ?   ?   C . n 
C 2 349 GLN 349 328 ?   ?   ?   C . n 
C 2 350 ILE 350 329 ?   ?   ?   C . n 
D 2 1   MET 1   -20 ?   ?   ?   D . n 
D 2 2   GLY 2   -19 ?   ?   ?   D . n 
D 2 3   SER 3   -18 ?   ?   ?   D . n 
D 2 4   SER 4   -17 ?   ?   ?   D . n 
D 2 5   HIS 5   -16 ?   ?   ?   D . n 
D 2 6   HIS 6   -15 ?   ?   ?   D . n 
D 2 7   HIS 7   -14 ?   ?   ?   D . n 
D 2 8   HIS 8   -13 ?   ?   ?   D . n 
D 2 9   HIS 9   -12 ?   ?   ?   D . n 
D 2 10  HIS 10  -11 ?   ?   ?   D . n 
D 2 11  SER 11  -10 ?   ?   ?   D . n 
D 2 12  SER 12  -9  ?   ?   ?   D . n 
D 2 13  GLY 13  -8  ?   ?   ?   D . n 
D 2 14  LEU 14  -7  ?   ?   ?   D . n 
D 2 15  VAL 15  -6  ?   ?   ?   D . n 
D 2 16  PRO 16  -5  ?   ?   ?   D . n 
D 2 17  ARG 17  -4  ?   ?   ?   D . n 
D 2 18  GLY 18  -3  ?   ?   ?   D . n 
D 2 19  SER 19  -2  ?   ?   ?   D . n 
D 2 20  HIS 20  -1  ?   ?   ?   D . n 
D 2 21  MET 21  0   ?   ?   ?   D . n 
D 2 22  MET 22  1   ?   ?   ?   D . n 
D 2 23  THR 23  2   ?   ?   ?   D . n 
D 2 24  LYS 24  3   ?   ?   ?   D . n 
D 2 25  ILE 25  4   ?   ?   ?   D . n 
D 2 26  TYR 26  5   ?   ?   ?   D . n 
D 2 27  ASP 27  6   ?   ?   ?   D . n 
D 2 28  ALA 28  7   ?   ?   ?   D . n 
D 2 29  ALA 29  8   ?   ?   ?   D . n 
D 2 30  ASN 30  9   ?   ?   ?   D . n 
D 2 31  TRP 31  10  ?   ?   ?   D . n 
D 2 32  SER 32  11  ?   ?   ?   D . n 
D 2 33  LYS 33  12  ?   ?   ?   D . n 
D 2 34  HIS 34  13  ?   ?   ?   D . n 
D 2 35  GLU 35  14  ?   ?   ?   D . n 
D 2 36  ASP 36  15  ?   ?   ?   D . n 
D 2 37  ASP 37  16  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 330 309 309 LYS LYS D . n 
D 2 331 ALA 331 310 310 ALA ALA D . n 
D 2 332 THR 332 311 311 THR THR D . n 
D 2 333 VAL 333 312 312 VAL VAL D . n 
D 2 334 GLU 334 313 313 GLU GLU D . n 
D 2 335 PRO 335 314 314 PRO PRO D . n 
D 2 336 LEU 336 315 315 LEU LEU D . n 
D 2 337 LYS 337 316 316 LYS LYS D . n 
D 2 338 ASP 338 317 317 ASP ASP D . n 
D 2 339 ASP 339 318 318 ASP ASP D . n 
D 2 340 ASP 340 319 319 ASP ASP D . n 
D 2 341 PHE 341 320 320 PHE PHE D . n 
D 2 342 TYR 342 321 321 TYR TYR D . n 
D 2 343 PHE 343 322 322 PHE PHE D . n 
D 2 344 GLU 344 323 ?   ?   ?   D . n 
D 2 345 ASP 345 324 ?   ?   ?   D . n 
D 2 346 GLU 346 325 ?   ?   ?   D . n 
D 2 347 LYS 347 326 ?   ?   ?   D . n 
D 2 348 GLU 348 327 ?   ?   ?   D . n 
D 2 349 GLN 349 328 ?   ?   ?   D . n 
D 2 350 ILE 350 329 ?   ?   ?   D . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 ATP ? ? ATP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 DGI ? ? DGI ? ? 'SUBJECT OF INVESTIGATION' ? 
3 MG  ? ? MG  ? ? 'SUBJECT OF INVESTIGATION' ? 
4 MN  ? ? MN  ? ? 'SUBJECT OF INVESTIGATION' ? 
5 TTP ? ? TTP ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 3 TTP 1 801 801 TTP TTP A . 
F 4 MG  1 802 802 MG  MG  A . 
G 5 ATP 1 803 803 ATP ATP A . 
H 6 DGI 1 804 804 DGI DGI A . 
I 3 TTP 1 801 801 TTP TTP B . 
J 4 MG  1 802 802 MG  MG  B . 
K 5 ATP 1 803 803 ATP ATP B . 
L 6 DGI 1 804 804 DGI DGI B . 
M 7 MN  1 401 401 MN  MN  C . 
N 7 MN  1 402 402 MN  MN  C . 
O 7 MN  1 401 401 MN  MN  D . 
P 7 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                   9BYC 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9BYC 
_struct.title                        'Class 12 model for product condition of Bacillus subtilis ribonucleotide reductase complex' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9BYC 
_struct_keywords.text            'Ribonucleotide Reductase, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 6 ? 
I N N 3 ? 
J N N 4 ? 
K N N 5 ? 
L N N 6 ? 
M N N 7 ? 
N N N 7 ? 
O N N 7 ? 
P N N 7 ? 
# 
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 9BYC A 1  ? 700 ? P50620 1 ? 700 ? 1 700 
2 1 9BYC B 1  ? 700 ? P50620 1 ? 700 ? 1 700 
3 2 9BYC C 22 ? 350 ? P50621 1 ? 329 ? 1 329 
4 2 9BYC 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 9BYC MET C 1  ? UNP P50621 ? ? 'initiating methionine' -20 1  
3 9BYC GLY C 2  ? UNP P50621 ? ? 'expression tag'        -19 2  
3 9BYC SER C 3  ? UNP P50621 ? ? 'expression tag'        -18 3  
3 9BYC SER C 4  ? UNP P50621 ? ? 'expression tag'        -17 4  
3 9BYC HIS C 5  ? UNP P50621 ? ? 'expression tag'        -16 5  
3 9BYC HIS C 6  ? UNP P50621 ? ? 'expression tag'        -15 6  
3 9BYC HIS C 7  ? UNP P50621 ? ? 'expression tag'        -14 7  
3 9BYC HIS C 8  ? UNP P50621 ? ? 'expression tag'        -13 8  
3 9BYC HIS C 9  ? UNP P50621 ? ? 'expression tag'        -12 9  
3 9BYC HIS C 10 ? UNP P50621 ? ? 'expression tag'        -11 10 
3 9BYC SER C 11 ? UNP P50621 ? ? 'expression tag'        -10 11 
3 9BYC SER C 12 ? UNP P50621 ? ? 'expression tag'        -9  12 
3 9BYC GLY C 13 ? UNP P50621 ? ? 'expression tag'        -8  13 
3 9BYC LEU C 14 ? UNP P50621 ? ? 'expression tag'        -7  14 
3 9BYC VAL C 15 ? UNP P50621 ? ? 'expression tag'        -6  15 
3 9BYC PRO C 16 ? UNP P50621 ? ? 'expression tag'        -5  16 
3 9BYC ARG C 17 ? UNP P50621 ? ? 'expression tag'        -4  17 
3 9BYC GLY C 18 ? UNP P50621 ? ? 'expression tag'        -3  18 
3 9BYC SER C 19 ? UNP P50621 ? ? 'expression tag'        -2  19 
3 9BYC HIS C 20 ? UNP P50621 ? ? 'expression tag'        -1  20 
3 9BYC MET C 21 ? UNP P50621 ? ? 'expression tag'        0   21 
4 9BYC MET D 1  ? UNP P50621 ? ? 'initiating methionine' -20 22 
4 9BYC GLY D 2  ? UNP P50621 ? ? 'expression tag'        -19 23 
4 9BYC SER D 3  ? UNP P50621 ? ? 'expression tag'        -18 24 
4 9BYC SER D 4  ? UNP P50621 ? ? 'expression tag'        -17 25 
4 9BYC HIS D 5  ? UNP P50621 ? ? 'expression tag'        -16 26 
4 9BYC HIS D 6  ? UNP P50621 ? ? 'expression tag'        -15 27 
4 9BYC HIS D 7  ? UNP P50621 ? ? 'expression tag'        -14 28 
4 9BYC HIS D 8  ? UNP P50621 ? ? 'expression tag'        -13 29 
4 9BYC HIS D 9  ? UNP P50621 ? ? 'expression tag'        -12 30 
4 9BYC HIS D 10 ? UNP P50621 ? ? 'expression tag'        -11 31 
4 9BYC SER D 11 ? UNP P50621 ? ? 'expression tag'        -10 32 
4 9BYC SER D 12 ? UNP P50621 ? ? 'expression tag'        -9  33 
4 9BYC GLY D 13 ? UNP P50621 ? ? 'expression tag'        -8  34 
4 9BYC LEU D 14 ? UNP P50621 ? ? 'expression tag'        -7  35 
4 9BYC VAL D 15 ? UNP P50621 ? ? 'expression tag'        -6  36 
4 9BYC PRO D 16 ? UNP P50621 ? ? 'expression tag'        -5  37 
4 9BYC ARG D 17 ? UNP P50621 ? ? 'expression tag'        -4  38 
4 9BYC GLY D 18 ? UNP P50621 ? ? 'expression tag'        -3  39 
4 9BYC SER D 19 ? UNP P50621 ? ? 'expression tag'        -2  40 
4 9BYC HIS D 20 ? UNP P50621 ? ? 'expression tag'        -1  41 
4 9BYC 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,O,P 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 7   ? ASN A 14  ? PRO A 7   ASN A 14  1 ? 8  
HELX_P HELX_P2  AA2 GLU A 15  ? MET A 17  ? GLU A 15  MET A 17  5 ? 3  
HELX_P HELX_P3  AA3 ASP A 27  ? TYR A 40  ? ASP A 27  TYR A 40  1 ? 14 
HELX_P HELX_P4  AA4 TYR A 40  ? THR A 45  ? TYR A 40  THR A 45  1 ? 6  
HELX_P HELX_P5  AA5 ASN A 50  ? ASN A 61  ? ASN A 50  ASN A 61  1 ? 12 
HELX_P HELX_P6  AA6 GLU A 65  ? SER A 70  ? GLU A 65  SER A 70  1 ? 6  
HELX_P HELX_P7  AA7 SER A 73  ? LYS A 87  ? SER A 73  LYS A 87  1 ? 15 
HELX_P HELX_P8  AA8 SER A 93  ? TYR A 104 ? SER A 93  TYR A 104 1 ? 12 
HELX_P HELX_P9  AA9 ARG A 117 ? ASN A 131 ? ARG A 117 ASN A 131 1 ? 15 
HELX_P HELX_P10 AB1 ASP A 133 ? ASN A 146 ? ASP A 133 ASN A 146 1 ? 14 
HELX_P HELX_P11 AB2 SER A 152 ? ALA A 159 ? SER A 152 ALA A 159 1 ? 8  
HELX_P HELX_P12 AB3 SER A 178 ? LEU A 195 ? SER A 178 LEU A 195 1 ? 18 
HELX_P HELX_P13 AB4 GLY A 222 ? ALA A 237 ? GLY A 222 ALA A 237 1 ? 16 
HELX_P HELX_P14 AB5 ASP A 238 ? GLN A 242 ? ASP A 238 GLN A 242 5 ? 5  
HELX_P HELX_P15 AB6 ASP A 257 ? THR A 264 ? ASP A 257 THR A 264 1 ? 8  
HELX_P HELX_P16 AB7 PRO A 285 ? GLU A 294 ? PRO A 285 GLU A 294 1 ? 10 
HELX_P HELX_P17 AB8 TYR A 302 ? GLY A 311 ? TYR A 302 GLY A 311 1 ? 10 
HELX_P HELX_P18 AB9 HIS A 313 ? MET A 317 ? HIS A 313 MET A 317 5 ? 5  
HELX_P HELX_P19 AC1 ASP A 318 ? ASN A 329 ? ASP A 318 ASN A 329 1 ? 12 
HELX_P HELX_P20 AC2 ASN A 338 ? GLY A 354 ? ASN A 338 GLY A 354 1 ? 17 
HELX_P HELX_P21 AC3 GLN A 361 ? LYS A 366 ? GLN A 361 LYS A 366 1 ? 6  
HELX_P HELX_P22 AC4 ILE A 416 ? LYS A 423 ? ILE A 416 LYS A 423 1 ? 8  
HELX_P HELX_P23 AC5 SER A 424 ? THR A 443 ? SER A 424 THR A 443 1 ? 20 
HELX_P HELX_P24 AC6 ALA A 448 ? LYS A 459 ? ALA A 448 LYS A 459 1 ? 12 
HELX_P HELX_P25 AC7 ASN A 467 ? GLN A 474 ? ASN A 467 GLN A 474 1 ? 8  
HELX_P HELX_P26 AC8 SER A 481 ? GLY A 511 ? SER A 481 GLY A 511 1 ? 31 
HELX_P HELX_P27 AC9 SER A 520 ? GLY A 525 ? SER A 520 GLY A 525 1 ? 6  
HELX_P HELX_P28 AD1 PHE A 528 ? THR A 534 ? PHE A 528 THR A 534 1 ? 7  
HELX_P HELX_P29 AD2 TYR A 540 ? PHE A 547 ? TYR A 540 PHE A 547 1 ? 8  
HELX_P HELX_P30 AD3 THR A 554 ? GLY A 569 ? THR A 554 GLY A 569 1 ? 16 
HELX_P HELX_P31 AD4 SER A 583 ? GLN A 588 ? SER A 583 GLN A 588 1 ? 6  
HELX_P HELX_P32 AD5 GLU A 628 ? MET A 632 ? GLU A 628 MET A 632 5 ? 5  
HELX_P HELX_P33 AD6 ASP A 633 ? GLN A 646 ? ASP A 633 GLN A 646 1 ? 14 
HELX_P HELX_P34 AD7 THR A 663 ? ARG A 677 ? THR A 663 ARG A 677 1 ? 15 
HELX_P HELX_P35 AD8 PRO B 7   ? GLU B 15  ? PRO B 7   GLU B 15  1 ? 9  
HELX_P HELX_P36 AD9 ASP B 27  ? THR B 45  ? ASP B 27  THR B 45  1 ? 19 
HELX_P HELX_P37 AE1 ASN B 50  ? ASN B 61  ? ASN B 50  ASN B 61  1 ? 12 
HELX_P HELX_P38 AE2 GLU B 65  ? SER B 70  ? GLU B 65  SER B 70  1 ? 6  
HELX_P HELX_P39 AE3 SER B 73  ? LYS B 87  ? SER B 73  LYS B 87  1 ? 15 
HELX_P HELX_P40 AE4 SER B 93  ? TYR B 104 ? SER B 93  TYR B 104 1 ? 12 
HELX_P HELX_P41 AE5 ARG B 117 ? ASN B 131 ? ARG B 117 ASN B 131 1 ? 15 
HELX_P HELX_P42 AE6 ASP B 133 ? ASN B 146 ? ASP B 133 ASN B 146 1 ? 14 
HELX_P HELX_P43 AE7 SER B 152 ? ALA B 159 ? SER B 152 ALA B 159 1 ? 8  
HELX_P HELX_P44 AE8 SER B 178 ? LEU B 195 ? SER B 178 LEU B 195 1 ? 18 
HELX_P HELX_P45 AE9 GLY B 222 ? ALA B 237 ? GLY B 222 ALA B 237 1 ? 16 
HELX_P HELX_P46 AF1 ASP B 257 ? THR B 264 ? ASP B 257 THR B 264 1 ? 8  
HELX_P HELX_P47 AF2 PRO B 285 ? GLU B 294 ? PRO B 285 GLU B 294 1 ? 10 
HELX_P HELX_P48 AF3 TYR B 302 ? GLY B 311 ? TYR B 302 GLY B 311 1 ? 10 
HELX_P HELX_P49 AF4 HIS B 313 ? MET B 317 ? HIS B 313 MET B 317 5 ? 5  
HELX_P HELX_P50 AF5 ASP B 318 ? ASN B 329 ? ASP B 318 ASN B 329 1 ? 12 
HELX_P HELX_P51 AF6 ASN B 338 ? GLY B 354 ? ASN B 338 GLY B 354 1 ? 17 
HELX_P HELX_P52 AF7 GLN B 361 ? LYS B 366 ? GLN B 361 LYS B 366 1 ? 6  
HELX_P HELX_P53 AF8 ILE B 416 ? LYS B 423 ? ILE B 416 LYS B 423 1 ? 8  
HELX_P HELX_P54 AF9 SER B 424 ? THR B 443 ? SER B 424 THR B 443 1 ? 20 
HELX_P HELX_P55 AG1 ALA B 448 ? LYS B 459 ? ALA B 448 LYS B 459 1 ? 12 
HELX_P HELX_P56 AG2 ASN B 467 ? GLN B 474 ? ASN B 467 GLN B 474 1 ? 8  
HELX_P HELX_P57 AG3 SER B 481 ? GLY B 511 ? SER B 481 GLY B 511 1 ? 31 
HELX_P HELX_P58 AG4 SER B 520 ? GLY B 525 ? SER B 520 GLY B 525 1 ? 6  
HELX_P HELX_P59 AG5 PHE B 528 ? THR B 534 ? PHE B 528 THR B 534 1 ? 7  
HELX_P HELX_P60 AG6 TYR B 540 ? PHE B 547 ? TYR B 540 PHE B 547 1 ? 8  
HELX_P HELX_P61 AG7 THR B 554 ? GLY B 569 ? THR B 554 GLY B 569 1 ? 16 
HELX_P HELX_P62 AG8 SER B 583 ? GLN B 588 ? SER B 583 GLN B 588 1 ? 6  
HELX_P HELX_P63 AG9 ASP B 633 ? GLN B 646 ? ASP B 633 GLN B 646 1 ? 14 
HELX_P HELX_P64 AH1 THR B 663 ? ARG B 677 ? THR B 663 ARG B 677 1 ? 15 
HELX_P HELX_P65 AH2 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 ? ? ? ? ? ? ? 2.048 ? ? 
metalc2  metalc ? ? E TTP .   O2B ? ? ? 1_555 F MG . MG ? ? A TTP 801 A MG 802 1_555 ? ? ? ? ? ? ? 2.471 ? ? 
metalc3  metalc ? ? E TTP .   O1G ? ? ? 1_555 F MG . MG ? ? A TTP 801 A MG 802 1_555 ? ? ? ? ? ? ? 2.484 ? ? 
metalc4  metalc ? ? I TTP .   O2A ? ? ? 1_555 J MG . MG ? ? B TTP 801 B MG 802 1_555 ? ? ? ? ? ? ? 2.343 ? ? 
metalc5  metalc ? ? I TTP .   O3G ? ? ? 1_555 J MG . MG ? ? B TTP 801 B MG 802 1_555 ? ? ? ? ? ? ? 2.104 ? ? 
metalc6  metalc ? ? C ASP 87  OD1 ? ? ? 1_555 N MN . MN ? ? C ASP 66  C MN 402 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
metalc7  metalc ? ? C GLU 118 OE2 ? ? ? 1_555 M MN . MN ? ? C GLU 97  C MN 401 1_555 ? ? ? ? ? ? ? 1.960 ? ? 
metalc8  metalc ? ? C GLU 118 OE1 ? ? ? 1_555 N MN . MN ? ? C GLU 97  C MN 402 1_555 ? ? ? ? ? ? ? 2.113 ? ? 
metalc9  metalc ? ? C HIS 122 ND1 ? ? ? 1_555 N MN . MN ? ? C HIS 101 C MN 402 1_555 ? ? ? ? ? ? ? 2.176 ? ? 
metalc10 metalc ? ? C GLU 185 OE1 ? ? ? 1_555 M MN . MN ? ? C GLU 164 C MN 401 1_555 ? ? ? ? ? ? ? 2.129 ? ? 
metalc11 metalc ? ? C GLU 185 OE2 ? ? ? 1_555 M MN . MN ? ? C GLU 164 C MN 401 1_555 ? ? ? ? ? ? ? 1.965 ? ? 
metalc12 metalc ? ? C GLU 219 OE1 ? ? ? 1_555 M MN . MN ? ? C GLU 198 C MN 401 1_555 ? ? ? ? ? ? ? 2.172 ? ? 
metalc13 metalc ? ? C GLU 219 OE1 ? ? ? 1_555 N MN . MN ? ? C GLU 198 C MN 402 1_555 ? ? ? ? ? ? ? 2.710 ? ? 
metalc14 metalc ? ? C GLU 219 OE2 ? ? ? 1_555 N MN . MN ? ? C GLU 198 C MN 402 1_555 ? ? ? ? ? ? ? 2.095 ? ? 
metalc15 metalc ? ? C HIS 222 ND1 ? ? ? 1_555 M MN . MN ? ? C HIS 201 C MN 401 1_555 ? ? ? ? ? ? ? 2.409 ? ? 
metalc16 metalc ? ? D ASP 87  OD1 ? ? ? 1_555 P MN . MN ? ? D ASP 66  D MN 402 1_555 ? ? ? ? ? ? ? 2.327 ? ? 
metalc17 metalc ? ? D ASP 87  OD2 ? ? ? 1_555 P MN . MN ? ? D ASP 66  D MN 402 1_555 ? ? ? ? ? ? ? 2.157 ? ? 
metalc18 metalc ? ? D GLU 118 OE2 ? ? ? 1_555 O MN . MN ? ? D GLU 97  D MN 401 1_555 ? ? ? ? ? ? ? 1.911 ? ? 
metalc19 metalc ? ? D GLU 118 OE1 ? ? ? 1_555 P MN . MN ? ? D GLU 97  D MN 402 1_555 ? ? ? ? ? ? ? 1.991 ? ? 
metalc20 metalc ? ? D HIS 122 ND1 ? ? ? 1_555 P MN . MN ? ? D HIS 101 D MN 402 1_555 ? ? ? ? ? ? ? 2.147 ? ? 
metalc21 metalc ? ? D GLU 185 OE1 ? ? ? 1_555 O MN . MN ? ? D GLU 164 D MN 401 1_555 ? ? ? ? ? ? ? 2.304 ? ? 
metalc22 metalc ? ? D GLU 185 OE2 ? ? ? 1_555 O MN . MN ? ? D GLU 164 D MN 401 1_555 ? ? ? ? ? ? ? 2.318 ? ? 
metalc23 metalc ? ? D GLU 219 OE1 ? ? ? 1_555 O MN . MN ? ? D GLU 198 D MN 401 1_555 ? ? ? ? ? ? ? 2.082 ? ? 
metalc24 metalc ? ? D GLU 219 OE2 ? ? ? 1_555 P MN . MN ? ? D GLU 198 D MN 402 1_555 ? ? ? ? ? ? ? 2.084 ? ? 
metalc25 metalc ? ? D HIS 222 ND1 ? ? ? 1_555 O 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 O2B ? E TTP .   ? A TTP 801 ? 1_555 71.9  ? 
2  O2A ? E TTP .   ? A TTP 801 ? 1_555 MG ? F MG . ? A MG 802 ? 1_555 O1G ? E TTP .   ? A TTP 801 ? 1_555 88.8  ? 
3  O2B ? E TTP .   ? A TTP 801 ? 1_555 MG ? F MG . ? A MG 802 ? 1_555 O1G ? E TTP .   ? A TTP 801 ? 1_555 68.1  ? 
4  O2A ? I TTP .   ? B TTP 801 ? 1_555 MG ? J MG . ? B MG 802 ? 1_555 O3G ? I TTP .   ? B TTP 801 ? 1_555 102.3 ? 
5  OD1 ? C ASP 87  ? C ASP 66  ? 1_555 MN ? N MN . ? C MN 402 ? 1_555 OE1 ? C GLU 118 ? C GLU 97  ? 1_555 89.5  ? 
6  OD1 ? C ASP 87  ? C ASP 66  ? 1_555 MN ? N 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 ? N 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 ? N 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 ? N 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 ? N 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 ? N 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 ? N 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 ? N 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 ? N 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 ? M 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 ? M 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 ? M 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 ? M 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 ? M 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 ? M 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 ? M 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 ? M 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 ? M MN . ? C MN 401 ? 1_555 ND1 ? C HIS 222 ? C HIS 201 ? 1_555 103.9 ? 
24 OE1 ? C GLU 219 ? C GLU 198 ? 1_555 MN ? M 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 ? P 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 ? P 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 ? P 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 ? P 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 ? P MN . ? D MN 402 ? 1_555 ND1 ? D HIS 122 ? D HIS 101 ? 1_555 107.0 ? 
30 OE1 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? P 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 ? P 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 ? P 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 ? P MN . ? D MN 402 ? 1_555 OE2 ? D GLU 219 ? D GLU 198 ? 1_555 122.1 ? 
34 ND1 ? D HIS 122 ? D HIS 101 ? 1_555 MN ? P MN . ? D MN 402 ? 1_555 OE2 ? D GLU 219 ? D GLU 198 ? 1_555 96.6  ? 
35 OE2 ? D GLU 118 ? D GLU 97  ? 1_555 MN ? O 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 ? O MN . ? D MN 401 ? 1_555 OE2 ? D GLU 185 ? D GLU 164 ? 1_555 99.7  ? 
37 OE1 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? O 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 ? O 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 ? O 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 ? O 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 ? O 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 ? O MN . ? D MN 401 ? 1_555 ND1 ? D HIS 222 ? D HIS 201 ? 1_555 102.9 ? 
43 OE2 ? D GLU 185 ? D GLU 164 ? 1_555 MN ? O 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 ? O 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 1.27  
2 TYR 355 B . ? TYR 355 B PRO 356 B ? PRO 356 B 1 -0.29 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 3 ? 
AA7 ? 6 ? 
AA8 ? 2 ? 
AA9 ? 2 ? 
AB1 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? parallel      
AA6 1 2 ? anti-parallel 
AA6 2 3 ? parallel      
AA7 1 2 ? parallel      
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA7 4 5 ? parallel      
AA7 5 6 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AB1 1 2 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TYR A 149 ? PRO A 151 ? TYR A 149 PRO A 151 
AA1 2 ASN A 410 ? ASN A 415 ? ASN A 410 ASN A 415 
AA1 3 ILE A 461 ? MET A 466 ? ILE A 461 MET A 466 
AA2 1 ILE A 407 ? SER A 408 ? ILE A 407 SER A 408 
AA2 2 CYS A 170 ? GLU A 174 ? CYS A 170 GLU A 174 
AA2 3 GLY A 198 ? ASN A 202 ? GLY A 198 ASN A 202 
AA2 4 GLY A 247 ? ASN A 252 ? GLY A 247 ASN A 252 
AA2 5 LEU A 278 ? ILE A 284 ? LEU A 278 ILE A 284 
AA2 6 TYR A 357 ? PHE A 360 ? TYR A 357 PHE A 360 
AA2 7 THR A 681 ? ILE A 682 ? THR A 681 ILE A 682 
AA3 1 ALA A 298 ? PHE A 301 ? ALA A 298 PHE A 301 
AA3 2 LYS A 334 ? ILE A 337 ? LYS A 334 ILE A 337 
AA4 1 ILE A 601 ? TYR A 606 ? ILE A 601 TYR A 606 
AA4 2 SER A 609 ? PRO A 614 ? SER A 609 PRO A 614 
AA5 1 THR A 655 ? LEU A 658 ? THR A 655 LEU A 658 
AA5 2 TYR A 684 ? THR A 687 ? TYR A 684 THR A 687 
AA6 1 TYR B 149 ? PRO B 151 ? TYR B 149 PRO B 151 
AA6 2 ASN B 410 ? ASN B 415 ? ASN B 410 ASN B 415 
AA6 3 ILE B 461 ? MET B 466 ? ILE B 461 MET B 466 
AA7 1 CYS B 170 ? GLU B 174 ? CYS B 170 GLU B 174 
AA7 2 GLY B 198 ? ASN B 202 ? GLY B 198 ASN B 202 
AA7 3 GLY B 247 ? ASN B 252 ? GLY B 247 ASN B 252 
AA7 4 LEU B 278 ? ILE B 284 ? LEU B 278 ILE B 284 
AA7 5 TYR B 357 ? PHE B 360 ? TYR B 357 PHE B 360 
AA7 6 THR B 681 ? ILE B 682 ? THR B 681 ILE B 682 
AA8 1 ALA B 298 ? PHE B 301 ? ALA B 298 PHE B 301 
AA8 2 LYS B 334 ? ILE B 337 ? LYS B 334 ILE B 337 
AA9 1 ILE B 601 ? TYR B 606 ? ILE B 601 TYR B 606 
AA9 2 SER B 609 ? PRO B 614 ? SER B 609 PRO B 614 
AB1 1 THR B 655 ? LEU B 658 ? THR B 655 LEU B 658 
AB1 2 TYR B 684 ? THR B 687 ? TYR B 684 THR B 687 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLN A 150 ? N GLN A 150 O SER A 413 ? O SER A 413 
AA1 2 3 N GLY A 412 ? N GLY A 412 O GLY A 464 ? O GLY A 464 
AA2 1 2 O ILE A 407 ? O ILE A 407 N LEU A 172 ? N LEU A 172 
AA2 2 3 N LEU A 173 ? N LEU A 173 O SER A 200 ? O SER A 200 
AA2 3 4 N LEU A 201 ? N LEU A 201 O ALA A 248 ? O ALA A 248 
AA2 4 5 N GLY A 247 ? N GLY A 247 O SER A 279 ? O SER A 279 
AA2 5 6 N VAL A 282 ? N VAL A 282 O TYR A 357 ? O TYR A 357 
AA2 6 7 N ILE A 358 ? N ILE A 358 O ILE A 682 ? O ILE A 682 
AA3 1 2 N VAL A 300 ? N VAL A 300 O GLU A 335 ? O GLU A 335 
AA4 1 2 N GLU A 602 ? N GLU A 602 O TYR A 613 ? O TYR A 613 
AA5 1 2 N LEU A 656 ? N LEU A 656 O TYR A 684 ? O TYR A 684 
AA6 1 2 N GLN B 150 ? N GLN B 150 O SER B 413 ? O SER B 413 
AA6 2 3 N GLY B 412 ? N GLY B 412 O GLY B 464 ? O GLY B 464 
AA7 1 2 N LEU B 173 ? N LEU B 173 O SER B 200 ? O SER B 200 
AA7 2 3 N LEU B 201 ? N LEU B 201 O TYR B 250 ? O TYR B 250 
AA7 3 4 N GLY B 247 ? N GLY B 247 O SER B 279 ? O SER B 279 
AA7 4 5 N VAL B 282 ? N VAL B 282 O TYR B 357 ? O TYR B 357 
AA7 5 6 N ILE B 358 ? N ILE B 358 O ILE B 682 ? O ILE B 682 
AA8 1 2 N ALA B 298 ? N ALA B 298 O ILE B 337 ? O ILE B 337 
AA9 1 2 N ARG B 604 ? N ARG B 604 O THR B 611 ? O THR B 611 
AB1 1 2 N LEU B 656 ? N LEU B 656 O TYR B 684 ? O TYR B 684 
# 
_pdbx_entry_details.entry_id                   9BYC 
_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   A CYS 382 ? ? OG  A SER 653 ? ? 2.13 
2 1 O   B PRO 616 ? ? OH  B TYR 626 ? ? 2.13 
3 1 O   A PRO 616 ? ? OH  A TYR 626 ? ? 2.14 
4 1 ND2 B ASN 608 ? ? CA  D GLU 278 ? ? 2.18 
5 1 NH2 D ARG 86  ? ? OE1 D GLU 211 ? ? 2.18 
6 1 O   B CYS 382 ? ? OG  B SER 653 ? ? 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 MET A 240 ? ? 72.15   -7.43   
2  1 SER A 593 ? ? 59.73   -154.77 
3  1 SER A 653 ? ? -68.93  99.31   
4  1 ASP B 215 ? ? 79.64   -0.91   
5  1 ASP B 238 ? ? -95.50  31.31   
6  1 SER B 408 ? ? -160.51 113.50  
7  1 SER B 593 ? ? 58.47   -151.23 
8  1 THR C 72  ? ? -128.04 -59.10  
9  1 ASP C 148 ? ? 58.11   15.66   
10 1 PHE C 166 ? ? -125.61 -60.81  
11 1 THR D 72  ? ? -128.19 -58.44  
12 1 PHE D 166 ? ? -144.18 -61.17  
13 1 THR D 311 ? ? -168.67 116.05  
14 1 ASP D 317 ? ? 61.69   167.65  
15 1 ASP D 318 ? ? 67.15   -4.07   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BYC 
_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 9BY1 ? ?      'Rigid-body docking of consensus model 9BY1 containing alpha subunits and beta C-terminal tails' ? ?      PDB 
'experimental model' 9BY1 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                    9BYC 
_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                  3.94 
_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               26000 
_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                        9BYC 
_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              9BYC 
_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                9BYC 
_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              9BYC 
_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 GLU 323 ? C GLU 344 
90  1 Y 1 C ASP 324 ? C ASP 345 
91  1 Y 1 C GLU 325 ? C GLU 346 
92  1 Y 1 C LYS 326 ? C LYS 347 
93  1 Y 1 C GLU 327 ? C GLU 348 
94  1 Y 1 C GLN 328 ? C GLN 349 
95  1 Y 1 C ILE 329 ? C ILE 350 
96  1 Y 1 D MET -20 ? D MET 1   
97  1 Y 1 D GLY -19 ? D GLY 2   
98  1 Y 1 D SER -18 ? D SER 3   
99  1 Y 1 D SER -17 ? D SER 4   
100 1 Y 1 D HIS -16 ? D HIS 5   
101 1 Y 1 D HIS -15 ? D HIS 6   
102 1 Y 1 D HIS -14 ? D HIS 7   
103 1 Y 1 D HIS -13 ? D HIS 8   
104 1 Y 1 D HIS -12 ? D HIS 9   
105 1 Y 1 D HIS -11 ? D HIS 10  
106 1 Y 1 D SER -10 ? D SER 11  
107 1 Y 1 D SER -9  ? D SER 12  
108 1 Y 1 D GLY -8  ? D GLY 13  
109 1 Y 1 D LEU -7  ? D LEU 14  
110 1 Y 1 D VAL -6  ? D VAL 15  
111 1 Y 1 D PRO -5  ? D PRO 16  
112 1 Y 1 D ARG -4  ? D ARG 17  
113 1 Y 1 D GLY -3  ? D GLY 18  
114 1 Y 1 D SER -2  ? D SER 19  
115 1 Y 1 D HIS -1  ? D HIS 20  
116 1 Y 1 D MET 0   ? D MET 21  
117 1 Y 1 D MET 1   ? D MET 22  
118 1 Y 1 D THR 2   ? D THR 23  
119 1 Y 1 D LYS 3   ? D LYS 24  
120 1 Y 1 D ILE 4   ? D ILE 25  
121 1 Y 1 D TYR 5   ? D TYR 26  
122 1 Y 1 D ASP 6   ? D ASP 27  
123 1 Y 1 D ALA 7   ? D ALA 28  
124 1 Y 1 D ALA 8   ? D ALA 29  
125 1 Y 1 D ASN 9   ? D ASN 30  
126 1 Y 1 D TRP 10  ? D TRP 31  
127 1 Y 1 D SER 11  ? D SER 32  
128 1 Y 1 D LYS 12  ? D LYS 33  
129 1 Y 1 D HIS 13  ? D HIS 34  
130 1 Y 1 D GLU 14  ? D GLU 35  
131 1 Y 1 D ASP 15  ? D ASP 36  
132 1 Y 1 D ASN 291 ? D ASN 312 
133 1 Y 1 D THR 292 ? D THR 313 
134 1 Y 1 D LYS 293 ? D LYS 314 
135 1 Y 1 D THR 294 ? D THR 315 
136 1 Y 1 D LYS 295 ? D LYS 316 
137 1 Y 1 D SER 296 ? D SER 317 
138 1 Y 1 D HIS 297 ? D HIS 318 
139 1 Y 1 D ASP 298 ? D ASP 319 
140 1 Y 1 D PHE 299 ? D PHE 320 
141 1 Y 1 D PHE 300 ? D PHE 321 
142 1 Y 1 D SER 301 ? D SER 322 
143 1 Y 1 D MET 302 ? D MET 323 
144 1 Y 1 D LYS 303 ? D LYS 324 
145 1 Y 1 D GLY 304 ? D GLY 325 
146 1 Y 1 D ASN 305 ? D ASN 326 
147 1 Y 1 D GLY 306 ? D GLY 327 
148 1 Y 1 D TYR 307 ? D TYR 328 
149 1 Y 1 D LYS 308 ? D LYS 329 
150 1 Y 1 D GLU 323 ? D GLU 344 
151 1 Y 1 D ASP 324 ? D ASP 345 
152 1 Y 1 D GLU 325 ? D GLU 346 
153 1 Y 1 D LYS 326 ? D LYS 347 
154 1 Y 1 D GLU 327 ? D GLU 348 
155 1 Y 1 D GLN 328 ? D GLN 349 
156 1 Y 1 D ILE 329 ? D ILE 350 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ARG N      N  N N 14  
ARG CA     C  N S 15  
ARG C      C  N N 16  
ARG O      O  N N 17  
ARG CB     C  N N 18  
ARG CG     C  N N 19  
ARG CD     C  N N 20  
ARG NE     N  N N 21  
ARG CZ     C  N N 22  
ARG NH1    N  N N 23  
ARG NH2    N  N N 24  
ARG OXT    O  N N 25  
ARG H      H  N N 26  
ARG H2     H  N N 27  
ARG HA     H  N N 28  
ARG HB2    H  N N 29  
ARG HB3    H  N N 30  
ARG HG2    H  N N 31  
ARG HG3    H  N N 32  
ARG HD2    H  N N 33  
ARG HD3    H  N N 34  
ARG HE     H  N N 35  
ARG HH11   H  N N 36  
ARG HH12   H  N N 37  
ARG HH21   H  N N 38  
ARG HH22   H  N N 39  
ARG HXT    H  N N 40  
ASN N      N  N N 41  
ASN CA     C  N S 42  
ASN C      C  N N 43  
ASN O      O  N N 44  
ASN CB     C  N N 45  
ASN CG     C  N N 46  
ASN OD1    O  N N 47  
ASN ND2    N  N N 48  
ASN OXT    O  N N 49  
ASN H      H  N N 50  
ASN H2     H  N N 51  
ASN HA     H  N N 52  
ASN HB2    H  N N 53  
ASN HB3    H  N N 54  
ASN HD21   H  N N 55  
ASN HD22   H  N N 56  
ASN HXT    H  N N 57  
ASP N      N  N N 58  
ASP CA     C  N S 59  
ASP C      C  N N 60  
ASP O      O  N N 61  
ASP CB     C  N N 62  
ASP CG     C  N N 63  
ASP OD1    O  N N 64  
ASP OD2    O  N N 65  
ASP OXT    O  N N 66  
ASP H      H  N N 67  
ASP H2     H  N N 68  
ASP HA     H  N N 69  
ASP HB2    H  N N 70  
ASP HB3    H  N N 71  
ASP HD2    H  N N 72  
ASP HXT    H  N N 73  
ATP PG     P  N N 74  
ATP O1G    O  N N 75  
ATP O2G    O  N N 76  
ATP O3G    O  N N 77  
ATP PB     P  N R 78  
ATP O1B    O  N N 79  
ATP O2B    O  N N 80  
ATP O3B    O  N N 81  
ATP PA     P  N R 82  
ATP O1A    O  N N 83  
ATP O2A    O  N N 84  
ATP O3A    O  N N 85  
ATP "O5'"  O  N N 86  
ATP "C5'"  C  N N 87  
ATP "C4'"  C  N R 88  
ATP "O4'"  O  N N 89  
ATP "C3'"  C  N S 90  
ATP "O3'"  O  N N 91  
ATP "C2'"  C  N R 92  
ATP "O2'"  O  N N 93  
ATP "C1'"  C  N R 94  
ATP N9     N  Y N 95  
ATP C8     C  Y N 96  
ATP N7     N  Y N 97  
ATP C5     C  Y N 98  
ATP C6     C  Y N 99  
ATP N6     N  N N 100 
ATP N1     N  Y N 101 
ATP C2     C  Y N 102 
ATP N3     N  Y N 103 
ATP C4     C  Y N 104 
ATP HOG2   H  N N 105 
ATP HOG3   H  N N 106 
ATP HOB2   H  N N 107 
ATP HOA2   H  N N 108 
ATP "H5'1" H  N N 109 
ATP "H5'2" H  N N 110 
ATP "H4'"  H  N N 111 
ATP "H3'"  H  N N 112 
ATP "HO3'" H  N N 113 
ATP "H2'"  H  N N 114 
ATP "HO2'" H  N N 115 
ATP "H1'"  H  N N 116 
ATP H8     H  N N 117 
ATP HN61   H  N N 118 
ATP HN62   H  N N 119 
ATP H2     H  N N 120 
CYS N      N  N N 121 
CYS CA     C  N R 122 
CYS C      C  N N 123 
CYS O      O  N N 124 
CYS CB     C  N N 125 
CYS SG     S  N N 126 
CYS OXT    O  N N 127 
CYS H      H  N N 128 
CYS H2     H  N N 129 
CYS HA     H  N N 130 
CYS HB2    H  N N 131 
CYS HB3    H  N N 132 
CYS HG     H  N N 133 
CYS HXT    H  N N 134 
DGI O1B    O  N N 135 
DGI PB     P  N N 136 
DGI O2B    O  N N 137 
DGI O3B    O  N N 138 
DGI O3A    O  N N 139 
DGI PA     P  N S 140 
DGI O1A    O  N N 141 
DGI O2A    O  N N 142 
DGI "O5'"  O  N N 143 
DGI "C5'"  C  N N 144 
DGI "C4'"  C  N R 145 
DGI "O4'"  O  N N 146 
DGI "C3'"  C  N S 147 
DGI "O3'"  O  N N 148 
DGI "C2'"  C  N N 149 
DGI "C1'"  C  N R 150 
DGI N9     N  Y N 151 
DGI C8     C  Y N 152 
DGI N7     N  Y N 153 
DGI C5     C  Y N 154 
DGI C4     C  Y N 155 
DGI N3     N  N N 156 
DGI C2     C  N N 157 
DGI N2     N  N N 158 
DGI N1     N  N N 159 
DGI C6     C  N N 160 
DGI O6     O  N N 161 
DGI HOB2   H  N N 162 
DGI HOB3   H  N N 163 
DGI HOA2   H  N N 164 
DGI "H5'"  H  N N 165 
DGI "H5''" H  N N 166 
DGI "H4'"  H  N N 167 
DGI "H3'"  H  N N 168 
DGI "HO3'" H  N N 169 
DGI "H2'"  H  N N 170 
DGI "H2''" H  N N 171 
DGI "H1'"  H  N N 172 
DGI H8     H  N N 173 
DGI HN21   H  N N 174 
DGI HN22   H  N N 175 
DGI HN1    H  N N 176 
GLN N      N  N N 177 
GLN CA     C  N S 178 
GLN C      C  N N 179 
GLN O      O  N N 180 
GLN CB     C  N N 181 
GLN CG     C  N N 182 
GLN CD     C  N N 183 
GLN OE1    O  N N 184 
GLN NE2    N  N N 185 
GLN OXT    O  N N 186 
GLN H      H  N N 187 
GLN H2     H  N N 188 
GLN HA     H  N N 189 
GLN HB2    H  N N 190 
GLN HB3    H  N N 191 
GLN HG2    H  N N 192 
GLN HG3    H  N N 193 
GLN HE21   H  N N 194 
GLN HE22   H  N N 195 
GLN HXT    H  N N 196 
GLU N      N  N N 197 
GLU CA     C  N S 198 
GLU C      C  N N 199 
GLU O      O  N N 200 
GLU CB     C  N N 201 
GLU CG     C  N N 202 
GLU CD     C  N N 203 
GLU OE1    O  N N 204 
GLU OE2    O  N N 205 
GLU OXT    O  N N 206 
GLU H      H  N N 207 
GLU H2     H  N N 208 
GLU HA     H  N N 209 
GLU HB2    H  N N 210 
GLU HB3    H  N N 211 
GLU HG2    H  N N 212 
GLU HG3    H  N N 213 
GLU HE2    H  N N 214 
GLU HXT    H  N N 215 
GLY N      N  N N 216 
GLY CA     C  N N 217 
GLY C      C  N N 218 
GLY O      O  N N 219 
GLY OXT    O  N N 220 
GLY H      H  N N 221 
GLY H2     H  N N 222 
GLY HA2    H  N N 223 
GLY HA3    H  N N 224 
GLY HXT    H  N N 225 
HIS N      N  N N 226 
HIS CA     C  N S 227 
HIS C      C  N N 228 
HIS O      O  N N 229 
HIS CB     C  N N 230 
HIS CG     C  Y N 231 
HIS ND1    N  Y N 232 
HIS CD2    C  Y N 233 
HIS CE1    C  Y N 234 
HIS NE2    N  Y N 235 
HIS OXT    O  N N 236 
HIS H      H  N N 237 
HIS H2     H  N N 238 
HIS HA     H  N N 239 
HIS HB2    H  N N 240 
HIS HB3    H  N N 241 
HIS HD1    H  N N 242 
HIS HD2    H  N N 243 
HIS HE1    H  N N 244 
HIS HE2    H  N N 245 
HIS HXT    H  N N 246 
ILE N      N  N N 247 
ILE CA     C  N S 248 
ILE C      C  N N 249 
ILE O      O  N N 250 
ILE CB     C  N S 251 
ILE CG1    C  N N 252 
ILE CG2    C  N N 253 
ILE CD1    C  N N 254 
ILE OXT    O  N N 255 
ILE H      H  N N 256 
ILE H2     H  N N 257 
ILE HA     H  N N 258 
ILE HB     H  N N 259 
ILE HG12   H  N N 260 
ILE HG13   H  N N 261 
ILE HG21   H  N N 262 
ILE HG22   H  N N 263 
ILE HG23   H  N N 264 
ILE HD11   H  N N 265 
ILE HD12   H  N N 266 
ILE HD13   H  N N 267 
ILE HXT    H  N N 268 
LEU N      N  N N 269 
LEU CA     C  N S 270 
LEU C      C  N N 271 
LEU O      O  N N 272 
LEU CB     C  N N 273 
LEU CG     C  N N 274 
LEU CD1    C  N N 275 
LEU CD2    C  N N 276 
LEU OXT    O  N N 277 
LEU H      H  N N 278 
LEU H2     H  N N 279 
LEU HA     H  N N 280 
LEU HB2    H  N N 281 
LEU HB3    H  N N 282 
LEU HG     H  N N 283 
LEU HD11   H  N N 284 
LEU HD12   H  N N 285 
LEU HD13   H  N N 286 
LEU HD21   H  N N 287 
LEU HD22   H  N N 288 
LEU HD23   H  N N 289 
LEU HXT    H  N N 290 
LYS N      N  N N 291 
LYS CA     C  N S 292 
LYS C      C  N N 293 
LYS O      O  N N 294 
LYS CB     C  N N 295 
LYS CG     C  N N 296 
LYS CD     C  N N 297 
LYS CE     C  N N 298 
LYS NZ     N  N N 299 
LYS OXT    O  N N 300 
LYS H      H  N N 301 
LYS H2     H  N N 302 
LYS HA     H  N N 303 
LYS HB2    H  N N 304 
LYS HB3    H  N N 305 
LYS HG2    H  N N 306 
LYS HG3    H  N N 307 
LYS HD2    H  N N 308 
LYS HD3    H  N N 309 
LYS HE2    H  N N 310 
LYS HE3    H  N N 311 
LYS HZ1    H  N N 312 
LYS HZ2    H  N N 313 
LYS HZ3    H  N N 314 
LYS HXT    H  N N 315 
MET N      N  N N 316 
MET CA     C  N S 317 
MET C      C  N N 318 
MET O      O  N N 319 
MET CB     C  N N 320 
MET CG     C  N N 321 
MET SD     S  N N 322 
MET CE     C  N N 323 
MET OXT    O  N N 324 
MET H      H  N N 325 
MET H2     H  N N 326 
MET HA     H  N N 327 
MET HB2    H  N N 328 
MET HB3    H  N N 329 
MET HG2    H  N N 330 
MET HG3    H  N N 331 
MET HE1    H  N N 332 
MET HE2    H  N N 333 
MET HE3    H  N N 334 
MET HXT    H  N N 335 
MG  MG     MG N N 336 
MN  MN     MN N N 337 
PHE N      N  N N 338 
PHE CA     C  N S 339 
PHE C      C  N N 340 
PHE O      O  N N 341 
PHE CB     C  N N 342 
PHE CG     C  Y N 343 
PHE CD1    C  Y N 344 
PHE CD2    C  Y N 345 
PHE CE1    C  Y N 346 
PHE CE2    C  Y N 347 
PHE CZ     C  Y N 348 
PHE OXT    O  N N 349 
PHE H      H  N N 350 
PHE H2     H  N N 351 
PHE HA     H  N N 352 
PHE HB2    H  N N 353 
PHE HB3    H  N N 354 
PHE HD1    H  N N 355 
PHE HD2    H  N N 356 
PHE HE1    H  N N 357 
PHE HE2    H  N N 358 
PHE HZ     H  N N 359 
PHE HXT    H  N N 360 
PRO N      N  N N 361 
PRO CA     C  N S 362 
PRO C      C  N N 363 
PRO O      O  N N 364 
PRO CB     C  N N 365 
PRO CG     C  N N 366 
PRO CD     C  N N 367 
PRO OXT    O  N N 368 
PRO H      H  N N 369 
PRO HA     H  N N 370 
PRO HB2    H  N N 371 
PRO HB3    H  N N 372 
PRO HG2    H  N N 373 
PRO HG3    H  N N 374 
PRO HD2    H  N N 375 
PRO HD3    H  N N 376 
PRO HXT    H  N N 377 
SER N      N  N N 378 
SER CA     C  N S 379 
SER C      C  N N 380 
SER O      O  N N 381 
SER CB     C  N N 382 
SER OG     O  N N 383 
SER OXT    O  N N 384 
SER H      H  N N 385 
SER H2     H  N N 386 
SER HA     H  N N 387 
SER HB2    H  N N 388 
SER HB3    H  N N 389 
SER HG     H  N N 390 
SER HXT    H  N N 391 
THR N      N  N N 392 
THR CA     C  N S 393 
THR C      C  N N 394 
THR O      O  N N 395 
THR CB     C  N R 396 
THR OG1    O  N N 397 
THR CG2    C  N N 398 
THR OXT    O  N N 399 
THR H      H  N N 400 
THR H2     H  N N 401 
THR HA     H  N N 402 
THR HB     H  N N 403 
THR HG1    H  N N 404 
THR HG21   H  N N 405 
THR HG22   H  N N 406 
THR HG23   H  N N 407 
THR HXT    H  N N 408 
TRP N      N  N N 409 
TRP CA     C  N S 410 
TRP C      C  N N 411 
TRP O      O  N N 412 
TRP CB     C  N N 413 
TRP CG     C  Y N 414 
TRP CD1    C  Y N 415 
TRP CD2    C  Y N 416 
TRP NE1    N  Y N 417 
TRP CE2    C  Y N 418 
TRP CE3    C  Y N 419 
TRP CZ2    C  Y N 420 
TRP CZ3    C  Y N 421 
TRP CH2    C  Y N 422 
TRP OXT    O  N N 423 
TRP H      H  N N 424 
TRP H2     H  N N 425 
TRP HA     H  N N 426 
TRP HB2    H  N N 427 
TRP HB3    H  N N 428 
TRP HD1    H  N N 429 
TRP HE1    H  N N 430 
TRP HE3    H  N N 431 
TRP HZ2    H  N N 432 
TRP HZ3    H  N N 433 
TRP HH2    H  N N 434 
TRP HXT    H  N N 435 
TTP PA     P  N S 436 
TTP O1A    O  N N 437 
TTP O2A    O  N N 438 
TTP O3A    O  N N 439 
TTP PB     P  N S 440 
TTP O1B    O  N N 441 
TTP O2B    O  N N 442 
TTP O3B    O  N N 443 
TTP PG     P  N N 444 
TTP O1G    O  N N 445 
TTP O2G    O  N N 446 
TTP O3G    O  N N 447 
TTP "O5'"  O  N N 448 
TTP "C5'"  C  N N 449 
TTP "C4'"  C  N R 450 
TTP "O4'"  O  N N 451 
TTP "C3'"  C  N S 452 
TTP "O3'"  O  N N 453 
TTP "C2'"  C  N N 454 
TTP "C1'"  C  N R 455 
TTP N1     N  N N 456 
TTP C2     C  N N 457 
TTP O2     O  N N 458 
TTP N3     N  N N 459 
TTP C4     C  N N 460 
TTP O4     O  N N 461 
TTP C5     C  N N 462 
TTP C5M    C  N N 463 
TTP C6     C  N N 464 
TTP HOA2   H  N N 465 
TTP HOB2   H  N N 466 
TTP HOG2   H  N N 467 
TTP HOG3   H  N N 468 
TTP "H5'1" H  N N 469 
TTP "H5'2" H  N N 470 
TTP "H4'"  H  N N 471 
TTP "H3'"  H  N N 472 
TTP "HO3'" H  N N 473 
TTP "H2'1" H  N N 474 
TTP "H2'2" H  N N 475 
TTP "H1'"  H  N N 476 
TTP HN3    H  N N 477 
TTP HM51   H  N N 478 
TTP HM52   H  N N 479 
TTP HM53   H  N N 480 
TTP H6     H  N N 481 
TYR N      N  N N 482 
TYR CA     C  N S 483 
TYR C      C  N N 484 
TYR O      O  N N 485 
TYR CB     C  N N 486 
TYR CG     C  Y N 487 
TYR CD1    C  Y N 488 
TYR CD2    C  Y N 489 
TYR CE1    C  Y N 490 
TYR CE2    C  Y N 491 
TYR CZ     C  Y N 492 
TYR OH     O  N N 493 
TYR OXT    O  N N 494 
TYR H      H  N N 495 
TYR H2     H  N N 496 
TYR HA     H  N N 497 
TYR HB2    H  N N 498 
TYR HB3    H  N N 499 
TYR HD1    H  N N 500 
TYR HD2    H  N N 501 
TYR HE1    H  N N 502 
TYR HE2    H  N N 503 
TYR HH     H  N N 504 
TYR HXT    H  N N 505 
VAL N      N  N N 506 
VAL CA     C  N S 507 
VAL C      C  N N 508 
VAL O      O  N N 509 
VAL CB     C  N N 510 
VAL CG1    C  N N 511 
VAL CG2    C  N N 512 
VAL OXT    O  N N 513 
VAL H      H  N N 514 
VAL H2     H  N N 515 
VAL HA     H  N N 516 
VAL HB     H  N N 517 
VAL HG11   H  N N 518 
VAL HG12   H  N N 519 
VAL HG13   H  N N 520 
VAL HG21   H  N N 521 
VAL HG22   H  N N 522 
VAL HG23   H  N N 523 
VAL HXT    H  N N 524 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
ATP PG    O1G    doub N N 70  
ATP PG    O2G    sing N N 71  
ATP PG    O3G    sing N N 72  
ATP PG    O3B    sing N N 73  
ATP O2G   HOG2   sing N N 74  
ATP O3G   HOG3   sing N N 75  
ATP PB    O1B    doub N N 76  
ATP PB    O2B    sing N N 77  
ATP PB    O3B    sing N N 78  
ATP PB    O3A    sing N N 79  
ATP O2B   HOB2   sing N N 80  
ATP PA    O1A    doub N N 81  
ATP PA    O2A    sing N N 82  
ATP PA    O3A    sing N N 83  
ATP PA    "O5'"  sing N N 84  
ATP O2A   HOA2   sing N N 85  
ATP "O5'" "C5'"  sing N N 86  
ATP "C5'" "C4'"  sing N N 87  
ATP "C5'" "H5'1" sing N N 88  
ATP "C5'" "H5'2" sing N N 89  
ATP "C4'" "O4'"  sing N N 90  
ATP "C4'" "C3'"  sing N N 91  
ATP "C4'" "H4'"  sing N N 92  
ATP "O4'" "C1'"  sing N N 93  
ATP "C3'" "O3'"  sing N N 94  
ATP "C3'" "C2'"  sing N N 95  
ATP "C3'" "H3'"  sing N N 96  
ATP "O3'" "HO3'" sing N N 97  
ATP "C2'" "O2'"  sing N N 98  
ATP "C2'" "C1'"  sing N N 99  
ATP "C2'" "H2'"  sing N N 100 
ATP "O2'" "HO2'" sing N N 101 
ATP "C1'" N9     sing N N 102 
ATP "C1'" "H1'"  sing N N 103 
ATP N9    C8     sing Y N 104 
ATP N9    C4     sing Y N 105 
ATP C8    N7     doub Y N 106 
ATP C8    H8     sing N N 107 
ATP N7    C5     sing Y N 108 
ATP C5    C6     sing Y N 109 
ATP C5    C4     doub Y N 110 
ATP C6    N6     sing N N 111 
ATP C6    N1     doub Y N 112 
ATP N6    HN61   sing N N 113 
ATP N6    HN62   sing N N 114 
ATP N1    C2     sing Y N 115 
ATP C2    N3     doub Y N 116 
ATP C2    H2     sing N N 117 
ATP N3    C4     sing Y N 118 
CYS N     CA     sing N N 119 
CYS N     H      sing N N 120 
CYS N     H2     sing N N 121 
CYS CA    C      sing N N 122 
CYS CA    CB     sing N N 123 
CYS CA    HA     sing N N 124 
CYS C     O      doub N N 125 
CYS C     OXT    sing N N 126 
CYS CB    SG     sing N N 127 
CYS CB    HB2    sing N N 128 
CYS CB    HB3    sing N N 129 
CYS SG    HG     sing N N 130 
CYS OXT   HXT    sing N N 131 
DGI O1B   PB     doub N N 132 
DGI PB    O2B    sing N N 133 
DGI PB    O3B    sing N N 134 
DGI PB    O3A    sing N N 135 
DGI O2B   HOB2   sing N N 136 
DGI O3B   HOB3   sing N N 137 
DGI O3A   PA     sing N N 138 
DGI PA    O1A    doub N N 139 
DGI PA    O2A    sing N N 140 
DGI PA    "O5'"  sing N N 141 
DGI O2A   HOA2   sing N N 142 
DGI "O5'" "C5'"  sing N N 143 
DGI "C5'" "C4'"  sing N N 144 
DGI "C5'" "H5'"  sing N N 145 
DGI "C5'" "H5''" sing N N 146 
DGI "C4'" "O4'"  sing N N 147 
DGI "C4'" "C3'"  sing N N 148 
DGI "C4'" "H4'"  sing N N 149 
DGI "O4'" "C1'"  sing N N 150 
DGI "C3'" "O3'"  sing N N 151 
DGI "C3'" "C2'"  sing N N 152 
DGI "C3'" "H3'"  sing N N 153 
DGI "O3'" "HO3'" sing N N 154 
DGI "C2'" "C1'"  sing N N 155 
DGI "C2'" "H2'"  sing N N 156 
DGI "C2'" "H2''" sing N N 157 
DGI "C1'" N9     sing N N 158 
DGI "C1'" "H1'"  sing N N 159 
DGI N9    C8     sing Y N 160 
DGI N9    C4     sing Y N 161 
DGI C8    N7     doub Y N 162 
DGI C8    H8     sing N N 163 
DGI N7    C5     sing Y N 164 
DGI C5    C4     doub Y N 165 
DGI C5    C6     sing N N 166 
DGI C4    N3     sing N N 167 
DGI N3    C2     doub N N 168 
DGI C2    N2     sing N N 169 
DGI C2    N1     sing N N 170 
DGI N2    HN21   sing N N 171 
DGI N2    HN22   sing N N 172 
DGI N1    C6     sing N N 173 
DGI N1    HN1    sing N N 174 
DGI C6    O6     doub N N 175 
GLN N     CA     sing N N 176 
GLN N     H      sing N N 177 
GLN N     H2     sing N N 178 
GLN CA    C      sing N N 179 
GLN CA    CB     sing N N 180 
GLN CA    HA     sing N N 181 
GLN C     O      doub N N 182 
GLN C     OXT    sing N N 183 
GLN CB    CG     sing N N 184 
GLN CB    HB2    sing N N 185 
GLN CB    HB3    sing N N 186 
GLN CG    CD     sing N N 187 
GLN CG    HG2    sing N N 188 
GLN CG    HG3    sing N N 189 
GLN CD    OE1    doub N N 190 
GLN CD    NE2    sing N N 191 
GLN NE2   HE21   sing N N 192 
GLN NE2   HE22   sing N N 193 
GLN OXT   HXT    sing N N 194 
GLU N     CA     sing N N 195 
GLU N     H      sing N N 196 
GLU N     H2     sing N N 197 
GLU CA    C      sing N N 198 
GLU CA    CB     sing N N 199 
GLU CA    HA     sing N N 200 
GLU C     O      doub N N 201 
GLU C     OXT    sing N N 202 
GLU CB    CG     sing N N 203 
GLU CB    HB2    sing N N 204 
GLU CB    HB3    sing N N 205 
GLU CG    CD     sing N N 206 
GLU CG    HG2    sing N N 207 
GLU CG    HG3    sing N N 208 
GLU CD    OE1    doub N N 209 
GLU CD    OE2    sing N N 210 
GLU OE2   HE2    sing N N 211 
GLU OXT   HXT    sing N N 212 
GLY N     CA     sing N N 213 
GLY N     H      sing N N 214 
GLY N     H2     sing N N 215 
GLY CA    C      sing N N 216 
GLY CA    HA2    sing N N 217 
GLY CA    HA3    sing N N 218 
GLY C     O      doub N N 219 
GLY C     OXT    sing N N 220 
GLY OXT   HXT    sing N N 221 
HIS N     CA     sing N N 222 
HIS N     H      sing N N 223 
HIS N     H2     sing N N 224 
HIS CA    C      sing N N 225 
HIS CA    CB     sing N N 226 
HIS CA    HA     sing N N 227 
HIS C     O      doub N N 228 
HIS C     OXT    sing N N 229 
HIS CB    CG     sing N N 230 
HIS CB    HB2    sing N N 231 
HIS CB    HB3    sing N N 232 
HIS CG    ND1    sing Y N 233 
HIS CG    CD2    doub Y N 234 
HIS ND1   CE1    doub Y N 235 
HIS ND1   HD1    sing N N 236 
HIS CD2   NE2    sing Y N 237 
HIS CD2   HD2    sing N N 238 
HIS CE1   NE2    sing Y N 239 
HIS CE1   HE1    sing N N 240 
HIS NE2   HE2    sing N N 241 
HIS OXT   HXT    sing N N 242 
ILE N     CA     sing N N 243 
ILE N     H      sing N N 244 
ILE N     H2     sing N N 245 
ILE CA    C      sing N N 246 
ILE CA    CB     sing N N 247 
ILE CA    HA     sing N N 248 
ILE C     O      doub N N 249 
ILE C     OXT    sing N N 250 
ILE CB    CG1    sing N N 251 
ILE CB    CG2    sing N N 252 
ILE CB    HB     sing N N 253 
ILE CG1   CD1    sing N N 254 
ILE CG1   HG12   sing N N 255 
ILE CG1   HG13   sing N N 256 
ILE CG2   HG21   sing N N 257 
ILE CG2   HG22   sing N N 258 
ILE CG2   HG23   sing N N 259 
ILE CD1   HD11   sing N N 260 
ILE CD1   HD12   sing N N 261 
ILE CD1   HD13   sing N N 262 
ILE OXT   HXT    sing N N 263 
LEU N     CA     sing N N 264 
LEU N     H      sing N N 265 
LEU N     H2     sing N N 266 
LEU CA    C      sing N N 267 
LEU CA    CB     sing N N 268 
LEU CA    HA     sing N N 269 
LEU C     O      doub N N 270 
LEU C     OXT    sing N N 271 
LEU CB    CG     sing N N 272 
LEU CB    HB2    sing N N 273 
LEU CB    HB3    sing N N 274 
LEU CG    CD1    sing N N 275 
LEU CG    CD2    sing N N 276 
LEU CG    HG     sing N N 277 
LEU CD1   HD11   sing N N 278 
LEU CD1   HD12   sing N N 279 
LEU CD1   HD13   sing N N 280 
LEU CD2   HD21   sing N N 281 
LEU CD2   HD22   sing N N 282 
LEU CD2   HD23   sing N N 283 
LEU OXT   HXT    sing N N 284 
LYS N     CA     sing N N 285 
LYS N     H      sing N N 286 
LYS N     H2     sing N N 287 
LYS CA    C      sing N N 288 
LYS CA    CB     sing N N 289 
LYS CA    HA     sing N N 290 
LYS C     O      doub N N 291 
LYS C     OXT    sing N N 292 
LYS CB    CG     sing N N 293 
LYS CB    HB2    sing N N 294 
LYS CB    HB3    sing N N 295 
LYS CG    CD     sing N N 296 
LYS CG    HG2    sing N N 297 
LYS CG    HG3    sing N N 298 
LYS CD    CE     sing N N 299 
LYS CD    HD2    sing N N 300 
LYS CD    HD3    sing N N 301 
LYS CE    NZ     sing N N 302 
LYS CE    HE2    sing N N 303 
LYS CE    HE3    sing N N 304 
LYS NZ    HZ1    sing N N 305 
LYS NZ    HZ2    sing N N 306 
LYS NZ    HZ3    sing N N 307 
LYS OXT   HXT    sing N N 308 
MET N     CA     sing N N 309 
MET N     H      sing N N 310 
MET N     H2     sing N N 311 
MET CA    C      sing N N 312 
MET CA    CB     sing N N 313 
MET CA    HA     sing N N 314 
MET C     O      doub N N 315 
MET C     OXT    sing N N 316 
MET CB    CG     sing N N 317 
MET CB    HB2    sing N N 318 
MET CB    HB3    sing N N 319 
MET CG    SD     sing N N 320 
MET CG    HG2    sing N N 321 
MET CG    HG3    sing N N 322 
MET SD    CE     sing N N 323 
MET CE    HE1    sing N N 324 
MET CE    HE2    sing N N 325 
MET CE    HE3    sing N N 326 
MET OXT   HXT    sing N N 327 
PHE N     CA     sing N N 328 
PHE N     H      sing N N 329 
PHE N     H2     sing N N 330 
PHE CA    C      sing N N 331 
PHE CA    CB     sing N N 332 
PHE CA    HA     sing N N 333 
PHE C     O      doub N N 334 
PHE C     OXT    sing N N 335 
PHE CB    CG     sing N N 336 
PHE CB    HB2    sing N N 337 
PHE CB    HB3    sing N N 338 
PHE CG    CD1    doub Y N 339 
PHE CG    CD2    sing Y N 340 
PHE CD1   CE1    sing Y N 341 
PHE CD1   HD1    sing N N 342 
PHE CD2   CE2    doub Y N 343 
PHE CD2   HD2    sing N N 344 
PHE CE1   CZ     doub Y N 345 
PHE CE1   HE1    sing N N 346 
PHE CE2   CZ     sing Y N 347 
PHE CE2   HE2    sing N N 348 
PHE CZ    HZ     sing N N 349 
PHE OXT   HXT    sing N N 350 
PRO N     CA     sing N N 351 
PRO N     CD     sing N N 352 
PRO N     H      sing N N 353 
PRO CA    C      sing N N 354 
PRO CA    CB     sing N N 355 
PRO CA    HA     sing N N 356 
PRO C     O      doub N N 357 
PRO C     OXT    sing N N 358 
PRO CB    CG     sing N N 359 
PRO CB    HB2    sing N N 360 
PRO CB    HB3    sing N N 361 
PRO CG    CD     sing N N 362 
PRO CG    HG2    sing N N 363 
PRO CG    HG3    sing N N 364 
PRO CD    HD2    sing N N 365 
PRO CD    HD3    sing N N 366 
PRO OXT   HXT    sing N N 367 
SER N     CA     sing N N 368 
SER N     H      sing N N 369 
SER N     H2     sing N N 370 
SER CA    C      sing N N 371 
SER CA    CB     sing N N 372 
SER CA    HA     sing N N 373 
SER C     O      doub N N 374 
SER C     OXT    sing N N 375 
SER CB    OG     sing N N 376 
SER CB    HB2    sing N N 377 
SER CB    HB3    sing N N 378 
SER OG    HG     sing N N 379 
SER OXT   HXT    sing N N 380 
THR N     CA     sing N N 381 
THR N     H      sing N N 382 
THR N     H2     sing N N 383 
THR CA    C      sing N N 384 
THR CA    CB     sing N N 385 
THR CA    HA     sing N N 386 
THR C     O      doub N N 387 
THR C     OXT    sing N N 388 
THR CB    OG1    sing N N 389 
THR CB    CG2    sing N N 390 
THR CB    HB     sing N N 391 
THR OG1   HG1    sing N N 392 
THR CG2   HG21   sing N N 393 
THR CG2   HG22   sing N N 394 
THR CG2   HG23   sing N N 395 
THR OXT   HXT    sing N N 396 
TRP N     CA     sing N N 397 
TRP N     H      sing N N 398 
TRP N     H2     sing N N 399 
TRP CA    C      sing N N 400 
TRP CA    CB     sing N N 401 
TRP CA    HA     sing N N 402 
TRP C     O      doub N N 403 
TRP C     OXT    sing N N 404 
TRP CB    CG     sing N N 405 
TRP CB    HB2    sing N N 406 
TRP CB    HB3    sing N N 407 
TRP CG    CD1    doub Y N 408 
TRP CG    CD2    sing Y N 409 
TRP CD1   NE1    sing Y N 410 
TRP CD1   HD1    sing N N 411 
TRP CD2   CE2    doub Y N 412 
TRP CD2   CE3    sing Y N 413 
TRP NE1   CE2    sing Y N 414 
TRP NE1   HE1    sing N N 415 
TRP CE2   CZ2    sing Y N 416 
TRP CE3   CZ3    doub Y N 417 
TRP CE3   HE3    sing N N 418 
TRP CZ2   CH2    doub Y N 419 
TRP CZ2   HZ2    sing N N 420 
TRP CZ3   CH2    sing Y N 421 
TRP CZ3   HZ3    sing N N 422 
TRP CH2   HH2    sing N N 423 
TRP OXT   HXT    sing N N 424 
TTP PA    O1A    doub N N 425 
TTP PA    O2A    sing N N 426 
TTP PA    O3A    sing N N 427 
TTP PA    "O5'"  sing N N 428 
TTP O2A   HOA2   sing N N 429 
TTP O3A   PB     sing N N 430 
TTP PB    O1B    doub N N 431 
TTP PB    O2B    sing N N 432 
TTP PB    O3B    sing N N 433 
TTP O2B   HOB2   sing N N 434 
TTP O3B   PG     sing N N 435 
TTP PG    O1G    doub N N 436 
TTP PG    O2G    sing N N 437 
TTP PG    O3G    sing N N 438 
TTP O2G   HOG2   sing N N 439 
TTP O3G   HOG3   sing N N 440 
TTP "O5'" "C5'"  sing N N 441 
TTP "C5'" "C4'"  sing N N 442 
TTP "C5'" "H5'1" sing N N 443 
TTP "C5'" "H5'2" sing N N 444 
TTP "C4'" "O4'"  sing N N 445 
TTP "C4'" "C3'"  sing N N 446 
TTP "C4'" "H4'"  sing N N 447 
TTP "O4'" "C1'"  sing N N 448 
TTP "C3'" "O3'"  sing N N 449 
TTP "C3'" "C2'"  sing N N 450 
TTP "C3'" "H3'"  sing N N 451 
TTP "O3'" "HO3'" sing N N 452 
TTP "C2'" "C1'"  sing N N 453 
TTP "C2'" "H2'1" sing N N 454 
TTP "C2'" "H2'2" sing N N 455 
TTP "C1'" N1     sing N N 456 
TTP "C1'" "H1'"  sing N N 457 
TTP N1    C2     sing N N 458 
TTP N1    C6     sing N N 459 
TTP C2    O2     doub N N 460 
TTP C2    N3     sing N N 461 
TTP N3    C4     sing N N 462 
TTP N3    HN3    sing N N 463 
TTP C4    O4     doub N N 464 
TTP C4    C5     sing N N 465 
TTP C5    C5M    sing N N 466 
TTP C5    C6     doub N N 467 
TTP C5M   HM51   sing N N 468 
TTP C5M   HM52   sing N N 469 
TTP C5M   HM53   sing N N 470 
TTP C6    H6     sing N N 471 
TYR N     CA     sing N N 472 
TYR N     H      sing N N 473 
TYR N     H2     sing N N 474 
TYR CA    C      sing N N 475 
TYR CA    CB     sing N N 476 
TYR CA    HA     sing N N 477 
TYR C     O      doub N N 478 
TYR C     OXT    sing N N 479 
TYR CB    CG     sing N N 480 
TYR CB    HB2    sing N N 481 
TYR CB    HB3    sing N N 482 
TYR CG    CD1    doub Y N 483 
TYR CG    CD2    sing Y N 484 
TYR CD1   CE1    sing Y N 485 
TYR CD1   HD1    sing N N 486 
TYR CD2   CE2    doub Y N 487 
TYR CD2   HD2    sing N N 488 
TYR CE1   CZ     doub Y N 489 
TYR CE1   HE1    sing N N 490 
TYR CE2   CZ     sing Y N 491 
TYR CE2   HE2    sing N N 492 
TYR CZ    OH     sing N N 493 
TYR OH    HH     sing N N 494 
TYR OXT   HXT    sing N N 495 
VAL N     CA     sing N N 496 
VAL N     H      sing N N 497 
VAL N     H2     sing N N 498 
VAL CA    C      sing N N 499 
VAL CA    CB     sing N N 500 
VAL CA    HA     sing N N 501 
VAL C     O      doub N N 502 
VAL C     OXT    sing N N 503 
VAL CB    CG1    sing N N 504 
VAL CB    CG2    sing N N 505 
VAL CB    HB     sing N N 506 
VAL CG1   HG11   sing N N 507 
VAL CG1   HG12   sing N N 508 
VAL CG1   HG13   sing N N 509 
VAL CG2   HG21   sing N N 510 
VAL CG2   HG22   sing N N 511 
VAL CG2   HG23   sing N N 512 
VAL OXT   HXT    sing N N 513 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-05-23 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9BYC 
_em_admin.last_update        2025-03-26 
_em_admin.map_release_date   2025-03-19 
_em_admin.title              'Class 12 model for product condition of Bacillus subtilis ribonucleotide reductase complex' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          1423 
_em_entity_assembly_naturalsource.organism             'Bacillus subtilis' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          562 
_em_entity_assembly_recombinant.organism             'Escherichia coli' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         50 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       COUNTING 
_em_image_recording.film_or_detector_model              'GATAN K3 BIOQUANTUM (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
_em_imaging_optics.chr_aberration_corrector   ? 
_em_imaging_optics.energyfilter_lower         ? 
_em_imaging_optics.energyfilter_slit_width    20 
_em_imaging_optics.energyfilter_name          ? 
_em_imaging_optics.energyfilter_upper         ? 
_em_imaging_optics.id                         1 
_em_imaging_optics.imaging_id                 1 
_em_imaging_optics.phase_plate                ? 
_em_imaging_optics.sph_aberration_corrector   ? 
_em_imaging_optics.details                    ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'       ? 1  1 ? ? ?               ? 
'IMAGE ACQUISITION'        ? 2  ? ? ? ?               ? 
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 9BY1 
2 'experimental model' PDB 4DR0 
# 
_atom_sites.entry_id                    9BYC 
_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   ? 103.486 117.345 98.414  1.00 63.04 ?  6   VAL A N     1 
ATOM   2     C  CA    . VAL A 1 6   ? 104.795 117.841 98.010  1.00 62.74 ?  6   VAL A CA    1 
ATOM   3     C  C     . VAL A 1 6   ? 104.620 119.014 97.045  1.00 63.36 ?  6   VAL A C     1 
ATOM   4     O  O     . VAL A 1 6   ? 103.710 119.013 96.213  1.00 63.20 ?  6   VAL A O     1 
ATOM   5     C  CB    . VAL A 1 6   ? 105.653 116.701 97.393  1.00 64.24 ?  6   VAL A CB    1 
ATOM   6     C  CG1   . VAL A 1 6   ? 105.373 116.527 95.904  1.00 62.93 ?  6   VAL A CG1   1 
ATOM   7     C  CG2   . VAL A 1 6   ? 107.131 116.940 97.643  1.00 61.49 ?  6   VAL A CG2   1 
ATOM   8     N  N     . PRO A 1 7   ? 105.454 120.044 97.193  1.00 58.77 ?  7   PRO A N     1 
ATOM   9     C  CA    . PRO A 1 7   ? 105.413 121.158 96.241  1.00 54.02 ?  7   PRO A CA    1 
ATOM   10    C  C     . PRO A 1 7   ? 105.763 120.692 94.837  1.00 56.48 ?  7   PRO A C     1 
ATOM   11    O  O     . PRO A 1 7   ? 106.583 119.794 94.642  1.00 60.50 ?  7   PRO A O     1 
ATOM   12    C  CB    . PRO A 1 7   ? 106.463 122.130 96.786  1.00 55.37 ?  7   PRO A CB    1 
ATOM   13    C  CG    . PRO A 1 7   ? 106.531 121.821 98.239  1.00 57.08 ?  7   PRO A CG    1 
ATOM   14    C  CD    . PRO A 1 7   ? 106.327 120.337 98.341  1.00 57.20 ?  7   PRO A CD    1 
ATOM   15    N  N     . LYS A 1 8   ? 105.117 121.314 93.849  1.00 58.03 ?  8   LYS A N     1 
ATOM   16    C  CA    . LYS A 1 8   ? 105.352 120.928 92.462  1.00 56.12 ?  8   LYS A CA    1 
ATOM   17    C  C     . LYS A 1 8   ? 106.778 121.243 92.034  1.00 57.08 ?  8   LYS A C     1 
ATOM   18    O  O     . LYS A 1 8   ? 107.397 120.474 91.289  1.00 57.57 ?  8   LYS A O     1 
ATOM   19    C  CB    . LYS A 1 8   ? 104.352 121.626 91.543  1.00 55.64 ?  8   LYS A CB    1 
ATOM   20    C  CG    . LYS A 1 8   ? 104.181 120.944 90.196  1.00 56.25 ?  8   LYS A CG    1 
ATOM   21    C  CD    . LYS A 1 8   ? 103.933 121.952 89.091  1.00 57.80 ?  8   LYS A CD    1 
ATOM   22    C  CE    . LYS A 1 8   ? 104.117 121.322 87.721  1.00 57.13 ?  8   LYS A CE    1 
ATOM   23    N  NZ    . LYS A 1 8   ? 104.633 122.301 86.727  1.00 58.95 1  8   LYS A NZ    1 
ATOM   24    N  N     . TRP A 1 9   ? 107.317 122.374 92.494  1.00 57.42 ?  9   TRP A N     1 
ATOM   25    C  CA    . TRP A 1 9   ? 108.640 122.790 92.044  1.00 52.16 ?  9   TRP A CA    1 
ATOM   26    C  C     . TRP A 1 9   ? 109.733 121.895 92.611  1.00 54.06 ?  9   TRP A C     1 
ATOM   27    O  O     . TRP A 1 9   ? 110.699 121.577 91.909  1.00 57.94 ?  9   TRP A O     1 
ATOM   28    C  CB    . TRP A 1 9   ? 108.887 124.253 92.405  1.00 53.77 ?  9   TRP A CB    1 
ATOM   29    C  CG    . TRP A 1 9   ? 108.596 124.612 93.821  1.00 50.50 ?  9   TRP A CG    1 
ATOM   30    C  CD1   . TRP A 1 9   ? 109.449 124.524 94.875  1.00 51.38 ?  9   TRP A CD1   1 
ATOM   31    C  CD2   . TRP A 1 9   ? 107.369 125.131 94.340  1.00 51.33 ?  9   TRP A CD2   1 
ATOM   32    N  NE1   . TRP A 1 9   ? 108.831 124.949 96.024  1.00 52.90 ?  9   TRP A NE1   1 
ATOM   33    C  CE2   . TRP A 1 9   ? 107.551 125.329 95.722  1.00 52.26 ?  9   TRP A CE2   1 
ATOM   34    C  CE3   . TRP A 1 9   ? 106.132 125.444 93.772  1.00 51.69 ?  9   TRP A CE3   1 
ATOM   35    C  CZ2   . TRP A 1 9   ? 106.545 125.825 96.544  1.00 52.47 ?  9   TRP A CZ2   1 
ATOM   36    C  CZ3   . TRP A 1 9   ? 105.136 125.936 94.587  1.00 55.31 ?  9   TRP A CZ3   1 
ATOM   37    C  CH2   . TRP A 1 9   ? 105.347 126.123 95.958  1.00 54.90 ?  9   TRP A CH2   1 
ATOM   38    N  N     . ILE A 1 10  ? 109.608 121.469 93.871  1.00 54.45 ?  10  ILE A N     1 
ATOM   39    C  CA    . ILE A 1 10  ? 110.606 120.546 94.404  1.00 57.23 ?  10  ILE A CA    1 
ATOM   40    C  C     . ILE A 1 10  ? 110.403 119.135 93.873  1.00 55.75 ?  10  ILE A C     1 
ATOM   41    O  O     . ILE A 1 10  ? 111.355 118.346 93.858  1.00 59.01 ?  10  ILE A O     1 
ATOM   42    C  CB    . ILE A 1 10  ? 110.631 120.511 95.943  1.00 56.46 ?  10  ILE A CB    1 
ATOM   43    C  CG1   . ILE A 1 10  ? 109.656 119.472 96.494  1.00 58.14 ?  10  ILE A CG1   1 
ATOM   44    C  CG2   . ILE A 1 10  ? 110.345 121.876 96.530  1.00 55.14 ?  10  ILE A CG2   1 
ATOM   45    C  CD1   . ILE A 1 10  ? 109.878 119.168 97.954  1.00 58.28 ?  10  ILE A CD1   1 
ATOM   46    N  N     . GLN A 1 11  ? 109.190 118.791 93.439  1.00 57.10 ?  11  GLN A N     1 
ATOM   47    C  CA    . GLN A 1 11  ? 108.997 117.519 92.753  1.00 57.23 ?  11  GLN A CA    1 
ATOM   48    C  C     . GLN A 1 11  ? 109.685 117.529 91.394  1.00 56.41 ?  11  GLN A C     1 
ATOM   49    O  O     . GLN A 1 11  ? 110.330 116.546 91.011  1.00 58.51 ?  11  GLN A O     1 
ATOM   50    C  CB    . GLN A 1 11  ? 107.505 117.221 92.610  1.00 59.25 ?  11  GLN A CB    1 
ATOM   51    C  CG    . GLN A 1 11  ? 107.179 116.110 91.632  1.00 60.60 ?  11  GLN A CG    1 
ATOM   52    C  CD    . GLN A 1 11  ? 106.380 116.605 90.445  1.00 61.60 ?  11  GLN A CD    1 
ATOM   53    O  OE1   . GLN A 1 11  ? 105.398 117.329 90.602  1.00 60.15 ?  11  GLN A OE1   1 
ATOM   54    N  NE2   . GLN A 1 11  ? 106.800 116.218 89.246  1.00 60.38 ?  11  GLN A NE2   1 
ATOM   55    N  N     . LEU A 1 12  ? 109.566 118.637 90.659  1.00 56.36 ?  12  LEU A N     1 
ATOM   56    C  CA    . LEU A 1 12  ? 110.283 118.778 89.395  1.00 55.06 ?  12  LEU A CA    1 
ATOM   57    C  C     . LEU A 1 12  ? 111.790 118.816 89.615  1.00 57.48 ?  12  LEU A C     1 
ATOM   58    O  O     . LEU A 1 12  ? 112.556 118.278 88.808  1.00 59.89 ?  12  LEU A O     1 
ATOM   59    C  CB    . LEU A 1 12  ? 109.820 120.040 88.671  1.00 55.96 ?  12  LEU A CB    1 
ATOM   60    C  CG    . LEU A 1 12  ? 108.704 119.889 87.640  1.00 56.90 ?  12  LEU A CG    1 
ATOM   61    C  CD1   . LEU A 1 12  ? 107.953 121.200 87.482  1.00 55.45 ?  12  LEU A CD1   1 
ATOM   62    C  CD2   . LEU A 1 12  ? 109.268 119.428 86.308  1.00 57.52 ?  12  LEU A CD2   1 
ATOM   63    N  N     . ASN A 1 13  ? 112.233 119.459 90.698  1.00 56.01 ?  13  ASN A N     1 
ATOM   64    C  CA    . ASN A 1 13  ? 113.658 119.554 90.984  1.00 52.82 ?  13  ASN A CA    1 
ATOM   65    C  C     . ASN A 1 13  ? 114.252 118.198 91.341  1.00 54.86 ?  13  ASN A C     1 
ATOM   66    O  O     . ASN A 1 13  ? 115.447 117.970 91.123  1.00 60.62 ?  13  ASN A O     1 
ATOM   67    C  CB    . ASN A 1 13  ? 113.893 120.557 92.114  1.00 56.25 ?  13  ASN A CB    1 
ATOM   68    C  CG    . ASN A 1 13  ? 115.346 120.637 92.533  1.00 56.13 ?  13  ASN A CG    1 
ATOM   69    O  OD1   . ASN A 1 13  ? 115.740 120.079 93.555  1.00 54.72 ?  13  ASN A OD1   1 
ATOM   70    N  ND2   . ASN A 1 13  ? 116.150 121.337 91.742  1.00 55.92 ?  13  ASN A ND2   1 
ATOM   71    N  N     . ASN A 1 14  ? 113.443 117.291 91.885  1.00 57.72 ?  14  ASN A N     1 
ATOM   72    C  CA    . ASN A 1 14  ? 113.916 115.952 92.208  1.00 58.51 ?  14  ASN A CA    1 
ATOM   73    C  C     . ASN A 1 14  ? 113.983 115.040 90.991  1.00 57.77 ?  14  ASN A C     1 
ATOM   74    O  O     . ASN A 1 14  ? 114.561 113.953 91.086  1.00 60.03 ?  14  ASN A O     1 
ATOM   75    C  CB    . ASN A 1 14  ? 113.023 115.320 93.278  1.00 56.46 ?  14  ASN A CB    1 
ATOM   76    C  CG    . ASN A 1 14  ? 113.299 115.868 94.662  1.00 58.69 ?  14  ASN A CG    1 
ATOM   77    O  OD1   . ASN A 1 14  ? 113.642 117.039 94.821  1.00 60.90 ?  14  ASN A OD1   1 
ATOM   78    N  ND2   . ASN A 1 14  ? 113.148 115.024 95.675  1.00 59.30 ?  14  ASN A ND2   1 
ATOM   79    N  N     . GLU A 1 15  ? 113.417 115.451 89.858  1.00 57.87 ?  15  GLU A N     1 
ATOM   80    C  CA    . GLU A 1 15  ? 113.519 114.679 88.627  1.00 59.07 ?  15  GLU A CA    1 
ATOM   81    C  C     . GLU A 1 15  ? 114.877 114.825 87.954  1.00 61.72 ?  15  GLU A C     1 
ATOM   82    O  O     . GLU A 1 15  ? 115.118 114.169 86.936  1.00 63.52 ?  15  GLU A O     1 
ATOM   83    C  CB    . GLU A 1 15  ? 112.411 115.085 87.650  1.00 59.34 ?  15  GLU A CB    1 
ATOM   84    C  CG    . GLU A 1 15  ? 111.041 115.209 88.290  1.00 60.15 ?  15  GLU A CG    1 
ATOM   85    C  CD    . GLU A 1 15  ? 109.915 115.207 87.276  1.00 63.73 ?  15  GLU A CD    1 
ATOM   86    O  OE1   . GLU A 1 15  ? 110.201 115.308 86.066  1.00 63.57 ?  15  GLU A OE1   1 
ATOM   87    O  OE2   . GLU A 1 15  ? 108.741 115.104 87.690  1.00 63.84 -1 15  GLU A OE2   1 
ATOM   88    N  N     . ILE A 1 16  ? 115.756 115.676 88.488  1.00 59.98 ?  16  ILE A N     1 
ATOM   89    C  CA    . ILE A 1 16  ? 117.117 115.765 87.966  1.00 59.72 ?  16  ILE A CA    1 
ATOM   90    C  C     . ILE A 1 16  ? 117.853 114.451 88.184  1.00 59.78 ?  16  ILE A C     1 
ATOM   91    O  O     . ILE A 1 16  ? 118.561 113.962 87.295  1.00 61.09 ?  16  ILE A O     1 
ATOM   92    C  CB    . ILE A 1 16  ? 117.863 116.945 88.615  1.00 58.93 ?  16  ILE A CB    1 
ATOM   93    C  CG1   . ILE A 1 16  ? 117.142 118.262 88.329  1.00 57.54 ?  16  ILE A CG1   1 
ATOM   94    C  CG2   . ILE A 1 16  ? 119.302 117.010 88.122  1.00 59.58 ?  16  ILE A CG2   1 
ATOM   95    C  CD1   . ILE A 1 16  ? 117.649 119.422 89.151  1.00 56.90 ?  16  ILE A CD1   1 
ATOM   96    N  N     . MET A 1 17  ? 117.693 113.856 89.366  1.00 60.50 ?  17  MET A N     1 
ATOM   97    C  CA    . MET A 1 17  ? 118.403 112.630 89.701  1.00 61.98 ?  17  MET A CA    1 
ATOM   98    C  C     . MET A 1 17  ? 117.815 111.398 89.029  1.00 62.80 ?  17  MET A C     1 
ATOM   99    O  O     . MET A 1 17  ? 118.503 110.377 88.932  1.00 63.98 ?  17  MET A O     1 
ATOM   100   C  CB    . MET A 1 17  ? 118.412 112.432 91.216  1.00 61.29 ?  17  MET A CB    1 
ATOM   101   C  CG    . MET A 1 17  ? 118.885 113.650 91.973  1.00 61.55 ?  17  MET A CG    1 
ATOM   102   S  SD    . MET A 1 17  ? 120.420 114.332 91.319  1.00 68.12 ?  17  MET A SD    1 
ATOM   103   C  CE    . MET A 1 17  ? 121.629 113.328 92.176  1.00 61.05 ?  17  MET A CE    1 
ATOM   104   N  N     . ILE A 1 18  ? 116.567 111.462 88.570  1.00 62.62 ?  18  ILE A N     1 
ATOM   105   C  CA    . ILE A 1 18  ? 115.989 110.349 87.822  1.00 64.44 ?  18  ILE A CA    1 
ATOM   106   C  C     . ILE A 1 18  ? 116.711 110.280 86.480  1.00 65.28 ?  18  ILE A C     1 
ATOM   107   O  O     . ILE A 1 18  ? 116.516 111.136 85.611  1.00 66.44 ?  18  ILE A O     1 
ATOM   108   C  CB    . ILE A 1 18  ? 114.471 110.496 87.637  1.00 65.30 ?  18  ILE A CB    1 
ATOM   109   C  CG1   . ILE A 1 18  ? 113.674 110.221 88.930  1.00 64.60 ?  18  ILE A CG1   1 
ATOM   110   C  CG2   . ILE A 1 18  ? 113.972 109.562 86.541  1.00 64.87 ?  18  ILE A CG2   1 
ATOM   111   C  CD1   . ILE A 1 18  ? 114.143 110.887 90.209  1.00 64.07 ?  18  ILE A CD1   1 
ATOM   112   N  N     . GLN A 1 19  ? 117.563 109.273 86.317  1.00 68.96 ?  19  GLN A N     1 
ATOM   113   C  CA    . GLN A 1 19  ? 118.416 109.175 85.140  1.00 70.00 ?  19  GLN A CA    1 
ATOM   114   C  C     . GLN A 1 19  ? 117.616 108.618 83.970  1.00 69.78 ?  19  GLN A C     1 
ATOM   115   O  O     . GLN A 1 19  ? 117.184 107.461 83.998  1.00 71.76 ?  19  GLN A O     1 
ATOM   116   C  CB    . GLN A 1 19  ? 119.629 108.298 85.434  1.00 72.02 ?  19  GLN A CB    1 
ATOM   117   C  CG    . GLN A 1 19  ? 120.610 108.915 86.420  1.00 70.29 ?  19  GLN A CG    1 
ATOM   118   C  CD    . GLN A 1 19  ? 121.831 108.047 86.655  1.00 71.59 ?  19  GLN A CD    1 
ATOM   119   O  OE1   . GLN A 1 19  ? 121.954 106.962 86.088  1.00 71.28 ?  19  GLN A OE1   1 
ATOM   120   N  NE2   . GLN A 1 19  ? 122.741 108.523 87.496  1.00 71.39 ?  19  GLN A NE2   1 
ATOM   121   N  N     . LYS A 1 20  ? 117.419 109.443 82.947  1.00 71.28 ?  20  LYS A N     1 
ATOM   122   C  CA    . LYS A 1 20  ? 116.723 109.048 81.731  1.00 73.11 ?  20  LYS A CA    1 
ATOM   123   C  C     . LYS A 1 20  ? 117.749 108.902 80.617  1.00 73.64 ?  20  LYS A C     1 
ATOM   124   O  O     . LYS A 1 20  ? 118.498 109.844 80.335  1.00 73.55 ?  20  LYS A O     1 
ATOM   125   C  CB    . LYS A 1 20  ? 115.652 110.072 81.356  1.00 71.82 ?  20  LYS A CB    1 
ATOM   126   C  CG    . LYS A 1 20  ? 115.037 109.855 79.984  1.00 72.49 ?  20  LYS A CG    1 
ATOM   127   C  CD    . LYS A 1 20  ? 114.849 111.170 79.249  1.00 73.53 ?  20  LYS A CD    1 
ATOM   128   C  CE    . LYS A 1 20  ? 116.120 112.004 79.274  1.00 73.84 ?  20  LYS A CE    1 
ATOM   129   N  NZ    . LYS A 1 20  ? 117.254 111.307 78.609  1.00 73.93 1  20  LYS A NZ    1 
ATOM   130   N  N     . ASP A 1 21  ? 117.780 107.723 79.993  1.00 72.18 ?  21  ASP A N     1 
ATOM   131   C  CA    . ASP A 1 21  ? 118.750 107.402 78.945  1.00 73.50 ?  21  ASP A CA    1 
ATOM   132   C  C     . ASP A 1 21  ? 120.184 107.536 79.456  1.00 74.05 ?  21  ASP A C     1 
ATOM   133   O  O     . ASP A 1 21  ? 121.085 107.958 78.729  1.00 72.09 ?  21  ASP A O     1 
ATOM   134   C  CB    . ASP A 1 21  ? 118.531 108.268 77.701  1.00 73.43 ?  21  ASP A CB    1 
ATOM   135   C  CG    . ASP A 1 21  ? 117.072 108.353 77.302  1.00 74.57 ?  21  ASP A CG    1 
ATOM   136   O  OD1   . ASP A 1 21  ? 116.361 107.333 77.418  1.00 72.61 ?  21  ASP A OD1   1 
ATOM   137   O  OD2   . ASP A 1 21  ? 116.636 109.442 76.873  1.00 74.27 -1 21  ASP A OD2   1 
ATOM   138   N  N     . GLY A 1 22  ? 120.395 107.173 80.719  1.00 73.98 ?  22  GLY A N     1 
ATOM   139   C  CA    . GLY A 1 22  ? 121.722 107.179 81.300  1.00 74.01 ?  22  GLY A CA    1 
ATOM   140   C  C     . GLY A 1 22  ? 122.277 108.541 81.648  1.00 73.96 ?  22  GLY A C     1 
ATOM   141   O  O     . GLY A 1 22  ? 123.472 108.643 81.946  1.00 72.73 ?  22  GLY A O     1 
ATOM   142   N  N     . LYS A 1 23  ? 121.456 109.588 81.626  1.00 70.77 ?  23  LYS A N     1 
ATOM   143   C  CA    . LYS A 1 23  ? 121.911 110.940 81.908  1.00 68.48 ?  23  LYS A CA    1 
ATOM   144   C  C     . LYS A 1 23  ? 120.990 111.600 82.923  1.00 69.58 ?  23  LYS A C     1 
ATOM   145   O  O     . LYS A 1 23  ? 119.789 111.318 82.972  1.00 70.55 ?  23  LYS A O     1 
ATOM   146   C  CB    . LYS A 1 23  ? 121.958 111.797 80.637  1.00 68.39 ?  23  LYS A CB    1 
ATOM   147   C  CG    . LYS A 1 23  ? 123.027 111.395 79.638  1.00 68.46 ?  23  LYS A CG    1 
ATOM   148   C  CD    . LYS A 1 23  ? 123.042 112.357 78.461  1.00 68.57 ?  23  LYS A CD    1 
ATOM   149   C  CE    . LYS A 1 23  ? 124.024 111.918 77.391  1.00 68.95 ?  23  LYS A CE    1 
ATOM   150   N  NZ    . LYS A 1 23  ? 123.989 112.827 76.213  1.00 67.63 1  23  LYS A NZ    1 
ATOM   151   N  N     . PHE A 1 24  ? 121.568 112.482 83.734  1.00 63.30 ?  24  PHE A N     1 
ATOM   152   C  CA    . PHE A 1 24  ? 120.770 113.303 84.633  1.00 60.09 ?  24  PHE A CA    1 
ATOM   153   C  C     . PHE A 1 24  ? 119.898 114.260 83.831  1.00 60.84 ?  24  PHE A C     1 
ATOM   154   O  O     . PHE A 1 24  ? 120.325 114.809 82.812  1.00 59.40 ?  24  PHE A O     1 
ATOM   155   C  CB    . PHE A 1 24  ? 121.671 114.094 85.580  1.00 58.54 ?  24  PHE A CB    1 
ATOM   156   C  CG    . PHE A 1 24  ? 122.336 113.255 86.629  1.00 59.92 ?  24  PHE A CG    1 
ATOM   157   C  CD1   . PHE A 1 24  ? 121.672 112.930 87.798  1.00 60.45 ?  24  PHE A CD1   1 
ATOM   158   C  CD2   . PHE A 1 24  ? 123.630 112.798 86.449  1.00 59.89 ?  24  PHE A CD2   1 
ATOM   159   C  CE1   . PHE A 1 24  ? 122.285 112.161 88.766  1.00 60.18 ?  24  PHE A CE1   1 
ATOM   160   C  CE2   . PHE A 1 24  ? 124.247 112.029 87.415  1.00 59.21 ?  24  PHE A CE2   1 
ATOM   161   C  CZ    . PHE A 1 24  ? 123.573 111.710 88.574  1.00 60.10 ?  24  PHE A CZ    1 
ATOM   162   N  N     . GLN A 1 25  ? 118.666 114.457 84.296  1.00 61.85 ?  25  GLN A N     1 
ATOM   163   C  CA    . GLN A 1 25  ? 117.734 115.374 83.641  1.00 59.76 ?  25  GLN A CA    1 
ATOM   164   C  C     . GLN A 1 25  ? 117.984 116.775 84.190  1.00 60.95 ?  25  GLN A C     1 
ATOM   165   O  O     . GLN A 1 25  ? 117.288 117.270 85.079  1.00 61.19 ?  25  GLN A O     1 
ATOM   166   C  CB    . GLN A 1 25  ? 116.296 114.923 83.852  1.00 61.01 ?  25  GLN A CB    1 
ATOM   167   C  CG    . GLN A 1 25  ? 116.007 113.523 83.342  1.00 61.65 ?  25  GLN A CG    1 
ATOM   168   C  CD    . GLN A 1 25  ? 114.553 113.133 83.504  1.00 62.47 ?  25  GLN A CD    1 
ATOM   169   O  OE1   . GLN A 1 25  ? 113.728 113.394 82.629  1.00 62.18 ?  25  GLN A OE1   1 
ATOM   170   N  NE2   . GLN A 1 25  ? 114.231 112.503 84.628  1.00 60.78 ?  25  GLN A NE2   1 
ATOM   171   N  N     . PHE A 1 26  ? 119.012 117.422 83.637  1.00 57.38 ?  26  PHE A N     1 
ATOM   172   C  CA    . PHE A 1 26  ? 119.406 118.741 84.120  1.00 55.95 ?  26  PHE A CA    1 
ATOM   173   C  C     . PHE A 1 26  ? 118.387 119.809 83.746  1.00 57.41 ?  26  PHE A C     1 
ATOM   174   O  O     . PHE A 1 26  ? 118.249 120.807 84.461  1.00 56.88 ?  26  PHE A O     1 
ATOM   175   C  CB    . PHE A 1 26  ? 120.785 119.108 83.574  1.00 53.29 ?  26  PHE A CB    1 
ATOM   176   C  CG    . PHE A 1 26  ? 121.902 118.296 84.162  1.00 54.17 ?  26  PHE A CG    1 
ATOM   177   C  CD1   . PHE A 1 26  ? 122.092 118.244 85.531  1.00 54.44 ?  26  PHE A CD1   1 
ATOM   178   C  CD2   . PHE A 1 26  ? 122.760 117.582 83.345  1.00 55.39 ?  26  PHE A CD2   1 
ATOM   179   C  CE1   . PHE A 1 26  ? 123.117 117.496 86.074  1.00 53.11 ?  26  PHE A CE1   1 
ATOM   180   C  CE2   . PHE A 1 26  ? 123.786 116.833 83.883  1.00 54.08 ?  26  PHE A CE2   1 
ATOM   181   C  CZ    . PHE A 1 26  ? 123.965 116.791 85.249  1.00 51.66 ?  26  PHE A CZ    1 
ATOM   182   N  N     . ASP A 1 27  ? 117.667 119.623 82.637  1.00 62.63 ?  27  ASP A N     1 
ATOM   183   C  CA    . ASP A 1 27  ? 116.673 120.598 82.206  1.00 61.91 ?  27  ASP A CA    1 
ATOM   184   C  C     . ASP A 1 27  ? 115.474 120.676 83.141  1.00 62.06 ?  27  ASP A C     1 
ATOM   185   O  O     . ASP A 1 27  ? 114.671 121.607 83.009  1.00 62.82 ?  27  ASP A O     1 
ATOM   186   C  CB    . ASP A 1 27  ? 116.198 120.273 80.789  1.00 61.74 ?  27  ASP A CB    1 
ATOM   187   C  CG    . ASP A 1 27  ? 116.172 121.492 79.890  1.00 65.25 ?  27  ASP A CG    1 
ATOM   188   O  OD1   . ASP A 1 27  ? 116.153 121.322 78.652  1.00 66.74 ?  27  ASP A OD1   1 
ATOM   189   O  OD2   . ASP A 1 27  ? 116.170 122.623 80.419  1.00 65.33 -1 27  ASP A OD2   1 
ATOM   190   N  N     . LYS A 1 28  ? 115.327 119.727 84.067  1.00 58.49 ?  28  LYS A N     1 
ATOM   191   C  CA    . LYS A 1 28  ? 114.218 119.783 85.012  1.00 59.07 ?  28  LYS A CA    1 
ATOM   192   C  C     . LYS A 1 28  ? 114.335 120.979 85.947  1.00 59.76 ?  28  LYS A C     1 
ATOM   193   O  O     . LYS A 1 28  ? 113.316 121.478 86.439  1.00 62.05 ?  28  LYS A O     1 
ATOM   194   C  CB    . LYS A 1 28  ? 114.149 118.489 85.820  1.00 58.92 ?  28  LYS A CB    1 
ATOM   195   C  CG    . LYS A 1 28  ? 113.790 117.269 84.996  1.00 60.16 ?  28  LYS A CG    1 
ATOM   196   C  CD    . LYS A 1 28  ? 112.326 117.287 84.597  1.00 61.07 ?  28  LYS A CD    1 
ATOM   197   C  CE    . LYS A 1 28  ? 112.030 116.226 83.553  1.00 60.92 ?  28  LYS A CE    1 
ATOM   198   N  NZ    . LYS A 1 28  ? 110.576 116.138 83.252  1.00 61.66 1  28  LYS A NZ    1 
ATOM   199   N  N     . ASP A 1 29  ? 115.557 121.452 86.204  1.00 56.42 ?  29  ASP A N     1 
ATOM   200   C  CA    . ASP A 1 29  ? 115.736 122.581 87.108  1.00 54.47 ?  29  ASP A CA    1 
ATOM   201   C  C     . ASP A 1 29  ? 115.188 123.871 86.514  1.00 53.46 ?  29  ASP A C     1 
ATOM   202   O  O     . ASP A 1 29  ? 114.743 124.753 87.258  1.00 55.08 ?  29  ASP A O     1 
ATOM   203   C  CB    . ASP A 1 29  ? 117.212 122.741 87.464  1.00 52.84 ?  29  ASP A CB    1 
ATOM   204   C  CG    . ASP A 1 29  ? 117.432 122.946 88.948  1.00 56.37 ?  29  ASP A CG    1 
ATOM   205   O  OD1   . ASP A 1 29  ? 116.561 122.530 89.739  1.00 56.68 ?  29  ASP A OD1   1 
ATOM   206   O  OD2   . ASP A 1 29  ? 118.477 123.514 89.324  1.00 55.59 -1 29  ASP A OD2   1 
ATOM   207   N  N     . LYS A 1 30  ? 115.221 124.009 85.187  1.00 54.13 ?  30  LYS A N     1 
ATOM   208   C  CA    . LYS A 1 30  ? 114.555 125.139 84.548  1.00 56.39 ?  30  LYS A CA    1 
ATOM   209   C  C     . LYS A 1 30  ? 113.046 125.051 84.734  1.00 55.12 ?  30  LYS A C     1 
ATOM   210   O  O     . LYS A 1 30  ? 112.391 126.039 85.091  1.00 59.35 ?  30  LYS A O     1 
ATOM   211   C  CB    . LYS A 1 30  ? 114.918 125.188 83.064  1.00 55.60 ?  30  LYS A CB    1 
ATOM   212   C  CG    . LYS A 1 30  ? 114.320 126.365 82.314  1.00 57.24 ?  30  LYS A CG    1 
ATOM   213   C  CD    . LYS A 1 30  ? 115.310 126.939 81.314  1.00 57.04 ?  30  LYS A CD    1 
ATOM   214   C  CE    . LYS A 1 30  ? 114.737 128.156 80.607  1.00 57.35 ?  30  LYS A CE    1 
ATOM   215   N  NZ    . LYS A 1 30  ? 114.209 127.812 79.258  1.00 56.39 1  30  LYS A NZ    1 
ATOM   216   N  N     . GLU A 1 31  ? 112.480 123.864 84.516  1.00 52.94 ?  31  GLU A N     1 
ATOM   217   C  CA    . GLU A 1 31  ? 111.068 123.657 84.814  1.00 53.56 ?  31  GLU A CA    1 
ATOM   218   C  C     . GLU A 1 31  ? 110.802 123.808 86.304  1.00 54.66 ?  31  GLU A C     1 
ATOM   219   O  O     . GLU A 1 31  ? 109.753 124.321 86.707  1.00 56.52 ?  31  GLU A O     1 
ATOM   220   C  CB    . GLU A 1 31  ? 110.623 122.281 84.324  1.00 55.25 ?  31  GLU A CB    1 
ATOM   221   C  CG    . GLU A 1 31  ? 110.140 122.259 82.886  1.00 56.83 ?  31  GLU A CG    1 
ATOM   222   C  CD    . GLU A 1 31  ? 110.425 120.940 82.196  1.00 60.89 ?  31  GLU A CD    1 
ATOM   223   O  OE1   . GLU A 1 31  ? 111.144 120.105 82.782  1.00 60.98 ?  31  GLU A OE1   1 
ATOM   224   O  OE2   . GLU A 1 31  ? 109.929 120.738 81.068  1.00 58.42 -1 31  GLU A OE2   1 
ATOM   225   N  N     . ALA A 1 32  ? 111.749 123.374 87.140  1.00 50.02 ?  32  ALA A N     1 
ATOM   226   C  CA    . ALA A 1 32  ? 111.577 123.507 88.582  1.00 49.58 ?  32  ALA A CA    1 
ATOM   227   C  C     . ALA A 1 32  ? 111.476 124.968 88.995  1.00 52.01 ?  32  ALA A C     1 
ATOM   228   O  O     . ALA A 1 32  ? 110.595 125.335 89.777  1.00 51.91 ?  32  ALA A O     1 
ATOM   229   C  CB    . ALA A 1 32  ? 112.728 122.822 89.316  1.00 48.80 ?  32  ALA A CB    1 
ATOM   230   N  N     . VAL A 1 33  ? 112.354 125.824 88.467  1.00 53.52 ?  33  VAL A N     1 
ATOM   231   C  CA    . VAL A 1 33  ? 112.317 127.235 88.842  1.00 52.03 ?  33  VAL A CA    1 
ATOM   232   C  C     . VAL A 1 33  ? 111.107 127.928 88.221  1.00 52.95 ?  33  VAL A C     1 
ATOM   233   O  O     . VAL A 1 33  ? 110.505 128.818 88.835  1.00 54.60 ?  33  VAL A O     1 
ATOM   234   C  CB    . VAL A 1 33  ? 113.642 127.933 88.478  1.00 49.44 ?  33  VAL A CB    1 
ATOM   235   C  CG1   . VAL A 1 33  ? 113.784 128.122 86.978  1.00 51.09 ?  33  VAL A CG1   1 
ATOM   236   C  CG2   . VAL A 1 33  ? 113.752 129.267 89.195  1.00 49.46 ?  33  VAL A CG2   1 
ATOM   237   N  N     . HIS A 1 34  ? 110.721 127.527 87.006  1.00 50.73 ?  34  HIS A N     1 
ATOM   238   C  CA    . HIS A 1 34  ? 109.532 128.103 86.386  1.00 50.74 ?  34  HIS A CA    1 
ATOM   239   C  C     . HIS A 1 34  ? 108.290 127.798 87.218  1.00 52.66 ?  34  HIS A C     1 
ATOM   240   O  O     . HIS A 1 34  ? 107.466 128.685 87.483  1.00 53.04 ?  34  HIS A O     1 
ATOM   241   C  CB    . HIS A 1 34  ? 109.396 127.570 84.957  1.00 53.19 ?  34  HIS A CB    1 
ATOM   242   C  CG    . HIS A 1 34  ? 108.301 128.208 84.155  1.00 55.22 ?  34  HIS A CG    1 
ATOM   243   N  ND1   . HIS A 1 34  ? 107.069 128.530 84.682  1.00 54.82 ?  34  HIS A ND1   1 
ATOM   244   C  CD2   . HIS A 1 34  ? 108.262 128.584 82.856  1.00 54.74 ?  34  HIS A CD2   1 
ATOM   245   C  CE1   . HIS A 1 34  ? 106.317 129.073 83.741  1.00 55.21 ?  34  HIS A CE1   1 
ATOM   246   N  NE2   . HIS A 1 34  ? 107.020 129.121 82.624  1.00 55.54 ?  34  HIS A NE2   1 
ATOM   247   N  N     . SER A 1 35  ? 108.151 126.541 87.651  1.00 54.59 ?  35  SER A N     1 
ATOM   248   C  CA    . SER A 1 35  ? 107.037 126.168 88.513  1.00 51.97 ?  35  SER A CA    1 
ATOM   249   C  C     . SER A 1 35  ? 107.127 126.869 89.861  1.00 52.12 ?  35  SER A C     1 
ATOM   250   O  O     . SER A 1 35  ? 106.112 127.327 90.395  1.00 54.74 ?  35  SER A O     1 
ATOM   251   C  CB    . SER A 1 35  ? 107.003 124.652 88.701  1.00 51.86 ?  35  SER A CB    1 
ATOM   252   O  OG    . SER A 1 35  ? 106.224 124.300 89.828  1.00 54.09 ?  35  SER A OG    1 
ATOM   253   N  N     . TYR A 1 36  ? 108.334 126.962 90.424  1.00 51.70 ?  36  TYR A N     1 
ATOM   254   C  CA    . TYR A 1 36  ? 108.523 127.665 91.686  1.00 51.33 ?  36  TYR A CA    1 
ATOM   255   C  C     . TYR A 1 36  ? 107.978 129.077 91.599  1.00 48.41 ?  36  TYR A C     1 
ATOM   256   O  O     . TYR A 1 36  ? 107.179 129.500 92.440  1.00 48.38 ?  36  TYR A O     1 
ATOM   257   C  CB    . TYR A 1 36  ? 110.006 127.681 92.056  1.00 47.92 ?  36  TYR A CB    1 
ATOM   258   C  CG    . TYR A 1 36  ? 110.331 128.470 93.303  1.00 49.41 ?  36  TYR A CG    1 
ATOM   259   C  CD1   . TYR A 1 36  ? 109.783 128.127 94.531  1.00 47.81 ?  36  TYR A CD1   1 
ATOM   260   C  CD2   . TYR A 1 36  ? 111.195 129.556 93.253  1.00 48.66 ?  36  TYR A CD2   1 
ATOM   261   C  CE1   . TYR A 1 36  ? 110.084 128.843 95.670  1.00 46.14 ?  36  TYR A CE1   1 
ATOM   262   C  CE2   . TYR A 1 36  ? 111.500 130.279 94.386  1.00 46.68 ?  36  TYR A CE2   1 
ATOM   263   C  CZ    . TYR A 1 36  ? 110.942 129.918 95.592  1.00 48.10 ?  36  TYR A CZ    1 
ATOM   264   O  OH    . TYR A 1 36  ? 111.245 130.637 96.725  1.00 50.06 ?  36  TYR A OH    1 
ATOM   265   N  N     . PHE A 1 37  ? 108.355 129.801 90.548  1.00 52.38 ?  37  PHE A N     1 
ATOM   266   C  CA    . PHE A 1 37  ? 107.857 131.159 90.388  1.00 52.15 ?  37  PHE A CA    1 
ATOM   267   C  C     . PHE A 1 37  ? 106.345 131.167 90.219  1.00 53.54 ?  37  PHE A C     1 
ATOM   268   O  O     . PHE A 1 37  ? 105.626 131.660 91.094  1.00 56.56 ?  37  PHE A O     1 
ATOM   269   C  CB    . PHE A 1 37  ? 108.553 131.847 89.218  1.00 54.60 ?  37  PHE A CB    1 
ATOM   270   C  CG    . PHE A 1 37  ? 109.831 132.516 89.609  1.00 53.80 ?  37  PHE A CG    1 
ATOM   271   C  CD1   . PHE A 1 37  ? 109.815 133.773 90.185  1.00 51.23 ?  37  PHE A CD1   1 
ATOM   272   C  CD2   . PHE A 1 37  ? 111.043 131.877 89.437  1.00 53.12 ?  37  PHE A CD2   1 
ATOM   273   C  CE1   . PHE A 1 37  ? 110.986 134.388 90.562  1.00 52.41 ?  37  PHE A CE1   1 
ATOM   274   C  CE2   . PHE A 1 37  ? 112.214 132.488 89.811  1.00 52.36 ?  37  PHE A CE2   1 
ATOM   275   C  CZ    . PHE A 1 37  ? 112.187 133.743 90.377  1.00 52.98 ?  37  PHE A CZ    1 
ATOM   276   N  N     . VAL A 1 38  ? 105.842 130.539 89.151  1.00 56.41 ?  38  VAL A N     1 
ATOM   277   C  CA    . VAL A 1 38  ? 104.427 130.661 88.812  1.00 55.88 ?  38  VAL A CA    1 
ATOM   278   C  C     . VAL A 1 38  ? 103.495 129.973 89.798  1.00 55.62 ?  38  VAL A C     1 
ATOM   279   O  O     . VAL A 1 38  ? 102.273 130.072 89.639  1.00 57.68 ?  38  VAL A O     1 
ATOM   280   C  CB    . VAL A 1 38  ? 104.143 130.116 87.399  1.00 54.03 ?  38  VAL A CB    1 
ATOM   281   C  CG1   . VAL A 1 38  ? 105.071 130.766 86.389  1.00 55.29 ?  38  VAL A CG1   1 
ATOM   282   C  CG2   . VAL A 1 38  ? 104.269 128.602 87.373  1.00 52.16 ?  38  VAL A CG2   1 
ATOM   283   N  N     . ASP A 1 39  ? 104.019 129.281 90.812  1.00 54.34 ?  39  ASP A N     1 
ATOM   284   C  CA    . ASP A 1 39  ? 103.162 128.661 91.809  1.00 53.08 ?  39  ASP A CA    1 
ATOM   285   C  C     . ASP A 1 39  ? 103.370 129.172 93.226  1.00 57.49 ?  39  ASP A C     1 
ATOM   286   O  O     . ASP A 1 39  ? 102.470 129.002 94.054  1.00 61.79 ?  39  ASP A O     1 
ATOM   287   C  CB    . ASP A 1 39  ? 103.352 127.136 91.805  1.00 55.36 ?  39  ASP A CB    1 
ATOM   288   C  CG    . ASP A 1 39  ? 103.068 126.517 90.450  1.00 58.49 ?  39  ASP A CG    1 
ATOM   289   O  OD1   . ASP A 1 39  ? 102.224 127.064 89.711  1.00 59.03 ?  39  ASP A OD1   1 
ATOM   290   O  OD2   . ASP A 1 39  ? 103.684 125.481 90.124  1.00 58.25 -1 39  ASP A OD2   1 
ATOM   291   N  N     . TYR A 1 40  ? 104.515 129.778 93.538  1.00 56.20 ?  40  TYR A N     1 
ATOM   292   C  CA    . TYR A 1 40  ? 104.752 130.336 94.862  1.00 55.34 ?  40  TYR A CA    1 
ATOM   293   C  C     . TYR A 1 40  ? 105.053 131.825 94.825  1.00 59.10 ?  40  TYR A C     1 
ATOM   294   O  O     . TYR A 1 40  ? 104.463 132.591 95.593  1.00 61.95 ?  40  TYR A O     1 
ATOM   295   C  CB    . TYR A 1 40  ? 105.910 129.587 95.540  1.00 54.12 ?  40  TYR A CB    1 
ATOM   296   C  CG    . TYR A 1 40  ? 106.064 129.896 97.010  1.00 54.91 ?  40  TYR A CG    1 
ATOM   297   C  CD1   . TYR A 1 40  ? 105.045 129.615 97.909  1.00 55.80 ?  40  TYR A CD1   1 
ATOM   298   C  CD2   . TYR A 1 40  ? 107.228 130.472 97.497  1.00 55.91 ?  40  TYR A CD2   1 
ATOM   299   C  CE1   . TYR A 1 40  ? 105.183 129.897 99.253  1.00 57.94 ?  40  TYR A CE1   1 
ATOM   300   C  CE2   . TYR A 1 40  ? 107.375 130.757 98.839  1.00 58.46 ?  40  TYR A CE2   1 
ATOM   301   C  CZ    . TYR A 1 40  ? 106.350 130.470 99.712  1.00 60.69 ?  40  TYR A CZ    1 
ATOM   302   O  OH    . TYR A 1 40  ? 106.492 130.753 101.050 1.00 61.32 ?  40  TYR A OH    1 
ATOM   303   N  N     . ILE A 1 41  ? 105.946 132.261 93.936  1.00 55.06 ?  41  ILE A N     1 
ATOM   304   C  CA    . ILE A 1 41  ? 106.535 133.588 94.071  1.00 54.10 ?  41  ILE A CA    1 
ATOM   305   C  C     . ILE A 1 41  ? 105.574 134.657 93.575  1.00 53.77 ?  41  ILE A C     1 
ATOM   306   O  O     . ILE A 1 41  ? 105.295 135.633 94.280  1.00 56.11 ?  41  ILE A O     1 
ATOM   307   C  CB    . ILE A 1 41  ? 107.883 133.648 93.328  1.00 53.23 ?  41  ILE A CB    1 
ATOM   308   C  CG1   . ILE A 1 41  ? 108.897 132.711 93.984  1.00 51.97 ?  41  ILE A CG1   1 
ATOM   309   C  CG2   . ILE A 1 41  ? 108.416 135.069 93.310  1.00 52.91 ?  41  ILE A CG2   1 
ATOM   310   C  CD1   . ILE A 1 41  ? 109.197 133.044 95.420  1.00 49.09 ?  41  ILE A CD1   1 
ATOM   311   N  N     . ASN A 1 42  ? 105.050 134.490 92.359  1.00 55.14 ?  42  ASN A N     1 
ATOM   312   C  CA    . ASN A 1 42  ? 104.090 135.454 91.835  1.00 57.04 ?  42  ASN A CA    1 
ATOM   313   C  C     . ASN A 1 42  ? 102.821 135.489 92.675  1.00 60.67 ?  42  ASN A C     1 
ATOM   314   O  O     . ASN A 1 42  ? 102.152 136.526 92.747  1.00 60.98 ?  42  ASN A O     1 
ATOM   315   C  CB    . ASN A 1 42  ? 103.763 135.125 90.379  1.00 56.57 ?  42  ASN A CB    1 
ATOM   316   C  CG    . ASN A 1 42  ? 104.993 135.124 89.492  1.00 57.49 ?  42  ASN A CG    1 
ATOM   317   O  OD1   . ASN A 1 42  ? 106.046 135.631 89.874  1.00 61.31 ?  42  ASN A OD1   1 
ATOM   318   N  ND2   . ASN A 1 42  ? 104.864 134.552 88.302  1.00 57.43 ?  42  ASN A ND2   1 
ATOM   319   N  N     . GLN A 1 43  ? 102.474 134.370 93.313  1.00 62.95 ?  43  GLN A N     1 
ATOM   320   C  CA    . GLN A 1 43  ? 101.313 134.351 94.196  1.00 61.34 ?  43  GLN A CA    1 
ATOM   321   C  C     . GLN A 1 43  ? 101.591 135.101 95.493  1.00 59.55 ?  43  GLN A C     1 
ATOM   322   O  O     . GLN A 1 43  ? 100.748 135.875 95.962  1.00 62.85 ?  43  GLN A O     1 
ATOM   323   C  CB    . GLN A 1 43  ? 100.899 132.909 94.488  1.00 60.93 ?  43  GLN A CB    1 
ATOM   324   C  CG    . GLN A 1 43  ? 101.070 131.953 93.314  1.00 61.60 ?  43  GLN A CG    1 
ATOM   325   C  CD    . GLN A 1 43  ? 100.016 132.138 92.237  1.00 64.24 ?  43  GLN A CD    1 
ATOM   326   O  OE1   . GLN A 1 43  ? 99.967  133.170 91.567  1.00 62.89 ?  43  GLN A OE1   1 
ATOM   327   N  NE2   . GLN A 1 43  ? 99.168  131.132 92.064  1.00 62.68 ?  43  GLN A NE2   1 
ATOM   328   N  N     . ASN A 1 44  ? 102.766 134.892 96.083  1.00 54.88 ?  44  ASN A N     1 
ATOM   329   C  CA    . ASN A 1 44  ? 103.119 135.496 97.360  1.00 56.20 ?  44  ASN A CA    1 
ATOM   330   C  C     . ASN A 1 44  ? 103.752 136.873 97.221  1.00 56.44 ?  44  ASN A C     1 
ATOM   331   O  O     . ASN A 1 44  ? 104.127 137.470 98.234  1.00 57.09 ?  44  ASN A O     1 
ATOM   332   C  CB    . ASN A 1 44  ? 104.067 134.573 98.133  1.00 56.48 ?  44  ASN A CB    1 
ATOM   333   C  CG    . ASN A 1 44  ? 103.353 133.380 98.739  1.00 59.38 ?  44  ASN A CG    1 
ATOM   334   O  OD1   . ASN A 1 44  ? 102.997 133.389 99.917  1.00 60.88 ?  44  ASN A OD1   1 
ATOM   335   N  ND2   . ASN A 1 44  ? 103.140 132.347 97.934  1.00 58.08 ?  44  ASN A ND2   1 
ATOM   336   N  N     . THR A 1 45  ? 103.885 137.390 96.004  1.00 58.13 ?  45  THR A N     1 
ATOM   337   C  CA    . THR A 1 45  ? 104.473 138.703 95.783  1.00 59.07 ?  45  THR A CA    1 
ATOM   338   C  C     . THR A 1 45  ? 103.409 139.782 95.920  1.00 59.02 ?  45  THR A C     1 
ATOM   339   O  O     . THR A 1 45  ? 102.359 139.714 95.273  1.00 60.05 ?  45  THR A O     1 
ATOM   340   C  CB    . THR A 1 45  ? 105.120 138.785 94.401  1.00 58.07 ?  45  THR A CB    1 
ATOM   341   O  OG1   . THR A 1 45  ? 106.177 137.822 94.310  1.00 59.58 ?  45  THR A OG1   1 
ATOM   342   C  CG2   . THR A 1 45  ? 105.683 140.175 94.158  1.00 55.65 ?  45  THR A CG2   1 
ATOM   343   N  N     . VAL A 1 46  ? 103.684 140.776 96.764  1.00 60.32 ?  46  VAL A N     1 
ATOM   344   C  CA    . VAL A 1 46  ? 102.818 141.945 96.854  1.00 60.71 ?  46  VAL A CA    1 
ATOM   345   C  C     . VAL A 1 46  ? 103.052 142.814 95.627  1.00 60.62 ?  46  VAL A C     1 
ATOM   346   O  O     . VAL A 1 46  ? 104.185 143.225 95.347  1.00 62.72 ?  46  VAL A O     1 
ATOM   347   C  CB    . VAL A 1 46  ? 103.080 142.728 98.146  1.00 60.03 ?  46  VAL A CB    1 
ATOM   348   C  CG1   . VAL A 1 46  ? 102.038 143.816 98.326  1.00 60.24 ?  46  VAL A CG1   1 
ATOM   349   C  CG2   . VAL A 1 46  ? 103.091 141.795 99.339  1.00 59.25 ?  46  VAL A CG2   1 
ATOM   350   N  N     . PHE A 1 47  ? 101.985 143.100 94.889  1.00 64.09 ?  47  PHE A N     1 
ATOM   351   C  CA    . PHE A 1 47  ? 102.063 143.910 93.682  1.00 66.23 ?  47  PHE A CA    1 
ATOM   352   C  C     . PHE A 1 47  ? 101.266 145.188 93.885  1.00 67.45 ?  47  PHE A C     1 
ATOM   353   O  O     . PHE A 1 47  ? 100.121 145.147 94.346  1.00 67.74 ?  47  PHE A O     1 
ATOM   354   C  CB    . PHE A 1 47  ? 101.543 143.144 92.462  1.00 67.11 ?  47  PHE A CB    1 
ATOM   355   C  CG    . PHE A 1 47  ? 101.668 143.906 91.174  1.00 68.09 ?  47  PHE A CG    1 
ATOM   356   C  CD1   . PHE A 1 47  ? 102.869 143.934 90.484  1.00 67.12 ?  47  PHE A CD1   1 
ATOM   357   C  CD2   . PHE A 1 47  ? 100.584 144.591 90.649  1.00 66.60 ?  47  PHE A CD2   1 
ATOM   358   C  CE1   . PHE A 1 47  ? 102.988 144.633 89.299  1.00 67.08 ?  47  PHE A CE1   1 
ATOM   359   C  CE2   . PHE A 1 47  ? 100.697 145.291 89.463  1.00 67.40 ?  47  PHE A CE2   1 
ATOM   360   C  CZ    . PHE A 1 47  ? 101.901 145.313 88.787  1.00 68.47 ?  47  PHE A CZ    1 
ATOM   361   N  N     . PHE A 1 48  ? 101.879 146.316 93.546  1.00 66.92 ?  48  PHE A N     1 
ATOM   362   C  CA    . PHE A 1 48  ? 101.272 147.627 93.686  1.00 64.94 ?  48  PHE A CA    1 
ATOM   363   C  C     . PHE A 1 48  ? 100.900 148.167 92.313  1.00 65.55 ?  48  PHE A C     1 
ATOM   364   O  O     . PHE A 1 48  ? 101.425 147.726 91.286  1.00 67.21 ?  48  PHE A O     1 
ATOM   365   C  CB    . PHE A 1 48  ? 102.217 148.599 94.402  1.00 63.60 ?  48  PHE A CB    1 
ATOM   366   C  CG    . PHE A 1 48  ? 102.675 148.119 95.754  1.00 63.28 ?  48  PHE A CG    1 
ATOM   367   C  CD1   . PHE A 1 48  ? 102.177 148.692 96.910  1.00 64.12 ?  48  PHE A CD1   1 
ATOM   368   C  CD2   . PHE A 1 48  ? 103.622 147.114 95.868  1.00 63.11 ?  48  PHE A CD2   1 
ATOM   369   C  CE1   . PHE A 1 48  ? 102.596 148.257 98.149  1.00 65.24 ?  48  PHE A CE1   1 
ATOM   370   C  CE2   . PHE A 1 48  ? 104.044 146.677 97.105  1.00 63.83 ?  48  PHE A CE2   1 
ATOM   371   C  CZ    . PHE A 1 48  ? 103.532 147.249 98.245  1.00 64.21 ?  48  PHE A CZ    1 
ATOM   372   N  N     . HIS A 1 49  ? 99.974  149.128 92.304  1.00 68.07 ?  49  HIS A N     1 
ATOM   373   C  CA    . HIS A 1 49  ? 99.504  149.685 91.038  1.00 70.19 ?  49  HIS A CA    1 
ATOM   374   C  C     . HIS A 1 49  ? 100.639 150.351 90.271  1.00 69.96 ?  49  HIS A C     1 
ATOM   375   O  O     . HIS A 1 49  ? 100.758 150.179 89.053  1.00 70.21 ?  49  HIS A O     1 
ATOM   376   C  CB    . HIS A 1 49  ? 98.368  150.676 91.290  1.00 69.80 ?  49  HIS A CB    1 
ATOM   377   C  CG    . HIS A 1 49  ? 97.212  150.090 92.039  1.00 71.45 ?  49  HIS A CG    1 
ATOM   378   N  ND1   . HIS A 1 49  ? 97.257  149.825 93.390  1.00 71.84 ?  49  HIS A ND1   1 
ATOM   379   C  CD2   . HIS A 1 49  ? 95.978  149.718 91.624  1.00 70.55 ?  49  HIS A CD2   1 
ATOM   380   C  CE1   . HIS A 1 49  ? 96.101  149.315 93.776  1.00 69.89 ?  49  HIS A CE1   1 
ATOM   381   N  NE2   . HIS A 1 49  ? 95.308  149.239 92.723  1.00 71.70 ?  49  HIS A NE2   1 
ATOM   382   N  N     . ASN A 1 50  ? 101.483 151.109 90.965  1.00 67.49 ?  50  ASN A N     1 
ATOM   383   C  CA    . ASN A 1 50  ? 102.647 151.731 90.354  1.00 66.95 ?  50  ASN A CA    1 
ATOM   384   C  C     . ASN A 1 50  ? 103.806 151.686 91.338  1.00 65.92 ?  50  ASN A C     1 
ATOM   385   O  O     . ASN A 1 50  ? 103.627 151.420 92.529  1.00 67.91 ?  50  ASN A O     1 
ATOM   386   C  CB    . ASN A 1 50  ? 102.361 153.175 89.913  1.00 66.30 ?  50  ASN A CB    1 
ATOM   387   C  CG    . ASN A 1 50  ? 101.793 154.029 91.029  1.00 66.97 ?  50  ASN A CG    1 
ATOM   388   O  OD1   . ASN A 1 50  ? 101.684 153.590 92.172  1.00 66.48 ?  50  ASN A OD1   1 
ATOM   389   N  ND2   . ASN A 1 50  ? 101.430 155.263 90.700  1.00 66.32 ?  50  ASN A ND2   1 
ATOM   390   N  N     . LEU A 1 51  ? 105.010 151.941 90.818  1.00 60.19 ?  51  LEU A N     1 
ATOM   391   C  CA    . LEU A 1 51  ? 106.200 151.913 91.661  1.00 60.44 ?  51  LEU A CA    1 
ATOM   392   C  C     . LEU A 1 51  ? 106.147 152.980 92.748  1.00 62.18 ?  51  LEU A C     1 
ATOM   393   O  O     . LEU A 1 51  ? 106.736 152.799 93.819  1.00 64.40 ?  51  LEU A O     1 
ATOM   394   C  CB    . LEU A 1 51  ? 107.452 152.089 90.800  1.00 61.12 ?  51  LEU A CB    1 
ATOM   395   C  CG    . LEU A 1 51  ? 108.798 152.120 91.528  1.00 58.98 ?  51  LEU A CG    1 
ATOM   396   C  CD1   . LEU A 1 51  ? 109.072 150.789 92.204  1.00 58.21 ?  51  LEU A CD1   1 
ATOM   397   C  CD2   . LEU A 1 51  ? 109.918 152.488 90.572  1.00 58.63 ?  51  LEU A CD2   1 
ATOM   398   N  N     . LYS A 1 52  ? 105.456 154.094 92.492  1.00 62.24 ?  52  LYS A N     1 
ATOM   399   C  CA    . LYS A 1 52  ? 105.348 155.144 93.501  1.00 60.33 ?  52  LYS A CA    1 
ATOM   400   C  C     . LYS A 1 52  ? 104.627 154.642 94.744  1.00 61.87 ?  52  LYS A C     1 
ATOM   401   O  O     . LYS A 1 52  ? 105.068 154.895 95.871  1.00 61.87 ?  52  LYS A O     1 
ATOM   402   C  CB    . LYS A 1 52  ? 104.628 156.359 92.918  1.00 59.33 ?  52  LYS A CB    1 
ATOM   403   C  CG    . LYS A 1 52  ? 104.921 157.661 93.644  1.00 62.17 ?  52  LYS A CG    1 
ATOM   404   C  CD    . LYS A 1 52  ? 104.807 158.850 92.705  1.00 63.90 ?  52  LYS A CD    1 
ATOM   405   C  CE    . LYS A 1 52  ? 105.701 159.996 93.148  1.00 63.03 ?  52  LYS A CE    1 
ATOM   406   N  NZ    . LYS A 1 52  ? 105.952 159.974 94.615  1.00 61.51 1  52  LYS A NZ    1 
ATOM   407   N  N     . GLU A 1 53  ? 103.520 153.921 94.556  1.00 65.07 ?  53  GLU A N     1 
ATOM   408   C  CA    . GLU A 1 53  ? 102.802 153.358 95.693  1.00 65.62 ?  53  GLU A CA    1 
ATOM   409   C  C     . GLU A 1 53  ? 103.666 152.347 96.435  1.00 64.75 ?  53  GLU A C     1 
ATOM   410   O  O     . GLU A 1 53  ? 103.663 152.307 97.669  1.00 65.93 ?  53  GLU A O     1 
ATOM   411   C  CB    . GLU A 1 53  ? 101.497 152.715 95.223  1.00 65.41 ?  53  GLU A CB    1 
ATOM   412   C  CG    . GLU A 1 53  ? 100.804 151.857 96.268  1.00 67.11 ?  53  GLU A CG    1 
ATOM   413   C  CD    . GLU A 1 53  ? 99.548  151.194 95.735  1.00 69.03 ?  53  GLU A CD    1 
ATOM   414   O  OE1   . GLU A 1 53  ? 99.079  151.593 94.648  1.00 69.01 ?  53  GLU A OE1   1 
ATOM   415   O  OE2   . GLU A 1 53  ? 99.030  150.274 96.402  1.00 68.53 -1 53  GLU A OE2   1 
ATOM   416   N  N     . LYS A 1 54  ? 104.423 151.534 95.696  1.00 60.53 ?  54  LYS A N     1 
ATOM   417   C  CA    . LYS A 1 54  ? 105.302 150.554 96.326  1.00 62.09 ?  54  LYS A CA    1 
ATOM   418   C  C     . LYS A 1 54  ? 106.356 151.232 97.190  1.00 58.42 ?  54  LYS A C     1 
ATOM   419   O  O     . LYS A 1 54  ? 106.577 150.843 98.345  1.00 60.89 ?  54  LYS A O     1 
ATOM   420   C  CB    . LYS A 1 54  ? 105.964 149.691 95.253  1.00 61.73 ?  54  LYS A CB    1 
ATOM   421   C  CG    . LYS A 1 54  ? 107.050 148.773 95.778  1.00 59.32 ?  54  LYS A CG    1 
ATOM   422   C  CD    . LYS A 1 54  ? 107.358 147.668 94.790  1.00 59.69 ?  54  LYS A CD    1 
ATOM   423   C  CE    . LYS A 1 54  ? 108.274 146.626 95.399  1.00 60.84 ?  54  LYS A CE    1 
ATOM   424   N  NZ    . LYS A 1 54  ? 108.197 145.330 94.673  1.00 61.90 1  54  LYS A NZ    1 
ATOM   425   N  N     . LEU A 1 55  ? 107.019 152.253 96.646  1.00 56.48 ?  55  LEU A N     1 
ATOM   426   C  CA    . LEU A 1 55  ? 108.068 152.936 97.396  1.00 58.32 ?  55  LEU A CA    1 
ATOM   427   C  C     . LEU A 1 55  ? 107.495 153.679 98.595  1.00 61.53 ?  55  LEU A C     1 
ATOM   428   O  O     . LEU A 1 55  ? 108.100 153.680 99.673  1.00 63.78 ?  55  LEU A O     1 
ATOM   429   C  CB    . LEU A 1 55  ? 108.833 153.888 96.482  1.00 59.39 ?  55  LEU A CB    1 
ATOM   430   C  CG    . LEU A 1 55  ? 109.691 153.203 95.417  1.00 59.74 ?  55  LEU A CG    1 
ATOM   431   C  CD1   . LEU A 1 55  ? 110.334 154.232 94.511  1.00 59.60 ?  55  LEU A CD1   1 
ATOM   432   C  CD2   . LEU A 1 55  ? 110.743 152.317 96.063  1.00 59.41 ?  55  LEU A CD2   1 
ATOM   433   N  N     . ASP A 1 56  ? 106.332 154.315 98.432  1.00 65.92 ?  56  ASP A N     1 
ATOM   434   C  CA    . ASP A 1 56  ? 105.699 154.985 99.561  1.00 64.75 ?  56  ASP A CA    1 
ATOM   435   C  C     . ASP A 1 56  ? 105.327 153.988 100.652 1.00 64.19 ?  56  ASP A C     1 
ATOM   436   O  O     . ASP A 1 56  ? 105.537 154.250 101.841 1.00 65.16 ?  56  ASP A O     1 
ATOM   437   C  CB    . ASP A 1 56  ? 104.466 155.753 99.087  1.00 65.50 ?  56  ASP A CB    1 
ATOM   438   C  CG    . ASP A 1 56  ? 104.824 156.994 98.292  1.00 68.31 ?  56  ASP A CG    1 
ATOM   439   O  OD1   . ASP A 1 56  ? 105.956 157.496 98.450  1.00 67.57 ?  56  ASP A OD1   1 
ATOM   440   O  OD2   . ASP A 1 56  ? 103.974 157.467 97.509  1.00 67.50 -1 56  ASP A OD2   1 
ATOM   441   N  N     . TYR A 1 57  ? 104.788 152.831 100.261 1.00 59.50 ?  57  TYR A N     1 
ATOM   442   C  CA    . TYR A 1 57  ? 104.429 151.802 101.228 1.00 62.04 ?  57  TYR A CA    1 
ATOM   443   C  C     . TYR A 1 57  ? 105.657 151.295 101.971 1.00 61.86 ?  57  TYR A C     1 
ATOM   444   O  O     . TYR A 1 57  ? 105.609 151.066 103.185 1.00 63.68 ?  57  TYR A O     1 
ATOM   445   C  CB    . TYR A 1 57  ? 103.728 150.650 100.508 1.00 61.52 ?  57  TYR A CB    1 
ATOM   446   C  CG    . TYR A 1 57  ? 103.476 149.429 101.360 1.00 62.14 ?  57  TYR A CG    1 
ATOM   447   C  CD1   . TYR A 1 57  ? 102.420 149.393 102.259 1.00 62.07 ?  57  TYR A CD1   1 
ATOM   448   C  CD2   . TYR A 1 57  ? 104.307 148.321 101.284 1.00 63.16 ?  57  TYR A CD2   1 
ATOM   449   C  CE1   . TYR A 1 57  ? 102.184 148.277 103.034 1.00 62.91 ?  57  TYR A CE1   1 
ATOM   450   C  CE2   . TYR A 1 57  ? 104.083 147.207 102.063 1.00 63.73 ?  57  TYR A CE2   1 
ATOM   451   C  CZ    . TYR A 1 57  ? 103.022 147.191 102.938 1.00 63.36 ?  57  TYR A CZ    1 
ATOM   452   O  OH    . TYR A 1 57  ? 102.796 146.079 103.716 1.00 62.05 ?  57  TYR A OH    1 
ATOM   453   N  N     . LEU A 1 58  ? 106.768 151.107 101.255 1.00 56.04 ?  58  LEU A N     1 
ATOM   454   C  CA    . LEU A 1 58  ? 107.967 150.568 101.885 1.00 54.62 ?  58  LEU A CA    1 
ATOM   455   C  C     . LEU A 1 58  ? 108.628 151.591 102.801 1.00 55.12 ?  58  LEU A C     1 
ATOM   456   O  O     . LEU A 1 58  ? 109.145 151.234 103.866 1.00 58.06 ?  58  LEU A O     1 
ATOM   457   C  CB    . LEU A 1 58  ? 108.946 150.085 100.816 1.00 56.32 ?  58  LEU A CB    1 
ATOM   458   C  CG    . LEU A 1 58  ? 108.473 148.870 100.017 1.00 56.27 ?  58  LEU A CG    1 
ATOM   459   C  CD1   . LEU A 1 58  ? 109.233 148.757 98.710  1.00 55.04 ?  58  LEU A CD1   1 
ATOM   460   C  CD2   . LEU A 1 58  ? 108.617 147.601 100.832 1.00 56.23 ?  58  LEU A CD2   1 
ATOM   461   N  N     . VAL A 1 59  ? 108.630 152.865 102.407 1.00 60.11 ?  59  VAL A N     1 
ATOM   462   C  CA    . VAL A 1 59  ? 109.231 153.896 103.248 1.00 62.24 ?  59  VAL A CA    1 
ATOM   463   C  C     . VAL A 1 59  ? 108.382 154.138 104.490 1.00 64.10 ?  59  VAL A C     1 
ATOM   464   O  O     . VAL A 1 59  ? 108.902 154.237 105.607 1.00 63.20 ?  59  VAL A O     1 
ATOM   465   C  CB    . VAL A 1 59  ? 109.440 155.192 102.444 1.00 62.74 ?  59  VAL A CB    1 
ATOM   466   C  CG1   . VAL A 1 59  ? 109.884 156.319 103.359 1.00 60.59 ?  59  VAL A CG1   1 
ATOM   467   C  CG2   . VAL A 1 59  ? 110.466 154.971 101.343 1.00 62.18 ?  59  VAL A CG2   1 
ATOM   468   N  N     . GLU A 1 60  ? 107.060 154.233 104.314 1.00 64.88 ?  60  GLU A N     1 
ATOM   469   C  CA    . GLU A 1 60  ? 106.184 154.567 105.433 1.00 64.28 ?  60  GLU A CA    1 
ATOM   470   C  C     . GLU A 1 60  ? 106.176 153.473 106.493 1.00 65.21 ?  60  GLU A C     1 
ATOM   471   O  O     . GLU A 1 60  ? 106.156 153.768 107.694 1.00 67.47 ?  60  GLU A O     1 
ATOM   472   C  CB    . GLU A 1 60  ? 104.768 154.837 104.925 1.00 64.16 ?  60  GLU A CB    1 
ATOM   473   C  CG    . GLU A 1 60  ? 104.624 156.151 104.170 1.00 65.72 ?  60  GLU A CG    1 
ATOM   474   C  CD    . GLU A 1 60  ? 103.423 156.166 103.243 1.00 69.17 ?  60  GLU A CD    1 
ATOM   475   O  OE1   . GLU A 1 60  ? 102.584 155.246 103.337 1.00 68.12 ?  60  GLU A OE1   1 
ATOM   476   O  OE2   . GLU A 1 60  ? 103.318 157.099 102.418 1.00 67.57 -1 60  GLU A OE2   1 
ATOM   477   N  N     . ASN A 1 61  ? 106.190 152.208 106.077 1.00 59.25 ?  61  ASN A N     1 
ATOM   478   C  CA    . ASN A 1 61  ? 106.121 151.096 107.019 1.00 60.01 ?  61  ASN A CA    1 
ATOM   479   C  C     . ASN A 1 61  ? 107.488 150.618 107.484 1.00 61.33 ?  61  ASN A C     1 
ATOM   480   O  O     . ASN A 1 61  ? 107.625 149.437 107.831 1.00 64.86 ?  61  ASN A O     1 
ATOM   481   C  CB    . ASN A 1 61  ? 105.336 149.933 106.416 1.00 60.81 ?  61  ASN A CB    1 
ATOM   482   C  CG    . ASN A 1 61  ? 103.973 150.355 105.919 1.00 62.46 ?  61  ASN A CG    1 
ATOM   483   O  OD1   . ASN A 1 61  ? 103.679 151.544 105.813 1.00 63.19 ?  61  ASN A OD1   1 
ATOM   484   N  ND2   . ASN A 1 61  ? 103.117 149.382 105.653 1.00 61.88 ?  61  ASN A ND2   1 
ATOM   485   N  N     . GLN A 1 62  ? 108.490 151.498 107.482 1.00 57.49 ?  62  GLN A N     1 
ATOM   486   C  CA    . GLN A 1 62  ? 109.790 151.230 108.097 1.00 58.44 ?  62  GLN A CA    1 
ATOM   487   C  C     . GLN A 1 62  ? 110.519 150.070 107.426 1.00 57.89 ?  62  GLN A C     1 
ATOM   488   O  O     . GLN A 1 62  ? 111.292 149.356 108.069 1.00 58.51 ?  62  GLN A O     1 
ATOM   489   C  CB    . GLN A 1 62  ? 109.645 150.966 109.599 1.00 58.21 ?  62  GLN A CB    1 
ATOM   490   C  CG    . GLN A 1 62  ? 108.960 152.084 110.374 1.00 57.65 ?  62  GLN A CG    1 
ATOM   491   C  CD    . GLN A 1 62  ? 109.581 153.443 110.127 1.00 60.19 ?  62  GLN A CD    1 
ATOM   492   O  OE1   . GLN A 1 62  ? 110.557 153.822 110.776 1.00 59.91 ?  62  GLN A OE1   1 
ATOM   493   N  NE2   . GLN A 1 62  ? 109.022 154.184 109.178 1.00 58.82 ?  62  GLN A NE2   1 
ATOM   494   N  N     . TYR A 1 63  ? 110.280 149.866 106.130 1.00 55.04 ?  63  TYR A N     1 
ATOM   495   C  CA    . TYR A 1 63  ? 111.013 148.848 105.388 1.00 53.55 ?  63  TYR A CA    1 
ATOM   496   C  C     . TYR A 1 63  ? 112.268 149.410 104.737 1.00 53.47 ?  63  TYR A C     1 
ATOM   497   O  O     . TYR A 1 63  ? 113.314 148.752 104.738 1.00 52.88 ?  63  TYR A O     1 
ATOM   498   C  CB    . TYR A 1 63  ? 110.115 148.216 104.320 1.00 52.78 ?  63  TYR A CB    1 
ATOM   499   C  CG    . TYR A 1 63  ? 109.069 147.280 104.876 1.00 53.89 ?  63  TYR A CG    1 
ATOM   500   C  CD1   . TYR A 1 63  ? 109.421 146.243 105.728 1.00 52.87 ?  63  TYR A CD1   1 
ATOM   501   C  CD2   . TYR A 1 63  ? 107.730 147.430 104.545 1.00 55.05 ?  63  TYR A CD2   1 
ATOM   502   C  CE1   . TYR A 1 63  ? 108.469 145.385 106.238 1.00 53.91 ?  63  TYR A CE1   1 
ATOM   503   C  CE2   . TYR A 1 63  ? 106.770 146.578 105.051 1.00 55.36 ?  63  TYR A CE2   1 
ATOM   504   C  CZ    . TYR A 1 63  ? 107.145 145.558 105.896 1.00 56.36 ?  63  TYR A CZ    1 
ATOM   505   O  OH    . TYR A 1 63  ? 106.190 144.706 106.400 1.00 55.76 ?  63  TYR A OH    1 
ATOM   506   N  N     . TYR A 1 64  ? 112.186 150.616 104.187 1.00 49.94 ?  64  TYR A N     1 
ATOM   507   C  CA    . TYR A 1 64  ? 113.304 151.269 103.529 1.00 48.26 ?  64  TYR A CA    1 
ATOM   508   C  C     . TYR A 1 64  ? 113.766 152.469 104.343 1.00 50.88 ?  64  TYR A C     1 
ATOM   509   O  O     . TYR A 1 64  ? 113.165 152.837 105.355 1.00 53.87 ?  64  TYR A O     1 
ATOM   510   C  CB    . TYR A 1 64  ? 112.920 151.715 102.115 1.00 47.96 ?  64  TYR A CB    1 
ATOM   511   C  CG    . TYR A 1 64  ? 112.940 150.607 101.092 1.00 50.04 ?  64  TYR A CG    1 
ATOM   512   C  CD1   . TYR A 1 64  ? 113.382 149.334 101.425 1.00 48.97 ?  64  TYR A CD1   1 
ATOM   513   C  CD2   . TYR A 1 64  ? 112.517 150.834 99.792  1.00 49.89 ?  64  TYR A CD2   1 
ATOM   514   C  CE1   . TYR A 1 64  ? 113.399 148.320 100.493 1.00 45.60 ?  64  TYR A CE1   1 
ATOM   515   C  CE2   . TYR A 1 64  ? 112.533 149.829 98.854  1.00 48.10 ?  64  TYR A CE2   1 
ATOM   516   C  CZ    . TYR A 1 64  ? 112.973 148.574 99.208  1.00 47.41 ?  64  TYR A CZ    1 
ATOM   517   O  OH    . TYR A 1 64  ? 112.985 147.572 98.269  1.00 50.79 ?  64  TYR A OH    1 
ATOM   518   N  N     . GLU A 1 65  ? 114.849 153.082 103.882 1.00 53.79 ?  65  GLU A N     1 
ATOM   519   C  CA    . GLU A 1 65  ? 115.349 154.325 104.451 1.00 52.12 ?  65  GLU A CA    1 
ATOM   520   C  C     . GLU A 1 65  ? 114.978 155.476 103.529 1.00 55.07 ?  65  GLU A C     1 
ATOM   521   O  O     . GLU A 1 65  ? 115.186 155.397 102.314 1.00 56.78 ?  65  GLU A O     1 
ATOM   522   C  CB    . GLU A 1 65  ? 116.863 154.271 104.654 1.00 52.60 ?  65  GLU A CB    1 
ATOM   523   C  CG    . GLU A 1 65  ? 117.345 153.049 105.412 1.00 51.39 ?  65  GLU A CG    1 
ATOM   524   C  CD    . GLU A 1 65  ? 118.857 152.971 105.486 1.00 55.09 ?  65  GLU A CD    1 
ATOM   525   O  OE1   . GLU A 1 65  ? 119.523 153.363 104.504 1.00 57.01 ?  65  GLU A OE1   1 
ATOM   526   O  OE2   . GLU A 1 65  ? 119.379 152.520 106.526 1.00 54.12 -1 65  GLU A OE2   1 
ATOM   527   N  N     . GLU A 1 66  ? 114.420 156.539 104.106 1.00 58.01 ?  66  GLU A N     1 
ATOM   528   C  CA    . GLU A 1 66  ? 114.007 157.687 103.310 1.00 56.33 ?  66  GLU A CA    1 
ATOM   529   C  C     . GLU A 1 66  ? 115.190 158.517 102.831 1.00 56.91 ?  66  GLU A C     1 
ATOM   530   O  O     . GLU A 1 66  ? 115.109 159.129 101.762 1.00 57.92 ?  66  GLU A O     1 
ATOM   531   C  CB    . GLU A 1 66  ? 113.043 158.557 104.122 1.00 57.09 ?  66  GLU A CB    1 
ATOM   532   C  CG    . GLU A 1 66  ? 112.612 159.856 103.451 1.00 59.42 ?  66  GLU A CG    1 
ATOM   533   C  CD    . GLU A 1 66  ? 111.681 159.632 102.273 1.00 61.01 ?  66  GLU A CD    1 
ATOM   534   O  OE1   . GLU A 1 66  ? 110.483 159.968 102.392 1.00 58.42 ?  66  GLU A OE1   1 
ATOM   535   O  OE2   . GLU A 1 66  ? 112.145 159.135 101.225 1.00 62.31 -1 66  GLU A OE2   1 
ATOM   536   N  N     . GLU A 1 67  ? 116.288 158.538 103.591 1.00 58.05 ?  67  GLU A N     1 
ATOM   537   C  CA    . GLU A 1 67  ? 117.389 159.448 103.294 1.00 56.47 ?  67  GLU A CA    1 
ATOM   538   C  C     . GLU A 1 67  ? 118.023 159.149 101.939 1.00 57.31 ?  67  GLU A C     1 
ATOM   539   O  O     . GLU A 1 67  ? 118.276 160.066 101.149 1.00 57.76 ?  67  GLU A O     1 
ATOM   540   C  CB    . GLU A 1 67  ? 118.437 159.378 104.405 1.00 56.92 ?  67  GLU A CB    1 
ATOM   541   C  CG    . GLU A 1 67  ? 118.537 158.019 105.076 1.00 58.91 ?  67  GLU A CG    1 
ATOM   542   C  CD    . GLU A 1 67  ? 117.749 157.948 106.369 1.00 59.42 ?  67  GLU A CD    1 
ATOM   543   O  OE1   . GLU A 1 67  ? 116.502 157.943 106.308 1.00 57.57 ?  67  GLU A OE1   1 
ATOM   544   O  OE2   . GLU A 1 67  ? 118.377 157.901 107.447 1.00 62.17 -1 67  GLU A OE2   1 
ATOM   545   N  N     . PHE A 1 68  ? 118.286 157.874 101.648 1.00 54.61 ?  68  PHE A N     1 
ATOM   546   C  CA    . PHE A 1 68  ? 118.961 157.544 100.397 1.00 52.02 ?  68  PHE A CA    1 
ATOM   547   C  C     . PHE A 1 68  ? 118.020 157.624 99.203  1.00 51.81 ?  68  PHE A C     1 
ATOM   548   O  O     . PHE A 1 68  ? 118.462 157.941 98.094  1.00 55.05 ?  68  PHE A O     1 
ATOM   549   C  CB    . PHE A 1 68  ? 119.609 156.159 100.492 1.00 51.38 ?  68  PHE A CB    1 
ATOM   550   C  CG    . PHE A 1 68  ? 118.718 155.027 100.064 1.00 50.85 ?  68  PHE A CG    1 
ATOM   551   C  CD1   . PHE A 1 68  ? 117.811 154.471 100.945 1.00 51.28 ?  68  PHE A CD1   1 
ATOM   552   C  CD2   . PHE A 1 68  ? 118.813 154.499 98.786  1.00 48.03 ?  68  PHE A CD2   1 
ATOM   553   C  CE1   . PHE A 1 68  ? 116.997 153.427 100.555 1.00 48.97 ?  68  PHE A CE1   1 
ATOM   554   C  CE2   . PHE A 1 68  ? 118.004 153.454 98.393  1.00 46.98 ?  68  PHE A CE2   1 
ATOM   555   C  CZ    . PHE A 1 68  ? 117.098 152.915 99.279  1.00 48.15 ?  68  PHE A CZ    1 
ATOM   556   N  N     . LEU A 1 69  ? 116.730 157.346 99.403  1.00 50.98 ?  69  LEU A N     1 
ATOM   557   C  CA    . LEU A 1 69  ? 115.768 157.478 98.316  1.00 53.18 ?  69  LEU A CA    1 
ATOM   558   C  C     . LEU A 1 69  ? 115.417 158.930 98.030  1.00 53.68 ?  69  LEU A C     1 
ATOM   559   O  O     . LEU A 1 69  ? 114.876 159.223 96.958  1.00 54.19 ?  69  LEU A O     1 
ATOM   560   C  CB    . LEU A 1 69  ? 114.496 156.692 98.638  1.00 54.09 ?  69  LEU A CB    1 
ATOM   561   C  CG    . LEU A 1 69  ? 114.559 155.180 98.422  1.00 52.44 ?  69  LEU A CG    1 
ATOM   562   C  CD1   . LEU A 1 69  ? 113.344 154.500 99.026  1.00 51.87 ?  69  LEU A CD1   1 
ATOM   563   C  CD2   . LEU A 1 69  ? 114.680 154.855 96.945  1.00 50.13 ?  69  LEU A CD2   1 
ATOM   564   N  N     . SER A 1 70  ? 115.711 159.842 98.956  1.00 55.83 ?  70  SER A N     1 
ATOM   565   C  CA    . SER A 1 70  ? 115.389 161.251 98.775  1.00 54.06 ?  70  SER A CA    1 
ATOM   566   C  C     . SER A 1 70  ? 116.398 161.988 97.906  1.00 53.45 ?  70  SER A C     1 
ATOM   567   O  O     . SER A 1 70  ? 116.143 163.137 97.534  1.00 56.79 ?  70  SER A O     1 
ATOM   568   C  CB    . SER A 1 70  ? 115.286 161.945 100.136 1.00 54.37 ?  70  SER A CB    1 
ATOM   569   O  OG    . SER A 1 70  ? 116.558 162.065 100.744 1.00 54.27 ?  70  SER A OG    1 
ATOM   570   N  N     . LEU A 1 71  ? 117.529 161.365 97.576  1.00 50.47 ?  71  LEU A N     1 
ATOM   571   C  CA    . LEU A 1 71  ? 118.520 161.997 96.716  1.00 50.14 ?  71  LEU A CA    1 
ATOM   572   C  C     . LEU A 1 71  ? 118.176 161.888 95.238  1.00 50.99 ?  71  LEU A C     1 
ATOM   573   O  O     . LEU A 1 71  ? 118.865 162.495 94.412  1.00 50.24 ?  71  LEU A O     1 
ATOM   574   C  CB    . LEU A 1 71  ? 119.902 161.387 96.965  1.00 48.19 ?  71  LEU A CB    1 
ATOM   575   C  CG    . LEU A 1 71  ? 120.249 161.076 98.420  1.00 49.88 ?  71  LEU A CG    1 
ATOM   576   C  CD1   . LEU A 1 71  ? 121.255 159.944 98.497  1.00 51.77 ?  71  LEU A CD1   1 
ATOM   577   C  CD2   . LEU A 1 71  ? 120.781 162.318 99.113  1.00 51.24 ?  71  LEU A CD2   1 
ATOM   578   N  N     . TYR A 1 72  ? 117.136 161.137 94.887  1.00 48.11 ?  72  TYR A N     1 
ATOM   579   C  CA    . TYR A 1 72  ? 116.696 160.986 93.511  1.00 50.38 ?  72  TYR A CA    1 
ATOM   580   C  C     . TYR A 1 72  ? 115.259 161.463 93.375  1.00 52.50 ?  72  TYR A C     1 
ATOM   581   O  O     . TYR A 1 72  ? 114.420 161.187 94.238  1.00 52.67 ?  72  TYR A O     1 
ATOM   582   C  CB    . TYR A 1 72  ? 116.774 159.527 93.042  1.00 48.01 ?  72  TYR A CB    1 
ATOM   583   C  CG    . TYR A 1 72  ? 118.062 158.809 93.360  1.00 47.76 ?  72  TYR A CG    1 
ATOM   584   C  CD1   . TYR A 1 72  ? 118.251 158.192 94.589  1.00 46.66 ?  72  TYR A CD1   1 
ATOM   585   C  CD2   . TYR A 1 72  ? 119.077 158.719 92.419  1.00 46.11 ?  72  TYR A CD2   1 
ATOM   586   C  CE1   . TYR A 1 72  ? 119.419 157.527 94.879  1.00 44.18 ?  72  TYR A CE1   1 
ATOM   587   C  CE2   . TYR A 1 72  ? 120.248 158.051 92.698  1.00 42.59 ?  72  TYR A CE2   1 
ATOM   588   C  CZ    . TYR A 1 72  ? 120.414 157.459 93.930  1.00 44.18 ?  72  TYR A CZ    1 
ATOM   589   O  OH    . TYR A 1 72  ? 121.582 156.793 94.214  1.00 49.45 ?  72  TYR A OH    1 
ATOM   590   N  N     . SER A 1 73  ? 114.977 162.177 92.290  1.00 55.03 ?  73  SER A N     1 
ATOM   591   C  CA    . SER A 1 73  ? 113.595 162.403 91.904  1.00 56.45 ?  73  SER A CA    1 
ATOM   592   C  C     . SER A 1 73  ? 112.972 161.078 91.482  1.00 57.84 ?  73  SER A C     1 
ATOM   593   O  O     . SER A 1 73  ? 113.658 160.178 90.992  1.00 58.76 ?  73  SER A O     1 
ATOM   594   C  CB    . SER A 1 73  ? 113.510 163.419 90.765  1.00 57.18 ?  73  SER A CB    1 
ATOM   595   O  OG    . SER A 1 73  ? 113.699 162.795 89.509  1.00 57.54 ?  73  SER A OG    1 
ATOM   596   N  N     . PHE A 1 74  ? 111.658 160.955 91.687  1.00 58.15 ?  74  PHE A N     1 
ATOM   597   C  CA    . PHE A 1 74  ? 111.006 159.681 91.403  1.00 55.90 ?  74  PHE A CA    1 
ATOM   598   C  C     . PHE A 1 74  ? 111.124 159.272 89.943  1.00 58.32 ?  74  PHE A C     1 
ATOM   599   O  O     . PHE A 1 74  ? 111.048 158.077 89.642  1.00 60.17 ?  74  PHE A O     1 
ATOM   600   C  CB    . PHE A 1 74  ? 109.531 159.710 91.795  1.00 58.40 ?  74  PHE A CB    1 
ATOM   601   C  CG    . PHE A 1 74  ? 108.834 158.406 91.547  1.00 58.85 ?  74  PHE A CG    1 
ATOM   602   C  CD1   . PHE A 1 74  ? 109.074 157.314 92.361  1.00 57.77 ?  74  PHE A CD1   1 
ATOM   603   C  CD2   . PHE A 1 74  ? 107.973 158.261 90.472  1.00 58.58 ?  74  PHE A CD2   1 
ATOM   604   C  CE1   . PHE A 1 74  ? 108.453 156.107 92.120  1.00 59.26 ?  74  PHE A CE1   1 
ATOM   605   C  CE2   . PHE A 1 74  ? 107.348 157.058 90.228  1.00 59.84 ?  74  PHE A CE2   1 
ATOM   606   C  CZ    . PHE A 1 74  ? 107.590 155.980 91.050  1.00 61.18 ?  74  PHE A CZ    1 
ATOM   607   N  N     . GLU A 1 75  ? 111.309 160.223 89.026  1.00 61.63 ?  75  GLU A N     1 
ATOM   608   C  CA    . GLU A 1 75  ? 111.550 159.848 87.638  1.00 61.08 ?  75  GLU A CA    1 
ATOM   609   C  C     . GLU A 1 75  ? 112.861 159.083 87.502  1.00 62.99 ?  75  GLU A C     1 
ATOM   610   O  O     . GLU A 1 75  ? 112.947 158.111 86.744  1.00 62.51 ?  75  GLU A O     1 
ATOM   611   C  CB    . GLU A 1 75  ? 111.547 161.089 86.748  1.00 60.87 ?  75  GLU A CB    1 
ATOM   612   C  CG    . GLU A 1 75  ? 110.164 161.685 86.542  1.00 62.72 ?  75  GLU A CG    1 
ATOM   613   C  CD    . GLU A 1 75  ? 109.139 160.646 86.126  1.00 65.19 ?  75  GLU A CD    1 
ATOM   614   O  OE1   . GLU A 1 75  ? 109.325 160.014 85.065  1.00 65.33 ?  75  GLU A OE1   1 
ATOM   615   O  OE2   . GLU A 1 75  ? 108.148 160.459 86.862  1.00 64.89 -1 75  GLU A OE2   1 
ATOM   616   N  N     . ASP A 1 76  ? 113.888 159.498 88.245  1.00 58.05 ?  76  ASP A N     1 
ATOM   617   C  CA    . ASP A 1 76  ? 115.165 158.790 88.214  1.00 55.77 ?  76  ASP A CA    1 
ATOM   618   C  C     . ASP A 1 76  ? 115.047 157.394 88.815  1.00 55.43 ?  76  ASP A C     1 
ATOM   619   O  O     . ASP A 1 76  ? 115.618 156.433 88.284  1.00 60.04 ?  76  ASP A O     1 
ATOM   620   C  CB    . ASP A 1 76  ? 116.224 159.605 88.950  1.00 57.42 ?  76  ASP A CB    1 
ATOM   621   C  CG    . ASP A 1 76  ? 116.426 160.978 88.342  1.00 60.39 ?  76  ASP A CG    1 
ATOM   622   O  OD1   . ASP A 1 76  ? 116.395 161.088 87.098  1.00 59.97 ?  76  ASP A OD1   1 
ATOM   623   O  OD2   . ASP A 1 76  ? 116.618 161.946 89.106  1.00 59.16 -1 76  ASP A OD2   1 
ATOM   624   N  N     . ILE A 1 77  ? 114.320 157.261 89.927  1.00 51.09 ?  77  ILE A N     1 
ATOM   625   C  CA    . ILE A 1 77  ? 114.111 155.945 90.527  1.00 51.47 ?  77  ILE A CA    1 
ATOM   626   C  C     . ILE A 1 77  ? 113.334 155.049 89.574  1.00 51.41 ?  77  ILE A C     1 
ATOM   627   O  O     . ILE A 1 77  ? 113.622 153.852 89.442  1.00 53.07 ?  77  ILE A O     1 
ATOM   628   C  CB    . ILE A 1 77  ? 113.395 156.083 91.882  1.00 52.51 ?  77  ILE A CB    1 
ATOM   629   C  CG1   . ILE A 1 77  ? 114.098 157.124 92.751  1.00 52.79 ?  77  ILE A CG1   1 
ATOM   630   C  CG2   . ILE A 1 77  ? 113.341 154.740 92.588  1.00 51.51 ?  77  ILE A CG2   1 
ATOM   631   C  CD1   . ILE A 1 77  ? 113.689 157.087 94.204  1.00 52.94 ?  77  ILE A CD1   1 
ATOM   632   N  N     . LYS A 1 78  ? 112.330 155.614 88.901  1.00 54.77 ?  78  LYS A N     1 
ATOM   633   C  CA    . LYS A 1 78  ? 111.578 154.863 87.906  1.00 54.72 ?  78  LYS A CA    1 
ATOM   634   C  C     . LYS A 1 78  ? 112.480 154.407 86.769  1.00 54.66 ?  78  LYS A C     1 
ATOM   635   O  O     . LYS A 1 78  ? 112.374 153.268 86.308  1.00 57.65 ?  78  LYS A O     1 
ATOM   636   C  CB    . LYS A 1 78  ? 110.428 155.717 87.373  1.00 57.81 ?  78  LYS A CB    1 
ATOM   637   C  CG    . LYS A 1 78  ? 109.184 154.935 86.994  1.00 56.70 ?  78  LYS A CG    1 
ATOM   638   C  CD    . LYS A 1 78  ? 108.162 155.840 86.330  1.00 56.73 ?  78  LYS A CD    1 
ATOM   639   C  CE    . LYS A 1 78  ? 107.359 155.093 85.282  1.00 57.73 ?  78  LYS A CE    1 
ATOM   640   N  NZ    . LYS A 1 78  ? 105.929 154.964 85.675  1.00 57.58 1  78  LYS A NZ    1 
ATOM   641   N  N     . GLU A 1 79  ? 113.375 155.283 86.304  1.00 55.66 ?  79  GLU A N     1 
ATOM   642   C  CA    . GLU A 1 79  ? 114.312 154.902 85.251  1.00 55.52 ?  79  GLU A CA    1 
ATOM   643   C  C     . GLU A 1 79  ? 115.225 153.772 85.709  1.00 52.99 ?  79  GLU A C     1 
ATOM   644   O  O     . GLU A 1 79  ? 115.512 152.845 84.943  1.00 55.14 ?  79  GLU A O     1 
ATOM   645   C  CB    . GLU A 1 79  ? 115.140 156.114 84.825  1.00 56.06 ?  79  GLU A CB    1 
ATOM   646   C  CG    . GLU A 1 79  ? 114.398 157.113 83.958  1.00 56.91 ?  79  GLU A CG    1 
ATOM   647   C  CD    . GLU A 1 79  ? 115.266 158.291 83.563  1.00 60.38 ?  79  GLU A CD    1 
ATOM   648   O  OE1   . GLU A 1 79  ? 116.294 158.072 82.889  1.00 60.58 ?  79  GLU A OE1   1 
ATOM   649   O  OE2   . GLU A 1 79  ? 114.925 159.434 83.931  1.00 61.84 -1 79  GLU A OE2   1 
ATOM   650   N  N     . VAL A 1 80  ? 115.694 153.837 86.955  1.00 45.61 ?  80  VAL A N     1 
ATOM   651   C  CA    . VAL A 1 80  ? 116.544 152.776 87.492  1.00 43.99 ?  80  VAL A CA    1 
ATOM   652   C  C     . VAL A 1 80  ? 115.789 151.452 87.527  1.00 48.77 ?  80  VAL A C     1 
ATOM   653   O  O     . VAL A 1 80  ? 116.316 150.403 87.130  1.00 49.84 ?  80  VAL A O     1 
ATOM   654   C  CB    . VAL A 1 80  ? 117.063 153.176 88.886  1.00 43.52 ?  80  VAL A CB    1 
ATOM   655   C  CG1   . VAL A 1 80  ? 117.635 151.976 89.612  1.00 45.04 ?  80  VAL A CG1   1 
ATOM   656   C  CG2   . VAL A 1 80  ? 118.104 154.272 88.763  1.00 44.18 ?  80  VAL A CG2   1 
ATOM   657   N  N     . PHE A 1 81  ? 114.538 151.481 87.993  1.00 48.14 ?  81  PHE A N     1 
ATOM   658   C  CA    . PHE A 1 81  ? 113.748 150.256 88.059  1.00 44.30 ?  81  PHE A CA    1 
ATOM   659   C  C     . PHE A 1 81  ? 113.436 149.715 86.668  1.00 47.34 ?  81  PHE A C     1 
ATOM   660   O  O     . PHE A 1 81  ? 113.393 148.496 86.466  1.00 49.22 ?  81  PHE A O     1 
ATOM   661   C  CB    . PHE A 1 81  ? 112.465 150.503 88.850  1.00 44.78 ?  81  PHE A CB    1 
ATOM   662   C  CG    . PHE A 1 81  ? 112.602 150.237 90.322  1.00 44.53 ?  81  PHE A CG    1 
ATOM   663   C  CD1   . PHE A 1 81  ? 113.220 151.158 91.148  1.00 45.67 ?  81  PHE A CD1   1 
ATOM   664   C  CD2   . PHE A 1 81  ? 112.113 149.069 90.877  1.00 46.79 ?  81  PHE A CD2   1 
ATOM   665   C  CE1   . PHE A 1 81  ? 113.348 150.919 92.503  1.00 45.99 ?  81  PHE A CE1   1 
ATOM   666   C  CE2   . PHE A 1 81  ? 112.238 148.825 92.230  1.00 45.17 ?  81  PHE A CE2   1 
ATOM   667   C  CZ    . PHE A 1 81  ? 112.856 149.750 93.043  1.00 43.40 ?  81  PHE A CZ    1 
ATOM   668   N  N     . LYS A 1 82  ? 113.207 150.601 85.695  1.00 47.06 ?  82  LYS A N     1 
ATOM   669   C  CA    . LYS A 1 82  ? 113.052 150.153 84.313  1.00 50.44 ?  82  LYS A CA    1 
ATOM   670   C  C     . LYS A 1 82  ? 114.321 149.481 83.813  1.00 50.45 ?  82  LYS A C     1 
ATOM   671   O  O     . LYS A 1 82  ? 114.261 148.452 83.133  1.00 52.83 ?  82  LYS A O     1 
ATOM   672   C  CB    . LYS A 1 82  ? 112.687 151.323 83.396  1.00 51.75 ?  82  LYS A CB    1 
ATOM   673   C  CG    . LYS A 1 82  ? 111.409 152.066 83.745  1.00 53.41 ?  82  LYS A CG    1 
ATOM   674   C  CD    . LYS A 1 82  ? 110.206 151.150 83.752  1.00 53.59 ?  82  LYS A CD    1 
ATOM   675   C  CE    . LYS A 1 82  ? 109.119 151.670 82.827  1.00 54.29 ?  82  LYS A CE    1 
ATOM   676   N  NZ    . LYS A 1 82  ? 109.641 151.934 81.457  1.00 52.75 1  82  LYS A NZ    1 
ATOM   677   N  N     . THR A 1 83  ? 115.480 150.055 84.141  1.00 43.33 ?  83  THR A N     1 
ATOM   678   C  CA    . THR A 1 83  ? 116.745 149.451 83.737  1.00 45.07 ?  83  THR A CA    1 
ATOM   679   C  C     . THR A 1 83  ? 116.901 148.060 84.336  1.00 46.81 ?  83  THR A C     1 
ATOM   680   O  O     . THR A 1 83  ? 117.380 147.137 83.666  1.00 47.75 ?  83  THR A O     1 
ATOM   681   C  CB    . THR A 1 83  ? 117.910 150.351 84.149  1.00 46.72 ?  83  THR A CB    1 
ATOM   682   O  OG1   . THR A 1 83  ? 117.701 151.668 83.630  1.00 50.88 ?  83  THR A OG1   1 
ATOM   683   C  CG2   . THR A 1 83  ? 119.220 149.810 83.607  1.00 46.24 ?  83  THR A CG2   1 
ATOM   684   N  N     . ALA A 1 84  ? 116.500 147.888 85.597  1.00 46.18 ?  84  ALA A N     1 
ATOM   685   C  CA    . ALA A 1 84  ? 116.567 146.565 86.212  1.00 41.53 ?  84  ALA A CA    1 
ATOM   686   C  C     . ALA A 1 84  ? 115.630 145.580 85.526  1.00 42.96 ?  84  ALA A C     1 
ATOM   687   O  O     . ALA A 1 84  ? 116.017 144.441 85.239  1.00 47.86 ?  84  ALA A O     1 
ATOM   688   C  CB    . ALA A 1 84  ? 116.241 146.661 87.700  1.00 43.85 ?  84  ALA A CB    1 
ATOM   689   N  N     . TYR A 1 85  ? 114.394 145.999 85.250  1.00 47.92 ?  85  TYR A N     1 
ATOM   690   C  CA    . TYR A 1 85  ? 113.411 145.099 84.663  1.00 47.31 ?  85  TYR A CA    1 
ATOM   691   C  C     . TYR A 1 85  ? 113.567 144.943 83.156  1.00 46.51 ?  85  TYR A C     1 
ATOM   692   O  O     . TYR A 1 85  ? 113.005 144.003 82.586  1.00 49.04 ?  85  TYR A O     1 
ATOM   693   C  CB    . TYR A 1 85  ? 111.996 145.584 84.986  1.00 47.59 ?  85  TYR A CB    1 
ATOM   694   C  CG    . TYR A 1 85  ? 111.532 145.227 86.380  1.00 48.42 ?  85  TYR A CG    1 
ATOM   695   C  CD1   . TYR A 1 85  ? 111.784 146.069 87.455  1.00 47.29 ?  85  TYR A CD1   1 
ATOM   696   C  CD2   . TYR A 1 85  ? 110.845 144.047 86.622  1.00 46.70 ?  85  TYR A CD2   1 
ATOM   697   C  CE1   . TYR A 1 85  ? 111.362 145.747 88.728  1.00 46.62 ?  85  TYR A CE1   1 
ATOM   698   C  CE2   . TYR A 1 85  ? 110.420 143.716 87.892  1.00 46.81 ?  85  TYR A CE2   1 
ATOM   699   C  CZ    . TYR A 1 85  ? 110.682 144.568 88.941  1.00 47.28 ?  85  TYR A CZ    1 
ATOM   700   O  OH    . TYR A 1 85  ? 110.260 144.242 90.207  1.00 49.55 ?  85  TYR A OH    1 
ATOM   701   N  N     . ALA A 1 86  ? 114.311 145.837 82.498  1.00 45.11 ?  86  ALA A N     1 
ATOM   702   C  CA    . ALA A 1 86  ? 114.519 145.704 81.061  1.00 44.63 ?  86  ALA A CA    1 
ATOM   703   C  C     . ALA A 1 86  ? 115.352 144.476 80.724  1.00 47.07 ?  86  ALA A C     1 
ATOM   704   O  O     . ALA A 1 86  ? 115.195 143.899 79.642  1.00 48.77 ?  86  ALA A O     1 
ATOM   705   C  CB    . ALA A 1 86  ? 115.186 146.960 80.501  1.00 44.19 ?  86  ALA A CB    1 
ATOM   706   N  N     . LYS A 1 87  ? 116.243 144.068 81.629  1.00 46.25 ?  87  LYS A N     1 
ATOM   707   C  CA    . LYS A 1 87  ? 117.058 142.884 81.388  1.00 45.97 ?  87  LYS A CA    1 
ATOM   708   C  C     . LYS A 1 87  ? 116.205 141.623 81.328  1.00 45.92 ?  87  LYS A C     1 
ATOM   709   O  O     . LYS A 1 87  ? 116.557 140.670 80.623  1.00 45.76 ?  87  LYS A O     1 
ATOM   710   C  CB    . LYS A 1 87  ? 118.131 142.767 82.474  1.00 42.62 ?  87  LYS A CB    1 
ATOM   711   C  CG    . LYS A 1 87  ? 118.714 141.375 82.663  1.00 44.03 ?  87  LYS A CG    1 
ATOM   712   C  CD    . LYS A 1 87  ? 120.076 141.244 82.002  1.00 45.15 ?  87  LYS A CD    1 
ATOM   713   C  CE    . LYS A 1 87  ? 120.691 139.884 82.283  1.00 45.16 ?  87  LYS A CE    1 
ATOM   714   N  NZ    . LYS A 1 87  ? 122.026 139.732 81.644  1.00 42.00 1  87  LYS A NZ    1 
ATOM   715   N  N     . LYS A 1 88  ? 115.069 141.615 82.027  1.00 48.62 ?  88  LYS A N     1 
ATOM   716   C  CA    . LYS A 1 88  ? 114.216 140.434 82.147  1.00 47.59 ?  88  LYS A CA    1 
ATOM   717   C  C     . LYS A 1 88  ? 115.022 139.243 82.654  1.00 43.20 ?  88  LYS A C     1 
ATOM   718   O  O     . LYS A 1 88  ? 115.060 138.174 82.041  1.00 46.03 ?  88  LYS A O     1 
ATOM   719   C  CB    . LYS A 1 88  ? 113.526 140.111 80.820  1.00 49.47 ?  88  LYS A CB    1 
ATOM   720   C  CG    . LYS A 1 88  ? 112.218 140.856 80.601  1.00 49.24 ?  88  LYS A CG    1 
ATOM   721   C  CD    . LYS A 1 88  ? 111.786 140.814 79.143  1.00 47.96 ?  88  LYS A CD    1 
ATOM   722   C  CE    . LYS A 1 88  ? 112.974 140.900 78.200  1.00 49.54 ?  88  LYS A CE    1 
ATOM   723   N  NZ    . LYS A 1 88  ? 112.550 140.880 76.774  1.00 47.96 1  88  LYS A NZ    1 
ATOM   724   N  N     . PHE A 1 89  ? 115.687 139.446 83.789  1.00 42.48 ?  89  PHE A N     1 
ATOM   725   C  CA    . PHE A 1 89  ? 116.527 138.407 84.363  1.00 38.98 ?  89  PHE A CA    1 
ATOM   726   C  C     . PHE A 1 89  ? 115.686 137.212 84.785  1.00 41.01 ?  89  PHE A C     1 
ATOM   727   O  O     . PHE A 1 89  ? 114.612 137.360 85.373  1.00 44.65 ?  89  PHE A O     1 
ATOM   728   C  CB    . PHE A 1 89  ? 117.303 138.956 85.561  1.00 35.95 ?  89  PHE A CB    1 
ATOM   729   C  CG    . PHE A 1 89  ? 118.005 137.901 86.367  1.00 37.82 ?  89  PHE A CG    1 
ATOM   730   C  CD1   . PHE A 1 89  ? 119.265 137.462 86.006  1.00 35.27 ?  89  PHE A CD1   1 
ATOM   731   C  CD2   . PHE A 1 89  ? 117.407 137.349 87.488  1.00 35.78 ?  89  PHE A CD2   1 
ATOM   732   C  CE1   . PHE A 1 89  ? 119.912 136.493 86.741  1.00 37.73 ?  89  PHE A CE1   1 
ATOM   733   C  CE2   . PHE A 1 89  ? 118.050 136.379 88.225  1.00 35.76 ?  89  PHE A CE2   1 
ATOM   734   C  CZ    . PHE A 1 89  ? 119.303 135.951 87.852  1.00 38.16 ?  89  PHE A CZ    1 
ATOM   735   N  N     . ARG A 1 90  ? 116.184 136.017 84.480  1.00 41.13 ?  90  ARG A N     1 
ATOM   736   C  CA    . ARG A 1 90  ? 115.542 134.775 84.878  1.00 40.95 ?  90  ARG A CA    1 
ATOM   737   C  C     . ARG A 1 90  ? 116.556 133.912 85.611  1.00 41.23 ?  90  ARG A C     1 
ATOM   738   O  O     . ARG A 1 90  ? 117.674 133.715 85.123  1.00 43.62 ?  90  ARG A O     1 
ATOM   739   C  CB    . ARG A 1 90  ? 114.978 134.022 83.669  1.00 42.51 ?  90  ARG A CB    1 
ATOM   740   C  CG    . ARG A 1 90  ? 114.011 134.835 82.829  1.00 42.59 ?  90  ARG A CG    1 
ATOM   741   C  CD    . ARG A 1 90  ? 112.604 134.774 83.396  1.00 45.13 ?  90  ARG A CD    1 
ATOM   742   N  NE    . ARG A 1 90  ? 111.718 135.736 82.751  1.00 45.28 ?  90  ARG A NE    1 
ATOM   743   C  CZ    . ARG A 1 90  ? 111.505 136.969 83.190  1.00 47.41 ?  90  ARG A CZ    1 
ATOM   744   N  NH1   . ARG A 1 90  ? 112.081 137.421 84.290  1.00 46.93 1  90  ARG A NH1   1 
ATOM   745   N  NH2   . ARG A 1 90  ? 110.690 137.768 82.507  1.00 44.82 ?  90  ARG A NH2   1 
ATOM   746   N  N     . PHE A 1 91  ? 116.170 133.414 86.774  1.00 36.44 ?  91  PHE A N     1 
ATOM   747   C  CA    . PHE A 1 91  ? 117.036 132.513 87.519  1.00 36.22 ?  91  PHE A CA    1 
ATOM   748   C  C     . PHE A 1 91  ? 117.198 131.210 86.745  1.00 42.87 ?  91  PHE A C     1 
ATOM   749   O  O     . PHE A 1 91  ? 116.198 130.611 86.332  1.00 45.07 ?  91  PHE A O     1 
ATOM   750   C  CB    . PHE A 1 91  ? 116.457 132.245 88.903  1.00 35.20 ?  91  PHE A CB    1 
ATOM   751   C  CG    . PHE A 1 91  ? 116.566 133.413 89.841  1.00 39.44 ?  91  PHE A CG    1 
ATOM   752   C  CD1   . PHE A 1 91  ? 117.722 133.630 90.570  1.00 42.42 ?  91  PHE A CD1   1 
ATOM   753   C  CD2   . PHE A 1 91  ? 115.514 134.297 89.991  1.00 39.20 ?  91  PHE A CD2   1 
ATOM   754   C  CE1   . PHE A 1 91  ? 117.824 134.701 91.432  1.00 38.91 ?  91  PHE A CE1   1 
ATOM   755   C  CE2   . PHE A 1 91  ? 115.610 135.372 90.852  1.00 39.18 ?  91  PHE A CE2   1 
ATOM   756   C  CZ    . PHE A 1 91  ? 116.766 135.573 91.574  1.00 38.29 ?  91  PHE A CZ    1 
ATOM   757   N  N     . PRO A 1 92  ? 118.430 130.740 86.522  1.00 41.57 ?  92  PRO A N     1 
ATOM   758   C  CA    . PRO A 1 92  ? 118.613 129.527 85.715  1.00 37.12 ?  92  PRO A CA    1 
ATOM   759   C  C     . PRO A 1 92  ? 118.302 128.244 86.457  1.00 38.04 ?  92  PRO A C     1 
ATOM   760   O  O     . PRO A 1 92  ? 118.132 127.202 85.810  1.00 40.67 ?  92  PRO A O     1 
ATOM   761   C  CB    . PRO A 1 92  ? 120.094 129.595 85.329  1.00 38.47 ?  92  PRO A CB    1 
ATOM   762   C  CG    . PRO A 1 92  ? 120.728 130.292 86.484  1.00 39.59 ?  92  PRO A CG    1 
ATOM   763   C  CD    . PRO A 1 92  ? 119.709 131.264 87.032  1.00 40.78 ?  92  PRO A CD    1 
ATOM   764   N  N     . SER A 1 93  ? 118.222 128.280 87.784  1.00 39.30 ?  93  SER A N     1 
ATOM   765   C  CA    . SER A 1 93  ? 118.014 127.083 88.580  1.00 42.91 ?  93  SER A CA    1 
ATOM   766   C  C     . SER A 1 93  ? 117.049 127.398 89.712  1.00 44.00 ?  93  SER A C     1 
ATOM   767   O  O     . SER A 1 93  ? 116.854 128.555 90.086  1.00 46.31 ?  93  SER A O     1 
ATOM   768   C  CB    . SER A 1 93  ? 119.338 126.548 89.140  1.00 41.29 ?  93  SER A CB    1 
ATOM   769   O  OG    . SER A 1 93  ? 119.777 127.322 90.241  1.00 40.49 ?  93  SER A OG    1 
ATOM   770   N  N     . PHE A 1 94  ? 116.440 126.342 90.254  1.00 41.93 ?  94  PHE A N     1 
ATOM   771   C  CA    . PHE A 1 94  ? 115.522 126.520 91.373  1.00 42.32 ?  94  PHE A CA    1 
ATOM   772   C  C     . PHE A 1 94  ? 116.252 127.008 92.616  1.00 43.88 ?  94  PHE A C     1 
ATOM   773   O  O     . PHE A 1 94  ? 115.709 127.808 93.385  1.00 46.67 ?  94  PHE A O     1 
ATOM   774   C  CB    . PHE A 1 94  ? 114.779 125.218 91.667  1.00 41.55 ?  94  PHE A CB    1 
ATOM   775   C  CG    . PHE A 1 94  ? 114.147 125.182 93.028  1.00 43.53 ?  94  PHE A CG    1 
ATOM   776   C  CD1   . PHE A 1 94  ? 113.050 125.973 93.315  1.00 44.19 ?  94  PHE A CD1   1 
ATOM   777   C  CD2   . PHE A 1 94  ? 114.652 124.362 94.021  1.00 44.94 ?  94  PHE A CD2   1 
ATOM   778   C  CE1   . PHE A 1 94  ? 112.470 125.949 94.566  1.00 43.92 ?  94  PHE A CE1   1 
ATOM   779   C  CE2   . PHE A 1 94  ? 114.074 124.333 95.274  1.00 46.60 ?  94  PHE A CE2   1 
ATOM   780   C  CZ    . PHE A 1 94  ? 112.983 125.128 95.547  1.00 44.64 ?  94  PHE A CZ    1 
ATOM   781   N  N     . MET A 1 95  ? 117.478 126.529 92.840  1.00 41.38 ?  95  MET A N     1 
ATOM   782   C  CA    . MET A 1 95  ? 118.210 126.909 94.043  1.00 36.23 ?  95  MET A CA    1 
ATOM   783   C  C     . MET A 1 95  ? 118.516 128.399 94.072  1.00 39.46 ?  95  MET A C     1 
ATOM   784   O  O     . MET A 1 95  ? 118.463 129.023 95.133  1.00 45.02 ?  95  MET A O     1 
ATOM   785   C  CB    . MET A 1 95  ? 119.501 126.100 94.159  1.00 42.26 ?  95  MET A CB    1 
ATOM   786   C  CG    . MET A 1 95  ? 119.926 125.700 95.581  1.00 44.32 ?  95  MET A CG    1 
ATOM   787   S  SD    . MET A 1 95  ? 118.686 125.402 96.869  1.00 53.46 ?  95  MET A SD    1 
ATOM   788   C  CE    . MET A 1 95  ? 117.515 124.317 96.057  1.00 45.67 ?  95  MET A CE    1 
ATOM   789   N  N     . SER A 1 96  ? 118.849 128.986 92.921  1.00 35.10 ?  96  SER A N     1 
ATOM   790   C  CA    . SER A 1 96  ? 119.157 130.412 92.884  1.00 33.05 ?  96  SER A CA    1 
ATOM   791   C  C     . SER A 1 96  ? 117.978 131.241 93.379  1.00 34.07 ?  96  SER A C     1 
ATOM   792   O  O     . SER A 1 96  ? 118.109 132.047 94.312  1.00 34.98 ?  96  SER A O     1 
ATOM   793   C  CB    . SER A 1 96  ? 119.535 130.817 91.461  1.00 35.24 ?  96  SER A CB    1 
ATOM   794   O  OG    . SER A 1 96  ? 120.295 129.803 90.833  1.00 38.59 ?  96  SER A OG    1 
ATOM   795   N  N     . ALA A 1 97  ? 116.806 131.028 92.778  1.00 40.03 ?  97  ALA A N     1 
ATOM   796   C  CA    . ALA A 1 97  ? 115.619 131.783 93.160  1.00 37.07 ?  97  ALA A CA    1 
ATOM   797   C  C     . ALA A 1 97  ? 115.187 131.454 94.580  1.00 37.56 ?  97  ALA A C     1 
ATOM   798   O  O     . ALA A 1 97  ? 114.760 132.342 95.323  1.00 45.57 ?  97  ALA A O     1 
ATOM   799   C  CB    . ALA A 1 97  ? 114.488 131.501 92.177  1.00 36.46 ?  97  ALA A CB    1 
ATOM   800   N  N     . PHE A 1 98  ? 115.276 130.181 94.970  1.00 33.25 ?  98  PHE A N     1 
ATOM   801   C  CA    . PHE A 1 98  ? 114.875 129.794 96.316  1.00 35.49 ?  98  PHE A CA    1 
ATOM   802   C  C     . PHE A 1 98  ? 115.746 130.478 97.359  1.00 37.06 ?  98  PHE A C     1 
ATOM   803   O  O     . PHE A 1 98  ? 115.240 131.035 98.340  1.00 45.07 ?  98  PHE A O     1 
ATOM   804   C  CB    . PHE A 1 98  ? 114.945 128.275 96.466  1.00 40.98 ?  98  PHE A CB    1 
ATOM   805   C  CG    . PHE A 1 98  ? 114.779 127.801 97.879  1.00 42.29 ?  98  PHE A CG    1 
ATOM   806   C  CD1   . PHE A 1 98  ? 113.519 127.720 98.448  1.00 41.66 ?  98  PHE A CD1   1 
ATOM   807   C  CD2   . PHE A 1 98  ? 115.877 127.444 98.641  1.00 42.38 ?  98  PHE A CD2   1 
ATOM   808   C  CE1   . PHE A 1 98  ? 113.361 127.291 99.747  1.00 41.14 ?  98  PHE A CE1   1 
ATOM   809   C  CE2   . PHE A 1 98  ? 115.723 127.013 99.941  1.00 42.94 ?  98  PHE A CE2   1 
ATOM   810   C  CZ    . PHE A 1 98  ? 114.463 126.936 100.495 1.00 42.27 ?  98  PHE A CZ    1 
ATOM   811   N  N     . LYS A 1 99  ? 117.063 130.457 97.155  1.00 39.01 ?  99  LYS A N     1 
ATOM   812   C  CA    . LYS A 1 99  ? 117.970 131.103 98.092  1.00 38.77 ?  99  LYS A CA    1 
ATOM   813   C  C     . LYS A 1 99  ? 117.731 132.603 98.139  1.00 39.03 ?  99  LYS A C     1 
ATOM   814   O  O     . LYS A 1 99  ? 117.714 133.197 99.223  1.00 41.24 ?  99  LYS A O     1 
ATOM   815   C  CB    . LYS A 1 99  ? 119.420 130.798 97.718  1.00 38.86 ?  99  LYS A CB    1 
ATOM   816   C  CG    . LYS A 1 99  ? 119.847 129.375 98.031  1.00 41.35 ?  99  LYS A CG    1 
ATOM   817   C  CD    . LYS A 1 99  ? 119.458 128.976 99.441  1.00 43.43 ?  99  LYS A CD    1 
ATOM   818   C  CE    . LYS A 1 99  ? 120.616 128.318 100.166 1.00 41.25 ?  99  LYS A CE    1 
ATOM   819   N  NZ    . LYS A 1 99  ? 120.521 128.509 101.638 1.00 42.13 1  99  LYS A NZ    1 
ATOM   820   N  N     . PHE A 1 100 ? 117.519 133.237 96.980  1.00 34.65 ?  100 PHE A N     1 
ATOM   821   C  CA    . PHE A 1 100 ? 117.260 134.672 97.000  1.00 34.54 ?  100 PHE A CA    1 
ATOM   822   C  C     . PHE A 1 100 ? 115.984 134.991 97.767  1.00 36.68 ?  100 PHE A C     1 
ATOM   823   O  O     . PHE A 1 100 ? 115.992 135.808 98.693  1.00 42.14 ?  100 PHE A O     1 
ATOM   824   C  CB    . PHE A 1 100 ? 117.171 135.242 95.588  1.00 36.23 ?  100 PHE A CB    1 
ATOM   825   C  CG    . PHE A 1 100 ? 116.772 136.686 95.571  1.00 36.68 ?  100 PHE A CG    1 
ATOM   826   C  CD1   . PHE A 1 100 ? 117.668 137.664 95.967  1.00 37.98 ?  100 PHE A CD1   1 
ATOM   827   C  CD2   . PHE A 1 100 ? 115.492 137.065 95.206  1.00 36.45 ?  100 PHE A CD2   1 
ATOM   828   C  CE1   . PHE A 1 100 ? 117.304 138.992 95.977  1.00 38.96 ?  100 PHE A CE1   1 
ATOM   829   C  CE2   . PHE A 1 100 ? 115.123 138.393 95.214  1.00 39.45 ?  100 PHE A CE2   1 
ATOM   830   C  CZ    . PHE A 1 100 ? 116.030 139.358 95.600  1.00 39.03 ?  100 PHE A CZ    1 
ATOM   831   N  N     . TYR A 1 101 ? 114.878 134.339 97.413  1.00 41.22 ?  101 TYR A N     1 
ATOM   832   C  CA    . TYR A 1 101 ? 113.596 134.670 98.015  1.00 38.44 ?  101 TYR A CA    1 
ATOM   833   C  C     . TYR A 1 101 ? 113.442 134.126 99.427  1.00 40.02 ?  101 TYR A C     1 
ATOM   834   O  O     . TYR A 1 101 ? 112.448 134.445 100.088 1.00 46.64 ?  101 TYR A O     1 
ATOM   835   C  CB    . TYR A 1 101 ? 112.457 134.174 97.122  1.00 38.76 ?  101 TYR A CB    1 
ATOM   836   C  CG    . TYR A 1 101 ? 112.300 135.003 95.868  1.00 36.64 ?  101 TYR A CG    1 
ATOM   837   C  CD1   . TYR A 1 101 ? 111.789 136.291 95.928  1.00 39.62 ?  101 TYR A CD1   1 
ATOM   838   C  CD2   . TYR A 1 101 ? 112.689 134.511 94.632  1.00 35.22 ?  101 TYR A CD2   1 
ATOM   839   C  CE1   . TYR A 1 101 ? 111.655 137.059 94.788  1.00 39.29 ?  101 TYR A CE1   1 
ATOM   840   C  CE2   . TYR A 1 101 ? 112.559 135.270 93.489  1.00 39.50 ?  101 TYR A CE2   1 
ATOM   841   C  CZ    . TYR A 1 101 ? 112.042 136.543 93.572  1.00 41.13 ?  101 TYR A CZ    1 
ATOM   842   O  OH    . TYR A 1 101 ? 111.912 137.303 92.433  1.00 39.45 ?  101 TYR A OH    1 
ATOM   843   N  N     . ASN A 1 102 ? 114.390 133.322 99.906  1.00 40.55 ?  102 ASN A N     1 
ATOM   844   C  CA    . ASN A 1 102 ? 114.377 132.883 101.293 1.00 41.46 ?  102 ASN A CA    1 
ATOM   845   C  C     . ASN A 1 102 ? 115.356 133.638 102.181 1.00 43.05 ?  102 ASN A C     1 
ATOM   846   O  O     . ASN A 1 102 ? 115.135 133.704 103.395 1.00 45.65 ?  102 ASN A O     1 
ATOM   847   C  CB    . ASN A 1 102 ? 114.687 131.383 101.375 1.00 42.60 ?  102 ASN A CB    1 
ATOM   848   C  CG    . ASN A 1 102 ? 113.436 130.528 101.376 1.00 44.82 ?  102 ASN A CG    1 
ATOM   849   O  OD1   . ASN A 1 102 ? 112.531 130.732 100.568 1.00 46.40 ?  102 ASN A OD1   1 
ATOM   850   N  ND2   . ASN A 1 102 ? 113.378 129.567 102.288 1.00 44.73 ?  102 ASN A ND2   1 
ATOM   851   N  N     . ASP A 1 103 ? 116.424 134.206 101.623 1.00 43.44 ?  103 ASP A N     1 
ATOM   852   C  CA    . ASP A 1 103 ? 117.452 134.858 102.427 1.00 41.09 ?  103 ASP A CA    1 
ATOM   853   C  C     . ASP A 1 103 ? 117.543 136.360 102.219 1.00 41.31 ?  103 ASP A C     1 
ATOM   854   O  O     . ASP A 1 103 ? 117.761 137.093 103.184 1.00 47.96 ?  103 ASP A O     1 
ATOM   855   C  CB    . ASP A 1 103 ? 118.821 134.235 102.131 1.00 44.45 ?  103 ASP A CB    1 
ATOM   856   C  CG    . ASP A 1 103 ? 118.916 132.790 102.580 1.00 46.42 ?  103 ASP A CG    1 
ATOM   857   O  OD1   . ASP A 1 103 ? 117.908 132.253 103.085 1.00 47.25 ?  103 ASP A OD1   1 
ATOM   858   O  OD2   . ASP A 1 103 ? 120.000 132.190 102.427 1.00 48.74 -1 103 ASP A OD2   1 
ATOM   859   N  N     . TYR A 1 104 ? 117.385 136.848 100.987 1.00 31.26 ?  104 TYR A N     1 
ATOM   860   C  CA    . TYR A 1 104 ? 117.660 138.241 100.674 1.00 37.51 ?  104 TYR A CA    1 
ATOM   861   C  C     . TYR A 1 104 ? 116.439 139.039 100.241 1.00 39.68 ?  104 TYR A C     1 
ATOM   862   O  O     . TYR A 1 104 ? 116.456 140.267 100.368 1.00 44.70 ?  104 TYR A O     1 
ATOM   863   C  CB    . TYR A 1 104 ? 118.726 138.335 99.573  1.00 36.23 ?  104 TYR A CB    1 
ATOM   864   C  CG    . TYR A 1 104 ? 119.999 137.598 99.910  1.00 39.20 ?  104 TYR A CG    1 
ATOM   865   C  CD1   . TYR A 1 104 ? 120.991 138.201 100.668 1.00 34.99 ?  104 TYR A CD1   1 
ATOM   866   C  CD2   . TYR A 1 104 ? 120.204 136.294 99.480  1.00 34.27 ?  104 TYR A CD2   1 
ATOM   867   C  CE1   . TYR A 1 104 ? 122.153 137.530 100.984 1.00 36.30 ?  104 TYR A CE1   1 
ATOM   868   C  CE2   . TYR A 1 104 ? 121.363 135.613 99.792  1.00 34.79 ?  104 TYR A CE2   1 
ATOM   869   C  CZ    . TYR A 1 104 ? 122.335 136.237 100.544 1.00 39.47 ?  104 TYR A CZ    1 
ATOM   870   O  OH    . TYR A 1 104 ? 123.492 135.566 100.859 1.00 37.58 ?  104 TYR A OH    1 
ATOM   871   N  N     . ALA A 1 105 ? 115.397 138.390 99.733  1.00 39.31 ?  105 ALA A N     1 
ATOM   872   C  CA    . ALA A 1 105 ? 114.211 139.120 99.311  1.00 40.02 ?  105 ALA A CA    1 
ATOM   873   C  C     . ALA A 1 105 ? 113.486 139.703 100.517 1.00 43.24 ?  105 ALA A C     1 
ATOM   874   O  O     . ALA A 1 105 ? 113.316 139.037 101.542 1.00 41.64 ?  105 ALA A O     1 
ATOM   875   C  CB    . ALA A 1 105 ? 113.270 138.209 98.526  1.00 37.86 ?  105 ALA A CB    1 
ATOM   876   N  N     . LEU A 1 106 ? 113.069 140.958 100.393 1.00 47.41 ?  106 LEU A N     1 
ATOM   877   C  CA    . LEU A 1 106 ? 112.337 141.610 101.469 1.00 45.87 ?  106 LEU A CA    1 
ATOM   878   C  C     . LEU A 1 106 ? 110.960 140.982 101.632 1.00 47.88 ?  106 LEU A C     1 
ATOM   879   O  O     . LEU A 1 106 ? 110.249 140.734 100.655 1.00 46.17 ?  106 LEU A O     1 
ATOM   880   C  CB    . LEU A 1 106 ? 112.203 143.106 101.193 1.00 46.17 ?  106 LEU A CB    1 
ATOM   881   C  CG    . LEU A 1 106 ? 111.583 143.955 102.303 1.00 44.92 ?  106 LEU A CG    1 
ATOM   882   C  CD1   . LEU A 1 106 ? 112.499 144.013 103.511 1.00 43.99 ?  106 LEU A CD1   1 
ATOM   883   C  CD2   . LEU A 1 106 ? 111.287 145.350 101.793 1.00 45.17 ?  106 LEU A CD2   1 
ATOM   884   N  N     . LYS A 1 107 ? 110.587 140.728 102.880 1.00 54.76 ?  107 LYS A N     1 
ATOM   885   C  CA    . LYS A 1 107 ? 109.298 140.151 103.218 1.00 53.91 ?  107 LYS A CA    1 
ATOM   886   C  C     . LYS A 1 107 ? 108.568 141.068 104.189 1.00 54.18 ?  107 LYS A C     1 
ATOM   887   O  O     . LYS A 1 107 ? 109.171 141.922 104.844 1.00 54.39 ?  107 LYS A O     1 
ATOM   888   C  CB    . LYS A 1 107 ? 109.456 138.753 103.830 1.00 51.79 ?  107 LYS A CB    1 
ATOM   889   C  CG    . LYS A 1 107 ? 109.859 137.685 102.830 1.00 50.81 ?  107 LYS A CG    1 
ATOM   890   C  CD    . LYS A 1 107 ? 110.149 136.365 103.521 1.00 55.44 ?  107 LYS A CD    1 
ATOM   891   C  CE    . LYS A 1 107 ? 110.510 135.288 102.514 1.00 54.96 ?  107 LYS A CE    1 
ATOM   892   N  NZ    . LYS A 1 107 ? 111.118 134.094 103.166 1.00 51.84 1  107 LYS A NZ    1 
ATOM   893   N  N     . THR A 1 108 ? 107.252 140.887 104.266 1.00 60.48 ?  108 THR A N     1 
ATOM   894   C  CA    . THR A 1 108 ? 106.441 141.676 105.176 1.00 61.10 ?  108 THR A CA    1 
ATOM   895   C  C     . THR A 1 108 ? 106.855 141.406 106.623 1.00 62.03 ?  108 THR A C     1 
ATOM   896   O  O     . THR A 1 108 ? 107.591 140.465 106.925 1.00 60.42 ?  108 THR A O     1 
ATOM   897   C  CB    . THR A 1 108 ? 104.959 141.368 104.975 1.00 60.24 ?  108 THR A CB    1 
ATOM   898   O  OG1   . THR A 1 108 ? 104.778 139.956 104.819 1.00 62.28 ?  108 THR A OG1   1 
ATOM   899   C  CG2   . THR A 1 108 ? 104.432 142.079 103.738 1.00 59.01 ?  108 THR A CG2   1 
ATOM   900   N  N     . ASN A 1 109 ? 106.364 142.257 107.527 1.00 63.53 ?  109 ASN A N     1 
ATOM   901   C  CA    . ASN A 1 109 ? 106.798 142.198 108.919 1.00 62.62 ?  109 ASN A CA    1 
ATOM   902   C  C     . ASN A 1 109 ? 106.461 140.863 109.569 1.00 64.06 ?  109 ASN A C     1 
ATOM   903   O  O     . ASN A 1 109 ? 107.141 140.445 110.514 1.00 65.05 ?  109 ASN A O     1 
ATOM   904   C  CB    . ASN A 1 109 ? 106.172 143.346 109.710 1.00 62.62 ?  109 ASN A CB    1 
ATOM   905   C  CG    . ASN A 1 109 ? 106.932 144.645 109.543 1.00 62.85 ?  109 ASN A CG    1 
ATOM   906   O  OD1   . ASN A 1 109 ? 108.153 144.647 109.400 1.00 64.74 ?  109 ASN A OD1   1 
ATOM   907   N  ND2   . ASN A 1 109 ? 106.210 145.759 109.559 1.00 63.04 ?  109 ASN A ND2   1 
ATOM   908   N  N     . ASP A 1 110 ? 105.427 140.179 109.084 1.00 68.70 ?  110 ASP A N     1 
ATOM   909   C  CA    . ASP A 1 110 ? 105.045 138.873 109.597 1.00 67.94 ?  110 ASP A CA    1 
ATOM   910   C  C     . ASP A 1 110 ? 105.674 137.728 108.813 1.00 68.31 ?  110 ASP A C     1 
ATOM   911   O  O     . ASP A 1 110 ? 105.303 136.569 109.027 1.00 69.86 ?  110 ASP A O     1 
ATOM   912   C  CB    . ASP A 1 110 ? 103.521 138.732 109.600 1.00 67.40 ?  110 ASP A CB    1 
ATOM   913   C  CG    . ASP A 1 110 ? 102.882 139.305 108.352 1.00 68.90 ?  110 ASP A CG    1 
ATOM   914   O  OD1   . ASP A 1 110 ? 103.509 140.168 107.705 1.00 69.20 ?  110 ASP A OD1   1 
ATOM   915   O  OD2   . ASP A 1 110 ? 101.752 138.893 108.018 1.00 70.98 -1 110 ASP A OD2   1 
ATOM   916   N  N     . LYS A 1 111 ? 106.615 138.029 107.914 1.00 66.46 ?  111 LYS A N     1 
ATOM   917   C  CA    . LYS A 1 111 ? 107.278 137.021 107.083 1.00 65.58 ?  111 LYS A CA    1 
ATOM   918   C  C     . LYS A 1 111 ? 106.263 136.211 106.282 1.00 65.91 ?  111 LYS A C     1 
ATOM   919   O  O     . LYS A 1 111 ? 106.399 134.998 106.114 1.00 67.92 ?  111 LYS A O     1 
ATOM   920   C  CB    . LYS A 1 111 ? 108.164 136.096 107.923 1.00 65.10 ?  111 LYS A CB    1 
ATOM   921   C  CG    . LYS A 1 111 ? 109.333 136.774 108.630 1.00 65.13 ?  111 LYS A CG    1 
ATOM   922   C  CD    . LYS A 1 111 ? 109.895 137.941 107.835 1.00 66.65 ?  111 LYS A CD    1 
ATOM   923   C  CE    . LYS A 1 111 ? 109.912 139.214 108.665 1.00 66.83 ?  111 LYS A CE    1 
ATOM   924   N  NZ    . LYS A 1 111 ? 110.403 140.382 107.884 1.00 64.70 1  111 LYS A NZ    1 
ATOM   925   N  N     . LYS A 1 112 ? 105.232 136.889 105.778 1.00 64.63 ?  112 LYS A N     1 
ATOM   926   C  CA    . LYS A 1 112 ? 104.123 136.229 105.101 1.00 66.88 ?  112 LYS A CA    1 
ATOM   927   C  C     . LYS A 1 112 ? 104.209 136.336 103.584 1.00 66.69 ?  112 LYS A C     1 
ATOM   928   O  O     . LYS A 1 112 ? 104.159 135.318 102.888 1.00 68.00 ?  112 LYS A O     1 
ATOM   929   C  CB    . LYS A 1 112 ? 102.793 136.813 105.591 1.00 66.48 ?  112 LYS A CB    1 
ATOM   930   C  CG    . LYS A 1 112 ? 101.577 135.973 105.238 1.00 67.80 ?  112 LYS A CG    1 
ATOM   931   C  CD    . LYS A 1 112 ? 101.566 134.661 106.008 1.00 68.20 ?  112 LYS A CD    1 
ATOM   932   C  CE    . LYS A 1 112 ? 101.733 134.887 107.504 1.00 68.46 ?  112 LYS A CE    1 
ATOM   933   N  NZ    . LYS A 1 112 ? 100.731 135.849 108.042 1.00 66.80 1  112 LYS A NZ    1 
ATOM   934   N  N     . LYS A 1 113 ? 104.334 137.547 103.059 1.00 59.74 ?  113 LYS A N     1 
ATOM   935   C  CA    . LYS A 1 113 ? 104.377 137.793 101.627 1.00 57.63 ?  113 LYS A CA    1 
ATOM   936   C  C     . LYS A 1 113 ? 105.753 138.325 101.233 1.00 57.10 ?  113 LYS A C     1 
ATOM   937   O  O     . LYS A 1 113 ? 106.631 138.537 102.073 1.00 58.08 ?  113 LYS A O     1 
ATOM   938   C  CB    . LYS A 1 113 ? 103.267 138.764 101.220 1.00 58.63 ?  113 LYS A CB    1 
ATOM   939   C  CG    . LYS A 1 113 ? 101.865 138.193 101.349 1.00 58.57 ?  113 LYS A CG    1 
ATOM   940   C  CD    . LYS A 1 113 ? 101.568 137.200 100.238 1.00 61.20 ?  113 LYS A CD    1 
ATOM   941   C  CE    . LYS A 1 113 ? 100.148 136.670 100.331 1.00 59.99 ?  113 LYS A CE    1 
ATOM   942   N  NZ    . LYS A 1 113 ? 99.873  135.644 99.288  1.00 58.80 1  113 LYS A NZ    1 
ATOM   943   N  N     . ILE A 1 114 ? 105.931 138.544 99.934  1.00 53.70 ?  114 ILE A N     1 
ATOM   944   C  CA    . ILE A 1 114 ? 107.205 138.968 99.363  1.00 52.40 ?  114 ILE A CA    1 
ATOM   945   C  C     . ILE A 1 114 ? 107.031 140.375 98.808  1.00 50.13 ?  114 ILE A C     1 
ATOM   946   O  O     . ILE A 1 114 ? 106.137 140.621 97.988  1.00 52.75 ?  114 ILE A O     1 
ATOM   947   C  CB    . ILE A 1 114 ? 107.686 137.998 98.274  1.00 52.98 ?  114 ILE A CB    1 
ATOM   948   C  CG1   . ILE A 1 114 ? 108.208 136.706 98.904  1.00 51.59 ?  114 ILE A CG1   1 
ATOM   949   C  CG2   . ILE A 1 114 ? 108.762 138.640 97.416  1.00 52.71 ?  114 ILE A CG2   1 
ATOM   950   C  CD1   . ILE A 1 114 ? 108.269 135.545 97.942  1.00 51.35 ?  114 ILE A CD1   1 
ATOM   951   N  N     . LEU A 1 115 ? 107.884 141.295 99.253  1.00 49.22 ?  115 LEU A N     1 
ATOM   952   C  CA    . LEU A 1 115 ? 107.839 142.682 98.808  1.00 51.09 ?  115 LEU A CA    1 
ATOM   953   C  C     . LEU A 1 115 ? 108.808 142.978 97.674  1.00 51.90 ?  115 LEU A C     1 
ATOM   954   O  O     . LEU A 1 115 ? 108.471 143.738 96.763  1.00 52.05 ?  115 LEU A O     1 
ATOM   955   C  CB    . LEU A 1 115 ? 108.133 143.623 99.980  1.00 50.85 ?  115 LEU A CB    1 
ATOM   956   C  CG    . LEU A 1 115 ? 107.091 143.642 101.096 1.00 49.79 ?  115 LEU A CG    1 
ATOM   957   C  CD1   . LEU A 1 115 ? 107.728 144.038 102.415 1.00 50.56 ?  115 LEU A CD1   1 
ATOM   958   C  CD2   . LEU A 1 115 ? 105.957 144.581 100.736 1.00 50.74 ?  115 LEU A CD2   1 
ATOM   959   N  N     . GLU A 1 116 ? 110.000 142.393 97.706  1.00 49.12 ?  116 GLU A N     1 
ATOM   960   C  CA    . GLU A 1 116 ? 111.047 142.677 96.734  1.00 45.80 ?  116 GLU A CA    1 
ATOM   961   C  C     . GLU A 1 116 ? 111.231 141.494 95.797  1.00 46.41 ?  116 GLU A C     1 
ATOM   962   O  O     . GLU A 1 116 ? 111.290 140.344 96.245  1.00 50.13 ?  116 GLU A O     1 
ATOM   963   C  CB    . GLU A 1 116 ? 112.372 142.986 97.431  1.00 44.75 ?  116 GLU A CB    1 
ATOM   964   C  CG    . GLU A 1 116 ? 112.670 144.459 97.592  1.00 44.63 ?  116 GLU A CG    1 
ATOM   965   C  CD    . GLU A 1 116 ? 113.920 144.703 98.409  1.00 47.03 ?  116 GLU A CD    1 
ATOM   966   O  OE1   . GLU A 1 116 ? 114.417 143.744 99.032  1.00 46.08 ?  116 GLU A OE1   1 
ATOM   967   O  OE2   . GLU A 1 116 ? 114.407 145.853 98.425  1.00 48.24 -1 116 GLU A OE2   1 
ATOM   968   N  N     . ARG A 1 117 ? 111.320 141.779 94.503  1.00 42.37 ?  117 ARG A N     1 
ATOM   969   C  CA    . ARG A 1 117 ? 111.811 140.811 93.537  1.00 42.21 ?  117 ARG A CA    1 
ATOM   970   C  C     . ARG A 1 117 ? 113.330 140.954 93.450  1.00 43.77 ?  117 ARG A C     1 
ATOM   971   O  O     . ARG A 1 117 ? 113.944 141.720 94.195  1.00 47.51 ?  117 ARG A O     1 
ATOM   972   C  CB    . ARG A 1 117 ? 111.130 141.011 92.184  1.00 42.43 ?  117 ARG A CB    1 
ATOM   973   C  CG    . ARG A 1 117 ? 109.612 141.021 92.240  1.00 44.77 ?  117 ARG A CG    1 
ATOM   974   C  CD    . ARG A 1 117 ? 109.074 139.810 92.987  1.00 49.50 ?  117 ARG A CD    1 
ATOM   975   N  NE    . ARG A 1 117 ? 109.164 138.587 92.198  1.00 47.61 ?  117 ARG A NE    1 
ATOM   976   C  CZ    . ARG A 1 117 ? 108.339 138.267 91.210  1.00 47.19 ?  117 ARG A CZ    1 
ATOM   977   N  NH1   . ARG A 1 117 ? 107.337 139.058 90.862  1.00 48.28 1  117 ARG A NH1   1 
ATOM   978   N  NH2   . ARG A 1 117 ? 108.521 137.123 90.558  1.00 47.65 ?  117 ARG A NH2   1 
ATOM   979   N  N     . TYR A 1 118 ? 113.958 140.206 92.543  1.00 42.19 ?  118 TYR A N     1 
ATOM   980   C  CA    . TYR A 1 118 ? 115.391 140.371 92.332  1.00 36.17 ?  118 TYR A CA    1 
ATOM   981   C  C     . TYR A 1 118 ? 115.701 141.751 91.768  1.00 37.76 ?  118 TYR A C     1 
ATOM   982   O  O     . TYR A 1 118 ? 116.658 142.410 92.196  1.00 40.66 ?  118 TYR A O     1 
ATOM   983   C  CB    . TYR A 1 118 ? 115.908 139.274 91.402  1.00 36.88 ?  118 TYR A CB    1 
ATOM   984   C  CG    . TYR A 1 118 ? 117.408 139.111 91.402  1.00 36.73 ?  118 TYR A CG    1 
ATOM   985   C  CD1   . TYR A 1 118 ? 118.102 138.900 92.585  1.00 36.21 ?  118 TYR A CD1   1 
ATOM   986   C  CD2   . TYR A 1 118 ? 118.130 139.160 90.221  1.00 36.96 ?  118 TYR A CD2   1 
ATOM   987   C  CE1   . TYR A 1 118 ? 119.470 138.748 92.588  1.00 35.71 ?  118 TYR A CE1   1 
ATOM   988   C  CE2   . TYR A 1 118 ? 119.497 139.002 90.213  1.00 31.19 ?  118 TYR A CE2   1 
ATOM   989   C  CZ    . TYR A 1 118 ? 120.163 138.798 91.399  1.00 35.72 ?  118 TYR A CZ    1 
ATOM   990   O  OH    . TYR A 1 118 ? 121.529 138.646 91.396  1.00 45.66 ?  118 TYR A OH    1 
ATOM   991   N  N     . GLU A 1 119 ? 114.885 142.212 90.818  1.00 41.38 ?  119 GLU A N     1 
ATOM   992   C  CA    . GLU A 1 119 ? 115.094 143.527 90.226  1.00 38.57 ?  119 GLU A CA    1 
ATOM   993   C  C     . GLU A 1 119 ? 114.895 144.638 91.249  1.00 40.41 ?  119 GLU A C     1 
ATOM   994   O  O     . GLU A 1 119 ? 115.627 145.631 91.236  1.00 43.54 ?  119 GLU A O     1 
ATOM   995   C  CB    . GLU A 1 119 ? 114.158 143.718 89.035  1.00 40.57 ?  119 GLU A CB    1 
ATOM   996   C  CG    . GLU A 1 119 ? 114.605 142.994 87.780  1.00 41.16 ?  119 GLU A CG    1 
ATOM   997   C  CD    . GLU A 1 119 ? 114.031 141.595 87.673  1.00 43.69 ?  119 GLU A CD    1 
ATOM   998   O  OE1   . GLU A 1 119 ? 113.616 141.038 88.710  1.00 43.92 ?  119 GLU A OE1   1 
ATOM   999   O  OE2   . GLU A 1 119 ? 114.002 141.052 86.550  1.00 44.72 -1 119 GLU A OE2   1 
ATOM   1000  N  N     . ASP A 1 120 ? 113.913 144.492 92.140  1.00 42.16 ?  120 ASP A N     1 
ATOM   1001  C  CA    . ASP A 1 120 ? 113.685 145.513 93.158  1.00 38.20 ?  120 ASP A CA    1 
ATOM   1002  C  C     . ASP A 1 120 ? 114.870 145.615 94.110  1.00 38.64 ?  120 ASP A C     1 
ATOM   1003  O  O     . ASP A 1 120 ? 115.342 146.717 94.414  1.00 45.44 ?  120 ASP A O     1 
ATOM   1004  C  CB    . ASP A 1 120 ? 112.402 145.207 93.933  1.00 42.51 ?  120 ASP A CB    1 
ATOM   1005  C  CG    . ASP A 1 120 ? 111.216 144.976 93.025  1.00 47.73 ?  120 ASP A CG    1 
ATOM   1006  O  OD1   . ASP A 1 120 ? 111.125 145.656 91.982  1.00 46.98 ?  120 ASP A OD1   1 
ATOM   1007  O  OD2   . ASP A 1 120 ? 110.374 144.115 93.351  1.00 51.12 -1 120 ASP A OD2   1 
ATOM   1008  N  N     . ARG A 1 121 ? 115.362 144.471 94.591  1.00 33.43 ?  121 ARG A N     1 
ATOM   1009  C  CA    . ARG A 1 121 ? 116.516 144.475 95.482  1.00 32.95 ?  121 ARG A CA    1 
ATOM   1010  C  C     . ARG A 1 121 ? 117.741 145.056 94.790  1.00 34.25 ?  121 ARG A C     1 
ATOM   1011  O  O     . ARG A 1 121 ? 118.475 145.857 95.381  1.00 41.31 ?  121 ARG A O     1 
ATOM   1012  C  CB    . ARG A 1 121 ? 116.803 143.056 95.973  1.00 34.34 ?  121 ARG A CB    1 
ATOM   1013  C  CG    . ARG A 1 121 ? 117.969 142.952 96.940  1.00 32.95 ?  121 ARG A CG    1 
ATOM   1014  C  CD    . ARG A 1 121 ? 117.501 143.075 98.378  1.00 33.48 ?  121 ARG A CD    1 
ATOM   1015  N  NE    . ARG A 1 121 ? 118.377 143.931 99.168  1.00 38.02 ?  121 ARG A NE    1 
ATOM   1016  C  CZ    . ARG A 1 121 ? 118.105 145.187 99.493  1.00 37.23 ?  121 ARG A CZ    1 
ATOM   1017  N  NH1   . ARG A 1 121 ? 116.988 145.776 99.101  1.00 36.19 1  121 ARG A NH1   1 
ATOM   1018  N  NH2   . ARG A 1 121 ? 118.977 145.870 100.228 1.00 34.72 ?  121 ARG A NH2   1 
ATOM   1019  N  N     . ILE A 1 122 ? 117.971 144.674 93.532  1.00 33.17 ?  122 ILE A N     1 
ATOM   1020  C  CA    . ILE A 1 122 ? 119.130 145.184 92.807  1.00 29.12 ?  122 ILE A CA    1 
ATOM   1021  C  C     . ILE A 1 122 ? 119.015 146.688 92.595  1.00 30.95 ?  122 ILE A C     1 
ATOM   1022  O  O     . ILE A 1 122 ? 119.995 147.422 92.751  1.00 36.66 ?  122 ILE A O     1 
ATOM   1023  C  CB    . ILE A 1 122 ? 119.304 144.423 91.481  1.00 32.31 ?  122 ILE A CB    1 
ATOM   1024  C  CG1   . ILE A 1 122 ? 120.042 143.110 91.733  1.00 27.19 ?  122 ILE A CG1   1 
ATOM   1025  C  CG2   . ILE A 1 122 ? 120.053 145.267 90.461  1.00 33.57 ?  122 ILE A CG2   1 
ATOM   1026  C  CD1   . ILE A 1 122 ? 120.342 142.344 90.487  1.00 33.73 ?  122 ILE A CD1   1 
ATOM   1027  N  N     . SER A 1 123 ? 117.821 147.174 92.245  1.00 34.94 ?  123 SER A N     1 
ATOM   1028  C  CA    . SER A 1 123 ? 117.631 148.606 92.045  1.00 32.04 ?  123 SER A CA    1 
ATOM   1029  C  C     . SER A 1 123 ? 117.846 149.380 93.336  1.00 31.85 ?  123 SER A C     1 
ATOM   1030  O  O     . SER A 1 123 ? 118.444 150.461 93.328  1.00 39.19 ?  123 SER A O     1 
ATOM   1031  C  CB    . SER A 1 123 ? 116.232 148.877 91.495  1.00 34.60 ?  123 SER A CB    1 
ATOM   1032  O  OG    . SER A 1 123 ? 115.870 147.911 90.530  1.00 39.38 ?  123 SER A OG    1 
ATOM   1033  N  N     . ILE A 1 124 ? 117.353 148.850 94.458  1.00 31.75 ?  124 ILE A N     1 
ATOM   1034  C  CA    . ILE A 1 124 ? 117.548 149.530 95.734  1.00 34.84 ?  124 ILE A CA    1 
ATOM   1035  C  C     . ILE A 1 124 ? 119.027 149.565 96.103  1.00 36.09 ?  124 ILE A C     1 
ATOM   1036  O  O     . ILE A 1 124 ? 119.543 150.597 96.549  1.00 39.49 ?  124 ILE A O     1 
ATOM   1037  C  CB    . ILE A 1 124 ? 116.697 148.864 96.829  1.00 38.69 ?  124 ILE A CB    1 
ATOM   1038  C  CG1   . ILE A 1 124 ? 115.214 149.126 96.565  1.00 39.24 ?  124 ILE A CG1   1 
ATOM   1039  C  CG2   . ILE A 1 124 ? 117.088 149.376 98.201  1.00 33.39 ?  124 ILE A CG2   1 
ATOM   1040  C  CD1   . ILE A 1 124 ? 114.899 150.574 96.247  1.00 37.19 ?  124 ILE A CD1   1 
ATOM   1041  N  N     . VAL A 1 125 ? 119.734 148.448 95.911  1.00 32.10 ?  125 VAL A N     1 
ATOM   1042  C  CA    . VAL A 1 125 ? 121.164 148.414 96.205  1.00 29.01 ?  125 VAL A CA    1 
ATOM   1043  C  C     . VAL A 1 125 ? 121.921 149.386 95.305  1.00 28.32 ?  125 VAL A C     1 
ATOM   1044  O  O     . VAL A 1 125 ? 122.858 150.060 95.744  1.00 39.80 ?  125 VAL A O     1 
ATOM   1045  C  CB    . VAL A 1 125 ? 121.698 146.975 96.075  1.00 33.53 ?  125 VAL A CB    1 
ATOM   1046  C  CG1   . VAL A 1 125 ? 123.203 146.948 96.198  1.00 30.75 ?  125 VAL A CG1   1 
ATOM   1047  C  CG2   . VAL A 1 125 ? 121.079 146.087 97.138  1.00 28.67 ?  125 VAL A CG2   1 
ATOM   1048  N  N     . ALA A 1 126 ? 121.510 149.491 94.041  1.00 26.22 ?  126 ALA A N     1 
ATOM   1049  C  CA    . ALA A 1 126 ? 122.183 150.391 93.110  1.00 26.65 ?  126 ALA A CA    1 
ATOM   1050  C  C     . ALA A 1 126 ? 121.942 151.850 93.466  1.00 34.15 ?  126 ALA A C     1 
ATOM   1051  O  O     . ALA A 1 126 ? 122.864 152.671 93.401  1.00 39.43 ?  126 ALA A O     1 
ATOM   1052  C  CB    . ALA A 1 126 ? 121.713 150.109 91.688  1.00 29.39 ?  126 ALA A CB    1 
ATOM   1053  N  N     . LEU A 1 127 ? 120.706 152.197 93.831  1.00 36.11 ?  127 LEU A N     1 
ATOM   1054  C  CA    . LEU A 1 127 ? 120.415 153.563 94.250  1.00 32.17 ?  127 LEU A CA    1 
ATOM   1055  C  C     . LEU A 1 127 ? 121.126 153.904 95.551  1.00 30.19 ?  127 LEU A C     1 
ATOM   1056  O  O     . LEU A 1 127 ? 121.515 155.059 95.759  1.00 35.16 ?  127 LEU A O     1 
ATOM   1057  C  CB    . LEU A 1 127 ? 118.907 153.758 94.395  1.00 33.59 ?  127 LEU A CB    1 
ATOM   1058  C  CG    . LEU A 1 127 ? 118.100 153.728 93.096  1.00 34.25 ?  127 LEU A CG    1 
ATOM   1059  C  CD1   . LEU A 1 127 ? 116.663 153.322 93.367  1.00 36.24 ?  127 LEU A CD1   1 
ATOM   1060  C  CD2   . LEU A 1 127 ? 118.153 155.069 92.390  1.00 34.84 ?  127 LEU A CD2   1 
ATOM   1061  N  N     . PHE A 1 128 ? 121.294 152.921 96.438  1.00 32.75 ?  128 PHE A N     1 
ATOM   1062  C  CA    . PHE A 1 128 ? 122.097 153.130 97.636  1.00 32.86 ?  128 PHE A CA    1 
ATOM   1063  C  C     . PHE A 1 128 ? 123.560 153.377 97.284  1.00 30.93 ?  128 PHE A C     1 
ATOM   1064  O  O     . PHE A 1 128 ? 124.200 154.265 97.857  1.00 38.78 ?  128 PHE A O     1 
ATOM   1065  C  CB    . PHE A 1 128 ? 121.955 151.923 98.563  1.00 30.53 ?  128 PHE A CB    1 
ATOM   1066  C  CG    . PHE A 1 128 ? 122.836 151.977 99.775  1.00 35.69 ?  128 PHE A CG    1 
ATOM   1067  C  CD1   . PHE A 1 128 ? 122.422 152.640 100.916 1.00 37.91 ?  128 PHE A CD1   1 
ATOM   1068  C  CD2   . PHE A 1 128 ? 124.070 151.351 99.780  1.00 33.56 ?  128 PHE A CD2   1 
ATOM   1069  C  CE1   . PHE A 1 128 ? 123.227 152.687 102.035 1.00 38.80 ?  128 PHE A CE1   1 
ATOM   1070  C  CE2   . PHE A 1 128 ? 124.880 151.400 100.892 1.00 33.60 ?  128 PHE A CE2   1 
ATOM   1071  C  CZ    . PHE A 1 128 ? 124.458 152.066 102.022 1.00 35.48 ?  128 PHE A CZ    1 
ATOM   1072  N  N     . PHE A 1 129 ? 124.104 152.599 96.345  1.00 28.02 ?  129 PHE A N     1 
ATOM   1073  C  CA    . PHE A 1 129 ? 125.503 152.756 95.958  1.00 25.55 ?  129 PHE A CA    1 
ATOM   1074  C  C     . PHE A 1 129 ? 125.759 154.103 95.296  1.00 29.30 ?  129 PHE A C     1 
ATOM   1075  O  O     . PHE A 1 129 ? 126.764 154.762 95.583  1.00 33.20 ?  129 PHE A O     1 
ATOM   1076  C  CB    . PHE A 1 129 ? 125.921 151.630 95.013  1.00 26.16 ?  129 PHE A CB    1 
ATOM   1077  C  CG    . PHE A 1 129 ? 126.152 150.316 95.691  1.00 25.05 ?  129 PHE A CG    1 
ATOM   1078  C  CD1   . PHE A 1 129 ? 126.319 150.244 97.060  1.00 27.59 ?  129 PHE A CD1   1 
ATOM   1079  C  CD2   . PHE A 1 129 ? 126.219 149.150 94.950  1.00 26.52 ?  129 PHE A CD2   1 
ATOM   1080  C  CE1   . PHE A 1 129 ? 126.533 149.032 97.679  1.00 24.89 ?  129 PHE A CE1   1 
ATOM   1081  C  CE2   . PHE A 1 129 ? 126.438 147.937 95.563  1.00 26.00 ?  129 PHE A CE2   1 
ATOM   1082  C  CZ    . PHE A 1 129 ? 126.595 147.879 96.930  1.00 27.59 ?  129 PHE A CZ    1 
ATOM   1083  N  N     . ALA A 1 130 ? 124.863 154.525 94.402  1.00 35.43 ?  130 ALA A N     1 
ATOM   1084  C  CA    . ALA A 1 130 ? 125.135 155.700 93.580  1.00 35.20 ?  130 ALA A CA    1 
ATOM   1085  C  C     . ALA A 1 130 ? 125.110 156.988 94.389  1.00 42.34 ?  130 ALA A C     1 
ATOM   1086  O  O     . ALA A 1 130 ? 125.816 157.943 94.045  1.00 47.09 ?  130 ALA A O     1 
ATOM   1087  C  CB    . ALA A 1 130 ? 124.131 155.774 92.435  1.00 34.43 ?  130 ALA A CB    1 
ATOM   1088  N  N     . ASN A 1 131 ? 124.302 157.041 95.450  1.00 42.79 ?  131 ASN A N     1 
ATOM   1089  C  CA    . ASN A 1 131 ? 124.248 158.190 96.354  1.00 43.74 ?  131 ASN A CA    1 
ATOM   1090  C  C     . ASN A 1 131 ? 123.865 159.471 95.611  1.00 43.29 ?  131 ASN A C     1 
ATOM   1091  O  O     . ASN A 1 131 ? 124.547 160.494 95.694  1.00 47.94 ?  131 ASN A O     1 
ATOM   1092  C  CB    . ASN A 1 131 ? 125.576 158.358 97.098  1.00 43.48 ?  131 ASN A CB    1 
ATOM   1093  C  CG    . ASN A 1 131 ? 125.445 159.216 98.340  1.00 48.16 ?  131 ASN A CG    1 
ATOM   1094  O  OD1   . ASN A 1 131 ? 124.501 159.066 99.116  1.00 44.83 ?  131 ASN A OD1   1 
ATOM   1095  N  ND2   . ASN A 1 131 ? 126.394 160.121 98.535  1.00 46.49 ?  131 ASN A ND2   1 
ATOM   1096  N  N     . GLY A 1 132 ? 122.756 159.407 94.877  1.00 41.46 ?  132 GLY A N     1 
ATOM   1097  C  CA    . GLY A 1 132 ? 122.203 160.554 94.197  1.00 41.96 ?  132 GLY A CA    1 
ATOM   1098  C  C     . GLY A 1 132 ? 122.446 160.600 92.701  1.00 44.87 ?  132 GLY A C     1 
ATOM   1099  O  O     . GLY A 1 132 ? 121.775 161.371 92.007  1.00 49.08 ?  132 GLY A O     1 
ATOM   1100  N  N     . ASP A 1 133 ? 123.374 159.800 92.186  1.00 47.04 ?  133 ASP A N     1 
ATOM   1101  C  CA    . ASP A 1 133 ? 123.704 159.807 90.766  1.00 46.05 ?  133 ASP A CA    1 
ATOM   1102  C  C     . ASP A 1 133 ? 122.801 158.824 90.027  1.00 49.14 ?  133 ASP A C     1 
ATOM   1103  O  O     . ASP A 1 133 ? 122.786 157.631 90.343  1.00 49.71 ?  133 ASP A O     1 
ATOM   1104  C  CB    . ASP A 1 133 ? 125.175 159.454 90.555  1.00 48.23 ?  133 ASP A CB    1 
ATOM   1105  C  CG    . ASP A 1 133 ? 125.724 159.992 89.248  1.00 53.27 ?  133 ASP A CG    1 
ATOM   1106  O  OD1   . ASP A 1 133 ? 124.931 160.204 88.305  1.00 52.24 ?  133 ASP A OD1   1 
ATOM   1107  O  OD2   . ASP A 1 133 ? 126.951 160.205 89.162  1.00 52.57 -1 133 ASP A OD2   1 
ATOM   1108  N  N     . THR A 1 134 ? 122.051 159.326 89.046  1.00 48.73 ?  134 THR A N     1 
ATOM   1109  C  CA    . THR A 1 134 ? 121.141 158.462 88.300  1.00 47.99 ?  134 THR A CA    1 
ATOM   1110  C  C     . THR A 1 134 ? 121.897 157.563 87.328  1.00 49.88 ?  134 THR A C     1 
ATOM   1111  O  O     . THR A 1 134 ? 121.610 156.364 87.229  1.00 51.80 ?  134 THR A O     1 
ATOM   1112  C  CB    . THR A 1 134 ? 120.114 159.312 87.556  1.00 52.41 ?  134 THR A CB    1 
ATOM   1113  O  OG1   . THR A 1 134 ? 119.284 159.986 88.508  1.00 53.72 ?  134 THR A OG1   1 
ATOM   1114  C  CG2   . THR A 1 134 ? 119.242 158.441 86.665  1.00 51.31 ?  134 THR A CG2   1 
ATOM   1115  N  N     . GLU A 1 135 ? 122.869 158.125 86.604  1.00 47.24 ?  135 GLU A N     1 
ATOM   1116  C  CA    . GLU A 1 135 ? 123.638 157.331 85.653  1.00 47.75 ?  135 GLU A CA    1 
ATOM   1117  C  C     . GLU A 1 135 ? 124.466 156.268 86.363  1.00 48.60 ?  135 GLU A C     1 
ATOM   1118  O  O     . GLU A 1 135 ? 124.574 155.134 85.884  1.00 51.03 ?  135 GLU A O     1 
ATOM   1119  C  CB    . GLU A 1 135 ? 124.534 158.241 84.816  1.00 49.48 ?  135 GLU A CB    1 
ATOM   1120  C  CG    . GLU A 1 135 ? 123.773 159.263 83.994  1.00 48.79 ?  135 GLU A CG    1 
ATOM   1121  C  CD    . GLU A 1 135 ? 122.657 158.638 83.182  1.00 54.08 ?  135 GLU A CD    1 
ATOM   1122  O  OE1   . GLU A 1 135 ? 122.948 157.752 82.352  1.00 54.31 ?  135 GLU A OE1   1 
ATOM   1123  O  OE2   . GLU A 1 135 ? 121.487 159.031 83.377  1.00 55.23 -1 135 GLU A OE2   1 
ATOM   1124  N  N     . LYS A 1 136 ? 125.062 156.618 87.505  1.00 40.59 ?  136 LYS A N     1 
ATOM   1125  C  CA    . LYS A 1 136 ? 125.804 155.632 88.281  1.00 40.58 ?  136 LYS A CA    1 
ATOM   1126  C  C     . LYS A 1 136 ? 124.878 154.545 88.812  1.00 41.54 ?  136 LYS A C     1 
ATOM   1127  O  O     . LYS A 1 136 ? 125.256 153.370 88.867  1.00 44.71 ?  136 LYS A O     1 
ATOM   1128  C  CB    . LYS A 1 136 ? 126.546 156.320 89.426  1.00 45.00 ?  136 LYS A CB    1 
ATOM   1129  C  CG    . LYS A 1 136 ? 127.707 155.522 89.986  1.00 42.10 ?  136 LYS A CG    1 
ATOM   1130  C  CD    . LYS A 1 136 ? 128.908 155.581 89.064  1.00 43.50 ?  136 LYS A CD    1 
ATOM   1131  C  CE    . LYS A 1 136 ? 130.194 155.281 89.812  1.00 46.23 ?  136 LYS A CE    1 
ATOM   1132  N  NZ    . LYS A 1 136 ? 131.389 155.494 88.951  1.00 47.84 1  136 LYS A NZ    1 
ATOM   1133  N  N     . ALA A 1 137 ? 123.660 154.919 89.211  1.00 39.31 ?  137 ALA A N     1 
ATOM   1134  C  CA    . ALA A 1 137 ? 122.692 153.922 89.655  1.00 34.47 ?  137 ALA A CA    1 
ATOM   1135  C  C     . ALA A 1 137 ? 122.327 152.969 88.525  1.00 36.75 ?  137 ALA A C     1 
ATOM   1136  O  O     . ALA A 1 137 ? 122.203 151.759 88.740  1.00 39.98 ?  137 ALA A O     1 
ATOM   1137  C  CB    . ALA A 1 137 ? 121.444 154.610 90.207  1.00 36.06 ?  137 ALA A CB    1 
ATOM   1138  N  N     . LYS A 1 138 ? 122.151 153.499 87.312  1.00 40.72 ?  138 LYS A N     1 
ATOM   1139  C  CA    . LYS A 1 138 ? 121.883 152.638 86.164  1.00 40.87 ?  138 LYS A CA    1 
ATOM   1140  C  C     . LYS A 1 138 ? 123.070 151.732 85.860  1.00 41.41 ?  138 LYS A C     1 
ATOM   1141  O  O     . LYS A 1 138 ? 122.890 150.565 85.492  1.00 43.37 ?  138 LYS A O     1 
ATOM   1142  C  CB    . LYS A 1 138 ? 121.524 153.485 84.944  1.00 45.21 ?  138 LYS A CB    1 
ATOM   1143  C  CG    . LYS A 1 138 ? 120.110 154.037 84.969  1.00 44.02 ?  138 LYS A CG    1 
ATOM   1144  C  CD    . LYS A 1 138 ? 120.000 155.306 84.146  1.00 43.87 ?  138 LYS A CD    1 
ATOM   1145  C  CE    . LYS A 1 138 ? 119.729 154.992 82.686  1.00 47.11 ?  138 LYS A CE    1 
ATOM   1146  N  NZ    . LYS A 1 138 ? 119.744 156.218 81.844  1.00 48.97 1  138 LYS A NZ    1 
ATOM   1147  N  N     . GLU A 1 139 ? 124.290 152.252 86.001  1.00 40.08 ?  139 GLU A N     1 
ATOM   1148  C  CA    . GLU A 1 139 ? 125.477 151.426 85.801  1.00 36.52 ?  139 GLU A CA    1 
ATOM   1149  C  C     . GLU A 1 139 ? 125.540 150.290 86.816  1.00 34.97 ?  139 GLU A C     1 
ATOM   1150  O  O     . GLU A 1 139 ? 125.858 149.150 86.466  1.00 40.47 ?  139 GLU A O     1 
ATOM   1151  C  CB    . GLU A 1 139 ? 126.736 152.289 85.884  1.00 38.10 ?  139 GLU A CB    1 
ATOM   1152  C  CG    . GLU A 1 139 ? 127.092 152.998 84.591  1.00 41.30 ?  139 GLU A CG    1 
ATOM   1153  C  CD    . GLU A 1 139 ? 128.219 153.995 84.766  1.00 48.31 ?  139 GLU A CD    1 
ATOM   1154  O  OE1   . GLU A 1 139 ? 128.292 154.630 85.838  1.00 45.67 ?  139 GLU A OE1   1 
ATOM   1155  O  OE2   . GLU A 1 139 ? 129.033 154.147 83.832  1.00 48.32 -1 139 GLU A OE2   1 
ATOM   1156  N  N     . TYR A 1 140 ? 125.239 150.585 88.083  1.00 32.51 ?  140 TYR A N     1 
ATOM   1157  C  CA    . TYR A 1 140 ? 125.214 149.544 89.106  1.00 30.56 ?  140 TYR A CA    1 
ATOM   1158  C  C     . TYR A 1 140 ? 124.117 148.524 88.826  1.00 33.75 ?  140 TYR A C     1 
ATOM   1159  O  O     . TYR A 1 140 ? 124.303 147.321 89.049  1.00 34.13 ?  140 TYR A O     1 
ATOM   1160  C  CB    . TYR A 1 140 ? 125.012 150.164 90.486  1.00 32.61 ?  140 TYR A CB    1 
ATOM   1161  C  CG    . TYR A 1 140 ? 126.235 150.812 91.081  1.00 32.42 ?  140 TYR A CG    1 
ATOM   1162  C  CD1   . TYR A 1 140 ? 127.408 150.095 91.268  1.00 34.45 ?  140 TYR A CD1   1 
ATOM   1163  C  CD2   . TYR A 1 140 ? 126.211 152.140 91.475  1.00 33.15 ?  140 TYR A CD2   1 
ATOM   1164  C  CE1   . TYR A 1 140 ? 128.522 150.689 91.820  1.00 34.20 ?  140 TYR A CE1   1 
ATOM   1165  C  CE2   . TYR A 1 140 ? 127.317 152.741 92.024  1.00 35.74 ?  140 TYR A CE2   1 
ATOM   1166  C  CZ    . TYR A 1 140 ? 128.469 152.014 92.195  1.00 30.78 ?  140 TYR A CZ    1 
ATOM   1167  O  OH    . TYR A 1 140 ? 129.567 152.624 92.747  1.00 33.69 ?  140 TYR A OH    1 
ATOM   1168  N  N     . VAL A 1 141 ? 122.958 148.993 88.356  1.00 33.86 ?  141 VAL A N     1 
ATOM   1169  C  CA    . VAL A 1 141 ? 121.875 148.086 87.991  1.00 33.00 ?  141 VAL A CA    1 
ATOM   1170  C  C     . VAL A 1 141 ? 122.318 147.148 86.881  1.00 35.02 ?  141 VAL A C     1 
ATOM   1171  O  O     . VAL A 1 141 ? 122.074 145.940 86.935  1.00 39.42 ?  141 VAL A O     1 
ATOM   1172  C  CB    . VAL A 1 141 ? 120.621 148.881 87.587  1.00 36.37 ?  141 VAL A CB    1 
ATOM   1173  C  CG1   . VAL A 1 141 ? 119.714 148.026 86.741  1.00 36.42 ?  141 VAL A CG1   1 
ATOM   1174  C  CG2   . VAL A 1 141 ? 119.880 149.341 88.812  1.00 35.34 ?  141 VAL A CG2   1 
ATOM   1175  N  N     . ASN A 1 142 ? 122.976 147.688 85.854  1.00 35.68 ?  142 ASN A N     1 
ATOM   1176  C  CA    . ASN A 1 142 ? 123.476 146.842 84.776  1.00 31.75 ?  142 ASN A CA    1 
ATOM   1177  C  C     . ASN A 1 142 ? 124.515 145.857 85.293  1.00 33.91 ?  142 ASN A C     1 
ATOM   1178  O  O     . ASN A 1 142 ? 124.541 144.695 84.877  1.00 40.10 ?  142 ASN A O     1 
ATOM   1179  C  CB    . ASN A 1 142 ? 124.061 147.705 83.661  1.00 32.37 ?  142 ASN A CB    1 
ATOM   1180  C  CG    . ASN A 1 142 ? 122.997 148.272 82.751  1.00 38.00 ?  142 ASN A CG    1 
ATOM   1181  O  OD1   . ASN A 1 142 ? 122.098 147.558 82.308  1.00 37.20 ?  142 ASN A OD1   1 
ATOM   1182  N  ND2   . ASN A 1 142 ? 123.090 149.565 82.467  1.00 36.90 ?  142 ASN A ND2   1 
ATOM   1183  N  N     . LEU A 1 143 ? 125.383 146.309 86.199  1.00 34.59 ?  143 LEU A N     1 
ATOM   1184  C  CA    . LEU A 1 143 ? 126.428 145.443 86.732  1.00 27.88 ?  143 LEU A CA    1 
ATOM   1185  C  C     . LEU A 1 143 ? 125.845 144.273 87.517  1.00 29.22 ?  143 LEU A C     1 
ATOM   1186  O  O     . LEU A 1 143 ? 126.314 143.137 87.389  1.00 29.56 ?  143 LEU A O     1 
ATOM   1187  C  CB    . LEU A 1 143 ? 127.372 146.261 87.611  1.00 27.94 ?  143 LEU A CB    1 
ATOM   1188  C  CG    . LEU A 1 143 ? 128.797 145.742 87.766  1.00 32.99 ?  143 LEU A CG    1 
ATOM   1189  C  CD1   . LEU A 1 143 ? 129.573 145.986 86.489  1.00 33.82 ?  143 LEU A CD1   1 
ATOM   1190  C  CD2   . LEU A 1 143 ? 129.464 146.430 88.935  1.00 28.96 ?  143 LEU A CD2   1 
ATOM   1191  N  N     . MET A 1 144 ? 124.827 144.529 88.340  1.00 33.23 ?  144 MET A N     1 
ATOM   1192  C  CA    . MET A 1 144 ? 124.304 143.467 89.194  1.00 27.56 ?  144 MET A CA    1 
ATOM   1193  C  C     . MET A 1 144 ? 123.260 142.608 88.486  1.00 28.03 ?  144 MET A C     1 
ATOM   1194  O  O     . MET A 1 144 ? 123.167 141.406 88.754  1.00 31.91 ?  144 MET A O     1 
ATOM   1195  C  CB    . MET A 1 144 ? 123.729 144.053 90.482  1.00 28.77 ?  144 MET A CB    1 
ATOM   1196  C  CG    . MET A 1 144 ? 124.733 144.846 91.300  1.00 30.13 ?  144 MET A CG    1 
ATOM   1197  S  SD    . MET A 1 144 ? 124.066 145.360 92.890  1.00 44.79 ?  144 MET A SD    1 
ATOM   1198  C  CE    . MET A 1 144 ? 123.315 146.918 92.447  1.00 33.81 ?  144 MET A CE    1 
ATOM   1199  N  N     . ILE A 1 145 ? 122.455 143.198 87.599  1.00 28.21 ?  145 ILE A N     1 
ATOM   1200  C  CA    . ILE A 1 145 ? 121.464 142.412 86.869  1.00 30.79 ?  145 ILE A CA    1 
ATOM   1201  C  C     . ILE A 1 145 ? 122.142 141.508 85.848  1.00 33.87 ?  145 ILE A C     1 
ATOM   1202  O  O     . ILE A 1 145 ? 121.655 140.406 85.567  1.00 37.32 ?  145 ILE A O     1 
ATOM   1203  C  CB    . ILE A 1 145 ? 120.403 143.330 86.226  1.00 31.53 ?  145 ILE A CB    1 
ATOM   1204  C  CG1   . ILE A 1 145 ? 119.073 142.588 86.089  1.00 30.46 ?  145 ILE A CG1   1 
ATOM   1205  C  CG2   . ILE A 1 145 ? 120.854 143.851 84.868  1.00 30.98 ?  145 ILE A CG2   1 
ATOM   1206  C  CD1   . ILE A 1 145 ? 118.416 142.251 87.405  1.00 28.31 ?  145 ILE A CD1   1 
ATOM   1207  N  N     . ASN A 1 146 ? 123.266 141.944 85.277  1.00 29.04 ?  146 ASN A N     1 
ATOM   1208  C  CA    . ASN A 1 146 ? 124.103 141.044 84.499  1.00 27.56 ?  146 ASN A CA    1 
ATOM   1209  C  C     . ASN A 1 146 ? 124.856 140.067 85.386  1.00 29.54 ?  146 ASN A C     1 
ATOM   1210  O  O     . ASN A 1 146 ? 125.492 139.146 84.867  1.00 36.63 ?  146 ASN A O     1 
ATOM   1211  C  CB    . ASN A 1 146 ? 125.097 141.834 83.647  1.00 29.11 ?  146 ASN A CB    1 
ATOM   1212  C  CG    . ASN A 1 146 ? 124.417 142.700 82.610  1.00 33.00 ?  146 ASN A CG    1 
ATOM   1213  O  OD1   . ASN A 1 146 ? 123.245 142.503 82.293  1.00 34.73 ?  146 ASN A OD1   1 
ATOM   1214  N  ND2   . ASN A 1 146 ? 125.150 143.667 82.074  1.00 35.28 ?  146 ASN A ND2   1 
ATOM   1215  N  N     . GLN A 1 147 ? 124.794 140.262 86.704  1.00 28.22 ?  147 GLN A N     1 
ATOM   1216  C  CA    . GLN A 1 147 ? 125.462 139.412 87.683  1.00 24.26 ?  147 GLN A CA    1 
ATOM   1217  C  C     . GLN A 1 147 ? 126.967 139.379 87.460  1.00 27.66 ?  147 GLN A C     1 
ATOM   1218  O  O     . GLN A 1 147 ? 127.614 138.359 87.682  1.00 34.10 ?  147 GLN A O     1 
ATOM   1219  C  CB    . GLN A 1 147 ? 124.873 137.999 87.682  1.00 24.18 ?  147 GLN A CB    1 
ATOM   1220  C  CG    . GLN A 1 147 ? 123.437 137.947 88.173  1.00 23.63 ?  147 GLN A CG    1 
ATOM   1221  C  CD    . GLN A 1 147 ? 122.998 136.557 88.564  1.00 27.67 ?  147 GLN A CD    1 
ATOM   1222  O  OE1   . GLN A 1 147 ? 122.353 136.363 89.594  1.00 31.18 ?  147 GLN A OE1   1 
ATOM   1223  N  NE2   . GLN A 1 147 ? 123.337 135.576 87.738  1.00 35.38 ?  147 GLN A NE2   1 
ATOM   1224  N  N     . GLU A 1 148 ? 127.531 140.498 87.001  1.00 26.16 ?  148 GLU A N     1 
ATOM   1225  C  CA    . GLU A 1 148 ? 128.979 140.626 86.899  1.00 22.83 ?  148 GLU A CA    1 
ATOM   1226  C  C     . GLU A 1 148 ? 129.618 140.889 88.254  1.00 26.73 ?  148 GLU A C     1 
ATOM   1227  O  O     . GLU A 1 148 ? 130.739 140.435 88.507  1.00 28.77 ?  148 GLU A O     1 
ATOM   1228  C  CB    . GLU A 1 148 ? 129.337 141.746 85.924  1.00 21.54 ?  148 GLU A CB    1 
ATOM   1229  C  CG    . GLU A 1 148 ? 128.798 141.537 84.524  1.00 25.93 ?  148 GLU A CG    1 
ATOM   1230  C  CD    . GLU A 1 148 ? 128.944 142.768 83.657  1.00 32.88 ?  148 GLU A CD    1 
ATOM   1231  O  OE1   . GLU A 1 148 ? 128.021 143.608 83.651  1.00 33.79 ?  148 GLU A OE1   1 
ATOM   1232  O  OE2   . GLU A 1 148 ? 129.986 142.899 82.982  1.00 36.84 -1 148 GLU A OE2   1 
ATOM   1233  N  N     . TYR A 1 149 ? 128.929 141.616 89.127  1.00 24.71 ?  149 TYR A N     1 
ATOM   1234  C  CA    . TYR A 1 149 ? 129.402 141.899 90.473  1.00 19.22 ?  149 TYR A CA    1 
ATOM   1235  C  C     . TYR A 1 149 ? 128.289 141.606 91.464  1.00 22.08 ?  149 TYR A C     1 
ATOM   1236  O  O     . TYR A 1 149 ? 127.121 141.910 91.208  1.00 27.63 ?  149 TYR A O     1 
ATOM   1237  C  CB    . TYR A 1 149 ? 129.858 143.354 90.608  1.00 19.77 ?  149 TYR A CB    1 
ATOM   1238  C  CG    . TYR A 1 149 ? 130.071 143.810 92.033  1.00 24.10 ?  149 TYR A CG    1 
ATOM   1239  C  CD1   . TYR A 1 149 ? 131.083 143.270 92.813  1.00 16.11 ?  149 TYR A CD1   1 
ATOM   1240  C  CD2   . TYR A 1 149 ? 129.258 144.782 92.598  1.00 21.98 ?  149 TYR A CD2   1 
ATOM   1241  C  CE1   . TYR A 1 149 ? 131.279 143.687 94.113  1.00 16.16 ?  149 TYR A CE1   1 
ATOM   1242  C  CE2   . TYR A 1 149 ? 129.445 145.202 93.895  1.00 21.75 ?  149 TYR A CE2   1 
ATOM   1243  C  CZ    . TYR A 1 149 ? 130.458 144.653 94.648  1.00 18.88 ?  149 TYR A CZ    1 
ATOM   1244  O  OH    . TYR A 1 149 ? 130.648 145.070 95.943  1.00 21.26 ?  149 TYR A OH    1 
ATOM   1245  N  N     . GLN A 1 150 ? 128.655 141.008 92.588  1.00 18.57 ?  150 GLN A N     1 
ATOM   1246  C  CA    . GLN A 1 150 ? 127.701 140.685 93.645  1.00 14.00 ?  150 GLN A CA    1 
ATOM   1247  C  C     . GLN A 1 150 ? 128.166 141.285 94.961  1.00 16.18 ?  150 GLN A C     1 
ATOM   1248  O  O     . GLN A 1 150 ? 129.211 140.866 95.495  1.00 23.41 ?  150 GLN A O     1 
ATOM   1249  C  CB    . GLN A 1 150 ? 127.540 139.172 93.776  1.00 19.28 ?  150 GLN A CB    1 
ATOM   1250  C  CG    . GLN A 1 150 ? 126.801 138.714 95.019  1.00 21.38 ?  150 GLN A CG    1 
ATOM   1251  C  CD    . GLN A 1 150 ? 125.371 139.204 95.069  1.00 16.86 ?  150 GLN A CD    1 
ATOM   1252  O  OE1   . GLN A 1 150 ? 124.535 138.801 94.262  1.00 29.61 ?  150 GLN A OE1   1 
ATOM   1253  N  NE2   . GLN A 1 150 ? 125.080 140.077 96.022  1.00 14.13 ?  150 GLN A NE2   1 
ATOM   1254  N  N     . PRO A 1 151 ? 127.450 142.262 95.514  1.00 25.42 ?  151 PRO A N     1 
ATOM   1255  C  CA    . PRO A 1 151 ? 127.778 142.739 96.860  1.00 16.72 ?  151 PRO A CA    1 
ATOM   1256  C  C     . PRO A 1 151 ? 127.614 141.624 97.881  1.00 18.06 ?  151 PRO A C     1 
ATOM   1257  O  O     . PRO A 1 151 ? 126.815 140.702 97.704  1.00 24.62 ?  151 PRO A O     1 
ATOM   1258  C  CB    . PRO A 1 151 ? 126.770 143.869 97.095  1.00 15.05 ?  151 PRO A CB    1 
ATOM   1259  C  CG    . PRO A 1 151 ? 126.327 144.278 95.731  1.00 20.42 ?  151 PRO A CG    1 
ATOM   1260  C  CD    . PRO A 1 151 ? 126.364 143.040 94.897  1.00 22.10 ?  151 PRO A CD    1 
ATOM   1261  N  N     . SER A 1 152 ? 128.395 141.711 98.953  1.00 20.26 ?  152 SER A N     1 
ATOM   1262  C  CA    . SER A 1 152 ? 128.383 140.677 99.975  1.00 16.72 ?  152 SER A CA    1 
ATOM   1263  C  C     . SER A 1 152 ? 126.998 140.542 100.600 1.00 23.77 ?  152 SER A C     1 
ATOM   1264  O  O     . SER A 1 152 ? 126.124 141.397 100.439 1.00 26.90 ?  152 SER A O     1 
ATOM   1265  C  CB    . SER A 1 152 ? 129.415 140.986 101.057 1.00 25.81 ?  152 SER A CB    1 
ATOM   1266  O  OG    . SER A 1 152 ? 129.021 142.106 101.828 1.00 28.95 ?  152 SER A OG    1 
ATOM   1267  N  N     . THR A 1 153 ? 126.804 139.435 101.316 1.00 30.12 ?  153 THR A N     1 
ATOM   1268  C  CA    . THR A 1 153 ? 125.531 139.175 101.986 1.00 23.96 ?  153 THR A CA    1 
ATOM   1269  C  C     . THR A 1 153 ? 125.076 140.317 102.888 1.00 30.26 ?  153 THR A C     1 
ATOM   1270  O  O     . THR A 1 153 ? 123.897 140.694 102.808 1.00 27.34 ?  153 THR A O     1 
ATOM   1271  C  CB    . THR A 1 153 ? 125.631 137.854 102.763 1.00 23.09 ?  153 THR A CB    1 
ATOM   1272  O  OG1   . THR A 1 153 ? 125.663 136.758 101.842 1.00 35.60 ?  153 THR A OG1   1 
ATOM   1273  C  CG2   . THR A 1 153 ? 124.448 137.682 103.704 1.00 24.13 ?  153 THR A CG2   1 
ATOM   1274  N  N     . PRO A 1 154 ? 125.922 140.915 103.737 1.00 29.45 ?  154 PRO A N     1 
ATOM   1275  C  CA    . PRO A 1 154 ? 125.443 142.068 104.522 1.00 21.01 ?  154 PRO A CA    1 
ATOM   1276  C  C     . PRO A 1 154 ? 124.996 143.237 103.662 1.00 22.76 ?  154 PRO A C     1 
ATOM   1277  O  O     . PRO A 1 154 ? 123.906 143.782 103.877 1.00 30.56 ?  154 PRO A O     1 
ATOM   1278  C  CB    . PRO A 1 154 ? 126.657 142.426 105.388 1.00 23.98 ?  154 PRO A CB    1 
ATOM   1279  C  CG    . PRO A 1 154 ? 127.465 141.200 105.435 1.00 21.87 ?  154 PRO A CG    1 
ATOM   1280  C  CD    . PRO A 1 154 ? 127.299 140.548 104.114 1.00 22.33 ?  154 PRO A CD    1 
ATOM   1281  N  N     . THR A 1 155 ? 125.808 143.634 102.682 1.00 22.52 ?  155 THR A N     1 
ATOM   1282  C  CA    . THR A 1 155 ? 125.453 144.769 101.837 1.00 22.76 ?  155 THR A CA    1 
ATOM   1283  C  C     . THR A 1 155 ? 124.228 144.460 100.985 1.00 25.20 ?  155 THR A C     1 
ATOM   1284  O  O     . THR A 1 155 ? 123.272 145.239 100.954 1.00 25.43 ?  155 THR A O     1 
ATOM   1285  C  CB    . THR A 1 155 ? 126.637 145.157 100.953 1.00 21.27 ?  155 THR A CB    1 
ATOM   1286  O  OG1   . THR A 1 155 ? 127.771 145.453 101.774 1.00 27.97 ?  155 THR A OG1   1 
ATOM   1287  C  CG2   . THR A 1 155 ? 126.297 146.376 100.119 1.00 16.40 ?  155 THR A CG2   1 
ATOM   1288  N  N     . PHE A 1 156 ? 124.235 143.318 100.296 1.00 27.54 ?  156 PHE A N     1 
ATOM   1289  C  CA    . PHE A 1 156 ? 123.113 142.970 99.429  1.00 25.07 ?  156 PHE A CA    1 
ATOM   1290  C  C     . PHE A 1 156 ? 121.826 142.799 100.226 1.00 27.98 ?  156 PHE A C     1 
ATOM   1291  O  O     . PHE A 1 156 ? 120.736 143.105 99.733  1.00 29.53 ?  156 PHE A O     1 
ATOM   1292  C  CB    . PHE A 1 156 ? 123.433 141.695 98.648  1.00 25.40 ?  156 PHE A CB    1 
ATOM   1293  C  CG    . PHE A 1 156 ? 122.545 141.473 97.460  1.00 27.47 ?  156 PHE A CG    1 
ATOM   1294  C  CD1   . PHE A 1 156 ? 122.444 142.430 96.466  1.00 24.32 ?  156 PHE A CD1   1 
ATOM   1295  C  CD2   . PHE A 1 156 ? 121.813 140.305 97.336  1.00 26.19 ?  156 PHE A CD2   1 
ATOM   1296  C  CE1   . PHE A 1 156 ? 121.629 142.227 95.371  1.00 28.99 ?  156 PHE A CE1   1 
ATOM   1297  C  CE2   . PHE A 1 156 ? 120.997 140.097 96.245  1.00 24.92 ?  156 PHE A CE2   1 
ATOM   1298  C  CZ    . PHE A 1 156 ? 120.906 141.059 95.261  1.00 29.97 ?  156 PHE A CZ    1 
ATOM   1299  N  N     . LEU A 1 157 ? 121.935 142.312 101.461 1.00 31.66 ?  157 LEU A N     1 
ATOM   1300  C  CA    . LEU A 1 157 ? 120.760 142.076 102.289 1.00 28.13 ?  157 LEU A CA    1 
ATOM   1301  C  C     . LEU A 1 157 ? 120.229 143.349 102.936 1.00 29.68 ?  157 LEU A C     1 
ATOM   1302  O  O     . LEU A 1 157 ? 119.016 143.480 103.117 1.00 37.88 ?  157 LEU A O     1 
ATOM   1303  C  CB    . LEU A 1 157 ? 121.090 141.039 103.364 1.00 31.34 ?  157 LEU A CB    1 
ATOM   1304  C  CG    . LEU A 1 157 ? 120.001 140.691 104.379 1.00 31.00 ?  157 LEU A CG    1 
ATOM   1305  C  CD1   . LEU A 1 157 ? 118.791 140.106 103.683 1.00 29.27 ?  157 LEU A CD1   1 
ATOM   1306  C  CD2   . LEU A 1 157 ? 120.535 139.727 105.424 1.00 28.33 ?  157 LEU A CD2   1 
ATOM   1307  N  N     . ASN A 1 158 ? 121.101 144.293 103.283 1.00 32.61 ?  158 ASN A N     1 
ATOM   1308  C  CA    . ASN A 1 158 ? 120.708 145.420 104.116 1.00 26.65 ?  158 ASN A CA    1 
ATOM   1309  C  C     . ASN A 1 158 ? 120.781 146.770 103.413 1.00 31.48 ?  158 ASN A C     1 
ATOM   1310  O  O     . ASN A 1 158 ? 120.399 147.777 104.013 1.00 38.42 ?  158 ASN A O     1 
ATOM   1311  C  CB    . ASN A 1 158 ? 121.573 145.454 105.380 1.00 29.21 ?  158 ASN A CB    1 
ATOM   1312  C  CG    . ASN A 1 158 ? 121.552 144.142 106.135 1.00 36.03 ?  158 ASN A CG    1 
ATOM   1313  O  OD1   . ASN A 1 158 ? 120.513 143.493 106.245 1.00 38.85 ?  158 ASN A OD1   1 
ATOM   1314  N  ND2   . ASN A 1 158 ? 122.703 143.741 106.657 1.00 32.53 ?  158 ASN A ND2   1 
ATOM   1315  N  N     . ALA A 1 159 ? 121.256 146.828 102.169 1.00 33.82 ?  159 ALA A N     1 
ATOM   1316  C  CA    . ALA A 1 159 ? 121.386 148.113 101.491 1.00 29.94 ?  159 ALA A CA    1 
ATOM   1317  C  C     . ALA A 1 159 ? 120.028 148.768 101.283 1.00 36.52 ?  159 ALA A C     1 
ATOM   1318  O  O     . ALA A 1 159 ? 119.194 148.260 100.527 1.00 42.82 ?  159 ALA A O     1 
ATOM   1319  C  CB    . ALA A 1 159 ? 122.100 147.954 100.149 1.00 34.55 ?  159 ALA A CB    1 
ATOM   1320  N  N     . GLY A 1 160 ? 119.798 149.895 101.951 1.00 43.17 ?  160 GLY A N     1 
ATOM   1321  C  CA    . GLY A 1 160 ? 118.562 150.631 101.810 1.00 40.60 ?  160 GLY A CA    1 
ATOM   1322  C  C     . GLY A 1 160 ? 117.432 150.204 102.717 1.00 44.10 ?  160 GLY A C     1 
ATOM   1323  O  O     . GLY A 1 160 ? 116.314 150.704 102.556 1.00 45.10 ?  160 GLY A O     1 
ATOM   1324  N  N     . ARG A 1 161 ? 117.679 149.300 103.660 1.00 44.10 ?  161 ARG A N     1 
ATOM   1325  C  CA    . ARG A 1 161 ? 116.660 148.847 104.595 1.00 43.77 ?  161 ARG A CA    1 
ATOM   1326  C  C     . ARG A 1 161 ? 116.789 149.600 105.912 1.00 45.82 ?  161 ARG A C     1 
ATOM   1327  O  O     . ARG A 1 161 ? 117.900 149.888 106.367 1.00 48.53 ?  161 ARG A O     1 
ATOM   1328  C  CB    . ARG A 1 161 ? 116.768 147.341 104.835 1.00 41.51 ?  161 ARG A CB    1 
ATOM   1329  C  CG    . ARG A 1 161 ? 116.495 146.506 103.597 1.00 42.22 ?  161 ARG A CG    1 
ATOM   1330  C  CD    . ARG A 1 161 ? 116.260 145.049 103.942 1.00 41.57 ?  161 ARG A CD    1 
ATOM   1331  N  NE    . ARG A 1 161 ? 116.260 144.209 102.750 1.00 45.49 ?  161 ARG A NE    1 
ATOM   1332  C  CZ    . ARG A 1 161 ? 116.127 142.890 102.760 1.00 45.46 ?  161 ARG A CZ    1 
ATOM   1333  N  NH1   . ARG A 1 161 ? 115.975 142.218 103.890 1.00 43.98 1  161 ARG A NH1   1 
ATOM   1334  N  NH2   . ARG A 1 161 ? 116.152 142.227 101.608 1.00 42.72 ?  161 ARG A NH2   1 
ATOM   1335  N  N     . LYS A 1 162 ? 115.645 149.923 106.519 1.00 53.82 ?  162 LYS A N     1 
ATOM   1336  C  CA    . LYS A 1 162 ? 115.656 150.695 107.757 1.00 52.61 ?  162 LYS A CA    1 
ATOM   1337  C  C     . LYS A 1 162 ? 116.126 149.848 108.933 1.00 54.80 ?  162 LYS A C     1 
ATOM   1338  O  O     . LYS A 1 162 ? 117.153 150.144 109.554 1.00 55.62 ?  162 LYS A O     1 
ATOM   1339  C  CB    . LYS A 1 162 ? 114.263 151.264 108.032 1.00 52.45 ?  162 LYS A CB    1 
ATOM   1340  C  CG    . LYS A 1 162 ? 114.266 152.683 108.571 1.00 55.20 ?  162 LYS A CG    1 
ATOM   1341  C  CD    . LYS A 1 162 ? 112.887 153.314 108.477 1.00 55.29 ?  162 LYS A CD    1 
ATOM   1342  C  CE    . LYS A 1 162 ? 112.969 154.830 108.506 1.00 54.69 ?  162 LYS A CE    1 
ATOM   1343  N  NZ    . LYS A 1 162 ? 114.189 155.306 109.214 1.00 55.20 1  162 LYS A NZ    1 
ATOM   1344  N  N     . ARG A 1 163 ? 115.386 148.789 109.252 1.00 57.23 ?  163 ARG A N     1 
ATOM   1345  C  CA    . ARG A 1 163 ? 115.736 147.904 110.362 1.00 57.25 ?  163 ARG A CA    1 
ATOM   1346  C  C     . ARG A 1 163 ? 116.730 146.855 109.870 1.00 58.83 ?  163 ARG A C     1 
ATOM   1347  O  O     . ARG A 1 163 ? 116.395 145.707 109.573 1.00 57.95 ?  163 ARG A O     1 
ATOM   1348  C  CB    . ARG A 1 163 ? 114.478 147.272 110.949 1.00 60.18 ?  163 ARG A CB    1 
ATOM   1349  C  CG    . ARG A 1 163 ? 113.516 148.283 111.552 1.00 58.41 ?  163 ARG A CG    1 
ATOM   1350  C  CD    . ARG A 1 163 ? 112.162 147.660 111.837 1.00 58.40 ?  163 ARG A CD    1 
ATOM   1351  N  NE    . ARG A 1 163 ? 111.489 147.255 110.611 1.00 60.59 ?  163 ARG A NE    1 
ATOM   1352  C  CZ    . ARG A 1 163 ? 110.375 146.537 110.569 1.00 62.32 ?  163 ARG A CZ    1 
ATOM   1353  N  NH1   . ARG A 1 163 ? 109.771 146.135 111.676 1.00 61.42 1  163 ARG A NH1   1 
ATOM   1354  N  NH2   . ARG A 1 163 ? 109.853 146.215 109.389 1.00 59.59 ?  163 ARG A NH2   1 
ATOM   1355  N  N     . ARG A 1 164 ? 117.983 147.287 109.790 1.00 53.64 ?  164 ARG A N     1 
ATOM   1356  C  CA    . ARG A 1 164 ? 119.052 146.520 109.176 1.00 50.73 ?  164 ARG A CA    1 
ATOM   1357  C  C     . ARG A 1 164 ? 120.250 146.431 110.110 1.00 51.26 ?  164 ARG A C     1 
ATOM   1358  O  O     . ARG A 1 164 ? 120.421 147.245 111.022 1.00 52.65 ?  164 ARG A O     1 
ATOM   1359  C  CB    . ARG A 1 164 ? 119.492 147.156 107.853 1.00 49.66 ?  164 ARG A CB    1 
ATOM   1360  C  CG    . ARG A 1 164 ? 120.257 148.461 108.036 1.00 46.69 ?  164 ARG A CG    1 
ATOM   1361  C  CD    . ARG A 1 164 ? 121.144 148.755 106.844 1.00 49.28 ?  164 ARG A CD    1 
ATOM   1362  N  NE    . ARG A 1 164 ? 121.949 149.958 107.022 1.00 50.57 ?  164 ARG A NE    1 
ATOM   1363  C  CZ    . ARG A 1 164 ? 122.167 150.857 106.072 1.00 51.84 ?  164 ARG A CZ    1 
ATOM   1364  N  NH1   . ARG A 1 164 ? 121.643 150.727 104.864 1.00 47.62 1  164 ARG A NH1   1 
ATOM   1365  N  NH2   . ARG A 1 164 ? 122.931 151.912 106.340 1.00 50.81 ?  164 ARG A NH2   1 
ATOM   1366  N  N     . GLY A 1 165 ? 121.080 145.421 109.870 1.00 45.41 ?  165 GLY A N     1 
ATOM   1367  C  CA    . GLY A 1 165 ? 122.390 145.351 110.474 1.00 42.70 ?  165 GLY A CA    1 
ATOM   1368  C  C     . GLY A 1 165 ? 123.392 146.168 109.683 1.00 47.81 ?  165 GLY A C     1 
ATOM   1369  O  O     . GLY A 1 165 ? 123.053 146.914 108.763 1.00 44.98 ?  165 GLY A O     1 
ATOM   1370  N  N     . GLU A 1 166 ? 124.658 146.020 110.056 1.00 45.86 ?  166 GLU A N     1 
ATOM   1371  C  CA    . GLU A 1 166 ? 125.707 146.730 109.344 1.00 39.66 ?  166 GLU A CA    1 
ATOM   1372  C  C     . GLU A 1 166 ? 125.986 146.064 108.000 1.00 37.91 ?  166 GLU A C     1 
ATOM   1373  O  O     . GLU A 1 166 ? 125.691 144.886 107.783 1.00 38.58 ?  166 GLU A O     1 
ATOM   1374  C  CB    . GLU A 1 166 ? 126.985 146.788 110.179 1.00 37.81 ?  166 GLU A CB    1 
ATOM   1375  C  CG    . GLU A 1 166 ? 126.939 147.804 111.308 1.00 41.94 ?  166 GLU A CG    1 
ATOM   1376  C  CD    . GLU A 1 166 ? 126.716 149.223 110.818 1.00 47.92 ?  166 GLU A CD    1 
ATOM   1377  O  OE1   . GLU A 1 166 ? 127.141 149.545 109.689 1.00 46.33 ?  166 GLU A OE1   1 
ATOM   1378  O  OE2   . GLU A 1 166 ? 126.114 150.021 111.568 1.00 45.41 -1 166 GLU A OE2   1 
ATOM   1379  N  N     . LEU A 1 167 ? 126.561 146.845 107.087 1.00 33.25 ?  167 LEU A N     1 
ATOM   1380  C  CA    . LEU A 1 167 ? 126.957 146.327 105.784 1.00 25.75 ?  167 LEU A CA    1 
ATOM   1381  C  C     . LEU A 1 167 ? 128.295 145.605 105.825 1.00 30.06 ?  167 LEU A C     1 
ATOM   1382  O  O     . LEU A 1 167 ? 128.682 144.995 104.824 1.00 32.58 ?  167 LEU A O     1 
ATOM   1383  C  CB    . LEU A 1 167 ? 127.017 147.463 104.761 1.00 27.51 ?  167 LEU A CB    1 
ATOM   1384  C  CG    . LEU A 1 167 ? 125.730 148.236 104.475 1.00 28.18 ?  167 LEU A CG    1 
ATOM   1385  C  CD1   . LEU A 1 167 ? 125.813 148.897 103.117 1.00 31.34 ?  167 LEU A CD1   1 
ATOM   1386  C  CD2   . LEU A 1 167 ? 124.518 147.331 104.543 1.00 28.89 ?  167 LEU A CD2   1 
ATOM   1387  N  N     . VAL A 1 168 ? 129.002 145.662 106.948 1.00 33.17 ?  168 VAL A N     1 
ATOM   1388  C  CA    . VAL A 1 168 ? 130.254 144.947 107.147 1.00 26.44 ?  168 VAL A CA    1 
ATOM   1389  C  C     . VAL A 1 168 ? 130.019 143.864 108.189 1.00 30.61 ?  168 VAL A C     1 
ATOM   1390  O  O     . VAL A 1 168 ? 129.388 144.111 109.223 1.00 36.41 ?  168 VAL A O     1 
ATOM   1391  C  CB    . VAL A 1 168 ? 131.383 145.900 107.588 1.00 26.26 ?  168 VAL A CB    1 
ATOM   1392  C  CG1   . VAL A 1 168 ? 132.691 145.146 107.740 1.00 29.07 ?  168 VAL A CG1   1 
ATOM   1393  C  CG2   . VAL A 1 168 ? 131.532 147.036 106.592 1.00 31.34 ?  168 VAL A CG2   1 
ATOM   1394  N  N     . SER A 1 169 ? 130.521 142.661 107.917 1.00 29.13 ?  169 SER A N     1 
ATOM   1395  C  CA    . SER A 1 169 ? 130.346 141.541 108.828 1.00 30.02 ?  169 SER A CA    1 
ATOM   1396  C  C     . SER A 1 169 ? 131.654 140.919 109.294 1.00 25.74 ?  169 SER A C     1 
ATOM   1397  O  O     . SER A 1 169 ? 131.619 139.999 110.117 1.00 31.17 ?  169 SER A O     1 
ATOM   1398  C  CB    . SER A 1 169 ? 129.473 140.456 108.187 1.00 33.72 ?  169 SER A CB    1 
ATOM   1399  O  OG    . SER A 1 169 ? 128.110 140.642 108.525 1.00 37.71 ?  169 SER A OG    1 
ATOM   1400  N  N     . CYS A 1 170 ? 132.796 141.378 108.798 1.00 28.39 ?  170 CYS A N     1 
ATOM   1401  C  CA    . CYS A 1 170 ? 134.090 140.883 109.247 1.00 26.92 ?  170 CYS A CA    1 
ATOM   1402  C  C     . CYS A 1 170 ? 134.783 141.983 110.037 1.00 25.20 ?  170 CYS A C     1 
ATOM   1403  O  O     . CYS A 1 170 ? 134.965 143.096 109.534 1.00 27.42 ?  170 CYS A O     1 
ATOM   1404  C  CB    . CYS A 1 170 ? 134.947 140.415 108.067 1.00 33.70 ?  170 CYS A CB    1 
ATOM   1405  S  SG    . CYS A 1 170 ? 135.500 141.692 106.909 1.00 51.33 ?  170 CYS A SG    1 
ATOM   1406  N  N     . PHE A 1 171 ? 135.137 141.677 111.281 1.00 22.44 ?  171 PHE A N     1 
ATOM   1407  C  CA    . PHE A 1 171 ? 135.851 142.598 112.151 1.00 16.13 ?  171 PHE A CA    1 
ATOM   1408  C  C     . PHE A 1 171 ? 137.014 141.869 112.802 1.00 16.35 ?  171 PHE A C     1 
ATOM   1409  O  O     . PHE A 1 171 ? 136.899 140.693 113.158 1.00 27.33 ?  171 PHE A O     1 
ATOM   1410  C  CB    . PHE A 1 171 ? 134.932 143.186 113.227 1.00 17.63 ?  171 PHE A CB    1 
ATOM   1411  C  CG    . PHE A 1 171 ? 133.703 143.846 112.676 1.00 17.41 ?  171 PHE A CG    1 
ATOM   1412  C  CD1   . PHE A 1 171 ? 133.758 145.135 112.181 1.00 16.60 ?  171 PHE A CD1   1 
ATOM   1413  C  CD2   . PHE A 1 171 ? 132.492 143.176 112.657 1.00 16.10 ?  171 PHE A CD2   1 
ATOM   1414  C  CE1   . PHE A 1 171 ? 132.632 145.743 111.673 1.00 15.99 ?  171 PHE A CE1   1 
ATOM   1415  C  CE2   . PHE A 1 171 ? 131.364 143.781 112.151 1.00 16.69 ?  171 PHE A CE2   1 
ATOM   1416  C  CZ    . PHE A 1 171 ? 131.434 145.065 111.660 1.00 14.78 ?  171 PHE A CZ    1 
ATOM   1417  N  N     . LEU A 1 172 ? 138.132 142.572 112.947 1.00 17.80 ?  172 LEU A N     1 
ATOM   1418  C  CA    . LEU A 1 172 ? 139.337 142.028 113.555 1.00 7.46  ?  172 LEU A CA    1 
ATOM   1419  C  C     . LEU A 1 172 ? 139.746 142.941 114.698 1.00 13.17 ?  172 LEU A C     1 
ATOM   1420  O  O     . LEU A 1 172 ? 139.918 144.146 114.498 1.00 17.99 ?  172 LEU A O     1 
ATOM   1421  C  CB    . LEU A 1 172 ? 140.475 141.910 112.534 1.00 12.46 ?  172 LEU A CB    1 
ATOM   1422  C  CG    . LEU A 1 172 ? 140.369 140.861 111.425 1.00 7.26  ?  172 LEU A CG    1 
ATOM   1423  C  CD1   . LEU A 1 172 ? 139.468 141.344 110.302 1.00 11.37 ?  172 LEU A CD1   1 
ATOM   1424  C  CD2   . LEU A 1 172 ? 141.747 140.530 110.892 1.00 11.04 ?  172 LEU A CD2   1 
ATOM   1425  N  N     . LEU A 1 173 ? 139.902 142.371 115.889 1.00 22.03 ?  173 LEU A N     1 
ATOM   1426  C  CA    . LEU A 1 173 ? 140.200 143.137 117.090 1.00 9.24  ?  173 LEU A CA    1 
ATOM   1427  C  C     . LEU A 1 173 ? 141.539 142.711 117.672 1.00 16.79 ?  173 LEU A C     1 
ATOM   1428  O  O     . LEU A 1 173 ? 141.828 141.517 117.783 1.00 26.59 ?  173 LEU A O     1 
ATOM   1429  C  CB    . LEU A 1 173 ? 139.113 142.959 118.152 1.00 14.56 ?  173 LEU A CB    1 
ATOM   1430  C  CG    . LEU A 1 173 ? 137.655 143.199 117.764 1.00 16.55 ?  173 LEU A CG    1 
ATOM   1431  C  CD1   . LEU A 1 173 ? 136.777 143.051 118.991 1.00 20.59 ?  173 LEU A CD1   1 
ATOM   1432  C  CD2   . LEU A 1 173 ? 137.469 144.562 117.125 1.00 15.88 ?  173 LEU A CD2   1 
ATOM   1433  N  N     . GLU A 1 174 ? 142.349 143.694 118.045 1.00 23.22 ?  174 GLU A N     1 
ATOM   1434  C  CA    . GLU A 1 174 ? 143.583 143.462 118.780 1.00 19.58 ?  174 GLU A CA    1 
ATOM   1435  C  C     . GLU A 1 174 ? 143.308 143.672 120.263 1.00 17.36 ?  174 GLU A C     1 
ATOM   1436  O  O     . GLU A 1 174 ? 142.785 144.719 120.657 1.00 29.19 ?  174 GLU A O     1 
ATOM   1437  C  CB    . GLU A 1 174 ? 144.694 144.396 118.302 1.00 22.04 ?  174 GLU A CB    1 
ATOM   1438  C  CG    . GLU A 1 174 ? 145.225 144.085 116.921 1.00 20.41 ?  174 GLU A CG    1 
ATOM   1439  C  CD    . GLU A 1 174 ? 146.701 143.756 116.932 1.00 19.96 ?  174 GLU A CD    1 
ATOM   1440  O  OE1   . GLU A 1 174 ? 147.521 144.696 116.937 1.00 22.11 ?  174 GLU A OE1   1 
ATOM   1441  O  OE2   . GLU A 1 174 ? 147.043 142.556 116.934 1.00 32.00 -1 174 GLU A OE2   1 
ATOM   1442  N  N     . VAL A 1 175 ? 143.656 142.683 121.078 1.00 18.09 ?  175 VAL A N     1 
ATOM   1443  C  CA    . VAL A 1 175 ? 143.421 142.730 122.516 1.00 21.78 ?  175 VAL A CA    1 
ATOM   1444  C  C     . VAL A 1 175 ? 144.751 142.979 123.213 1.00 19.70 ?  175 VAL A C     1 
ATOM   1445  O  O     . VAL A 1 175 ? 145.703 142.207 123.045 1.00 21.46 ?  175 VAL A O     1 
ATOM   1446  C  CB    . VAL A 1 175 ? 142.769 141.434 123.022 1.00 21.89 ?  175 VAL A CB    1 
ATOM   1447  C  CG1   . VAL A 1 175 ? 142.127 141.657 124.382 1.00 15.48 ?  175 VAL A CG1   1 
ATOM   1448  C  CG2   . VAL A 1 175 ? 141.747 140.928 122.020 1.00 17.38 ?  175 VAL A CG2   1 
ATOM   1449  N  N     . ASN A 1 176 ? 144.819 144.053 123.993 1.00 15.24 ?  176 ASN A N     1 
ATOM   1450  C  CA    . ASN A 1 176 ? 146.014 144.355 124.761 1.00 18.20 ?  176 ASN A CA    1 
ATOM   1451  C  C     . ASN A 1 176 ? 146.036 143.545 126.054 1.00 21.81 ?  176 ASN A C     1 
ATOM   1452  O  O     . ASN A 1 176 ? 145.019 143.012 126.505 1.00 21.13 ?  176 ASN A O     1 
ATOM   1453  C  CB    . ASN A 1 176 ? 146.093 145.849 125.070 1.00 18.41 ?  176 ASN A CB    1 
ATOM   1454  C  CG    . ASN A 1 176 ? 147.497 146.392 124.961 1.00 23.52 ?  176 ASN A CG    1 
ATOM   1455  O  OD1   . ASN A 1 176 ? 148.471 145.649 125.067 1.00 27.38 ?  176 ASN A OD1   1 
ATOM   1456  N  ND2   . ASN A 1 176 ? 147.610 147.694 124.741 1.00 21.82 ?  176 ASN A ND2   1 
ATOM   1457  N  N     . ASP A 1 177 ? 147.222 143.466 126.657 1.00 29.34 ?  177 ASP A N     1 
ATOM   1458  C  CA    . ASP A 1 177 ? 147.446 142.623 127.831 1.00 22.42 ?  177 ASP A CA    1 
ATOM   1459  C  C     . ASP A 1 177 ? 147.049 143.377 129.102 1.00 22.88 ?  177 ASP A C     1 
ATOM   1460  O  O     . ASP A 1 177 ? 147.875 143.781 129.920 1.00 27.43 ?  177 ASP A O     1 
ATOM   1461  C  CB    . ASP A 1 177 ? 148.898 142.167 127.880 1.00 21.20 ?  177 ASP A CB    1 
ATOM   1462  C  CG    . ASP A 1 177 ? 149.143 141.111 128.934 1.00 27.82 ?  177 ASP A CG    1 
ATOM   1463  O  OD1   . ASP A 1 177 ? 148.241 140.281 129.164 1.00 30.56 ?  177 ASP A OD1   1 
ATOM   1464  O  OD2   . ASP A 1 177 ? 150.240 141.109 129.529 1.00 29.71 -1 177 ASP A OD2   1 
ATOM   1465  N  N     . SER A 1 178 ? 145.741 143.559 129.255 1.00 22.26 ?  178 SER A N     1 
ATOM   1466  C  CA    . SER A 1 178 ? 145.205 144.211 130.441 1.00 18.11 ?  178 SER A CA    1 
ATOM   1467  C  C     . SER A 1 178 ? 143.762 143.770 130.635 1.00 20.63 ?  178 SER A C     1 
ATOM   1468  O  O     . SER A 1 178 ? 143.091 143.349 129.693 1.00 29.47 ?  178 SER A O     1 
ATOM   1469  C  CB    . SER A 1 178 ? 145.298 145.736 130.335 1.00 19.31 ?  178 SER A CB    1 
ATOM   1470  O  OG    . SER A 1 178 ? 144.081 146.293 129.881 1.00 25.10 ?  178 SER A OG    1 
ATOM   1471  N  N     . LEU A 1 179 ? 143.296 143.872 131.882 1.00 27.75 ?  179 LEU A N     1 
ATOM   1472  C  CA    . LEU A 1 179 ? 141.909 143.533 132.182 1.00 20.46 ?  179 LEU A CA    1 
ATOM   1473  C  C     . LEU A 1 179 ? 140.951 144.558 131.591 1.00 22.67 ?  179 LEU A C     1 
ATOM   1474  O  O     . LEU A 1 179 ? 139.847 144.206 131.163 1.00 27.44 ?  179 LEU A O     1 
ATOM   1475  C  CB    . LEU A 1 179 ? 141.704 143.422 133.693 1.00 23.33 ?  179 LEU A CB    1 
ATOM   1476  C  CG    . LEU A 1 179 ? 140.353 142.868 134.148 1.00 22.04 ?  179 LEU A CG    1 
ATOM   1477  C  CD1   . LEU A 1 179 ? 140.245 141.387 133.828 1.00 24.32 ?  179 LEU A CD1   1 
ATOM   1478  C  CD2   . LEU A 1 179 ? 140.144 143.121 135.630 1.00 21.57 ?  179 LEU A CD2   1 
ATOM   1479  N  N     . ASN A 1 180 ? 141.347 145.833 131.575 1.00 23.10 ?  180 ASN A N     1 
ATOM   1480  C  CA    . ASN A 1 180 ? 140.530 146.849 130.921 1.00 21.89 ?  180 ASN A CA    1 
ATOM   1481  C  C     . ASN A 1 180 ? 140.375 146.544 129.438 1.00 26.71 ?  180 ASN A C     1 
ATOM   1482  O  O     . ASN A 1 180 ? 139.273 146.638 128.886 1.00 30.16 ?  180 ASN A O     1 
ATOM   1483  C  CB    . ASN A 1 180 ? 141.154 148.229 131.116 1.00 22.57 ?  180 ASN A CB    1 
ATOM   1484  C  CG    . ASN A 1 180 ? 140.809 148.844 132.454 1.00 27.08 ?  180 ASN A CG    1 
ATOM   1485  O  OD1   . ASN A 1 180 ? 139.789 148.516 133.058 1.00 33.00 ?  180 ASN A OD1   1 
ATOM   1486  N  ND2   . ASN A 1 180 ? 141.661 149.745 132.924 1.00 27.92 ?  180 ASN A ND2   1 
ATOM   1487  N  N     . ASP A 1 181 ? 141.471 146.156 128.786 1.00 25.42 ?  181 ASP A N     1 
ATOM   1488  C  CA    . ASP A 1 181 ? 141.416 145.833 127.366 1.00 16.89 ?  181 ASP A CA    1 
ATOM   1489  C  C     . ASP A 1 181 ? 140.653 144.542 127.108 1.00 20.98 ?  181 ASP A C     1 
ATOM   1490  O  O     . ASP A 1 181 ? 139.974 144.429 126.087 1.00 25.91 ?  181 ASP A O     1 
ATOM   1491  C  CB    . ASP A 1 181 ? 142.829 145.753 126.800 1.00 20.00 ?  181 ASP A CB    1 
ATOM   1492  C  CG    . ASP A 1 181 ? 143.460 147.119 126.627 1.00 32.71 ?  181 ASP A CG    1 
ATOM   1493  O  OD1   . ASP A 1 181 ? 143.116 147.813 125.649 1.00 36.80 ?  181 ASP A OD1   1 
ATOM   1494  O  OD2   . ASP A 1 181 ? 144.302 147.501 127.467 1.00 30.19 -1 181 ASP A OD2   1 
ATOM   1495  N  N     . ILE A 1 182 ? 140.734 143.569 128.014 1.00 21.36 ?  182 ILE A N     1 
ATOM   1496  C  CA    . ILE A 1 182 ? 139.965 142.338 127.844 1.00 21.47 ?  182 ILE A CA    1 
ATOM   1497  C  C     . ILE A 1 182 ? 138.474 142.612 128.002 1.00 18.86 ?  182 ILE A C     1 
ATOM   1498  O  O     . ILE A 1 182 ? 137.648 142.094 127.239 1.00 24.47 ?  182 ILE A O     1 
ATOM   1499  C  CB    . ILE A 1 182 ? 140.461 141.265 128.831 1.00 24.51 ?  182 ILE A CB    1 
ATOM   1500  C  CG1   . ILE A 1 182 ? 141.811 140.716 128.371 1.00 20.55 ?  182 ILE A CG1   1 
ATOM   1501  C  CG2   . ILE A 1 182 ? 139.447 140.139 128.963 1.00 26.74 ?  182 ILE A CG2   1 
ATOM   1502  C  CD1   . ILE A 1 182 ? 142.507 139.880 129.404 1.00 22.39 ?  182 ILE A CD1   1 
ATOM   1503  N  N     . SER A 1 183 ? 138.105 143.434 128.988 1.00 22.49 ?  183 SER A N     1 
ATOM   1504  C  CA    . SER A 1 183 ? 136.707 143.815 129.153 1.00 21.31 ?  183 SER A CA    1 
ATOM   1505  C  C     . SER A 1 183 ? 136.201 144.584 127.941 1.00 24.12 ?  183 SER A C     1 
ATOM   1506  O  O     . SER A 1 183 ? 135.084 144.344 127.464 1.00 30.09 ?  183 SER A O     1 
ATOM   1507  C  CB    . SER A 1 183 ? 136.539 144.649 130.421 1.00 21.24 ?  183 SER A CB    1 
ATOM   1508  O  OG    . SER A 1 183 ? 137.158 144.029 131.531 1.00 32.18 ?  183 SER A OG    1 
ATOM   1509  N  N     . ARG A 1 184 ? 137.008 145.513 127.427 1.00 23.49 ?  184 ARG A N     1 
ATOM   1510  C  CA    . ARG A 1 184 ? 136.612 146.241 126.227 1.00 23.99 ?  184 ARG A CA    1 
ATOM   1511  C  C     . ARG A 1 184 ? 136.513 145.322 125.020 1.00 28.93 ?  184 ARG A C     1 
ATOM   1512  O  O     . ARG A 1 184 ? 135.646 145.522 124.167 1.00 33.36 ?  184 ARG A O     1 
ATOM   1513  C  CB    . ARG A 1 184 ? 137.589 147.378 125.950 1.00 23.38 ?  184 ARG A CB    1 
ATOM   1514  C  CG    . ARG A 1 184 ? 136.985 148.504 125.136 1.00 27.12 ?  184 ARG A CG    1 
ATOM   1515  C  CD    . ARG A 1 184 ? 136.432 149.591 126.034 1.00 31.20 ?  184 ARG A CD    1 
ATOM   1516  N  NE    . ARG A 1 184 ? 134.994 149.755 125.864 1.00 31.34 ?  184 ARG A NE    1 
ATOM   1517  C  CZ    . ARG A 1 184 ? 134.266 150.664 126.497 1.00 35.55 ?  184 ARG A CZ    1 
ATOM   1518  N  NH1   . ARG A 1 184 ? 134.813 151.512 127.351 1.00 33.29 1  184 ARG A NH1   1 
ATOM   1519  N  NH2   . ARG A 1 184 ? 132.958 150.722 126.267 1.00 29.20 ?  184 ARG A NH2   1 
ATOM   1520  N  N     . ALA A 1 185 ? 137.387 144.318 124.924 1.00 28.47 ?  185 ALA A N     1 
ATOM   1521  C  CA    . ALA A 1 185 ? 137.296 143.358 123.832 1.00 15.38 ?  185 ALA A CA    1 
ATOM   1522  C  C     . ALA A 1 185 ? 136.005 142.559 123.912 1.00 21.04 ?  185 ALA A C     1 
ATOM   1523  O  O     . ALA A 1 185 ? 135.346 142.335 122.894 1.00 25.07 ?  185 ALA A O     1 
ATOM   1524  C  CB    . ALA A 1 185 ? 138.506 142.427 123.849 1.00 17.48 ?  185 ALA A CB    1 
ATOM   1525  N  N     . ILE A 1 186 ? 135.624 142.128 125.116 1.00 24.51 ?  186 ILE A N     1 
ATOM   1526  C  CA    . ILE A 1 186 ? 134.361 141.411 125.283 1.00 20.17 ?  186 ILE A CA    1 
ATOM   1527  C  C     . ILE A 1 186 ? 133.188 142.304 124.899 1.00 20.92 ?  186 ILE A C     1 
ATOM   1528  O  O     . ILE A 1 186 ? 132.267 141.880 124.185 1.00 27.02 ?  186 ILE A O     1 
ATOM   1529  C  CB    . ILE A 1 186 ? 134.226 140.898 126.729 1.00 27.30 ?  186 ILE A CB    1 
ATOM   1530  C  CG1   . ILE A 1 186 ? 135.218 139.768 126.995 1.00 24.05 ?  186 ILE A CG1   1 
ATOM   1531  C  CG2   . ILE A 1 186 ? 132.805 140.433 127.006 1.00 27.00 ?  186 ILE A CG2   1 
ATOM   1532  C  CD1   . ILE A 1 186 ? 135.439 139.503 128.466 1.00 25.30 ?  186 ILE A CD1   1 
ATOM   1533  N  N     . ASP A 1 187 ? 133.208 143.557 125.360 1.00 27.48 ?  187 ASP A N     1 
ATOM   1534  C  CA    . ASP A 1 187 ? 132.126 144.486 125.053 1.00 23.22 ?  187 ASP A CA    1 
ATOM   1535  C  C     . ASP A 1 187 ? 132.017 144.729 123.554 1.00 27.24 ?  187 ASP A C     1 
ATOM   1536  O  O     . ASP A 1 187 ? 130.923 144.676 122.986 1.00 32.57 ?  187 ASP A O     1 
ATOM   1537  C  CB    . ASP A 1 187 ? 132.346 145.802 125.799 1.00 22.13 ?  187 ASP A CB    1 
ATOM   1538  C  CG    . ASP A 1 187 ? 131.494 146.932 125.255 1.00 34.84 ?  187 ASP A CG    1 
ATOM   1539  O  OD1   . ASP A 1 187 ? 130.263 146.757 125.145 1.00 36.41 ?  187 ASP A OD1   1 
ATOM   1540  O  OD2   . ASP A 1 187 ? 132.058 147.999 124.932 1.00 37.56 -1 187 ASP A OD2   1 
ATOM   1541  N  N     . ILE A 1 188 ? 133.148 144.988 122.896 1.00 25.83 ?  188 ILE A N     1 
ATOM   1542  C  CA    . ILE A 1 188 ? 133.142 145.274 121.465 1.00 22.68 ?  188 ILE A CA    1 
ATOM   1543  C  C     . ILE A 1 188 ? 132.739 144.037 120.676 1.00 22.53 ?  188 ILE A C     1 
ATOM   1544  O  O     . ILE A 1 188 ? 132.039 144.135 119.663 1.00 28.19 ?  188 ILE A O     1 
ATOM   1545  C  CB    . ILE A 1 188 ? 134.516 145.812 121.026 1.00 25.08 ?  188 ILE A CB    1 
ATOM   1546  C  CG1   . ILE A 1 188 ? 134.762 147.197 121.624 1.00 23.81 ?  188 ILE A CG1   1 
ATOM   1547  C  CG2   . ILE A 1 188 ? 134.612 145.891 119.516 1.00 21.04 ?  188 ILE A CG2   1 
ATOM   1548  C  CD1   . ILE A 1 188 ? 136.113 147.768 121.286 1.00 23.99 ?  188 ILE A CD1   1 
ATOM   1549  N  N     . SER A 1 189 ? 133.167 142.856 121.124 1.00 24.80 ?  189 SER A N     1 
ATOM   1550  C  CA    . SER A 1 189 ? 132.764 141.624 120.462 1.00 14.85 ?  189 SER A CA    1 
ATOM   1551  C  C     . SER A 1 189 ? 131.257 141.433 120.537 1.00 21.48 ?  189 SER A C     1 
ATOM   1552  O  O     . SER A 1 189 ? 130.625 141.068 119.541 1.00 28.50 ?  189 SER A O     1 
ATOM   1553  C  CB    . SER A 1 189 ? 133.488 140.431 121.087 1.00 20.15 ?  189 SER A CB    1 
ATOM   1554  O  OG    . SER A 1 189 ? 134.883 140.659 121.150 1.00 24.99 ?  189 SER A OG    1 
ATOM   1555  N  N     . MET A 1 190 ? 130.662 141.681 121.705 1.00 24.96 ?  190 MET A N     1 
ATOM   1556  C  CA    . MET A 1 190 ? 129.210 141.572 121.810 1.00 25.46 ?  190 MET A CA    1 
ATOM   1557  C  C     . MET A 1 190 ? 128.506 142.638 120.977 1.00 24.52 ?  190 MET A C     1 
ATOM   1558  O  O     . MET A 1 190 ? 127.473 142.362 120.358 1.00 25.65 ?  190 MET A O     1 
ATOM   1559  C  CB    . MET A 1 190 ? 128.768 141.649 123.271 1.00 24.20 ?  190 MET A CB    1 
ATOM   1560  C  CG    . MET A 1 190 ? 128.937 140.340 124.024 1.00 25.61 ?  190 MET A CG    1 
ATOM   1561  S  SD    . MET A 1 190 ? 128.739 140.474 125.810 1.00 39.39 ?  190 MET A SD    1 
ATOM   1562  C  CE    . MET A 1 190 ? 128.952 142.231 126.050 1.00 30.50 ?  190 MET A CE    1 
ATOM   1563  N  N     . GLN A 1 191 ? 129.047 143.858 120.944 1.00 20.97 ?  191 GLN A N     1 
ATOM   1564  C  CA    . GLN A 1 191 ? 128.434 144.916 120.143 1.00 27.46 ?  191 GLN A CA    1 
ATOM   1565  C  C     . GLN A 1 191 ? 128.459 144.578 118.658 1.00 26.57 ?  191 GLN A C     1 
ATOM   1566  O  O     . GLN A 1 191 ? 127.472 144.802 117.947 1.00 30.30 ?  191 GLN A O     1 
ATOM   1567  C  CB    . GLN A 1 191 ? 129.138 146.250 120.394 1.00 28.45 ?  191 GLN A CB    1 
ATOM   1568  C  CG    . GLN A 1 191 ? 129.011 146.775 121.812 1.00 26.96 ?  191 GLN A CG    1 
ATOM   1569  C  CD    . GLN A 1 191 ? 127.597 147.184 122.168 1.00 29.87 ?  191 GLN A CD    1 
ATOM   1570  O  OE1   . GLN A 1 191 ? 127.201 147.128 123.330 1.00 30.00 ?  191 GLN A OE1   1 
ATOM   1571  N  NE2   . GLN A 1 191 ? 126.832 147.614 121.171 1.00 30.62 ?  191 GLN A NE2   1 
ATOM   1572  N  N     . LEU A 1 192 ? 129.579 144.043 118.168 1.00 26.64 ?  192 LEU A N     1 
ATOM   1573  C  CA    . LEU A 1 192 ? 129.697 143.726 116.751 1.00 21.91 ?  192 LEU A CA    1 
ATOM   1574  C  C     . LEU A 1 192 ? 128.935 142.461 116.380 1.00 24.46 ?  192 LEU A C     1 
ATOM   1575  O  O     . LEU A 1 192 ? 128.389 142.378 115.276 1.00 33.12 ?  192 LEU A O     1 
ATOM   1576  C  CB    . LEU A 1 192 ? 131.170 143.590 116.364 1.00 21.31 ?  192 LEU A CB    1 
ATOM   1577  C  CG    . LEU A 1 192 ? 132.008 144.869 116.425 1.00 20.35 ?  192 LEU A CG    1 
ATOM   1578  C  CD1   . LEU A 1 192 ? 133.485 144.551 116.294 1.00 20.92 ?  192 LEU A CD1   1 
ATOM   1579  C  CD2   . LEU A 1 192 ? 131.574 145.855 115.356 1.00 18.19 ?  192 LEU A CD2   1 
ATOM   1580  N  N     . SER A 1 193 ? 128.887 141.472 117.276 1.00 29.05 ?  193 SER A N     1 
ATOM   1581  C  CA    . SER A 1 193 ? 128.058 140.296 117.041 1.00 26.96 ?  193 SER A CA    1 
ATOM   1582  C  C     . SER A 1 193 ? 126.581 140.663 117.044 1.00 30.56 ?  193 SER A C     1 
ATOM   1583  O  O     . SER A 1 193 ? 125.784 140.066 116.313 1.00 34.58 ?  193 SER A O     1 
ATOM   1584  C  CB    . SER A 1 193 ? 128.355 139.232 118.096 1.00 28.66 ?  193 SER A CB    1 
ATOM   1585  O  OG    . SER A 1 193 ? 127.587 138.064 117.874 1.00 37.95 ?  193 SER A OG    1 
ATOM   1586  N  N     . LYS A 1 194 ? 126.198 141.641 117.868 1.00 33.77 ?  194 LYS A N     1 
ATOM   1587  C  CA    . LYS A 1 194 ? 124.828 142.140 117.855 1.00 31.64 ?  194 LYS A CA    1 
ATOM   1588  C  C     . LYS A 1 194 ? 124.484 142.753 116.504 1.00 36.17 ?  194 LYS A C     1 
ATOM   1589  O  O     . LYS A 1 194 ? 123.360 142.601 116.012 1.00 39.77 ?  194 LYS A O     1 
ATOM   1590  C  CB    . LYS A 1 194 ? 124.646 143.155 118.983 1.00 29.29 ?  194 LYS A CB    1 
ATOM   1591  C  CG    . LYS A 1 194 ? 123.453 144.073 118.832 1.00 33.70 ?  194 LYS A CG    1 
ATOM   1592  C  CD    . LYS A 1 194 ? 123.562 145.257 119.777 1.00 36.36 ?  194 LYS A CD    1 
ATOM   1593  C  CE    . LYS A 1 194 ? 122.238 145.990 119.906 1.00 34.10 ?  194 LYS A CE    1 
ATOM   1594  N  NZ    . LYS A 1 194 ? 122.333 147.132 120.854 1.00 34.07 1  194 LYS A NZ    1 
ATOM   1595  N  N     . LEU A 1 195 ? 125.443 143.442 115.885 1.00 34.21 ?  195 LEU A N     1 
ATOM   1596  C  CA    . LEU A 1 195 ? 125.247 143.992 114.550 1.00 31.80 ?  195 LEU A CA    1 
ATOM   1597  C  C     . LEU A 1 195 ? 125.207 142.918 113.472 1.00 34.40 ?  195 LEU A C     1 
ATOM   1598  O  O     . LEU A 1 195 ? 124.876 143.230 112.324 1.00 38.44 ?  195 LEU A O     1 
ATOM   1599  C  CB    . LEU A 1 195 ? 126.354 144.995 114.228 1.00 33.76 ?  195 LEU A CB    1 
ATOM   1600  C  CG    . LEU A 1 195 ? 126.431 146.220 115.137 1.00 34.19 ?  195 LEU A CG    1 
ATOM   1601  C  CD1   . LEU A 1 195 ? 127.688 147.019 114.841 1.00 30.68 ?  195 LEU A CD1   1 
ATOM   1602  C  CD2   . LEU A 1 195 ? 125.190 147.080 114.979 1.00 36.49 ?  195 LEU A CD2   1 
ATOM   1603  N  N     . GLY A 1 196 ? 125.538 141.674 113.809 1.00 31.78 ?  196 GLY A N     1 
ATOM   1604  C  CA    . GLY A 1 196 ? 125.529 140.585 112.859 1.00 30.65 ?  196 GLY A CA    1 
ATOM   1605  C  C     . GLY A 1 196 ? 126.879 140.226 112.283 1.00 35.94 ?  196 GLY A C     1 
ATOM   1606  O  O     . GLY A 1 196 ? 126.961 139.288 111.483 1.00 40.43 ?  196 GLY A O     1 
ATOM   1607  N  N     . GLY A 1 197 ? 127.935 140.935 112.664 1.00 30.13 ?  197 GLY A N     1 
ATOM   1608  C  CA    . GLY A 1 197 ? 129.247 140.689 112.109 1.00 24.75 ?  197 GLY A CA    1 
ATOM   1609  C  C     . GLY A 1 197 ? 130.003 139.579 112.817 1.00 24.86 ?  197 GLY A C     1 
ATOM   1610  O  O     . GLY A 1 197 ? 129.786 139.301 113.992 1.00 30.82 ?  197 GLY A O     1 
ATOM   1611  N  N     . GLY A 1 198 ? 130.903 138.942 112.070 1.00 20.05 ?  198 GLY A N     1 
ATOM   1612  C  CA    . GLY A 1 198 ? 131.824 137.979 112.641 1.00 17.92 ?  198 GLY A CA    1 
ATOM   1613  C  C     . GLY A 1 198 ? 133.061 138.696 113.143 1.00 16.53 ?  198 GLY A C     1 
ATOM   1614  O  O     . GLY A 1 198 ? 133.627 139.540 112.444 1.00 22.13 ?  198 GLY A O     1 
ATOM   1615  N  N     . VAL A 1 199 ? 133.478 138.358 114.358 1.00 20.68 ?  199 VAL A N     1 
ATOM   1616  C  CA    . VAL A 1 199 ? 134.547 139.068 115.048 1.00 16.18 ?  199 VAL A CA    1 
ATOM   1617  C  C     . VAL A 1 199 ? 135.725 138.126 115.235 1.00 11.98 ?  199 VAL A C     1 
ATOM   1618  O  O     . VAL A 1 199 ? 135.562 137.008 115.733 1.00 15.18 ?  199 VAL A O     1 
ATOM   1619  C  CB    . VAL A 1 199 ? 134.075 139.622 116.405 1.00 14.84 ?  199 VAL A CB    1 
ATOM   1620  C  CG1   . VAL A 1 199 ? 135.143 140.506 117.014 1.00 14.75 ?  199 VAL A CG1   1 
ATOM   1621  C  CG2   . VAL A 1 199 ? 132.776 140.384 116.239 1.00 18.84 ?  199 VAL A CG2   1 
ATOM   1622  N  N     . SER A 1 200 ? 136.907 138.580 114.837 1.00 16.69 ?  200 SER A N     1 
ATOM   1623  C  CA    . SER A 1 200 ? 138.151 137.870 115.083 1.00 7.23  ?  200 SER A CA    1 
ATOM   1624  C  C     . SER A 1 200 ? 138.987 138.666 116.074 1.00 12.61 ?  200 SER A C     1 
ATOM   1625  O  O     . SER A 1 200 ? 139.046 139.897 116.004 1.00 19.88 ?  200 SER A O     1 
ATOM   1626  C  CB    . SER A 1 200 ? 138.934 137.657 113.789 1.00 14.12 ?  200 SER A CB    1 
ATOM   1627  O  OG    . SER A 1 200 ? 139.869 136.606 113.929 1.00 19.62 ?  200 SER A OG    1 
ATOM   1628  N  N     . LEU A 1 201 ? 139.628 137.962 117.000 1.00 18.50 ?  201 LEU A N     1 
ATOM   1629  C  CA    . LEU A 1 201 ? 140.421 138.595 118.040 1.00 10.78 ?  201 LEU A CA    1 
ATOM   1630  C  C     . LEU A 1 201 ? 141.820 138.001 118.061 1.00 10.09 ?  201 LEU A C     1 
ATOM   1631  O  O     . LEU A 1 201 ? 141.990 136.783 117.969 1.00 15.23 ?  201 LEU A O     1 
ATOM   1632  C  CB    . LEU A 1 201 ? 139.766 138.432 119.417 1.00 14.87 ?  201 LEU A CB    1 
ATOM   1633  C  CG    . LEU A 1 201 ? 138.370 139.039 119.568 1.00 15.59 ?  201 LEU A CG    1 
ATOM   1634  C  CD1   . LEU A 1 201 ? 137.312 137.949 119.613 1.00 20.18 ?  201 LEU A CD1   1 
ATOM   1635  C  CD2   . LEU A 1 201 ? 138.296 139.915 120.803 1.00 12.72 ?  201 LEU A CD2   1 
ATOM   1636  N  N     . ASN A 1 202 ? 142.818 138.872 118.178 1.00 10.92 ?  202 ASN A N     1 
ATOM   1637  C  CA    . ASN A 1 202 ? 144.198 138.453 118.371 1.00 8.56  ?  202 ASN A CA    1 
ATOM   1638  C  C     . ASN A 1 202 ? 144.463 138.322 119.864 1.00 18.53 ?  202 ASN A C     1 
ATOM   1639  O  O     . ASN A 1 202 ? 144.307 139.290 120.615 1.00 29.15 ?  202 ASN A O     1 
ATOM   1640  C  CB    . ASN A 1 202 ? 145.163 139.452 117.739 1.00 9.92  ?  202 ASN A CB    1 
ATOM   1641  C  CG    . ASN A 1 202 ? 146.550 138.878 117.545 1.00 12.50 ?  202 ASN A CG    1 
ATOM   1642  O  OD1   . ASN A 1 202 ? 146.718 137.670 117.397 1.00 17.38 ?  202 ASN A OD1   1 
ATOM   1643  N  ND2   . ASN A 1 202 ? 147.553 139.746 117.546 1.00 10.64 ?  202 ASN A ND2   1 
ATOM   1644  N  N     . LEU A 1 203 ? 144.863 137.126 120.295 1.00 13.46 ?  203 LEU A N     1 
ATOM   1645  C  CA    . LEU A 1 203 ? 145.127 136.854 121.700 1.00 11.52 ?  203 LEU A CA    1 
ATOM   1646  C  C     . LEU A 1 203 ? 146.614 136.682 121.984 1.00 13.48 ?  203 LEU A C     1 
ATOM   1647  O  O     . LEU A 1 203 ? 146.986 136.185 123.050 1.00 21.45 ?  203 LEU A O     1 
ATOM   1648  C  CB    . LEU A 1 203 ? 144.351 135.615 122.150 1.00 17.29 ?  203 LEU A CB    1 
ATOM   1649  C  CG    . LEU A 1 203 ? 142.828 135.672 122.017 1.00 16.61 ?  203 LEU A CG    1 
ATOM   1650  C  CD1   . LEU A 1 203 ? 142.187 134.575 122.843 1.00 17.98 ?  203 LEU A CD1   1 
ATOM   1651  C  CD2   . LEU A 1 203 ? 142.288 137.033 122.428 1.00 13.98 ?  203 LEU A CD2   1 
ATOM   1652  N  N     . SER A 1 204 ? 147.474 137.094 121.052 1.00 12.80 ?  204 SER A N     1 
ATOM   1653  C  CA    . SER A 1 204 ? 148.908 136.888 121.214 1.00 15.21 ?  204 SER A CA    1 
ATOM   1654  C  C     . SER A 1 204 ? 149.524 137.856 122.215 1.00 20.30 ?  204 SER A C     1 
ATOM   1655  O  O     . SER A 1 204 ? 150.474 137.490 122.915 1.00 27.24 ?  204 SER A O     1 
ATOM   1656  C  CB    . SER A 1 204 ? 149.609 137.015 119.864 1.00 15.24 ?  204 SER A CB    1 
ATOM   1657  O  OG    . SER A 1 204 ? 149.024 136.152 118.907 1.00 22.85 ?  204 SER A OG    1 
ATOM   1658  N  N     . LYS A 1 205 ? 149.013 139.087 122.294 1.00 19.51 ?  205 LYS A N     1 
ATOM   1659  C  CA    . LYS A 1 205 ? 149.552 140.047 123.249 1.00 16.00 ?  205 LYS A CA    1 
ATOM   1660  C  C     . LYS A 1 205 ? 149.202 139.693 124.685 1.00 18.09 ?  205 LYS A C     1 
ATOM   1661  O  O     . LYS A 1 205 ? 149.873 140.167 125.606 1.00 22.70 ?  205 LYS A O     1 
ATOM   1662  C  CB    . LYS A 1 205 ? 149.056 141.456 122.928 1.00 16.09 ?  205 LYS A CB    1 
ATOM   1663  C  CG    . LYS A 1 205 ? 149.646 142.037 121.663 1.00 18.07 ?  205 LYS A CG    1 
ATOM   1664  C  CD    . LYS A 1 205 ? 149.154 143.447 121.421 1.00 23.59 ?  205 LYS A CD    1 
ATOM   1665  C  CE    . LYS A 1 205 ? 149.898 144.091 120.266 1.00 26.62 ?  205 LYS A CE    1 
ATOM   1666  N  NZ    . LYS A 1 205 ? 149.698 143.349 118.993 1.00 19.06 1  205 LYS A NZ    1 
ATOM   1667  N  N     . LEU A 1 206 ? 148.174 138.875 124.894 1.00 17.87 ?  206 LEU A N     1 
ATOM   1668  C  CA    . LEU A 1 206 ? 147.808 138.453 126.237 1.00 12.12 ?  206 LEU A CA    1 
ATOM   1669  C  C     . LEU A 1 206 ? 148.887 137.550 126.814 1.00 17.25 ?  206 LEU A C     1 
ATOM   1670  O  O     . LEU A 1 206 ? 149.387 136.649 126.133 1.00 21.62 ?  206 LEU A O     1 
ATOM   1671  C  CB    . LEU A 1 206 ? 146.468 137.725 126.212 1.00 19.76 ?  206 LEU A CB    1 
ATOM   1672  C  CG    . LEU A 1 206 ? 145.263 138.563 125.791 1.00 20.73 ?  206 LEU A CG    1 
ATOM   1673  C  CD1   . LEU A 1 206 ? 144.008 137.717 125.801 1.00 16.80 ?  206 LEU A CD1   1 
ATOM   1674  C  CD2   . LEU A 1 206 ? 145.112 139.767 126.701 1.00 23.23 ?  206 LEU A CD2   1 
ATOM   1675  N  N     . ARG A 1 207 ? 149.245 137.786 128.072 1.00 24.80 ?  207 ARG A N     1 
ATOM   1676  C  CA    . ARG A 1 207 ? 150.285 136.988 128.703 1.00 22.16 ?  207 ARG A CA    1 
ATOM   1677  C  C     . ARG A 1 207 ? 149.775 135.583 129.001 1.00 27.34 ?  207 ARG A C     1 
ATOM   1678  O  O     . ARG A 1 207 ? 148.577 135.353 129.186 1.00 27.88 ?  207 ARG A O     1 
ATOM   1679  C  CB    . ARG A 1 207 ? 150.785 137.663 129.977 1.00 22.25 ?  207 ARG A CB    1 
ATOM   1680  C  CG    . ARG A 1 207 ? 149.784 137.748 131.105 1.00 23.35 ?  207 ARG A CG    1 
ATOM   1681  C  CD    . ARG A 1 207 ? 150.324 138.630 132.213 1.00 26.39 ?  207 ARG A CD    1 
ATOM   1682  N  NE    . ARG A 1 207 ? 150.370 140.031 131.813 1.00 28.94 ?  207 ARG A NE    1 
ATOM   1683  C  CZ    . ARG A 1 207 ? 150.395 141.052 132.658 1.00 24.31 ?  207 ARG A CZ    1 
ATOM   1684  N  NH1   . ARG A 1 207 ? 150.404 140.866 133.966 1.00 28.75 1  207 ARG A NH1   1 
ATOM   1685  N  NH2   . ARG A 1 207 ? 150.406 142.291 132.177 1.00 20.66 ?  207 ARG A NH2   1 
ATOM   1686  N  N     . ALA A 1 208 ? 150.707 134.638 129.041 1.00 33.04 ?  208 ALA A N     1 
ATOM   1687  C  CA    . ALA A 1 208 ? 150.377 133.227 129.108 1.00 24.77 ?  208 ALA A CA    1 
ATOM   1688  C  C     . ALA A 1 208 ? 149.935 132.828 130.514 1.00 31.73 ?  208 ALA A C     1 
ATOM   1689  O  O     . ALA A 1 208 ? 149.955 133.622 131.458 1.00 36.14 ?  208 ALA A O     1 
ATOM   1690  C  CB    . ALA A 1 208 ? 151.571 132.386 128.665 1.00 25.67 ?  208 ALA A CB    1 
ATOM   1691  N  N     . LYS A 1 209 ? 149.515 131.573 130.640 1.00 32.25 ?  209 LYS A N     1 
ATOM   1692  C  CA    . LYS A 1 209 ? 149.114 131.036 131.931 1.00 29.35 ?  209 LYS A CA    1 
ATOM   1693  C  C     . LYS A 1 209 ? 150.320 130.914 132.853 1.00 33.86 ?  209 LYS A C     1 
ATOM   1694  O  O     . LYS A 1 209 ? 151.394 130.465 132.443 1.00 34.76 ?  209 LYS A O     1 
ATOM   1695  C  CB    . LYS A 1 209 ? 148.447 129.673 131.752 1.00 29.71 ?  209 LYS A CB    1 
ATOM   1696  C  CG    . LYS A 1 209 ? 147.520 129.277 132.885 1.00 32.21 ?  209 LYS A CG    1 
ATOM   1697  C  CD    . LYS A 1 209 ? 147.197 127.793 132.838 1.00 31.43 ?  209 LYS A CD    1 
ATOM   1698  C  CE    . LYS A 1 209 ? 148.432 126.965 132.525 1.00 35.68 ?  209 LYS A CE    1 
ATOM   1699  N  NZ    . LYS A 1 209 ? 148.079 125.586 132.086 1.00 36.68 1  209 LYS A NZ    1 
ATOM   1700  N  N     . GLY A 1 210 ? 150.135 131.316 134.108 1.00 35.89 ?  210 GLY A N     1 
ATOM   1701  C  CA    . GLY A 1 210 ? 151.219 131.277 135.066 1.00 34.31 ?  210 GLY A CA    1 
ATOM   1702  C  C     . GLY A 1 210 ? 152.116 132.490 135.067 1.00 36.82 ?  210 GLY A C     1 
ATOM   1703  O  O     . GLY A 1 210 ? 153.240 132.413 135.571 1.00 38.71 ?  210 GLY A O     1 
ATOM   1704  N  N     . GLU A 1 211 ? 151.663 133.606 134.512 1.00 37.12 ?  211 GLU A N     1 
ATOM   1705  C  CA    . GLU A 1 211 ? 152.408 134.854 134.551 1.00 33.53 ?  211 GLU A CA    1 
ATOM   1706  C  C     . GLU A 1 211 ? 151.896 135.735 135.684 1.00 36.61 ?  211 GLU A C     1 
ATOM   1707  O  O     . GLU A 1 211 ? 150.786 135.559 136.189 1.00 37.11 ?  211 GLU A O     1 
ATOM   1708  C  CB    . GLU A 1 211 ? 152.306 135.593 133.216 1.00 32.02 ?  211 GLU A CB    1 
ATOM   1709  C  CG    . GLU A 1 211 ? 152.840 134.800 132.042 1.00 32.88 ?  211 GLU A CG    1 
ATOM   1710  C  CD    . GLU A 1 211 ? 153.790 135.603 131.182 1.00 37.46 ?  211 GLU A CD    1 
ATOM   1711  O  OE1   . GLU A 1 211 ? 154.908 135.899 131.652 1.00 41.10 ?  211 GLU A OE1   1 
ATOM   1712  O  OE2   . GLU A 1 211 ? 153.428 135.926 130.032 1.00 30.94 -1 211 GLU A OE2   1 
ATOM   1713  N  N     . ALA A 1 212 ? 152.729 136.691 136.080 1.00 34.70 ?  212 ALA A N     1 
ATOM   1714  C  CA    . ALA A 1 212 ? 152.419 137.541 137.219 1.00 31.46 ?  212 ALA A CA    1 
ATOM   1715  C  C     . ALA A 1 212 ? 151.465 138.662 136.831 1.00 36.01 ?  212 ALA A C     1 
ATOM   1716  O  O     . ALA A 1 212 ? 151.528 139.200 135.722 1.00 39.23 ?  212 ALA A O     1 
ATOM   1717  C  CB    . ALA A 1 212 ? 153.701 138.132 137.805 1.00 35.89 ?  212 ALA A CB    1 
ATOM   1718  N  N     . ILE A 1 213 ? 150.574 139.006 137.753 1.00 34.91 ?  213 ILE A N     1 
ATOM   1719  C  CA    . ILE A 1 213 ? 149.715 140.182 137.632 1.00 33.44 ?  213 ILE A CA    1 
ATOM   1720  C  C     . ILE A 1 213 ? 150.088 141.102 138.787 1.00 35.43 ?  213 ILE A C     1 
ATOM   1721  O  O     . ILE A 1 213 ? 149.555 140.978 139.892 1.00 40.52 ?  213 ILE A O     1 
ATOM   1722  C  CB    . ILE A 1 213 ? 148.225 139.835 137.659 1.00 35.77 ?  213 ILE A CB    1 
ATOM   1723  C  CG1   . ILE A 1 213 ? 147.922 138.654 136.740 1.00 37.06 ?  213 ILE A CG1   1 
ATOM   1724  C  CG2   . ILE A 1 213 ? 147.394 141.041 137.265 1.00 32.96 ?  213 ILE A CG2   1 
ATOM   1725  C  CD1   . ILE A 1 213 ? 146.580 138.019 137.009 1.00 30.23 ?  213 ILE A CD1   1 
ATOM   1726  N  N     . LYS A 1 214 ? 150.995 142.046 138.533 1.00 41.20 ?  214 LYS A N     1 
ATOM   1727  C  CA    . LYS A 1 214 ? 151.490 142.975 139.549 1.00 40.66 ?  214 LYS A CA    1 
ATOM   1728  C  C     . LYS A 1 214 ? 152.148 142.215 140.705 1.00 44.42 ?  214 LYS A C     1 
ATOM   1729  O  O     . LYS A 1 214 ? 151.648 142.161 141.830 1.00 46.37 ?  214 LYS A O     1 
ATOM   1730  C  CB    . LYS A 1 214 ? 150.370 143.897 140.046 1.00 39.51 ?  214 LYS A CB    1 
ATOM   1731  C  CG    . LYS A 1 214 ? 150.538 145.348 139.634 1.00 42.74 ?  214 LYS A CG    1 
ATOM   1732  C  CD    . LYS A 1 214 ? 149.388 146.205 140.135 1.00 42.94 ?  214 LYS A CD    1 
ATOM   1733  C  CE    . LYS A 1 214 ? 149.309 147.512 139.365 1.00 45.18 ?  214 LYS A CE    1 
ATOM   1734  N  NZ    . LYS A 1 214 ? 147.946 148.108 139.411 1.00 43.21 1  214 LYS A NZ    1 
ATOM   1735  N  N     . ASP A 1 215 ? 153.265 141.575 140.358 1.00 45.21 ?  215 ASP A N     1 
ATOM   1736  C  CA    . ASP A 1 215 ? 154.242 140.958 141.257 1.00 50.42 ?  215 ASP A CA    1 
ATOM   1737  C  C     . ASP A 1 215 ? 153.680 139.812 142.096 1.00 50.21 ?  215 ASP A C     1 
ATOM   1738  O  O     . ASP A 1 215 ? 154.335 139.379 143.052 1.00 52.51 ?  215 ASP A O     1 
ATOM   1739  C  CB    . ASP A 1 215 ? 154.930 142.002 142.161 1.00 49.52 ?  215 ASP A CB    1 
ATOM   1740  C  CG    . ASP A 1 215 ? 154.040 142.514 143.285 1.00 52.69 ?  215 ASP A CG    1 
ATOM   1741  O  OD1   . ASP A 1 215 ? 153.779 141.767 144.251 1.00 51.32 ?  215 ASP A OD1   1 
ATOM   1742  O  OD2   . ASP A 1 215 ? 153.603 143.681 143.203 1.00 51.14 -1 215 ASP A OD2   1 
ATOM   1743  N  N     . VAL A 1 216 ? 152.505 139.286 141.767 1.00 43.00 ?  216 VAL A N     1 
ATOM   1744  C  CA    . VAL A 1 216 ? 152.043 138.018 142.323 1.00 45.82 ?  216 VAL A CA    1 
ATOM   1745  C  C     . VAL A 1 216 ? 152.065 136.984 141.204 1.00 47.78 ?  216 VAL A C     1 
ATOM   1746  O  O     . VAL A 1 216 ? 151.382 137.140 140.185 1.00 50.41 ?  216 VAL A O     1 
ATOM   1747  C  CB    . VAL A 1 216 ? 150.651 138.140 142.970 1.00 45.53 ?  216 VAL A CB    1 
ATOM   1748  C  CG1   . VAL A 1 216 ? 149.672 138.825 142.053 1.00 44.93 ?  216 VAL A CG1   1 
ATOM   1749  C  CG2   . VAL A 1 216 ? 150.131 136.766 143.360 1.00 45.66 ?  216 VAL A CG2   1 
ATOM   1750  N  N     . GLU A 1 217 ? 152.855 135.934 141.390 1.00 48.05 ?  217 GLU A N     1 
ATOM   1751  C  CA    . GLU A 1 217 ? 153.201 135.016 140.318 1.00 46.87 ?  217 GLU A CA    1 
ATOM   1752  C  C     . GLU A 1 217 ? 152.158 133.915 140.164 1.00 48.29 ?  217 GLU A C     1 
ATOM   1753  O  O     . GLU A 1 217 ? 151.354 133.653 141.062 1.00 49.42 ?  217 GLU A O     1 
ATOM   1754  C  CB    . GLU A 1 217 ? 154.578 134.402 140.576 1.00 48.30 ?  217 GLU A CB    1 
ATOM   1755  C  CG    . GLU A 1 217 ? 155.582 135.388 141.147 1.00 49.23 ?  217 GLU A CG    1 
ATOM   1756  C  CD    . GLU A 1 217 ? 156.456 136.014 140.079 1.00 51.51 ?  217 GLU A CD    1 
ATOM   1757  O  OE1   . GLU A 1 217 ? 156.946 135.274 139.200 1.00 53.39 ?  217 GLU A OE1   1 
ATOM   1758  O  OE2   . GLU A 1 217 ? 156.649 137.247 140.116 1.00 49.38 -1 217 GLU A OE2   1 
ATOM   1759  N  N     . ASN A 1 218 ? 152.189 133.267 138.996 1.00 45.48 ?  218 ASN A N     1 
ATOM   1760  C  CA    . ASN A 1 218 ? 151.262 132.188 138.656 1.00 43.90 ?  218 ASN A CA    1 
ATOM   1761  C  C     . ASN A 1 218 ? 149.814 132.634 138.828 1.00 47.78 ?  218 ASN A C     1 
ATOM   1762  O  O     . ASN A 1 218 ? 148.951 131.876 139.276 1.00 49.11 ?  218 ASN A O     1 
ATOM   1763  C  CB    . ASN A 1 218 ? 151.552 130.932 139.479 1.00 45.70 ?  218 ASN A CB    1 
ATOM   1764  C  CG    . ASN A 1 218 ? 152.724 130.142 138.937 1.00 48.95 ?  218 ASN A CG    1 
ATOM   1765  O  OD1   . ASN A 1 218 ? 152.559 129.279 138.076 1.00 48.93 ?  218 ASN A OD1   1 
ATOM   1766  N  ND2   . ASN A 1 218 ? 153.919 130.439 139.434 1.00 46.74 ?  218 ASN A ND2   1 
ATOM   1767  N  N     . ALA A 1 219 ? 149.545 133.885 138.464 1.00 40.88 ?  219 ALA A N     1 
ATOM   1768  C  CA    . ALA A 1 219 ? 148.243 134.495 138.685 1.00 38.59 ?  219 ALA A CA    1 
ATOM   1769  C  C     . ALA A 1 219 ? 147.384 134.560 137.433 1.00 40.39 ?  219 ALA A C     1 
ATOM   1770  O  O     . ALA A 1 219 ? 146.155 134.510 137.537 1.00 41.10 ?  219 ALA A O     1 
ATOM   1771  C  CB    . ALA A 1 219 ? 148.420 135.907 139.249 1.00 37.28 ?  219 ALA A CB    1 
ATOM   1772  N  N     . THR A 1 220 ? 147.997 134.666 136.258 1.00 37.47 ?  220 THR A N     1 
ATOM   1773  C  CA    . THR A 1 220 ? 147.246 134.821 135.023 1.00 34.68 ?  220 THR A CA    1 
ATOM   1774  C  C     . THR A 1 220 ? 146.683 133.477 134.578 1.00 35.72 ?  220 THR A C     1 
ATOM   1775  O  O     . THR A 1 220 ? 147.367 132.451 134.632 1.00 37.02 ?  220 THR A O     1 
ATOM   1776  C  CB    . THR A 1 220 ? 148.144 135.416 133.935 1.00 33.58 ?  220 THR A CB    1 
ATOM   1777  O  OG1   . THR A 1 220 ? 148.406 136.791 134.234 1.00 36.06 ?  220 THR A OG1   1 
ATOM   1778  C  CG2   . THR A 1 220 ? 147.468 135.351 132.584 1.00 35.48 ?  220 THR A CG2   1 
ATOM   1779  N  N     . LYS A 1 221 ? 145.423 133.486 134.142 1.00 37.24 ?  221 LYS A N     1 
ATOM   1780  C  CA    . LYS A 1 221 ? 144.760 132.277 133.671 1.00 32.88 ?  221 LYS A CA    1 
ATOM   1781  C  C     . LYS A 1 221 ? 145.103 131.936 132.229 1.00 38.04 ?  221 LYS A C     1 
ATOM   1782  O  O     . LYS A 1 221 ? 144.644 130.904 131.727 1.00 43.49 ?  221 LYS A O     1 
ATOM   1783  C  CB    . LYS A 1 221 ? 143.243 132.416 133.810 1.00 33.02 ?  221 LYS A CB    1 
ATOM   1784  C  CG    . LYS A 1 221 ? 142.789 133.036 135.113 1.00 37.07 ?  221 LYS A CG    1 
ATOM   1785  C  CD    . LYS A 1 221 ? 141.293 132.868 135.299 1.00 36.66 ?  221 LYS A CD    1 
ATOM   1786  C  CE    . LYS A 1 221 ? 140.944 131.475 135.784 1.00 35.69 ?  221 LYS A CE    1 
ATOM   1787  N  NZ    . LYS A 1 221 ? 141.752 131.082 136.968 1.00 37.36 1  221 LYS A NZ    1 
ATOM   1788  N  N     . GLY A 1 222 ? 145.885 132.769 131.556 1.00 32.91 ?  222 GLY A N     1 
ATOM   1789  C  CA    . GLY A 1 222 ? 146.263 132.514 130.187 1.00 30.90 ?  222 GLY A CA    1 
ATOM   1790  C  C     . GLY A 1 222 ? 145.216 132.980 129.196 1.00 30.75 ?  222 GLY A C     1 
ATOM   1791  O  O     . GLY A 1 222 ? 144.229 133.639 129.536 1.00 31.07 ?  222 GLY A O     1 
ATOM   1792  N  N     . VAL A 1 223 ? 145.447 132.621 127.934 1.00 31.96 ?  223 VAL A N     1 
ATOM   1793  C  CA    . VAL A 1 223 ? 144.519 133.007 126.879 1.00 26.30 ?  223 VAL A CA    1 
ATOM   1794  C  C     . VAL A 1 223 ? 143.259 132.157 126.881 1.00 22.89 ?  223 VAL A C     1 
ATOM   1795  O  O     . VAL A 1 223 ? 142.268 132.542 126.257 1.00 31.06 ?  223 VAL A O     1 
ATOM   1796  C  CB    . VAL A 1 223 ? 145.185 132.940 125.493 1.00 25.90 ?  223 VAL A CB    1 
ATOM   1797  C  CG1   . VAL A 1 223 ? 146.519 133.662 125.508 1.00 25.11 ?  223 VAL A CG1   1 
ATOM   1798  C  CG2   . VAL A 1 223 ? 145.352 131.498 125.043 1.00 26.84 ?  223 VAL A CG2   1 
ATOM   1799  N  N     . VAL A 1 224 ? 143.264 131.011 127.564 1.00 25.50 ?  224 VAL A N     1 
ATOM   1800  C  CA    . VAL A 1 224 ? 142.088 130.145 127.563 1.00 25.72 ?  224 VAL A CA    1 
ATOM   1801  C  C     . VAL A 1 224 ? 140.962 130.730 128.414 1.00 27.40 ?  224 VAL A C     1 
ATOM   1802  O  O     . VAL A 1 224 ? 139.783 130.550 128.094 1.00 30.19 ?  224 VAL A O     1 
ATOM   1803  C  CB    . VAL A 1 224 ? 142.475 128.729 128.019 1.00 32.71 ?  224 VAL A CB    1 
ATOM   1804  C  CG1   . VAL A 1 224 ? 141.260 127.818 128.038 1.00 31.81 ?  224 VAL A CG1   1 
ATOM   1805  C  CG2   . VAL A 1 224 ? 143.540 128.163 127.099 1.00 29.46 ?  224 VAL A CG2   1 
ATOM   1806  N  N     . GLY A 1 225 ? 141.288 131.439 129.495 1.00 24.18 ?  225 GLY A N     1 
ATOM   1807  C  CA    . GLY A 1 225 ? 140.251 132.120 130.252 1.00 21.73 ?  225 GLY A CA    1 
ATOM   1808  C  C     . GLY A 1 225 ? 139.576 133.218 129.453 1.00 22.30 ?  225 GLY A C     1 
ATOM   1809  O  O     . GLY A 1 225 ? 138.346 133.348 129.465 1.00 31.46 ?  225 GLY A O     1 
ATOM   1810  N  N     . VAL A 1 226 ? 140.370 134.015 128.736 1.00 19.34 ?  226 VAL A N     1 
ATOM   1811  C  CA    . VAL A 1 226 ? 139.809 135.012 127.831 1.00 20.35 ?  226 VAL A CA    1 
ATOM   1812  C  C     . VAL A 1 226 ? 139.028 134.336 126.718 1.00 24.85 ?  226 VAL A C     1 
ATOM   1813  O  O     . VAL A 1 226 ? 138.024 134.870 126.238 1.00 26.82 ?  226 VAL A O     1 
ATOM   1814  C  CB    . VAL A 1 226 ? 140.930 135.910 127.275 1.00 18.19 ?  226 VAL A CB    1 
ATOM   1815  C  CG1   . VAL A 1 226 ? 140.344 137.065 126.477 1.00 25.76 ?  226 VAL A CG1   1 
ATOM   1816  C  CG2   . VAL A 1 226 ? 141.799 136.419 128.405 1.00 20.82 ?  226 VAL A CG2   1 
ATOM   1817  N  N     . MET A 1 227 ? 139.476 133.158 126.286 1.00 28.39 ?  227 MET A N     1 
ATOM   1818  C  CA    . MET A 1 227 ? 138.755 132.403 125.268 1.00 22.22 ?  227 MET A CA    1 
ATOM   1819  C  C     . MET A 1 227 ? 137.377 131.990 125.762 1.00 22.95 ?  227 MET A C     1 
ATOM   1820  O  O     . MET A 1 227 ? 136.396 132.074 125.022 1.00 29.97 ?  227 MET A O     1 
ATOM   1821  C  CB    . MET A 1 227 ? 139.574 131.177 124.869 1.00 19.68 ?  227 MET A CB    1 
ATOM   1822  C  CG    . MET A 1 227 ? 140.631 131.450 123.821 1.00 17.85 ?  227 MET A CG    1 
ATOM   1823  S  SD    . MET A 1 227 ? 141.299 129.935 123.121 1.00 33.28 ?  227 MET A SD    1 
ATOM   1824  C  CE    . MET A 1 227 ? 139.989 129.487 122.000 1.00 29.81 ?  227 MET A CE    1 
ATOM   1825  N  N     . LYS A 1 228 ? 137.288 131.533 127.013 1.00 26.79 ?  228 LYS A N     1 
ATOM   1826  C  CA    . LYS A 1 228 ? 135.991 131.187 127.590 1.00 23.10 ?  228 LYS A CA    1 
ATOM   1827  C  C     . LYS A 1 228 ? 135.104 132.418 127.730 1.00 24.38 ?  228 LYS A C     1 
ATOM   1828  O  O     . LYS A 1 228 ? 133.898 132.363 127.445 1.00 26.05 ?  228 LYS A O     1 
ATOM   1829  C  CB    . LYS A 1 228 ? 136.180 130.510 128.946 1.00 23.32 ?  228 LYS A CB    1 
ATOM   1830  C  CG    . LYS A 1 228 ? 136.960 129.210 128.888 1.00 29.04 ?  228 LYS A CG    1 
ATOM   1831  C  CD    . LYS A 1 228 ? 137.036 128.555 130.255 1.00 36.78 ?  228 LYS A CD    1 
ATOM   1832  C  CE    . LYS A 1 228 ? 138.175 129.127 131.084 1.00 36.15 ?  228 LYS A CE    1 
ATOM   1833  N  NZ    . LYS A 1 228 ? 139.334 128.196 131.157 1.00 30.76 1  228 LYS A NZ    1 
ATOM   1834  N  N     . LEU A 1 229 ? 135.686 133.536 128.172 1.00 24.46 ?  229 LEU A N     1 
ATOM   1835  C  CA    . LEU A 1 229 ? 134.933 134.784 128.253 1.00 21.84 ?  229 LEU A CA    1 
ATOM   1836  C  C     . LEU A 1 229 ? 134.362 135.168 126.894 1.00 21.51 ?  229 LEU A C     1 
ATOM   1837  O  O     . LEU A 1 229 ? 133.182 135.513 126.776 1.00 22.24 ?  229 LEU A O     1 
ATOM   1838  C  CB    . LEU A 1 229 ? 135.828 135.903 128.781 1.00 24.43 ?  229 LEU A CB    1 
ATOM   1839  C  CG    . LEU A 1 229 ? 136.221 135.923 130.256 1.00 23.02 ?  229 LEU A CG    1 
ATOM   1840  C  CD1   . LEU A 1 229 ? 137.364 136.896 130.444 1.00 24.40 ?  229 LEU A CD1   1 
ATOM   1841  C  CD2   . LEU A 1 229 ? 135.041 136.307 131.126 1.00 18.49 ?  229 LEU A CD2   1 
ATOM   1842  N  N     . LEU A 1 230 ? 135.193 135.109 125.853 1.00 26.92 ?  230 LEU A N     1 
ATOM   1843  C  CA    . LEU A 1 230 ? 134.753 135.475 124.511 1.00 18.66 ?  230 LEU A CA    1 
ATOM   1844  C  C     . LEU A 1 230 ? 133.724 134.490 123.977 1.00 17.88 ?  230 LEU A C     1 
ATOM   1845  O  O     . LEU A 1 230 ? 132.781 134.885 123.283 1.00 29.69 ?  230 LEU A O     1 
ATOM   1846  C  CB    . LEU A 1 230 ? 135.953 135.557 123.572 1.00 20.57 ?  230 LEU A CB    1 
ATOM   1847  C  CG    . LEU A 1 230 ? 136.864 136.768 123.760 1.00 27.78 ?  230 LEU A CG    1 
ATOM   1848  C  CD1   . LEU A 1 230 ? 138.197 136.544 123.068 1.00 28.12 ?  230 LEU A CD1   1 
ATOM   1849  C  CD2   . LEU A 1 230 ? 136.186 138.027 123.245 1.00 21.05 ?  230 LEU A CD2   1 
ATOM   1850  N  N     . ASP A 1 231 ? 133.891 133.203 124.279 1.00 20.37 ?  231 ASP A N     1 
ATOM   1851  C  CA    . ASP A 1 231 ? 132.931 132.205 123.829 1.00 24.19 ?  231 ASP A CA    1 
ATOM   1852  C  C     . ASP A 1 231 ? 131.558 132.458 124.433 1.00 28.73 ?  231 ASP A C     1 
ATOM   1853  O  O     . ASP A 1 231 ? 130.541 132.391 123.733 1.00 33.36 ?  231 ASP A O     1 
ATOM   1854  C  CB    . ASP A 1 231 ? 133.434 130.807 124.184 1.00 27.44 ?  231 ASP A CB    1 
ATOM   1855  C  CG    . ASP A 1 231 ? 132.482 129.716 123.748 1.00 35.91 ?  231 ASP A CG    1 
ATOM   1856  O  OD1   . ASP A 1 231 ? 132.326 129.515 122.526 1.00 39.62 ?  231 ASP A OD1   1 
ATOM   1857  O  OD2   . ASP A 1 231 ? 131.892 129.055 124.626 1.00 38.47 -1 231 ASP A OD2   1 
ATOM   1858  N  N     . ASN A 1 232 ? 131.505 132.778 125.728 1.00 29.49 ?  232 ASN A N     1 
ATOM   1859  C  CA    . ASN A 1 232 ? 130.213 133.097 126.330 1.00 27.94 ?  232 ASN A CA    1 
ATOM   1860  C  C     . ASN A 1 232 ? 129.674 134.438 125.852 1.00 28.52 ?  232 ASN A C     1 
ATOM   1861  O  O     . ASN A 1 232 ? 128.454 134.607 125.745 1.00 33.99 ?  232 ASN A O     1 
ATOM   1862  C  CB    . ASN A 1 232 ? 130.310 133.069 127.850 1.00 29.32 ?  232 ASN A CB    1 
ATOM   1863  C  CG    . ASN A 1 232 ? 130.166 131.675 128.404 1.00 36.30 ?  232 ASN A CG    1 
ATOM   1864  O  OD1   . ASN A 1 232 ? 131.054 130.838 128.250 1.00 38.87 ?  232 ASN A OD1   1 
ATOM   1865  N  ND2   . ASN A 1 232 ? 129.035 131.411 129.048 1.00 33.39 ?  232 ASN A ND2   1 
ATOM   1866  N  N     . ALA A 1 233 ? 130.553 135.397 125.557 1.00 25.87 ?  233 ALA A N     1 
ATOM   1867  C  CA    . ALA A 1 233 ? 130.097 136.667 125.006 1.00 17.88 ?  233 ALA A CA    1 
ATOM   1868  C  C     . ALA A 1 233 ? 129.461 136.473 123.636 1.00 30.07 ?  233 ALA A C     1 
ATOM   1869  O  O     . ALA A 1 233 ? 128.470 137.132 123.302 1.00 36.37 ?  233 ALA A O     1 
ATOM   1870  C  CB    . ALA A 1 233 ? 131.262 137.651 124.926 1.00 23.66 ?  233 ALA A CB    1 
ATOM   1871  N  N     . PHE A 1 234 ? 130.023 135.576 122.825 1.00 32.09 ?  234 PHE A N     1 
ATOM   1872  C  CA    . PHE A 1 234 ? 129.460 135.295 121.511 1.00 25.48 ?  234 PHE A CA    1 
ATOM   1873  C  C     . PHE A 1 234 ? 128.209 134.433 121.600 1.00 23.30 ?  234 PHE A C     1 
ATOM   1874  O  O     . PHE A 1 234 ? 127.309 134.571 120.765 1.00 29.86 ?  234 PHE A O     1 
ATOM   1875  C  CB    . PHE A 1 234 ? 130.511 134.631 120.624 1.00 24.96 ?  234 PHE A CB    1 
ATOM   1876  C  CG    . PHE A 1 234 ? 131.526 135.591 120.074 1.00 24.03 ?  234 PHE A CG    1 
ATOM   1877  C  CD1   . PHE A 1 234 ? 131.130 136.675 119.312 1.00 27.38 ?  234 PHE A CD1   1 
ATOM   1878  C  CD2   . PHE A 1 234 ? 132.873 135.420 120.331 1.00 23.01 ?  234 PHE A CD2   1 
ATOM   1879  C  CE1   . PHE A 1 234 ? 132.059 137.563 118.812 1.00 26.14 ?  234 PHE A CE1   1 
ATOM   1880  C  CE2   . PHE A 1 234 ? 133.805 136.307 119.839 1.00 24.47 ?  234 PHE A CE2   1 
ATOM   1881  C  CZ    . PHE A 1 234 ? 133.398 137.378 119.077 1.00 26.41 ?  234 PHE A CZ    1 
ATOM   1882  N  N     . ARG A 1 235 ? 128.132 133.541 122.587 1.00 31.26 ?  235 ARG A N     1 
ATOM   1883  C  CA    . ARG A 1 235 ? 126.884 132.822 122.822 1.00 26.90 ?  235 ARG A CA    1 
ATOM   1884  C  C     . ARG A 1 235 ? 125.770 133.759 123.260 1.00 32.93 ?  235 ARG A C     1 
ATOM   1885  O  O     . ARG A 1 235 ? 124.611 133.559 122.883 1.00 39.75 ?  235 ARG A O     1 
ATOM   1886  C  CB    . ARG A 1 235 ? 127.084 131.721 123.861 1.00 23.83 ?  235 ARG A CB    1 
ATOM   1887  C  CG    . ARG A 1 235 ? 126.981 130.324 123.288 1.00 35.16 ?  235 ARG A CG    1 
ATOM   1888  C  CD    . ARG A 1 235 ? 126.671 129.293 124.367 1.00 37.47 ?  235 ARG A CD    1 
ATOM   1889  N  NE    . ARG A 1 235 ? 127.582 129.339 125.507 1.00 36.06 ?  235 ARG A NE    1 
ATOM   1890  C  CZ    . ARG A 1 235 ? 128.895 129.160 125.440 1.00 36.85 ?  235 ARG A CZ    1 
ATOM   1891  N  NH1   . ARG A 1 235 ? 129.499 128.867 124.300 1.00 35.35 1  235 ARG A NH1   1 
ATOM   1892  N  NH2   . ARG A 1 235 ? 129.619 129.256 126.551 1.00 33.99 ?  235 ARG A NH2   1 
ATOM   1893  N  N     . TYR A 1 236 ? 126.092 134.776 124.061 1.00 29.33 ?  236 TYR A N     1 
ATOM   1894  C  CA    . TYR A 1 236 ? 125.066 135.709 124.510 1.00 27.39 ?  236 TYR A CA    1 
ATOM   1895  C  C     . TYR A 1 236 ? 124.550 136.559 123.356 1.00 26.88 ?  236 TYR A C     1 
ATOM   1896  O  O     . TYR A 1 236 ? 123.337 136.703 123.171 1.00 32.69 ?  236 TYR A O     1 
ATOM   1897  C  CB    . TYR A 1 236 ? 125.612 136.597 125.625 1.00 28.09 ?  236 TYR A CB    1 
ATOM   1898  C  CG    . TYR A 1 236 ? 124.575 137.527 126.199 1.00 29.84 ?  236 TYR A CG    1 
ATOM   1899  C  CD1   . TYR A 1 236 ? 123.563 137.041 127.013 1.00 26.03 ?  236 TYR A CD1   1 
ATOM   1900  C  CD2   . TYR A 1 236 ? 124.594 138.885 125.914 1.00 29.81 ?  236 TYR A CD2   1 
ATOM   1901  C  CE1   . TYR A 1 236 ? 122.610 137.878 127.534 1.00 30.09 ?  236 TYR A CE1   1 
ATOM   1902  C  CE2   . TYR A 1 236 ? 123.641 139.732 126.435 1.00 23.27 ?  236 TYR A CE2   1 
ATOM   1903  C  CZ    . TYR A 1 236 ? 122.652 139.220 127.246 1.00 24.22 ?  236 TYR A CZ    1 
ATOM   1904  O  OH    . TYR A 1 236 ? 121.694 140.048 127.774 1.00 29.49 ?  236 TYR A OH    1 
ATOM   1905  N  N     . ALA A 1 237 ? 125.458 137.134 122.568 1.00 30.76 ?  237 ALA A N     1 
ATOM   1906  C  CA    . ALA A 1 237 ? 125.079 137.980 121.436 1.00 33.92 ?  237 ALA A CA    1 
ATOM   1907  C  C     . ALA A 1 237 ? 124.942 137.092 120.203 1.00 38.01 ?  237 ALA A C     1 
ATOM   1908  O  O     . ALA A 1 237 ? 125.871 136.912 119.413 1.00 37.56 ?  237 ALA A O     1 
ATOM   1909  C  CB    . ALA A 1 237 ? 126.096 139.094 121.231 1.00 31.93 ?  237 ALA A CB    1 
ATOM   1910  N  N     . ASP A 1 238 ? 123.749 136.524 120.046 1.00 54.09 ?  238 ASP A N     1 
ATOM   1911  C  CA    . ASP A 1 238 ? 123.479 135.559 118.990 1.00 57.14 ?  238 ASP A CA    1 
ATOM   1912  C  C     . ASP A 1 238 ? 122.367 135.989 118.042 1.00 59.65 ?  238 ASP A C     1 
ATOM   1913  O  O     . ASP A 1 238 ? 122.063 135.248 117.102 1.00 62.01 ?  238 ASP A O     1 
ATOM   1914  C  CB    . ASP A 1 238 ? 123.132 134.199 119.603 1.00 56.12 ?  238 ASP A CB    1 
ATOM   1915  C  CG    . ASP A 1 238 ? 121.910 134.258 120.495 1.00 59.17 ?  238 ASP A CG    1 
ATOM   1916  O  OD1   . ASP A 1 238 ? 121.554 135.364 120.949 1.00 58.79 ?  238 ASP A OD1   1 
ATOM   1917  O  OD2   . ASP A 1 238 ? 121.303 133.194 120.742 1.00 61.73 -1 238 ASP A OD2   1 
ATOM   1918  N  N     . GLN A 1 239 ? 121.753 137.154 118.262 1.00 61.84 ?  239 GLN A N     1 
ATOM   1919  C  CA    . GLN A 1 239 ? 120.731 137.706 117.370 1.00 63.57 ?  239 GLN A CA    1 
ATOM   1920  C  C     . GLN A 1 239 ? 119.577 136.714 117.184 1.00 64.40 ?  239 GLN A C     1 
ATOM   1921  O  O     . GLN A 1 239 ? 119.373 136.149 116.107 1.00 64.50 ?  239 GLN A O     1 
ATOM   1922  C  CB    . GLN A 1 239 ? 121.332 138.090 116.012 1.00 62.58 ?  239 GLN A CB    1 
ATOM   1923  C  CG    . GLN A 1 239 ? 122.721 138.694 116.074 1.00 60.47 ?  239 GLN A CG    1 
ATOM   1924  C  CD    . GLN A 1 239 ? 123.465 138.522 114.767 1.00 63.61 ?  239 GLN A CD    1 
ATOM   1925  O  OE1   . GLN A 1 239 ? 124.623 138.104 114.746 1.00 63.04 ?  239 GLN A OE1   1 
ATOM   1926  N  NE2   . GLN A 1 239 ? 122.800 138.842 113.664 1.00 62.96 ?  239 GLN A NE2   1 
ATOM   1927  N  N     . MET A 1 240 ? 118.863 136.480 118.292 1.00 72.88 ?  240 MET A N     1 
ATOM   1928  C  CA    . MET A 1 240 ? 117.732 135.554 118.353 1.00 74.86 ?  240 MET A CA    1 
ATOM   1929  C  C     . MET A 1 240 ? 118.181 134.098 118.285 1.00 74.66 ?  240 MET A C     1 
ATOM   1930  O  O     . MET A 1 240 ? 117.373 133.184 118.482 1.00 76.79 ?  240 MET A O     1 
ATOM   1931  C  CB    . MET A 1 240 ? 116.726 135.833 117.227 1.00 75.37 ?  240 MET A CB    1 
ATOM   1932  C  CG    . MET A 1 240 ? 115.345 135.235 117.441 1.00 74.25 ?  240 MET A CG    1 
ATOM   1933  S  SD    . MET A 1 240 ? 113.975 136.358 117.147 1.00 82.10 ?  240 MET A SD    1 
ATOM   1934  C  CE    . MET A 1 240 ? 112.603 135.213 117.281 1.00 74.95 ?  240 MET A CE    1 
ATOM   1935  N  N     . GLY A 1 241 ? 119.464 133.866 118.032 1.00 73.27 ?  241 GLY A N     1 
ATOM   1936  C  CA    . GLY A 1 241 ? 119.940 132.529 117.765 1.00 72.70 ?  241 GLY A CA    1 
ATOM   1937  C  C     . GLY A 1 241 ? 119.719 132.057 116.345 1.00 75.66 ?  241 GLY A C     1 
ATOM   1938  O  O     . GLY A 1 241 ? 120.117 130.932 116.017 1.00 74.83 ?  241 GLY A O     1 
ATOM   1939  N  N     . GLN A 1 242 ? 119.087 132.876 115.498 1.00 79.13 ?  242 GLN A N     1 
ATOM   1940  C  CA    . GLN A 1 242 ? 118.929 132.519 114.092 1.00 78.63 ?  242 GLN A CA    1 
ATOM   1941  C  C     . GLN A 1 242 ? 120.287 132.311 113.437 1.00 80.35 ?  242 GLN A C     1 
ATOM   1942  O  O     . GLN A 1 242 ? 120.510 131.319 112.735 1.00 79.65 ?  242 GLN A O     1 
ATOM   1943  C  CB    . GLN A 1 242 ? 118.144 133.611 113.362 1.00 77.99 ?  242 GLN A CB    1 
ATOM   1944  C  CG    . GLN A 1 242 ? 116.637 133.540 113.543 1.00 79.49 ?  242 GLN A CG    1 
ATOM   1945  C  CD    . GLN A 1 242 ? 115.893 134.417 112.555 1.00 79.66 ?  242 GLN A CD    1 
ATOM   1946  O  OE1   . GLN A 1 242 ? 116.502 135.065 111.703 1.00 78.67 ?  242 GLN A OE1   1 
ATOM   1947  N  NE2   . GLN A 1 242 ? 114.570 134.445 112.666 1.00 79.18 ?  242 GLN A NE2   1 
ATOM   1948  N  N     . ARG A 1 243 ? 121.209 133.244 113.665 1.00 67.57 ?  243 ARG A N     1 
ATOM   1949  C  CA    . ARG A 1 243 ? 122.618 133.076 113.333 1.00 64.53 ?  243 ARG A CA    1 
ATOM   1950  C  C     . ARG A 1 243 ? 123.403 133.379 114.600 1.00 65.13 ?  243 ARG A C     1 
ATOM   1951  O  O     . ARG A 1 243 ? 123.634 134.549 114.924 1.00 64.19 ?  243 ARG A O     1 
ATOM   1952  C  CB    . ARG A 1 243 ? 123.043 133.998 112.190 1.00 63.99 ?  243 ARG A CB    1 
ATOM   1953  C  CG    . ARG A 1 243 ? 124.452 133.736 111.684 1.00 65.11 ?  243 ARG A CG    1 
ATOM   1954  C  CD    . ARG A 1 243 ? 125.250 135.025 111.575 1.00 63.87 ?  243 ARG A CD    1 
ATOM   1955  N  NE    . ARG A 1 243 ? 125.579 135.567 112.888 1.00 65.64 ?  243 ARG A NE    1 
ATOM   1956  C  CZ    . ARG A 1 243 ? 126.658 136.292 113.152 1.00 62.31 ?  243 ARG A CZ    1 
ATOM   1957  N  NH1   . ARG A 1 243 ? 127.545 136.577 112.213 1.00 61.32 1  243 ARG A NH1   1 
ATOM   1958  N  NH2   . ARG A 1 243 ? 126.851 136.740 114.389 1.00 59.64 ?  243 ARG A NH2   1 
ATOM   1959  N  N     . GLN A 1 244 ? 123.803 132.329 115.316 1.00 62.49 ?  244 GLN A N     1 
ATOM   1960  C  CA    . GLN A 1 244 ? 124.467 132.508 116.599 1.00 60.92 ?  244 GLN A CA    1 
ATOM   1961  C  C     . GLN A 1 244 ? 125.775 133.269 116.426 1.00 61.50 ?  244 GLN A C     1 
ATOM   1962  O  O     . GLN A 1 244 ? 126.381 133.276 115.350 1.00 59.07 ?  244 GLN A O     1 
ATOM   1963  C  CB    . GLN A 1 244 ? 124.727 131.152 117.261 1.00 59.61 ?  244 GLN A CB    1 
ATOM   1964  C  CG    . GLN A 1 244 ? 125.975 130.436 116.770 1.00 61.35 ?  244 GLN A CG    1 
ATOM   1965  C  CD    . GLN A 1 244 ? 125.852 129.959 115.337 1.00 63.43 ?  244 GLN A CD    1 
ATOM   1966  O  OE1   . GLN A 1 244 ? 124.749 129.744 114.834 1.00 62.60 ?  244 GLN A OE1   1 
ATOM   1967  N  NE2   . GLN A 1 244 ? 126.988 129.793 114.668 1.00 60.79 ?  244 GLN A NE2   1 
ATOM   1968  N  N     . GLY A 1 245 ? 126.197 133.936 117.499 1.00 51.77 ?  245 GLY A N     1 
ATOM   1969  C  CA    . GLY A 1 245 ? 127.405 134.735 117.465 1.00 44.75 ?  245 GLY A CA    1 
ATOM   1970  C  C     . GLY A 1 245 ? 128.627 133.927 117.091 1.00 44.79 ?  245 GLY A C     1 
ATOM   1971  O  O     . GLY A 1 245 ? 128.931 132.911 117.724 1.00 45.23 ?  245 GLY A O     1 
ATOM   1972  N  N     . SER A 1 246 ? 129.333 134.368 116.056 1.00 39.42 ?  246 SER A N     1 
ATOM   1973  C  CA    . SER A 1 246 ? 130.500 133.669 115.541 1.00 34.17 ?  246 SER A CA    1 
ATOM   1974  C  C     . SER A 1 246 ? 131.745 134.489 115.833 1.00 31.18 ?  246 SER A C     1 
ATOM   1975  O  O     . SER A 1 246 ? 131.833 135.658 115.442 1.00 27.05 ?  246 SER A O     1 
ATOM   1976  C  CB    . SER A 1 246 ? 130.369 133.418 114.039 1.00 31.85 ?  246 SER A CB    1 
ATOM   1977  O  OG    . SER A 1 246 ? 129.362 132.460 113.768 1.00 41.80 ?  246 SER A OG    1 
ATOM   1978  N  N     . GLY A 1 247 ? 132.704 133.874 116.520 1.00 24.77 ?  247 GLY A N     1 
ATOM   1979  C  CA    . GLY A 1 247 ? 133.951 134.529 116.827 1.00 11.06 ?  247 GLY A CA    1 
ATOM   1980  C  C     . GLY A 1 247 ? 135.127 133.654 116.443 1.00 15.76 ?  247 GLY A C     1 
ATOM   1981  O  O     . GLY A 1 247 ? 135.012 132.437 116.311 1.00 22.75 ?  247 GLY A O     1 
ATOM   1982  N  N     . ALA A 1 248 ? 136.266 134.308 116.251 1.00 19.37 ?  248 ALA A N     1 
ATOM   1983  C  CA    . ALA A 1 248 ? 137.522 133.631 115.983 1.00 16.42 ?  248 ALA A CA    1 
ATOM   1984  C  C     . ALA A 1 248 ? 138.591 134.194 116.902 1.00 12.25 ?  248 ALA A C     1 
ATOM   1985  O  O     . ALA A 1 248 ? 138.631 135.400 117.157 1.00 20.81 ?  248 ALA A O     1 
ATOM   1986  C  CB    . ALA A 1 248 ? 137.950 133.784 114.520 1.00 9.18  ?  248 ALA A CB    1 
ATOM   1987  N  N     . ALA A 1 249 ? 139.447 133.316 117.406 1.00 17.17 ?  249 ALA A N     1 
ATOM   1988  C  CA    . ALA A 1 249 ? 140.594 133.707 118.207 1.00 11.41 ?  249 ALA A CA    1 
ATOM   1989  C  C     . ALA A 1 249 ? 141.862 133.285 117.484 1.00 10.22 ?  249 ALA A C     1 
ATOM   1990  O  O     . ALA A 1 249 ? 141.927 132.194 116.915 1.00 19.58 ?  249 ALA A O     1 
ATOM   1991  C  CB    . ALA A 1 249 ? 140.545 133.081 119.602 1.00 13.14 ?  249 ALA A CB    1 
ATOM   1992  N  N     . TYR A 1 250 ? 142.862 134.155 117.497 1.00 11.19 ?  250 TYR A N     1 
ATOM   1993  C  CA    . TYR A 1 250 ? 144.132 133.874 116.850 1.00 7.84  ?  250 TYR A CA    1 
ATOM   1994  C  C     . TYR A 1 250 ? 145.252 133.949 117.872 1.00 8.84  ?  250 TYR A C     1 
ATOM   1995  O  O     . TYR A 1 250 ? 145.281 134.850 118.715 1.00 13.20 ?  250 TYR A O     1 
ATOM   1996  C  CB    . TYR A 1 250 ? 144.399 134.847 115.701 1.00 10.59 ?  250 TYR A CB    1 
ATOM   1997  C  CG    . TYR A 1 250 ? 143.755 134.435 114.398 1.00 19.08 ?  250 TYR A CG    1 
ATOM   1998  C  CD1   . TYR A 1 250 ? 142.403 134.646 114.173 1.00 8.70  ?  250 TYR A CD1   1 
ATOM   1999  C  CD2   . TYR A 1 250 ? 144.497 133.820 113.398 1.00 12.91 ?  250 TYR A CD2   1 
ATOM   2000  C  CE1   . TYR A 1 250 ? 141.811 134.267 112.991 1.00 0.00  ?  250 TYR A CE1   1 
ATOM   2001  C  CE2   . TYR A 1 250 ? 143.911 133.438 112.210 1.00 7.59  ?  250 TYR A CE2   1 
ATOM   2002  C  CZ    . TYR A 1 250 ? 142.567 133.663 112.013 1.00 7.54  ?  250 TYR A CZ    1 
ATOM   2003  O  OH    . TYR A 1 250 ? 141.972 133.287 110.833 1.00 22.46 ?  250 TYR A OH    1 
ATOM   2004  N  N     . LEU A 1 251 ? 146.167 132.991 117.795 1.00 10.93 ?  251 LEU A N     1 
ATOM   2005  C  CA    . LEU A 1 251 ? 147.330 132.946 118.664 1.00 12.86 ?  251 LEU A CA    1 
ATOM   2006  C  C     . LEU A 1 251 ? 148.568 132.657 117.837 1.00 11.61 ?  251 LEU A C     1 
ATOM   2007  O  O     . LEU A 1 251 ? 148.551 131.790 116.958 1.00 17.27 ?  251 LEU A O     1 
ATOM   2008  C  CB    . LEU A 1 251 ? 147.173 131.882 119.752 1.00 18.54 ?  251 LEU A CB    1 
ATOM   2009  C  CG    . LEU A 1 251 ? 147.942 132.159 121.042 1.00 14.33 ?  251 LEU A CG    1 
ATOM   2010  C  CD1   . LEU A 1 251 ? 147.225 133.205 121.867 1.00 16.35 ?  251 LEU A CD1   1 
ATOM   2011  C  CD2   . LEU A 1 251 ? 148.127 130.885 121.834 1.00 13.33 ?  251 LEU A CD2   1 
ATOM   2012  N  N     . ASN A 1 252 ? 149.638 133.394 118.112 1.00 12.05 ?  252 ASN A N     1 
ATOM   2013  C  CA    . ASN A 1 252 ? 150.923 133.093 117.501 1.00 12.86 ?  252 ASN A CA    1 
ATOM   2014  C  C     . ASN A 1 252 ? 151.429 131.748 118.004 1.00 17.68 ?  252 ASN A C     1 
ATOM   2015  O  O     . ASN A 1 252 ? 151.263 131.402 119.175 1.00 23.42 ?  252 ASN A O     1 
ATOM   2016  C  CB    . ASN A 1 252 ? 151.931 134.197 117.811 1.00 15.86 ?  252 ASN A CB    1 
ATOM   2017  C  CG    . ASN A 1 252 ? 153.177 134.106 116.957 1.00 20.25 ?  252 ASN A CG    1 
ATOM   2018  O  OD1   . ASN A 1 252 ? 154.142 133.437 117.320 1.00 25.80 ?  252 ASN A OD1   1 
ATOM   2019  N  ND2   . ASN A 1 252 ? 153.160 134.775 115.813 1.00 15.68 ?  252 ASN A ND2   1 
ATOM   2020  N  N     . ILE A 1 253 ? 152.047 130.981 117.102 1.00 15.99 ?  253 ILE A N     1 
ATOM   2021  C  CA    . ILE A 1 253 ? 152.502 129.641 117.451 1.00 14.48 ?  253 ILE A CA    1 
ATOM   2022  C  C     . ILE A 1 253 ? 153.598 129.671 118.509 1.00 19.81 ?  253 ILE A C     1 
ATOM   2023  O  O     . ILE A 1 253 ? 153.835 128.659 119.178 1.00 23.62 ?  253 ILE A O     1 
ATOM   2024  C  CB    . ILE A 1 253 ? 152.965 128.898 116.182 1.00 17.64 ?  253 ILE A CB    1 
ATOM   2025  C  CG1   . ILE A 1 253 ? 153.018 127.390 116.431 1.00 19.79 ?  253 ILE A CG1   1 
ATOM   2026  C  CG2   . ILE A 1 253 ? 154.313 129.421 115.710 1.00 14.47 ?  253 ILE A CG2   1 
ATOM   2027  C  CD1   . ILE A 1 253 ? 152.489 126.566 115.287 1.00 16.32 ?  253 ILE A CD1   1 
ATOM   2028  N  N     . PHE A 1 254 ? 154.266 130.807 118.689 1.00 23.04 ?  254 PHE A N     1 
ATOM   2029  C  CA    . PHE A 1 254 ? 155.314 130.946 119.690 1.00 20.04 ?  254 PHE A CA    1 
ATOM   2030  C  C     . PHE A 1 254 ? 154.788 131.433 121.032 1.00 19.83 ?  254 PHE A C     1 
ATOM   2031  O  O     . PHE A 1 254 ? 155.579 131.626 121.960 1.00 29.11 ?  254 PHE A O     1 
ATOM   2032  C  CB    . PHE A 1 254 ? 156.403 131.891 119.179 1.00 23.31 ?  254 PHE A CB    1 
ATOM   2033  C  CG    . PHE A 1 254 ? 157.354 131.246 118.216 1.00 23.76 ?  254 PHE A CG    1 
ATOM   2034  C  CD1   . PHE A 1 254 ? 158.215 130.250 118.638 1.00 25.73 ?  254 PHE A CD1   1 
ATOM   2035  C  CD2   . PHE A 1 254 ? 157.377 131.624 116.886 1.00 24.41 ?  254 PHE A CD2   1 
ATOM   2036  C  CE1   . PHE A 1 254 ? 159.089 129.650 117.754 1.00 24.63 ?  254 PHE A CE1   1 
ATOM   2037  C  CE2   . PHE A 1 254 ? 158.249 131.027 115.998 1.00 28.73 ?  254 PHE A CE2   1 
ATOM   2038  C  CZ    . PHE A 1 254 ? 159.107 130.039 116.434 1.00 26.32 ?  254 PHE A CZ    1 
ATOM   2039  N  N     . HIS A 1 255 ? 153.483 131.648 121.152 1.00 22.21 ?  255 HIS A N     1 
ATOM   2040  C  CA    . HIS A 1 255 ? 152.875 131.909 122.447 1.00 22.02 ?  255 HIS A CA    1 
ATOM   2041  C  C     . HIS A 1 255 ? 152.966 130.660 123.314 1.00 23.79 ?  255 HIS A C     1 
ATOM   2042  O  O     . HIS A 1 255 ? 152.823 129.537 122.828 1.00 27.87 ?  255 HIS A O     1 
ATOM   2043  C  CB    . HIS A 1 255 ? 151.415 132.324 122.264 1.00 23.90 ?  255 HIS A CB    1 
ATOM   2044  C  CG    . HIS A 1 255 ? 150.836 133.059 123.433 1.00 19.97 ?  255 HIS A CG    1 
ATOM   2045  N  ND1   . HIS A 1 255 ? 150.464 132.428 124.600 1.00 16.34 ?  255 HIS A ND1   1 
ATOM   2046  C  CD2   . HIS A 1 255 ? 150.535 134.368 123.601 1.00 17.37 ?  255 HIS A CD2   1 
ATOM   2047  C  CE1   . HIS A 1 255 ? 149.977 133.320 125.444 1.00 17.98 ?  255 HIS A CE1   1 
ATOM   2048  N  NE2   . HIS A 1 255 ? 150.007 134.504 124.861 1.00 17.01 ?  255 HIS A NE2   1 
ATOM   2049  N  N     . ARG A 1 256 ? 153.219 130.859 124.609 1.00 23.57 ?  256 ARG A N     1 
ATOM   2050  C  CA    . ARG A 1 256 ? 153.344 129.721 125.514 1.00 26.08 ?  256 ARG A CA    1 
ATOM   2051  C  C     . ARG A 1 256 ? 152.040 128.942 125.626 1.00 25.39 ?  256 ARG A C     1 
ATOM   2052  O  O     . ARG A 1 256 ? 152.059 127.718 125.792 1.00 31.14 ?  256 ARG A O     1 
ATOM   2053  C  CB    . ARG A 1 256 ? 153.797 130.195 126.892 1.00 28.03 ?  256 ARG A CB    1 
ATOM   2054  C  CG    . ARG A 1 256 ? 154.057 129.069 127.869 1.00 29.43 ?  256 ARG A CG    1 
ATOM   2055  C  CD    . ARG A 1 256 ? 153.140 129.155 129.074 1.00 29.65 ?  256 ARG A CD    1 
ATOM   2056  N  NE    . ARG A 1 256 ? 151.870 128.474 128.859 1.00 31.35 ?  256 ARG A NE    1 
ATOM   2057  C  CZ    . ARG A 1 256 ? 151.621 127.226 129.225 1.00 34.72 ?  256 ARG A CZ    1 
ATOM   2058  N  NH1   . ARG A 1 256 ? 152.539 126.486 129.825 1.00 33.44 1  256 ARG A NH1   1 
ATOM   2059  N  NH2   . ARG A 1 256 ? 150.421 126.705 128.982 1.00 30.56 ?  256 ARG A NH2   1 
ATOM   2060  N  N     . ASP A 1 257 ? 150.904 129.626 125.527 1.00 23.03 ?  257 ASP A N     1 
ATOM   2061  C  CA    . ASP A 1 257 ? 149.595 129.002 125.652 1.00 19.77 ?  257 ASP A CA    1 
ATOM   2062  C  C     . ASP A 1 257 ? 149.140 128.302 124.381 1.00 23.50 ?  257 ASP A C     1 
ATOM   2063  O  O     . ASP A 1 257 ? 147.950 127.989 124.274 1.00 29.98 ?  257 ASP A O     1 
ATOM   2064  C  CB    . ASP A 1 257 ? 148.549 130.045 126.050 1.00 25.21 ?  257 ASP A CB    1 
ATOM   2065  C  CG    . ASP A 1 257 ? 148.665 130.468 127.494 1.00 31.90 ?  257 ASP A CG    1 
ATOM   2066  O  OD1   . ASP A 1 257 ? 149.387 129.798 128.262 1.00 32.69 ?  257 ASP A OD1   1 
ATOM   2067  O  OD2   . ASP A 1 257 ? 148.028 131.471 127.862 1.00 32.98 -1 257 ASP A OD2   1 
ATOM   2068  N  N     . ILE A 1 258 ? 150.036 128.047 123.427 1.00 24.69 ?  258 ILE A N     1 
ATOM   2069  C  CA    . ILE A 1 258 ? 149.610 127.518 122.134 1.00 21.61 ?  258 ILE A CA    1 
ATOM   2070  C  C     . ILE A 1 258 ? 149.016 126.123 122.287 1.00 20.20 ?  258 ILE A C     1 
ATOM   2071  O  O     . ILE A 1 258 ? 148.030 125.781 121.625 1.00 27.04 ?  258 ILE A O     1 
ATOM   2072  C  CB    . ILE A 1 258 ? 150.778 127.543 121.128 1.00 24.23 ?  258 ILE A CB    1 
ATOM   2073  C  CG1   . ILE A 1 258 ? 150.301 127.100 119.742 1.00 22.62 ?  258 ILE A CG1   1 
ATOM   2074  C  CG2   . ILE A 1 258 ? 151.947 126.691 121.607 1.00 17.77 ?  258 ILE A CG2   1 
ATOM   2075  C  CD1   . ILE A 1 258 ? 149.284 128.029 119.120 1.00 17.72 ?  258 ILE A CD1   1 
ATOM   2076  N  N     . ASN A 1 259 ? 149.592 125.298 123.164 1.00 31.20 ?  259 ASN A N     1 
ATOM   2077  C  CA    . ASN A 1 259 ? 149.073 123.947 123.345 1.00 25.53 ?  259 ASN A CA    1 
ATOM   2078  C  C     . ASN A 1 259 ? 147.714 123.963 124.033 1.00 29.96 ?  259 ASN A C     1 
ATOM   2079  O  O     . ASN A 1 259 ? 146.809 123.218 123.644 1.00 34.90 ?  259 ASN A O     1 
ATOM   2080  C  CB    . ASN A 1 259 ? 150.075 123.107 124.132 1.00 30.04 ?  259 ASN A CB    1 
ATOM   2081  C  CG    . ASN A 1 259 ? 151.361 122.875 123.369 1.00 34.90 ?  259 ASN A CG    1 
ATOM   2082  O  OD1   . ASN A 1 259 ? 151.373 122.200 122.342 1.00 34.38 ?  259 ASN A OD1   1 
ATOM   2083  N  ND2   . ASN A 1 259 ? 152.455 123.439 123.866 1.00 36.03 ?  259 ASN A ND2   1 
ATOM   2084  N  N     . ASP A 1 260 ? 147.549 124.805 125.056 1.00 29.27 ?  260 ASP A N     1 
ATOM   2085  C  CA    . ASP A 1 260 ? 146.236 124.965 125.669 1.00 25.18 ?  260 ASP A CA    1 
ATOM   2086  C  C     . ASP A 1 260 ? 145.257 125.635 124.716 1.00 26.78 ?  260 ASP A C     1 
ATOM   2087  O  O     . ASP A 1 260 ? 144.057 125.342 124.752 1.00 35.48 ?  260 ASP A O     1 
ATOM   2088  C  CB    . ASP A 1 260 ? 146.350 125.772 126.962 1.00 27.48 ?  260 ASP A CB    1 
ATOM   2089  C  CG    . ASP A 1 260 ? 147.487 125.299 127.845 1.00 39.93 ?  260 ASP A CG    1 
ATOM   2090  O  OD1   . ASP A 1 260 ? 147.632 124.073 128.027 1.00 37.41 ?  260 ASP A OD1   1 
ATOM   2091  O  OD2   . ASP A 1 260 ? 148.239 126.157 128.355 1.00 39.68 -1 260 ASP A OD2   1 
ATOM   2092  N  N     . PHE A 1 261 ? 145.750 126.544 123.871 1.00 31.54 ?  261 PHE A N     1 
ATOM   2093  C  CA    . PHE A 1 261 ? 144.909 127.170 122.857 1.00 22.38 ?  261 PHE A CA    1 
ATOM   2094  C  C     . PHE A 1 261 ? 144.364 126.130 121.888 1.00 21.58 ?  261 PHE A C     1 
ATOM   2095  O  O     . PHE A 1 261 ? 143.189 126.180 121.506 1.00 24.08 ?  261 PHE A O     1 
ATOM   2096  C  CB    . PHE A 1 261 ? 145.723 128.238 122.122 1.00 15.65 ?  261 PHE A CB    1 
ATOM   2097  C  CG    . PHE A 1 261 ? 144.996 128.911 120.995 1.00 22.10 ?  261 PHE A CG    1 
ATOM   2098  C  CD1   . PHE A 1 261 ? 144.154 129.979 121.241 1.00 20.48 ?  261 PHE A CD1   1 
ATOM   2099  C  CD2   . PHE A 1 261 ? 145.194 128.510 119.686 1.00 24.42 ?  261 PHE A CD2   1 
ATOM   2100  C  CE1   . PHE A 1 261 ? 143.498 130.613 120.208 1.00 14.82 ?  261 PHE A CE1   1 
ATOM   2101  C  CE2   . PHE A 1 261 ? 144.540 129.141 118.650 1.00 20.16 ?  261 PHE A CE2   1 
ATOM   2102  C  CZ    . PHE A 1 261 ? 143.694 130.195 118.913 1.00 14.38 ?  261 PHE A CZ    1 
ATOM   2103  N  N     . LEU A 1 262 ? 145.204 125.176 121.483 1.00 26.28 ?  262 LEU A N     1 
ATOM   2104  C  CA    . LEU A 1 262 ? 144.769 124.111 120.588 1.00 22.74 ?  262 LEU A CA    1 
ATOM   2105  C  C     . LEU A 1 262 ? 143.926 123.063 121.301 1.00 30.54 ?  262 LEU A C     1 
ATOM   2106  O  O     . LEU A 1 262 ? 143.061 122.442 120.674 1.00 34.37 ?  262 LEU A O     1 
ATOM   2107  C  CB    . LEU A 1 262 ? 145.981 123.444 119.938 1.00 26.69 ?  262 LEU A CB    1 
ATOM   2108  C  CG    . LEU A 1 262 ? 146.848 124.335 119.052 1.00 23.46 ?  262 LEU A CG    1 
ATOM   2109  C  CD1   . LEU A 1 262 ? 148.102 123.593 118.635 1.00 24.29 ?  262 LEU A CD1   1 
ATOM   2110  C  CD2   . LEU A 1 262 ? 146.069 124.810 117.842 1.00 22.16 ?  262 LEU A CD2   1 
ATOM   2111  N  N     . ASP A 1 263 ? 144.158 122.845 122.597 1.00 38.57 ?  263 ASP A N     1 
ATOM   2112  C  CA    . ASP A 1 263 ? 143.400 121.847 123.341 1.00 30.89 ?  263 ASP A CA    1 
ATOM   2113  C  C     . ASP A 1 263 ? 141.944 122.238 123.546 1.00 32.35 ?  263 ASP A C     1 
ATOM   2114  O  O     . ASP A 1 263 ? 141.146 121.387 123.952 1.00 41.94 ?  263 ASP A O     1 
ATOM   2115  C  CB    . ASP A 1 263 ? 144.054 121.584 124.697 1.00 33.94 ?  263 ASP A CB    1 
ATOM   2116  C  CG    . ASP A 1 263 ? 145.341 120.795 124.582 1.00 40.92 ?  263 ASP A CG    1 
ATOM   2117  O  OD1   . ASP A 1 263 ? 145.570 120.183 123.518 1.00 37.88 ?  263 ASP A OD1   1 
ATOM   2118  O  OD2   . ASP A 1 263 ? 146.123 120.788 125.555 1.00 42.51 -1 263 ASP A OD2   1 
ATOM   2119  N  N     . THR A 1 264 ? 141.578 123.494 123.289 1.00 37.53 ?  264 THR A N     1 
ATOM   2120  C  CA    . THR A 1 264 ? 140.183 123.902 123.372 1.00 36.65 ?  264 THR A CA    1 
ATOM   2121  C  C     . THR A 1 264 ? 139.332 123.313 122.256 1.00 38.27 ?  264 THR A C     1 
ATOM   2122  O  O     . THR A 1 264 ? 138.102 123.360 122.349 1.00 42.43 ?  264 THR A O     1 
ATOM   2123  C  CB    . THR A 1 264 ? 140.075 125.429 123.345 1.00 37.79 ?  264 THR A CB    1 
ATOM   2124  O  OG1   . THR A 1 264 ? 140.628 125.929 122.122 1.00 41.67 ?  264 THR A OG1   1 
ATOM   2125  C  CG2   . THR A 1 264 ? 140.825 126.037 124.518 1.00 33.19 ?  264 THR A CG2   1 
ATOM   2126  N  N     . LYS A 1 265 ? 139.951 122.761 121.214 1.00 34.74 ?  265 LYS A N     1 
ATOM   2127  C  CA    . LYS A 1 265 ? 139.231 122.184 120.089 1.00 38.69 ?  265 LYS A CA    1 
ATOM   2128  C  C     . LYS A 1 265 ? 139.286 120.664 120.057 1.00 38.10 ?  265 LYS A C     1 
ATOM   2129  O  O     . LYS A 1 265 ? 138.672 120.057 119.173 1.00 42.13 ?  265 LYS A O     1 
ATOM   2130  C  CB    . LYS A 1 265 ? 139.773 122.744 118.771 1.00 37.22 ?  265 LYS A CB    1 
ATOM   2131  C  CG    . LYS A 1 265 ? 139.257 124.125 118.433 1.00 37.99 ?  265 LYS A CG    1 
ATOM   2132  C  CD    . LYS A 1 265 ? 137.772 124.232 118.700 1.00 38.69 ?  265 LYS A CD    1 
ATOM   2133  C  CE    . LYS A 1 265 ? 137.242 125.581 118.279 1.00 36.61 ?  265 LYS A CE    1 
ATOM   2134  N  NZ    . LYS A 1 265 ? 135.865 125.812 118.789 1.00 42.06 1  265 LYS A NZ    1 
ATOM   2135  N  N     . LYS A 1 266 ? 140.002 120.036 120.983 1.00 40.85 ?  266 LYS A N     1 
ATOM   2136  C  CA    . LYS A 1 266 ? 140.034 118.583 121.036 1.00 45.78 ?  266 LYS A CA    1 
ATOM   2137  C  C     . LYS A 1 266 ? 138.665 118.035 121.419 1.00 51.25 ?  266 LYS A C     1 
ATOM   2138  O  O     . LYS A 1 266 ? 137.921 118.638 122.197 1.00 51.79 ?  266 LYS A O     1 
ATOM   2139  C  CB    . LYS A 1 266 ? 141.091 118.105 122.030 1.00 44.22 ?  266 LYS A CB    1 
ATOM   2140  C  CG    . LYS A 1 266 ? 142.503 118.102 121.473 1.00 46.23 ?  266 LYS A CG    1 
ATOM   2141  C  CD    . LYS A 1 266 ? 143.504 117.594 122.495 1.00 48.71 ?  266 LYS A CD    1 
ATOM   2142  C  CE    . LYS A 1 266 ? 144.851 117.314 121.850 1.00 49.28 ?  266 LYS A CE    1 
ATOM   2143  N  NZ    . LYS A 1 266 ? 145.940 117.185 122.858 1.00 47.87 1  266 LYS A NZ    1 
ATOM   2144  N  N     . ILE A 1 267 ? 138.329 116.878 120.848 1.00 54.28 ?  267 ILE A N     1 
ATOM   2145  C  CA    . ILE A 1 267 ? 137.041 116.253 121.133 1.00 55.14 ?  267 ILE A CA    1 
ATOM   2146  C  C     . ILE A 1 267 ? 136.958 115.836 122.596 1.00 57.07 ?  267 ILE A C     1 
ATOM   2147  O  O     . ILE A 1 267 ? 135.888 115.901 123.213 1.00 54.69 ?  267 ILE A O     1 
ATOM   2148  C  CB    . ILE A 1 267 ? 136.805 115.066 120.182 1.00 55.54 ?  267 ILE A CB    1 
ATOM   2149  C  CG1   . ILE A 1 267 ? 138.077 114.223 120.055 1.00 57.04 ?  267 ILE A CG1   1 
ATOM   2150  C  CG2   . ILE A 1 267 ? 136.343 115.557 118.821 1.00 55.23 ?  267 ILE A CG2   1 
ATOM   2151  C  CD1   . ILE A 1 267 ? 137.914 112.997 119.189 1.00 55.54 ?  267 ILE A CD1   1 
ATOM   2152  N  N     . SER A 1 268 ? 138.078 115.408 123.174 1.00 60.16 ?  268 SER A N     1 
ATOM   2153  C  CA    . SER A 1 268 ? 138.136 114.991 124.569 1.00 61.20 ?  268 SER A CA    1 
ATOM   2154  C  C     . SER A 1 268 ? 138.335 116.156 125.535 1.00 63.52 ?  268 SER A C     1 
ATOM   2155  O  O     . SER A 1 268 ? 138.732 115.928 126.684 1.00 63.03 ?  268 SER A O     1 
ATOM   2156  C  CB    . SER A 1 268 ? 139.251 113.961 124.761 1.00 63.43 ?  268 SER A CB    1 
ATOM   2157  O  OG    . SER A 1 268 ? 140.491 114.460 124.289 1.00 62.04 ?  268 SER A OG    1 
ATOM   2158  N  N     . ALA A 1 269 ? 138.075 117.388 125.105 1.00 67.34 ?  269 ALA A N     1 
ATOM   2159  C  CA    . ALA A 1 269 ? 138.269 118.538 125.978 1.00 66.38 ?  269 ALA A CA    1 
ATOM   2160  C  C     . ALA A 1 269 ? 137.148 118.632 127.005 1.00 67.63 ?  269 ALA A C     1 
ATOM   2161  O  O     . ALA A 1 269 ? 135.986 118.338 126.713 1.00 65.73 ?  269 ALA A O     1 
ATOM   2162  C  CB    . ALA A 1 269 ? 138.338 119.825 125.155 1.00 63.69 ?  269 ALA A CB    1 
ATOM   2163  N  N     . ASP A 1 270 ? 137.507 119.048 128.217 1.00 75.07 ?  270 ASP A N     1 
ATOM   2164  C  CA    . ASP A 1 270 ? 136.531 119.189 129.285 1.00 75.00 ?  270 ASP A CA    1 
ATOM   2165  C  C     . ASP A 1 270 ? 135.683 120.442 129.078 1.00 74.74 ?  270 ASP A C     1 
ATOM   2166  O  O     . ASP A 1 270 ? 136.043 121.356 128.331 1.00 75.33 ?  270 ASP A O     1 
ATOM   2167  C  CB    . ASP A 1 270 ? 137.231 119.244 130.644 1.00 75.61 ?  270 ASP A CB    1 
ATOM   2168  C  CG    . ASP A 1 270 ? 136.319 118.845 131.788 1.00 77.85 ?  270 ASP A CG    1 
ATOM   2169  O  OD1   . ASP A 1 270 ? 135.298 119.531 132.006 1.00 77.52 ?  270 ASP A OD1   1 
ATOM   2170  O  OD2   . ASP A 1 270 ? 136.622 117.843 132.470 1.00 76.02 -1 270 ASP A OD2   1 
ATOM   2171  N  N     . GLU A 1 271 ? 134.535 120.472 129.758 1.00 75.70 ?  271 GLU A N     1 
ATOM   2172  C  CA    . GLU A 1 271 ? 133.622 121.603 129.639 1.00 76.74 ?  271 GLU A CA    1 
ATOM   2173  C  C     . GLU A 1 271 ? 134.201 122.887 130.220 1.00 76.23 ?  271 GLU A C     1 
ATOM   2174  O  O     . GLU A 1 271 ? 133.744 123.976 129.857 1.00 75.27 ?  271 GLU A O     1 
ATOM   2175  C  CB    . GLU A 1 271 ? 132.292 121.277 130.318 1.00 75.14 ?  271 GLU A CB    1 
ATOM   2176  C  CG    . GLU A 1 271 ? 131.555 120.101 129.700 1.00 75.56 ?  271 GLU A CG    1 
ATOM   2177  C  CD    . GLU A 1 271 ? 131.153 120.359 128.261 1.00 76.58 ?  271 GLU A CD    1 
ATOM   2178  O  OE1   . GLU A 1 271 ? 130.733 121.495 127.953 1.00 76.79 ?  271 GLU A OE1   1 
ATOM   2179  O  OE2   . GLU A 1 271 ? 131.260 119.427 127.436 1.00 75.92 -1 271 GLU A OE2   1 
ATOM   2180  N  N     . ASP A 1 272 ? 135.188 122.788 131.109 1.00 74.59 ?  272 ASP A N     1 
ATOM   2181  C  CA    . ASP A 1 272 ? 135.825 123.967 131.681 1.00 75.23 ?  272 ASP A CA    1 
ATOM   2182  C  C     . ASP A 1 272 ? 136.942 124.519 130.806 1.00 73.89 ?  272 ASP A C     1 
ATOM   2183  O  O     . ASP A 1 272 ? 137.550 125.532 131.172 1.00 71.80 ?  272 ASP A O     1 
ATOM   2184  C  CB    . ASP A 1 272 ? 136.377 123.646 133.072 1.00 74.63 ?  272 ASP A CB    1 
ATOM   2185  C  CG    . ASP A 1 272 ? 135.318 123.731 134.155 1.00 76.48 ?  272 ASP A CG    1 
ATOM   2186  O  OD1   . ASP A 1 272 ? 134.243 124.311 133.894 1.00 76.29 ?  272 ASP A OD1   1 
ATOM   2187  O  OD2   . ASP A 1 272 ? 135.565 123.221 135.268 1.00 74.73 -1 272 ASP A OD2   1 
ATOM   2188  N  N     . VAL A 1 273 ? 137.234 123.878 129.674 1.00 64.46 ?  273 VAL A N     1 
ATOM   2189  C  CA    . VAL A 1 273 ? 138.284 124.306 128.760 1.00 63.69 ?  273 VAL A CA    1 
ATOM   2190  C  C     . VAL A 1 273 ? 137.744 124.522 127.351 1.00 61.79 ?  273 VAL A C     1 
ATOM   2191  O  O     . VAL A 1 273 ? 138.058 125.521 126.697 1.00 62.73 ?  273 VAL A O     1 
ATOM   2192  C  CB    . VAL A 1 273 ? 139.461 123.303 128.746 1.00 64.13 ?  273 VAL A CB    1 
ATOM   2193  C  CG1   . VAL A 1 273 ? 140.373 123.558 127.557 1.00 60.73 ?  273 VAL A CG1   1 
ATOM   2194  C  CG2   . VAL A 1 273 ? 140.238 123.380 130.049 1.00 62.17 ?  273 VAL A CG2   1 
ATOM   2195  N  N     . ARG A 1 274 ? 136.918 123.594 126.870 1.00 58.79 ?  274 ARG A N     1 
ATOM   2196  C  CA    . ARG A 1 274 ? 136.478 123.614 125.481 1.00 56.27 ?  274 ARG A CA    1 
ATOM   2197  C  C     . ARG A 1 274 ? 135.635 124.847 125.179 1.00 56.31 ?  274 ARG A C     1 
ATOM   2198  O  O     . ARG A 1 274 ? 134.775 125.245 125.971 1.00 59.27 ?  274 ARG A O     1 
ATOM   2199  C  CB    . ARG A 1 274 ? 135.686 122.343 125.168 1.00 58.56 ?  274 ARG A CB    1 
ATOM   2200  C  CG    . ARG A 1 274 ? 134.522 122.542 124.211 1.00 56.98 ?  274 ARG A CG    1 
ATOM   2201  C  CD    . ARG A 1 274 ? 133.954 121.210 123.738 1.00 57.29 ?  274 ARG A CD    1 
ATOM   2202  N  NE    . ARG A 1 274 ? 134.845 120.490 122.833 1.00 60.77 ?  274 ARG A NE    1 
ATOM   2203  C  CZ    . ARG A 1 274 ? 135.281 120.944 121.664 1.00 60.46 ?  274 ARG A CZ    1 
ATOM   2204  N  NH1   . ARG A 1 274 ? 134.893 122.113 121.181 1.00 59.29 1  274 ARG A NH1   1 
ATOM   2205  N  NH2   . ARG A 1 274 ? 136.117 120.194 120.951 1.00 56.10 ?  274 ARG A NH2   1 
ATOM   2206  N  N     . VAL A 1 275 ? 135.895 125.454 124.024 1.00 47.22 ?  275 VAL A N     1 
ATOM   2207  C  CA    . VAL A 1 275 ? 135.091 126.545 123.489 1.00 47.42 ?  275 VAL A CA    1 
ATOM   2208  C  C     . VAL A 1 275 ? 134.381 126.035 122.243 1.00 47.78 ?  275 VAL A C     1 
ATOM   2209  O  O     . VAL A 1 275 ? 134.969 125.304 121.438 1.00 49.68 ?  275 VAL A O     1 
ATOM   2210  C  CB    . VAL A 1 275 ? 135.943 127.790 123.173 1.00 45.57 ?  275 VAL A CB    1 
ATOM   2211  C  CG1   . VAL A 1 275 ? 136.451 128.422 124.457 1.00 42.16 ?  275 VAL A CG1   1 
ATOM   2212  C  CG2   . VAL A 1 275 ? 137.103 127.427 122.266 1.00 46.32 ?  275 VAL A CG2   1 
ATOM   2213  N  N     . LYS A 1 276 ? 133.112 126.400 122.097 1.00 47.35 ?  276 LYS A N     1 
ATOM   2214  C  CA    . LYS A 1 276 ? 132.269 125.862 121.036 1.00 48.92 ?  276 LYS A CA    1 
ATOM   2215  C  C     . LYS A 1 276 ? 131.945 126.865 119.941 1.00 45.86 ?  276 LYS A C     1 
ATOM   2216  O  O     . LYS A 1 276 ? 131.962 126.506 118.761 1.00 51.39 ?  276 LYS A O     1 
ATOM   2217  C  CB    . LYS A 1 276 ? 130.963 125.326 121.635 1.00 49.48 ?  276 LYS A CB    1 
ATOM   2218  C  CG    . LYS A 1 276 ? 131.172 124.159 122.588 1.00 50.86 ?  276 LYS A CG    1 
ATOM   2219  C  CD    . LYS A 1 276 ? 129.879 123.740 123.265 1.00 51.93 ?  276 LYS A CD    1 
ATOM   2220  C  CE    . LYS A 1 276 ? 130.115 122.573 124.211 1.00 52.38 ?  276 LYS A CE    1 
ATOM   2221  N  NZ    . LYS A 1 276 ? 128.964 122.355 125.131 1.00 54.84 1  276 LYS A NZ    1 
ATOM   2222  N  N     . THR A 1 277 ? 131.652 128.114 120.293 1.00 37.03 ?  277 THR A N     1 
ATOM   2223  C  CA    . THR A 1 277 ? 131.279 129.135 119.326 1.00 38.81 ?  277 THR A CA    1 
ATOM   2224  C  C     . THR A 1 277 ? 132.469 129.948 118.835 1.00 40.67 ?  277 THR A C     1 
ATOM   2225  O  O     . THR A 1 277 ? 132.282 130.908 118.081 1.00 39.52 ?  277 THR A O     1 
ATOM   2226  C  CB    . THR A 1 277 ? 130.229 130.072 119.927 1.00 39.99 ?  277 THR A CB    1 
ATOM   2227  O  OG1   . THR A 1 277 ? 130.883 131.147 120.614 1.00 38.24 ?  277 THR A OG1   1 
ATOM   2228  C  CG2   . THR A 1 277 ? 129.352 129.316 120.902 1.00 38.90 ?  277 THR A CG2   1 
ATOM   2229  N  N     . LEU A 1 278 ? 133.683 129.588 119.241 1.00 36.61 ?  278 LEU A N     1 
ATOM   2230  C  CA    . LEU A 1 278 ? 134.879 130.365 118.937 1.00 30.45 ?  278 LEU A CA    1 
ATOM   2231  C  C     . LEU A 1 278 ? 135.785 129.546 118.028 1.00 24.23 ?  278 LEU A C     1 
ATOM   2232  O  O     . LEU A 1 278 ? 136.368 128.550 118.464 1.00 32.43 ?  278 LEU A O     1 
ATOM   2233  C  CB    . LEU A 1 278 ? 135.609 130.762 120.220 1.00 30.01 ?  278 LEU A CB    1 
ATOM   2234  C  CG    . LEU A 1 278 ? 136.502 131.999 120.155 1.00 28.95 ?  278 LEU A CG    1 
ATOM   2235  C  CD1   . LEU A 1 278 ? 135.669 133.261 120.069 1.00 23.64 ?  278 LEU A CD1   1 
ATOM   2236  C  CD2   . LEU A 1 278 ? 137.415 132.049 121.363 1.00 26.19 ?  278 LEU A CD2   1 
ATOM   2237  N  N     . SER A 1 279 ? 135.900 129.967 116.772 1.00 24.49 ?  279 SER A N     1 
ATOM   2238  C  CA    . SER A 1 279 ? 136.906 129.406 115.886 1.00 15.83 ?  279 SER A CA    1 
ATOM   2239  C  C     . SER A 1 279 ? 138.292 129.833 116.352 1.00 17.60 ?  279 SER A C     1 
ATOM   2240  O  O     . SER A 1 279 ? 138.458 130.828 117.060 1.00 28.53 ?  279 SER A O     1 
ATOM   2241  C  CB    . SER A 1 279 ? 136.671 129.860 114.446 1.00 18.86 ?  279 SER A CB    1 
ATOM   2242  O  OG    . SER A 1 279 ? 135.370 129.519 114.006 1.00 26.41 ?  279 SER A OG    1 
ATOM   2243  N  N     . ILE A 1 280 ? 139.300 129.061 115.962 1.00 15.31 ?  280 ILE A N     1 
ATOM   2244  C  CA    . ILE A 1 280 ? 140.668 129.325 116.384 1.00 16.70 ?  280 ILE A CA    1 
ATOM   2245  C  C     . ILE A 1 280 ? 141.574 129.350 115.163 1.00 15.46 ?  280 ILE A C     1 
ATOM   2246  O  O     . ILE A 1 280 ? 141.393 128.570 114.223 1.00 20.73 ?  280 ILE A O     1 
ATOM   2247  C  CB    . ILE A 1 280 ? 141.166 128.296 117.422 1.00 17.82 ?  280 ILE A CB    1 
ATOM   2248  C  CG1   . ILE A 1 280 ? 141.163 126.878 116.855 1.00 23.63 ?  280 ILE A CG1   1 
ATOM   2249  C  CG2   . ILE A 1 280 ? 140.323 128.359 118.675 1.00 18.85 ?  280 ILE A CG2   1 
ATOM   2250  C  CD1   . ILE A 1 280 ? 142.152 125.965 117.538 1.00 18.27 ?  280 ILE A CD1   1 
ATOM   2251  N  N     . GLY A 1 281 ? 142.525 130.273 115.169 1.00 9.44  ?  281 GLY A N     1 
ATOM   2252  C  CA    . GLY A 1 281 ? 143.549 130.318 114.148 1.00 4.46  ?  281 GLY A CA    1 
ATOM   2253  C  C     . GLY A 1 281 ? 144.917 130.413 114.787 1.00 11.28 ?  281 GLY A C     1 
ATOM   2254  O  O     . GLY A 1 281 ? 145.081 130.953 115.879 1.00 21.39 ?  281 GLY A O     1 
ATOM   2255  N  N     . VAL A 1 282 ? 145.907 129.866 114.090 1.00 18.47 ?  282 VAL A N     1 
ATOM   2256  C  CA    . VAL A 1 282 ? 147.286 129.861 114.558 1.00 16.31 ?  282 VAL A CA    1 
ATOM   2257  C  C     . VAL A 1 282 ? 148.137 130.616 113.550 1.00 14.87 ?  282 VAL A C     1 
ATOM   2258  O  O     . VAL A 1 282 ? 148.105 130.317 112.352 1.00 19.62 ?  282 VAL A O     1 
ATOM   2259  C  CB    . VAL A 1 282 ? 147.818 128.431 114.764 1.00 12.54 ?  282 VAL A CB    1 
ATOM   2260  C  CG1   . VAL A 1 282 ? 149.319 128.448 114.965 1.00 19.43 ?  282 VAL A CG1   1 
ATOM   2261  C  CG2   . VAL A 1 282 ? 147.145 127.796 115.959 1.00 20.97 ?  282 VAL A CG2   1 
ATOM   2262  N  N     . VAL A 1 283 ? 148.891 131.595 114.038 1.00 12.30 ?  283 VAL A N     1 
ATOM   2263  C  CA    . VAL A 1 283 ? 149.786 132.390 113.211 1.00 8.37  ?  283 VAL A CA    1 
ATOM   2264  C  C     . VAL A 1 283 ? 151.172 131.770 113.300 1.00 13.12 ?  283 VAL A C     1 
ATOM   2265  O  O     . VAL A 1 283 ? 151.750 131.674 114.389 1.00 25.22 ?  283 VAL A O     1 
ATOM   2266  C  CB    . VAL A 1 283 ? 149.797 133.858 113.658 1.00 9.54  ?  283 VAL A CB    1 
ATOM   2267  C  CG1   . VAL A 1 283 ? 150.562 134.712 112.668 1.00 12.39 ?  283 VAL A CG1   1 
ATOM   2268  C  CG2   . VAL A 1 283 ? 148.376 134.357 113.817 1.00 9.73  ?  283 VAL A CG2   1 
ATOM   2269  N  N     . ILE A 1 284 ? 151.703 131.343 112.159 1.00 15.63 ?  284 ILE A N     1 
ATOM   2270  C  CA    . ILE A 1 284 ? 152.973 130.623 112.125 1.00 15.39 ?  284 ILE A CA    1 
ATOM   2271  C  C     . ILE A 1 284 ? 154.016 131.441 111.374 1.00 21.61 ?  284 ILE A C     1 
ATOM   2272  O  O     . ILE A 1 284 ? 153.937 131.568 110.144 1.00 21.50 ?  284 ILE A O     1 
ATOM   2273  C  CB    . ILE A 1 284 ? 152.806 129.234 111.493 1.00 15.46 ?  284 ILE A CB    1 
ATOM   2274  C  CG1   . ILE A 1 284 ? 151.647 128.486 112.152 1.00 12.76 ?  284 ILE A CG1   1 
ATOM   2275  C  CG2   . ILE A 1 284 ? 154.093 128.440 111.614 1.00 16.89 ?  284 ILE A CG2   1 
ATOM   2276  C  CD1   . ILE A 1 284 ? 151.459 127.081 111.641 1.00 16.53 ?  284 ILE A CD1   1 
ATOM   2277  N  N     . PRO A 1 285 ? 154.998 132.014 112.063 1.00 25.53 ?  285 PRO A N     1 
ATOM   2278  C  CA    . PRO A 1 285 ? 156.107 132.664 111.362 1.00 25.30 ?  285 PRO A CA    1 
ATOM   2279  C  C     . PRO A 1 285 ? 156.997 131.643 110.670 1.00 25.79 ?  285 PRO A C     1 
ATOM   2280  O  O     . PRO A 1 285 ? 156.991 130.451 110.984 1.00 25.01 ?  285 PRO A O     1 
ATOM   2281  C  CB    . PRO A 1 285 ? 156.863 133.390 112.481 1.00 26.35 ?  285 PRO A CB    1 
ATOM   2282  C  CG    . PRO A 1 285 ? 155.891 133.469 113.617 1.00 23.82 ?  285 PRO A CG    1 
ATOM   2283  C  CD    . PRO A 1 285 ? 155.065 132.232 113.515 1.00 19.89 ?  285 PRO A CD    1 
ATOM   2284  N  N     . ASP A 1 286 ? 157.770 132.137 109.699 1.00 31.22 ?  286 ASP A N     1 
ATOM   2285  C  CA    . ASP A 1 286 ? 158.721 131.284 108.995 1.00 25.97 ?  286 ASP A CA    1 
ATOM   2286  C  C     . ASP A 1 286 ? 159.731 130.649 109.940 1.00 34.55 ?  286 ASP A C     1 
ATOM   2287  O  O     . ASP A 1 286 ? 160.292 129.595 109.616 1.00 35.11 ?  286 ASP A O     1 
ATOM   2288  C  CB    . ASP A 1 286 ? 159.454 132.090 107.921 1.00 27.60 ?  286 ASP A CB    1 
ATOM   2289  C  CG    . ASP A 1 286 ? 158.895 131.858 106.534 1.00 38.61 ?  286 ASP A CG    1 
ATOM   2290  O  OD1   . ASP A 1 286 ? 157.659 131.739 106.401 1.00 42.79 ?  286 ASP A OD1   1 
ATOM   2291  O  OD2   . ASP A 1 286 ? 159.691 131.799 105.575 1.00 42.45 -1 286 ASP A OD2   1 
ATOM   2292  N  N     . LYS A 1 287 ? 159.974 131.268 111.098 1.00 32.80 ?  287 LYS A N     1 
ATOM   2293  C  CA    . LYS A 1 287 ? 160.902 130.700 112.069 1.00 27.94 ?  287 LYS A CA    1 
ATOM   2294  C  C     . LYS A 1 287 ? 160.429 129.339 112.561 1.00 27.59 ?  287 LYS A C     1 
ATOM   2295  O  O     . LYS A 1 287 ? 161.234 128.415 112.707 1.00 35.74 ?  287 LYS A O     1 
ATOM   2296  C  CB    . LYS A 1 287 ? 161.082 131.661 113.244 1.00 28.97 ?  287 LYS A CB    1 
ATOM   2297  C  CG    . LYS A 1 287 ? 162.208 131.276 114.187 1.00 27.77 ?  287 LYS A CG    1 
ATOM   2298  C  CD    . LYS A 1 287 ? 163.503 131.075 113.424 1.00 31.66 ?  287 LYS A CD    1 
ATOM   2299  C  CE    . LYS A 1 287 ? 164.649 130.739 114.355 1.00 32.61 ?  287 LYS A CE    1 
ATOM   2300  N  NZ    . LYS A 1 287 ? 165.952 130.721 113.638 1.00 33.85 1  287 LYS A NZ    1 
ATOM   2301  N  N     . PHE A 1 288 ? 159.130 129.199 112.834 1.00 27.34 ?  288 PHE A N     1 
ATOM   2302  C  CA    . PHE A 1 288 ? 158.613 127.918 113.307 1.00 22.62 ?  288 PHE A CA    1 
ATOM   2303  C  C     . PHE A 1 288 ? 158.757 126.833 112.248 1.00 25.80 ?  288 PHE A C     1 
ATOM   2304  O  O     . PHE A 1 288 ? 159.129 125.696 112.561 1.00 34.63 ?  288 PHE A O     1 
ATOM   2305  C  CB    . PHE A 1 288 ? 157.152 128.061 113.726 1.00 24.92 ?  288 PHE A CB    1 
ATOM   2306  C  CG    . PHE A 1 288 ? 156.585 126.830 114.368 1.00 27.45 ?  288 PHE A CG    1 
ATOM   2307  C  CD1   . PHE A 1 288 ? 156.764 126.593 115.720 1.00 23.19 ?  288 PHE A CD1   1 
ATOM   2308  C  CD2   . PHE A 1 288 ? 155.882 125.903 113.620 1.00 26.73 ?  288 PHE A CD2   1 
ATOM   2309  C  CE1   . PHE A 1 288 ? 156.249 125.462 116.311 1.00 27.14 ?  288 PHE A CE1   1 
ATOM   2310  C  CE2   . PHE A 1 288 ? 155.364 124.769 114.207 1.00 24.01 ?  288 PHE A CE2   1 
ATOM   2311  C  CZ    . PHE A 1 288 ? 155.548 124.549 115.552 1.00 27.79 ?  288 PHE A CZ    1 
ATOM   2312  N  N     . VAL A 1 289 ? 158.456 127.162 110.991 1.00 32.00 ?  289 VAL A N     1 
ATOM   2313  C  CA    . VAL A 1 289 ? 158.590 126.185 109.915 1.00 29.47 ?  289 VAL A CA    1 
ATOM   2314  C  C     . VAL A 1 289 ? 160.050 125.796 109.732 1.00 30.02 ?  289 VAL A C     1 
ATOM   2315  O  O     . VAL A 1 289 ? 160.370 124.629 109.480 1.00 35.14 ?  289 VAL A O     1 
ATOM   2316  C  CB    . VAL A 1 289 ? 157.980 126.738 108.614 1.00 30.34 ?  289 VAL A CB    1 
ATOM   2317  C  CG1   . VAL A 1 289 ? 158.142 125.740 107.481 1.00 30.45 ?  289 VAL A CG1   1 
ATOM   2318  C  CG2   . VAL A 1 289 ? 156.515 127.082 108.825 1.00 23.88 ?  289 VAL A CG2   1 
ATOM   2319  N  N     . GLU A 1 290 ? 160.959 126.766 109.858 1.00 37.54 ?  290 GLU A N     1 
ATOM   2320  C  CA    . GLU A 1 290 ? 162.382 126.460 109.769 1.00 34.55 ?  290 GLU A CA    1 
ATOM   2321  C  C     . GLU A 1 290 ? 162.827 125.554 110.913 1.00 35.20 ?  290 GLU A C     1 
ATOM   2322  O  O     . GLU A 1 290 ? 163.593 124.608 110.702 1.00 41.82 ?  290 GLU A O     1 
ATOM   2323  C  CB    . GLU A 1 290 ? 163.193 127.757 109.753 1.00 34.45 ?  290 GLU A CB    1 
ATOM   2324  C  CG    . GLU A 1 290 ? 164.548 127.663 110.431 1.00 39.30 ?  290 GLU A CG    1 
ATOM   2325  C  CD    . GLU A 1 290 ? 165.292 128.984 110.427 1.00 45.41 ?  290 GLU A CD    1 
ATOM   2326  O  OE1   . GLU A 1 290 ? 164.627 130.041 110.445 1.00 46.66 ?  290 GLU A OE1   1 
ATOM   2327  O  OE2   . GLU A 1 290 ? 166.540 128.965 110.408 1.00 43.61 -1 290 GLU A OE2   1 
ATOM   2328  N  N     . LEU A 1 291 ? 162.352 125.827 112.130 1.00 28.22 ?  291 LEU A N     1 
ATOM   2329  C  CA    . LEU A 1 291 ? 162.719 125.004 113.279 1.00 26.89 ?  291 LEU A CA    1 
ATOM   2330  C  C     . LEU A 1 291 ? 162.198 123.581 113.130 1.00 35.32 ?  291 LEU A C     1 
ATOM   2331  O  O     . LEU A 1 291 ? 162.900 122.618 113.455 1.00 38.89 ?  291 LEU A O     1 
ATOM   2332  C  CB    . LEU A 1 291 ? 162.188 125.632 114.567 1.00 31.08 ?  291 LEU A CB    1 
ATOM   2333  C  CG    . LEU A 1 291 ? 162.876 126.909 115.051 1.00 33.94 ?  291 LEU A CG    1 
ATOM   2334  C  CD1   . LEU A 1 291 ? 162.024 127.610 116.094 1.00 28.25 ?  291 LEU A CD1   1 
ATOM   2335  C  CD2   . LEU A 1 291 ? 164.254 126.602 115.598 1.00 31.72 ?  291 LEU A CD2   1 
ATOM   2336  N  N     . ALA A 1 292 ? 160.960 123.431 112.653 1.00 37.20 ?  292 ALA A N     1 
ATOM   2337  C  CA    . ALA A 1 292 ? 160.413 122.096 112.432 1.00 30.50 ?  292 ALA A CA    1 
ATOM   2338  C  C     . ALA A 1 292 ? 161.146 121.379 111.304 1.00 32.10 ?  292 ALA A C     1 
ATOM   2339  O  O     . ALA A 1 292 ? 161.343 120.161 111.361 1.00 35.83 ?  292 ALA A O     1 
ATOM   2340  C  CB    . ALA A 1 292 ? 158.918 122.185 112.134 1.00 26.04 ?  292 ALA A CB    1 
ATOM   2341  N  N     . ARG A 1 293 ? 161.552 122.119 110.271 1.00 32.95 ?  293 ARG A N     1 
ATOM   2342  C  CA    . ARG A 1 293 ? 162.266 121.518 109.150 1.00 33.13 ?  293 ARG A CA    1 
ATOM   2343  C  C     . ARG A 1 293 ? 163.604 120.940 109.590 1.00 39.16 ?  293 ARG A C     1 
ATOM   2344  O  O     . ARG A 1 293 ? 163.990 119.848 109.154 1.00 41.45 ?  293 ARG A O     1 
ATOM   2345  C  CB    . ARG A 1 293 ? 162.461 122.556 108.046 1.00 34.94 ?  293 ARG A CB    1 
ATOM   2346  C  CG    . ARG A 1 293 ? 163.317 122.092 106.884 1.00 35.23 ?  293 ARG A CG    1 
ATOM   2347  C  CD    . ARG A 1 293 ? 163.730 123.267 106.022 1.00 37.62 ?  293 ARG A CD    1 
ATOM   2348  N  NE    . ARG A 1 293 ? 162.604 124.150 105.743 1.00 42.26 ?  293 ARG A NE    1 
ATOM   2349  C  CZ    . ARG A 1 293 ? 162.631 125.467 105.891 1.00 40.70 ?  293 ARG A CZ    1 
ATOM   2350  N  NH1   . ARG A 1 293 ? 163.715 126.093 106.317 1.00 41.69 1  293 ARG A NH1   1 
ATOM   2351  N  NH2   . ARG A 1 293 ? 161.541 126.174 105.604 1.00 35.59 ?  293 ARG A NH2   1 
ATOM   2352  N  N     . GLU A 1 294 ? 164.324 121.652 110.451 1.00 44.74 ?  294 GLU A N     1 
ATOM   2353  C  CA    . GLU A 1 294 ? 165.616 121.195 110.943 1.00 43.18 ?  294 GLU A CA    1 
ATOM   2354  C  C     . GLU A 1 294 ? 165.496 120.231 112.114 1.00 44.44 ?  294 GLU A C     1 
ATOM   2355  O  O     . GLU A 1 294 ? 166.524 119.751 112.603 1.00 48.04 ?  294 GLU A O     1 
ATOM   2356  C  CB    . GLU A 1 294 ? 166.476 122.395 111.347 1.00 41.64 ?  294 GLU A CB    1 
ATOM   2357  C  CG    . GLU A 1 294 ? 166.584 123.467 110.274 1.00 43.84 ?  294 GLU A CG    1 
ATOM   2358  C  CD    . GLU A 1 294 ? 166.905 124.833 110.845 1.00 52.67 ?  294 GLU A CD    1 
ATOM   2359  O  OE1   . GLU A 1 294 ? 166.472 125.121 111.980 1.00 50.44 ?  294 GLU A OE1   1 
ATOM   2360  O  OE2   . GLU A 1 294 ? 167.590 125.620 110.158 1.00 51.67 -1 294 GLU A OE2   1 
ATOM   2361  N  N     . ASP A 1 295 ? 164.274 119.944 112.569 1.00 44.22 ?  295 ASP A N     1 
ATOM   2362  C  CA    . ASP A 1 295 ? 164.025 119.054 113.704 1.00 43.82 ?  295 ASP A CA    1 
ATOM   2363  C  C     . ASP A 1 295 ? 164.719 119.547 114.969 1.00 48.16 ?  295 ASP A C     1 
ATOM   2364  O  O     . ASP A 1 295 ? 165.072 118.757 115.847 1.00 51.21 ?  295 ASP A O     1 
ATOM   2365  C  CB    . ASP A 1 295 ? 164.443 117.614 113.390 1.00 46.89 ?  295 ASP A CB    1 
ATOM   2366  C  CG    . ASP A 1 295 ? 163.502 116.591 113.995 1.00 51.48 ?  295 ASP A CG    1 
ATOM   2367  O  OD1   . ASP A 1 295 ? 162.769 116.940 114.943 1.00 49.59 ?  295 ASP A OD1   1 
ATOM   2368  O  OD2   . ASP A 1 295 ? 163.493 115.435 113.520 1.00 50.75 -1 295 ASP A OD2   1 
ATOM   2369  N  N     . LYS A 1 296 ? 164.916 120.857 115.070 1.00 45.61 ?  296 LYS A N     1 
ATOM   2370  C  CA    . LYS A 1 296 ? 165.546 121.447 116.237 1.00 45.38 ?  296 LYS A CA    1 
ATOM   2371  C  C     . LYS A 1 296 ? 164.525 121.622 117.357 1.00 44.84 ?  296 LYS A C     1 
ATOM   2372  O  O     . LYS A 1 296 ? 163.323 121.416 117.178 1.00 45.52 ?  296 LYS A O     1 
ATOM   2373  C  CB    . LYS A 1 296 ? 166.191 122.783 115.875 1.00 45.77 ?  296 LYS A CB    1 
ATOM   2374  C  CG    . LYS A 1 296 ? 167.381 122.652 114.941 1.00 45.88 ?  296 LYS A CG    1 
ATOM   2375  C  CD    . LYS A 1 296 ? 168.016 123.999 114.653 1.00 46.45 ?  296 LYS A CD    1 
ATOM   2376  C  CE    . LYS A 1 296 ? 169.353 123.831 113.947 1.00 45.56 ?  296 LYS A CE    1 
ATOM   2377  N  NZ    . LYS A 1 296 ? 169.870 125.122 113.416 1.00 46.99 1  296 LYS A NZ    1 
ATOM   2378  N  N     . ALA A 1 297 ? 165.019 121.998 118.531 1.00 46.02 ?  297 ALA A N     1 
ATOM   2379  C  CA    . ALA A 1 297 ? 164.155 122.230 119.680 1.00 44.58 ?  297 ALA A CA    1 
ATOM   2380  C  C     . ALA A 1 297 ? 163.668 123.673 119.665 1.00 44.70 ?  297 ALA A C     1 
ATOM   2381  O  O     . ALA A 1 297 ? 164.462 124.604 119.832 1.00 46.57 ?  297 ALA A O     1 
ATOM   2382  C  CB    . ALA A 1 297 ? 164.896 121.923 120.977 1.00 44.33 ?  297 ALA A CB    1 
ATOM   2383  N  N     . ALA A 1 298 ? 162.369 123.857 119.463 1.00 38.12 ?  298 ALA A N     1 
ATOM   2384  C  CA    . ALA A 1 298 ? 161.776 125.183 119.466 1.00 36.96 ?  298 ALA A CA    1 
ATOM   2385  C  C     . ALA A 1 298 ? 161.367 125.574 120.882 1.00 35.89 ?  298 ALA A C     1 
ATOM   2386  O  O     . ALA A 1 298 ? 161.293 124.745 121.790 1.00 36.72 ?  298 ALA A O     1 
ATOM   2387  C  CB    . ALA A 1 298 ? 160.574 125.238 118.526 1.00 36.58 ?  298 ALA A CB    1 
ATOM   2388  N  N     . TYR A 1 299 ? 161.099 126.863 121.064 1.00 35.49 ?  299 TYR A N     1 
ATOM   2389  C  CA    . TYR A 1 299 ? 160.699 127.399 122.357 1.00 28.47 ?  299 TYR A CA    1 
ATOM   2390  C  C     . TYR A 1 299 ? 159.475 128.281 122.182 1.00 31.38 ?  299 TYR A C     1 
ATOM   2391  O  O     . TYR A 1 299 ? 159.452 129.147 121.303 1.00 40.14 ?  299 TYR A O     1 
ATOM   2392  C  CB    . TYR A 1 299 ? 161.833 128.205 122.997 1.00 34.24 ?  299 TYR A CB    1 
ATOM   2393  C  CG    . TYR A 1 299 ? 162.869 127.360 123.696 1.00 37.70 ?  299 TYR A CG    1 
ATOM   2394  C  CD1   . TYR A 1 299 ? 162.690 126.959 125.010 1.00 35.43 ?  299 TYR A CD1   1 
ATOM   2395  C  CD2   . TYR A 1 299 ? 164.033 126.978 123.046 1.00 37.20 ?  299 TYR A CD2   1 
ATOM   2396  C  CE1   . TYR A 1 299 ? 163.634 126.192 125.655 1.00 35.26 ?  299 TYR A CE1   1 
ATOM   2397  C  CE2   . TYR A 1 299 ? 164.984 126.210 123.682 1.00 37.25 ?  299 TYR A CE2   1 
ATOM   2398  C  CZ    . TYR A 1 299 ? 164.779 125.820 124.988 1.00 40.47 ?  299 TYR A CZ    1 
ATOM   2399  O  OH    . TYR A 1 299 ? 165.722 125.054 125.632 1.00 45.23 ?  299 TYR A OH    1 
ATOM   2400  N  N     . VAL A 1 300 ? 158.466 128.058 123.005 1.00 31.06 ?  300 VAL A N     1 
ATOM   2401  C  CA    . VAL A 1 300 ? 157.358 128.994 123.136 1.00 24.27 ?  300 VAL A CA    1 
ATOM   2402  C  C     . VAL A 1 300 ? 157.682 129.929 124.290 1.00 29.18 ?  300 VAL A C     1 
ATOM   2403  O  O     . VAL A 1 300 ? 158.371 129.556 125.243 1.00 29.35 ?  300 VAL A O     1 
ATOM   2404  C  CB    . VAL A 1 300 ? 156.015 128.266 123.348 1.00 26.12 ?  300 VAL A CB    1 
ATOM   2405  C  CG1   . VAL A 1 300 ? 155.607 127.534 122.082 1.00 29.40 ?  300 VAL A CG1   1 
ATOM   2406  C  CG2   . VAL A 1 300 ? 156.107 127.306 124.520 1.00 29.28 ?  300 VAL A CG2   1 
ATOM   2407  N  N     . PHE A 1 301 ? 157.193 131.159 124.207 1.00 27.32 ?  301 PHE A N     1 
ATOM   2408  C  CA    . PHE A 1 301 ? 157.625 132.213 125.109 1.00 25.15 ?  301 PHE A CA    1 
ATOM   2409  C  C     . PHE A 1 301 ? 156.456 132.774 125.902 1.00 25.22 ?  301 PHE A C     1 
ATOM   2410  O  O     . PHE A 1 301 ? 155.303 132.735 125.461 1.00 31.04 ?  301 PHE A O     1 
ATOM   2411  C  CB    . PHE A 1 301 ? 158.315 133.340 124.339 1.00 27.97 ?  301 PHE A CB    1 
ATOM   2412  C  CG    . PHE A 1 301 ? 159.464 132.875 123.498 1.00 31.39 ?  301 PHE A CG    1 
ATOM   2413  C  CD1   . PHE A 1 301 ? 160.701 132.637 124.068 1.00 29.04 ?  301 PHE A CD1   1 
ATOM   2414  C  CD2   . PHE A 1 301 ? 159.305 132.667 122.142 1.00 26.23 ?  301 PHE A CD2   1 
ATOM   2415  C  CE1   . PHE A 1 301 ? 161.758 132.203 123.300 1.00 31.76 ?  301 PHE A CE1   1 
ATOM   2416  C  CE2   . PHE A 1 301 ? 160.359 132.235 121.370 1.00 28.48 ?  301 PHE A CE2   1 
ATOM   2417  C  CZ    . PHE A 1 301 ? 161.587 132.004 121.951 1.00 32.52 ?  301 PHE A CZ    1 
ATOM   2418  N  N     . TYR A 1 302 ? 156.775 133.290 127.086 1.00 26.97 ?  302 TYR A N     1 
ATOM   2419  C  CA    . TYR A 1 302 ? 155.805 133.992 127.912 1.00 27.45 ?  302 TYR A CA    1 
ATOM   2420  C  C     . TYR A 1 302 ? 155.766 135.441 127.453 1.00 30.56 ?  302 TYR A C     1 
ATOM   2421  O  O     . TYR A 1 302 ? 156.776 136.148 127.590 1.00 29.62 ?  302 TYR A O     1 
ATOM   2422  C  CB    . TYR A 1 302 ? 156.186 133.904 129.381 1.00 28.30 ?  302 TYR A CB    1 
ATOM   2423  C  CG    . TYR A 1 302 ? 156.000 132.531 129.990 1.00 26.25 ?  302 TYR A CG    1 
ATOM   2424  C  CD1   . TYR A 1 302 ? 156.843 131.482 129.655 1.00 27.65 ?  302 TYR A CD1   1 
ATOM   2425  C  CD2   . TYR A 1 302 ? 154.988 132.290 130.906 1.00 27.48 ?  302 TYR A CD2   1 
ATOM   2426  C  CE1   . TYR A 1 302 ? 156.678 130.231 130.208 1.00 30.31 ?  302 TYR A CE1   1 
ATOM   2427  C  CE2   . TYR A 1 302 ? 154.817 131.043 131.468 1.00 30.14 ?  302 TYR A CE2   1 
ATOM   2428  C  CZ    . TYR A 1 302 ? 155.665 130.017 131.117 1.00 33.71 ?  302 TYR A CZ    1 
ATOM   2429  O  OH    . TYR A 1 302 ? 155.498 128.771 131.673 1.00 37.78 ?  302 TYR A OH    1 
ATOM   2430  N  N     . PRO A 1 303 ? 154.651 135.922 126.899 1.00 29.03 ?  303 PRO A N     1 
ATOM   2431  C  CA    . PRO A 1 303 ? 154.644 137.269 126.305 1.00 24.96 ?  303 PRO A CA    1 
ATOM   2432  C  C     . PRO A 1 303 ? 154.956 138.383 127.286 1.00 27.56 ?  303 PRO A C     1 
ATOM   2433  O  O     . PRO A 1 303 ? 155.576 139.381 126.895 1.00 30.61 ?  303 PRO A O     1 
ATOM   2434  C  CB    . PRO A 1 303 ? 153.218 137.398 125.751 1.00 24.83 ?  303 PRO A CB    1 
ATOM   2435  C  CG    . PRO A 1 303 ? 152.724 136.008 125.635 1.00 24.18 ?  303 PRO A CG    1 
ATOM   2436  C  CD    . PRO A 1 303 ? 153.359 135.240 126.739 1.00 25.44 ?  303 PRO A CD    1 
ATOM   2437  N  N     . HIS A 1 304 ? 154.538 138.255 128.547 1.00 32.27 ?  304 HIS A N     1 
ATOM   2438  C  CA    . HIS A 1 304 ? 154.765 139.335 129.498 1.00 27.96 ?  304 HIS A CA    1 
ATOM   2439  C  C     . HIS A 1 304 ? 156.242 139.507 129.815 1.00 32.41 ?  304 HIS A C     1 
ATOM   2440  O  O     . HIS A 1 304 ? 156.700 140.635 130.012 1.00 40.50 ?  304 HIS A O     1 
ATOM   2441  C  CB    . HIS A 1 304 ? 153.979 139.099 130.784 1.00 29.89 ?  304 HIS A CB    1 
ATOM   2442  C  CG    . HIS A 1 304 ? 153.871 140.315 131.648 1.00 32.74 ?  304 HIS A CG    1 
ATOM   2443  N  ND1   . HIS A 1 304 ? 153.606 141.566 131.137 1.00 31.93 ?  304 HIS A ND1   1 
ATOM   2444  C  CD2   . HIS A 1 304 ? 154.002 140.475 132.986 1.00 35.88 ?  304 HIS A CD2   1 
ATOM   2445  C  CE1   . HIS A 1 304 ? 153.573 142.445 132.122 1.00 33.55 ?  304 HIS A CE1   1 
ATOM   2446  N  NE2   . HIS A 1 304 ? 153.810 141.809 133.254 1.00 34.35 ?  304 HIS A NE2   1 
ATOM   2447  N  N     . THR A 1 305 ? 157.000 138.411 129.869 1.00 25.74 ?  305 THR A N     1 
ATOM   2448  C  CA    . THR A 1 305 ? 158.437 138.525 130.083 1.00 29.41 ?  305 THR A CA    1 
ATOM   2449  C  C     . THR A 1 305 ? 159.107 139.266 128.932 1.00 28.69 ?  305 THR A C     1 
ATOM   2450  O  O     . THR A 1 305 ? 159.974 140.119 129.153 1.00 37.07 ?  305 THR A O     1 
ATOM   2451  C  CB    . THR A 1 305 ? 159.052 137.139 130.261 1.00 33.48 ?  305 THR A CB    1 
ATOM   2452  O  OG1   . THR A 1 305 ? 158.901 136.389 129.049 1.00 32.73 ?  305 THR A OG1   1 
ATOM   2453  C  CG2   . THR A 1 305 ? 158.363 136.403 131.394 1.00 30.50 ?  305 THR A CG2   1 
ATOM   2454  N  N     . ILE A 1 306 ? 158.707 138.962 127.696 1.00 32.69 ?  306 ILE A N     1 
ATOM   2455  C  CA    . ILE A 1 306 ? 159.262 139.661 126.541 1.00 28.02 ?  306 ILE A CA    1 
ATOM   2456  C  C     . ILE A 1 306 ? 158.888 141.136 126.580 1.00 29.49 ?  306 ILE A C     1 
ATOM   2457  O  O     . ILE A 1 306 ? 159.716 142.008 126.292 1.00 35.55 ?  306 ILE A O     1 
ATOM   2458  C  CB    . ILE A 1 306 ? 158.794 138.990 125.238 1.00 30.36 ?  306 ILE A CB    1 
ATOM   2459  C  CG1   . ILE A 1 306 ? 159.448 137.619 125.083 1.00 28.05 ?  306 ILE A CG1   1 
ATOM   2460  C  CG2   . ILE A 1 306 ? 159.113 139.863 124.035 1.00 30.85 ?  306 ILE A CG2   1 
ATOM   2461  C  CD1   . ILE A 1 306 ? 158.937 136.838 123.909 1.00 31.24 ?  306 ILE A CD1   1 
ATOM   2462  N  N     . TYR A 1 307 ? 157.638 141.444 126.928 1.00 33.59 ?  307 TYR A N     1 
ATOM   2463  C  CA    . TYR A 1 307 ? 157.216 142.839 126.994 1.00 31.54 ?  307 TYR A CA    1 
ATOM   2464  C  C     . TYR A 1 307 ? 157.972 143.597 128.078 1.00 35.23 ?  307 TYR A C     1 
ATOM   2465  O  O     . TYR A 1 307 ? 158.360 144.754 127.879 1.00 36.72 ?  307 TYR A O     1 
ATOM   2466  C  CB    . TYR A 1 307 ? 155.708 142.923 127.229 1.00 29.33 ?  307 TYR A CB    1 
ATOM   2467  C  CG    . TYR A 1 307 ? 155.173 144.334 127.216 1.00 33.59 ?  307 TYR A CG    1 
ATOM   2468  C  CD1   . TYR A 1 307 ? 154.870 144.969 126.021 1.00 29.32 ?  307 TYR A CD1   1 
ATOM   2469  C  CD2   . TYR A 1 307 ? 154.973 145.033 128.399 1.00 34.47 ?  307 TYR A CD2   1 
ATOM   2470  C  CE1   . TYR A 1 307 ? 154.383 146.258 126.002 1.00 33.46 ?  307 TYR A CE1   1 
ATOM   2471  C  CE2   . TYR A 1 307 ? 154.486 146.324 128.390 1.00 34.77 ?  307 TYR A CE2   1 
ATOM   2472  C  CZ    . TYR A 1 307 ? 154.193 146.931 127.188 1.00 35.97 ?  307 TYR A CZ    1 
ATOM   2473  O  OH    . TYR A 1 307 ? 153.708 148.217 127.173 1.00 38.80 ?  307 TYR A OH    1 
ATOM   2474  N  N     . LYS A 1 308 ? 158.179 142.969 129.237 1.00 35.92 ?  308 LYS A N     1 
ATOM   2475  C  CA    . LYS A 1 308 ? 158.930 143.613 130.310 1.00 33.02 ?  308 LYS A CA    1 
ATOM   2476  C  C     . LYS A 1 308 ? 160.385 143.827 129.916 1.00 32.74 ?  308 LYS A C     1 
ATOM   2477  O  O     . LYS A 1 308 ? 160.966 144.878 130.210 1.00 39.07 ?  308 LYS A O     1 
ATOM   2478  C  CB    . LYS A 1 308 ? 158.839 142.775 131.585 1.00 34.34 ?  308 LYS A CB    1 
ATOM   2479  C  CG    . LYS A 1 308 ? 157.483 142.827 132.267 1.00 34.02 ?  308 LYS A CG    1 
ATOM   2480  C  CD    . LYS A 1 308 ? 157.508 142.106 133.603 1.00 34.74 ?  308 LYS A CD    1 
ATOM   2481  C  CE    . LYS A 1 308 ? 158.035 140.688 133.462 1.00 38.99 ?  308 LYS A CE    1 
ATOM   2482  N  NZ    . LYS A 1 308 ? 157.025 139.674 133.871 1.00 36.46 1  308 LYS A NZ    1 
ATOM   2483  N  N     . GLU A 1 309 ? 160.989 142.844 129.248 1.00 30.34 ?  309 GLU A N     1 
ATOM   2484  C  CA    . GLU A 1 309 ? 162.406 142.932 128.921 1.00 35.08 ?  309 GLU A CA    1 
ATOM   2485  C  C     . GLU A 1 309 ? 162.677 143.910 127.783 1.00 36.49 ?  309 GLU A C     1 
ATOM   2486  O  O     . GLU A 1 309 ? 163.660 144.656 127.827 1.00 39.85 ?  309 GLU A O     1 
ATOM   2487  C  CB    . GLU A 1 309 ? 162.940 141.542 128.570 1.00 32.16 ?  309 GLU A CB    1 
ATOM   2488  C  CG    . GLU A 1 309 ? 164.343 141.540 128.001 1.00 36.68 ?  309 GLU A CG    1 
ATOM   2489  C  CD    . GLU A 1 309 ? 165.398 141.849 129.039 1.00 43.34 ?  309 GLU A CD    1 
ATOM   2490  O  OE1   . GLU A 1 309 ? 165.074 141.830 130.244 1.00 44.25 ?  309 GLU A OE1   1 
ATOM   2491  O  OE2   . GLU A 1 309 ? 166.555 142.115 128.649 1.00 42.50 -1 309 GLU A OE2   1 
ATOM   2492  N  N     . TYR A 1 310 ? 161.818 143.928 126.764 1.00 34.65 ?  310 TYR A N     1 
ATOM   2493  C  CA    . TYR A 1 310 ? 162.084 144.681 125.547 1.00 35.73 ?  310 TYR A CA    1 
ATOM   2494  C  C     . TYR A 1 310 ? 161.181 145.889 125.357 1.00 33.98 ?  310 TYR A C     1 
ATOM   2495  O  O     . TYR A 1 310 ? 161.477 146.729 124.500 1.00 35.70 ?  310 TYR A O     1 
ATOM   2496  C  CB    . TYR A 1 310 ? 161.954 143.760 124.325 1.00 34.26 ?  310 TYR A CB    1 
ATOM   2497  C  CG    . TYR A 1 310 ? 162.985 142.658 124.289 1.00 34.23 ?  310 TYR A CG    1 
ATOM   2498  C  CD1   . TYR A 1 310 ? 164.238 142.871 123.737 1.00 33.53 ?  310 TYR A CD1   1 
ATOM   2499  C  CD2   . TYR A 1 310 ? 162.706 141.406 124.819 1.00 32.13 ?  310 TYR A CD2   1 
ATOM   2500  C  CE1   . TYR A 1 310 ? 165.183 141.868 123.706 1.00 36.62 ?  310 TYR A CE1   1 
ATOM   2501  C  CE2   . TYR A 1 310 ? 163.644 140.398 124.794 1.00 33.39 ?  310 TYR A CE2   1 
ATOM   2502  C  CZ    . TYR A 1 310 ? 164.881 140.634 124.237 1.00 36.69 ?  310 TYR A CZ    1 
ATOM   2503  O  OH    . TYR A 1 310 ? 165.819 139.632 124.209 1.00 35.81 ?  310 TYR A OH    1 
ATOM   2504  N  N     . GLY A 1 311 ? 160.099 146.005 126.119 1.00 31.00 ?  311 GLY A N     1 
ATOM   2505  C  CA    . GLY A 1 311 ? 159.182 147.112 125.959 1.00 32.53 ?  311 GLY A CA    1 
ATOM   2506  C  C     . GLY A 1 311 ? 158.205 146.971 124.815 1.00 35.66 ?  311 GLY A C     1 
ATOM   2507  O  O     . GLY A 1 311 ? 157.398 147.884 124.597 1.00 39.25 ?  311 GLY A O     1 
ATOM   2508  N  N     . GLN A 1 312 ? 158.250 145.865 124.078 1.00 36.16 ?  312 GLN A N     1 
ATOM   2509  C  CA    . GLN A 1 312 ? 157.342 145.613 122.972 1.00 32.63 ?  312 GLN A CA    1 
ATOM   2510  C  C     . GLN A 1 312 ? 156.705 144.244 123.149 1.00 33.64 ?  312 GLN A C     1 
ATOM   2511  O  O     . GLN A 1 312 ? 157.283 143.350 123.770 1.00 38.49 ?  312 GLN A O     1 
ATOM   2512  C  CB    . GLN A 1 312 ? 158.064 145.672 121.620 1.00 32.24 ?  312 GLN A CB    1 
ATOM   2513  C  CG    . GLN A 1 312 ? 158.746 146.992 121.327 1.00 35.80 ?  312 GLN A CG    1 
ATOM   2514  C  CD    . GLN A 1 312 ? 160.032 146.818 120.544 1.00 40.31 ?  312 GLN A CD    1 
ATOM   2515  O  OE1   . GLN A 1 312 ? 160.039 146.894 119.315 1.00 39.60 ?  312 GLN A OE1   1 
ATOM   2516  N  NE2   . GLN A 1 312 ? 161.129 146.579 121.253 1.00 37.60 ?  312 GLN A NE2   1 
ATOM   2517  N  N     . HIS A 1 313 ? 155.505 144.091 122.598 1.00 30.44 ?  313 HIS A N     1 
ATOM   2518  C  CA    . HIS A 1 313 ? 154.848 142.797 122.600 1.00 28.09 ?  313 HIS A CA    1 
ATOM   2519  C  C     . HIS A 1 313 ? 155.595 141.826 121.690 1.00 32.02 ?  313 HIS A C     1 
ATOM   2520  O  O     . HIS A 1 313 ? 156.291 142.222 120.752 1.00 32.61 ?  313 HIS A O     1 
ATOM   2521  C  CB    . HIS A 1 313 ? 153.395 142.931 122.152 1.00 25.78 ?  313 HIS A CB    1 
ATOM   2522  C  CG    . HIS A 1 313 ? 152.553 143.762 123.071 1.00 31.16 ?  313 HIS A CG    1 
ATOM   2523  N  ND1   . HIS A 1 313 ? 152.089 143.295 124.281 1.00 29.95 ?  313 HIS A ND1   1 
ATOM   2524  C  CD2   . HIS A 1 313 ? 152.091 145.029 122.955 1.00 30.97 ?  313 HIS A CD2   1 
ATOM   2525  C  CE1   . HIS A 1 313 ? 151.377 144.238 124.871 1.00 29.39 ?  313 HIS A CE1   1 
ATOM   2526  N  NE2   . HIS A 1 313 ? 151.363 145.300 124.087 1.00 31.94 ?  313 HIS A NE2   1 
ATOM   2527  N  N     . MET A 1 314 ? 155.451 140.533 121.990 1.00 35.83 ?  314 MET A N     1 
ATOM   2528  C  CA    . MET A 1 314 ? 156.149 139.518 121.209 1.00 29.72 ?  314 MET A CA    1 
ATOM   2529  C  C     . MET A 1 314 ? 155.678 139.508 119.761 1.00 35.52 ?  314 MET A C     1 
ATOM   2530  O  O     . MET A 1 314 ? 156.493 139.403 118.836 1.00 38.07 ?  314 MET A O     1 
ATOM   2531  C  CB    . MET A 1 314 ? 155.956 138.140 121.840 1.00 27.22 ?  314 MET A CB    1 
ATOM   2532  C  CG    . MET A 1 314 ? 156.578 137.012 121.037 1.00 32.36 ?  314 MET A CG    1 
ATOM   2533  S  SD    . MET A 1 314 ? 156.356 135.374 121.755 1.00 41.78 ?  314 MET A SD    1 
ATOM   2534  C  CE    . MET A 1 314 ? 155.012 135.675 122.891 1.00 30.24 ?  314 MET A CE    1 
ATOM   2535  N  N     . ASP A 1 315 ? 154.367 139.618 119.540 1.00 33.93 ?  315 ASP A N     1 
ATOM   2536  C  CA    . ASP A 1 315 ? 153.837 139.586 118.184 1.00 38.13 ?  315 ASP A CA    1 
ATOM   2537  C  C     . ASP A 1 315 ? 154.081 140.881 117.423 1.00 31.39 ?  315 ASP A C     1 
ATOM   2538  O  O     . ASP A 1 315 ? 153.884 140.909 116.204 1.00 39.47 ?  315 ASP A O     1 
ATOM   2539  C  CB    . ASP A 1 315 ? 152.339 139.273 118.203 1.00 31.26 ?  315 ASP A CB    1 
ATOM   2540  C  CG    . ASP A 1 315 ? 151.567 140.188 119.123 1.00 35.74 ?  315 ASP A CG    1 
ATOM   2541  O  OD1   . ASP A 1 315 ? 152.166 140.692 120.094 1.00 39.29 ?  315 ASP A OD1   1 
ATOM   2542  O  OD2   . ASP A 1 315 ? 150.362 140.404 118.873 1.00 32.58 -1 315 ASP A OD2   1 
ATOM   2543  N  N     . GLU A 1 316 ? 154.498 141.944 118.103 1.00 24.36 ?  316 GLU A N     1 
ATOM   2544  C  CA    . GLU A 1 316 ? 154.906 143.173 117.437 1.00 28.82 ?  316 GLU A CA    1 
ATOM   2545  C  C     . GLU A 1 316 ? 156.367 143.151 117.014 1.00 33.83 ?  316 GLU A C     1 
ATOM   2546  O  O     . GLU A 1 316 ? 156.836 144.121 116.410 1.00 32.98 ?  316 GLU A O     1 
ATOM   2547  C  CB    . GLU A 1 316 ? 154.653 144.376 118.349 1.00 31.77 ?  316 GLU A CB    1 
ATOM   2548  C  CG    . GLU A 1 316 ? 153.190 144.615 118.664 1.00 31.04 ?  316 GLU A CG    1 
ATOM   2549  C  CD    . GLU A 1 316 ? 152.512 145.502 117.641 1.00 38.93 ?  316 GLU A CD    1 
ATOM   2550  O  OE1   . GLU A 1 316 ? 151.370 145.938 117.891 1.00 41.23 ?  316 GLU A OE1   1 
ATOM   2551  O  OE2   . GLU A 1 316 ? 153.123 145.764 116.584 1.00 41.62 -1 316 GLU A OE2   1 
ATOM   2552  N  N     . MET A 1 317 ? 157.090 142.079 117.317 1.00 39.09 ?  317 MET A N     1 
ATOM   2553  C  CA    . MET A 1 317 ? 158.499 141.945 116.992 1.00 35.78 ?  317 MET A CA    1 
ATOM   2554  C  C     . MET A 1 317 ? 158.692 140.877 115.925 1.00 34.44 ?  317 MET A C     1 
ATOM   2555  O  O     . MET A 1 317 ? 157.843 140.006 115.724 1.00 36.95 ?  317 MET A O     1 
ATOM   2556  C  CB    . MET A 1 317 ? 159.318 141.593 118.240 1.00 34.12 ?  317 MET A CB    1 
ATOM   2557  C  CG    . MET A 1 317 ? 159.231 142.624 119.350 1.00 34.36 ?  317 MET A CG    1 
ATOM   2558  S  SD    . MET A 1 317 ? 160.083 142.108 120.849 1.00 44.92 ?  317 MET A SD    1 
ATOM   2559  C  CE    . MET A 1 317 ? 161.576 143.087 120.741 1.00 38.89 ?  317 MET A CE    1 
ATOM   2560  N  N     . ASP A 1 318 ? 159.830 140.957 115.240 1.00 41.30 ?  318 ASP A N     1 
ATOM   2561  C  CA    . ASP A 1 318 ? 160.168 139.995 114.198 1.00 38.66 ?  318 ASP A CA    1 
ATOM   2562  C  C     . ASP A 1 318 ? 160.747 138.749 114.852 1.00 37.96 ?  318 ASP A C     1 
ATOM   2563  O  O     . ASP A 1 318 ? 161.837 138.792 115.428 1.00 41.69 ?  318 ASP A O     1 
ATOM   2564  C  CB    . ASP A 1 318 ? 161.156 140.607 113.209 1.00 36.96 ?  318 ASP A CB    1 
ATOM   2565  C  CG    . ASP A 1 318 ? 161.276 139.800 111.933 1.00 46.58 ?  318 ASP A CG    1 
ATOM   2566  O  OD1   . ASP A 1 318 ? 160.307 139.096 111.579 1.00 43.51 ?  318 ASP A OD1   1 
ATOM   2567  O  OD2   . ASP A 1 318 ? 162.340 139.870 111.285 1.00 49.50 -1 318 ASP A OD2   1 
ATOM   2568  N  N     . MET A 1 319 ? 160.018 137.635 114.766 1.00 34.59 ?  319 MET A N     1 
ATOM   2569  C  CA    . MET A 1 319 ? 160.495 136.408 115.391 1.00 35.93 ?  319 MET A CA    1 
ATOM   2570  C  C     . MET A 1 319 ? 161.703 135.834 114.664 1.00 33.84 ?  319 MET A C     1 
ATOM   2571  O  O     . MET A 1 319 ? 162.588 135.260 115.303 1.00 37.29 ?  319 MET A O     1 
ATOM   2572  C  CB    . MET A 1 319 ? 159.372 135.374 115.457 1.00 33.86 ?  319 MET A CB    1 
ATOM   2573  C  CG    . MET A 1 319 ? 159.700 134.185 116.338 1.00 35.19 ?  319 MET A CG    1 
ATOM   2574  S  SD    . MET A 1 319 ? 160.057 134.649 118.043 1.00 43.77 ?  319 MET A SD    1 
ATOM   2575  C  CE    . MET A 1 319 ? 158.405 134.905 118.678 1.00 36.00 ?  319 MET A CE    1 
ATOM   2576  N  N     . ASN A 1 320 ? 161.770 135.994 113.342 1.00 39.08 ?  320 ASN A N     1 
ATOM   2577  C  CA    . ASN A 1 320 ? 162.907 135.478 112.591 1.00 40.11 ?  320 ASN A CA    1 
ATOM   2578  C  C     . ASN A 1 320 ? 164.208 136.188 112.942 1.00 41.59 ?  320 ASN A C     1 
ATOM   2579  O  O     . ASN A 1 320 ? 165.285 135.672 112.623 1.00 41.30 ?  320 ASN A O     1 
ATOM   2580  C  CB    . ASN A 1 320 ? 162.635 135.586 111.091 1.00 42.00 ?  320 ASN A CB    1 
ATOM   2581  C  CG    . ASN A 1 320 ? 161.643 134.549 110.608 1.00 43.63 ?  320 ASN A CG    1 
ATOM   2582  O  OD1   . ASN A 1 320 ? 160.440 134.802 110.554 1.00 38.11 ?  320 ASN A OD1   1 
ATOM   2583  N  ND2   . ASN A 1 320 ? 162.144 133.372 110.250 1.00 40.53 ?  320 ASN A ND2   1 
ATOM   2584  N  N     . GLU A 1 321 ? 164.137 137.354 113.586 1.00 42.57 ?  321 GLU A N     1 
ATOM   2585  C  CA    . GLU A 1 321 ? 165.328 138.071 114.015 1.00 41.38 ?  321 GLU A CA    1 
ATOM   2586  C  C     . GLU A 1 321 ? 165.475 138.168 115.525 1.00 43.34 ?  321 GLU A C     1 
ATOM   2587  O  O     . GLU A 1 321 ? 166.570 138.483 116.001 1.00 46.03 ?  321 GLU A O     1 
ATOM   2588  C  CB    . GLU A 1 321 ? 165.340 139.488 113.416 1.00 41.68 ?  321 GLU A CB    1 
ATOM   2589  C  CG    . GLU A 1 321 ? 164.820 140.569 114.348 1.00 44.45 ?  321 GLU A CG    1 
ATOM   2590  C  CD    . GLU A 1 321 ? 164.469 141.854 113.624 1.00 47.32 ?  321 GLU A CD    1 
ATOM   2591  O  OE1   . GLU A 1 321 ? 164.325 141.819 112.384 1.00 47.11 ?  321 GLU A OE1   1 
ATOM   2592  O  OE2   . GLU A 1 321 ? 164.335 142.898 114.297 1.00 43.73 -1 321 GLU A OE2   1 
ATOM   2593  N  N     . MET A 1 322 ? 164.418 137.895 116.290 1.00 40.61 ?  322 MET A N     1 
ATOM   2594  C  CA    . MET A 1 322 ? 164.457 138.015 117.741 1.00 38.13 ?  322 MET A CA    1 
ATOM   2595  C  C     . MET A 1 322 ? 164.270 136.694 118.470 1.00 35.74 ?  322 MET A C     1 
ATOM   2596  O  O     . MET A 1 322 ? 164.305 136.684 119.703 1.00 41.25 ?  322 MET A O     1 
ATOM   2597  C  CB    . MET A 1 322 ? 163.396 139.012 118.225 1.00 37.48 ?  322 MET A CB    1 
ATOM   2598  C  CG    . MET A 1 322 ? 163.532 140.409 117.650 1.00 38.97 ?  322 MET A CG    1 
ATOM   2599  S  SD    . MET A 1 322 ? 164.712 141.450 118.531 1.00 48.56 ?  322 MET A SD    1 
ATOM   2600  C  CE    . MET A 1 322 ? 164.521 140.858 120.206 1.00 39.49 ?  322 MET A CE    1 
ATOM   2601  N  N     . TYR A 1 323 ? 164.060 135.584 117.759 1.00 33.93 ?  323 TYR A N     1 
ATOM   2602  C  CA    . TYR A 1 323 ? 163.861 134.304 118.433 1.00 32.83 ?  323 TYR A CA    1 
ATOM   2603  C  C     . TYR A 1 323 ? 165.107 133.891 119.203 1.00 36.92 ?  323 TYR A C     1 
ATOM   2604  O  O     . TYR A 1 323 ? 165.025 133.454 120.358 1.00 39.12 ?  323 TYR A O     1 
ATOM   2605  C  CB    . TYR A 1 323 ? 163.474 133.229 117.416 1.00 33.05 ?  323 TYR A CB    1 
ATOM   2606  C  CG    . TYR A 1 323 ? 163.451 131.829 117.988 1.00 34.69 ?  323 TYR A CG    1 
ATOM   2607  C  CD1   . TYR A 1 323 ? 162.334 131.350 118.656 1.00 33.75 ?  323 TYR A CD1   1 
ATOM   2608  C  CD2   . TYR A 1 323 ? 164.546 130.984 117.859 1.00 32.20 ?  323 TYR A CD2   1 
ATOM   2609  C  CE1   . TYR A 1 323 ? 162.309 130.074 119.181 1.00 32.07 ?  323 TYR A CE1   1 
ATOM   2610  C  CE2   . TYR A 1 323 ? 164.530 129.711 118.382 1.00 32.37 ?  323 TYR A CE2   1 
ATOM   2611  C  CZ    . TYR A 1 323 ? 163.409 129.260 119.041 1.00 31.69 ?  323 TYR A CZ    1 
ATOM   2612  O  OH    . TYR A 1 323 ? 163.392 127.989 119.561 1.00 31.64 ?  323 TYR A OH    1 
ATOM   2613  N  N     . ASP A 1 324 ? 166.276 134.024 118.576 1.00 38.72 ?  324 ASP A N     1 
ATOM   2614  C  CA    . ASP A 1 324 ? 167.521 133.667 119.243 1.00 35.27 ?  324 ASP A CA    1 
ATOM   2615  C  C     . ASP A 1 324 ? 167.800 134.592 120.419 1.00 40.31 ?  324 ASP A C     1 
ATOM   2616  O  O     . ASP A 1 324 ? 168.322 134.154 121.449 1.00 47.00 ?  324 ASP A O     1 
ATOM   2617  C  CB    . ASP A 1 324 ? 168.676 133.697 118.245 1.00 41.26 ?  324 ASP A CB    1 
ATOM   2618  C  CG    . ASP A 1 324 ? 168.541 132.639 117.170 1.00 44.72 ?  324 ASP A CG    1 
ATOM   2619  O  OD1   . ASP A 1 324 ? 168.332 131.459 117.518 1.00 41.76 ?  324 ASP A OD1   1 
ATOM   2620  O  OD2   . ASP A 1 324 ? 168.642 132.988 115.975 1.00 44.08 -1 324 ASP A OD2   1 
ATOM   2621  N  N     . LYS A 1 325 ? 167.467 135.877 120.282 1.00 38.81 ?  325 LYS A N     1 
ATOM   2622  C  CA    . LYS A 1 325 ? 167.629 136.805 121.395 1.00 35.53 ?  325 LYS A CA    1 
ATOM   2623  C  C     . LYS A 1 325 ? 166.709 136.442 122.555 1.00 38.86 ?  325 LYS A C     1 
ATOM   2624  O  O     . LYS A 1 325 ? 167.113 136.518 123.720 1.00 43.73 ?  325 LYS A O     1 
ATOM   2625  C  CB    . LYS A 1 325 ? 167.372 138.235 120.923 1.00 37.33 ?  325 LYS A CB    1 
ATOM   2626  C  CG    . LYS A 1 325 ? 168.370 138.723 119.890 1.00 37.87 ?  325 LYS A CG    1 
ATOM   2627  C  CD    . LYS A 1 325 ? 168.037 140.124 119.415 1.00 41.16 ?  325 LYS A CD    1 
ATOM   2628  C  CE    . LYS A 1 325 ? 168.986 140.573 118.318 1.00 42.11 ?  325 LYS A CE    1 
ATOM   2629  N  NZ    . LYS A 1 325 ? 168.483 141.779 117.606 1.00 43.60 1  325 LYS A NZ    1 
ATOM   2630  N  N     . PHE A 1 326 ? 165.467 136.051 122.257 1.00 39.16 ?  326 PHE A N     1 
ATOM   2631  C  CA    . PHE A 1 326 ? 164.554 135.609 123.305 1.00 33.41 ?  326 PHE A CA    1 
ATOM   2632  C  C     . PHE A 1 326 ? 165.077 134.358 123.996 1.00 36.37 ?  326 PHE A C     1 
ATOM   2633  O  O     . PHE A 1 326 ? 164.995 134.235 125.224 1.00 40.55 ?  326 PHE A O     1 
ATOM   2634  C  CB    . PHE A 1 326 ? 163.166 135.336 122.722 1.00 32.69 ?  326 PHE A CB    1 
ATOM   2635  C  CG    . PHE A 1 326 ? 162.476 136.552 122.176 1.00 35.56 ?  326 PHE A CG    1 
ATOM   2636  C  CD1   . PHE A 1 326 ? 162.880 137.824 122.539 1.00 35.09 ?  326 PHE A CD1   1 
ATOM   2637  C  CD2   . PHE A 1 326 ? 161.416 136.415 121.298 1.00 34.20 ?  326 PHE A CD2   1 
ATOM   2638  C  CE1   . PHE A 1 326 ? 162.238 138.935 122.033 1.00 33.20 ?  326 PHE A CE1   1 
ATOM   2639  C  CE2   . PHE A 1 326 ? 160.773 137.523 120.790 1.00 37.15 ?  326 PHE A CE2   1 
ATOM   2640  C  CZ    . PHE A 1 326 ? 161.185 138.784 121.158 1.00 38.91 ?  326 PHE A CZ    1 
ATOM   2641  N  N     . VAL A 1 327 ? 165.605 133.411 123.219 1.00 39.05 ?  327 VAL A N     1 
ATOM   2642  C  CA    . VAL A 1 327 ? 166.116 132.171 123.798 1.00 38.24 ?  327 VAL A CA    1 
ATOM   2643  C  C     . VAL A 1 327 ? 167.332 132.448 124.672 1.00 40.04 ?  327 VAL A C     1 
ATOM   2644  O  O     . VAL A 1 327 ? 167.456 131.906 125.777 1.00 45.64 ?  327 VAL A O     1 
ATOM   2645  C  CB    . VAL A 1 327 ? 166.430 131.158 122.682 1.00 36.91 ?  327 VAL A CB    1 
ATOM   2646  C  CG1   . VAL A 1 327 ? 167.226 129.987 123.232 1.00 40.92 ?  327 VAL A CG1   1 
ATOM   2647  C  CG2   . VAL A 1 327 ? 165.147 130.672 122.038 1.00 33.27 ?  327 VAL A CG2   1 
ATOM   2648  N  N     . ASP A 1 328 ? 168.242 133.300 124.201 1.00 38.45 ?  328 ASP A N     1 
ATOM   2649  C  CA    . ASP A 1 328 ? 169.452 133.613 124.949 1.00 36.87 ?  328 ASP A CA    1 
ATOM   2650  C  C     . ASP A 1 328 ? 169.197 134.539 126.129 1.00 40.52 ?  328 ASP A C     1 
ATOM   2651  O  O     . ASP A 1 328 ? 170.036 134.609 127.034 1.00 45.52 ?  328 ASP A O     1 
ATOM   2652  C  CB    . ASP A 1 328 ? 170.492 134.248 124.022 1.00 38.98 ?  328 ASP A CB    1 
ATOM   2653  C  CG    . ASP A 1 328 ? 170.947 133.305 122.929 1.00 44.83 ?  328 ASP A CG    1 
ATOM   2654  O  OD1   . ASP A 1 328 ? 170.774 132.080 123.091 1.00 48.01 ?  328 ASP A OD1   1 
ATOM   2655  O  OD2   . ASP A 1 328 ? 171.478 133.791 121.908 1.00 44.15 -1 328 ASP A OD2   1 
ATOM   2656  N  N     . ASN A 1 329 ? 168.074 135.246 126.143 1.00 41.66 ?  329 ASN A N     1 
ATOM   2657  C  CA    . ASN A 1 329 ? 167.789 136.187 127.219 1.00 38.80 ?  329 ASN A CA    1 
ATOM   2658  C  C     . ASN A 1 329 ? 167.374 135.432 128.474 1.00 42.53 ?  329 ASN A C     1 
ATOM   2659  O  O     . ASN A 1 329 ? 166.382 134.696 128.440 1.00 42.49 ?  329 ASN A O     1 
ATOM   2660  C  CB    . ASN A 1 329 ? 166.691 137.154 126.800 1.00 33.89 ?  329 ASN A CB    1 
ATOM   2661  C  CG    . ASN A 1 329 ? 166.678 138.419 127.632 1.00 40.78 ?  329 ASN A CG    1 
ATOM   2662  O  OD1   . ASN A 1 329 ? 166.620 138.369 128.859 1.00 45.18 ?  329 ASN A OD1   1 
ATOM   2663  N  ND2   . ASN A 1 329 ? 166.739 139.565 126.965 1.00 41.09 ?  329 ASN A ND2   1 
ATOM   2664  N  N     . PRO A 1 330 ? 168.096 135.574 129.589 1.00 44.27 ?  330 PRO A N     1 
ATOM   2665  C  CA    . PRO A 1 330 ? 167.668 134.892 130.819 1.00 40.96 ?  330 PRO A CA    1 
ATOM   2666  C  C     . PRO A 1 330 ? 166.403 135.475 131.421 1.00 39.46 ?  330 PRO A C     1 
ATOM   2667  O  O     . PRO A 1 330 ? 165.648 134.742 132.070 1.00 40.15 ?  330 PRO A O     1 
ATOM   2668  C  CB    . PRO A 1 330 ? 168.872 135.070 131.754 1.00 39.08 ?  330 PRO A CB    1 
ATOM   2669  C  CG    . PRO A 1 330 ? 169.547 136.298 131.257 1.00 36.96 ?  330 PRO A CG    1 
ATOM   2670  C  CD    . PRO A 1 330 ? 169.365 136.298 129.768 1.00 38.41 ?  330 PRO A CD    1 
ATOM   2671  N  N     . ARG A 1 331 ? 166.146 136.768 131.226 1.00 38.41 ?  331 ARG A N     1 
ATOM   2672  C  CA    . ARG A 1 331 ? 164.970 137.406 131.802 1.00 40.80 ?  331 ARG A CA    1 
ATOM   2673  C  C     . ARG A 1 331 ? 163.693 137.096 131.034 1.00 41.59 ?  331 ARG A C     1 
ATOM   2674  O  O     . ARG A 1 331 ? 162.601 137.366 131.546 1.00 40.35 ?  331 ARG A O     1 
ATOM   2675  C  CB    . ARG A 1 331 ? 165.180 138.920 131.875 1.00 39.81 ?  331 ARG A CB    1 
ATOM   2676  C  CG    . ARG A 1 331 ? 166.150 139.348 132.964 1.00 40.33 ?  331 ARG A CG    1 
ATOM   2677  C  CD    . ARG A 1 331 ? 166.771 140.699 132.659 1.00 42.11 ?  331 ARG A CD    1 
ATOM   2678  N  NE    . ARG A 1 331 ? 167.377 140.736 131.333 1.00 41.88 ?  331 ARG A NE    1 
ATOM   2679  C  CZ    . ARG A 1 331 ? 168.546 140.191 131.026 1.00 43.13 ?  331 ARG A CZ    1 
ATOM   2680  N  NH1   . ARG A 1 331 ? 169.278 139.566 131.933 1.00 42.61 1  331 ARG A NH1   1 
ATOM   2681  N  NH2   . ARG A 1 331 ? 168.994 140.279 129.777 1.00 43.39 ?  331 ARG A NH2   1 
ATOM   2682  N  N     . VAL A 1 332 ? 163.801 136.546 129.833 1.00 37.30 ?  332 VAL A N     1 
ATOM   2683  C  CA    . VAL A 1 332 ? 162.647 136.061 129.088 1.00 32.98 ?  332 VAL A CA    1 
ATOM   2684  C  C     . VAL A 1 332 ? 162.369 134.632 129.530 1.00 37.43 ?  332 VAL A C     1 
ATOM   2685  O  O     . VAL A 1 332 ? 163.287 133.808 129.610 1.00 38.83 ?  332 VAL A O     1 
ATOM   2686  C  CB    . VAL A 1 332 ? 162.896 136.136 127.572 1.00 33.47 ?  332 VAL A CB    1 
ATOM   2687  C  CG1   . VAL A 1 332 ? 161.809 135.398 126.812 1.00 33.96 ?  332 VAL A CG1   1 
ATOM   2688  C  CG2   . VAL A 1 332 ? 162.976 137.584 127.119 1.00 34.85 ?  332 VAL A CG2   1 
ATOM   2689  N  N     . LYS A 1 333 ? 161.111 134.339 129.844 1.00 35.97 ?  333 LYS A N     1 
ATOM   2690  C  CA    . LYS A 1 333 ? 160.712 132.994 130.233 1.00 29.96 ?  333 LYS A CA    1 
ATOM   2691  C  C     . LYS A 1 333 ? 160.238 132.233 129.002 1.00 32.69 ?  333 LYS A C     1 
ATOM   2692  O  O     . LYS A 1 333 ? 159.401 132.728 128.242 1.00 35.64 ?  333 LYS A O     1 
ATOM   2693  C  CB    . LYS A 1 333 ? 159.612 133.035 131.292 1.00 28.38 ?  333 LYS A CB    1 
ATOM   2694  C  CG    . LYS A 1 333 ? 159.500 131.765 132.116 1.00 34.79 ?  333 LYS A CG    1 
ATOM   2695  C  CD    . LYS A 1 333 ? 158.316 131.825 133.064 1.00 35.04 ?  333 LYS A CD    1 
ATOM   2696  C  CE    . LYS A 1 333 ? 158.061 130.474 133.714 1.00 37.13 ?  333 LYS A CE    1 
ATOM   2697  N  NZ    . LYS A 1 333 ? 156.896 130.508 134.641 1.00 37.74 1  333 LYS A NZ    1 
ATOM   2698  N  N     . LYS A 1 334 ? 160.781 131.036 128.808 1.00 38.85 ?  334 LYS A N     1 
ATOM   2699  C  CA    . LYS A 1 334 ? 160.476 130.233 127.635 1.00 34.29 ?  334 LYS A CA    1 
ATOM   2700  C  C     . LYS A 1 334 ? 160.236 128.790 128.052 1.00 36.06 ?  334 LYS A C     1 
ATOM   2701  O  O     . LYS A 1 334 ? 160.746 128.330 129.076 1.00 39.70 ?  334 LYS A O     1 
ATOM   2702  C  CB    . LYS A 1 334 ? 161.606 130.300 126.600 1.00 32.87 ?  334 LYS A CB    1 
ATOM   2703  C  CG    . LYS A 1 334 ? 162.896 129.644 127.049 1.00 35.31 ?  334 LYS A CG    1 
ATOM   2704  C  CD    . LYS A 1 334 ? 164.105 130.482 126.687 1.00 35.92 ?  334 LYS A CD    1 
ATOM   2705  C  CE    . LYS A 1 334 ? 164.073 131.821 127.390 1.00 38.84 ?  334 LYS A CE    1 
ATOM   2706  N  NZ    . LYS A 1 334 ? 165.359 132.555 127.262 1.00 39.45 1  334 LYS A NZ    1 
ATOM   2707  N  N     . GLU A 1 335 ? 159.442 128.086 127.251 1.00 38.00 ?  335 GLU A N     1 
ATOM   2708  C  CA    . GLU A 1 335 ? 159.149 126.677 127.463 1.00 36.54 ?  335 GLU A CA    1 
ATOM   2709  C  C     . GLU A 1 335 ? 159.565 125.881 126.234 1.00 36.29 ?  335 GLU A C     1 
ATOM   2710  O  O     . GLU A 1 335 ? 159.297 126.287 125.100 1.00 40.84 ?  335 GLU A O     1 
ATOM   2711  C  CB    . GLU A 1 335 ? 157.663 126.451 127.753 1.00 36.06 ?  335 GLU A CB    1 
ATOM   2712  C  CG    . GLU A 1 335 ? 157.401 125.468 128.880 1.00 38.94 ?  335 GLU A CG    1 
ATOM   2713  C  CD    . GLU A 1 335 ? 156.137 125.784 129.651 1.00 44.57 ?  335 GLU A CD    1 
ATOM   2714  O  OE1   . GLU A 1 335 ? 156.071 125.442 130.850 1.00 44.53 ?  335 GLU A OE1   1 
ATOM   2715  O  OE2   . GLU A 1 335 ? 155.206 126.367 129.059 1.00 42.08 -1 335 GLU A OE2   1 
ATOM   2716  N  N     . LYS A 1 336 ? 160.220 124.749 126.467 1.00 37.35 ?  336 LYS A N     1 
ATOM   2717  C  CA    . LYS A 1 336 ? 160.710 123.912 125.381 1.00 32.44 ?  336 LYS A CA    1 
ATOM   2718  C  C     . LYS A 1 336 ? 159.565 123.117 124.769 1.00 37.58 ?  336 LYS A C     1 
ATOM   2719  O  O     . LYS A 1 336 ? 158.776 122.492 125.484 1.00 40.53 ?  336 LYS A O     1 
ATOM   2720  C  CB    . LYS A 1 336 ? 161.797 122.969 125.895 1.00 38.26 ?  336 LYS A CB    1 
ATOM   2721  C  CG    . LYS A 1 336 ? 162.685 122.378 124.818 1.00 43.11 ?  336 LYS A CG    1 
ATOM   2722  C  CD    . LYS A 1 336 ? 163.641 121.360 125.418 1.00 41.37 ?  336 LYS A CD    1 
ATOM   2723  C  CE    . LYS A 1 336 ? 164.828 121.099 124.507 1.00 41.46 ?  336 LYS A CE    1 
ATOM   2724  N  NZ    . LYS A 1 336 ? 164.635 119.879 123.677 1.00 42.28 1  336 LYS A NZ    1 
ATOM   2725  N  N     . ILE A 1 337 ? 159.475 123.144 123.439 1.00 34.86 ?  337 ILE A N     1 
ATOM   2726  C  CA    . ILE A 1 337 ? 158.482 122.383 122.698 1.00 30.93 ?  337 ILE A CA    1 
ATOM   2727  C  C     . ILE A 1 337 ? 159.167 121.709 121.519 1.00 34.73 ?  337 ILE A C     1 
ATOM   2728  O  O     . ILE A 1 337 ? 160.274 122.075 121.120 1.00 42.14 ?  337 ILE A O     1 
ATOM   2729  C  CB    . ILE A 1 337 ? 157.309 123.257 122.202 1.00 32.72 ?  337 ILE A CB    1 
ATOM   2730  C  CG1   . ILE A 1 337 ? 157.831 124.416 121.353 1.00 35.14 ?  337 ILE A CG1   1 
ATOM   2731  C  CG2   . ILE A 1 337 ? 156.486 123.769 123.371 1.00 36.24 ?  337 ILE A CG2   1 
ATOM   2732  C  CD1   . ILE A 1 337 ? 157.017 124.674 120.111 1.00 32.24 ?  337 ILE A CD1   1 
ATOM   2733  N  N     . ASN A 1 338 ? 158.489 120.707 120.963 1.00 36.42 ?  338 ASN A N     1 
ATOM   2734  C  CA    . ASN A 1 338 ? 158.951 120.067 119.742 1.00 31.75 ?  338 ASN A CA    1 
ATOM   2735  C  C     . ASN A 1 338 ? 158.156 120.627 118.575 1.00 33.43 ?  338 ASN A C     1 
ATOM   2736  O  O     . ASN A 1 338 ? 156.948 120.365 118.481 1.00 36.67 ?  338 ASN A O     1 
ATOM   2737  C  CB    . ASN A 1 338 ? 158.785 118.552 119.825 1.00 33.95 ?  338 ASN A CB    1 
ATOM   2738  C  CG    . ASN A 1 338 ? 159.486 117.827 118.694 1.00 36.09 ?  338 ASN A CG    1 
ATOM   2739  O  OD1   . ASN A 1 338 ? 158.844 117.331 117.769 1.00 38.24 ?  338 ASN A OD1   1 
ATOM   2740  N  ND2   . ASN A 1 338 ? 160.809 117.765 118.761 1.00 35.46 ?  338 ASN A ND2   1 
ATOM   2741  N  N     . PRO A 1 339 ? 158.768 121.408 117.682 1.00 35.15 ?  339 PRO A N     1 
ATOM   2742  C  CA    . PRO A 1 339 ? 157.995 122.016 116.587 1.00 29.42 ?  339 PRO A CA    1 
ATOM   2743  C  C     . PRO A 1 339 ? 157.340 121.006 115.664 1.00 32.59 ?  339 PRO A C     1 
ATOM   2744  O  O     . PRO A 1 339 ? 156.232 121.258 115.178 1.00 37.75 ?  339 PRO A O     1 
ATOM   2745  C  CB    . PRO A 1 339 ? 159.042 122.863 115.850 1.00 33.56 ?  339 PRO A CB    1 
ATOM   2746  C  CG    . PRO A 1 339 ? 160.350 122.255 116.211 1.00 36.27 ?  339 PRO A CG    1 
ATOM   2747  C  CD    . PRO A 1 339 ? 160.199 121.743 117.607 1.00 36.81 ?  339 PRO A CD    1 
ATOM   2748  N  N     . ARG A 1 340 ? 157.985 119.866 115.407 1.00 35.29 ?  340 ARG A N     1 
ATOM   2749  C  CA    . ARG A 1 340 ? 157.362 118.845 114.571 1.00 28.41 ?  340 ARG A CA    1 
ATOM   2750  C  C     . ARG A 1 340 ? 156.181 118.199 115.282 1.00 30.40 ?  340 ARG A C     1 
ATOM   2751  O  O     . ARG A 1 340 ? 155.171 117.875 114.649 1.00 37.55 ?  340 ARG A O     1 
ATOM   2752  C  CB    . ARG A 1 340 ? 158.390 117.794 114.163 1.00 28.21 ?  340 ARG A CB    1 
ATOM   2753  C  CG    . ARG A 1 340 ? 159.334 118.265 113.079 1.00 29.17 ?  340 ARG A CG    1 
ATOM   2754  C  CD    . ARG A 1 340 ? 159.966 117.100 112.346 1.00 33.78 ?  340 ARG A CD    1 
ATOM   2755  N  NE    . ARG A 1 340 ? 161.006 117.549 111.430 1.00 35.44 ?  340 ARG A NE    1 
ATOM   2756  C  CZ    . ARG A 1 340 ? 161.730 116.745 110.667 1.00 32.17 ?  340 ARG A CZ    1 
ATOM   2757  N  NH1   . ARG A 1 340 ? 161.556 115.435 110.683 1.00 30.86 1  340 ARG A NH1   1 
ATOM   2758  N  NH2   . ARG A 1 340 ? 162.653 117.268 109.864 1.00 33.45 ?  340 ARG A NH2   1 
ATOM   2759  N  N     . LYS A 1 341 ? 156.288 118.003 116.597 1.00 32.09 ?  341 LYS A N     1 
ATOM   2760  C  CA    . LYS A 1 341 ? 155.147 117.504 117.357 1.00 30.76 ?  341 LYS A CA    1 
ATOM   2761  C  C     . LYS A 1 341 ? 153.997 118.500 117.327 1.00 33.23 ?  341 LYS A C     1 
ATOM   2762  O  O     . LYS A 1 341 ? 152.830 118.108 117.226 1.00 36.39 ?  341 LYS A O     1 
ATOM   2763  C  CB    . LYS A 1 341 ? 155.564 117.204 118.795 1.00 35.55 ?  341 LYS A CB    1 
ATOM   2764  C  CG    . LYS A 1 341 ? 155.479 115.737 119.169 1.00 35.82 ?  341 LYS A CG    1 
ATOM   2765  C  CD    . LYS A 1 341 ? 156.229 114.873 118.170 1.00 38.75 ?  341 LYS A CD    1 
ATOM   2766  C  CE    . LYS A 1 341 ? 156.262 113.419 118.613 1.00 41.67 ?  341 LYS A CE    1 
ATOM   2767  N  NZ    . LYS A 1 341 ? 157.347 113.169 119.602 1.00 36.89 1  341 LYS A NZ    1 
ATOM   2768  N  N     . LEU A 1 342 ? 154.307 119.795 117.410 1.00 30.62 ?  342 LEU A N     1 
ATOM   2769  C  CA    . LEU A 1 342 ? 153.267 120.813 117.308 1.00 27.32 ?  342 LEU A CA    1 
ATOM   2770  C  C     . LEU A 1 342 ? 152.621 120.808 115.927 1.00 29.90 ?  342 LEU A C     1 
ATOM   2771  O  O     . LEU A 1 342 ? 151.404 120.975 115.806 1.00 33.99 ?  342 LEU A O     1 
ATOM   2772  C  CB    . LEU A 1 342 ? 153.849 122.189 117.628 1.00 31.11 ?  342 LEU A CB    1 
ATOM   2773  C  CG    . LEU A 1 342 ? 152.856 123.311 117.933 1.00 30.19 ?  342 LEU A CG    1 
ATOM   2774  C  CD1   . LEU A 1 342 ? 151.704 122.790 118.772 1.00 28.04 ?  342 LEU A CD1   1 
ATOM   2775  C  CD2   . LEU A 1 342 ? 153.553 124.459 118.640 1.00 26.81 ?  342 LEU A CD2   1 
ATOM   2776  N  N     . LEU A 1 343 ? 153.421 120.618 114.875 1.00 31.54 ?  343 LEU A N     1 
ATOM   2777  C  CA    . LEU A 1 343 ? 152.868 120.531 113.527 1.00 25.59 ?  343 LEU A CA    1 
ATOM   2778  C  C     . LEU A 1 343 ? 151.959 119.317 113.378 1.00 26.60 ?  343 LEU A C     1 
ATOM   2779  O  O     . LEU A 1 343 ? 150.886 119.402 112.768 1.00 37.59 ?  343 LEU A O     1 
ATOM   2780  C  CB    . LEU A 1 343 ? 153.999 120.480 112.501 1.00 30.44 ?  343 LEU A CB    1 
ATOM   2781  C  CG    . LEU A 1 343 ? 154.324 121.769 111.751 1.00 29.59 ?  343 LEU A CG    1 
ATOM   2782  C  CD1   . LEU A 1 343 ? 155.335 121.497 110.654 1.00 25.32 ?  343 LEU A CD1   1 
ATOM   2783  C  CD2   . LEU A 1 343 ? 153.062 122.392 111.180 1.00 33.56 ?  343 LEU A CD2   1 
ATOM   2784  N  N     . GLU A 1 344 ? 152.381 118.173 113.919 1.00 33.26 ?  344 GLU A N     1 
ATOM   2785  C  CA    . GLU A 1 344 ? 151.547 116.978 113.872 1.00 33.22 ?  344 GLU A CA    1 
ATOM   2786  C  C     . GLU A 1 344 ? 150.257 117.179 114.656 1.00 31.00 ?  344 GLU A C     1 
ATOM   2787  O  O     . GLU A 1 344 ? 149.192 116.708 114.243 1.00 34.27 ?  344 GLU A O     1 
ATOM   2788  C  CB    . GLU A 1 344 ? 152.323 115.774 114.406 1.00 30.91 ?  344 GLU A CB    1 
ATOM   2789  C  CG    . GLU A 1 344 ? 153.500 115.363 113.532 1.00 34.30 ?  344 GLU A CG    1 
ATOM   2790  C  CD    . GLU A 1 344 ? 154.583 114.642 114.309 1.00 41.97 ?  344 GLU A CD    1 
ATOM   2791  O  OE1   . GLU A 1 344 ? 154.321 114.235 115.461 1.00 44.43 ?  344 GLU A OE1   1 
ATOM   2792  O  OE2   . GLU A 1 344 ? 155.698 114.482 113.769 1.00 38.74 -1 344 GLU A OE2   1 
ATOM   2793  N  N     . LYS A 1 345 ? 150.335 117.867 115.797 1.00 29.36 ?  345 LYS A N     1 
ATOM   2794  C  CA    . LYS A 1 345 ? 149.130 118.173 116.561 1.00 28.66 ?  345 LYS A CA    1 
ATOM   2795  C  C     . LYS A 1 345 ? 148.200 119.086 115.776 1.00 31.02 ?  345 LYS A C     1 
ATOM   2796  O  O     . LYS A 1 345 ? 146.977 118.908 115.803 1.00 36.42 ?  345 LYS A O     1 
ATOM   2797  C  CB    . LYS A 1 345 ? 149.505 118.807 117.900 1.00 29.68 ?  345 LYS A CB    1 
ATOM   2798  C  CG    . LYS A 1 345 ? 148.312 119.270 118.716 1.00 30.37 ?  345 LYS A CG    1 
ATOM   2799  C  CD    . LYS A 1 345 ? 148.723 119.671 120.118 1.00 32.15 ?  345 LYS A CD    1 
ATOM   2800  C  CE    . LYS A 1 345 ? 147.521 120.101 120.939 1.00 36.64 ?  345 LYS A CE    1 
ATOM   2801  N  NZ    . LYS A 1 345 ? 147.888 120.386 122.352 1.00 33.99 1  345 LYS A NZ    1 
ATOM   2802  N  N     . LEU A 1 346 ? 148.760 120.074 115.075 1.00 30.76 ?  346 LEU A N     1 
ATOM   2803  C  CA    . LEU A 1 346 ? 147.950 120.933 114.218 1.00 25.94 ?  346 LEU A CA    1 
ATOM   2804  C  C     . LEU A 1 346 ? 147.241 120.116 113.146 1.00 28.41 ?  346 LEU A C     1 
ATOM   2805  O  O     . LEU A 1 346 ? 146.043 120.295 112.902 1.00 29.87 ?  346 LEU A O     1 
ATOM   2806  C  CB    . LEU A 1 346 ? 148.823 122.009 113.571 1.00 27.27 ?  346 LEU A CB    1 
ATOM   2807  C  CG    . LEU A 1 346 ? 149.425 123.105 114.448 1.00 29.07 ?  346 LEU A CG    1 
ATOM   2808  C  CD1   . LEU A 1 346 ? 150.395 123.945 113.640 1.00 29.73 ?  346 LEU A CD1   1 
ATOM   2809  C  CD2   . LEU A 1 346 ? 148.339 123.972 115.038 1.00 29.79 ?  346 LEU A CD2   1 
ATOM   2810  N  N     . ALA A 1 347 ? 147.973 119.209 112.497 1.00 30.42 ?  347 ALA A N     1 
ATOM   2811  C  CA    . ALA A 1 347 ? 147.373 118.382 111.454 1.00 26.76 ?  347 ALA A CA    1 
ATOM   2812  C  C     . ALA A 1 347 ? 146.273 117.491 112.016 1.00 32.78 ?  347 ALA A C     1 
ATOM   2813  O  O     . ALA A 1 347 ? 145.208 117.349 111.406 1.00 34.48 ?  347 ALA A O     1 
ATOM   2814  C  CB    . ALA A 1 347 ? 148.446 117.538 110.769 1.00 28.67 ?  347 ALA A CB    1 
ATOM   2815  N  N     . MET A 1 348 ? 146.513 116.884 113.180 1.00 35.83 ?  348 MET A N     1 
ATOM   2816  C  CA    . MET A 1 348 ? 145.505 116.029 113.798 1.00 34.31 ?  348 MET A CA    1 
ATOM   2817  C  C     . MET A 1 348 ? 144.262 116.824 114.178 1.00 34.62 ?  348 MET A C     1 
ATOM   2818  O  O     . MET A 1 348 ? 143.132 116.360 113.983 1.00 39.98 ?  348 MET A O     1 
ATOM   2819  C  CB    . MET A 1 348 ? 146.098 115.334 115.024 1.00 35.33 ?  348 MET A CB    1 
ATOM   2820  C  CG    . MET A 1 348 ? 145.087 114.601 115.884 1.00 42.25 ?  348 MET A CG    1 
ATOM   2821  S  SD    . MET A 1 348 ? 144.902 115.347 117.515 1.00 54.03 ?  348 MET A SD    1 
ATOM   2822  C  CE    . MET A 1 348 ? 146.587 115.271 118.113 1.00 37.83 ?  348 MET A CE    1 
ATOM   2823  N  N     . LEU A 1 349 ? 144.452 118.028 114.720 1.00 30.71 ?  349 LEU A N     1 
ATOM   2824  C  CA    . LEU A 1 349 ? 143.319 118.862 115.102 1.00 28.89 ?  349 LEU A CA    1 
ATOM   2825  C  C     . LEU A 1 349 ? 142.523 119.308 113.883 1.00 24.96 ?  349 LEU A C     1 
ATOM   2826  O  O     . LEU A 1 349 ? 141.292 119.382 113.936 1.00 29.91 ?  349 LEU A O     1 
ATOM   2827  C  CB    . LEU A 1 349 ? 143.806 120.068 115.901 1.00 31.98 ?  349 LEU A CB    1 
ATOM   2828  C  CG    . LEU A 1 349 ? 142.818 120.654 116.909 1.00 32.78 ?  349 LEU A CG    1 
ATOM   2829  C  CD1   . LEU A 1 349 ? 142.584 119.683 118.054 1.00 35.13 ?  349 LEU A CD1   1 
ATOM   2830  C  CD2   . LEU A 1 349 ? 143.313 121.993 117.427 1.00 28.86 ?  349 LEU A CD2   1 
ATOM   2831  N  N     . ARG A 1 350 ? 143.206 119.624 112.780 1.00 27.26 ?  350 ARG A N     1 
ATOM   2832  C  CA    . ARG A 1 350 ? 142.486 119.987 111.563 1.00 26.52 ?  350 ARG A CA    1 
ATOM   2833  C  C     . ARG A 1 350 ? 141.758 118.791 110.966 1.00 31.57 ?  350 ARG A C     1 
ATOM   2834  O  O     . ARG A 1 350 ? 140.671 118.948 110.401 1.00 35.26 ?  350 ARG A O     1 
ATOM   2835  C  CB    . ARG A 1 350 ? 143.442 120.593 110.536 1.00 24.25 ?  350 ARG A CB    1 
ATOM   2836  C  CG    . ARG A 1 350 ? 144.176 121.828 111.019 1.00 27.97 ?  350 ARG A CG    1 
ATOM   2837  C  CD    . ARG A 1 350 ? 144.867 122.544 109.878 1.00 29.70 ?  350 ARG A CD    1 
ATOM   2838  N  NE    . ARG A 1 350 ? 144.020 123.595 109.327 1.00 36.09 ?  350 ARG A NE    1 
ATOM   2839  C  CZ    . ARG A 1 350 ? 143.875 123.842 108.034 1.00 34.03 ?  350 ARG A CZ    1 
ATOM   2840  N  NH1   . ARG A 1 350 ? 144.509 123.130 107.119 1.00 30.09 1  350 ARG A NH1   1 
ATOM   2841  N  NH2   . ARG A 1 350 ? 143.066 124.826 107.651 1.00 30.10 ?  350 ARG A NH2   1 
ATOM   2842  N  N     . SER A 1 351 ? 142.342 117.596 111.071 1.00 35.31 ?  351 SER A N     1 
ATOM   2843  C  CA    . SER A 1 351 ? 141.659 116.397 110.596 1.00 32.15 ?  351 SER A CA    1 
ATOM   2844  C  C     . SER A 1 351 ? 140.406 116.112 111.414 1.00 37.40 ?  351 SER A C     1 
ATOM   2845  O  O     . SER A 1 351 ? 139.363 115.751 110.858 1.00 43.54 ?  351 SER A O     1 
ATOM   2846  C  CB    . SER A 1 351 ? 142.609 115.202 110.642 1.00 34.90 ?  351 SER A CB    1 
ATOM   2847  O  OG    . SER A 1 351 ? 143.652 115.343 109.696 1.00 45.11 ?  351 SER A OG    1 
ATOM   2848  N  N     . GLU A 1 352 ? 140.488 116.266 112.734 1.00 34.86 ?  352 GLU A N     1 
ATOM   2849  C  CA    . GLU A 1 352 ? 139.378 115.895 113.602 1.00 32.54 ?  352 GLU A CA    1 
ATOM   2850  C  C     . GLU A 1 352 ? 138.324 116.987 113.750 1.00 37.94 ?  352 GLU A C     1 
ATOM   2851  O  O     . GLU A 1 352 ? 137.173 116.671 114.070 1.00 46.70 ?  352 GLU A O     1 
ATOM   2852  C  CB    . GLU A 1 352 ? 139.903 115.496 114.986 1.00 38.24 ?  352 GLU A CB    1 
ATOM   2853  C  CG    . GLU A 1 352 ? 139.998 116.634 115.986 1.00 41.92 ?  352 GLU A CG    1 
ATOM   2854  C  CD    . GLU A 1 352 ? 140.565 116.190 117.319 1.00 45.83 ?  352 GLU A CD    1 
ATOM   2855  O  OE1   . GLU A 1 352 ? 141.600 115.493 117.324 1.00 43.39 ?  352 GLU A OE1   1 
ATOM   2856  O  OE2   . GLU A 1 352 ? 139.975 116.538 118.363 1.00 46.21 -1 352 GLU A OE2   1 
ATOM   2857  N  N     . SER A 1 353 ? 138.676 118.254 113.530 1.00 35.27 ?  353 SER A N     1 
ATOM   2858  C  CA    . SER A 1 353 ? 137.722 119.341 113.716 1.00 36.63 ?  353 SER A CA    1 
ATOM   2859  C  C     . SER A 1 353 ? 137.761 120.415 112.639 1.00 32.80 ?  353 SER A C     1 
ATOM   2860  O  O     . SER A 1 353 ? 136.833 121.227 112.588 1.00 32.09 ?  353 SER A O     1 
ATOM   2861  C  CB    . SER A 1 353 ? 137.942 120.010 115.080 1.00 35.94 ?  353 SER A CB    1 
ATOM   2862  O  OG    . SER A 1 353 ? 139.226 120.601 115.157 1.00 33.36 ?  353 SER A OG    1 
ATOM   2863  N  N     . GLY A 1 354 ? 138.784 120.461 111.787 1.00 25.10 ?  354 GLY A N     1 
ATOM   2864  C  CA    . GLY A 1 354 ? 138.934 121.529 110.826 1.00 27.40 ?  354 GLY A CA    1 
ATOM   2865  C  C     . GLY A 1 354 ? 139.675 122.743 111.339 1.00 23.52 ?  354 GLY A C     1 
ATOM   2866  O  O     . GLY A 1 354 ? 139.971 123.648 110.549 1.00 29.14 ?  354 GLY A O     1 
ATOM   2867  N  N     . TYR A 1 355 ? 139.993 122.787 112.629 1.00 22.42 ?  355 TYR A N     1 
ATOM   2868  C  CA    . TYR A 1 355 ? 140.684 123.871 113.299 1.00 16.59 ?  355 TYR A CA    1 
ATOM   2869  C  C     . TYR A 1 355 ? 142.100 123.446 113.671 1.00 22.01 ?  355 TYR A C     1 
ATOM   2870  O  O     . TYR A 1 355 ? 142.364 122.256 113.851 1.00 27.95 ?  355 TYR A O     1 
ATOM   2871  C  CB    . TYR A 1 355 ? 139.932 124.300 114.564 1.00 23.87 ?  355 TYR A CB    1 
ATOM   2872  C  CG    . TYR A 1 355 ? 138.592 124.935 114.288 1.00 28.43 ?  355 TYR A CG    1 
ATOM   2873  C  CD1   . TYR A 1 355 ? 138.485 126.033 113.446 1.00 21.92 ?  355 TYR A CD1   1 
ATOM   2874  C  CD2   . TYR A 1 355 ? 137.434 124.436 114.866 1.00 30.32 ?  355 TYR A CD2   1 
ATOM   2875  C  CE1   . TYR A 1 355 ? 137.264 126.614 113.188 1.00 28.77 ?  355 TYR A CE1   1 
ATOM   2876  C  CE2   . TYR A 1 355 ? 136.208 125.013 114.614 1.00 26.19 ?  355 TYR A CE2   1 
ATOM   2877  C  CZ    . TYR A 1 355 ? 136.128 126.102 113.776 1.00 29.94 ?  355 TYR A CZ    1 
ATOM   2878  O  OH    . TYR A 1 355 ? 134.907 126.679 113.523 1.00 31.97 ?  355 TYR A OH    1 
ATOM   2879  N  N     . PRO A 1 356 ? 143.039 124.388 113.804 1.00 30.72 ?  356 PRO A N     1 
ATOM   2880  C  CA    . PRO A 1 356 ? 142.911 125.842 113.665 1.00 15.39 ?  356 PRO A CA    1 
ATOM   2881  C  C     . PRO A 1 356 ? 143.045 126.338 112.234 1.00 15.29 ?  356 PRO A C     1 
ATOM   2882  O  O     . PRO A 1 356 ? 143.489 125.614 111.350 1.00 24.86 ?  356 PRO A O     1 
ATOM   2883  C  CB    . PRO A 1 356 ? 144.061 126.354 114.532 1.00 17.74 ?  356 PRO A CB    1 
ATOM   2884  C  CG    . PRO A 1 356 ? 145.131 125.334 114.307 1.00 22.45 ?  356 PRO A CG    1 
ATOM   2885  C  CD    . PRO A 1 356 ? 144.412 124.009 114.184 1.00 19.53 ?  356 PRO A CD    1 
ATOM   2886  N  N     . TYR A 1 357 ? 142.645 127.581 111.982 1.00 24.77 ?  357 TYR A N     1 
ATOM   2887  C  CA    . TYR A 1 357 ? 143.073 128.263 110.774 1.00 12.22 ?  357 TYR A CA    1 
ATOM   2888  C  C     . TYR A 1 357 ? 144.578 128.470 110.835 1.00 13.71 ?  357 TYR A C     1 
ATOM   2889  O  O     . TYR A 1 357 ? 145.138 128.735 111.900 1.00 26.45 ?  357 TYR A O     1 
ATOM   2890  C  CB    . TYR A 1 357 ? 142.367 129.613 110.632 1.00 13.47 ?  357 TYR A CB    1 
ATOM   2891  C  CG    . TYR A 1 357 ? 140.864 129.573 110.783 1.00 15.80 ?  357 TYR A CG    1 
ATOM   2892  C  CD1   . TYR A 1 357 ? 140.138 128.454 110.415 1.00 17.54 ?  357 TYR A CD1   1 
ATOM   2893  C  CD2   . TYR A 1 357 ? 140.172 130.663 111.287 1.00 18.09 ?  357 TYR A CD2   1 
ATOM   2894  C  CE1   . TYR A 1 357 ? 138.767 128.415 110.545 1.00 20.23 ?  357 TYR A CE1   1 
ATOM   2895  C  CE2   . TYR A 1 357 ? 138.802 130.634 111.424 1.00 15.86 ?  357 TYR A CE2   1 
ATOM   2896  C  CZ    . TYR A 1 357 ? 138.103 129.508 111.049 1.00 19.73 ?  357 TYR A CZ    1 
ATOM   2897  O  OH    . TYR A 1 357 ? 136.735 129.474 111.181 1.00 28.22 ?  357 TYR A OH    1 
ATOM   2898  N  N     . ILE A 1 358 ? 145.243 128.341 109.694 1.00 16.22 ?  358 ILE A N     1 
ATOM   2899  C  CA    . ILE A 1 358 ? 146.691 128.478 109.618 1.00 22.30 ?  358 ILE A CA    1 
ATOM   2900  C  C     . ILE A 1 358 ? 147.005 129.754 108.854 1.00 18.25 ?  358 ILE A C     1 
ATOM   2901  O  O     . ILE A 1 358 ? 146.610 129.902 107.693 1.00 20.96 ?  358 ILE A O     1 
ATOM   2902  C  CB    . ILE A 1 358 ? 147.350 127.262 108.952 1.00 22.40 ?  358 ILE A CB    1 
ATOM   2903  C  CG1   . ILE A 1 358 ? 146.973 125.971 109.684 1.00 19.24 ?  358 ILE A CG1   1 
ATOM   2904  C  CG2   . ILE A 1 358 ? 148.859 127.434 108.910 1.00 16.40 ?  358 ILE A CG2   1 
ATOM   2905  C  CD1   . ILE A 1 358 ? 147.205 126.020 111.171 1.00 19.28 ?  358 ILE A CD1   1 
ATOM   2906  N  N     . MET A 1 359 ? 147.714 130.671 109.504 1.00 15.72 ?  359 MET A N     1 
ATOM   2907  C  CA    . MET A 1 359 ? 148.220 131.877 108.863 1.00 9.17  ?  359 MET A CA    1 
ATOM   2908  C  C     . MET A 1 359 ? 149.737 131.799 108.816 1.00 11.86 ?  359 MET A C     1 
ATOM   2909  O  O     . MET A 1 359 ? 150.388 131.697 109.859 1.00 21.73 ?  359 MET A O     1 
ATOM   2910  C  CB    . MET A 1 359 ? 147.774 133.135 109.606 1.00 11.58 ?  359 MET A CB    1 
ATOM   2911  C  CG    . MET A 1 359 ? 148.122 134.415 108.869 1.00 12.28 ?  359 MET A CG    1 
ATOM   2912  S  SD    . MET A 1 359 ? 147.802 135.905 109.821 1.00 30.94 ?  359 MET A SD    1 
ATOM   2913  C  CE    . MET A 1 359 ? 149.390 136.717 109.720 1.00 9.99  ?  359 MET A CE    1 
ATOM   2914  N  N     . PHE A 1 360 ? 150.293 131.848 107.612 1.00 12.36 ?  360 PHE A N     1 
ATOM   2915  C  CA    . PHE A 1 360 ? 151.741 131.870 107.427 1.00 10.56 ?  360 PHE A CA    1 
ATOM   2916  C  C     . PHE A 1 360 ? 152.173 133.329 107.454 1.00 14.38 ?  360 PHE A C     1 
ATOM   2917  O  O     . PHE A 1 360 ? 152.075 134.037 106.451 1.00 20.45 ?  360 PHE A O     1 
ATOM   2918  C  CB    . PHE A 1 360 ? 152.126 131.169 106.133 1.00 14.32 ?  360 PHE A CB    1 
ATOM   2919  C  CG    . PHE A 1 360 ? 151.778 129.710 106.120 1.00 19.70 ?  360 PHE A CG    1 
ATOM   2920  C  CD1   . PHE A 1 360 ? 152.298 128.853 107.074 1.00 19.15 ?  360 PHE A CD1   1 
ATOM   2921  C  CD2   . PHE A 1 360 ? 150.912 129.199 105.171 1.00 14.52 ?  360 PHE A CD2   1 
ATOM   2922  C  CE1   . PHE A 1 360 ? 151.973 127.514 107.072 1.00 19.62 ?  360 PHE A CE1   1 
ATOM   2923  C  CE2   . PHE A 1 360 ? 150.584 127.862 105.164 1.00 15.20 ?  360 PHE A CE2   1 
ATOM   2924  C  CZ    . PHE A 1 360 ? 151.114 127.018 106.115 1.00 17.18 ?  360 PHE A CZ    1 
ATOM   2925  N  N     . GLN A 1 361 ? 152.659 133.773 108.616 1.00 17.83 ?  361 GLN A N     1 
ATOM   2926  C  CA    . GLN A 1 361 ? 152.835 135.199 108.871 1.00 10.93 ?  361 GLN A CA    1 
ATOM   2927  C  C     . GLN A 1 361 ? 153.843 135.826 107.917 1.00 17.63 ?  361 GLN A C     1 
ATOM   2928  O  O     . GLN A 1 361 ? 153.629 136.938 107.421 1.00 22.44 ?  361 GLN A O     1 
ATOM   2929  C  CB    . GLN A 1 361 ? 153.258 135.409 110.323 1.00 19.39 ?  361 GLN A CB    1 
ATOM   2930  C  CG    . GLN A 1 361 ? 153.878 136.758 110.618 1.00 22.88 ?  361 GLN A CG    1 
ATOM   2931  C  CD    . GLN A 1 361 ? 153.274 137.408 111.843 1.00 22.79 ?  361 GLN A CD    1 
ATOM   2932  O  OE1   . GLN A 1 361 ? 153.183 136.793 112.903 1.00 24.42 ?  361 GLN A OE1   1 
ATOM   2933  N  NE2   . GLN A 1 361 ? 152.852 138.658 111.703 1.00 23.32 ?  361 GLN A NE2   1 
ATOM   2934  N  N     . ASP A 1 362 ? 154.951 135.135 107.647 1.00 25.25 ?  362 ASP A N     1 
ATOM   2935  C  CA    . ASP A 1 362 ? 155.948 135.684 106.737 1.00 18.40 ?  362 ASP A CA    1 
ATOM   2936  C  C     . ASP A 1 362 ? 155.503 135.623 105.284 1.00 17.69 ?  362 ASP A C     1 
ATOM   2937  O  O     . ASP A 1 362 ? 156.016 136.388 104.462 1.00 28.33 ?  362 ASP A O     1 
ATOM   2938  C  CB    . ASP A 1 362 ? 157.280 134.960 106.910 1.00 24.85 ?  362 ASP A CB    1 
ATOM   2939  C  CG    . ASP A 1 362 ? 157.892 135.192 108.275 1.00 31.03 ?  362 ASP A CG    1 
ATOM   2940  O  OD1   . ASP A 1 362 ? 157.258 134.824 109.285 1.00 29.17 ?  362 ASP A OD1   1 
ATOM   2941  O  OD2   . ASP A 1 362 ? 159.004 135.754 108.336 1.00 33.69 -1 362 ASP A OD2   1 
ATOM   2942  N  N     . ASN A 1 363 ? 154.572 134.730 104.946 1.00 24.62 ?  363 ASN A N     1 
ATOM   2943  C  CA    . ASN A 1 363 ? 153.983 134.753 103.612 1.00 14.12 ?  363 ASN A CA    1 
ATOM   2944  C  C     . ASN A 1 363 ? 153.089 135.971 103.437 1.00 18.06 ?  363 ASN A C     1 
ATOM   2945  O  O     . ASN A 1 363 ? 153.017 136.548 102.347 1.00 28.52 ?  363 ASN A O     1 
ATOM   2946  C  CB    . ASN A 1 363 ? 153.194 133.469 103.363 1.00 12.26 ?  363 ASN A CB    1 
ATOM   2947  C  CG    . ASN A 1 363 ? 154.069 132.331 102.890 1.00 18.23 ?  363 ASN A CG    1 
ATOM   2948  O  OD1   . ASN A 1 363 ? 155.208 132.538 102.478 1.00 21.41 ?  363 ASN A OD1   1 
ATOM   2949  N  ND2   . ASN A 1 363 ? 153.541 131.116 102.948 1.00 20.23 ?  363 ASN A ND2   1 
ATOM   2950  N  N     . VAL A 1 364 ? 152.392 136.368 104.501 1.00 14.61 ?  364 VAL A N     1 
ATOM   2951  C  CA    . VAL A 1 364 ? 151.546 137.553 104.443 1.00 9.24  ?  364 VAL A CA    1 
ATOM   2952  C  C     . VAL A 1 364 ? 152.392 138.818 104.379 1.00 16.15 ?  364 VAL A C     1 
ATOM   2953  O  O     . VAL A 1 364 ? 152.096 139.740 103.613 1.00 19.34 ?  364 VAL A O     1 
ATOM   2954  C  CB    . VAL A 1 364 ? 150.590 137.578 105.648 1.00 1.23  ?  364 VAL A CB    1 
ATOM   2955  C  CG1   . VAL A 1 364 ? 149.630 138.742 105.532 1.00 9.60  ?  364 VAL A CG1   1 
ATOM   2956  C  CG2   . VAL A 1 364 ? 149.843 136.267 105.756 1.00 6.84  ?  364 VAL A CG2   1 
ATOM   2957  N  N     . ASN A 1 365 ? 153.459 138.879 105.175 1.00 22.21 ?  365 ASN A N     1 
ATOM   2958  C  CA    . ASN A 1 365 ? 154.165 140.131 105.402 1.00 11.29 ?  365 ASN A CA    1 
ATOM   2959  C  C     . ASN A 1 365 ? 155.307 140.383 104.431 1.00 14.01 ?  365 ASN A C     1 
ATOM   2960  O  O     . ASN A 1 365 ? 155.779 141.521 104.343 1.00 23.15 ?  365 ASN A O     1 
ATOM   2961  C  CB    . ASN A 1 365 ? 154.701 140.177 106.835 1.00 17.60 ?  365 ASN A CB    1 
ATOM   2962  C  CG    . ASN A 1 365 ? 153.626 140.522 107.840 1.00 16.59 ?  365 ASN A CG    1 
ATOM   2963  O  OD1   . ASN A 1 365 ? 152.935 141.528 107.701 1.00 22.15 ?  365 ASN A OD1   1 
ATOM   2964  N  ND2   . ASN A 1 365 ? 153.476 139.687 108.856 1.00 15.77 ?  365 ASN A ND2   1 
ATOM   2965  N  N     . LYS A 1 366 ? 155.769 139.364 103.705 1.00 19.65 ?  366 LYS A N     1 
ATOM   2966  C  CA    . LYS A 1 366 ? 156.794 139.605 102.698 1.00 22.10 ?  366 LYS A CA    1 
ATOM   2967  C  C     . LYS A 1 366 ? 156.237 140.335 101.486 1.00 24.85 ?  366 LYS A C     1 
ATOM   2968  O  O     . LYS A 1 366 ? 157.001 140.968 100.750 1.00 30.20 ?  366 LYS A O     1 
ATOM   2969  C  CB    . LYS A 1 366 ? 157.443 138.287 102.271 1.00 18.14 ?  366 LYS A CB    1 
ATOM   2970  C  CG    . LYS A 1 366 ? 156.551 137.380 101.446 1.00 27.92 ?  366 LYS A CG    1 
ATOM   2971  C  CD    . LYS A 1 366 ? 157.376 136.410 100.618 1.00 29.61 ?  366 LYS A CD    1 
ATOM   2972  C  CE    . LYS A 1 366 ? 157.874 135.247 101.461 1.00 24.39 ?  366 LYS A CE    1 
ATOM   2973  N  NZ    . LYS A 1 366 ? 159.057 134.586 100.843 1.00 31.12 1  366 LYS A NZ    1 
ATOM   2974  N  N     . VAL A 1 367 ? 154.924 140.266 101.271 1.00 24.91 ?  367 VAL A N     1 
ATOM   2975  C  CA    . VAL A 1 367 ? 154.249 140.995 100.207 1.00 13.81 ?  367 VAL A CA    1 
ATOM   2976  C  C     . VAL A 1 367 ? 153.301 142.053 100.743 1.00 21.55 ?  367 VAL A C     1 
ATOM   2977  O  O     . VAL A 1 367 ? 152.639 142.732 99.953  1.00 26.26 ?  367 VAL A O     1 
ATOM   2978  C  CB    . VAL A 1 367 ? 153.498 140.034 99.264  1.00 16.64 ?  367 VAL A CB    1 
ATOM   2979  C  CG1   . VAL A 1 367 ? 154.469 139.360 98.315  1.00 22.54 ?  367 VAL A CG1   1 
ATOM   2980  C  CG2   . VAL A 1 367 ? 152.743 138.998 100.068 1.00 13.91 ?  367 VAL A CG2   1 
ATOM   2981  N  N     . HIS A 1 368 ? 153.210 142.208 102.062 1.00 21.75 ?  368 HIS A N     1 
ATOM   2982  C  CA    . HIS A 1 368 ? 152.317 143.190 102.658 1.00 9.89  ?  368 HIS A CA    1 
ATOM   2983  C  C     . HIS A 1 368 ? 152.758 144.601 102.288 1.00 14.33 ?  368 HIS A C     1 
ATOM   2984  O  O     . HIS A 1 368 ? 153.938 144.946 102.404 1.00 24.79 ?  368 HIS A O     1 
ATOM   2985  C  CB    . HIS A 1 368 ? 152.292 143.017 104.173 1.00 8.77  ?  368 HIS A CB    1 
ATOM   2986  C  CG    . HIS A 1 368 ? 151.355 143.948 104.876 1.00 10.72 ?  368 HIS A CG    1 
ATOM   2987  N  ND1   . HIS A 1 368 ? 151.578 144.392 106.160 1.00 18.69 ?  368 HIS A ND1   1 
ATOM   2988  C  CD2   . HIS A 1 368 ? 150.191 144.512 104.479 1.00 6.90  ?  368 HIS A CD2   1 
ATOM   2989  C  CE1   . HIS A 1 368 ? 150.593 145.191 106.524 1.00 16.05 ?  368 HIS A CE1   1 
ATOM   2990  N  NE2   . HIS A 1 368 ? 149.738 145.282 105.521 1.00 10.79 ?  368 HIS A NE2   1 
ATOM   2991  N  N     . ALA A 1 369 ? 151.804 145.417 101.844 1.00 18.19 ?  369 ALA A N     1 
ATOM   2992  C  CA    . ALA A 1 369 ? 152.116 146.745 101.335 1.00 9.05  ?  369 ALA A CA    1 
ATOM   2993  C  C     . ALA A 1 369 ? 152.195 147.806 102.423 1.00 20.16 ?  369 ALA A C     1 
ATOM   2994  O  O     . ALA A 1 369 ? 152.703 148.901 102.160 1.00 24.96 ?  369 ALA A O     1 
ATOM   2995  C  CB    . ALA A 1 369 ? 151.075 147.160 100.296 1.00 14.58 ?  369 ALA A CB    1 
ATOM   2996  N  N     . ASN A 1 370 ? 151.718 147.516 103.629 1.00 19.06 ?  370 ASN A N     1 
ATOM   2997  C  CA    . ASN A 1 370 ? 151.619 148.507 104.694 1.00 9.80  ?  370 ASN A CA    1 
ATOM   2998  C  C     . ASN A 1 370 ? 152.306 148.011 105.954 1.00 8.58  ?  370 ASN A C     1 
ATOM   2999  O  O     . ASN A 1 370 ? 151.773 148.106 107.061 1.00 18.09 ?  370 ASN A O     1 
ATOM   3000  C  CB    . ASN A 1 370 ? 150.162 148.856 104.976 1.00 10.11 ?  370 ASN A CB    1 
ATOM   3001  C  CG    . ASN A 1 370 ? 149.450 149.403 103.762 1.00 12.97 ?  370 ASN A CG    1 
ATOM   3002  O  OD1   . ASN A 1 370 ? 149.872 150.399 103.180 1.00 28.26 ?  370 ASN A OD1   1 
ATOM   3003  N  ND2   . ASN A 1 370 ? 148.362 148.754 103.370 1.00 13.93 ?  370 ASN A ND2   1 
ATOM   3004  N  N     . ASN A 1 371 ? 153.513 147.467 105.802 1.00 17.89 ?  371 ASN A N     1 
ATOM   3005  C  CA    . ASN A 1 371 ? 154.278 147.038 106.967 1.00 11.60 ?  371 ASN A CA    1 
ATOM   3006  C  C     . ASN A 1 371 ? 154.760 148.215 107.802 1.00 19.41 ?  371 ASN A C     1 
ATOM   3007  O  O     . ASN A 1 371 ? 155.066 148.034 108.985 1.00 22.71 ?  371 ASN A O     1 
ATOM   3008  C  CB    . ASN A 1 371 ? 155.472 146.188 106.536 1.00 6.17  ?  371 ASN A CB    1 
ATOM   3009  C  CG    . ASN A 1 371 ? 155.106 144.738 106.317 1.00 15.84 ?  371 ASN A CG    1 
ATOM   3010  O  OD1   . ASN A 1 371 ? 154.123 144.245 106.865 1.00 23.36 ?  371 ASN A OD1   1 
ATOM   3011  N  ND2   . ASN A 1 371 ? 155.897 144.046 105.510 1.00 18.12 ?  371 ASN A ND2   1 
ATOM   3012  N  N     . HIS A 1 372 ? 154.842 149.409 107.211 1.00 20.00 ?  372 HIS A N     1 
ATOM   3013  C  CA    . HIS A 1 372 ? 155.202 150.596 107.979 1.00 17.08 ?  372 HIS A CA    1 
ATOM   3014  C  C     . HIS A 1 372 ? 154.154 150.901 109.041 1.00 20.55 ?  372 HIS A C     1 
ATOM   3015  O  O     . HIS A 1 372 ? 154.496 151.277 110.168 1.00 30.06 ?  372 HIS A O     1 
ATOM   3016  C  CB    . HIS A 1 372 ? 155.386 151.788 107.041 1.00 18.82 ?  372 HIS A CB    1 
ATOM   3017  C  CG    . HIS A 1 372 ? 154.117 152.247 106.396 1.00 19.92 ?  372 HIS A CG    1 
ATOM   3018  N  ND1   . HIS A 1 372 ? 153.379 151.444 105.554 1.00 19.60 ?  372 HIS A ND1   1 
ATOM   3019  C  CD2   . HIS A 1 372 ? 153.446 153.421 106.479 1.00 23.20 ?  372 HIS A CD2   1 
ATOM   3020  C  CE1   . HIS A 1 372 ? 152.313 152.104 105.141 1.00 18.35 ?  372 HIS A CE1   1 
ATOM   3021  N  NE2   . HIS A 1 372 ? 152.330 153.306 105.687 1.00 23.99 ?  372 HIS A NE2   1 
ATOM   3022  N  N     . ILE A 1 373 ? 152.873 150.762 108.698 1.00 14.86 ?  373 ILE A N     1 
ATOM   3023  C  CA    . ILE A 1 373 ? 151.819 150.926 109.690 1.00 16.32 ?  373 ILE A CA    1 
ATOM   3024  C  C     . ILE A 1 373 ? 151.918 149.835 110.746 1.00 19.30 ?  373 ILE A C     1 
ATOM   3025  O  O     . ILE A 1 373 ? 151.955 150.113 111.950 1.00 29.97 ?  373 ILE A O     1 
ATOM   3026  C  CB    . ILE A 1 373 ? 150.437 150.925 109.009 1.00 17.88 ?  373 ILE A CB    1 
ATOM   3027  C  CG1   . ILE A 1 373 ? 150.332 152.074 108.007 1.00 16.77 ?  373 ILE A CG1   1 
ATOM   3028  C  CG2   . ILE A 1 373 ? 149.328 151.012 110.044 1.00 17.56 ?  373 ILE A CG2   1 
ATOM   3029  C  CD1   . ILE A 1 373 ? 149.142 151.971 107.085 1.00 13.85 ?  373 ILE A CD1   1 
ATOM   3030  N  N     . SER A 1 374 ? 151.990 148.582 110.307 1.00 20.52 ?  374 SER A N     1 
ATOM   3031  C  CA    . SER A 1 374 ? 152.080 147.418 111.175 1.00 12.72 ?  374 SER A CA    1 
ATOM   3032  C  C     . SER A 1 374 ? 152.211 146.185 110.297 1.00 15.89 ?  374 SER A C     1 
ATOM   3033  O  O     . SER A 1 374 ? 151.865 146.208 109.113 1.00 16.80 ?  374 SER A O     1 
ATOM   3034  C  CB    . SER A 1 374 ? 150.859 147.285 112.086 1.00 17.29 ?  374 SER A CB    1 
ATOM   3035  O  OG    . SER A 1 374 ? 151.031 146.236 113.016 1.00 25.82 ?  374 SER A OG    1 
ATOM   3036  N  N     . LYS A 1 375 ? 152.715 145.111 110.888 1.00 22.63 ?  375 LYS A N     1 
ATOM   3037  C  CA    . LYS A 1 375 ? 152.678 143.814 110.235 1.00 15.46 ?  375 LYS A CA    1 
ATOM   3038  C  C     . LYS A 1 375 ? 151.331 143.149 110.480 1.00 14.23 ?  375 LYS A C     1 
ATOM   3039  O  O     . LYS A 1 375 ? 150.662 143.405 111.484 1.00 25.63 ?  375 LYS A O     1 
ATOM   3040  C  CB    . LYS A 1 375 ? 153.802 142.916 110.746 1.00 11.70 ?  375 LYS A CB    1 
ATOM   3041  C  CG    . LYS A 1 375 ? 155.178 143.537 110.665 1.00 19.34 ?  375 LYS A CG    1 
ATOM   3042  C  CD    . LYS A 1 375 ? 156.045 142.798 109.669 1.00 19.61 ?  375 LYS A CD    1 
ATOM   3043  C  CE    . LYS A 1 375 ? 157.346 143.530 109.411 1.00 20.30 ?  375 LYS A CE    1 
ATOM   3044  N  NZ    . LYS A 1 375 ? 158.058 142.975 108.229 1.00 25.16 1  375 LYS A NZ    1 
ATOM   3045  N  N     . VAL A 1 376 ? 150.930 142.294 109.544 1.00 11.48 ?  376 VAL A N     1 
ATOM   3046  C  CA    . VAL A 1 376 ? 149.711 141.520 109.734 1.00 17.46 ?  376 VAL A CA    1 
ATOM   3047  C  C     . VAL A 1 376 ? 149.990 140.439 110.768 1.00 14.05 ?  376 VAL A C     1 
ATOM   3048  O  O     . VAL A 1 376 ? 150.891 139.611 110.597 1.00 20.12 ?  376 VAL A O     1 
ATOM   3049  C  CB    . VAL A 1 376 ? 149.226 140.919 108.410 1.00 12.52 ?  376 VAL A CB    1 
ATOM   3050  C  CG1   . VAL A 1 376 ? 147.918 140.179 108.617 1.00 13.55 ?  376 VAL A CG1   1 
ATOM   3051  C  CG2   . VAL A 1 376 ? 149.069 142.004 107.365 1.00 3.43  ?  376 VAL A CG2   1 
ATOM   3052  N  N     . LYS A 1 377 ? 149.220 140.447 111.856 1.00 17.05 ?  377 LYS A N     1 
ATOM   3053  C  CA    . LYS A 1 377 ? 149.434 139.513 112.950 1.00 10.87 ?  377 LYS A CA    1 
ATOM   3054  C  C     . LYS A 1 377 ? 148.361 138.449 113.068 1.00 11.62 ?  377 LYS A C     1 
ATOM   3055  O  O     . LYS A 1 377 ? 148.582 137.457 113.766 1.00 27.28 ?  377 LYS A O     1 
ATOM   3056  C  CB    . LYS A 1 377 ? 149.525 140.260 114.287 1.00 13.24 ?  377 LYS A CB    1 
ATOM   3057  C  CG    . LYS A 1 377 ? 150.425 141.475 114.271 1.00 11.59 ?  377 LYS A CG    1 
ATOM   3058  C  CD    . LYS A 1 377 ? 149.988 142.461 115.331 1.00 22.02 ?  377 LYS A CD    1 
ATOM   3059  C  CE    . LYS A 1 377 ? 150.220 143.885 114.893 1.00 18.69 ?  377 LYS A CE    1 
ATOM   3060  N  NZ    . LYS A 1 377 ? 149.535 144.850 115.793 1.00 20.26 1  377 LYS A NZ    1 
ATOM   3061  N  N     . PHE A 1 378 ? 147.212 138.629 112.426 1.00 13.99 ?  378 PHE A N     1 
ATOM   3062  C  CA    . PHE A 1 378 ? 146.147 137.639 112.485 1.00 7.50  ?  378 PHE A CA    1 
ATOM   3063  C  C     . PHE A 1 378 ? 145.171 137.898 111.349 1.00 10.29 ?  378 PHE A C     1 
ATOM   3064  O  O     . PHE A 1 378 ? 145.185 138.962 110.725 1.00 18.96 ?  378 PHE A O     1 
ATOM   3065  C  CB    . PHE A 1 378 ? 145.433 137.644 113.846 1.00 6.96  ?  378 PHE A CB    1 
ATOM   3066  C  CG    . PHE A 1 378 ? 144.605 138.872 114.118 1.00 6.75  ?  378 PHE A CG    1 
ATOM   3067  C  CD1   . PHE A 1 378 ? 145.139 140.142 113.987 1.00 10.61 ?  378 PHE A CD1   1 
ATOM   3068  C  CD2   . PHE A 1 378 ? 143.294 138.747 114.539 1.00 4.93  ?  378 PHE A CD2   1 
ATOM   3069  C  CE1   . PHE A 1 378 ? 144.378 141.258 114.252 1.00 8.34  ?  378 PHE A CE1   1 
ATOM   3070  C  CE2   . PHE A 1 378 ? 142.530 139.860 114.806 1.00 10.30 ?  378 PHE A CE2   1 
ATOM   3071  C  CZ    . PHE A 1 378 ? 143.074 141.116 114.664 1.00 8.75  ?  378 PHE A CZ    1 
ATOM   3072  N  N     . SER A 1 379 ? 144.335 136.905 111.084 1.00 5.32  ?  379 SER A N     1 
ATOM   3073  C  CA    . SER A 1 379 ? 143.327 136.970 110.042 1.00 7.81  ?  379 SER A CA    1 
ATOM   3074  C  C     . SER A 1 379 ? 141.947 137.085 110.680 1.00 8.33  ?  379 SER A C     1 
ATOM   3075  O  O     . SER A 1 379 ? 141.811 137.225 111.899 1.00 16.72 ?  379 SER A O     1 
ATOM   3076  C  CB    . SER A 1 379 ? 143.436 135.752 109.123 1.00 13.39 ?  379 SER A CB    1 
ATOM   3077  O  OG    . SER A 1 379 ? 143.013 136.073 107.813 1.00 14.39 ?  379 SER A OG    1 
ATOM   3078  N  N     . ASN A 1 380 ? 140.916 137.042 109.845 1.00 8.33  ?  380 ASN A N     1 
ATOM   3079  C  CA    . ASN A 1 380 ? 139.545 137.193 110.296 1.00 7.79  ?  380 ASN A CA    1 
ATOM   3080  C  C     . ASN A 1 380 ? 138.917 135.824 110.548 1.00 16.69 ?  380 ASN A C     1 
ATOM   3081  O  O     . ASN A 1 380 ? 139.588 134.788 110.524 1.00 19.66 ?  380 ASN A O     1 
ATOM   3082  C  CB    . ASN A 1 380 ? 138.746 138.009 109.280 1.00 10.47 ?  380 ASN A CB    1 
ATOM   3083  C  CG    . ASN A 1 380 ? 138.622 137.316 107.944 1.00 7.14  ?  380 ASN A CG    1 
ATOM   3084  O  OD1   . ASN A 1 380 ? 139.577 136.726 107.446 1.00 18.25 ?  380 ASN A OD1   1 
ATOM   3085  N  ND2   . ASN A 1 380 ? 137.440 137.389 107.352 1.00 14.30 ?  380 ASN A ND2   1 
ATOM   3086  N  N     . LEU A 1 381 ? 137.609 135.819 110.805 1.00 17.42 ?  381 LEU A N     1 
ATOM   3087  C  CA    . LEU A 1 381 ? 136.896 134.567 111.031 1.00 10.98 ?  381 LEU A CA    1 
ATOM   3088  C  C     . LEU A 1 381 ? 136.863 133.706 109.775 1.00 10.10 ?  381 LEU A C     1 
ATOM   3089  O  O     . LEU A 1 381 ? 136.852 132.474 109.871 1.00 20.39 ?  381 LEU A O     1 
ATOM   3090  C  CB    . LEU A 1 381 ? 135.480 134.865 111.525 1.00 12.55 ?  381 LEU A CB    1 
ATOM   3091  C  CG    . LEU A 1 381 ? 134.480 133.716 111.646 1.00 14.65 ?  381 LEU A CG    1 
ATOM   3092  C  CD1   . LEU A 1 381 ? 134.830 132.806 112.808 1.00 16.28 ?  381 LEU A CD1   1 
ATOM   3093  C  CD2   . LEU A 1 381 ? 133.078 134.269 111.799 1.00 17.94 ?  381 LEU A CD2   1 
ATOM   3094  N  N     . CYS A 1 382 ? 136.848 134.325 108.600 1.00 18.94 ?  382 CYS A N     1 
ATOM   3095  C  CA    . CYS A 1 382 ? 136.890 133.597 107.341 1.00 13.00 ?  382 CYS A CA    1 
ATOM   3096  C  C     . CYS A 1 382 ? 138.309 133.390 106.829 1.00 7.71  ?  382 CYS A C     1 
ATOM   3097  O  O     . CYS A 1 382 ? 138.488 132.768 105.779 1.00 17.19 ?  382 CYS A O     1 
ATOM   3098  C  CB    . CYS A 1 382 ? 136.052 134.322 106.284 1.00 20.13 ?  382 CYS A CB    1 
ATOM   3099  S  SG    . CYS A 1 382 ? 134.349 134.649 106.788 1.00 26.50 ?  382 CYS A SG    1 
ATOM   3100  N  N     . SER A 1 383 ? 139.311 133.905 107.543 1.00 15.62 ?  383 SER A N     1 
ATOM   3101  C  CA    . SER A 1 383 ? 140.722 133.615 107.280 1.00 10.49 ?  383 SER A CA    1 
ATOM   3102  C  C     . SER A 1 383 ? 141.171 134.132 105.914 1.00 12.80 ?  383 SER A C     1 
ATOM   3103  O  O     . SER A 1 383 ? 141.965 133.496 105.222 1.00 26.33 ?  383 SER A O     1 
ATOM   3104  C  CB    . SER A 1 383 ? 141.006 132.117 107.415 1.00 16.56 ?  383 SER A CB    1 
ATOM   3105  O  OG    . SER A 1 383 ? 142.383 131.835 107.249 1.00 24.81 ?  383 SER A OG    1 
ATOM   3106  N  N     . GLU A 1 384 ? 140.664 135.299 105.518 1.00 14.02 ?  384 GLU A N     1 
ATOM   3107  C  CA    . GLU A 1 384 ? 141.122 135.916 104.278 1.00 5.78  ?  384 GLU A CA    1 
ATOM   3108  C  C     . GLU A 1 384 ? 141.431 137.401 104.395 1.00 14.42 ?  384 GLU A C     1 
ATOM   3109  O  O     . GLU A 1 384 ? 142.090 137.938 103.502 1.00 20.38 ?  384 GLU A O     1 
ATOM   3110  C  CB    . GLU A 1 384 ? 140.095 135.695 103.153 1.00 9.03  ?  384 GLU A CB    1 
ATOM   3111  C  CG    . GLU A 1 384 ? 139.260 136.901 102.755 1.00 10.86 ?  384 GLU A CG    1 
ATOM   3112  C  CD    . GLU A 1 384 ? 138.132 137.185 103.719 1.00 21.19 ?  384 GLU A CD    1 
ATOM   3113  O  OE1   . GLU A 1 384 ? 137.762 136.274 104.485 1.00 14.47 ?  384 GLU A OE1   1 
ATOM   3114  O  OE2   . GLU A 1 384 ? 137.601 138.312 103.695 1.00 27.61 -1 384 GLU A OE2   1 
ATOM   3115  N  N     . VAL A 1 385 ? 141.009 138.079 105.456 1.00 17.24 ?  385 VAL A N     1 
ATOM   3116  C  CA    . VAL A 1 385 ? 141.335 139.486 105.656 1.00 5.14  ?  385 VAL A CA    1 
ATOM   3117  C  C     . VAL A 1 385 ? 142.714 139.567 106.296 1.00 15.31 ?  385 VAL A C     1 
ATOM   3118  O  O     . VAL A 1 385 ? 142.936 139.027 107.384 1.00 23.18 ?  385 VAL A O     1 
ATOM   3119  C  CB    . VAL A 1 385 ? 140.283 140.185 106.527 1.00 7.09  ?  385 VAL A CB    1 
ATOM   3120  C  CG1   . VAL A 1 385 ? 140.727 141.592 106.836 1.00 8.27  ?  385 VAL A CG1   1 
ATOM   3121  C  CG2   . VAL A 1 385 ? 138.946 140.198 105.828 1.00 7.56  ?  385 VAL A CG2   1 
ATOM   3122  N  N     . LEU A 1 386 ? 143.643 140.242 105.618 1.00 16.57 ?  386 LEU A N     1 
ATOM   3123  C  CA    . LEU A 1 386 ? 145.037 140.339 106.049 1.00 2.61  ?  386 LEU A CA    1 
ATOM   3124  C  C     . LEU A 1 386 ? 145.468 141.797 105.938 1.00 5.27  ?  386 LEU A C     1 
ATOM   3125  O  O     . LEU A 1 386 ? 145.963 142.231 104.897 1.00 11.88 ?  386 LEU A O     1 
ATOM   3126  C  CB    . LEU A 1 386 ? 145.922 139.422 105.219 1.00 2.13  ?  386 LEU A CB    1 
ATOM   3127  C  CG    . LEU A 1 386 ? 145.667 137.932 105.442 1.00 6.65  ?  386 LEU A CG    1 
ATOM   3128  C  CD1   . LEU A 1 386 ? 146.514 137.113 104.510 1.00 10.46 ?  386 LEU A CD1   1 
ATOM   3129  C  CD2   . LEU A 1 386 ? 145.946 137.557 106.885 1.00 13.82 ?  386 LEU A CD2   1 
ATOM   3130  N  N     . GLN A 1 387 ? 145.283 142.546 107.022 1.00 14.61 ?  387 GLN A N     1 
ATOM   3131  C  CA    . GLN A 1 387 ? 145.557 143.972 107.049 1.00 10.55 ?  387 GLN A CA    1 
ATOM   3132  C  C     . GLN A 1 387 ? 146.353 144.324 108.297 1.00 12.82 ?  387 GLN A C     1 
ATOM   3133  O  O     . GLN A 1 387 ? 146.360 143.589 109.286 1.00 25.68 ?  387 GLN A O     1 
ATOM   3134  C  CB    . GLN A 1 387 ? 144.259 144.790 107.009 1.00 3.94  ?  387 GLN A CB    1 
ATOM   3135  C  CG    . GLN A 1 387 ? 143.351 144.446 105.849 1.00 7.66  ?  387 GLN A CG    1 
ATOM   3136  C  CD    . GLN A 1 387 ? 142.117 145.307 105.806 1.00 9.54  ?  387 GLN A CD    1 
ATOM   3137  O  OE1   . GLN A 1 387 ? 142.043 146.334 106.476 1.00 26.99 ?  387 GLN A OE1   1 
ATOM   3138  N  NE2   . GLN A 1 387 ? 141.134 144.896 105.018 1.00 13.40 ?  387 GLN A NE2   1 
ATOM   3139  N  N     . ALA A 1 388 ? 147.037 145.463 108.233 1.00 12.69 ?  388 ALA A N     1 
ATOM   3140  C  CA    . ALA A 1 388 ? 147.792 145.951 109.377 1.00 10.57 ?  388 ALA A CA    1 
ATOM   3141  C  C     . ALA A 1 388 ? 146.849 146.436 110.470 1.00 13.36 ?  388 ALA A C     1 
ATOM   3142  O  O     . ALA A 1 388 ? 145.835 147.083 110.199 1.00 25.27 ?  388 ALA A O     1 
ATOM   3143  C  CB    . ALA A 1 388 ? 148.726 147.081 108.951 1.00 11.56 ?  388 ALA A CB    1 
ATOM   3144  N  N     . SER A 1 389 ? 147.186 146.116 111.715 1.00 19.36 ?  389 SER A N     1 
ATOM   3145  C  CA    . SER A 1 389 ? 146.404 146.536 112.866 1.00 13.85 ?  389 SER A CA    1 
ATOM   3146  C  C     . SER A 1 389 ? 147.324 147.088 113.941 1.00 15.70 ?  389 SER A C     1 
ATOM   3147  O  O     . SER A 1 389 ? 148.466 146.647 114.093 1.00 23.18 ?  389 SER A O     1 
ATOM   3148  C  CB    . SER A 1 389 ? 145.575 145.382 113.446 1.00 14.60 ?  389 SER A CB    1 
ATOM   3149  O  OG    . SER A 1 389 ? 146.381 144.245 113.695 1.00 25.24 ?  389 SER A OG    1 
ATOM   3150  N  N     . GLN A 1 390 ? 146.813 148.061 114.688 1.00 17.82 ?  390 GLN A N     1 
ATOM   3151  C  CA    . GLN A 1 390 ? 147.503 148.621 115.841 1.00 14.43 ?  390 GLN A CA    1 
ATOM   3152  C  C     . GLN A 1 390 ? 146.616 148.445 117.062 1.00 14.63 ?  390 GLN A C     1 
ATOM   3153  O  O     . GLN A 1 390 ? 145.438 148.812 117.034 1.00 27.28 ?  390 GLN A O     1 
ATOM   3154  C  CB    . GLN A 1 390 ? 147.836 150.098 115.623 1.00 17.79 ?  390 GLN A CB    1 
ATOM   3155  C  CG    . GLN A 1 390 ? 148.857 150.338 114.530 1.00 17.56 ?  390 GLN A CG    1 
ATOM   3156  C  CD    . GLN A 1 390 ? 149.021 151.804 114.195 1.00 22.86 ?  390 GLN A CD    1 
ATOM   3157  O  OE1   . GLN A 1 390 ? 148.258 152.649 114.662 1.00 31.19 ?  390 GLN A OE1   1 
ATOM   3158  N  NE2   . GLN A 1 390 ? 150.024 152.116 113.385 1.00 21.59 ?  390 GLN A NE2   1 
ATOM   3159  N  N     . VAL A 1 391 ? 147.180 147.875 118.127 1.00 23.96 ?  391 VAL A N     1 
ATOM   3160  C  CA    . VAL A 1 391 ? 146.389 147.576 119.312 1.00 24.92 ?  391 VAL A CA    1 
ATOM   3161  C  C     . VAL A 1 391 ? 145.999 148.868 120.021 1.00 25.86 ?  391 VAL A C     1 
ATOM   3162  O  O     . VAL A 1 391 ? 146.733 149.865 120.011 1.00 26.45 ?  391 VAL A O     1 
ATOM   3163  C  CB    . VAL A 1 391 ? 147.156 146.624 120.251 1.00 15.46 ?  391 VAL A CB    1 
ATOM   3164  C  CG1   . VAL A 1 391 ? 148.231 147.368 121.026 1.00 21.40 ?  391 VAL A CG1   1 
ATOM   3165  C  CG2   . VAL A 1 391 ? 146.198 145.921 121.196 1.00 16.26 ?  391 VAL A CG2   1 
ATOM   3166  N  N     . SER A 1 392 ? 144.813 148.860 120.616 1.00 28.22 ?  392 SER A N     1 
ATOM   3167  C  CA    . SER A 1 392 ? 144.334 149.984 121.399 1.00 18.16 ?  392 SER A CA    1 
ATOM   3168  C  C     . SER A 1 392 ? 144.758 149.830 122.855 1.00 27.95 ?  392 SER A C     1 
ATOM   3169  O  O     . SER A 1 392 ? 145.080 148.736 123.324 1.00 36.07 ?  392 SER A O     1 
ATOM   3170  C  CB    . SER A 1 392 ? 142.813 150.103 121.306 1.00 24.73 ?  392 SER A CB    1 
ATOM   3171  O  OG    . SER A 1 392 ? 142.403 150.410 119.987 1.00 33.95 ?  392 SER A OG    1 
ATOM   3172  N  N     . SER A 1 393 ? 144.758 150.949 123.570 1.00 33.60 ?  393 SER A N     1 
ATOM   3173  C  CA    . SER A 1 393 ? 145.095 150.981 124.989 1.00 31.95 ?  393 SER A CA    1 
ATOM   3174  C  C     . SER A 1 393 ? 143.883 151.539 125.729 1.00 32.73 ?  393 SER A C     1 
ATOM   3175  O  O     . SER A 1 393 ? 143.798 152.742 125.986 1.00 34.99 ?  393 SER A O     1 
ATOM   3176  C  CB    . SER A 1 393 ? 146.347 151.812 125.242 1.00 31.84 ?  393 SER A CB    1 
ATOM   3177  O  OG    . SER A 1 393 ? 147.112 151.270 126.303 1.00 39.31 ?  393 SER A OG    1 
ATOM   3178  N  N     . TYR A 1 394 ? 142.948 150.659 126.068 1.00 34.05 ?  394 TYR A N     1 
ATOM   3179  C  CA    . TYR A 1 394 ? 141.764 151.056 126.817 1.00 31.62 ?  394 TYR A CA    1 
ATOM   3180  C  C     . TYR A 1 394 ? 142.129 151.170 128.290 1.00 35.26 ?  394 TYR A C     1 
ATOM   3181  O  O     . TYR A 1 394 ? 142.514 150.180 128.921 1.00 37.43 ?  394 TYR A O     1 
ATOM   3182  C  CB    . TYR A 1 394 ? 140.634 150.054 126.604 1.00 28.57 ?  394 TYR A CB    1 
ATOM   3183  C  CG    . TYR A 1 394 ? 140.160 149.977 125.170 1.00 30.05 ?  394 TYR A CG    1 
ATOM   3184  C  CD1   . TYR A 1 394 ? 139.430 151.014 124.605 1.00 31.16 ?  394 TYR A CD1   1 
ATOM   3185  C  CD2   . TYR A 1 394 ? 140.448 148.874 124.381 1.00 31.12 ?  394 TYR A CD2   1 
ATOM   3186  C  CE1   . TYR A 1 394 ? 138.998 150.950 123.298 1.00 33.30 ?  394 TYR A CE1   1 
ATOM   3187  C  CE2   . TYR A 1 394 ? 140.019 148.800 123.074 1.00 30.57 ?  394 TYR A CE2   1 
ATOM   3188  C  CZ    . TYR A 1 394 ? 139.295 149.841 122.537 1.00 37.78 ?  394 TYR A CZ    1 
ATOM   3189  O  OH    . TYR A 1 394 ? 138.868 149.771 121.230 1.00 39.81 ?  394 TYR A OH    1 
ATOM   3190  N  N     . THR A 1 395 ? 142.014 152.374 128.832 1.00 34.33 ?  395 THR A N     1 
ATOM   3191  C  CA    . THR A 1 395 ? 142.457 152.689 130.177 1.00 36.56 ?  395 THR A CA    1 
ATOM   3192  C  C     . THR A 1 395 ? 141.267 152.681 131.134 1.00 37.82 ?  395 THR A C     1 
ATOM   3193  O  O     . THR A 1 395 ? 140.163 152.250 130.787 1.00 34.94 ?  395 THR A O     1 
ATOM   3194  C  CB    . THR A 1 395 ? 143.183 154.035 130.174 1.00 35.93 ?  395 THR A CB    1 
ATOM   3195  O  OG1   . THR A 1 395 ? 142.304 155.049 129.673 1.00 37.71 ?  395 THR A OG1   1 
ATOM   3196  C  CG2   . THR A 1 395 ? 144.412 153.965 129.287 1.00 34.69 ?  395 THR A CG2   1 
ATOM   3197  N  N     . ASP A 1 396 ? 141.496 153.146 132.360 1.00 39.46 ?  396 ASP A N     1 
ATOM   3198  C  CA    . ASP A 1 396 ? 140.436 153.227 133.351 1.00 35.04 ?  396 ASP A CA    1 
ATOM   3199  C  C     . ASP A 1 396 ? 139.321 154.156 132.871 1.00 37.72 ?  396 ASP A C     1 
ATOM   3200  O  O     . ASP A 1 396 ? 139.452 154.875 131.879 1.00 43.75 ?  396 ASP A O     1 
ATOM   3201  C  CB    . ASP A 1 396 ? 140.990 153.711 134.690 1.00 37.84 ?  396 ASP A CB    1 
ATOM   3202  C  CG    . ASP A 1 396 ? 141.997 152.748 135.287 1.00 43.06 ?  396 ASP A CG    1 
ATOM   3203  O  OD1   . ASP A 1 396 ? 141.680 151.544 135.390 1.00 40.24 ?  396 ASP A OD1   1 
ATOM   3204  O  OD2   . ASP A 1 396 ? 143.102 153.193 135.656 1.00 44.39 -1 396 ASP A OD2   1 
ATOM   3205  N  N     . TYR A 1 397 ? 138.204 154.126 133.601 1.00 35.15 ?  397 TYR A N     1 
ATOM   3206  C  CA    . TYR A 1 397 ? 137.029 154.889 133.193 1.00 35.34 ?  397 TYR A CA    1 
ATOM   3207  C  C     . TYR A 1 397 ? 137.325 156.382 133.132 1.00 36.99 ?  397 TYR A C     1 
ATOM   3208  O  O     . TYR A 1 397 ? 136.900 157.069 132.196 1.00 41.13 ?  397 TYR A O     1 
ATOM   3209  C  CB    . TYR A 1 397 ? 135.869 154.613 134.149 1.00 30.96 ?  397 TYR A CB    1 
ATOM   3210  C  CG    . TYR A 1 397 ? 134.587 155.317 133.771 1.00 33.12 ?  397 TYR A CG    1 
ATOM   3211  C  CD1   . TYR A 1 397 ? 133.699 154.745 132.872 1.00 33.56 ?  397 TYR A CD1   1 
ATOM   3212  C  CD2   . TYR A 1 397 ? 134.269 156.558 134.309 1.00 34.28 ?  397 TYR A CD2   1 
ATOM   3213  C  CE1   . TYR A 1 397 ? 132.530 155.387 132.521 1.00 29.73 ?  397 TYR A CE1   1 
ATOM   3214  C  CE2   . TYR A 1 397 ? 133.104 157.205 133.962 1.00 33.91 ?  397 TYR A CE2   1 
ATOM   3215  C  CZ    . TYR A 1 397 ? 132.238 156.616 133.070 1.00 34.95 ?  397 TYR A CZ    1 
ATOM   3216  O  OH    . TYR A 1 397 ? 131.074 157.260 132.725 1.00 39.62 ?  397 TYR A OH    1 
ATOM   3217  N  N     . ASP A 1 398 ? 138.054 156.902 134.116 1.00 40.12 ?  398 ASP A N     1 
ATOM   3218  C  CA    . ASP A 1 398 ? 138.336 158.328 134.186 1.00 39.48 ?  398 ASP A CA    1 
ATOM   3219  C  C     . ASP A 1 398 ? 139.386 158.786 133.183 1.00 45.32 ?  398 ASP A C     1 
ATOM   3220  O  O     . ASP A 1 398 ? 139.478 159.989 132.918 1.00 46.74 ?  398 ASP A O     1 
ATOM   3221  C  CB    . ASP A 1 398 ? 138.787 158.700 135.601 1.00 43.35 ?  398 ASP A CB    1 
ATOM   3222  C  CG    . ASP A 1 398 ? 139.671 157.638 136.227 1.00 46.91 ?  398 ASP A CG    1 
ATOM   3223  O  OD1   . ASP A 1 398 ? 139.167 156.529 136.498 1.00 43.86 ?  398 ASP A OD1   1 
ATOM   3224  O  OD2   . ASP A 1 398 ? 140.869 157.910 136.449 1.00 45.84 -1 398 ASP A OD2   1 
ATOM   3225  N  N     . GLU A 1 399 ? 140.171 157.872 132.622 1.00 46.09 ?  399 GLU A N     1 
ATOM   3226  C  CA    . GLU A 1 399 ? 141.274 158.222 131.742 1.00 42.81 ?  399 GLU A CA    1 
ATOM   3227  C  C     . GLU A 1 399 ? 140.872 158.086 130.278 1.00 45.49 ?  399 GLU A C     1 
ATOM   3228  O  O     . GLU A 1 399 ? 139.944 157.355 129.924 1.00 45.00 ?  399 GLU A O     1 
ATOM   3229  C  CB    . GLU A 1 399 ? 142.493 157.343 132.028 1.00 42.35 ?  399 GLU A CB    1 
ATOM   3230  C  CG    . GLU A 1 399 ? 142.585 156.853 133.458 1.00 44.59 ?  399 GLU A CG    1 
ATOM   3231  C  CD    . GLU A 1 399 ? 143.945 156.274 133.787 1.00 50.14 ?  399 GLU A CD    1 
ATOM   3232  O  OE1   . GLU A 1 399 ? 144.224 155.132 133.364 1.00 46.87 ?  399 GLU A OE1   1 
ATOM   3233  O  OE2   . GLU A 1 399 ? 144.735 156.959 134.469 1.00 49.31 -1 399 GLU A OE2   1 
ATOM   3234  N  N     . GLU A 1 400 ? 141.592 158.813 129.427 1.00 43.20 ?  400 GLU A N     1 
ATOM   3235  C  CA    . GLU A 1 400 ? 141.370 158.733 127.991 1.00 40.44 ?  400 GLU A CA    1 
ATOM   3236  C  C     . GLU A 1 400 ? 141.992 157.462 127.425 1.00 41.95 ?  400 GLU A C     1 
ATOM   3237  O  O     . GLU A 1 400 ? 143.049 157.014 127.873 1.00 41.73 ?  400 GLU A O     1 
ATOM   3238  C  CB    . GLU A 1 400 ? 141.958 159.959 127.294 1.00 40.61 ?  400 GLU A CB    1 
ATOM   3239  C  CG    . GLU A 1 400 ? 141.121 161.217 127.435 1.00 44.10 ?  400 GLU A CG    1 
ATOM   3240  C  CD    . GLU A 1 400 ? 140.129 161.387 126.302 1.00 49.46 ?  400 GLU A CD    1 
ATOM   3241  O  OE1   . GLU A 1 400 ? 139.045 161.959 126.540 1.00 45.54 ?  400 GLU A OE1   1 
ATOM   3242  O  OE2   . GLU A 1 400 ? 140.431 160.947 125.174 1.00 49.57 -1 400 GLU A OE2   1 
ATOM   3243  N  N     . ASP A 1 401 ? 141.324 156.881 126.433 1.00 39.60 ?  401 ASP A N     1 
ATOM   3244  C  CA    . ASP A 1 401 ? 141.797 155.662 125.795 1.00 36.96 ?  401 ASP A CA    1 
ATOM   3245  C  C     . ASP A 1 401 ? 142.629 155.994 124.566 1.00 37.21 ?  401 ASP A C     1 
ATOM   3246  O  O     . ASP A 1 401 ? 142.328 156.938 123.831 1.00 39.03 ?  401 ASP A O     1 
ATOM   3247  C  CB    . ASP A 1 401 ? 140.623 154.769 125.396 1.00 35.70 ?  401 ASP A CB    1 
ATOM   3248  C  CG    . ASP A 1 401 ? 139.737 154.409 126.570 1.00 39.29 ?  401 ASP A CG    1 
ATOM   3249  O  OD1   . ASP A 1 401 ? 140.247 154.350 127.707 1.00 41.78 ?  401 ASP A OD1   1 
ATOM   3250  O  OD2   . ASP A 1 401 ? 138.529 154.182 126.354 1.00 40.69 -1 401 ASP A OD2   1 
ATOM   3251  N  N     . GLU A 1 402 ? 143.684 155.212 124.350 1.00 33.55 ?  402 GLU A N     1 
ATOM   3252  C  CA    . GLU A 1 402 ? 144.489 155.304 123.138 1.00 32.92 ?  402 GLU A CA    1 
ATOM   3253  C  C     . GLU A 1 402 ? 143.898 154.350 122.108 1.00 31.86 ?  402 GLU A C     1 
ATOM   3254  O  O     . GLU A 1 402 ? 144.059 153.131 122.216 1.00 39.81 ?  402 GLU A O     1 
ATOM   3255  C  CB    . GLU A 1 402 ? 145.950 154.969 123.426 1.00 36.93 ?  402 GLU A CB    1 
ATOM   3256  C  CG    . GLU A 1 402 ? 146.640 155.943 124.361 1.00 36.37 ?  402 GLU A CG    1 
ATOM   3257  C  CD    . GLU A 1 402 ? 147.486 155.246 125.409 1.00 43.09 ?  402 GLU A CD    1 
ATOM   3258  O  OE1   . GLU A 1 402 ? 148.664 154.946 125.122 1.00 43.53 ?  402 GLU A OE1   1 
ATOM   3259  O  OE2   . GLU A 1 402 ? 146.973 155.000 126.521 1.00 43.84 -1 402 GLU A OE2   1 
ATOM   3260  N  N     . ILE A 1 403 ? 143.212 154.900 121.116 1.00 29.35 ?  403 ILE A N     1 
ATOM   3261  C  CA    . ILE A 1 403 ? 142.501 154.104 120.124 1.00 30.38 ?  403 ILE A CA    1 
ATOM   3262  C  C     . ILE A 1 403 ? 143.469 153.696 119.023 1.00 29.83 ?  403 ILE A C     1 
ATOM   3263  O  O     . ILE A 1 403 ? 144.149 154.544 118.433 1.00 31.37 ?  403 ILE A O     1 
ATOM   3264  C  CB    . ILE A 1 403 ? 141.308 154.886 119.550 1.00 27.23 ?  403 ILE A CB    1 
ATOM   3265  C  CG1   . ILE A 1 403 ? 140.286 155.180 120.652 1.00 30.31 ?  403 ILE A CG1   1 
ATOM   3266  C  CG2   . ILE A 1 403 ? 140.667 154.119 118.409 1.00 22.57 ?  403 ILE A CG2   1 
ATOM   3267  C  CD1   . ILE A 1 403 ? 139.931 153.977 121.497 1.00 30.63 ?  403 ILE A CD1   1 
ATOM   3268  N  N     . GLY A 1 404 ? 143.532 152.396 118.746 1.00 24.83 ?  404 GLY A N     1 
ATOM   3269  C  CA    . GLY A 1 404 ? 144.378 151.881 117.688 1.00 15.92 ?  404 GLY A CA    1 
ATOM   3270  C  C     . GLY A 1 404 ? 143.642 151.699 116.378 1.00 22.98 ?  404 GLY A C     1 
ATOM   3271  O  O     . GLY A 1 404 ? 142.748 152.482 116.048 1.00 33.56 ?  404 GLY A O     1 
ATOM   3272  N  N     . LEU A 1 405 ? 144.010 150.669 115.617 1.00 21.63 ?  405 LEU A N     1 
ATOM   3273  C  CA    . LEU A 1 405 ? 143.397 150.381 114.325 1.00 8.88  ?  405 LEU A CA    1 
ATOM   3274  C  C     . LEU A 1 405 ? 142.915 148.937 114.326 1.00 15.28 ?  405 LEU A C     1 
ATOM   3275  O  O     . LEU A 1 405 ? 143.729 148.009 114.339 1.00 16.33 ?  405 LEU A O     1 
ATOM   3276  C  CB    . LEU A 1 405 ? 144.381 150.620 113.179 1.00 18.00 ?  405 LEU A CB    1 
ATOM   3277  C  CG    . LEU A 1 405 ? 144.914 152.038 112.979 1.00 17.66 ?  405 LEU A CG    1 
ATOM   3278  C  CD1   . LEU A 1 405 ? 146.025 152.039 111.946 1.00 18.80 ?  405 LEU A CD1   1 
ATOM   3279  C  CD2   . LEU A 1 405 ? 143.803 152.986 112.574 1.00 16.03 ?  405 LEU A CD2   1 
ATOM   3280  N  N     . ASP A 1 406 ? 141.600 148.749 114.308 1.00 23.95 ?  406 ASP A N     1 
ATOM   3281  C  CA    . ASP A 1 406 ? 140.998 147.426 114.222 1.00 12.97 ?  406 ASP A CA    1 
ATOM   3282  C  C     . ASP A 1 406 ? 140.444 147.208 112.822 1.00 17.53 ?  406 ASP A C     1 
ATOM   3283  O  O     . ASP A 1 406 ? 139.750 148.068 112.273 1.00 31.72 ?  406 ASP A O     1 
ATOM   3284  C  CB    . ASP A 1 406 ? 139.891 147.256 115.262 1.00 16.10 ?  406 ASP A CB    1 
ATOM   3285  C  CG    . ASP A 1 406 ? 140.426 146.859 116.625 1.00 30.19 ?  406 ASP A CG    1 
ATOM   3286  O  OD1   . ASP A 1 406 ? 141.634 146.563 116.734 1.00 30.73 ?  406 ASP A OD1   1 
ATOM   3287  O  OD2   . ASP A 1 406 ? 139.639 146.850 117.594 1.00 30.34 -1 406 ASP A OD2   1 
ATOM   3288  N  N     . ILE A 1 407 ? 140.733 146.047 112.258 1.00 23.30 ?  407 ILE A N     1 
ATOM   3289  C  CA    . ILE A 1 407 ? 140.505 145.808 110.839 1.00 17.70 ?  407 ILE A CA    1 
ATOM   3290  C  C     . ILE A 1 407 ? 139.029 145.545 110.573 1.00 18.01 ?  407 ILE A C     1 
ATOM   3291  O  O     . ILE A 1 407 ? 138.339 144.887 111.361 1.00 21.33 ?  407 ILE A O     1 
ATOM   3292  C  CB    . ILE A 1 407 ? 141.374 144.634 110.356 1.00 13.02 ?  407 ILE A CB    1 
ATOM   3293  C  CG1   . ILE A 1 407 ? 142.852 144.914 110.618 1.00 2.81  ?  407 ILE A CG1   1 
ATOM   3294  C  CG2   . ILE A 1 407 ? 141.144 144.371 108.895 1.00 16.48 ?  407 ILE A CG2   1 
ATOM   3295  C  CD1   . ILE A 1 407 ? 143.616 143.696 111.043 1.00 18.29 ?  407 ILE A CD1   1 
ATOM   3296  N  N     . SER A 1 408 ? 138.547 146.069 109.449 1.00 27.38 ?  408 SER A N     1 
ATOM   3297  C  CA    . SER A 1 408 ? 137.246 145.726 108.895 1.00 20.37 ?  408 SER A CA    1 
ATOM   3298  C  C     . SER A 1 408 ? 137.234 146.166 107.439 1.00 24.30 ?  408 SER A C     1 
ATOM   3299  O  O     . SER A 1 408 ? 137.678 147.272 107.121 1.00 36.21 ?  408 SER A O     1 
ATOM   3300  C  CB    . SER A 1 408 ? 136.101 146.391 109.668 1.00 21.57 ?  408 SER A CB    1 
ATOM   3301  O  OG    . SER A 1 408 ? 135.769 147.651 109.114 1.00 28.81 ?  408 SER A OG    1 
ATOM   3302  N  N     . CYS A 1 409 ? 136.741 145.300 106.560 1.00 20.11 ?  409 CYS A N     1 
ATOM   3303  C  CA    . CYS A 1 409 ? 136.641 145.625 105.146 1.00 26.27 ?  409 CYS A CA    1 
ATOM   3304  C  C     . CYS A 1 409 ? 135.295 145.169 104.603 1.00 26.33 ?  409 CYS A C     1 
ATOM   3305  O  O     . CYS A 1 409 ? 134.690 144.213 105.092 1.00 24.50 ?  409 CYS A O     1 
ATOM   3306  C  CB    . CYS A 1 409 ? 137.787 145.000 104.332 1.00 22.59 ?  409 CYS A CB    1 
ATOM   3307  S  SG    . CYS A 1 409 ? 137.680 143.218 104.078 1.00 39.49 ?  409 CYS A SG    1 
ATOM   3308  N  N     . ASN A 1 410 ? 134.830 145.882 103.582 1.00 22.83 ?  410 ASN A N     1 
ATOM   3309  C  CA    . ASN A 1 410 ? 133.583 145.555 102.911 1.00 18.43 ?  410 ASN A CA    1 
ATOM   3310  C  C     . ASN A 1 410 ? 133.864 144.555 101.803 1.00 20.75 ?  410 ASN A C     1 
ATOM   3311  O  O     . ASN A 1 410 ? 134.810 144.725 101.029 1.00 22.15 ?  410 ASN A O     1 
ATOM   3312  C  CB    . ASN A 1 410 ? 132.929 146.806 102.331 1.00 22.82 ?  410 ASN A CB    1 
ATOM   3313  C  CG    . ASN A 1 410 ? 133.618 148.071 102.765 1.00 30.14 ?  410 ASN A CG    1 
ATOM   3314  O  OD1   . ASN A 1 410 ? 134.111 148.173 103.888 1.00 31.24 ?  410 ASN A OD1   1 
ATOM   3315  N  ND2   . ASN A 1 410 ? 133.672 149.044 101.870 1.00 28.88 ?  410 ASN A ND2   1 
ATOM   3316  N  N     . LEU A 1 411 ? 133.038 143.522 101.726 1.00 17.79 ?  411 LEU A N     1 
ATOM   3317  C  CA    . LEU A 1 411 ? 133.250 142.426 100.798 1.00 12.06 ?  411 LEU A CA    1 
ATOM   3318  C  C     . LEU A 1 411 ? 132.405 142.614 99.546  1.00 13.10 ?  411 LEU A C     1 
ATOM   3319  O  O     . LEU A 1 411 ? 131.317 143.193 99.585  1.00 19.18 ?  411 LEU A O     1 
ATOM   3320  C  CB    . LEU A 1 411 ? 132.911 141.092 101.463 1.00 21.93 ?  411 LEU A CB    1 
ATOM   3321  C  CG    . LEU A 1 411 ? 133.646 140.756 102.758 1.00 14.94 ?  411 LEU A CG    1 
ATOM   3322  C  CD1   . LEU A 1 411 ? 133.579 139.272 103.014 1.00 20.54 ?  411 LEU A CD1   1 
ATOM   3323  C  CD2   . LEU A 1 411 ? 135.091 141.205 102.689 1.00 19.17 ?  411 LEU A CD2   1 
ATOM   3324  N  N     . GLY A 1 412 ? 132.927 142.119 98.430  1.00 21.24 ?  412 GLY A N     1 
ATOM   3325  C  CA    . GLY A 1 412 ? 132.215 142.120 97.171  1.00 10.26 ?  412 GLY A CA    1 
ATOM   3326  C  C     . GLY A 1 412 ? 132.907 141.202 96.190  1.00 11.55 ?  412 GLY A C     1 
ATOM   3327  O  O     . GLY A 1 412 ? 134.139 141.182 96.129  1.00 25.53 ?  412 GLY A O     1 
ATOM   3328  N  N     . SER A 1 413 ? 132.144 140.435 95.420  1.00 15.23 ?  413 SER A N     1 
ATOM   3329  C  CA    . SER A 1 413 ? 132.705 139.415 94.548  1.00 9.33  ?  413 SER A CA    1 
ATOM   3330  C  C     . SER A 1 413 ? 132.383 139.719 93.095  1.00 15.97 ?  413 SER A C     1 
ATOM   3331  O  O     . SER A 1 413 ? 131.234 140.025 92.760  1.00 24.07 ?  413 SER A O     1 
ATOM   3332  C  CB    . SER A 1 413 ? 132.179 138.030 94.918  1.00 10.90 ?  413 SER A CB    1 
ATOM   3333  O  OG    . SER A 1 413 ? 132.718 137.603 96.152  1.00 29.53 ?  413 SER A OG    1 
ATOM   3334  N  N     . LEU A 1 414 ? 133.397 139.634 92.242  1.00 20.43 ?  414 LEU A N     1 
ATOM   3335  C  CA    . LEU A 1 414 ? 133.175 139.578 90.808  1.00 13.30 ?  414 LEU A CA    1 
ATOM   3336  C  C     . LEU A 1 414 ? 132.765 138.168 90.414  1.00 21.18 ?  414 LEU A C     1 
ATOM   3337  O  O     . LEU A 1 414 ? 133.294 137.185 90.938  1.00 21.96 ?  414 LEU A O     1 
ATOM   3338  C  CB    . LEU A 1 414 ? 134.437 139.977 90.045  1.00 14.83 ?  414 LEU A CB    1 
ATOM   3339  C  CG    . LEU A 1 414 ? 135.201 141.218 90.494  1.00 19.22 ?  414 LEU A CG    1 
ATOM   3340  C  CD1   . LEU A 1 414 ? 136.509 141.309 89.735  1.00 24.86 ?  414 LEU A CD1   1 
ATOM   3341  C  CD2   . LEU A 1 414 ? 134.365 142.463 90.274  1.00 24.81 ?  414 LEU A CD2   1 
ATOM   3342  N  N     . ASN A 1 415 ? 131.818 138.067 89.491  1.00 28.22 ?  415 ASN A N     1 
ATOM   3343  C  CA    . ASN A 1 415 ? 131.467 136.787 88.892  1.00 25.19 ?  415 ASN A CA    1 
ATOM   3344  C  C     . ASN A 1 415 ? 132.359 136.592 87.675  1.00 27.36 ?  415 ASN A C     1 
ATOM   3345  O  O     . ASN A 1 415 ? 132.167 137.247 86.647  1.00 29.83 ?  415 ASN A O     1 
ATOM   3346  C  CB    . ASN A 1 415 ? 129.989 136.746 88.520  1.00 20.33 ?  415 ASN A CB    1 
ATOM   3347  C  CG    . ASN A 1 415 ? 129.471 135.337 88.332  1.00 23.73 ?  415 ASN A CG    1 
ATOM   3348  O  OD1   . ASN A 1 415 ? 130.064 134.536 87.614  1.00 32.26 ?  415 ASN A OD1   1 
ATOM   3349  N  ND2   . ASN A 1 415 ? 128.357 135.027 88.980  1.00 30.02 ?  415 ASN A ND2   1 
ATOM   3350  N  N     . ILE A 1 416 ? 133.337 135.692 87.797  1.00 19.85 ?  416 ILE A N     1 
ATOM   3351  C  CA    . ILE A 1 416 ? 134.345 135.534 86.752  1.00 22.02 ?  416 ILE A CA    1 
ATOM   3352  C  C     . ILE A 1 416 ? 133.697 135.120 85.438  1.00 28.81 ?  416 ILE A C     1 
ATOM   3353  O  O     . ILE A 1 416 ? 134.076 135.603 84.364  1.00 26.69 ?  416 ILE A O     1 
ATOM   3354  C  CB    . ILE A 1 416 ? 135.423 134.530 87.201  1.00 24.02 ?  416 ILE A CB    1 
ATOM   3355  C  CG1   . ILE A 1 416 ? 136.211 135.096 88.383  1.00 21.73 ?  416 ILE A CG1   1 
ATOM   3356  C  CG2   . ILE A 1 416 ? 136.362 134.202 86.058  1.00 15.94 ?  416 ILE A CG2   1 
ATOM   3357  C  CD1   . ILE A 1 416 ? 137.130 134.101 89.044  1.00 19.62 ?  416 ILE A CD1   1 
ATOM   3358  N  N     . LEU A 1 417 ? 132.701 134.236 85.499  1.00 23.98 ?  417 LEU A N     1 
ATOM   3359  C  CA    . LEU A 1 417 ? 132.040 133.779 84.280  1.00 27.03 ?  417 LEU A CA    1 
ATOM   3360  C  C     . LEU A 1 417 ? 131.336 134.928 83.567  1.00 28.59 ?  417 LEU A C     1 
ATOM   3361  O  O     . LEU A 1 417 ? 131.509 135.123 82.359  1.00 36.05 ?  417 LEU A O     1 
ATOM   3362  C  CB    . LEU A 1 417 ? 131.048 132.666 84.612  1.00 27.64 ?  417 LEU A CB    1 
ATOM   3363  C  CG    . LEU A 1 417 ? 130.496 131.867 83.432  1.00 25.66 ?  417 LEU A CG    1 
ATOM   3364  C  CD1   . LEU A 1 417 ? 130.476 130.397 83.773  1.00 26.86 ?  417 LEU A CD1   1 
ATOM   3365  C  CD2   . LEU A 1 417 ? 129.105 132.346 83.065  1.00 32.99 ?  417 LEU A CD2   1 
ATOM   3366  N  N     . ASN A 1 418 ? 130.537 135.703 84.302  1.00 30.17 ?  418 ASN A N     1 
ATOM   3367  C  CA    . ASN A 1 418 ? 129.772 136.778 83.682  1.00 30.26 ?  418 ASN A CA    1 
ATOM   3368  C  C     . ASN A 1 418 ? 130.648 137.968 83.323  1.00 29.72 ?  418 ASN A C     1 
ATOM   3369  O  O     . ASN A 1 418 ? 130.377 138.654 82.330  1.00 32.38 ?  418 ASN A O     1 
ATOM   3370  C  CB    . ASN A 1 418 ? 128.639 137.215 84.608  1.00 26.41 ?  418 ASN A CB    1 
ATOM   3371  C  CG    . ASN A 1 418 ? 127.576 136.150 84.766  1.00 31.04 ?  418 ASN A CG    1 
ATOM   3372  O  OD1   . ASN A 1 418 ? 127.253 135.437 83.818  1.00 36.97 ?  418 ASN A OD1   1 
ATOM   3373  N  ND2   . ASN A 1 418 ? 127.028 136.032 85.969  1.00 32.23 ?  418 ASN A ND2   1 
ATOM   3374  N  N     . VAL A 1 419 ? 131.688 138.233 84.112  1.00 29.60 ?  419 VAL A N     1 
ATOM   3375  C  CA    . VAL A 1 419 ? 132.630 139.294 83.771  1.00 28.99 ?  419 VAL A CA    1 
ATOM   3376  C  C     . VAL A 1 419 ? 133.388 138.943 82.498  1.00 31.93 ?  419 VAL A C     1 
ATOM   3377  O  O     . VAL A 1 419 ? 133.579 139.790 81.618  1.00 35.55 ?  419 VAL A O     1 
ATOM   3378  C  CB    . VAL A 1 419 ? 133.582 139.555 84.954  1.00 27.28 ?  419 VAL A CB    1 
ATOM   3379  C  CG1   . VAL A 1 419 ? 134.822 140.276 84.492  1.00 31.92 ?  419 VAL A CG1   1 
ATOM   3380  C  CG2   . VAL A 1 419 ? 132.878 140.354 86.029  1.00 27.21 ?  419 VAL A CG2   1 
ATOM   3381  N  N     . MET A 1 420 ? 133.822 137.687 82.373  1.00 37.60 ?  420 MET A N     1 
ATOM   3382  C  CA    . MET A 1 420 ? 134.551 137.261 81.184  1.00 31.13 ?  420 MET A CA    1 
ATOM   3383  C  C     . MET A 1 420 ? 133.646 137.181 79.964  1.00 29.91 ?  420 MET A C     1 
ATOM   3384  O  O     . MET A 1 420 ? 134.091 137.462 78.845  1.00 35.71 ?  420 MET A O     1 
ATOM   3385  C  CB    . MET A 1 420 ? 135.220 135.912 81.440  1.00 32.87 ?  420 MET A CB    1 
ATOM   3386  C  CG    . MET A 1 420 ? 136.503 136.005 82.243  1.00 30.68 ?  420 MET A CG    1 
ATOM   3387  S  SD    . MET A 1 420 ? 137.715 137.082 81.467  1.00 39.19 ?  420 MET A SD    1 
ATOM   3388  C  CE    . MET A 1 420 ? 138.424 135.970 80.259  1.00 30.33 ?  420 MET A CE    1 
ATOM   3389  N  N     . GLU A 1 421 ? 132.382 136.794 80.152  1.00 38.79 ?  421 GLU A N     1 
ATOM   3390  C  CA    . GLU A 1 421 ? 131.439 136.766 79.039  1.00 37.01 ?  421 GLU A CA    1 
ATOM   3391  C  C     . GLU A 1 421 ? 131.195 138.165 78.489  1.00 41.48 ?  421 GLU A C     1 
ATOM   3392  O  O     . GLU A 1 421 ? 131.122 138.358 77.270  1.00 43.64 ?  421 GLU A O     1 
ATOM   3393  C  CB    . GLU A 1 421 ? 130.123 136.131 79.484  1.00 35.64 ?  421 GLU A CB    1 
ATOM   3394  C  CG    . GLU A 1 421 ? 130.077 134.619 79.344  1.00 40.90 ?  421 GLU A CG    1 
ATOM   3395  C  CD    . GLU A 1 421 ? 128.750 134.038 79.790  1.00 46.28 ?  421 GLU A CD    1 
ATOM   3396  O  OE1   . GLU A 1 421 ? 127.975 134.765 80.447  1.00 45.01 ?  421 GLU A OE1   1 
ATOM   3397  O  OE2   . GLU A 1 421 ? 128.480 132.858 79.484  1.00 45.47 -1 421 GLU A OE2   1 
ATOM   3398  N  N     . HIS A 1 422 ? 131.068 139.152 79.373  1.00 37.78 ?  422 HIS A N     1 
ATOM   3399  C  CA    . HIS A 1 422 ? 130.814 140.527 78.968  1.00 34.71 ?  422 HIS A CA    1 
ATOM   3400  C  C     . HIS A 1 422 ? 132.079 141.276 78.578  1.00 39.06 ?  422 HIS A C     1 
ATOM   3401  O  O     . HIS A 1 422 ? 131.977 142.421 78.120  1.00 39.00 ?  422 HIS A O     1 
ATOM   3402  C  CB    . HIS A 1 422 ? 130.101 141.280 80.095  1.00 34.38 ?  422 HIS A CB    1 
ATOM   3403  C  CG    . HIS A 1 422 ? 128.730 140.762 80.394  1.00 36.59 ?  422 HIS A CG    1 
ATOM   3404  N  ND1   . HIS A 1 422 ? 128.499 139.759 81.309  1.00 36.17 ?  422 HIS A ND1   1 
ATOM   3405  C  CD2   . HIS A 1 422 ? 127.517 141.110 79.903  1.00 38.64 ?  422 HIS A CD2   1 
ATOM   3406  C  CE1   . HIS A 1 422 ? 127.203 139.508 81.367  1.00 39.68 ?  422 HIS A CE1   1 
ATOM   3407  N  NE2   . HIS A 1 422 ? 126.585 140.314 80.523  1.00 41.23 ?  422 HIS A NE2   1 
ATOM   3408  N  N     . LYS A 1 423 ? 133.252 140.664 78.740  1.00 42.93 ?  423 LYS A N     1 
ATOM   3409  C  CA    . LYS A 1 423 ? 134.534 141.307 78.456  1.00 43.56 ?  423 LYS A CA    1 
ATOM   3410  C  C     . LYS A 1 423 ? 134.638 142.647 79.180  1.00 43.41 ?  423 LYS A C     1 
ATOM   3411  O  O     . LYS A 1 423 ? 135.009 143.672 78.603  1.00 46.66 ?  423 LYS A O     1 
ATOM   3412  C  CB    . LYS A 1 423 ? 134.743 141.480 76.952  1.00 40.83 ?  423 LYS A CB    1 
ATOM   3413  C  CG    . LYS A 1 423 ? 134.496 140.221 76.142  1.00 42.34 ?  423 LYS A CG    1 
ATOM   3414  C  CD    . LYS A 1 423 ? 135.776 139.423 75.970  1.00 46.49 ?  423 LYS A CD    1 
ATOM   3415  C  CE    . LYS A 1 423 ? 135.484 137.976 75.609  1.00 46.50 ?  423 LYS A CE    1 
ATOM   3416  N  NZ    . LYS A 1 423 ? 135.321 137.121 76.817  1.00 44.64 1  423 LYS A NZ    1 
ATOM   3417  N  N     . SER A 1 424 ? 134.304 142.630 80.465  1.00 33.13 ?  424 SER A N     1 
ATOM   3418  C  CA    . SER A 1 424 ? 134.147 143.844 81.257  1.00 32.99 ?  424 SER A CA    1 
ATOM   3419  C  C     . SER A 1 424 ? 134.887 143.731 82.578  1.00 36.41 ?  424 SER A C     1 
ATOM   3420  O  O     . SER A 1 424 ? 134.343 144.016 83.645  1.00 39.49 ?  424 SER A O     1 
ATOM   3421  C  CB    . SER A 1 424 ? 132.671 144.136 81.504  1.00 35.65 ?  424 SER A CB    1 
ATOM   3422  O  OG    . SER A 1 424 ? 132.127 143.222 82.439  1.00 32.10 ?  424 SER A OG    1 
ATOM   3423  N  N     . ILE A 1 425 ? 136.151 143.305 82.533  1.00 34.09 ?  425 ILE A N     1 
ATOM   3424  C  CA    . ILE A 1 425 ? 136.948 143.259 83.756  1.00 28.18 ?  425 ILE A CA    1 
ATOM   3425  C  C     . ILE A 1 425 ? 137.159 144.665 84.300  1.00 31.11 ?  425 ILE A C     1 
ATOM   3426  O  O     . ILE A 1 425 ? 136.953 144.928 85.489  1.00 36.98 ?  425 ILE A O     1 
ATOM   3427  C  CB    . ILE A 1 425 ? 138.287 142.541 83.506  1.00 32.28 ?  425 ILE A CB    1 
ATOM   3428  C  CG1   . ILE A 1 425 ? 138.079 141.028 83.460  1.00 33.29 ?  425 ILE A CG1   1 
ATOM   3429  C  CG2   . ILE A 1 425 ? 139.297 142.899 84.584  1.00 28.28 ?  425 ILE A CG2   1 
ATOM   3430  C  CD1   . ILE A 1 425 ? 139.322 140.244 83.146  1.00 32.74 ?  425 ILE A CD1   1 
ATOM   3431  N  N     . GLU A 1 426 ? 137.545 145.599 83.428  1.00 28.74 ?  426 GLU A N     1 
ATOM   3432  C  CA    . GLU A 1 426 ? 137.864 146.952 83.872  1.00 27.28 ?  426 GLU A CA    1 
ATOM   3433  C  C     . GLU A 1 426 ? 136.649 147.645 84.475  1.00 30.36 ?  426 GLU A C     1 
ATOM   3434  O  O     . GLU A 1 426 ? 136.706 148.160 85.598  1.00 37.14 ?  426 GLU A O     1 
ATOM   3435  C  CB    . GLU A 1 426 ? 138.413 147.762 82.700  1.00 29.43 ?  426 GLU A CB    1 
ATOM   3436  C  CG    . GLU A 1 426 ? 138.409 149.260 82.927  1.00 33.41 ?  426 GLU A CG    1 
ATOM   3437  C  CD    . GLU A 1 426 ? 139.106 150.018 81.817  1.00 39.47 ?  426 GLU A CD    1 
ATOM   3438  O  OE1   . GLU A 1 426 ? 139.376 149.410 80.760  1.00 38.35 ?  426 GLU A OE1   1 
ATOM   3439  O  OE2   . GLU A 1 426 ? 139.384 151.220 82.002  1.00 38.54 -1 426 GLU A OE2   1 
ATOM   3440  N  N     . LYS A 1 427 ? 135.537 147.667 83.738  1.00 32.91 ?  427 LYS A N     1 
ATOM   3441  C  CA    . LYS A 1 427 ? 134.352 148.379 84.204  1.00 28.97 ?  427 LYS A CA    1 
ATOM   3442  C  C     . LYS A 1 427 ? 133.786 147.742 85.464  1.00 30.16 ?  427 LYS A C     1 
ATOM   3443  O  O     . LYS A 1 427 ? 133.403 148.449 86.403  1.00 36.77 ?  427 LYS A O     1 
ATOM   3444  C  CB    . LYS A 1 427 ? 133.270 148.457 83.115  1.00 34.40 ?  427 LYS A CB    1 
ATOM   3445  C  CG    . LYS A 1 427 ? 133.597 149.129 81.747  1.00 38.16 ?  427 LYS A CG    1 
ATOM   3446  C  CD    . LYS A 1 427 ? 134.899 148.757 81.023  1.00 38.84 ?  427 LYS A CD    1 
ATOM   3447  C  CE    . LYS A 1 427 ? 135.026 147.258 80.782  1.00 34.59 ?  427 LYS A CE    1 
ATOM   3448  N  NZ    . LYS A 1 427 ? 136.320 146.897 80.142  1.00 35.02 1  427 LYS A NZ    1 
ATOM   3449  N  N     . THR A 1 428 ? 133.724 146.409 85.506  1.00 29.14 ?  428 THR A N     1 
ATOM   3450  C  CA    . THR A 1 428 ? 133.213 145.739 86.696  1.00 22.10 ?  428 THR A CA    1 
ATOM   3451  C  C     . THR A 1 428 ? 134.097 146.010 87.903  1.00 28.69 ?  428 THR A C     1 
ATOM   3452  O  O     . THR A 1 428 ? 133.592 146.296 88.994  1.00 31.20 ?  428 THR A O     1 
ATOM   3453  C  CB    . THR A 1 428 ? 133.092 144.237 86.459  1.00 24.52 ?  428 THR A CB    1 
ATOM   3454  O  OG1   . THR A 1 428 ? 132.470 143.998 85.192  1.00 28.64 ?  428 THR A OG1   1 
ATOM   3455  C  CG2   . THR A 1 428 ? 132.256 143.603 87.552  1.00 25.65 ?  428 THR A CG2   1 
ATOM   3456  N  N     . VAL A 1 429 ? 135.418 145.934 87.730  1.00 28.73 ?  429 VAL A N     1 
ATOM   3457  C  CA    . VAL A 1 429 ? 136.323 146.157 88.854  1.00 22.63 ?  429 VAL A CA    1 
ATOM   3458  C  C     . VAL A 1 429 ? 136.199 147.587 89.361  1.00 23.97 ?  429 VAL A C     1 
ATOM   3459  O  O     . VAL A 1 429 ? 136.138 147.825 90.571  1.00 30.65 ?  429 VAL A O     1 
ATOM   3460  C  CB    . VAL A 1 429 ? 137.772 145.817 88.459  1.00 24.00 ?  429 VAL A CB    1 
ATOM   3461  C  CG1   . VAL A 1 429 ? 138.741 146.405 89.461  1.00 19.09 ?  429 VAL A CG1   1 
ATOM   3462  C  CG2   . VAL A 1 429 ? 137.961 144.316 88.385  1.00 23.11 ?  429 VAL A CG2   1 
ATOM   3463  N  N     . LYS A 1 430 ? 136.133 148.560 88.448  1.00 24.20 ?  430 LYS A N     1 
ATOM   3464  C  CA    . LYS A 1 430 ? 136.051 149.953 88.876  1.00 23.38 ?  430 LYS A CA    1 
ATOM   3465  C  C     . LYS A 1 430 ? 134.718 150.258 89.553  1.00 23.32 ?  430 LYS A C     1 
ATOM   3466  O  O     . LYS A 1 430 ? 134.682 150.940 90.583  1.00 31.57 ?  430 LYS A O     1 
ATOM   3467  C  CB    . LYS A 1 430 ? 136.290 150.878 87.684  1.00 24.45 ?  430 LYS A CB    1 
ATOM   3468  C  CG    . LYS A 1 430 ? 137.695 150.768 87.119  1.00 26.85 ?  430 LYS A CG    1 
ATOM   3469  C  CD    . LYS A 1 430 ? 138.065 151.972 86.280  1.00 29.76 ?  430 LYS A CD    1 
ATOM   3470  C  CE    . LYS A 1 430 ? 139.506 151.879 85.813  1.00 29.64 ?  430 LYS A CE    1 
ATOM   3471  N  NZ    . LYS A 1 430 ? 139.895 153.041 84.970  1.00 33.48 1  430 LYS A NZ    1 
ATOM   3472  N  N     . LEU A 1 431 ? 133.611 149.756 88.999  1.00 24.92 ?  431 LEU A N     1 
ATOM   3473  C  CA    . LEU A 1 431 ? 132.309 149.994 89.614  1.00 20.54 ?  431 LEU A CA    1 
ATOM   3474  C  C     . LEU A 1 431 ? 132.197 149.300 90.966  1.00 22.83 ?  431 LEU A C     1 
ATOM   3475  O  O     . LEU A 1 431 ? 131.625 149.857 91.911  1.00 28.68 ?  431 LEU A O     1 
ATOM   3476  C  CB    . LEU A 1 431 ? 131.197 149.530 88.677  1.00 27.17 ?  431 LEU A CB    1 
ATOM   3477  C  CG    . LEU A 1 431 ? 130.500 150.597 87.833  1.00 30.22 ?  431 LEU A CG    1 
ATOM   3478  C  CD1   . LEU A 1 431 ? 129.384 149.971 87.017  1.00 29.53 ?  431 LEU A CD1   1 
ATOM   3479  C  CD2   . LEU A 1 431 ? 129.965 151.714 88.710  1.00 31.29 ?  431 LEU A CD2   1 
ATOM   3480  N  N     . ALA A 1 432 ? 132.730 148.080 91.079  1.00 24.46 ?  432 ALA A N     1 
ATOM   3481  C  CA    . ALA A 1 432 ? 132.735 147.384 92.359  1.00 15.27 ?  432 ALA A CA    1 
ATOM   3482  C  C     . ALA A 1 432 ? 133.598 148.115 93.377  1.00 26.11 ?  432 ALA A C     1 
ATOM   3483  O  O     . ALA A 1 432 ? 133.253 148.177 94.560  1.00 28.99 ?  432 ALA A O     1 
ATOM   3484  C  CB    . ALA A 1 432 ? 133.228 145.951 92.170  1.00 21.06 ?  432 ALA A CB    1 
ATOM   3485  N  N     . THR A 1 433 ? 134.729 148.666 92.934  1.00 28.03 ?  433 THR A N     1 
ATOM   3486  C  CA    . THR A 1 433 ? 135.565 149.461 93.825  1.00 21.24 ?  433 THR A CA    1 
ATOM   3487  C  C     . THR A 1 433 ? 134.819 150.691 94.316  1.00 23.51 ?  433 THR A C     1 
ATOM   3488  O  O     . THR A 1 433 ? 134.894 151.038 95.499  1.00 34.90 ?  433 THR A O     1 
ATOM   3489  C  CB    . THR A 1 433 ? 136.855 149.863 93.111  1.00 27.47 ?  433 THR A CB    1 
ATOM   3490  O  OG1   . THR A 1 433 ? 137.567 148.686 92.709  1.00 29.32 ?  433 THR A OG1   1 
ATOM   3491  C  CG2   . THR A 1 433 ? 137.737 150.694 94.026  1.00 24.32 ?  433 THR A CG2   1 
ATOM   3492  N  N     . ASP A 1 434 ? 134.089 151.361 93.423  1.00 22.85 ?  434 ASP A N     1 
ATOM   3493  C  CA    . ASP A 1 434 ? 133.297 152.517 93.832  1.00 22.59 ?  434 ASP A CA    1 
ATOM   3494  C  C     . ASP A 1 434 ? 132.221 152.126 94.840  1.00 20.26 ?  434 ASP A C     1 
ATOM   3495  O  O     . ASP A 1 434 ? 132.008 152.825 95.837  1.00 24.84 ?  434 ASP A O     1 
ATOM   3496  C  CB    . ASP A 1 434 ? 132.666 153.179 92.609  1.00 24.86 ?  434 ASP A CB    1 
ATOM   3497  C  CG    . ASP A 1 434 ? 133.696 153.757 91.664  1.00 31.71 ?  434 ASP A CG    1 
ATOM   3498  O  OD1   . ASP A 1 434 ? 134.819 154.056 92.119  1.00 35.06 ?  434 ASP A OD1   1 
ATOM   3499  O  OD2   . ASP A 1 434 ? 133.382 153.917 90.466  1.00 33.12 -1 434 ASP A OD2   1 
ATOM   3500  N  N     . SER A 1 435 ? 131.528 151.012 94.591  1.00 22.09 ?  435 SER A N     1 
ATOM   3501  C  CA    . SER A 1 435 ? 130.480 150.569 95.508  1.00 20.46 ?  435 SER A CA    1 
ATOM   3502  C  C     . SER A 1 435 ? 131.052 150.204 96.873  1.00 23.29 ?  435 SER A C     1 
ATOM   3503  O  O     . SER A 1 435 ? 130.472 150.547 97.911  1.00 29.51 ?  435 SER A O     1 
ATOM   3504  C  CB    . SER A 1 435 ? 129.726 149.386 94.905  1.00 23.10 ?  435 SER A CB    1 
ATOM   3505  O  OG    . SER A 1 435 ? 130.492 148.199 94.982  1.00 20.02 ?  435 SER A OG    1 
ATOM   3506  N  N     . LEU A 1 436 ? 132.195 149.515 96.894  1.00 19.07 ?  436 LEU A N     1 
ATOM   3507  C  CA    . LEU A 1 436 ? 132.821 149.155 98.161  1.00 10.90 ?  436 LEU A CA    1 
ATOM   3508  C  C     . LEU A 1 436 ? 133.333 150.388 98.892  1.00 17.35 ?  436 LEU A C     1 
ATOM   3509  O  O     . LEU A 1 436 ? 133.267 150.458 100.123 1.00 21.46 ?  436 LEU A O     1 
ATOM   3510  C  CB    . LEU A 1 436 ? 133.950 148.156 97.915  1.00 22.54 ?  436 LEU A CB    1 
ATOM   3511  C  CG    . LEU A 1 436 ? 133.518 146.759 97.468  1.00 19.18 ?  436 LEU A CG    1 
ATOM   3512  C  CD1   . LEU A 1 436 ? 134.704 145.961 96.953  1.00 10.93 ?  436 LEU A CD1   1 
ATOM   3513  C  CD2   . LEU A 1 436 ? 132.827 146.022 98.597  1.00 20.99 ?  436 LEU A CD2   1 
ATOM   3514  N  N     . THR A 1 437 ? 133.843 151.374 98.150  1.00 23.18 ?  437 THR A N     1 
ATOM   3515  C  CA    . THR A 1 437 ? 134.242 152.637 98.761  1.00 21.46 ?  437 THR A CA    1 
ATOM   3516  C  C     . THR A 1 437 ? 133.050 153.337 99.397  1.00 24.16 ?  437 THR A C     1 
ATOM   3517  O  O     . THR A 1 437 ? 133.156 153.884 100.500 1.00 35.32 ?  437 THR A O     1 
ATOM   3518  C  CB    . THR A 1 437 ? 134.892 153.539 97.714  1.00 19.83 ?  437 THR A CB    1 
ATOM   3519  O  OG1   . THR A 1 437 ? 135.873 152.793 96.986  1.00 21.94 ?  437 THR A OG1   1 
ATOM   3520  C  CG2   . THR A 1 437 ? 135.553 154.733 98.373  1.00 22.56 ?  437 THR A CG2   1 
ATOM   3521  N  N     . HIS A 1 438 ? 131.906 153.336 98.712  1.00 21.99 ?  438 HIS A N     1 
ATOM   3522  C  CA    . HIS A 1 438 ? 130.708 153.943 99.281  1.00 23.39 ?  438 HIS A CA    1 
ATOM   3523  C  C     . HIS A 1 438 ? 130.260 153.207 100.538 1.00 23.90 ?  438 HIS A C     1 
ATOM   3524  O  O     . HIS A 1 438 ? 129.857 153.835 101.524 1.00 31.71 ?  438 HIS A O     1 
ATOM   3525  C  CB    . HIS A 1 438 ? 129.586 153.968 98.245  1.00 26.69 ?  438 HIS A CB    1 
ATOM   3526  C  CG    . HIS A 1 438 ? 128.290 154.492 98.778  1.00 27.28 ?  438 HIS A CG    1 
ATOM   3527  N  ND1   . HIS A 1 438 ? 128.021 155.839 98.887  1.00 27.32 ?  438 HIS A ND1   1 
ATOM   3528  C  CD2   . HIS A 1 438 ? 127.190 153.851 99.238  1.00 28.60 ?  438 HIS A CD2   1 
ATOM   3529  C  CE1   . HIS A 1 438 ? 126.811 156.005 99.390  1.00 31.76 ?  438 HIS A CE1   1 
ATOM   3530  N  NE2   . HIS A 1 438 ? 126.286 154.813 99.612  1.00 31.05 ?  438 HIS A NE2   1 
ATOM   3531  N  N     . VAL A 1 439 ? 130.321 151.873 100.521 1.00 25.03 ?  439 VAL A N     1 
ATOM   3532  C  CA    . VAL A 1 439 ? 129.943 151.103 101.703 1.00 20.09 ?  439 VAL A CA    1 
ATOM   3533  C  C     . VAL A 1 439 ? 130.882 151.411 102.863 1.00 27.11 ?  439 VAL A C     1 
ATOM   3534  O  O     . VAL A 1 439 ? 130.453 151.518 104.017 1.00 36.62 ?  439 VAL A O     1 
ATOM   3535  C  CB    . VAL A 1 439 ? 129.913 149.597 101.378 1.00 23.14 ?  439 VAL A CB    1 
ATOM   3536  C  CG1   . VAL A 1 439 ? 129.650 148.789 102.633 1.00 24.30 ?  439 VAL A CG1   1 
ATOM   3537  C  CG2   . VAL A 1 439 ? 128.853 149.305 100.340 1.00 25.36 ?  439 VAL A CG2   1 
ATOM   3538  N  N     . SER A 1 440 ? 132.176 151.560 102.575 1.00 25.44 ?  440 SER A N     1 
ATOM   3539  C  CA    . SER A 1 440 ? 133.129 151.939 103.612 1.00 20.24 ?  440 SER A CA    1 
ATOM   3540  C  C     . SER A 1 440 ? 132.819 153.323 104.165 1.00 26.38 ?  440 SER A C     1 
ATOM   3541  O  O     . SER A 1 440 ? 132.897 153.550 105.378 1.00 34.05 ?  440 SER A O     1 
ATOM   3542  C  CB    . SER A 1 440 ? 134.553 151.894 103.057 1.00 25.82 ?  440 SER A CB    1 
ATOM   3543  O  OG    . SER A 1 440 ? 135.511 151.904 104.100 1.00 30.51 ?  440 SER A OG    1 
ATOM   3544  N  N     . GLU A 1 441 ? 132.467 154.265 103.288 1.00 29.54 ?  441 GLU A N     1 
ATOM   3545  C  CA    . GLU A 1 441 ? 132.217 155.633 103.724 1.00 21.89 ?  441 GLU A CA    1 
ATOM   3546  C  C     . GLU A 1 441 ? 130.933 155.752 104.535 1.00 31.00 ?  441 GLU A C     1 
ATOM   3547  O  O     . GLU A 1 441 ? 130.852 156.588 105.441 1.00 40.06 ?  441 GLU A O     1 
ATOM   3548  C  CB    . GLU A 1 441 ? 132.166 156.563 102.514 1.00 22.46 ?  441 GLU A CB    1 
ATOM   3549  C  CG    . GLU A 1 441 ? 133.526 156.861 101.913 1.00 28.54 ?  441 GLU A CG    1 
ATOM   3550  C  CD    . GLU A 1 441 ? 133.434 157.675 100.642 1.00 38.58 ?  441 GLU A CD    1 
ATOM   3551  O  OE1   . GLU A 1 441 ? 133.014 157.119 99.604  1.00 38.78 ?  441 GLU A OE1   1 
ATOM   3552  O  OE2   . GLU A 1 441 ? 133.779 158.875 100.676 1.00 37.83 -1 441 GLU A OE2   1 
ATOM   3553  N  N     . THR A 1 442 ? 129.923 154.941 104.231 1.00 32.28 ?  442 THR A N     1 
ATOM   3554  C  CA    . THR A 1 442 ? 128.651 155.014 104.938 1.00 31.30 ?  442 THR A CA    1 
ATOM   3555  C  C     . THR A 1 442 ? 128.610 154.150 106.190 1.00 32.40 ?  442 THR A C     1 
ATOM   3556  O  O     . THR A 1 442 ? 127.593 154.149 106.891 1.00 38.71 ?  442 THR A O     1 
ATOM   3557  C  CB    . THR A 1 442 ? 127.497 154.617 104.011 1.00 30.83 ?  442 THR A CB    1 
ATOM   3558  O  OG1   . THR A 1 442 ? 127.656 153.254 103.597 1.00 30.72 ?  442 THR A OG1   1 
ATOM   3559  C  CG2   . THR A 1 442 ? 127.461 155.519 102.791 1.00 30.57 ?  442 THR A CG2   1 
ATOM   3560  N  N     . THR A 1 443 ? 129.677 153.418 106.490 1.00 31.71 ?  443 THR A N     1 
ATOM   3561  C  CA    . THR A 1 443 ? 129.739 152.605 107.696 1.00 34.28 ?  443 THR A CA    1 
ATOM   3562  C  C     . THR A 1 443 ? 130.290 153.436 108.846 1.00 37.40 ?  443 THR A C     1 
ATOM   3563  O  O     . THR A 1 443 ? 131.332 154.085 108.707 1.00 39.22 ?  443 THR A O     1 
ATOM   3564  C  CB    . THR A 1 443 ? 130.609 151.367 107.472 1.00 33.99 ?  443 THR A CB    1 
ATOM   3565  O  OG1   . THR A 1 443 ? 130.001 150.527 106.484 1.00 38.06 ?  443 THR A OG1   1 
ATOM   3566  C  CG2   . THR A 1 443 ? 130.763 150.586 108.764 1.00 30.56 ?  443 THR A CG2   1 
ATOM   3567  N  N     . ASP A 1 444 ? 129.586 153.421 109.976 1.00 42.90 ?  444 ASP A N     1 
ATOM   3568  C  CA    . ASP A 1 444 ? 130.007 154.157 111.168 1.00 42.22 ?  444 ASP A CA    1 
ATOM   3569  C  C     . ASP A 1 444 ? 129.651 153.318 112.391 1.00 41.14 ?  444 ASP A C     1 
ATOM   3570  O  O     . ASP A 1 444 ? 128.501 153.321 112.839 1.00 42.24 ?  444 ASP A O     1 
ATOM   3571  C  CB    . ASP A 1 444 ? 129.355 155.534 111.228 1.00 43.39 ?  444 ASP A CB    1 
ATOM   3572  C  CG    . ASP A 1 444 ? 130.264 156.582 111.833 1.00 46.17 ?  444 ASP A CG    1 
ATOM   3573  O  OD1   . ASP A 1 444 ? 130.649 156.425 113.010 1.00 45.39 ?  444 ASP A OD1   1 
ATOM   3574  O  OD2   . ASP A 1 444 ? 130.597 157.560 111.133 1.00 47.95 -1 444 ASP A OD2   1 
ATOM   3575  N  N     . ILE A 1 445 ? 130.638 152.608 112.925 1.00 38.07 ?  445 ILE A N     1 
ATOM   3576  C  CA    . ILE A 1 445 ? 130.453 151.775 114.108 1.00 40.95 ?  445 ILE A CA    1 
ATOM   3577  C  C     . ILE A 1 445 ? 130.724 152.647 115.328 1.00 44.55 ?  445 ILE A C     1 
ATOM   3578  O  O     . ILE A 1 445 ? 131.867 153.032 115.587 1.00 44.52 ?  445 ILE A O     1 
ATOM   3579  C  CB    . ILE A 1 445 ? 131.374 150.550 114.084 1.00 39.74 ?  445 ILE A CB    1 
ATOM   3580  C  CG1   . ILE A 1 445 ? 131.278 149.842 112.730 1.00 37.73 ?  445 ILE A CG1   1 
ATOM   3581  C  CG2   . ILE A 1 445 ? 131.029 149.604 115.222 1.00 39.98 ?  445 ILE A CG2   1 
ATOM   3582  C  CD1   . ILE A 1 445 ? 130.207 148.776 112.658 1.00 37.05 ?  445 ILE A CD1   1 
ATOM   3583  N  N     . ARG A 1 446 ? 129.672 152.957 116.086 1.00 47.24 ?  446 ARG A N     1 
ATOM   3584  C  CA    . ARG A 1 446 ? 129.761 153.892 117.199 1.00 50.94 ?  446 ARG A CA    1 
ATOM   3585  C  C     . ARG A 1 446 ? 129.950 153.193 118.541 1.00 49.67 ?  446 ARG A C     1 
ATOM   3586  O  O     . ARG A 1 446 ? 129.787 153.826 119.590 1.00 45.92 ?  446 ARG A O     1 
ATOM   3587  C  CB    . ARG A 1 446 ? 128.523 154.790 117.229 1.00 47.16 ?  446 ARG A CB    1 
ATOM   3588  C  CG    . ARG A 1 446 ? 127.205 154.043 117.129 1.00 46.72 ?  446 ARG A CG    1 
ATOM   3589  C  CD    . ARG A 1 446 ? 126.063 154.972 116.735 1.00 50.06 ?  446 ARG A CD    1 
ATOM   3590  N  NE    . ARG A 1 446 ? 126.292 155.611 115.443 1.00 52.22 ?  446 ARG A NE    1 
ATOM   3591  C  CZ    . ARG A 1 446 ? 126.729 156.852 115.282 1.00 52.70 ?  446 ARG A CZ    1 
ATOM   3592  N  NH1   . ARG A 1 446 ? 126.981 157.637 116.316 1.00 49.54 1  446 ARG A NH1   1 
ATOM   3593  N  NH2   . ARG A 1 446 ? 126.918 157.319 114.051 1.00 51.25 ?  446 ARG A NH2   1 
ATOM   3594  N  N     . ASN A 1 447 ? 130.290 151.905 118.530 1.00 39.92 ?  447 ASN A N     1 
ATOM   3595  C  CA    . ASN A 1 447 ? 130.619 151.187 119.751 1.00 34.85 ?  447 ASN A CA    1 
ATOM   3596  C  C     . ASN A 1 447 ? 131.928 150.419 119.651 1.00 35.19 ?  447 ASN A C     1 
ATOM   3597  O  O     . ASN A 1 447 ? 132.312 149.751 120.617 1.00 36.74 ?  447 ASN A O     1 
ATOM   3598  C  CB    . ASN A 1 447 ? 129.487 150.223 120.133 1.00 34.46 ?  447 ASN A CB    1 
ATOM   3599  C  CG    . ASN A 1 447 ? 128.748 150.664 121.377 1.00 33.05 ?  447 ASN A CG    1 
ATOM   3600  O  OD1   . ASN A 1 447 ? 129.357 150.933 122.411 1.00 37.76 ?  447 ASN A OD1   1 
ATOM   3601  N  ND2   . ASN A 1 447 ? 127.429 150.752 121.281 1.00 34.04 ?  447 ASN A ND2   1 
ATOM   3602  N  N     . ALA A 1 448 ? 132.621 150.492 118.515 1.00 38.72 ?  448 ALA A N     1 
ATOM   3603  C  CA    . ALA A 1 448 ? 133.951 149.915 118.332 1.00 33.62 ?  448 ALA A CA    1 
ATOM   3604  C  C     . ALA A 1 448 ? 134.859 151.043 117.868 1.00 33.26 ?  448 ALA A C     1 
ATOM   3605  O  O     . ALA A 1 448 ? 134.972 151.304 116.661 1.00 33.62 ?  448 ALA A O     1 
ATOM   3606  C  CB    . ALA A 1 448 ? 133.927 148.763 117.331 1.00 29.25 ?  448 ALA A CB    1 
ATOM   3607  N  N     . PRO A 1 449 ? 135.507 151.756 118.795 1.00 30.75 ?  449 PRO A N     1 
ATOM   3608  C  CA    . PRO A 1 449 ? 136.269 152.953 118.398 1.00 27.60 ?  449 PRO A CA    1 
ATOM   3609  C  C     . PRO A 1 449 ? 137.397 152.666 117.424 1.00 29.34 ?  449 PRO A C     1 
ATOM   3610  O  O     . PRO A 1 449 ? 137.624 153.451 116.495 1.00 29.06 ?  449 PRO A O     1 
ATOM   3611  C  CB    . PRO A 1 449 ? 136.804 153.488 119.734 1.00 27.90 ?  449 PRO A CB    1 
ATOM   3612  C  CG    . PRO A 1 449 ? 136.045 152.762 120.793 1.00 31.86 ?  449 PRO A CG    1 
ATOM   3613  C  CD    . PRO A 1 449 ? 135.650 151.454 120.226 1.00 30.43 ?  449 PRO A CD    1 
ATOM   3614  N  N     . ALA A 1 450 ? 138.109 151.552 117.605 1.00 31.60 ?  450 ALA A N     1 
ATOM   3615  C  CA    . ALA A 1 450 ? 139.228 151.246 116.725 1.00 23.57 ?  450 ALA A CA    1 
ATOM   3616  C  C     . ALA A 1 450 ? 138.751 150.804 115.350 1.00 25.16 ?  450 ALA A C     1 
ATOM   3617  O  O     . ALA A 1 450 ? 139.384 151.134 114.342 1.00 27.25 ?  450 ALA A O     1 
ATOM   3618  C  CB    . ALA A 1 450 ? 140.117 150.179 117.358 1.00 24.69 ?  450 ALA A CB    1 
ATOM   3619  N  N     . VAL A 1 451 ? 137.636 150.074 115.287 1.00 30.39 ?  451 VAL A N     1 
ATOM   3620  C  CA    . VAL A 1 451 ? 137.049 149.713 114.000 1.00 23.44 ?  451 VAL A CA    1 
ATOM   3621  C  C     . VAL A 1 451 ? 136.649 150.968 113.235 1.00 24.66 ?  451 VAL A C     1 
ATOM   3622  O  O     . VAL A 1 451 ? 136.927 151.104 112.039 1.00 30.89 ?  451 VAL A O     1 
ATOM   3623  C  CB    . VAL A 1 451 ? 135.852 148.767 114.204 1.00 25.62 ?  451 VAL A CB    1 
ATOM   3624  C  CG1   . VAL A 1 451 ? 134.992 148.709 112.954 1.00 26.43 ?  451 VAL A CG1   1 
ATOM   3625  C  CG2   . VAL A 1 451 ? 136.333 147.381 114.585 1.00 25.40 ?  451 VAL A CG2   1 
ATOM   3626  N  N     . ARG A 1 452 ? 136.002 151.910 113.923 1.00 24.67 ?  452 ARG A N     1 
ATOM   3627  C  CA    . ARG A 1 452 ? 135.601 153.162 113.290 1.00 25.38 ?  452 ARG A CA    1 
ATOM   3628  C  C     . ARG A 1 452 ? 136.813 153.952 112.810 1.00 26.48 ?  452 ARG A C     1 
ATOM   3629  O  O     . ARG A 1 452 ? 136.836 154.459 111.680 1.00 31.93 ?  452 ARG A O     1 
ATOM   3630  C  CB    . ARG A 1 452 ? 134.774 153.989 114.275 1.00 26.48 ?  452 ARG A CB    1 
ATOM   3631  C  CG    . ARG A 1 452 ? 133.731 154.889 113.643 1.00 29.65 ?  452 ARG A CG    1 
ATOM   3632  C  CD    . ARG A 1 452 ? 133.916 156.325 114.096 1.00 28.18 ?  452 ARG A CD    1 
ATOM   3633  N  NE    . ARG A 1 452 ? 133.531 156.519 115.487 1.00 37.09 ?  452 ARG A NE    1 
ATOM   3634  C  CZ    . ARG A 1 452 ? 132.340 156.948 115.885 1.00 39.49 ?  452 ARG A CZ    1 
ATOM   3635  N  NH1   . ARG A 1 452 ? 131.387 157.243 115.017 1.00 35.94 1  452 ARG A NH1   1 
ATOM   3636  N  NH2   . ARG A 1 452 ? 132.103 157.088 117.186 1.00 36.35 ?  452 ARG A NH2   1 
ATOM   3637  N  N     . ARG A 1 453 ? 137.839 154.060 113.658 1.00 27.41 ?  453 ARG A N     1 
ATOM   3638  C  CA    . ARG A 1 453 ? 139.022 154.834 113.291 1.00 24.98 ?  453 ARG A CA    1 
ATOM   3639  C  C     . ARG A 1 453 ? 139.741 154.211 112.103 1.00 30.87 ?  453 ARG A C     1 
ATOM   3640  O  O     . ARG A 1 453 ? 140.163 154.921 111.183 1.00 35.58 ?  453 ARG A O     1 
ATOM   3641  C  CB    . ARG A 1 453 ? 139.966 154.955 114.486 1.00 26.76 ?  453 ARG A CB    1 
ATOM   3642  C  CG    . ARG A 1 453 ? 141.090 155.953 114.279 1.00 30.43 ?  453 ARG A CG    1 
ATOM   3643  C  CD    . ARG A 1 453 ? 142.236 155.713 115.243 1.00 27.05 ?  453 ARG A CD    1 
ATOM   3644  N  NE    . ARG A 1 453 ? 143.495 156.228 114.718 1.00 29.09 ?  453 ARG A NE    1 
ATOM   3645  C  CZ    . ARG A 1 453 ? 144.684 155.704 114.975 1.00 30.96 ?  453 ARG A CZ    1 
ATOM   3646  N  NH1   . ARG A 1 453 ? 144.819 154.649 115.761 1.00 31.00 1  453 ARG A NH1   1 
ATOM   3647  N  NH2   . ARG A 1 453 ? 145.765 156.250 114.428 1.00 30.21 ?  453 ARG A NH2   1 
ATOM   3648  N  N     . ALA A 1 454 ? 139.885 152.884 112.099 1.00 26.81 ?  454 ALA A N     1 
ATOM   3649  C  CA    . ALA A 1 454 ? 140.564 152.222 110.994 1.00 20.64 ?  454 ALA A CA    1 
ATOM   3650  C  C     . ALA A 1 454 ? 139.734 152.256 109.721 1.00 19.20 ?  454 ALA A C     1 
ATOM   3651  O  O     . ALA A 1 454 ? 140.295 152.302 108.625 1.00 25.25 ?  454 ALA A O     1 
ATOM   3652  C  CB    . ALA A 1 454 ? 140.906 150.784 111.371 1.00 23.13 ?  454 ALA A CB    1 
ATOM   3653  N  N     . ASN A 1 455 ? 138.406 152.235 109.835 1.00 23.57 ?  455 ASN A N     1 
ATOM   3654  C  CA    . ASN A 1 455 ? 137.574 152.386 108.649 1.00 23.02 ?  455 ASN A CA    1 
ATOM   3655  C  C     . ASN A 1 455 ? 137.721 153.777 108.050 1.00 26.24 ?  455 ASN A C     1 
ATOM   3656  O  O     . ASN A 1 455 ? 137.754 153.931 106.824 1.00 32.44 ?  455 ASN A O     1 
ATOM   3657  C  CB    . ASN A 1 455 ? 136.114 152.097 108.990 1.00 21.33 ?  455 ASN A CB    1 
ATOM   3658  C  CG    . ASN A 1 455 ? 135.214 152.141 107.774 1.00 27.83 ?  455 ASN A CG    1 
ATOM   3659  O  OD1   . ASN A 1 455 ? 135.362 151.342 106.851 1.00 34.90 ?  455 ASN A OD1   1 
ATOM   3660  N  ND2   . ASN A 1 455 ? 134.275 153.077 107.765 1.00 26.61 ?  455 ASN A ND2   1 
ATOM   3661  N  N     . LYS A 1 456 ? 137.805 154.803 108.898 1.00 29.69 ?  456 LYS A N     1 
ATOM   3662  C  CA    . LYS A 1 456 ? 137.983 156.157 108.382 1.00 26.25 ?  456 LYS A CA    1 
ATOM   3663  C  C     . LYS A 1 456 ? 139.381 156.364 107.810 1.00 27.17 ?  456 LYS A C     1 
ATOM   3664  O  O     . LYS A 1 456 ? 139.550 157.078 106.815 1.00 31.74 ?  456 LYS A O     1 
ATOM   3665  C  CB    . LYS A 1 456 ? 137.695 157.184 109.476 1.00 26.62 ?  456 LYS A CB    1 
ATOM   3666  C  CG    . LYS A 1 456 ? 136.298 157.093 110.057 1.00 29.67 ?  456 LYS A CG    1 
ATOM   3667  C  CD    . LYS A 1 456 ? 135.964 158.322 110.882 1.00 34.00 ?  456 LYS A CD    1 
ATOM   3668  C  CE    . LYS A 1 456 ? 134.480 158.386 111.196 1.00 32.56 ?  456 LYS A CE    1 
ATOM   3669  N  NZ    . LYS A 1 456 ? 133.647 158.024 110.017 1.00 33.57 1  456 LYS A NZ    1 
ATOM   3670  N  N     . ALA A 1 457 ? 140.397 155.750 108.416 1.00 26.25 ?  457 ALA A N     1 
ATOM   3671  C  CA    . ALA A 1 457 ? 141.779 156.016 108.035 1.00 22.46 ?  457 ALA A CA    1 
ATOM   3672  C  C     . ALA A 1 457 ? 142.261 155.132 106.889 1.00 27.03 ?  457 ALA A C     1 
ATOM   3673  O  O     . ALA A 1 457 ? 142.767 155.636 105.884 1.00 31.58 ?  457 ALA A O     1 
ATOM   3674  C  CB    . ALA A 1 457 ? 142.694 155.844 109.250 1.00 22.61 ?  457 ALA A CB    1 
ATOM   3675  N  N     . MET A 1 458 ? 142.117 153.814 107.029 1.00 29.41 ?  458 MET A N     1 
ATOM   3676  C  CA    . MET A 1 458 ? 142.634 152.882 106.034 1.00 19.45 ?  458 MET A CA    1 
ATOM   3677  C  C     . MET A 1 458 ? 141.776 152.853 104.777 1.00 21.76 ?  458 MET A C     1 
ATOM   3678  O  O     . MET A 1 458 ? 142.307 152.711 103.670 1.00 29.94 ?  458 MET A O     1 
ATOM   3679  C  CB    . MET A 1 458 ? 142.731 151.481 106.636 1.00 22.04 ?  458 MET A CB    1 
ATOM   3680  C  CG    . MET A 1 458 ? 143.418 151.433 107.985 1.00 22.23 ?  458 MET A CG    1 
ATOM   3681  S  SD    . MET A 1 458 ? 145.157 151.886 107.878 1.00 33.05 ?  458 MET A SD    1 
ATOM   3682  C  CE    . MET A 1 458 ? 145.913 150.266 107.776 1.00 25.27 ?  458 MET A CE    1 
ATOM   3683  N  N     . LYS A 1 459 ? 140.457 152.978 104.927 1.00 17.12 ?  459 LYS A N     1 
ATOM   3684  C  CA    . LYS A 1 459 ? 139.519 152.894 103.805 1.00 21.91 ?  459 LYS A CA    1 
ATOM   3685  C  C     . LYS A 1 459 ? 139.695 151.587 103.036 1.00 17.93 ?  459 LYS A C     1 
ATOM   3686  O  O     . LYS A 1 459 ? 139.677 151.562 101.804 1.00 25.40 ?  459 LYS A O     1 
ATOM   3687  C  CB    . LYS A 1 459 ? 139.661 154.098 102.873 1.00 21.80 ?  459 LYS A CB    1 
ATOM   3688  C  CG    . LYS A 1 459 ? 139.647 155.437 103.583 1.00 24.86 ?  459 LYS A CG    1 
ATOM   3689  C  CD    . LYS A 1 459 ? 140.568 156.426 102.900 1.00 25.02 ?  459 LYS A CD    1 
ATOM   3690  C  CE    . LYS A 1 459 ? 140.571 157.761 103.617 1.00 28.55 ?  459 LYS A CE    1 
ATOM   3691  N  NZ    . LYS A 1 459 ? 141.595 158.681 103.053 1.00 31.75 1  459 LYS A NZ    1 
ATOM   3692  N  N     . SER A 1 460 ? 139.866 150.492 103.770 1.00 20.38 ?  460 SER A N     1 
ATOM   3693  C  CA    . SER A 1 460 ? 140.121 149.195 103.161 1.00 14.03 ?  460 SER A CA    1 
ATOM   3694  C  C     . SER A 1 460 ? 138.834 148.580 102.630 1.00 20.49 ?  460 SER A C     1 
ATOM   3695  O  O     . SER A 1 460 ? 137.777 148.671 103.257 1.00 29.78 ?  460 SER A O     1 
ATOM   3696  C  CB    . SER A 1 460 ? 140.765 148.247 104.171 1.00 8.71  ?  460 SER A CB    1 
ATOM   3697  O  OG    . SER A 1 460 ? 141.856 148.864 104.827 1.00 30.12 ?  460 SER A OG    1 
ATOM   3698  N  N     . ILE A 1 461 ? 138.936 147.947 101.463 1.00 13.07 ?  461 ILE A N     1 
ATOM   3699  C  CA    . ILE A 1 461 ? 137.830 147.220 100.860 1.00 14.90 ?  461 ILE A CA    1 
ATOM   3700  C  C     . ILE A 1 461 ? 138.330 145.837 100.475 1.00 15.17 ?  461 ILE A C     1 
ATOM   3701  O  O     . ILE A 1 461 ? 139.530 145.602 100.333 1.00 22.96 ?  461 ILE A O     1 
ATOM   3702  C  CB    . ILE A 1 461 ? 137.248 147.945 99.627  1.00 14.02 ?  461 ILE A CB    1 
ATOM   3703  C  CG1   . ILE A 1 461 ? 138.319 148.100 98.547  1.00 7.16  ?  461 ILE A CG1   1 
ATOM   3704  C  CG2   . ILE A 1 461 ? 136.681 149.299 100.021 1.00 14.31 ?  461 ILE A CG2   1 
ATOM   3705  C  CD1   . ILE A 1 461 ? 137.837 148.798 97.306  1.00 7.09  ?  461 ILE A CD1   1 
ATOM   3706  N  N     . GLY A 1 462 ? 137.390 144.911 100.329 1.00 16.88 ?  462 GLY A N     1 
ATOM   3707  C  CA    . GLY A 1 462 ? 137.737 143.603 99.815  1.00 8.05  ?  462 GLY A CA    1 
ATOM   3708  C  C     . GLY A 1 462 ? 136.941 143.240 98.583  1.00 5.76  ?  462 GLY A C     1 
ATOM   3709  O  O     . GLY A 1 462 ? 135.735 142.999 98.669  1.00 24.60 ?  462 GLY A O     1 
ATOM   3710  N  N     . LEU A 1 463 ? 137.604 143.181 97.434  1.00 13.49 ?  463 LEU A N     1 
ATOM   3711  C  CA    . LEU A 1 463 ? 136.964 142.813 96.179  1.00 11.99 ?  463 LEU A CA    1 
ATOM   3712  C  C     . LEU A 1 463 ? 137.422 141.409 95.808  1.00 15.77 ?  463 LEU A C     1 
ATOM   3713  O  O     . LEU A 1 463 ? 138.562 141.212 95.377  1.00 27.78 ?  463 LEU A O     1 
ATOM   3714  C  CB    . LEU A 1 463 ? 137.296 143.815 95.076  1.00 18.12 ?  463 LEU A CB    1 
ATOM   3715  C  CG    . LEU A 1 463 ? 136.701 143.521 93.696  1.00 17.19 ?  463 LEU A CG    1 
ATOM   3716  C  CD1   . LEU A 1 463 ? 135.205 143.279 93.795  1.00 7.19  ?  463 LEU A CD1   1 
ATOM   3717  C  CD2   . LEU A 1 463 ? 137.001 144.652 92.726  1.00 15.33 ?  463 LEU A CD2   1 
ATOM   3718  N  N     . GLY A 1 464 ? 136.532 140.434 95.982  1.00 17.43 ?  464 GLY A N     1 
ATOM   3719  C  CA    . GLY A 1 464 ? 136.821 139.056 95.665  1.00 11.70 ?  464 GLY A CA    1 
ATOM   3720  C  C     . GLY A 1 464 ? 136.257 138.640 94.319  1.00 11.76 ?  464 GLY A C     1 
ATOM   3721  O  O     . GLY A 1 464 ? 135.764 139.450 93.531  1.00 18.98 ?  464 GLY A O     1 
ATOM   3722  N  N     . ALA A 1 465 ? 136.344 137.341 94.059  1.00 14.71 ?  465 ALA A N     1 
ATOM   3723  C  CA    . ALA A 1 465 ? 135.793 136.758 92.851  1.00 11.19 ?  465 ALA A CA    1 
ATOM   3724  C  C     . ALA A 1 465 ? 135.221 135.390 93.183  1.00 16.81 ?  465 ALA A C     1 
ATOM   3725  O  O     . ALA A 1 465 ? 135.603 134.758 94.170  1.00 29.03 ?  465 ALA A O     1 
ATOM   3726  C  CB    . ALA A 1 465 ? 136.850 136.648 91.745  1.00 15.71 ?  465 ALA A CB    1 
ATOM   3727  N  N     . MET A 1 466 ? 134.283 134.943 92.352  1.00 22.27 ?  466 MET A N     1 
ATOM   3728  C  CA    . MET A 1 466 ? 133.729 133.603 92.451  1.00 21.62 ?  466 MET A CA    1 
ATOM   3729  C  C     . MET A 1 466 ? 133.536 133.057 91.044  1.00 19.91 ?  466 MET A C     1 
ATOM   3730  O  O     . MET A 1 466 ? 133.838 133.726 90.050  1.00 23.91 ?  466 MET A O     1 
ATOM   3731  C  CB    . MET A 1 466 ? 132.406 133.579 93.220  1.00 26.40 ?  466 MET A CB    1 
ATOM   3732  C  CG    . MET A 1 466 ? 131.398 134.617 92.778  1.00 27.60 ?  466 MET A CG    1 
ATOM   3733  S  SD    . MET A 1 466 ? 129.877 134.481 93.729  1.00 40.18 ?  466 MET A SD    1 
ATOM   3734  C  CE    . MET A 1 466 ? 129.346 136.181 93.746  1.00 26.82 ?  466 MET A CE    1 
ATOM   3735  N  N     . ASN A 1 467 ? 133.026 131.827 90.970  1.00 20.36 ?  467 ASN A N     1 
ATOM   3736  C  CA    . ASN A 1 467 ? 132.746 131.148 89.706  1.00 20.74 ?  467 ASN A CA    1 
ATOM   3737  C  C     . ASN A 1 467 ? 134.014 130.903 88.895  1.00 21.97 ?  467 ASN A C     1 
ATOM   3738  O  O     . ASN A 1 467 ? 133.968 130.825 87.667  1.00 27.77 ?  467 ASN A O     1 
ATOM   3739  C  CB    . ASN A 1 467 ? 131.722 131.919 88.868  1.00 21.02 ?  467 ASN A CB    1 
ATOM   3740  C  CG    . ASN A 1 467 ? 130.670 131.018 88.263  1.00 26.60 ?  467 ASN A CG    1 
ATOM   3741  O  OD1   . ASN A 1 467 ? 130.616 129.826 88.556  1.00 30.58 ?  467 ASN A OD1   1 
ATOM   3742  N  ND2   . ASN A 1 467 ? 129.819 131.587 87.423  1.00 28.87 ?  467 ASN A ND2   1 
ATOM   3743  N  N     . LEU A 1 468 ? 135.160 130.786 89.568  1.00 17.20 ?  468 LEU A N     1 
ATOM   3744  C  CA    . LEU A 1 468 ? 136.384 130.426 88.863  1.00 18.24 ?  468 LEU A CA    1 
ATOM   3745  C  C     . LEU A 1 468 ? 136.300 129.004 88.327  1.00 22.11 ?  468 LEU A C     1 
ATOM   3746  O  O     . LEU A 1 468 ? 136.545 128.759 87.139  1.00 24.19 ?  468 LEU A O     1 
ATOM   3747  C  CB    . LEU A 1 468 ? 137.592 130.581 89.786  1.00 22.48 ?  468 LEU A CB    1 
ATOM   3748  C  CG    . LEU A 1 468 ? 138.898 129.991 89.248  1.00 20.24 ?  468 LEU A CG    1 
ATOM   3749  C  CD1   . LEU A 1 468 ? 139.460 130.848 88.129  1.00 17.75 ?  468 LEU A CD1   1 
ATOM   3750  C  CD2   . LEU A 1 468 ? 139.919 129.815 90.354  1.00 14.67 ?  468 LEU A CD2   1 
ATOM   3751  N  N     . HIS A 1 469 ? 135.937 128.052 89.189  1.00 25.00 ?  469 HIS A N     1 
ATOM   3752  C  CA    . HIS A 1 469 ? 135.791 126.675 88.738  1.00 15.91 ?  469 HIS A CA    1 
ATOM   3753  C  C     . HIS A 1 469 ? 134.623 126.535 87.774  1.00 25.43 ?  469 HIS A C     1 
ATOM   3754  O  O     . HIS A 1 469 ? 134.699 125.763 86.816  1.00 35.75 ?  469 HIS A O     1 
ATOM   3755  C  CB    . HIS A 1 469 ? 135.615 125.735 89.929  1.00 20.66 ?  469 HIS A CB    1 
ATOM   3756  C  CG    . HIS A 1 469 ? 135.740 124.286 89.573  1.00 24.47 ?  469 HIS A CG    1 
ATOM   3757  N  ND1   . HIS A 1 469 ? 135.468 123.273 90.465  1.00 30.41 ?  469 HIS A ND1   1 
ATOM   3758  C  CD2   . HIS A 1 469 ? 136.116 123.680 88.422  1.00 25.57 ?  469 HIS A CD2   1 
ATOM   3759  C  CE1   . HIS A 1 469 ? 135.664 122.107 89.878  1.00 26.91 ?  469 HIS A CE1   1 
ATOM   3760  N  NE2   . HIS A 1 469 ? 136.058 122.326 88.637  1.00 23.55 ?  469 HIS A NE2   1 
ATOM   3761  N  N     . GLY A 1 470 ? 133.533 127.264 88.012  1.00 23.18 ?  470 GLY A N     1 
ATOM   3762  C  CA    . GLY A 1 470 ? 132.422 127.226 87.076  1.00 18.91 ?  470 GLY A CA    1 
ATOM   3763  C  C     . GLY A 1 470 ? 132.812 127.724 85.699  1.00 13.76 ?  470 GLY A C     1 
ATOM   3764  O  O     . GLY A 1 470 ? 132.478 127.110 84.683  1.00 30.84 ?  470 GLY A O     1 
ATOM   3765  N  N     . TYR A 1 471 ? 133.541 128.841 85.652  1.00 17.80 ?  471 TYR A N     1 
ATOM   3766  C  CA    . TYR A 1 471 ? 133.993 129.379 84.375  1.00 20.66 ?  471 TYR A CA    1 
ATOM   3767  C  C     . TYR A 1 471 ? 134.951 128.422 83.678  1.00 26.74 ?  471 TYR A C     1 
ATOM   3768  O  O     . TYR A 1 471 ? 134.861 128.221 82.463  1.00 30.29 ?  471 TYR A O     1 
ATOM   3769  C  CB    . TYR A 1 471 ? 134.659 130.739 84.582  1.00 21.83 ?  471 TYR A CB    1 
ATOM   3770  C  CG    . TYR A 1 471 ? 135.262 131.317 83.325  1.00 25.96 ?  471 TYR A CG    1 
ATOM   3771  C  CD1   . TYR A 1 471 ? 134.460 131.895 82.353  1.00 25.94 ?  471 TYR A CD1   1 
ATOM   3772  C  CD2   . TYR A 1 471 ? 136.630 131.272 83.103  1.00 20.53 ?  471 TYR A CD2   1 
ATOM   3773  C  CE1   . TYR A 1 471 ? 135.003 132.421 81.200  1.00 26.67 ?  471 TYR A CE1   1 
ATOM   3774  C  CE2   . TYR A 1 471 ? 137.183 131.792 81.952  1.00 20.47 ?  471 TYR A CE2   1 
ATOM   3775  C  CZ    . TYR A 1 471 ? 136.364 132.366 81.005  1.00 28.50 ?  471 TYR A CZ    1 
ATOM   3776  O  OH    . TYR A 1 471 ? 136.912 132.886 79.857  1.00 31.36 ?  471 TYR A OH    1 
ATOM   3777  N  N     . LEU A 1 472 ? 135.880 127.825 84.429  1.00 22.56 ?  472 LEU A N     1 
ATOM   3778  C  CA    . LEU A 1 472 ? 136.845 126.916 83.816  1.00 21.54 ?  472 LEU A CA    1 
ATOM   3779  C  C     . LEU A 1 472 ? 136.174 125.642 83.316  1.00 26.87 ?  472 LEU A C     1 
ATOM   3780  O  O     . LEU A 1 472 ? 136.478 125.167 82.216  1.00 31.87 ?  472 LEU A O     1 
ATOM   3781  C  CB    . LEU A 1 472 ? 137.957 126.585 84.810  1.00 27.45 ?  472 LEU A CB    1 
ATOM   3782  C  CG    . LEU A 1 472 ? 138.855 127.746 85.238  1.00 29.85 ?  472 LEU A CG    1 
ATOM   3783  C  CD1   . LEU A 1 472 ? 139.637 127.374 86.484  1.00 22.43 ?  472 LEU A CD1   1 
ATOM   3784  C  CD2   . LEU A 1 472 ? 139.790 128.159 84.115  1.00 22.59 ?  472 LEU A CD2   1 
ATOM   3785  N  N     . ALA A 1 473 ? 135.264 125.073 84.109  1.00 28.89 ?  473 ALA A N     1 
ATOM   3786  C  CA    . ALA A 1 473 ? 134.588 123.844 83.712  1.00 25.05 ?  473 ALA A CA    1 
ATOM   3787  C  C     . ALA A 1 473 ? 133.649 124.082 82.537  1.00 32.50 ?  473 ALA A C     1 
ATOM   3788  O  O     . ALA A 1 473 ? 133.496 123.210 81.675  1.00 40.07 ?  473 ALA A O     1 
ATOM   3789  C  CB    . ALA A 1 473 ? 133.826 123.264 84.902  1.00 26.38 ?  473 ALA A CB    1 
ATOM   3790  N  N     . GLN A 1 474 ? 133.012 125.251 82.485  1.00 28.34 ?  474 GLN A N     1 
ATOM   3791  C  CA    . GLN A 1 474 ? 132.156 125.579 81.355  1.00 25.63 ?  474 GLN A CA    1 
ATOM   3792  C  C     . GLN A 1 474 ? 132.945 126.015 80.129  1.00 24.52 ?  474 GLN A C     1 
ATOM   3793  O  O     . GLN A 1 474 ? 132.344 126.235 79.073  1.00 35.27 ?  474 GLN A O     1 
ATOM   3794  C  CB    . GLN A 1 474 ? 131.158 126.669 81.749  1.00 27.87 ?  474 GLN A CB    1 
ATOM   3795  C  CG    . GLN A 1 474 ? 130.009 126.151 82.595  1.00 31.27 ?  474 GLN A CG    1 
ATOM   3796  C  CD    . GLN A 1 474 ? 129.205 127.262 83.230  1.00 30.88 ?  474 GLN A CD    1 
ATOM   3797  O  OE1   . GLN A 1 474 ? 128.514 128.014 82.543  1.00 33.25 ?  474 GLN A OE1   1 
ATOM   3798  N  NE2   . GLN A 1 474 ? 129.287 127.372 84.550  1.00 31.70 ?  474 GLN A NE2   1 
ATOM   3799  N  N     . ASN A 1 475 ? 134.265 126.150 80.243  1.00 30.94 ?  475 ASN A N     1 
ATOM   3800  C  CA    . ASN A 1 475 ? 135.128 126.463 79.114  1.00 32.64 ?  475 ASN A CA    1 
ATOM   3801  C  C     . ASN A 1 475 ? 136.072 125.317 78.772  1.00 33.12 ?  475 ASN A C     1 
ATOM   3802  O  O     . ASN A 1 475 ? 137.034 125.522 78.025  1.00 36.54 ?  475 ASN A O     1 
ATOM   3803  C  CB    . ASN A 1 475 ? 135.927 127.736 79.395  1.00 34.58 ?  475 ASN A CB    1 
ATOM   3804  C  CG    . ASN A 1 475 ? 135.086 128.989 79.274  1.00 30.33 ?  475 ASN A CG    1 
ATOM   3805  O  OD1   . ASN A 1 475 ? 135.032 129.613 78.216  1.00 35.59 ?  475 ASN A OD1   1 
ATOM   3806  N  ND2   . ASN A 1 475 ? 134.417 129.357 80.358  1.00 25.96 ?  475 ASN A ND2   1 
ATOM   3807  N  N     . GLY A 1 476 ? 135.821 124.124 79.301  1.00 29.91 ?  476 GLY A N     1 
ATOM   3808  C  CA    . GLY A 1 476 ? 136.657 122.971 79.014  1.00 30.17 ?  476 GLY A CA    1 
ATOM   3809  C  C     . GLY A 1 476 ? 138.069 123.063 79.550  1.00 34.66 ?  476 GLY A C     1 
ATOM   3810  O  O     . GLY A 1 476 ? 139.016 122.663 78.861  1.00 36.43 ?  476 GLY A O     1 
ATOM   3811  N  N     . ILE A 1 477 ? 138.238 123.582 80.763  1.00 31.37 ?  477 ILE A N     1 
ATOM   3812  C  CA    . ILE A 1 477 ? 139.545 123.702 81.397  1.00 28.71 ?  477 ILE A CA    1 
ATOM   3813  C  C     . ILE A 1 477 ? 139.486 123.016 82.753  1.00 31.58 ?  477 ILE A C     1 
ATOM   3814  O  O     . ILE A 1 477 ? 138.606 123.315 83.567  1.00 35.25 ?  477 ILE A O     1 
ATOM   3815  C  CB    . ILE A 1 477 ? 139.974 125.173 81.555  1.00 28.00 ?  477 ILE A CB    1 
ATOM   3816  C  CG1   . ILE A 1 477 ? 139.967 125.883 80.201  1.00 30.91 ?  477 ILE A CG1   1 
ATOM   3817  C  CG2   . ILE A 1 477 ? 141.348 125.257 82.188  1.00 31.37 ?  477 ILE A CG2   1 
ATOM   3818  C  CD1   . ILE A 1 477 ? 139.907 127.387 80.304  1.00 32.68 ?  477 ILE A CD1   1 
ATOM   3819  N  N     . ALA A 1 478 ? 140.416 122.095 82.991  1.00 31.56 ?  478 ALA A N     1 
ATOM   3820  C  CA    . ALA A 1 478 ? 140.499 121.437 84.287  1.00 26.59 ?  478 ALA A CA    1 
ATOM   3821  C  C     . ALA A 1 478 ? 141.053 122.397 85.330  1.00 33.48 ?  478 ALA A C     1 
ATOM   3822  O  O     . ALA A 1 478 ? 141.930 123.213 85.040  1.00 35.57 ?  478 ALA A O     1 
ATOM   3823  C  CB    . ALA A 1 478 ? 141.378 120.191 84.197  1.00 28.38 ?  478 ALA A CB    1 
ATOM   3824  N  N     . TYR A 1 479 ? 140.535 122.293 86.556  1.00 31.35 ?  479 TYR A N     1 
ATOM   3825  C  CA    . TYR A 1 479 ? 140.970 123.187 87.624  1.00 22.61 ?  479 TYR A CA    1 
ATOM   3826  C  C     . TYR A 1 479 ? 142.454 123.012 87.922  1.00 30.04 ?  479 TYR A C     1 
ATOM   3827  O  O     . TYR A 1 479 ? 143.164 123.992 88.173  1.00 39.24 ?  479 TYR A O     1 
ATOM   3828  C  CB    . TYR A 1 479 ? 140.136 122.941 88.881  1.00 21.64 ?  479 TYR A CB    1 
ATOM   3829  C  CG    . TYR A 1 479 ? 140.328 123.971 89.970  1.00 27.42 ?  479 TYR A CG    1 
ATOM   3830  C  CD1   . TYR A 1 479 ? 139.543 125.115 90.012  1.00 23.50 ?  479 TYR A CD1   1 
ATOM   3831  C  CD2   . TYR A 1 479 ? 141.285 123.796 90.961  1.00 28.82 ?  479 TYR A CD2   1 
ATOM   3832  C  CE1   . TYR A 1 479 ? 139.708 126.056 91.004  1.00 24.74 ?  479 TYR A CE1   1 
ATOM   3833  C  CE2   . TYR A 1 479 ? 141.458 124.735 91.957  1.00 26.82 ?  479 TYR A CE2   1 
ATOM   3834  C  CZ    . TYR A 1 479 ? 140.667 125.862 91.973  1.00 30.44 ?  479 TYR A CZ    1 
ATOM   3835  O  OH    . TYR A 1 479 ? 140.833 126.801 92.964  1.00 31.19 ?  479 TYR A OH    1 
ATOM   3836  N  N     . GLU A 1 480 ? 142.940 121.771 87.900  1.00 34.75 ?  480 GLU A N     1 
ATOM   3837  C  CA    . GLU A 1 480 ? 144.343 121.494 88.170  1.00 30.47 ?  480 GLU A CA    1 
ATOM   3838  C  C     . GLU A 1 480 ? 145.246 121.756 86.975  1.00 32.31 ?  480 GLU A C     1 
ATOM   3839  O  O     . GLU A 1 480 ? 146.471 121.720 87.132  1.00 38.83 ?  480 GLU A O     1 
ATOM   3840  C  CB    . GLU A 1 480 ? 144.519 120.039 88.602  1.00 35.32 ?  480 GLU A CB    1 
ATOM   3841  C  CG    . GLU A 1 480 ? 143.722 119.634 89.816  1.00 33.17 ?  480 GLU A CG    1 
ATOM   3842  C  CD    . GLU A 1 480 ? 143.409 118.155 89.812  1.00 41.41 ?  480 GLU A CD    1 
ATOM   3843  O  OE1   . GLU A 1 480 ? 142.383 117.766 89.216  1.00 41.14 ?  480 GLU A OE1   1 
ATOM   3844  O  OE2   . GLU A 1 480 ? 144.189 117.378 90.399  1.00 42.62 -1 480 GLU A OE2   1 
ATOM   3845  N  N     . SER A 1 481 ? 144.684 122.009 85.799  1.00 33.54 ?  481 SER A N     1 
ATOM   3846  C  CA    . SER A 1 481 ? 145.492 122.150 84.602  1.00 32.41 ?  481 SER A CA    1 
ATOM   3847  C  C     . SER A 1 481 ? 146.325 123.432 84.656  1.00 34.48 ?  481 SER A C     1 
ATOM   3848  O  O     . SER A 1 481 ? 145.933 124.413 85.291  1.00 37.49 ?  481 SER A O     1 
ATOM   3849  C  CB    . SER A 1 481 ? 144.606 122.159 83.362  1.00 32.23 ?  481 SER A CB    1 
ATOM   3850  O  OG    . SER A 1 481 ? 144.060 123.445 83.135  1.00 36.70 ?  481 SER A OG    1 
ATOM   3851  N  N     . PRO A 1 482 ? 147.493 123.438 84.008  1.00 39.26 ?  482 PRO A N     1 
ATOM   3852  C  CA    . PRO A 1 482 ? 148.273 124.682 83.924  1.00 35.92 ?  482 PRO A CA    1 
ATOM   3853  C  C     . PRO A 1 482 ? 147.544 125.802 83.206  1.00 35.70 ?  482 PRO A C     1 
ATOM   3854  O  O     . PRO A 1 482 ? 147.806 126.977 83.486  1.00 39.30 ?  482 PRO A O     1 
ATOM   3855  C  CB    . PRO A 1 482 ? 149.537 124.251 83.166  1.00 35.33 ?  482 PRO A CB    1 
ATOM   3856  C  CG    . PRO A 1 482 ? 149.620 122.779 83.364  1.00 36.84 ?  482 PRO A CG    1 
ATOM   3857  C  CD    . PRO A 1 482 ? 148.207 122.296 83.416  1.00 40.09 ?  482 PRO A CD    1 
ATOM   3858  N  N     . GLU A 1 483 ? 146.643 125.473 82.277  1.00 37.21 ?  483 GLU A N     1 
ATOM   3859  C  CA    . GLU A 1 483 ? 145.873 126.504 81.589  1.00 36.11 ?  483 GLU A CA    1 
ATOM   3860  C  C     . GLU A 1 483 ? 144.953 127.242 82.554  1.00 33.32 ?  483 GLU A C     1 
ATOM   3861  O  O     . GLU A 1 483 ? 144.743 128.452 82.419  1.00 36.83 ?  483 GLU A O     1 
ATOM   3862  C  CB    . GLU A 1 483 ? 145.069 125.884 80.447  1.00 38.31 ?  483 GLU A CB    1 
ATOM   3863  C  CG    . GLU A 1 483 ? 145.921 125.393 79.291  1.00 40.47 ?  483 GLU A CG    1 
ATOM   3864  C  CD    . GLU A 1 483 ? 146.343 123.948 79.455  1.00 43.75 ?  483 GLU A CD    1 
ATOM   3865  O  OE1   . GLU A 1 483 ? 146.072 123.368 80.527  1.00 41.03 ?  483 GLU A OE1   1 
ATOM   3866  O  OE2   . GLU A 1 483 ? 146.952 123.392 78.518  1.00 43.14 -1 483 GLU A OE2   1 
ATOM   3867  N  N     . ALA A 1 484 ? 144.390 126.526 83.529  1.00 27.96 ?  484 ALA A N     1 
ATOM   3868  C  CA    . ALA A 1 484 ? 143.558 127.175 84.535  1.00 28.48 ?  484 ALA A CA    1 
ATOM   3869  C  C     . ALA A 1 484 ? 144.362 128.171 85.357  1.00 29.73 ?  484 ALA A C     1 
ATOM   3870  O  O     . ALA A 1 484 ? 143.899 129.286 85.625  1.00 31.79 ?  484 ALA A O     1 
ATOM   3871  C  CB    . ALA A 1 484 ? 142.920 126.128 85.444  1.00 27.81 ?  484 ALA A CB    1 
ATOM   3872  N  N     . ARG A 1 485 ? 145.572 127.786 85.767  1.00 30.89 ?  485 ARG A N     1 
ATOM   3873  C  CA    . ARG A 1 485 ? 146.424 128.705 86.513  1.00 24.15 ?  485 ARG A CA    1 
ATOM   3874  C  C     . ARG A 1 485 ? 146.873 129.874 85.650  1.00 25.15 ?  485 ARG A C     1 
ATOM   3875  O  O     . ARG A 1 485 ? 147.014 130.990 86.153  1.00 35.58 ?  485 ARG A O     1 
ATOM   3876  C  CB    . ARG A 1 485 ? 147.630 127.960 87.079  1.00 27.04 ?  485 ARG A CB    1 
ATOM   3877  C  CG    . ARG A 1 485 ? 147.287 127.046 88.238  1.00 26.39 ?  485 ARG A CG    1 
ATOM   3878  C  CD    . ARG A 1 485 ? 148.536 126.503 88.901  1.00 28.57 ?  485 ARG A CD    1 
ATOM   3879  N  NE    . ARG A 1 485 ? 149.341 125.709 87.982  1.00 31.77 ?  485 ARG A NE    1 
ATOM   3880  C  CZ    . ARG A 1 485 ? 149.123 124.431 87.707  1.00 32.64 ?  485 ARG A CZ    1 
ATOM   3881  N  NH1   . ARG A 1 485 ? 148.125 123.764 88.264  1.00 30.58 1  485 ARG A NH1   1 
ATOM   3882  N  NH2   . ARG A 1 485 ? 149.928 123.805 86.855  1.00 29.50 ?  485 ARG A NH2   1 
ATOM   3883  N  N     . ASP A 1 486 ? 147.093 129.642 84.356  1.00 30.78 ?  486 ASP A N     1 
ATOM   3884  C  CA    . ASP A 1 486 ? 147.418 130.734 83.443  1.00 29.20 ?  486 ASP A CA    1 
ATOM   3885  C  C     . ASP A 1 486 ? 146.270 131.734 83.353  1.00 29.58 ?  486 ASP A C     1 
ATOM   3886  O  O     . ASP A 1 486 ? 146.480 132.956 83.411  1.00 36.63 ?  486 ASP A O     1 
ATOM   3887  C  CB    . ASP A 1 486 ? 147.750 130.159 82.067  1.00 33.34 ?  486 ASP A CB    1 
ATOM   3888  C  CG    . ASP A 1 486 ? 148.258 131.204 81.105  1.00 40.71 ?  486 ASP A CG    1 
ATOM   3889  O  OD1   . ASP A 1 486 ? 149.222 131.918 81.449  1.00 42.51 ?  486 ASP A OD1   1 
ATOM   3890  O  OD2   . ASP A 1 486 ? 147.694 131.305 79.997  1.00 39.27 -1 486 ASP A OD2   1 
ATOM   3891  N  N     . PHE A 1 487 ? 145.042 131.228 83.223  1.00 30.32 ?  487 PHE A N     1 
ATOM   3892  C  CA    . PHE A 1 487 ? 143.887 132.115 83.196  1.00 25.86 ?  487 PHE A CA    1 
ATOM   3893  C  C     . PHE A 1 487 ? 143.750 132.876 84.503  1.00 25.25 ?  487 PHE A C     1 
ATOM   3894  O  O     . PHE A 1 487 ? 143.457 134.073 84.498  1.00 31.24 ?  487 PHE A O     1 
ATOM   3895  C  CB    . PHE A 1 487 ? 142.598 131.347 82.920  1.00 26.95 ?  487 PHE A CB    1 
ATOM   3896  C  CG    . PHE A 1 487 ? 141.367 132.115 83.310  1.00 29.75 ?  487 PHE A CG    1 
ATOM   3897  C  CD1   . PHE A 1 487 ? 140.915 133.159 82.523  1.00 26.34 ?  487 PHE A CD1   1 
ATOM   3898  C  CD2   . PHE A 1 487 ? 140.687 131.823 84.481  1.00 26.22 ?  487 PHE A CD2   1 
ATOM   3899  C  CE1   . PHE A 1 487 ? 139.802 133.884 82.883  1.00 26.84 ?  487 PHE A CE1   1 
ATOM   3900  C  CE2   . PHE A 1 487 ? 139.572 132.547 84.844  1.00 25.28 ?  487 PHE A CE2   1 
ATOM   3901  C  CZ    . PHE A 1 487 ? 139.130 133.579 84.044  1.00 28.34 ?  487 PHE A CZ    1 
ATOM   3902  N  N     . ALA A 1 488 ? 143.918 132.188 85.634  1.00 25.81 ?  488 ALA A N     1 
ATOM   3903  C  CA    . ALA A 1 488 ? 143.806 132.859 86.922  1.00 20.51 ?  488 ALA A CA    1 
ATOM   3904  C  C     . ALA A 1 488 ? 144.863 133.945 87.062  1.00 27.80 ?  488 ALA A C     1 
ATOM   3905  O  O     . ALA A 1 488 ? 144.574 135.049 87.535  1.00 34.78 ?  488 ALA A O     1 
ATOM   3906  C  CB    . ALA A 1 488 ? 143.920 131.842 88.055  1.00 18.44 ?  488 ALA A CB    1 
ATOM   3907  N  N     . ASN A 1 489 ? 146.092 133.654 86.630  1.00 28.19 ?  489 ASN A N     1 
ATOM   3908  C  CA    . ASN A 1 489 ? 147.158 134.645 86.661  1.00 20.94 ?  489 ASN A CA    1 
ATOM   3909  C  C     . ASN A 1 489 ? 146.769 135.889 85.877  1.00 20.93 ?  489 ASN A C     1 
ATOM   3910  O  O     . ASN A 1 489 ? 146.804 137.005 86.406  1.00 30.25 ?  489 ASN A O     1 
ATOM   3911  C  CB    . ASN A 1 489 ? 148.442 134.032 86.102  1.00 22.28 ?  489 ASN A CB    1 
ATOM   3912  C  CG    . ASN A 1 489 ? 149.685 134.771 86.542  1.00 30.45 ?  489 ASN A CG    1 
ATOM   3913  O  OD1   . ASN A 1 489 ? 149.835 135.116 87.712  1.00 36.75 ?  489 ASN A OD1   1 
ATOM   3914  N  ND2   . ASN A 1 489 ? 150.592 135.007 85.604  1.00 28.71 ?  489 ASN A ND2   1 
ATOM   3915  N  N     . THR A 1 490 ? 146.365 135.711 84.616  1.00 26.43 ?  490 THR A N     1 
ATOM   3916  C  CA    . THR A 1 490 ? 146.026 136.870 83.793  1.00 24.41 ?  490 THR A CA    1 
ATOM   3917  C  C     . THR A 1 490 ? 144.816 137.615 84.345  1.00 26.18 ?  490 THR A C     1 
ATOM   3918  O  O     . THR A 1 490 ? 144.826 138.849 84.445  1.00 27.97 ?  490 THR A O     1 
ATOM   3919  C  CB    . THR A 1 490 ? 145.773 136.437 82.351  1.00 26.36 ?  490 THR A CB    1 
ATOM   3920  O  OG1   . THR A 1 490 ? 146.892 135.680 81.878  1.00 31.50 ?  490 THR A OG1   1 
ATOM   3921  C  CG2   . THR A 1 490 ? 145.577 137.652 81.458  1.00 25.93 ?  490 THR A CG2   1 
ATOM   3922  N  N     . PHE A 1 491 ? 143.771 136.879 84.727  1.00 21.58 ?  491 PHE A N     1 
ATOM   3923  C  CA    . PHE A 1 491 ? 142.534 137.496 85.187  1.00 18.72 ?  491 PHE A CA    1 
ATOM   3924  C  C     . PHE A 1 491 ? 142.762 138.308 86.452  1.00 25.92 ?  491 PHE A C     1 
ATOM   3925  O  O     . PHE A 1 491 ? 142.322 139.458 86.554  1.00 28.50 ?  491 PHE A O     1 
ATOM   3926  C  CB    . PHE A 1 491 ? 141.476 136.417 85.428  1.00 24.90 ?  491 PHE A CB    1 
ATOM   3927  C  CG    . PHE A 1 491 ? 140.187 136.945 85.984  1.00 22.44 ?  491 PHE A CG    1 
ATOM   3928  C  CD1   . PHE A 1 491 ? 139.205 137.432 85.141  1.00 18.33 ?  491 PHE A CD1   1 
ATOM   3929  C  CD2   . PHE A 1 491 ? 139.955 136.955 87.349  1.00 18.60 ?  491 PHE A CD2   1 
ATOM   3930  C  CE1   . PHE A 1 491 ? 138.021 137.921 85.645  1.00 15.30 ?  491 PHE A CE1   1 
ATOM   3931  C  CE2   . PHE A 1 491 ? 138.775 137.447 87.858  1.00 18.33 ?  491 PHE A CE2   1 
ATOM   3932  C  CZ    . PHE A 1 491 ? 137.805 137.929 87.004  1.00 19.82 ?  491 PHE A CZ    1 
ATOM   3933  N  N     . PHE A 1 492 ? 143.456 137.730 87.431  1.00 20.75 ?  492 PHE A N     1 
ATOM   3934  C  CA    . PHE A 1 492 ? 143.645 138.434 88.686  1.00 13.53 ?  492 PHE A CA    1 
ATOM   3935  C  C     . PHE A 1 492 ? 144.725 139.500 88.601  1.00 12.28 ?  492 PHE A C     1 
ATOM   3936  O  O     . PHE A 1 492 ? 144.653 140.480 89.346  1.00 22.08 ?  492 PHE A O     1 
ATOM   3937  C  CB    . PHE A 1 492 ? 143.931 137.432 89.802  1.00 20.06 ?  492 PHE A CB    1 
ATOM   3938  C  CG    . PHE A 1 492 ? 142.715 136.671 90.236  1.00 16.34 ?  492 PHE A CG    1 
ATOM   3939  C  CD1   . PHE A 1 492 ? 141.775 137.261 91.062  1.00 15.80 ?  492 PHE A CD1   1 
ATOM   3940  C  CD2   . PHE A 1 492 ? 142.487 135.385 89.783  1.00 21.73 ?  492 PHE A CD2   1 
ATOM   3941  C  CE1   . PHE A 1 492 ? 140.647 136.571 91.449  1.00 14.75 ?  492 PHE A CE1   1 
ATOM   3942  C  CE2   . PHE A 1 492 ? 141.360 134.690 90.166  1.00 16.11 ?  492 PHE A CE2   1 
ATOM   3943  C  CZ    . PHE A 1 492 ? 140.440 135.283 91.000  1.00 15.69 ?  492 PHE A CZ    1 
ATOM   3944  N  N     . MET A 1 493 ? 145.688 139.374 87.684  1.00 13.10 ?  493 MET A N     1 
ATOM   3945  C  CA    . MET A 1 493 ? 146.570 140.503 87.416  1.00 22.63 ?  493 MET A CA    1 
ATOM   3946  C  C     . MET A 1 493 ? 145.777 141.670 86.849  1.00 18.41 ?  493 MET A C     1 
ATOM   3947  O  O     . MET A 1 493 ? 146.002 142.824 87.226  1.00 28.96 ?  493 MET A O     1 
ATOM   3948  C  CB    . MET A 1 493 ? 147.696 140.087 86.467  1.00 25.38 ?  493 MET A CB    1 
ATOM   3949  C  CG    . MET A 1 493 ? 148.476 141.234 85.809  1.00 20.10 ?  493 MET A CG    1 
ATOM   3950  S  SD    . MET A 1 493 ? 147.717 142.012 84.368  1.00 34.53 ?  493 MET A SD    1 
ATOM   3951  C  CE    . MET A 1 493 ? 147.682 140.637 83.227  1.00 28.29 ?  493 MET A CE    1 
ATOM   3952  N  N     . MET A 1 494 ? 144.838 141.388 85.941  1.00 22.19 ?  494 MET A N     1 
ATOM   3953  C  CA    . MET A 1 494 ? 144.022 142.458 85.376  1.00 17.81 ?  494 MET A CA    1 
ATOM   3954  C  C     . MET A 1 494 ? 143.123 143.080 86.437  1.00 19.45 ?  494 MET A C     1 
ATOM   3955  O  O     . MET A 1 494 ? 142.942 144.305 86.473  1.00 32.12 ?  494 MET A O     1 
ATOM   3956  C  CB    . MET A 1 494 ? 143.190 141.918 84.212  1.00 24.00 ?  494 MET A CB    1 
ATOM   3957  C  CG    . MET A 1 494 ? 143.920 141.966 82.886  1.00 23.09 ?  494 MET A CG    1 
ATOM   3958  S  SD    . MET A 1 494 ? 143.132 141.057 81.547  1.00 41.86 ?  494 MET A SD    1 
ATOM   3959  C  CE    . MET A 1 494 ? 141.681 142.065 81.279  1.00 27.84 ?  494 MET A CE    1 
ATOM   3960  N  N     . VAL A 1 495 ? 142.552 142.247 87.308  1.00 22.31 ?  495 VAL A N     1 
ATOM   3961  C  CA    . VAL A 1 495 ? 141.726 142.750 88.400  1.00 13.04 ?  495 VAL A CA    1 
ATOM   3962  C  C     . VAL A 1 495 ? 142.547 143.641 89.321  1.00 19.56 ?  495 VAL A C     1 
ATOM   3963  O  O     . VAL A 1 495 ? 142.096 144.713 89.733  1.00 26.90 ?  495 VAL A O     1 
ATOM   3964  C  CB    . VAL A 1 495 ? 141.083 141.579 89.167  1.00 15.82 ?  495 VAL A CB    1 
ATOM   3965  C  CG1   . VAL A 1 495 ? 140.493 142.057 90.483  1.00 11.99 ?  495 VAL A CG1   1 
ATOM   3966  C  CG2   . VAL A 1 495 ? 140.021 140.911 88.317  1.00 18.51 ?  495 VAL A CG2   1 
ATOM   3967  N  N     . ASN A 1 496 ? 143.767 143.212 89.658  1.00 23.48 ?  496 ASN A N     1 
ATOM   3968  C  CA    . ASN A 1 496 ? 144.643 144.036 90.484  1.00 15.17 ?  496 ASN A CA    1 
ATOM   3969  C  C     . ASN A 1 496 ? 144.980 145.349 89.791  1.00 17.85 ?  496 ASN A C     1 
ATOM   3970  O  O     . ASN A 1 496 ? 144.971 146.411 90.420  1.00 23.80 ?  496 ASN A O     1 
ATOM   3971  C  CB    . ASN A 1 496 ? 145.919 143.265 90.821  1.00 19.22 ?  496 ASN A CB    1 
ATOM   3972  C  CG    . ASN A 1 496 ? 146.656 143.847 92.006  1.00 18.58 ?  496 ASN A CG    1 
ATOM   3973  O  OD1   . ASN A 1 496 ? 146.043 144.342 92.949  1.00 25.12 ?  496 ASN A OD1   1 
ATOM   3974  N  ND2   . ASN A 1 496 ? 147.979 143.790 91.965  1.00 18.92 ?  496 ASN A ND2   1 
ATOM   3975  N  N     . PHE A 1 497 ? 145.276 145.293 88.491  1.00 21.05 ?  497 PHE A N     1 
ATOM   3976  C  CA    . PHE A 1 497 ? 145.602 146.499 87.739  1.00 15.64 ?  497 PHE A CA    1 
ATOM   3977  C  C     . PHE A 1 497 ? 144.460 147.500 87.794  1.00 24.19 ?  497 PHE A C     1 
ATOM   3978  O  O     . PHE A 1 497 ? 144.665 148.680 88.098  1.00 28.93 ?  497 PHE A O     1 
ATOM   3979  C  CB    . PHE A 1 497 ? 145.920 146.136 86.288  1.00 17.27 ?  497 PHE A CB    1 
ATOM   3980  C  CG    . PHE A 1 497 ? 146.272 147.316 85.427  1.00 19.90 ?  497 PHE A CG    1 
ATOM   3981  C  CD1   . PHE A 1 497 ? 147.579 147.757 85.337  1.00 23.61 ?  497 PHE A CD1   1 
ATOM   3982  C  CD2   . PHE A 1 497 ? 145.295 147.982 84.707  1.00 21.10 ?  497 PHE A CD2   1 
ATOM   3983  C  CE1   . PHE A 1 497 ? 147.904 148.840 84.546  1.00 24.21 ?  497 PHE A CE1   1 
ATOM   3984  C  CE2   . PHE A 1 497 ? 145.616 149.065 83.917  1.00 22.95 ?  497 PHE A CE2   1 
ATOM   3985  C  CZ    . PHE A 1 497 ? 146.921 149.494 83.836  1.00 24.69 ?  497 PHE A CZ    1 
ATOM   3986  N  N     . TYR A 1 498 ? 143.241 147.040 87.523  1.00 26.98 ?  498 TYR A N     1 
ATOM   3987  C  CA    . TYR A 1 498 ? 142.120 147.966 87.470  1.00 18.45 ?  498 TYR A CA    1 
ATOM   3988  C  C     . TYR A 1 498 ? 141.669 148.407 88.856  1.00 22.85 ?  498 TYR A C     1 
ATOM   3989  O  O     . TYR A 1 498 ? 141.189 149.531 89.008  1.00 25.76 ?  498 TYR A O     1 
ATOM   3990  C  CB    . TYR A 1 498 ? 140.973 147.347 86.675  1.00 19.95 ?  498 TYR A CB    1 
ATOM   3991  C  CG    . TYR A 1 498 ? 141.289 147.286 85.201  1.00 24.72 ?  498 TYR A CG    1 
ATOM   3992  C  CD1   . TYR A 1 498 ? 141.559 148.444 84.487  1.00 24.50 ?  498 TYR A CD1   1 
ATOM   3993  C  CD2   . TYR A 1 498 ? 141.342 146.075 84.528  1.00 26.25 ?  498 TYR A CD2   1 
ATOM   3994  C  CE1   . TYR A 1 498 ? 141.862 148.399 83.144  1.00 25.80 ?  498 TYR A CE1   1 
ATOM   3995  C  CE2   . TYR A 1 498 ? 141.642 146.020 83.184  1.00 24.86 ?  498 TYR A CE2   1 
ATOM   3996  C  CZ    . TYR A 1 498 ? 141.901 147.186 82.497  1.00 30.37 ?  498 TYR A CZ    1 
ATOM   3997  O  OH    . TYR A 1 498 ? 142.200 147.143 81.156  1.00 32.57 ?  498 TYR A OH    1 
ATOM   3998  N  N     . SER A 1 499 ? 141.855 147.574 89.883  1.00 23.88 ?  499 SER A N     1 
ATOM   3999  C  CA    . SER A 1 499 ? 141.559 148.017 91.241  1.00 15.88 ?  499 SER A CA    1 
ATOM   4000  C  C     . SER A 1 499 ? 142.549 149.079 91.699  1.00 19.19 ?  499 SER A C     1 
ATOM   4001  O  O     . SER A 1 499 ? 142.158 150.064 92.335  1.00 30.15 ?  499 SER A O     1 
ATOM   4002  C  CB    . SER A 1 499 ? 141.558 146.828 92.200  1.00 15.23 ?  499 SER A CB    1 
ATOM   4003  O  OG    . SER A 1 499 ? 142.868 146.341 92.422  1.00 23.12 ?  499 SER A OG    1 
ATOM   4004  N  N     . ILE A 1 500 ? 143.834 148.906 91.376  1.00 17.80 ?  500 ILE A N     1 
ATOM   4005  C  CA    . ILE A 1 500 ? 144.825 149.927 91.701  1.00 19.65 ?  500 ILE A CA    1 
ATOM   4006  C  C     . ILE A 1 500 ? 144.536 151.208 90.931  1.00 18.17 ?  500 ILE A C     1 
ATOM   4007  O  O     . ILE A 1 500 ? 144.644 152.314 91.474  1.00 28.08 ?  500 ILE A O     1 
ATOM   4008  C  CB    . ILE A 1 500 ? 146.246 149.403 91.420  1.00 22.99 ?  500 ILE A CB    1 
ATOM   4009  C  CG1   . ILE A 1 500 ? 146.613 148.295 92.401  1.00 19.08 ?  500 ILE A CG1   1 
ATOM   4010  C  CG2   . ILE A 1 500 ? 147.260 150.522 91.519  1.00 20.01 ?  500 ILE A CG2   1 
ATOM   4011  C  CD1   . ILE A 1 500 ? 147.780 147.466 91.952  1.00 19.14 ?  500 ILE A CD1   1 
ATOM   4012  N  N     . GLN A 1 501 ? 144.158 151.079 89.658  1.00 24.23 ?  501 GLN A N     1 
ATOM   4013  C  CA    . GLN A 1 501 ? 143.819 152.253 88.861  1.00 22.16 ?  501 GLN A CA    1 
ATOM   4014  C  C     . GLN A 1 501 ? 142.620 152.991 89.439  1.00 28.31 ?  501 GLN A C     1 
ATOM   4015  O  O     . GLN A 1 501 ? 142.626 154.222 89.531  1.00 35.38 ?  501 GLN A O     1 
ATOM   4016  C  CB    . GLN A 1 501 ? 143.548 151.840 87.416  1.00 24.46 ?  501 GLN A CB    1 
ATOM   4017  C  CG    . GLN A 1 501 ? 144.023 152.845 86.389  1.00 25.08 ?  501 GLN A CG    1 
ATOM   4018  C  CD    . GLN A 1 501 ? 143.729 152.407 84.973  1.00 29.25 ?  501 GLN A CD    1 
ATOM   4019  O  OE1   . GLN A 1 501 ? 142.573 152.214 84.597  1.00 28.56 ?  501 GLN A OE1   1 
ATOM   4020  N  NE2   . GLN A 1 501 ? 144.776 152.243 84.176  1.00 33.56 ?  501 GLN A NE2   1 
ATOM   4021  N  N     . ARG A 1 502 ? 141.579 152.256 89.837  1.00 29.65 ?  502 ARG A N     1 
ATOM   4022  C  CA    . ARG A 1 502 ? 140.407 152.896 90.421  1.00 20.32 ?  502 ARG A CA    1 
ATOM   4023  C  C     . ARG A 1 502 ? 140.736 153.540 91.761  1.00 18.03 ?  502 ARG A C     1 
ATOM   4024  O  O     . ARG A 1 502 ? 140.240 154.626 92.067  1.00 30.49 ?  502 ARG A O     1 
ATOM   4025  C  CB    . ARG A 1 502 ? 139.274 151.882 90.575  1.00 24.31 ?  502 ARG A CB    1 
ATOM   4026  C  CG    . ARG A 1 502 ? 137.923 152.516 90.844  1.00 26.79 ?  502 ARG A CG    1 
ATOM   4027  C  CD    . ARG A 1 502 ? 137.621 153.623 89.854  1.00 27.43 ?  502 ARG A CD    1 
ATOM   4028  N  NE    . ARG A 1 502 ? 136.521 154.465 90.308  1.00 25.88 ?  502 ARG A NE    1 
ATOM   4029  C  CZ    . ARG A 1 502 ? 136.461 155.777 90.136  1.00 28.77 ?  502 ARG A CZ    1 
ATOM   4030  N  NH1   . ARG A 1 502 ? 137.424 156.436 89.512  1.00 32.34 1  502 ARG A NH1   1 
ATOM   4031  N  NH2   . ARG A 1 502 ? 135.412 156.446 90.601  1.00 30.22 ?  502 ARG A NH2   1 
ATOM   4032  N  N     . SER A 1 503 ? 141.565 152.885 92.577  1.00 18.39 ?  503 SER A N     1 
ATOM   4033  C  CA    . SER A 1 503 ? 141.962 153.475 93.852  1.00 23.96 ?  503 SER A CA    1 
ATOM   4034  C  C     . SER A 1 503 ? 142.744 154.764 93.639  1.00 24.98 ?  503 SER A C     1 
ATOM   4035  O  O     . SER A 1 503 ? 142.518 155.761 94.336  1.00 27.44 ?  503 SER A O     1 
ATOM   4036  C  CB    . SER A 1 503 ? 142.785 152.468 94.655  1.00 18.45 ?  503 SER A CB    1 
ATOM   4037  O  OG    . SER A 1 503 ? 142.739 152.757 96.038  1.00 22.93 ?  503 SER A OG    1 
ATOM   4038  N  N     . ALA A 1 504 ? 143.656 154.769 92.665  1.00 27.15 ?  504 ALA A N     1 
ATOM   4039  C  CA    . ALA A 1 504 ? 144.417 155.976 92.363  1.00 25.35 ?  504 ALA A CA    1 
ATOM   4040  C  C     . ALA A 1 504 ? 143.518 157.079 91.818  1.00 30.07 ?  504 ALA A C     1 
ATOM   4041  O  O     . ALA A 1 504 ? 143.696 158.254 92.154  1.00 37.59 ?  504 ALA A O     1 
ATOM   4042  C  CB    . ALA A 1 504 ? 145.536 155.652 91.375  1.00 27.51 ?  504 ALA A CB    1 
ATOM   4043  N  N     . GLU A 1 505 ? 142.546 156.722 90.976  1.00 28.85 ?  505 GLU A N     1 
ATOM   4044  C  CA    . GLU A 1 505 ? 141.616 157.716 90.451  1.00 28.97 ?  505 GLU A CA    1 
ATOM   4045  C  C     . GLU A 1 505 ? 140.742 158.298 91.557  1.00 30.69 ?  505 GLU A C     1 
ATOM   4046  O  O     . GLU A 1 505 ? 140.462 159.501 91.563  1.00 35.21 ?  505 GLU A O     1 
ATOM   4047  C  CB    . GLU A 1 505 ? 140.753 157.098 89.354  1.00 29.45 ?  505 GLU A CB    1 
ATOM   4048  C  CG    . GLU A 1 505 ? 141.499 156.832 88.059  1.00 32.55 ?  505 GLU A CG    1 
ATOM   4049  C  CD    . GLU A 1 505 ? 140.863 155.731 87.235  1.00 35.89 ?  505 GLU A CD    1 
ATOM   4050  O  OE1   . GLU A 1 505 ? 139.803 155.215 87.644  1.00 36.53 ?  505 GLU A OE1   1 
ATOM   4051  O  OE2   . GLU A 1 505 ? 141.425 155.382 86.177  1.00 39.44 -1 505 GLU A OE2   1 
ATOM   4052  N  N     . ILE A 1 506 ? 140.298 157.459 92.494  1.00 28.29 ?  506 ILE A N     1 
ATOM   4053  C  CA    . ILE A 1 506 ? 139.513 157.950 93.622  1.00 25.45 ?  506 ILE A CA    1 
ATOM   4054  C  C     . ILE A 1 506 ? 140.354 158.873 94.495  1.00 28.32 ?  506 ILE A C     1 
ATOM   4055  O  O     . ILE A 1 506 ? 139.877 159.913 94.959  1.00 37.79 ?  506 ILE A O     1 
ATOM   4056  C  CB    . ILE A 1 506 ? 138.941 156.769 94.427  1.00 25.65 ?  506 ILE A CB    1 
ATOM   4057  C  CG1   . ILE A 1 506 ? 137.875 156.037 93.613  1.00 28.37 ?  506 ILE A CG1   1 
ATOM   4058  C  CG2   . ILE A 1 506 ? 138.351 157.248 95.739  1.00 27.04 ?  506 ILE A CG2   1 
ATOM   4059  C  CD1   . ILE A 1 506 ? 137.508 154.684 94.174  1.00 22.37 ?  506 ILE A CD1   1 
ATOM   4060  N  N     . ALA A 1 507 ? 141.617 158.509 94.730  1.00 30.87 ?  507 ALA A N     1 
ATOM   4061  C  CA    . ALA A 1 507 ? 142.503 159.379 95.498  1.00 28.95 ?  507 ALA A CA    1 
ATOM   4062  C  C     . ALA A 1 507 ? 142.716 160.713 94.792  1.00 30.76 ?  507 ALA A C     1 
ATOM   4063  O  O     . ALA A 1 507 ? 142.750 161.766 95.438  1.00 33.56 ?  507 ALA A O     1 
ATOM   4064  C  CB    . ALA A 1 507 ? 143.839 158.679 95.744  1.00 25.37 ?  507 ALA A CB    1 
ATOM   4065  N  N     . LYS A 1 508 ? 142.870 160.686 93.467  1.00 36.54 ?  508 LYS A N     1 
ATOM   4066  C  CA    . LYS A 1 508 ? 143.032 161.923 92.708  1.00 33.53 ?  508 LYS A CA    1 
ATOM   4067  C  C     . LYS A 1 508 ? 141.778 162.787 92.772  1.00 38.04 ?  508 LYS A C     1 
ATOM   4068  O  O     . LYS A 1 508 ? 141.868 164.009 92.932  1.00 44.21 ?  508 LYS A O     1 
ATOM   4069  C  CB    . LYS A 1 508 ? 143.382 161.599 91.257  1.00 36.70 ?  508 LYS A CB    1 
ATOM   4070  C  CG    . LYS A 1 508 ? 143.361 162.801 90.331  1.00 40.47 ?  508 LYS A CG    1 
ATOM   4071  C  CD    . LYS A 1 508 ? 143.352 162.374 88.874  1.00 38.88 ?  508 LYS A CD    1 
ATOM   4072  C  CE    . LYS A 1 508 ? 143.591 163.558 87.953  1.00 39.18 ?  508 LYS A CE    1 
ATOM   4073  N  NZ    . LYS A 1 508 ? 144.405 163.182 86.768  1.00 42.23 1  508 LYS A NZ    1 
ATOM   4074  N  N     . GLU A 1 509 ? 140.602 162.170 92.646  1.00 36.02 ?  509 GLU A N     1 
ATOM   4075  C  CA    . GLU A 1 509 ? 139.357 162.931 92.646  1.00 36.32 ?  509 GLU A CA    1 
ATOM   4076  C  C     . GLU A 1 509 ? 139.077 163.528 94.018  1.00 39.00 ?  509 GLU A C     1 
ATOM   4077  O  O     . GLU A 1 509 ? 138.765 164.719 94.138  1.00 43.38 ?  509 GLU A O     1 
ATOM   4078  C  CB    . GLU A 1 509 ? 138.199 162.037 92.201  1.00 36.42 ?  509 GLU A CB    1 
ATOM   4079  C  CG    . GLU A 1 509 ? 138.182 161.734 90.713  1.00 42.34 ?  509 GLU A CG    1 
ATOM   4080  C  CD    . GLU A 1 509 ? 137.403 160.476 90.383  1.00 44.67 ?  509 GLU A CD    1 
ATOM   4081  O  OE1   . GLU A 1 509 ? 136.760 159.916 91.296  1.00 42.56 ?  509 GLU A OE1   1 
ATOM   4082  O  OE2   . GLU A 1 509 ? 137.431 160.048 89.210  1.00 42.61 -1 509 GLU A OE2   1 
ATOM   4083  N  N     . LYS A 1 510 ? 139.183 162.716 95.069  1.00 35.73 ?  510 LYS A N     1 
ATOM   4084  C  CA    . LYS A 1 510 ? 138.931 163.182 96.425  1.00 31.94 ?  510 LYS A CA    1 
ATOM   4085  C  C     . LYS A 1 510 ? 140.117 163.921 97.027  1.00 34.00 ?  510 LYS A C     1 
ATOM   4086  O  O     . LYS A 1 510 ? 139.977 164.504 98.107  1.00 39.30 ?  510 LYS A O     1 
ATOM   4087  C  CB    . LYS A 1 510 ? 138.550 162.001 97.318  1.00 30.48 ?  510 LYS A CB    1 
ATOM   4088  C  CG    . LYS A 1 510 ? 137.439 161.144 96.743  1.00 33.39 ?  510 LYS A CG    1 
ATOM   4089  C  CD    . LYS A 1 510 ? 136.830 160.231 97.788  1.00 33.07 ?  510 LYS A CD    1 
ATOM   4090  C  CE    . LYS A 1 510 ? 135.702 159.410 97.189  1.00 35.82 ?  510 LYS A CE    1 
ATOM   4091  N  NZ    . LYS A 1 510 ? 134.657 159.075 98.189  1.00 34.70 1  510 LYS A NZ    1 
ATOM   4092  N  N     . GLY A 1 511 ? 141.270 163.910 96.363  1.00 37.13 ?  511 GLY A N     1 
ATOM   4093  C  CA    . GLY A 1 511 ? 142.432 164.619 96.857  1.00 37.04 ?  511 GLY A CA    1 
ATOM   4094  C  C     . GLY A 1 511 ? 143.034 164.063 98.123  1.00 40.69 ?  511 GLY A C     1 
ATOM   4095  O  O     . GLY A 1 511 ? 143.894 164.717 98.720  1.00 42.75 ?  511 GLY A O     1 
ATOM   4096  N  N     . GLU A 1 512 ? 142.614 162.877 98.558  1.00 34.12 ?  512 GLU A N     1 
ATOM   4097  C  CA    . GLU A 1 512 ? 143.119 162.275 99.780  1.00 29.43 ?  512 GLU A CA    1 
ATOM   4098  C  C     . GLU A 1 512 ? 143.452 160.811 99.542  1.00 29.65 ?  512 GLU A C     1 
ATOM   4099  O  O     . GLU A 1 512 ? 142.798 160.125 98.752  1.00 33.10 ?  512 GLU A O     1 
ATOM   4100  C  CB    . GLU A 1 512 ? 142.107 162.401 100.928 1.00 31.02 ?  512 GLU A CB    1 
ATOM   4101  C  CG    . GLU A 1 512 ? 140.763 161.752 100.654 1.00 31.59 ?  512 GLU A CG    1 
ATOM   4102  C  CD    . GLU A 1 512 ? 140.078 161.288 101.921 1.00 35.46 ?  512 GLU A CD    1 
ATOM   4103  O  OE1   . GLU A 1 512 ? 140.790 160.948 102.888 1.00 35.24 ?  512 GLU A OE1   1 
ATOM   4104  O  OE2   . GLU A 1 512 ? 138.830 161.262 101.952 1.00 34.76 -1 512 GLU A OE2   1 
ATOM   4105  N  N     . THR A 1 513 ? 144.484 160.345 100.230 1.00 29.89 ?  513 THR A N     1 
ATOM   4106  C  CA    . THR A 1 513 ? 144.900 158.952 100.232 1.00 25.22 ?  513 THR A CA    1 
ATOM   4107  C  C     . THR A 1 513 ? 144.574 158.336 101.589 1.00 27.22 ?  513 THR A C     1 
ATOM   4108  O  O     . THR A 1 513 ? 144.098 159.011 102.505 1.00 36.88 ?  513 THR A O     1 
ATOM   4109  C  CB    . THR A 1 513 ? 146.393 158.836 99.918  1.00 24.19 ?  513 THR A CB    1 
ATOM   4110  O  OG1   . THR A 1 513 ? 147.145 159.561 100.897 1.00 28.55 ?  513 THR A OG1   1 
ATOM   4111  C  CG2   . THR A 1 513 ? 146.692 159.402 98.543  1.00 23.90 ?  513 THR A CG2   1 
ATOM   4112  N  N     . PHE A 1 514 ? 144.828 157.037 101.718 1.00 23.27 ?  514 PHE A N     1 
ATOM   4113  C  CA    . PHE A 1 514 ? 144.635 156.407 103.012 1.00 25.13 ?  514 PHE A CA    1 
ATOM   4114  C  C     . PHE A 1 514 ? 145.752 156.818 103.966 1.00 25.64 ?  514 PHE A C     1 
ATOM   4115  O  O     . PHE A 1 514 ? 146.847 157.206 103.552 1.00 28.15 ?  514 PHE A O     1 
ATOM   4116  C  CB    . PHE A 1 514 ? 144.552 154.883 102.877 1.00 18.28 ?  514 PHE A CB    1 
ATOM   4117  C  CG    . PHE A 1 514 ? 145.836 154.224 102.460 1.00 19.11 ?  514 PHE A CG    1 
ATOM   4118  C  CD1   . PHE A 1 514 ? 146.137 154.050 101.122 1.00 17.86 ?  514 PHE A CD1   1 
ATOM   4119  C  CD2   . PHE A 1 514 ? 146.726 153.745 103.407 1.00 22.51 ?  514 PHE A CD2   1 
ATOM   4120  C  CE1   . PHE A 1 514 ? 147.307 153.430 100.738 1.00 18.86 ?  514 PHE A CE1   1 
ATOM   4121  C  CE2   . PHE A 1 514 ? 147.895 153.125 103.027 1.00 17.63 ?  514 PHE A CE2   1 
ATOM   4122  C  CZ    . PHE A 1 514 ? 148.187 152.970 101.691 1.00 18.53 ?  514 PHE A CZ    1 
ATOM   4123  N  N     . ASP A 1 515 ? 145.452 156.751 105.260 1.00 29.13 ?  515 ASP A N     1 
ATOM   4124  C  CA    . ASP A 1 515 ? 146.386 157.229 106.270 1.00 27.15 ?  515 ASP A CA    1 
ATOM   4125  C  C     . ASP A 1 515 ? 147.697 156.457 106.206 1.00 29.36 ?  515 ASP A C     1 
ATOM   4126  O  O     . ASP A 1 515 ? 147.712 155.230 106.079 1.00 35.37 ?  515 ASP A O     1 
ATOM   4127  C  CB    . ASP A 1 515 ? 145.770 157.105 107.662 1.00 30.15 ?  515 ASP A CB    1 
ATOM   4128  C  CG    . ASP A 1 515 ? 144.863 158.271 108.001 1.00 38.05 ?  515 ASP A CG    1 
ATOM   4129  O  OD1   . ASP A 1 515 ? 144.367 158.933 107.066 1.00 36.62 ?  515 ASP A OD1   1 
ATOM   4130  O  OD2   . ASP A 1 515 ? 144.647 158.523 109.205 1.00 38.93 -1 515 ASP A OD2   1 
ATOM   4131  N  N     . GLN A 1 516 ? 148.803 157.196 106.301 1.00 27.50 ?  516 GLN A N     1 
ATOM   4132  C  CA    . GLN A 1 516 ? 150.151 156.636 106.201 1.00 28.05 ?  516 GLN A CA    1 
ATOM   4133  C  C     . GLN A 1 516 ? 150.365 155.935 104.862 1.00 25.00 ?  516 GLN A C     1 
ATOM   4134  O  O     . GLN A 1 516 ? 150.995 154.879 104.786 1.00 33.02 ?  516 GLN A O     1 
ATOM   4135  C  CB    . GLN A 1 516 ? 150.449 155.685 107.365 1.00 25.48 ?  516 GLN A CB    1 
ATOM   4136  C  CG    . GLN A 1 516 ? 150.294 156.311 108.738 1.00 27.14 ?  516 GLN A CG    1 
ATOM   4137  C  CD    . GLN A 1 516 ? 150.579 155.329 109.853 1.00 29.50 ?  516 GLN A CD    1 
ATOM   4138  O  OE1   . GLN A 1 516 ? 151.729 154.963 110.093 1.00 29.48 ?  516 GLN A OE1   1 
ATOM   4139  N  NE2   . GLN A 1 516 ? 149.532 154.898 110.543 1.00 28.58 ?  516 GLN A NE2   1 
ATOM   4140  N  N     . TYR A 1 517 ? 149.829 156.523 103.792 1.00 23.76 ?  517 TYR A N     1 
ATOM   4141  C  CA    . TYR A 1 517 ? 150.076 155.975 102.463 1.00 23.56 ?  517 TYR A CA    1 
ATOM   4142  C  C     . TYR A 1 517 ? 151.524 156.171 102.035 1.00 27.07 ?  517 TYR A C     1 
ATOM   4143  O  O     . TYR A 1 517 ? 152.086 155.308 101.352 1.00 34.91 ?  517 TYR A O     1 
ATOM   4144  C  CB    . TYR A 1 517 ? 149.141 156.609 101.431 1.00 24.34 ?  517 TYR A CB    1 
ATOM   4145  C  CG    . TYR A 1 517 ? 149.718 156.599 100.032 1.00 26.69 ?  517 TYR A CG    1 
ATOM   4146  C  CD1   . TYR A 1 517 ? 149.677 155.449 99.254  1.00 21.22 ?  517 TYR A CD1   1 
ATOM   4147  C  CD2   . TYR A 1 517 ? 150.318 157.731 99.497  1.00 25.97 ?  517 TYR A CD2   1 
ATOM   4148  C  CE1   . TYR A 1 517 ? 150.209 155.429 97.985  1.00 27.38 ?  517 TYR A CE1   1 
ATOM   4149  C  CE2   . TYR A 1 517 ? 150.856 157.717 98.231  1.00 25.76 ?  517 TYR A CE2   1 
ATOM   4150  C  CZ    . TYR A 1 517 ? 150.800 156.564 97.479  1.00 26.31 ?  517 TYR A CZ    1 
ATOM   4151  O  OH    . TYR A 1 517 ? 151.331 156.551 96.211  1.00 34.34 ?  517 TYR A OH    1 
ATOM   4152  N  N     . GLU A 1 518 ? 152.138 157.291 102.419 1.00 30.87 ?  518 GLU A N     1 
ATOM   4153  C  CA    . GLU A 1 518 ? 153.469 157.627 101.922 1.00 33.64 ?  518 GLU A CA    1 
ATOM   4154  C  C     . GLU A 1 518 ? 154.524 156.611 102.340 1.00 35.51 ?  518 GLU A C     1 
ATOM   4155  O  O     . GLU A 1 518 ? 155.551 156.490 101.664 1.00 38.35 ?  518 GLU A O     1 
ATOM   4156  C  CB    . GLU A 1 518 ? 153.868 159.023 102.399 1.00 34.11 ?  518 GLU A CB    1 
ATOM   4157  C  CG    . GLU A 1 518 ? 153.087 160.153 101.745 1.00 36.55 ?  518 GLU A CG    1 
ATOM   4158  C  CD    . GLU A 1 518 ? 153.337 160.260 100.250 1.00 43.50 ?  518 GLU A CD    1 
ATOM   4159  O  OE1   . GLU A 1 518 ? 154.399 159.798 99.781  1.00 39.21 ?  518 GLU A OE1   1 
ATOM   4160  O  OE2   . GLU A 1 518 ? 152.469 160.812 99.542  1.00 40.04 -1 518 GLU A OE2   1 
ATOM   4161  N  N     . GLY A 1 519 ? 154.303 155.886 103.434 1.00 24.41 ?  519 GLY A N     1 
ATOM   4162  C  CA    . GLY A 1 519 ? 155.204 154.825 103.828 1.00 20.56 ?  519 GLY A CA    1 
ATOM   4163  C  C     . GLY A 1 519 ? 154.941 153.482 103.195 1.00 21.97 ?  519 GLY A C     1 
ATOM   4164  O  O     . GLY A 1 519 ? 155.734 152.554 103.382 1.00 31.43 ?  519 GLY A O     1 
ATOM   4165  N  N     . SER A 1 520 ? 153.849 153.349 102.448 1.00 22.12 ?  520 SER A N     1 
ATOM   4166  C  CA    . SER A 1 520 ? 153.471 152.085 101.840 1.00 24.05 ?  520 SER A CA    1 
ATOM   4167  C  C     . SER A 1 520 ? 154.352 151.778 100.632 1.00 22.41 ?  520 SER A C     1 
ATOM   4168  O  O     . SER A 1 520 ? 155.075 152.635 100.118 1.00 27.98 ?  520 SER A O     1 
ATOM   4169  C  CB    . SER A 1 520 ? 152.000 152.110 101.430 1.00 20.05 ?  520 SER A CB    1 
ATOM   4170  O  OG    . SER A 1 520 ? 151.757 153.142 100.491 1.00 20.38 ?  520 SER A OG    1 
ATOM   4171  N  N     . THR A 1 521 ? 154.283 150.527 100.174 1.00 20.89 ?  521 THR A N     1 
ATOM   4172  C  CA    . THR A 1 521 ? 155.051 150.124 99.003  1.00 19.04 ?  521 THR A CA    1 
ATOM   4173  C  C     . THR A 1 521 ? 154.471 150.689 97.715  1.00 25.45 ?  521 THR A C     1 
ATOM   4174  O  O     . THR A 1 521 ? 155.181 150.751 96.706  1.00 28.88 ?  521 THR A O     1 
ATOM   4175  C  CB    . THR A 1 521 ? 155.121 148.601 98.909  1.00 28.33 ?  521 THR A CB    1 
ATOM   4176  O  OG1   . THR A 1 521 ? 153.796 148.061 98.934  1.00 29.39 ?  521 THR A OG1   1 
ATOM   4177  C  CG2   . THR A 1 521 ? 155.908 148.037 100.078 1.00 20.51 ?  521 THR A CG2   1 
ATOM   4178  N  N     . TYR A 1 522 ? 153.197 151.089 97.720  1.00 28.74 ?  522 TYR A N     1 
ATOM   4179  C  CA    . TYR A 1 522 ? 152.649 151.804 96.573  1.00 21.52 ?  522 TYR A CA    1 
ATOM   4180  C  C     . TYR A 1 522 ? 153.349 153.142 96.383  1.00 25.88 ?  522 TYR A C     1 
ATOM   4181  O  O     . TYR A 1 522 ? 153.679 153.526 95.255  1.00 29.89 ?  522 TYR A O     1 
ATOM   4182  C  CB    . TYR A 1 522 ? 151.145 152.017 96.743  1.00 18.60 ?  522 TYR A CB    1 
ATOM   4183  C  CG    . TYR A 1 522 ? 150.347 150.765 97.022  1.00 21.92 ?  522 TYR A CG    1 
ATOM   4184  C  CD1   . TYR A 1 522 ? 150.111 149.831 96.023  1.00 21.23 ?  522 TYR A CD1   1 
ATOM   4185  C  CD2   . TYR A 1 522 ? 149.803 150.533 98.277  1.00 23.68 ?  522 TYR A CD2   1 
ATOM   4186  C  CE1   . TYR A 1 522 ? 149.373 148.693 96.272  1.00 20.05 ?  522 TYR A CE1   1 
ATOM   4187  C  CE2   . TYR A 1 522 ? 149.061 149.400 98.534  1.00 22.90 ?  522 TYR A CE2   1 
ATOM   4188  C  CZ    . TYR A 1 522 ? 148.851 148.483 97.528  1.00 23.08 ?  522 TYR A CZ    1 
ATOM   4189  O  OH    . TYR A 1 522 ? 148.113 147.351 97.781  1.00 27.20 ?  522 TYR A OH    1 
ATOM   4190  N  N     . ALA A 1 523 ? 153.578 153.869 97.479  1.00 28.81 ?  523 ALA A N     1 
ATOM   4191  C  CA    . ALA A 1 523 ? 154.233 155.169 97.387  1.00 26.99 ?  523 ALA A CA    1 
ATOM   4192  C  C     . ALA A 1 523 ? 155.694 155.028 96.984  1.00 28.38 ?  523 ALA A C     1 
ATOM   4193  O  O     . ALA A 1 523 ? 156.198 155.809 96.169  1.00 32.27 ?  523 ALA A O     1 
ATOM   4194  C  CB    . ALA A 1 523 ? 154.110 155.911 98.717  1.00 23.69 ?  523 ALA A CB    1 
ATOM   4195  N  N     . THR A 1 524 ? 156.392 154.039 97.547  1.00 29.12 ?  524 THR A N     1 
ATOM   4196  C  CA    . THR A 1 524 ? 157.790 153.825 97.199  1.00 28.63 ?  524 THR A CA    1 
ATOM   4197  C  C     . THR A 1 524 ? 157.955 153.186 95.828  1.00 31.29 ?  524 THR A C     1 
ATOM   4198  O  O     . THR A 1 524 ? 159.054 153.236 95.265  1.00 36.00 ?  524 THR A O     1 
ATOM   4199  C  CB    . THR A 1 524 ? 158.469 152.956 98.257  1.00 30.58 ?  524 THR A CB    1 
ATOM   4200  O  OG1   . THR A 1 524 ? 157.996 151.608 98.148  1.00 32.71 ?  524 THR A OG1   1 
ATOM   4201  C  CG2   . THR A 1 524 ? 158.169 153.482 99.651  1.00 27.59 ?  524 THR A CG2   1 
ATOM   4202  N  N     . GLY A 1 525 ? 156.896 152.593 95.279  1.00 25.73 ?  525 GLY A N     1 
ATOM   4203  C  CA    . GLY A 1 525 ? 156.964 151.938 93.992  1.00 27.99 ?  525 GLY A CA    1 
ATOM   4204  C  C     . GLY A 1 525 ? 157.479 150.517 94.019  1.00 32.06 ?  525 GLY A C     1 
ATOM   4205  O  O     . GLY A 1 525 ? 157.544 149.882 92.959  1.00 31.32 ?  525 GLY A O     1 
ATOM   4206  N  N     . GLU A 1 526 ? 157.850 149.999 95.190  1.00 32.87 ?  526 GLU A N     1 
ATOM   4207  C  CA    . GLU A 1 526 ? 158.332 148.627 95.289  1.00 33.19 ?  526 GLU A CA    1 
ATOM   4208  C  C     . GLU A 1 526 ? 157.227 147.613 95.026  1.00 36.82 ?  526 GLU A C     1 
ATOM   4209  O  O     . GLU A 1 526 ? 157.515 146.501 94.567  1.00 40.66 ?  526 GLU A O     1 
ATOM   4210  C  CB    . GLU A 1 526 ? 158.965 148.409 96.668  1.00 33.10 ?  526 GLU A CB    1 
ATOM   4211  C  CG    . GLU A 1 526 ? 159.004 146.971 97.154  1.00 33.56 ?  526 GLU A CG    1 
ATOM   4212  C  CD    . GLU A 1 526 ? 159.056 146.871 98.665  1.00 40.85 ?  526 GLU A CD    1 
ATOM   4213  O  OE1   . GLU A 1 526 ? 159.074 147.926 99.331  1.00 44.68 ?  526 GLU A OE1   1 
ATOM   4214  O  OE2   . GLU A 1 526 ? 159.081 145.736 99.186  1.00 39.17 -1 526 GLU A OE2   1 
ATOM   4215  N  N     . TYR A 1 527 ? 155.969 147.984 95.277  1.00 34.23 ?  527 TYR A N     1 
ATOM   4216  C  CA    . TYR A 1 527 ? 154.853 147.076 95.028  1.00 25.64 ?  527 TYR A CA    1 
ATOM   4217  C  C     . TYR A 1 527 ? 154.770 146.668 93.562  1.00 26.99 ?  527 TYR A C     1 
ATOM   4218  O  O     . TYR A 1 527 ? 154.377 145.538 93.256  1.00 29.87 ?  527 TYR A O     1 
ATOM   4219  C  CB    . TYR A 1 527 ? 153.543 147.731 95.470  1.00 22.95 ?  527 TYR A CB    1 
ATOM   4220  C  CG    . TYR A 1 527 ? 152.312 146.889 95.225  1.00 27.51 ?  527 TYR A CG    1 
ATOM   4221  C  CD1   . TYR A 1 527 ? 151.861 145.991 96.183  1.00 24.78 ?  527 TYR A CD1   1 
ATOM   4222  C  CD2   . TYR A 1 527 ? 151.597 146.994 94.040  1.00 28.27 ?  527 TYR A CD2   1 
ATOM   4223  C  CE1   . TYR A 1 527 ? 150.738 145.220 95.964  1.00 26.06 ?  527 TYR A CE1   1 
ATOM   4224  C  CE2   . TYR A 1 527 ? 150.477 146.226 93.813  1.00 24.90 ?  527 TYR A CE2   1 
ATOM   4225  C  CZ    . TYR A 1 527 ? 150.050 145.343 94.778  1.00 18.91 ?  527 TYR A CZ    1 
ATOM   4226  O  OH    . TYR A 1 527 ? 148.931 144.578 94.555  1.00 30.61 ?  527 TYR A OH    1 
ATOM   4227  N  N     . PHE A 1 528 ? 155.134 147.566 92.650  1.00 29.56 ?  528 PHE A N     1 
ATOM   4228  C  CA    . PHE A 1 528 ? 154.957 147.354 91.222  1.00 28.24 ?  528 PHE A CA    1 
ATOM   4229  C  C     . PHE A 1 528 ? 156.154 146.684 90.558  1.00 34.05 ?  528 PHE A C     1 
ATOM   4230  O  O     . PHE A 1 528 ? 156.212 146.644 89.327  1.00 41.91 ?  528 PHE A O     1 
ATOM   4231  C  CB    . PHE A 1 528 ? 154.675 148.687 90.525  1.00 29.14 ?  528 PHE A CB    1 
ATOM   4232  C  CG    . PHE A 1 528 ? 153.478 149.415 91.061  1.00 31.18 ?  528 PHE A CG    1 
ATOM   4233  C  CD1   . PHE A 1 528 ? 153.605 150.310 92.109  1.00 29.96 ?  528 PHE A CD1   1 
ATOM   4234  C  CD2   . PHE A 1 528 ? 152.225 149.213 90.510  1.00 29.03 ?  528 PHE A CD2   1 
ATOM   4235  C  CE1   . PHE A 1 528 ? 152.505 150.984 92.599  1.00 32.17 ?  528 PHE A CE1   1 
ATOM   4236  C  CE2   . PHE A 1 528 ? 151.122 149.884 90.997  1.00 29.46 ?  528 PHE A CE2   1 
ATOM   4237  C  CZ    . PHE A 1 528 ? 151.262 150.770 92.042  1.00 28.16 ?  528 PHE A CZ    1 
ATOM   4238  N  N     . ASP A 1 529 ? 157.105 146.162 91.338  1.00 34.97 ?  529 ASP A N     1 
ATOM   4239  C  CA    . ASP A 1 529 ? 158.334 145.627 90.757  1.00 32.88 ?  529 ASP A CA    1 
ATOM   4240  C  C     . ASP A 1 529 ? 158.048 144.452 89.829  1.00 34.45 ?  529 ASP A C     1 
ATOM   4241  O  O     . ASP A 1 529 ? 158.471 144.445 88.665  1.00 41.56 ?  529 ASP A O     1 
ATOM   4242  C  CB    . ASP A 1 529 ? 159.293 145.205 91.870  1.00 35.83 ?  529 ASP A CB    1 
ATOM   4243  C  CG    . ASP A 1 529 ? 160.018 146.380 92.491  1.00 42.01 ?  529 ASP A CG    1 
ATOM   4244  O  OD1   . ASP A 1 529 ? 159.934 147.495 91.937  1.00 41.20 ?  529 ASP A OD1   1 
ATOM   4245  O  OD2   . ASP A 1 529 ? 160.675 146.187 93.536  1.00 42.29 -1 529 ASP A OD2   1 
ATOM   4246  N  N     . LYS A 1 530 ? 157.318 143.450 90.324  1.00 37.67 ?  530 LYS A N     1 
ATOM   4247  C  CA    . LYS A 1 530 ? 157.011 142.282 89.508  1.00 38.51 ?  530 LYS A CA    1 
ATOM   4248  C  C     . LYS A 1 530 ? 156.054 142.612 88.374  1.00 36.82 ?  530 LYS A C     1 
ATOM   4249  O  O     . LYS A 1 530 ? 155.970 141.848 87.407  1.00 40.77 ?  530 LYS A O     1 
ATOM   4250  C  CB    . LYS A 1 530 ? 156.426 141.168 90.375  1.00 38.22 ?  530 LYS A CB    1 
ATOM   4251  C  CG    . LYS A 1 530 ? 154.911 141.174 90.464  1.00 32.22 ?  530 LYS A CG    1 
ATOM   4252  C  CD    . LYS A 1 530 ? 154.420 140.196 91.511  1.00 34.28 ?  530 LYS A CD    1 
ATOM   4253  C  CE    . LYS A 1 530 ? 152.908 140.120 91.522  1.00 34.98 ?  530 LYS A CE    1 
ATOM   4254  N  NZ    . LYS A 1 530 ? 152.378 140.238 92.904  1.00 38.69 1  530 LYS A NZ    1 
ATOM   4255  N  N     . TYR A 1 531 ? 155.336 143.724 88.468  1.00 32.53 ?  531 TYR A N     1 
ATOM   4256  C  CA    . TYR A 1 531 ? 154.409 144.117 87.420  1.00 28.43 ?  531 TYR A CA    1 
ATOM   4257  C  C     . TYR A 1 531 ? 155.083 144.913 86.315  1.00 29.37 ?  531 TYR A C     1 
ATOM   4258  O  O     . TYR A 1 531 ? 154.682 144.804 85.151  1.00 35.21 ?  531 TYR A O     1 
ATOM   4259  C  CB    . TYR A 1 531 ? 153.263 144.924 88.024  1.00 25.66 ?  531 TYR A CB    1 
ATOM   4260  C  CG    . TYR A 1 531 ? 152.286 144.079 88.799  1.00 29.92 ?  531 TYR A CG    1 
ATOM   4261  C  CD1   . TYR A 1 531 ? 151.693 142.968 88.217  1.00 29.59 ?  531 TYR A CD1   1 
ATOM   4262  C  CD2   . TYR A 1 531 ? 151.958 144.384 90.111  1.00 27.27 ?  531 TYR A CD2   1 
ATOM   4263  C  CE1   . TYR A 1 531 ? 150.798 142.188 88.916  1.00 32.41 ?  531 TYR A CE1   1 
ATOM   4264  C  CE2   . TYR A 1 531 ? 151.065 143.610 90.818  1.00 25.93 ?  531 TYR A CE2   1 
ATOM   4265  C  CZ    . TYR A 1 531 ? 150.487 142.514 90.215  1.00 28.95 ?  531 TYR A CZ    1 
ATOM   4266  O  OH    . TYR A 1 531 ? 149.596 141.738 90.915  1.00 30.57 ?  531 TYR A OH    1 
ATOM   4267  N  N     . VAL A 1 532 ? 156.102 145.708 86.650  1.00 36.10 ?  532 VAL A N     1 
ATOM   4268  C  CA    . VAL A 1 532 ? 156.883 146.404 85.634  1.00 35.37 ?  532 VAL A CA    1 
ATOM   4269  C  C     . VAL A 1 532 ? 158.006 145.543 85.079  1.00 37.91 ?  532 VAL A C     1 
ATOM   4270  O  O     . VAL A 1 532 ? 158.586 145.895 84.039  1.00 42.70 ?  532 VAL A O     1 
ATOM   4271  C  CB    . VAL A 1 532 ? 157.474 147.719 86.185  1.00 36.98 ?  532 VAL A CB    1 
ATOM   4272  C  CG1   . VAL A 1 532 ? 156.368 148.612 86.724  1.00 33.66 ?  532 VAL A CG1   1 
ATOM   4273  C  CG2   . VAL A 1 532 ? 158.513 147.433 87.256  1.00 36.45 ?  532 VAL A CG2   1 
ATOM   4274  N  N     . SER A 1 533 ? 158.333 144.426 85.729  1.00 37.93 ?  533 SER A N     1 
ATOM   4275  C  CA    . SER A 1 533 ? 159.383 143.535 85.249  1.00 36.60 ?  533 SER A CA    1 
ATOM   4276  C  C     . SER A 1 533 ? 158.846 142.302 84.535  1.00 41.39 ?  533 SER A C     1 
ATOM   4277  O  O     . SER A 1 533 ? 159.414 141.885 83.522  1.00 43.93 ?  533 SER A O     1 
ATOM   4278  C  CB    . SER A 1 533 ? 160.274 143.095 86.413  1.00 41.09 ?  533 SER A CB    1 
ATOM   4279  O  OG    . SER A 1 533 ? 159.716 141.984 87.093  1.00 42.74 ?  533 SER A OG    1 
ATOM   4280  N  N     . THR A 1 534 ? 157.766 141.708 85.035  1.00 42.79 ?  534 THR A N     1 
ATOM   4281  C  CA    . THR A 1 534 ? 157.235 140.459 84.509  1.00 38.26 ?  534 THR A CA    1 
ATOM   4282  C  C     . THR A 1 534 ? 155.931 140.711 83.765  1.00 37.89 ?  534 THR A C     1 
ATOM   4283  O  O     . THR A 1 534 ? 155.060 141.441 84.247  1.00 42.30 ?  534 THR A O     1 
ATOM   4284  C  CB    . THR A 1 534 ? 157.003 139.447 85.637  1.00 36.43 ?  534 THR A CB    1 
ATOM   4285  O  OG1   . THR A 1 534 ? 158.260 139.071 86.212  1.00 42.70 ?  534 THR A OG1   1 
ATOM   4286  C  CG2   . THR A 1 534 ? 156.301 138.201 85.116  1.00 39.87 ?  534 THR A CG2   1 
ATOM   4287  N  N     . ASP A 1 535 ? 155.808 140.110 82.584  1.00 40.76 ?  535 ASP A N     1 
ATOM   4288  C  CA    . ASP A 1 535 ? 154.578 140.165 81.808  1.00 41.03 ?  535 ASP A CA    1 
ATOM   4289  C  C     . ASP A 1 535 ? 153.658 139.030 82.237  1.00 44.13 ?  535 ASP A C     1 
ATOM   4290  O  O     . ASP A 1 535 ? 154.102 137.889 82.398  1.00 45.35 ?  535 ASP A O     1 
ATOM   4291  C  CB    . ASP A 1 535 ? 154.878 140.069 80.313  1.00 41.69 ?  535 ASP A CB    1 
ATOM   4292  C  CG    . ASP A 1 535 ? 153.664 139.670 79.498  1.00 47.77 ?  535 ASP A CG    1 
ATOM   4293  O  OD1   . ASP A 1 535 ? 152.820 140.548 79.216  1.00 48.39 ?  535 ASP A OD1   1 
ATOM   4294  O  OD2   . ASP A 1 535 ? 153.552 138.478 79.143  1.00 46.71 -1 535 ASP A OD2   1 
ATOM   4295  N  N     . PHE A 1 536 ? 152.376 139.345 82.425  1.00 33.07 ?  536 PHE A N     1 
ATOM   4296  C  CA    . PHE A 1 536 ? 151.395 138.372 82.884  1.00 31.59 ?  536 PHE A CA    1 
ATOM   4297  C  C     . PHE A 1 536 ? 150.366 138.037 81.811  1.00 38.43 ?  536 PHE A C     1 
ATOM   4298  O  O     . PHE A 1 536 ? 149.259 137.598 82.132  1.00 40.84 ?  536 PHE A O     1 
ATOM   4299  C  CB    . PHE A 1 536 ? 150.705 138.876 84.151  1.00 32.63 ?  536 PHE A CB    1 
ATOM   4300  C  CG    . PHE A 1 536 ? 151.620 138.976 85.338  1.00 33.32 ?  536 PHE A CG    1 
ATOM   4301  C  CD1   . PHE A 1 536 ? 152.367 140.118 85.558  1.00 32.41 ?  536 PHE A CD1   1 
ATOM   4302  C  CD2   . PHE A 1 536 ? 151.739 137.923 86.227  1.00 29.13 ?  536 PHE A CD2   1 
ATOM   4303  C  CE1   . PHE A 1 536 ? 153.211 140.209 86.647  1.00 33.49 ?  536 PHE A CE1   1 
ATOM   4304  C  CE2   . PHE A 1 536 ? 152.582 138.008 87.315  1.00 28.57 ?  536 PHE A CE2   1 
ATOM   4305  C  CZ    . PHE A 1 536 ? 153.317 139.153 87.526  1.00 31.83 ?  536 PHE A CZ    1 
ATOM   4306  N  N     . SER A 1 537 ? 150.711 138.246 80.543  1.00 39.75 ?  537 SER A N     1 
ATOM   4307  C  CA    . SER A 1 537 ? 149.857 137.820 79.450  1.00 37.63 ?  537 SER A CA    1 
ATOM   4308  C  C     . SER A 1 537 ? 149.762 136.294 79.433  1.00 38.56 ?  537 SER A C     1 
ATOM   4309  O  O     . SER A 1 537 ? 150.706 135.606 79.831  1.00 43.02 ?  537 SER A O     1 
ATOM   4310  C  CB    . SER A 1 537 ? 150.411 138.332 78.122  1.00 38.04 ?  537 SER A CB    1 
ATOM   4311  O  OG    . SER A 1 537 ? 149.527 138.076 77.046  1.00 45.62 ?  537 SER A OG    1 
ATOM   4312  N  N     . PRO A 1 538 ? 148.628 135.741 78.999  1.00 39.69 ?  538 PRO A N     1 
ATOM   4313  C  CA    . PRO A 1 538 ? 148.479 134.281 78.999  1.00 38.42 ?  538 PRO A CA    1 
ATOM   4314  C  C     . PRO A 1 538 ? 149.538 133.603 78.143  1.00 41.89 ?  538 PRO A C     1 
ATOM   4315  O  O     . PRO A 1 538 ? 149.879 134.070 77.053  1.00 40.90 ?  538 PRO A O     1 
ATOM   4316  C  CB    . PRO A 1 538 ? 147.074 134.067 78.427  1.00 37.81 ?  538 PRO A CB    1 
ATOM   4317  C  CG    . PRO A 1 538 ? 146.365 135.351 78.663  1.00 39.79 ?  538 PRO A CG    1 
ATOM   4318  C  CD    . PRO A 1 538 ? 147.403 136.419 78.545  1.00 37.05 ?  538 PRO A CD    1 
ATOM   4319  N  N     . LYS A 1 539 ? 150.058 132.486 78.651  1.00 42.14 ?  539 LYS A N     1 
ATOM   4320  C  CA    . LYS A 1 539 ? 151.077 131.715 77.954  1.00 41.99 ?  539 LYS A CA    1 
ATOM   4321  C  C     . LYS A 1 539 ? 150.496 130.654 77.029  1.00 44.20 ?  539 LYS A C     1 
ATOM   4322  O  O     . LYS A 1 539 ? 151.248 130.051 76.257  1.00 48.33 ?  539 LYS A O     1 
ATOM   4323  C  CB    . LYS A 1 539 ? 152.016 131.045 78.962  1.00 44.26 ?  539 LYS A CB    1 
ATOM   4324  C  CG    . LYS A 1 539 ? 152.311 131.885 80.191  1.00 46.33 ?  539 LYS A CG    1 
ATOM   4325  C  CD    . LYS A 1 539 ? 153.634 132.622 80.055  1.00 45.75 ?  539 LYS A CD    1 
ATOM   4326  C  CE    . LYS A 1 539 ? 153.737 133.757 81.061  1.00 46.33 ?  539 LYS A CE    1 
ATOM   4327  N  NZ    . LYS A 1 539 ? 152.934 134.942 80.649  1.00 44.50 1  539 LYS A NZ    1 
ATOM   4328  N  N     . TYR A 1 540 ? 149.191 130.413 77.087  1.00 43.85 ?  540 TYR A N     1 
ATOM   4329  C  CA    . TYR A 1 540 ? 148.535 129.411 76.263  1.00 43.78 ?  540 TYR A CA    1 
ATOM   4330  C  C     . TYR A 1 540 ? 147.582 130.082 75.283  1.00 46.70 ?  540 TYR A C     1 
ATOM   4331  O  O     . TYR A 1 540 ? 146.892 131.045 75.634  1.00 45.29 ?  540 TYR A O     1 
ATOM   4332  C  CB    . TYR A 1 540 ? 147.776 128.397 77.124  1.00 41.74 ?  540 TYR A CB    1 
ATOM   4333  C  CG    . TYR A 1 540 ? 148.660 127.669 78.109  1.00 45.65 ?  540 TYR A CG    1 
ATOM   4334  C  CD1   . TYR A 1 540 ? 148.918 128.196 79.366  1.00 45.44 ?  540 TYR A CD1   1 
ATOM   4335  C  CD2   . TYR A 1 540 ? 149.248 126.457 77.774  1.00 45.66 ?  540 TYR A CD2   1 
ATOM   4336  C  CE1   . TYR A 1 540 ? 149.730 127.535 80.263  1.00 46.54 ?  540 TYR A CE1   1 
ATOM   4337  C  CE2   . TYR A 1 540 ? 150.061 125.788 78.664  1.00 41.75 ?  540 TYR A CE2   1 
ATOM   4338  C  CZ    . TYR A 1 540 ? 150.299 126.331 79.908  1.00 45.77 ?  540 TYR A CZ    1 
ATOM   4339  O  OH    . TYR A 1 540 ? 151.111 125.667 80.796  1.00 45.71 ?  540 TYR A OH    1 
ATOM   4340  N  N     . GLU A 1 541 ? 147.558 129.571 74.050  1.00 49.36 ?  541 GLU A N     1 
ATOM   4341  C  CA    . GLU A 1 541 ? 146.685 130.142 73.032  1.00 47.22 ?  541 GLU A CA    1 
ATOM   4342  C  C     . GLU A 1 541 ? 145.215 129.953 73.384  1.00 49.17 ?  541 GLU A C     1 
ATOM   4343  O  O     . GLU A 1 541 ? 144.382 130.793 73.031  1.00 47.50 ?  541 GLU A O     1 
ATOM   4344  C  CB    . GLU A 1 541 ? 147.001 129.533 71.663  1.00 48.57 ?  541 GLU A CB    1 
ATOM   4345  C  CG    . GLU A 1 541 ? 146.444 128.132 71.426  1.00 52.66 ?  541 GLU A CG    1 
ATOM   4346  C  CD    . GLU A 1 541 ? 147.152 127.066 72.245  1.00 57.43 ?  541 GLU A CD    1 
ATOM   4347  O  OE1   . GLU A 1 541 ? 148.284 127.319 72.710  1.00 55.11 ?  541 GLU A OE1   1 
ATOM   4348  O  OE2   . GLU A 1 541 ? 146.576 125.972 72.421  1.00 52.48 -1 541 GLU A OE2   1 
ATOM   4349  N  N     . LYS A 1 542 ? 144.878 128.862 74.078  1.00 47.03 ?  542 LYS A N     1 
ATOM   4350  C  CA    . LYS A 1 542 ? 143.500 128.661 74.511  1.00 44.20 ?  542 LYS A CA    1 
ATOM   4351  C  C     . LYS A 1 542 ? 143.070 129.742 75.493  1.00 43.71 ?  542 LYS A C     1 
ATOM   4352  O  O     . LYS A 1 542 ? 141.955 130.269 75.402  1.00 46.35 ?  542 LYS A O     1 
ATOM   4353  C  CB    . LYS A 1 542 ? 143.346 127.276 75.138  1.00 42.74 ?  542 LYS A CB    1 
ATOM   4354  C  CG    . LYS A 1 542 ? 141.906 126.849 75.353  1.00 44.00 ?  542 LYS A CG    1 
ATOM   4355  C  CD    . LYS A 1 542 ? 141.805 125.791 76.439  1.00 44.81 ?  542 LYS A CD    1 
ATOM   4356  C  CE    . LYS A 1 542 ? 140.472 125.066 76.381  1.00 46.45 ?  542 LYS A CE    1 
ATOM   4357  N  NZ    . LYS A 1 542 ? 139.335 126.009 76.202  1.00 47.24 1  542 LYS A NZ    1 
ATOM   4358  N  N     . ILE A 1 543 ? 143.941 130.081 76.444  1.00 40.29 ?  543 ILE A N     1 
ATOM   4359  C  CA    . ILE A 1 543 ? 143.622 131.118 77.418  1.00 38.16 ?  543 ILE A CA    1 
ATOM   4360  C  C     . ILE A 1 543 ? 143.635 132.493 76.762  1.00 39.04 ?  543 ILE A C     1 
ATOM   4361  O  O     . ILE A 1 543 ? 142.822 133.362 77.097  1.00 41.31 ?  543 ILE A O     1 
ATOM   4362  C  CB    . ILE A 1 543 ? 144.594 131.043 78.608  1.00 38.43 ?  543 ILE A CB    1 
ATOM   4363  C  CG1   . ILE A 1 543 ? 144.568 129.647 79.230  1.00 38.67 ?  543 ILE A CG1   1 
ATOM   4364  C  CG2   . ILE A 1 543 ? 144.246 132.091 79.644  1.00 39.41 ?  543 ILE A CG2   1 
ATOM   4365  C  CD1   . ILE A 1 543 ? 143.177 129.129 79.519  1.00 37.81 ?  543 ILE A CD1   1 
ATOM   4366  N  N     . ALA A 1 544 ? 144.561 132.715 75.826  1.00 41.27 ?  544 ALA A N     1 
ATOM   4367  C  CA    . ALA A 1 544 ? 144.663 134.019 75.179  1.00 43.83 ?  544 ALA A CA    1 
ATOM   4368  C  C     . ALA A 1 544 ? 143.409 134.359 74.385  1.00 43.06 ?  544 ALA A C     1 
ATOM   4369  O  O     . ALA A 1 544 ? 143.066 135.539 74.246  1.00 43.78 ?  544 ALA A O     1 
ATOM   4370  C  CB    . ALA A 1 544 ? 145.892 134.058 74.270  1.00 44.54 ?  544 ALA A CB    1 
ATOM   4371  N  N     . ASN A 1 545 ? 142.715 133.350 73.853  1.00 44.96 ?  545 ASN A N     1 
ATOM   4372  C  CA    . ASN A 1 545 ? 141.463 133.615 73.153  1.00 46.63 ?  545 ASN A CA    1 
ATOM   4373  C  C     . ASN A 1 545 ? 140.337 133.947 74.121  1.00 46.37 ?  545 ASN A C     1 
ATOM   4374  O  O     . ASN A 1 545 ? 139.377 134.625 73.741  1.00 45.67 ?  545 ASN A O     1 
ATOM   4375  C  CB    . ASN A 1 545 ? 141.078 132.422 72.278  1.00 46.98 ?  545 ASN A CB    1 
ATOM   4376  C  CG    . ASN A 1 545 ? 142.207 131.975 71.372  1.00 50.71 ?  545 ASN A CG    1 
ATOM   4377  O  OD1   . ASN A 1 545 ? 143.119 132.745 71.073  1.00 50.89 ?  545 ASN A OD1   1 
ATOM   4378  N  ND2   . ASN A 1 545 ? 142.151 130.725 70.929  1.00 49.17 ?  545 ASN A ND2   1 
ATOM   4379  N  N     . LEU A 1 546 ? 140.429 133.475 75.367  1.00 44.44 ?  546 LEU A N     1 
ATOM   4380  C  CA    . LEU A 1 546 ? 139.419 133.817 76.361  1.00 42.41 ?  546 LEU A CA    1 
ATOM   4381  C  C     . LEU A 1 546 ? 139.419 135.309 76.665  1.00 42.24 ?  546 LEU A C     1 
ATOM   4382  O  O     . LEU A 1 546 ? 138.378 135.870 77.024  1.00 45.24 ?  546 LEU A O     1 
ATOM   4383  C  CB    . LEU A 1 546 ? 139.648 133.017 77.643  1.00 40.80 ?  546 LEU A CB    1 
ATOM   4384  C  CG    . LEU A 1 546 ? 139.449 131.503 77.566  1.00 39.12 ?  546 LEU A CG    1 
ATOM   4385  C  CD1   . LEU A 1 546 ? 139.796 130.860 78.896  1.00 39.65 ?  546 LEU A CD1   1 
ATOM   4386  C  CD2   . LEU A 1 546 ? 138.024 131.165 77.165  1.00 40.10 ?  546 LEU A CD2   1 
ATOM   4387  N  N     . PHE A 1 547 ? 140.568 135.964 76.521  1.00 40.24 ?  547 PHE A N     1 
ATOM   4388  C  CA    . PHE A 1 547 ? 140.698 137.392 76.770  1.00 40.24 ?  547 PHE A CA    1 
ATOM   4389  C  C     . PHE A 1 547 ? 140.633 138.215 75.491  1.00 40.78 ?  547 PHE A C     1 
ATOM   4390  O  O     . PHE A 1 547 ? 140.900 139.420 75.528  1.00 42.05 ?  547 PHE A O     1 
ATOM   4391  C  CB    . PHE A 1 547 ? 142.005 137.678 77.511  1.00 36.73 ?  547 PHE A CB    1 
ATOM   4392  C  CG    . PHE A 1 547 ? 142.008 137.215 78.938  1.00 38.42 ?  547 PHE A CG    1 
ATOM   4393  C  CD1   . PHE A 1 547 ? 141.499 138.019 79.943  1.00 37.60 ?  547 PHE A CD1   1 
ATOM   4394  C  CD2   . PHE A 1 547 ? 142.521 135.975 79.276  1.00 37.01 ?  547 PHE A CD2   1 
ATOM   4395  C  CE1   . PHE A 1 547 ? 141.504 137.596 81.256  1.00 33.39 ?  547 PHE A CE1   1 
ATOM   4396  C  CE2   . PHE A 1 547 ? 142.527 135.546 80.587  1.00 35.07 ?  547 PHE A CE2   1 
ATOM   4397  C  CZ    . PHE A 1 547 ? 142.018 136.357 81.578  1.00 34.33 ?  547 PHE A CZ    1 
ATOM   4398  N  N     . GLU A 1 548 ? 140.293 137.594 74.364  1.00 50.24 ?  548 GLU A N     1 
ATOM   4399  C  CA    . GLU A 1 548 ? 140.193 138.318 73.105  1.00 52.22 ?  548 GLU A CA    1 
ATOM   4400  C  C     . GLU A 1 548 ? 139.076 139.349 73.176  1.00 51.05 ?  548 GLU A C     1 
ATOM   4401  O  O     . GLU A 1 548 ? 137.983 139.074 73.677  1.00 51.91 ?  548 GLU A O     1 
ATOM   4402  C  CB    . GLU A 1 548 ? 139.956 137.339 71.952  1.00 48.82 ?  548 GLU A CB    1 
ATOM   4403  C  CG    . GLU A 1 548 ? 139.305 137.940 70.710  1.00 51.53 ?  548 GLU A CG    1 
ATOM   4404  C  CD    . GLU A 1 548 ? 137.790 137.839 70.730  1.00 52.72 ?  548 GLU A CD    1 
ATOM   4405  O  OE1   . GLU A 1 548 ? 137.125 138.765 70.223  1.00 51.34 ?  548 GLU A OE1   1 
ATOM   4406  O  OE2   . GLU A 1 548 ? 137.268 136.829 71.249  1.00 53.80 -1 548 GLU A OE2   1 
ATOM   4407  N  N     . GLY A 1 549 ? 139.354 140.546 72.662  1.00 45.32 ?  549 GLY A N     1 
ATOM   4408  C  CA    . GLY A 1 549 ? 138.434 141.655 72.777  1.00 46.85 ?  549 GLY A CA    1 
ATOM   4409  C  C     . GLY A 1 549 ? 138.540 142.432 74.069  1.00 47.31 ?  549 GLY A C     1 
ATOM   4410  O  O     . GLY A 1 549 ? 137.746 143.357 74.284  1.00 46.90 ?  549 GLY A O     1 
ATOM   4411  N  N     . MET A 1 550 ? 139.492 142.089 74.934  1.00 47.64 ?  550 MET A N     1 
ATOM   4412  C  CA    . MET A 1 550 ? 139.693 142.764 76.206  1.00 44.25 ?  550 MET A CA    1 
ATOM   4413  C  C     . MET A 1 550 ? 141.179 143.034 76.377  1.00 44.66 ?  550 MET A C     1 
ATOM   4414  O  O     . MET A 1 550 ? 141.991 142.107 76.306  1.00 48.18 ?  550 MET A O     1 
ATOM   4415  C  CB    . MET A 1 550 ? 139.158 141.914 77.361  1.00 43.54 ?  550 MET A CB    1 
ATOM   4416  C  CG    . MET A 1 550 ? 138.607 142.712 78.525  1.00 48.40 ?  550 MET A CG    1 
ATOM   4417  S  SD    . MET A 1 550 ? 138.317 141.701 79.986  1.00 55.01 ?  550 MET A SD    1 
ATOM   4418  C  CE    . MET A 1 550 ? 138.292 140.054 79.284  1.00 44.39 ?  550 MET A CE    1 
ATOM   4419  N  N     . HIS A 1 551 ? 141.533 144.297 76.597  1.00 40.57 ?  551 HIS A N     1 
ATOM   4420  C  CA    . HIS A 1 551 ? 142.938 144.677 76.658  1.00 40.38 ?  551 HIS A CA    1 
ATOM   4421  C  C     . HIS A 1 551 ? 143.588 144.142 77.928  1.00 41.17 ?  551 HIS A C     1 
ATOM   4422  O  O     . HIS A 1 551 ? 143.068 144.324 79.033  1.00 42.19 ?  551 HIS A O     1 
ATOM   4423  C  CB    . HIS A 1 551 ? 143.084 146.195 76.592  1.00 39.62 ?  551 HIS A CB    1 
ATOM   4424  C  CG    . HIS A 1 551 ? 144.464 146.680 76.910  1.00 43.71 ?  551 HIS A CG    1 
ATOM   4425  N  ND1   . HIS A 1 551 ? 145.493 146.648 75.993  1.00 46.46 ?  551 HIS A ND1   1 
ATOM   4426  C  CD2   . HIS A 1 551 ? 144.987 147.205 78.044  1.00 43.40 ?  551 HIS A CD2   1 
ATOM   4427  C  CE1   . HIS A 1 551 ? 146.589 147.133 76.548  1.00 44.87 ?  551 HIS A CE1   1 
ATOM   4428  N  NE2   . HIS A 1 551 ? 146.309 147.478 77.791  1.00 43.03 ?  551 HIS A NE2   1 
ATOM   4429  N  N     . ILE A 1 552 ? 144.731 143.487 77.766  1.00 37.11 ?  552 ILE A N     1 
ATOM   4430  C  CA    . ILE A 1 552 ? 145.514 142.958 78.878  1.00 36.65 ?  552 ILE A CA    1 
ATOM   4431  C  C     . ILE A 1 552 ? 146.655 143.932 79.151  1.00 39.13 ?  552 ILE A C     1 
ATOM   4432  O  O     . ILE A 1 552 ? 147.486 144.154 78.257  1.00 41.15 ?  552 ILE A O     1 
ATOM   4433  C  CB    . ILE A 1 552 ? 146.052 141.554 78.571  1.00 36.39 ?  552 ILE A CB    1 
ATOM   4434  C  CG1   . ILE A 1 552 ? 144.896 140.593 78.289  1.00 35.61 ?  552 ILE A CG1   1 
ATOM   4435  C  CG2   . ILE A 1 552 ? 146.900 141.046 79.719  1.00 35.93 ?  552 ILE A CG2   1 
ATOM   4436  C  CD1   . ILE A 1 552 ? 145.331 139.285 77.679  1.00 39.04 ?  552 ILE A CD1   1 
ATOM   4437  N  N     . PRO A 1 553 ? 146.727 144.536 80.336  1.00 41.21 ?  553 PRO A N     1 
ATOM   4438  C  CA    . PRO A 1 553 ? 147.823 145.470 80.622  1.00 37.58 ?  553 PRO A CA    1 
ATOM   4439  C  C     . PRO A 1 553 ? 149.180 144.795 80.515  1.00 37.53 ?  553 PRO A C     1 
ATOM   4440  O  O     . PRO A 1 553 ? 149.385 143.679 80.998  1.00 35.05 ?  553 PRO A O     1 
ATOM   4441  C  CB    . PRO A 1 553 ? 147.534 145.927 82.056  1.00 34.42 ?  553 PRO A CB    1 
ATOM   4442  C  CG    . PRO A 1 553 ? 146.084 145.666 82.255  1.00 32.51 ?  553 PRO A CG    1 
ATOM   4443  C  CD    . PRO A 1 553 ? 145.767 144.456 81.446  1.00 33.93 ?  553 PRO A CD    1 
ATOM   4444  N  N     . THR A 1 554 ? 150.110 145.491 79.878  1.00 42.64 ?  554 THR A N     1 
ATOM   4445  C  CA    . THR A 1 554 ? 151.460 145.008 79.665  1.00 40.12 ?  554 THR A CA    1 
ATOM   4446  C  C     . THR A 1 554 ? 152.385 145.591 80.728  1.00 36.10 ?  554 THR A C     1 
ATOM   4447  O  O     . THR A 1 554 ? 151.939 146.188 81.713  1.00 38.78 ?  554 THR A O     1 
ATOM   4448  C  CB    . THR A 1 554 ? 151.921 145.364 78.250  1.00 38.52 ?  554 THR A CB    1 
ATOM   4449  O  OG1   . THR A 1 554 ? 151.916 146.788 78.091  1.00 43.66 ?  554 THR A OG1   1 
ATOM   4450  C  CG2   . THR A 1 554 ? 150.993 144.744 77.219  1.00 40.83 ?  554 THR A CG2   1 
ATOM   4451  N  N     . THR A 1 555 ? 153.693 145.410 80.540  1.00 38.32 ?  555 THR A N     1 
ATOM   4452  C  CA    . THR A 1 555 ? 154.652 146.037 81.441  1.00 35.88 ?  555 THR A CA    1 
ATOM   4453  C  C     . THR A 1 555 ? 154.623 147.554 81.304  1.00 38.84 ?  555 THR A C     1 
ATOM   4454  O  O     . THR A 1 555 ? 154.790 148.273 82.294  1.00 42.01 ?  555 THR A O     1 
ATOM   4455  C  CB    . THR A 1 555 ? 156.057 145.502 81.175  1.00 39.23 ?  555 THR A CB    1 
ATOM   4456  O  OG1   . THR A 1 555 ? 156.227 145.280 79.770  1.00 47.13 ?  555 THR A OG1   1 
ATOM   4457  C  CG2   . THR A 1 555 ? 156.274 144.193 81.919  1.00 38.19 ?  555 THR A CG2   1 
ATOM   4458  N  N     . GLU A 1 556 ? 154.416 148.059 80.085  1.00 39.45 ?  556 GLU A N     1 
ATOM   4459  C  CA    . GLU A 1 556 ? 154.316 149.502 79.886  1.00 41.11 ?  556 GLU A CA    1 
ATOM   4460  C  C     . GLU A 1 556 ? 153.088 150.073 80.586  1.00 41.76 ?  556 GLU A C     1 
ATOM   4461  O  O     . GLU A 1 556 ? 153.152 151.148 81.197  1.00 44.03 ?  556 GLU A O     1 
ATOM   4462  C  CB    . GLU A 1 556 ? 154.280 149.821 78.391  1.00 41.87 ?  556 GLU A CB    1 
ATOM   4463  C  CG    . GLU A 1 556 ? 155.488 149.339 77.580  1.00 45.29 ?  556 GLU A CG    1 
ATOM   4464  C  CD    . GLU A 1 556 ? 156.815 149.394 78.333  1.00 49.26 ?  556 GLU A CD    1 
ATOM   4465  O  OE1   . GLU A 1 556 ? 157.639 148.474 78.145  1.00 49.26 ?  556 GLU A OE1   1 
ATOM   4466  O  OE2   . GLU A 1 556 ? 157.066 150.377 79.062  1.00 43.00 -1 556 GLU A OE2   1 
ATOM   4467  N  N     . ASP A 1 557 ? 151.958 149.368 80.499  1.00 42.48 ?  557 ASP A N     1 
ATOM   4468  C  CA    . ASP A 1 557 ? 150.757 149.814 81.196  1.00 39.88 ?  557 ASP A CA    1 
ATOM   4469  C  C     . ASP A 1 557 ? 150.975 149.827 82.702  1.00 37.08 ?  557 ASP A C     1 
ATOM   4470  O  O     . ASP A 1 557 ? 150.523 150.745 83.396  1.00 37.78 ?  557 ASP A O     1 
ATOM   4471  C  CB    . ASP A 1 557 ? 149.577 148.915 80.833  1.00 37.18 ?  557 ASP A CB    1 
ATOM   4472  C  CG    . ASP A 1 557 ? 148.811 149.421 79.633  1.00 43.58 ?  557 ASP A CG    1 
ATOM   4473  O  OD1   . ASP A 1 557 ? 148.510 150.631 79.585  1.00 45.62 ?  557 ASP A OD1   1 
ATOM   4474  O  OD2   . ASP A 1 557 ? 148.511 148.608 78.733  1.00 43.98 -1 557 ASP A OD2   1 
ATOM   4475  N  N     . TRP A 1 558 ? 151.674 148.819 83.224  1.00 30.18 ?  558 TRP A N     1 
ATOM   4476  C  CA    . TRP A 1 558 ? 151.959 148.788 84.653  1.00 27.84 ?  558 TRP A CA    1 
ATOM   4477  C  C     . TRP A 1 558 ? 152.932 149.886 85.062  1.00 34.90 ?  558 TRP A C     1 
ATOM   4478  O  O     . TRP A 1 558 ? 152.814 150.426 86.163  1.00 35.93 ?  558 TRP A O     1 
ATOM   4479  C  CB    . TRP A 1 558 ? 152.497 147.417 85.050  1.00 30.23 ?  558 TRP A CB    1 
ATOM   4480  C  CG    . TRP A 1 558 ? 151.427 146.445 85.436  1.00 29.42 ?  558 TRP A CG    1 
ATOM   4481  C  CD1   . TRP A 1 558 ? 150.975 145.387 84.705  1.00 28.16 ?  558 TRP A CD1   1 
ATOM   4482  C  CD2   . TRP A 1 558 ? 150.667 146.446 86.651  1.00 28.54 ?  558 TRP A CD2   1 
ATOM   4483  N  NE1   . TRP A 1 558 ? 149.987 144.725 85.389  1.00 30.68 ?  558 TRP A NE1   1 
ATOM   4484  C  CE2   . TRP A 1 558 ? 149.779 145.354 86.588  1.00 29.91 ?  558 TRP A CE2   1 
ATOM   4485  C  CE3   . TRP A 1 558 ? 150.656 147.258 87.788  1.00 32.95 ?  558 TRP A CE3   1 
ATOM   4486  C  CZ2   . TRP A 1 558 ? 148.891 145.057 87.616  1.00 24.29 ?  558 TRP A CZ2   1 
ATOM   4487  C  CZ3   . TRP A 1 558 ? 149.771 146.961 88.806  1.00 27.71 ?  558 TRP A CZ3   1 
ATOM   4488  C  CH2   . TRP A 1 558 ? 148.901 145.872 88.714  1.00 19.86 ?  558 TRP A CH2   1 
ATOM   4489  N  N     . LYS A 1 559 ? 153.892 150.233 84.201  1.00 40.62 ?  559 LYS A N     1 
ATOM   4490  C  CA    . LYS A 1 559 ? 154.767 151.367 84.491  1.00 35.82 ?  559 LYS A CA    1 
ATOM   4491  C  C     . LYS A 1 559 ? 153.981 152.671 84.533  1.00 36.87 ?  559 LYS A C     1 
ATOM   4492  O  O     . LYS A 1 559 ? 154.202 153.515 85.412  1.00 40.72 ?  559 LYS A O     1 
ATOM   4493  C  CB    . LYS A 1 559 ? 155.884 151.453 83.451  1.00 38.77 ?  559 LYS A CB    1 
ATOM   4494  C  CG    . LYS A 1 559 ? 156.895 150.326 83.515  1.00 38.52 ?  559 LYS A CG    1 
ATOM   4495  C  CD    . LYS A 1 559 ? 157.737 150.276 82.252  1.00 41.10 ?  559 LYS A CD    1 
ATOM   4496  C  CE    . LYS A 1 559 ? 158.807 149.201 82.339  1.00 40.35 ?  559 LYS A CE    1 
ATOM   4497  N  NZ    . LYS A 1 559 ? 159.564 149.266 83.619  1.00 43.81 1  559 LYS A NZ    1 
ATOM   4498  N  N     . LYS A 1 560 ? 153.059 152.853 83.584  1.00 36.29 ?  560 LYS A N     1 
ATOM   4499  C  CA    . LYS A 1 560 ? 152.216 154.043 83.596  1.00 33.56 ?  560 LYS A CA    1 
ATOM   4500  C  C     . LYS A 1 560 ? 151.352 154.092 84.849  1.00 36.41 ?  560 LYS A C     1 
ATOM   4501  O  O     . LYS A 1 560 ? 151.189 155.155 85.459  1.00 42.03 ?  560 LYS A O     1 
ATOM   4502  C  CB    . LYS A 1 560 ? 151.344 154.083 82.340  1.00 34.44 ?  560 LYS A CB    1 
ATOM   4503  C  CG    . LYS A 1 560 ? 152.116 154.330 81.056  1.00 38.39 ?  560 LYS A CG    1 
ATOM   4504  C  CD    . LYS A 1 560 ? 151.188 154.376 79.855  1.00 39.77 ?  560 LYS A CD    1 
ATOM   4505  C  CE    . LYS A 1 560 ? 151.867 153.830 78.611  1.00 40.30 ?  560 LYS A CE    1 
ATOM   4506  N  NZ    . LYS A 1 560 ? 151.525 152.402 78.369  1.00 40.83 1  560 LYS A NZ    1 
ATOM   4507  N  N     . LEU A 1 561 ? 150.794 152.949 85.253  1.00 33.41 ?  561 LEU A N     1 
ATOM   4508  C  CA    . LEU A 1 561 ? 149.997 152.901 86.476  1.00 29.59 ?  561 LEU A CA    1 
ATOM   4509  C  C     . LEU A 1 561 ? 150.851 153.183 87.705  1.00 32.43 ?  561 LEU A C     1 
ATOM   4510  O  O     . LEU A 1 561 ? 150.390 153.829 88.650  1.00 36.45 ?  561 LEU A O     1 
ATOM   4511  C  CB    . LEU A 1 561 ? 149.306 151.544 86.605  1.00 31.12 ?  561 LEU A CB    1 
ATOM   4512  C  CG    . LEU A 1 561 ? 148.494 151.365 87.889  1.00 31.43 ?  561 LEU A CG    1 
ATOM   4513  C  CD1   . LEU A 1 561 ? 147.390 152.402 87.965  1.00 27.55 ?  561 LEU A CD1   1 
ATOM   4514  C  CD2   . LEU A 1 561 ? 147.922 149.967 87.990  1.00 28.89 ?  561 LEU A CD2   1 
ATOM   4515  N  N     . LYS A 1 562 ? 152.089 152.688 87.722  1.00 34.56 ?  562 LYS A N     1 
ATOM   4516  C  CA    . LYS A 1 562 ? 152.989 152.967 88.834  1.00 33.38 ?  562 LYS A CA    1 
ATOM   4517  C  C     . LYS A 1 562 ? 153.288 154.455 88.937  1.00 34.22 ?  562 LYS A C     1 
ATOM   4518  O  O     . LYS A 1 562 ? 153.288 155.021 90.036  1.00 38.77 ?  562 LYS A O     1 
ATOM   4519  C  CB    . LYS A 1 562 ? 154.281 152.165 88.668  1.00 35.62 ?  562 LYS A CB    1 
ATOM   4520  C  CG    . LYS A 1 562 ? 155.395 152.561 89.616  1.00 31.08 ?  562 LYS A CG    1 
ATOM   4521  C  CD    . LYS A 1 562 ? 156.680 151.830 89.278  1.00 28.64 ?  562 LYS A CD    1 
ATOM   4522  C  CE    . LYS A 1 562 ? 157.817 152.257 90.189  1.00 34.47 ?  562 LYS A CE    1 
ATOM   4523  N  NZ    . LYS A 1 562 ? 158.888 151.226 90.249  1.00 41.45 1  562 LYS A NZ    1 
ATOM   4524  N  N     . ALA A 1 563 ? 153.539 155.108 87.800  1.00 32.24 ?  563 ALA A N     1 
ATOM   4525  C  CA    . ALA A 1 563 ? 153.742 156.554 87.810  1.00 33.14 ?  563 ALA A CA    1 
ATOM   4526  C  C     . ALA A 1 563 ? 152.486 157.283 88.278  1.00 36.18 ?  563 ALA A C     1 
ATOM   4527  O  O     . ALA A 1 563 ? 152.566 158.240 89.059  1.00 42.44 ?  563 ALA A O     1 
ATOM   4528  C  CB    . ALA A 1 563 ? 154.159 157.034 86.422  1.00 35.79 ?  563 ALA A CB    1 
ATOM   4529  N  N     . PHE A 1 564 ? 151.318 156.836 87.814  1.00 34.18 ?  564 PHE A N     1 
ATOM   4530  C  CA    . PHE A 1 564 ? 150.057 157.449 88.222  1.00 31.53 ?  564 PHE A CA    1 
ATOM   4531  C  C     . PHE A 1 564 ? 149.846 157.329 89.727  1.00 35.60 ?  564 PHE A C     1 
ATOM   4532  O  O     . PHE A 1 564 ? 149.402 158.280 90.378  1.00 38.50 ?  564 PHE A O     1 
ATOM   4533  C  CB    . PHE A 1 564 ? 148.904 156.798 87.458  1.00 32.91 ?  564 PHE A CB    1 
ATOM   4534  C  CG    . PHE A 1 564 ? 147.616 157.562 87.522  1.00 33.21 ?  564 PHE A CG    1 
ATOM   4535  C  CD1   . PHE A 1 564 ? 147.324 158.533 86.581  1.00 35.68 ?  564 PHE A CD1   1 
ATOM   4536  C  CD2   . PHE A 1 564 ? 146.688 157.297 88.514  1.00 34.31 ?  564 PHE A CD2   1 
ATOM   4537  C  CE1   . PHE A 1 564 ? 146.134 159.233 86.634  1.00 39.13 ?  564 PHE A CE1   1 
ATOM   4538  C  CE2   . PHE A 1 564 ? 145.499 157.993 88.574  1.00 35.63 ?  564 PHE A CE2   1 
ATOM   4539  C  CZ    . PHE A 1 564 ? 145.220 158.962 87.632  1.00 38.90 ?  564 PHE A CZ    1 
ATOM   4540  N  N     . VAL A 1 565 ? 150.156 156.163 90.294  1.00 35.82 ?  565 VAL A N     1 
ATOM   4541  C  CA    . VAL A 1 565 ? 150.004 155.956 91.729  1.00 29.96 ?  565 VAL A CA    1 
ATOM   4542  C  C     . VAL A 1 565 ? 151.012 156.795 92.502  1.00 33.54 ?  565 VAL A C     1 
ATOM   4543  O  O     . VAL A 1 565 ? 150.685 157.387 93.537  1.00 36.12 ?  565 VAL A O     1 
ATOM   4544  C  CB    . VAL A 1 565 ? 150.133 154.458 92.062  1.00 29.53 ?  565 VAL A CB    1 
ATOM   4545  C  CG1   . VAL A 1 565 ? 150.350 154.251 93.550  1.00 28.69 ?  565 VAL A CG1   1 
ATOM   4546  C  CG2   . VAL A 1 565 ? 148.900 153.716 91.596  1.00 33.70 ?  565 VAL A CG2   1 
ATOM   4547  N  N     . ALA A 1 566 ? 152.252 156.866 92.014  1.00 36.68 ?  566 ALA A N     1 
ATOM   4548  C  CA    . ALA A 1 566 ? 153.265 157.665 92.690  1.00 36.24 ?  566 ALA A CA    1 
ATOM   4549  C  C     . ALA A 1 566 ? 152.919 159.146 92.671  1.00 38.26 ?  566 ALA A C     1 
ATOM   4550  O  O     . ALA A 1 566 ? 153.282 159.878 93.597  1.00 42.85 ?  566 ALA A O     1 
ATOM   4551  C  CB    . ALA A 1 566 ? 154.632 157.431 92.049  1.00 36.68 ?  566 ALA A CB    1 
ATOM   4552  N  N     . GLU A 1 567 ? 152.221 159.604 91.634  1.00 40.84 ?  567 GLU A N     1 
ATOM   4553  C  CA    . GLU A 1 567 ? 151.890 161.017 91.517  1.00 40.06 ?  567 GLU A CA    1 
ATOM   4554  C  C     . GLU A 1 567 ? 150.540 161.382 92.127  1.00 39.80 ?  567 GLU A C     1 
ATOM   4555  O  O     . GLU A 1 567 ? 150.329 162.555 92.455  1.00 43.67 ?  567 GLU A O     1 
ATOM   4556  C  CB    . GLU A 1 567 ? 151.937 161.433 90.041  1.00 42.38 ?  567 GLU A CB    1 
ATOM   4557  C  CG    . GLU A 1 567 ? 151.966 162.929 89.796  1.00 43.90 ?  567 GLU A CG    1 
ATOM   4558  C  CD    . GLU A 1 567 ? 150.678 163.434 89.188  1.00 47.55 ?  567 GLU A CD    1 
ATOM   4559  O  OE1   . GLU A 1 567 ? 150.011 162.645 88.488  1.00 46.07 ?  567 GLU A OE1   1 
ATOM   4560  O  OE2   . GLU A 1 567 ? 150.334 164.615 89.405  1.00 47.17 -1 567 GLU A OE2   1 
ATOM   4561  N  N     . HIS A 1 568 ? 149.631 160.419 92.300  1.00 39.70 ?  568 HIS A N     1 
ATOM   4562  C  CA    . HIS A 1 568 ? 148.324 160.683 92.890  1.00 38.76 ?  568 HIS A CA    1 
ATOM   4563  C  C     . HIS A 1 568 ? 148.028 159.912 94.167  1.00 35.94 ?  568 HIS A C     1 
ATOM   4564  O  O     . HIS A 1 568 ? 147.131 160.321 94.911  1.00 40.11 ?  568 HIS A O     1 
ATOM   4565  C  CB    . HIS A 1 568 ? 147.203 160.382 91.882  1.00 37.02 ?  568 HIS A CB    1 
ATOM   4566  C  CG    . HIS A 1 568 ? 147.120 161.363 90.756  1.00 38.46 ?  568 HIS A CG    1 
ATOM   4567  N  ND1   . HIS A 1 568 ? 146.427 161.105 89.594  1.00 42.97 ?  568 HIS A ND1   1 
ATOM   4568  C  CD2   . HIS A 1 568 ? 147.647 162.600 90.614  1.00 38.74 ?  568 HIS A CD2   1 
ATOM   4569  C  CE1   . HIS A 1 568 ? 146.537 162.141 88.781  1.00 42.21 ?  568 HIS A CE1   1 
ATOM   4570  N  NE2   . HIS A 1 568 ? 147.266 163.065 89.379  1.00 41.84 ?  568 HIS A NE2   1 
ATOM   4571  N  N     . GLY A 1 569 ? 148.734 158.821 94.444  1.00 29.47 ?  569 GLY A N     1 
ATOM   4572  C  CA    . GLY A 1 569 ? 148.473 158.054 95.645  1.00 29.61 ?  569 GLY A CA    1 
ATOM   4573  C  C     . GLY A 1 569 ? 147.360 157.040 95.470  1.00 28.19 ?  569 GLY A C     1 
ATOM   4574  O  O     . GLY A 1 569 ? 146.753 156.897 94.409  1.00 33.66 ?  569 GLY A O     1 
ATOM   4575  N  N     . MET A 1 570 ? 147.093 156.315 96.554  1.00 24.21 ?  570 MET A N     1 
ATOM   4576  C  CA    . MET A 1 570 ? 146.068 155.282 96.588  1.00 22.67 ?  570 MET A CA    1 
ATOM   4577  C  C     . MET A 1 570 ? 145.059 155.598 97.680  1.00 24.38 ?  570 MET A C     1 
ATOM   4578  O  O     . MET A 1 570 ? 145.432 156.014 98.780  1.00 31.69 ?  570 MET A O     1 
ATOM   4579  C  CB    . MET A 1 570 ? 146.683 153.900 96.832  1.00 26.83 ?  570 MET A CB    1 
ATOM   4580  C  CG    . MET A 1 570 ? 147.572 153.409 95.709  1.00 24.76 ?  570 MET A CG    1 
ATOM   4581  S  SD    . MET A 1 570 ? 146.713 152.281 94.606  1.00 38.07 ?  570 MET A SD    1 
ATOM   4582  C  CE    . MET A 1 570 ? 146.572 150.848 95.663  1.00 24.88 ?  570 MET A CE    1 
ATOM   4583  N  N     . TYR A 1 571 ? 143.779 155.392 97.373  1.00 15.53 ?  571 TYR A N     1 
ATOM   4584  C  CA    . TYR A 1 571 ? 142.731 155.694 98.340  1.00 9.58  ?  571 TYR A CA    1 
ATOM   4585  C  C     . TYR A 1 571 ? 142.521 154.563 99.337  1.00 18.52 ?  571 TYR A C     1 
ATOM   4586  O  O     . TYR A 1 571 ? 142.186 154.823 100.498 1.00 20.21 ?  571 TYR A O     1 
ATOM   4587  C  CB    . TYR A 1 571 ? 141.421 155.995 97.614  1.00 20.46 ?  571 TYR A CB    1 
ATOM   4588  C  CG    . TYR A 1 571 ? 140.366 156.610 98.499  1.00 24.83 ?  571 TYR A CG    1 
ATOM   4589  C  CD1   . TYR A 1 571 ? 140.437 157.944 98.868  1.00 23.83 ?  571 TYR A CD1   1 
ATOM   4590  C  CD2   . TYR A 1 571 ? 139.301 155.856 98.968  1.00 19.14 ?  571 TYR A CD2   1 
ATOM   4591  C  CE1   . TYR A 1 571 ? 139.479 158.511 99.676  1.00 26.06 ?  571 TYR A CE1   1 
ATOM   4592  C  CE2   . TYR A 1 571 ? 138.339 156.415 99.779  1.00 20.62 ?  571 TYR A CE2   1 
ATOM   4593  C  CZ    . TYR A 1 571 ? 138.430 157.743 100.129 1.00 28.45 ?  571 TYR A CZ    1 
ATOM   4594  O  OH    . TYR A 1 571 ? 137.471 158.305 100.936 1.00 27.40 ?  571 TYR A OH    1 
ATOM   4595  N  N     . HIS A 1 572 ? 142.702 153.316 98.915  1.00 23.11 ?  572 HIS A N     1 
ATOM   4596  C  CA    . HIS A 1 572 ? 142.474 152.154 99.761  1.00 14.41 ?  572 HIS A CA    1 
ATOM   4597  C  C     . HIS A 1 572 ? 143.804 151.514 100.121 1.00 13.07 ?  572 HIS A C     1 
ATOM   4598  O  O     . HIS A 1 572 ? 144.629 151.250 99.242  1.00 26.25 ?  572 HIS A O     1 
ATOM   4599  C  CB    . HIS A 1 572 ? 141.575 151.132 99.062  1.00 14.72 ?  572 HIS A CB    1 
ATOM   4600  C  CG    . HIS A 1 572 ? 140.398 151.737 98.365  1.00 9.11  ?  572 HIS A CG    1 
ATOM   4601  N  ND1   . HIS A 1 572 ? 140.421 152.083 97.032  1.00 18.58 ?  572 HIS A ND1   1 
ATOM   4602  C  CD2   . HIS A 1 572 ? 139.162 152.053 98.814  1.00 15.19 ?  572 HIS A CD2   1 
ATOM   4603  C  CE1   . HIS A 1 572 ? 139.251 152.590 96.691  1.00 19.44 ?  572 HIS A CE1   1 
ATOM   4604  N  NE2   . HIS A 1 572 ? 138.468 152.581 97.754  1.00 24.26 ?  572 HIS A NE2   1 
ATOM   4605  N  N     . SER A 1 573 ? 144.009 151.270 101.417 1.00 8.03  ?  573 SER A N     1 
ATOM   4606  C  CA    . SER A 1 573 ? 145.193 150.534 101.846 1.00 8.56  ?  573 SER A CA    1 
ATOM   4607  C  C     . SER A 1 573 ? 145.161 149.105 101.326 1.00 15.34 ?  573 SER A C     1 
ATOM   4608  O  O     . SER A 1 573 ? 146.191 148.563 100.909 1.00 24.43 ?  573 SER A O     1 
ATOM   4609  C  CB    . SER A 1 573 ? 145.298 150.553 103.370 1.00 12.75 ?  573 SER A CB    1 
ATOM   4610  O  OG    . SER A 1 573 ? 144.055 150.233 103.965 1.00 21.38 ?  573 SER A OG    1 
ATOM   4611  N  N     . TYR A 1 574 ? 143.986 148.483 101.340 1.00 16.85 ?  574 TYR A N     1 
ATOM   4612  C  CA    . TYR A 1 574 ? 143.786 147.138 100.827 1.00 5.31  ?  574 TYR A CA    1 
ATOM   4613  C  C     . TYR A 1 574 ? 142.563 147.142 99.925  1.00 9.09  ?  574 TYR A C     1 
ATOM   4614  O  O     . TYR A 1 574 ? 141.590 147.852 100.194 1.00 13.59 ?  574 TYR A O     1 
ATOM   4615  C  CB    . TYR A 1 574 ? 143.612 146.135 101.970 1.00 12.98 ?  574 TYR A CB    1 
ATOM   4616  C  CG    . TYR A 1 574 ? 144.729 146.196 102.982 1.00 7.77  ?  574 TYR A CG    1 
ATOM   4617  C  CD1   . TYR A 1 574 ? 144.688 147.103 104.030 1.00 6.39  ?  574 TYR A CD1   1 
ATOM   4618  C  CD2   . TYR A 1 574 ? 145.830 145.360 102.882 1.00 10.01 ?  574 TYR A CD2   1 
ATOM   4619  C  CE1   . TYR A 1 574 ? 145.705 147.175 104.950 1.00 9.56  ?  574 TYR A CE1   1 
ATOM   4620  C  CE2   . TYR A 1 574 ? 146.852 145.424 103.802 1.00 17.92 ?  574 TYR A CE2   1 
ATOM   4621  C  CZ    . TYR A 1 574 ? 146.783 146.334 104.834 1.00 8.20  ?  574 TYR A CZ    1 
ATOM   4622  O  OH    . TYR A 1 574 ? 147.795 146.406 105.759 1.00 14.62 ?  574 TYR A OH    1 
ATOM   4623  N  N     . ARG A 1 575 ? 142.618 146.368 98.858  1.00 16.15 ?  575 ARG A N     1 
ATOM   4624  C  CA    . ARG A 1 575 ? 141.535 146.404 97.882  1.00 7.89  ?  575 ARG A CA    1 
ATOM   4625  C  C     . ARG A 1 575 ? 140.919 145.043 97.605  1.00 12.24 ?  575 ARG A C     1 
ATOM   4626  O  O     . ARG A 1 575 ? 139.701 144.950 97.445  1.00 20.45 ?  575 ARG A O     1 
ATOM   4627  C  CB    . ARG A 1 575 ? 142.036 147.009 96.566  1.00 15.51 ?  575 ARG A CB    1 
ATOM   4628  C  CG    . ARG A 1 575 ? 142.577 148.417 96.688  1.00 6.14  ?  575 ARG A CG    1 
ATOM   4629  C  CD    . ARG A 1 575 ? 143.602 148.685 95.605  1.00 12.48 ?  575 ARG A CD    1 
ATOM   4630  N  NE    . ARG A 1 575 ? 144.853 147.984 95.866  1.00 22.24 ?  575 ARG A NE    1 
ATOM   4631  C  CZ    . ARG A 1 575 ? 145.259 146.905 95.215  1.00 14.81 ?  575 ARG A CZ    1 
ATOM   4632  N  NH1   . ARG A 1 575 ? 144.536 146.370 94.246  1.00 16.91 1  575 ARG A NH1   1 
ATOM   4633  N  NH2   . ARG A 1 575 ? 146.418 146.345 95.545  1.00 10.77 ?  575 ARG A NH2   1 
ATOM   4634  N  N     . LEU A 1 576 ? 141.724 143.987 97.542  1.00 20.61 ?  576 LEU A N     1 
ATOM   4635  C  CA    . LEU A 1 576 ? 141.275 142.686 97.069  1.00 8.99  ?  576 LEU A CA    1 
ATOM   4636  C  C     . LEU A 1 576 ? 141.412 141.652 98.175  1.00 6.92  ?  576 LEU A C     1 
ATOM   4637  O  O     . LEU A 1 576 ? 142.489 141.498 98.755  1.00 16.05 ?  576 LEU A O     1 
ATOM   4638  C  CB    . LEU A 1 576 ? 142.078 142.247 95.843  1.00 4.75  ?  576 LEU A CB    1 
ATOM   4639  C  CG    . LEU A 1 576 ? 142.149 143.237 94.682  1.00 10.05 ?  576 LEU A CG    1 
ATOM   4640  C  CD1   . LEU A 1 576 ? 143.089 142.731 93.606  1.00 12.27 ?  576 LEU A CD1   1 
ATOM   4641  C  CD2   . LEU A 1 576 ? 140.769 143.489 94.108  1.00 10.86 ?  576 LEU A CD2   1 
ATOM   4642  N  N     . CYS A 1 577 ? 140.319 140.952 98.460  1.00 5.06  ?  577 CYS A N     1 
ATOM   4643  C  CA    . CYS A 1 577 ? 140.340 139.786 99.330  1.00 3.41  ?  577 CYS A CA    1 
ATOM   4644  C  C     . CYS A 1 577 ? 139.263 138.831 98.841  1.00 17.51 ?  577 CYS A C     1 
ATOM   4645  O  O     . CYS A 1 577 ? 138.146 139.258 98.544  1.00 21.24 ?  577 CYS A O     1 
ATOM   4646  C  CB    . CYS A 1 577 ? 140.121 140.167 100.802 1.00 3.50  ?  577 CYS A CB    1 
ATOM   4647  S  SG    . CYS A 1 577 ? 138.413 140.414 101.336 1.00 32.82 ?  577 CYS A SG    1 
ATOM   4648  N  N     . ILE A 1 578 ? 139.606 137.552 98.734  1.00 15.25 ?  578 ILE A N     1 
ATOM   4649  C  CA    . ILE A 1 578 ? 138.708 136.545 98.184  1.00 10.66 ?  578 ILE A CA    1 
ATOM   4650  C  C     . ILE A 1 578 ? 138.073 135.807 99.357  1.00 4.01  ?  578 ILE A C     1 
ATOM   4651  O  O     . ILE A 1 578 ? 138.688 134.933 99.971  1.00 14.86 ?  578 ILE A O     1 
ATOM   4652  C  CB    . ILE A 1 578 ? 139.434 135.598 97.227  1.00 10.51 ?  578 ILE A CB    1 
ATOM   4653  C  CG1   . ILE A 1 578 ? 140.060 136.396 96.085  1.00 0.00  ?  578 ILE A CG1   1 
ATOM   4654  C  CG2   . ILE A 1 578 ? 138.472 134.572 96.667  1.00 13.45 ?  578 ILE A CG2   1 
ATOM   4655  C  CD1   . ILE A 1 578 ? 140.683 135.547 95.020  1.00 6.95  ?  578 ILE A CD1   1 
ATOM   4656  N  N     . ALA A 1 579 ? 136.832 136.168 99.661  1.00 17.63 ?  579 ALA A N     1 
ATOM   4657  C  CA    . ALA A 1 579 ? 136.068 135.589 100.754 1.00 12.12 ?  579 ALA A CA    1 
ATOM   4658  C  C     . ALA A 1 579 ? 135.413 134.284 100.315 1.00 21.37 ?  579 ALA A C     1 
ATOM   4659  O  O     . ALA A 1 579 ? 135.378 133.961 99.127  1.00 27.27 ?  579 ALA A O     1 
ATOM   4660  C  CB    . ALA A 1 579 ? 135.026 136.597 101.229 1.00 9.65  ?  579 ALA A CB    1 
ATOM   4661  N  N     . PRO A 1 580 ? 134.907 133.487 101.263 1.00 26.58 ?  580 PRO A N     1 
ATOM   4662  C  CA    . PRO A 1 580 ? 134.217 132.243 100.876 1.00 22.98 ?  580 PRO A CA    1 
ATOM   4663  C  C     . PRO A 1 580 ? 132.994 132.449 99.994  1.00 25.85 ?  580 PRO A C     1 
ATOM   4664  O  O     . PRO A 1 580 ? 132.723 131.596 99.141  1.00 33.51 ?  580 PRO A O     1 
ATOM   4665  C  CB    . PRO A 1 580 ? 133.838 131.614 102.227 1.00 23.37 ?  580 PRO A CB    1 
ATOM   4666  C  CG    . PRO A 1 580 ? 134.100 132.660 103.260 1.00 24.80 ?  580 PRO A CG    1 
ATOM   4667  C  CD    . PRO A 1 580 ? 135.164 133.534 102.711 1.00 21.17 ?  580 PRO A CD    1 
ATOM   4668  N  N     . THR A 1 581 ? 132.255 133.547 100.163 1.00 22.49 ?  581 THR A N     1 
ATOM   4669  C  CA    . THR A 1 581 ? 131.043 133.836 99.388  1.00 33.36 ?  581 THR A CA    1 
ATOM   4670  C  C     . THR A 1 581 ? 130.061 132.661 99.438  1.00 31.70 ?  581 THR A C     1 
ATOM   4671  O  O     . THR A 1 581 ? 129.754 132.018 98.435  1.00 32.03 ?  581 THR A O     1 
ATOM   4672  C  CB    . THR A 1 581 ? 131.369 134.199 97.934  1.00 32.67 ?  581 THR A CB    1 
ATOM   4673  O  OG1   . THR A 1 581 ? 131.422 133.007 97.139  1.00 26.83 ?  581 THR A OG1   1 
ATOM   4674  C  CG2   . THR A 1 581 ? 132.688 134.944 97.834  1.00 30.85 ?  581 THR A CG2   1 
ATOM   4675  N  N     . GLY A 1 582 ? 129.576 132.401 100.650 1.00 35.50 ?  582 GLY A N     1 
ATOM   4676  C  CA    . GLY A 1 582 ? 128.789 131.212 100.910 1.00 32.59 ?  582 GLY A CA    1 
ATOM   4677  C  C     . GLY A 1 582 ? 127.441 131.131 100.223 1.00 35.28 ?  582 GLY A C     1 
ATOM   4678  O  O     . GLY A 1 582 ? 127.242 130.278 99.352  1.00 37.33 ?  582 GLY A O     1 
ATOM   4679  N  N     . SER A 1 583 ? 126.506 132.007 100.589 1.00 37.73 ?  583 SER A N     1 
ATOM   4680  C  CA    . SER A 1 583 ? 125.131 131.879 100.119 1.00 38.50 ?  583 SER A CA    1 
ATOM   4681  C  C     . SER A 1 583 ? 124.824 132.714 98.885  1.00 36.64 ?  583 SER A C     1 
ATOM   4682  O  O     . SER A 1 583 ? 123.869 132.401 98.168  1.00 38.67 ?  583 SER A O     1 
ATOM   4683  C  CB    . SER A 1 583 ? 124.154 132.259 101.236 1.00 42.09 ?  583 SER A CB    1 
ATOM   4684  O  OG    . SER A 1 583 ? 122.874 131.699 101.004 1.00 39.94 ?  583 SER A OG    1 
ATOM   4685  N  N     . ILE A 1 584 ? 125.601 133.767 98.618  1.00 33.14 ?  584 ILE A N     1 
ATOM   4686  C  CA    . ILE A 1 584 ? 125.368 134.561 97.418  1.00 31.28 ?  584 ILE A CA    1 
ATOM   4687  C  C     . ILE A 1 584 ? 125.785 133.812 96.161  1.00 33.16 ?  584 ILE A C     1 
ATOM   4688  O  O     . ILE A 1 584 ? 125.439 134.232 95.051  1.00 40.10 ?  584 ILE A O     1 
ATOM   4689  C  CB    . ILE A 1 584 ? 126.100 135.913 97.508  1.00 34.85 ?  584 ILE A CB    1 
ATOM   4690  C  CG1   . ILE A 1 584 ? 127.574 135.702 97.860  1.00 34.66 ?  584 ILE A CG1   1 
ATOM   4691  C  CG2   . ILE A 1 584 ? 125.420 136.824 98.515  1.00 33.01 ?  584 ILE A CG2   1 
ATOM   4692  C  CD1   . ILE A 1 584 ? 128.397 136.971 97.835  1.00 33.24 ?  584 ILE A CD1   1 
ATOM   4693  N  N     . SER A 1 585 ? 126.529 132.713 96.304  1.00 32.18 ?  585 SER A N     1 
ATOM   4694  C  CA    . SER A 1 585 ? 126.919 131.926 95.141  1.00 29.46 ?  585 SER A CA    1 
ATOM   4695  C  C     . SER A 1 585 ? 125.721 131.239 94.501  1.00 31.36 ?  585 SER A C     1 
ATOM   4696  O  O     . SER A 1 585 ? 125.687 131.070 93.278  1.00 33.66 ?  585 SER A O     1 
ATOM   4697  C  CB    . SER A 1 585 ? 127.978 130.899 95.537  1.00 29.82 ?  585 SER A CB    1 
ATOM   4698  O  OG    . SER A 1 585 ? 127.547 130.123 96.641  1.00 35.57 ?  585 SER A OG    1 
ATOM   4699  N  N     . TYR A 1 586 ? 124.739 130.826 95.307  1.00 31.83 ?  586 TYR A N     1 
ATOM   4700  C  CA    . TYR A 1 586 ? 123.515 130.263 94.749  1.00 33.16 ?  586 TYR A CA    1 
ATOM   4701  C  C     . TYR A 1 586 ? 122.750 131.307 93.948  1.00 32.37 ?  586 TYR A C     1 
ATOM   4702  O  O     . TYR A 1 586 ? 122.331 131.049 92.815  1.00 39.34 ?  586 TYR A O     1 
ATOM   4703  C  CB    . TYR A 1 586 ? 122.633 129.707 95.865  1.00 33.29 ?  586 TYR A CB    1 
ATOM   4704  C  CG    . TYR A 1 586 ? 123.247 128.571 96.644  1.00 34.35 ?  586 TYR A CG    1 
ATOM   4705  C  CD1   . TYR A 1 586 ? 123.178 127.268 96.177  1.00 35.32 ?  586 TYR A CD1   1 
ATOM   4706  C  CD2   . TYR A 1 586 ? 123.883 128.800 97.855  1.00 31.34 ?  586 TYR A CD2   1 
ATOM   4707  C  CE1   . TYR A 1 586 ? 123.733 126.226 96.889  1.00 36.39 ?  586 TYR A CE1   1 
ATOM   4708  C  CE2   . TYR A 1 586 ? 124.442 127.766 98.573  1.00 33.62 ?  586 TYR A CE2   1 
ATOM   4709  C  CZ    . TYR A 1 586 ? 124.364 126.480 98.086  1.00 37.41 ?  586 TYR A CZ    1 
ATOM   4710  O  OH    . TYR A 1 586 ? 124.919 125.446 98.801  1.00 40.64 ?  586 TYR A OH    1 
ATOM   4711  N  N     . VAL A 1 587 ? 122.575 132.499 94.523  1.00 29.24 ?  587 VAL A N     1 
ATOM   4712  C  CA    . VAL A 1 587 ? 121.813 133.558 93.866  1.00 27.25 ?  587 VAL A CA    1 
ATOM   4713  C  C     . VAL A 1 587 ? 122.455 133.932 92.538  1.00 30.87 ?  587 VAL A C     1 
ATOM   4714  O  O     . VAL A 1 587 ? 121.765 134.127 91.530  1.00 33.39 ?  587 VAL A O     1 
ATOM   4715  C  CB    . VAL A 1 587 ? 121.690 134.776 94.801  1.00 29.69 ?  587 VAL A CB    1 
ATOM   4716  C  CG1   . VAL A 1 587 ? 121.083 135.957 94.067  1.00 30.93 ?  587 VAL A CG1   1 
ATOM   4717  C  CG2   . VAL A 1 587 ? 120.869 134.419 96.025  1.00 31.47 ?  587 VAL A CG2   1 
ATOM   4718  N  N     . GLN A 1 588 ? 123.780 134.029 92.513  1.00 32.92 ?  588 GLN A N     1 
ATOM   4719  C  CA    . GLN A 1 588 ? 124.506 134.363 91.297  1.00 29.21 ?  588 GLN A CA    1 
ATOM   4720  C  C     . GLN A 1 588 ? 124.700 133.167 90.378  1.00 28.76 ?  588 GLN A C     1 
ATOM   4721  O  O     . GLN A 1 588 ? 125.256 133.334 89.288  1.00 31.83 ?  588 GLN A O     1 
ATOM   4722  C  CB    . GLN A 1 588 ? 125.868 134.962 91.648  1.00 26.58 ?  588 GLN A CB    1 
ATOM   4723  C  CG    . GLN A 1 588 ? 125.802 136.372 92.195  1.00 24.83 ?  588 GLN A CG    1 
ATOM   4724  C  CD    . GLN A 1 588 ? 126.019 137.416 91.123  1.00 27.77 ?  588 GLN A CD    1 
ATOM   4725  O  OE1   . GLN A 1 588 ? 126.859 137.249 90.242  1.00 29.67 ?  588 GLN A OE1   1 
ATOM   4726  N  NE2   . GLN A 1 588 ? 125.266 138.505 91.196  1.00 29.68 ?  588 GLN A NE2   1 
ATOM   4727  N  N     . SER A 1 589 ? 124.253 131.981 90.790  1.00 32.59 ?  589 SER A N     1 
ATOM   4728  C  CA    . SER A 1 589 ? 124.451 130.744 90.041  1.00 29.72 ?  589 SER A CA    1 
ATOM   4729  C  C     . SER A 1 589 ? 125.930 130.559 89.712  1.00 32.19 ?  589 SER A C     1 
ATOM   4730  O  O     . SER A 1 589 ? 126.343 130.479 88.554  1.00 30.48 ?  589 SER A O     1 
ATOM   4731  C  CB    . SER A 1 589 ? 123.586 130.719 88.780  1.00 30.42 ?  589 SER A CB    1 
ATOM   4732  O  OG    . SER A 1 589 ? 123.241 129.390 88.430  1.00 40.48 ?  589 SER A OG    1 
ATOM   4733  N  N     . SER A 1 590 ? 126.730 130.505 90.772  1.00 33.30 ?  590 SER A N     1 
ATOM   4734  C  CA    . SER A 1 590 ? 128.177 130.487 90.652  1.00 26.43 ?  590 SER A CA    1 
ATOM   4735  C  C     . SER A 1 590 ? 128.759 129.518 91.667  1.00 27.25 ?  590 SER A C     1 
ATOM   4736  O  O     . SER A 1 590 ? 128.158 129.254 92.711  1.00 31.48 ?  590 SER A O     1 
ATOM   4737  C  CB    . SER A 1 590 ? 128.766 131.887 90.865  1.00 23.21 ?  590 SER A CB    1 
ATOM   4738  O  OG    . SER A 1 590 ? 129.194 132.059 92.201  1.00 32.45 ?  590 SER A OG    1 
ATOM   4739  N  N     . THR A 1 591 ? 129.931 128.981 91.345  1.00 27.43 ?  591 THR A N     1 
ATOM   4740  C  CA    . THR A 1 591 ? 130.665 128.178 92.310  1.00 22.38 ?  591 THR A CA    1 
ATOM   4741  C  C     . THR A 1 591 ? 131.242 129.074 93.399  1.00 27.07 ?  591 THR A C     1 
ATOM   4742  O  O     . THR A 1 591 ? 131.563 130.243 93.170  1.00 25.19 ?  591 THR A O     1 
ATOM   4743  C  CB    . THR A 1 591 ? 131.779 127.388 91.623  1.00 25.20 ?  591 THR A CB    1 
ATOM   4744  O  OG1   . THR A 1 591 ? 132.794 128.286 91.161  1.00 33.06 ?  591 THR A OG1   1 
ATOM   4745  C  CG2   . THR A 1 591 ? 131.225 126.615 90.442  1.00 25.62 ?  591 THR A CG2   1 
ATOM   4746  N  N     . ALA A 1 592 ? 131.368 128.516 94.599  1.00 26.79 ?  592 ALA A N     1 
ATOM   4747  C  CA    . ALA A 1 592 ? 131.747 129.309 95.760  1.00 24.60 ?  592 ALA A CA    1 
ATOM   4748  C  C     . ALA A 1 592 ? 133.211 129.720 95.670  1.00 28.69 ?  592 ALA A C     1 
ATOM   4749  O  O     . ALA A 1 592 ? 134.102 128.864 95.640  1.00 31.31 ?  592 ALA A O     1 
ATOM   4750  C  CB    . ALA A 1 592 ? 131.491 128.522 97.042  1.00 28.80 ?  592 ALA A CB    1 
ATOM   4751  N  N     . SER A 1 593 ? 133.450 131.027 95.624  1.00 27.10 ?  593 SER A N     1 
ATOM   4752  C  CA    . SER A 1 593 ? 134.791 131.621 95.688  1.00 11.59 ?  593 SER A CA    1 
ATOM   4753  C  C     . SER A 1 593 ? 135.625 131.097 94.516  1.00 13.13 ?  593 SER A C     1 
ATOM   4754  O  O     . SER A 1 593 ? 135.082 130.711 93.473  1.00 27.44 ?  593 SER A O     1 
ATOM   4755  C  CB    . SER A 1 593 ? 135.387 131.358 97.060  1.00 28.10 ?  593 SER A CB    1 
ATOM   4756  O  OG    . SER A 1 593 ? 136.612 132.043 97.233  1.00 29.10 ?  593 SER A OG    1 
ATOM   4757  N  N     . VAL A 1 594 ? 136.950 131.090 94.673  1.00 23.32 ?  594 VAL A N     1 
ATOM   4758  C  CA    . VAL A 1 594 ? 137.849 130.527 93.674  1.00 19.82 ?  594 VAL A CA    1 
ATOM   4759  C  C     . VAL A 1 594 ? 138.218 129.085 93.982  1.00 14.86 ?  594 VAL A C     1 
ATOM   4760  O  O     . VAL A 1 594 ? 139.043 128.497 93.273  1.00 17.59 ?  594 VAL A O     1 
ATOM   4761  C  CB    . VAL A 1 594 ? 139.118 131.391 93.532  1.00 18.67 ?  594 VAL A CB    1 
ATOM   4762  C  CG1   . VAL A 1 594 ? 138.773 132.734 92.912  1.00 11.94 ?  594 VAL A CG1   1 
ATOM   4763  C  CG2   . VAL A 1 594 ? 139.785 131.584 94.881  1.00 18.42 ?  594 VAL A CG2   1 
ATOM   4764  N  N     . MET A 1 595 ? 137.629 128.501 95.022  1.00 22.05 ?  595 MET A N     1 
ATOM   4765  C  CA    . MET A 1 595 ? 137.883 127.113 95.360  1.00 20.53 ?  595 MET A CA    1 
ATOM   4766  C  C     . MET A 1 595 ? 137.132 126.182 94.411  1.00 23.58 ?  595 MET A C     1 
ATOM   4767  O  O     . MET A 1 595 ? 136.107 126.560 93.836  1.00 25.01 ?  595 MET A O     1 
ATOM   4768  C  CB    . MET A 1 595 ? 137.467 126.837 96.804  1.00 22.89 ?  595 MET A CB    1 
ATOM   4769  C  CG    . MET A 1 595 ? 138.622 126.609 97.781  1.00 21.47 ?  595 MET A CG    1 
ATOM   4770  S  SD    . MET A 1 595 ? 140.105 127.599 97.503  1.00 30.92 ?  595 MET A SD    1 
ATOM   4771  C  CE    . MET A 1 595 ? 139.475 129.266 97.656  1.00 31.89 ?  595 MET A CE    1 
ATOM   4772  N  N     . PRO A 1 596 ? 137.628 124.963 94.220  1.00 30.79 ?  596 PRO A N     1 
ATOM   4773  C  CA    . PRO A 1 596 ? 136.907 123.992 93.394  1.00 20.09 ?  596 PRO A CA    1 
ATOM   4774  C  C     . PRO A 1 596 ? 135.642 123.498 94.079  1.00 25.96 ?  596 PRO A C     1 
ATOM   4775  O  O     . PRO A 1 596 ? 135.483 123.581 95.299  1.00 30.13 ?  596 PRO A O     1 
ATOM   4776  C  CB    . PRO A 1 596 ? 137.919 122.859 93.211  1.00 23.39 ?  596 PRO A CB    1 
ATOM   4777  C  CG    . PRO A 1 596 ? 138.824 122.975 94.385  1.00 29.22 ?  596 PRO A CG    1 
ATOM   4778  C  CD    . PRO A 1 596 ? 138.917 124.434 94.698  1.00 28.42 ?  596 PRO A CD    1 
ATOM   4779  N  N     . ILE A 1 597 ? 134.730 122.975 93.258  1.00 27.79 ?  597 ILE A N     1 
ATOM   4780  C  CA    . ILE A 1 597 ? 133.446 122.507 93.762  1.00 30.69 ?  597 ILE A CA    1 
ATOM   4781  C  C     . ILE A 1 597 ? 133.637 121.257 94.610  1.00 31.57 ?  597 ILE A C     1 
ATOM   4782  O  O     . ILE A 1 597 ? 134.549 120.451 94.385  1.00 31.34 ?  597 ILE A O     1 
ATOM   4783  C  CB    . ILE A 1 597 ? 132.473 122.241 92.599  1.00 31.28 ?  597 ILE A CB    1 
ATOM   4784  C  CG1   . ILE A 1 597 ? 132.933 121.031 91.782  1.00 27.57 ?  597 ILE A CG1   1 
ATOM   4785  C  CG2   . ILE A 1 597 ? 132.359 123.462 91.717  1.00 29.49 ?  597 ILE A CG2   1 
ATOM   4786  C  CD1   . ILE A 1 597 ? 131.810 120.236 91.177  1.00 28.63 ?  597 ILE A CD1   1 
ATOM   4787  N  N     . MET A 1 598 ? 132.763 121.091 95.600  1.00 40.39 ?  598 MET A N     1 
ATOM   4788  C  CA    . MET A 1 598 ? 132.790 119.914 96.457  1.00 41.34 ?  598 MET A CA    1 
ATOM   4789  C  C     . MET A 1 598 ? 131.951 118.774 95.893  1.00 40.72 ?  598 MET A C     1 
ATOM   4790  O  O     . MET A 1 598 ? 132.391 117.620 95.903  1.00 44.88 ?  598 MET A O     1 
ATOM   4791  C  CB    . MET A 1 598 ? 132.302 120.275 97.861  1.00 42.03 ?  598 MET A CB    1 
ATOM   4792  C  CG    . MET A 1 598 ? 132.837 121.598 98.378  1.00 39.71 ?  598 MET A CG    1 
ATOM   4793  S  SD    . MET A 1 598 ? 132.722 121.757 100.169 1.00 57.19 ?  598 MET A SD    1 
ATOM   4794  C  CE    . MET A 1 598 ? 131.397 120.609 100.533 1.00 44.70 ?  598 MET A CE    1 
ATOM   4795  N  N     . GLU A 1 599 ? 130.749 119.075 95.407  1.00 41.01 ?  599 GLU A N     1 
ATOM   4796  C  CA    . GLU A 1 599 ? 129.865 118.089 94.803  1.00 39.32 ?  599 GLU A CA    1 
ATOM   4797  C  C     . GLU A 1 599 ? 129.400 118.596 93.449  1.00 38.14 ?  599 GLU A C     1 
ATOM   4798  O  O     . GLU A 1 599 ? 129.129 119.789 93.287  1.00 42.33 ?  599 GLU A O     1 
ATOM   4799  C  CB    . GLU A 1 599 ? 128.646 117.804 95.692  1.00 42.81 ?  599 GLU A CB    1 
ATOM   4800  C  CG    . GLU A 1 599 ? 128.930 117.850 97.183  1.00 44.35 ?  599 GLU A CG    1 
ATOM   4801  C  CD    . GLU A 1 599 ? 127.665 117.834 98.020  1.00 48.19 ?  599 GLU A CD    1 
ATOM   4802  O  OE1   . GLU A 1 599 ? 127.019 116.770 98.102  1.00 47.76 ?  599 GLU A OE1   1 
ATOM   4803  O  OE2   . GLU A 1 599 ? 127.320 118.886 98.597  1.00 45.85 -1 599 GLU A OE2   1 
ATOM   4804  N  N     . ARG A 1 600 ? 129.315 117.689 92.473  1.00 41.41 ?  600 ARG A N     1 
ATOM   4805  C  CA    . ARG A 1 600 ? 128.779 118.062 91.168  1.00 36.75 ?  600 ARG A CA    1 
ATOM   4806  C  C     . ARG A 1 600 ? 127.300 118.411 91.270  1.00 37.88 ?  600 ARG A C     1 
ATOM   4807  O  O     . ARG A 1 600 ? 126.857 119.447 90.761  1.00 41.00 ?  600 ARG A O     1 
ATOM   4808  C  CB    . ARG A 1 600 ? 128.996 116.932 90.165  1.00 36.61 ?  600 ARG A CB    1 
ATOM   4809  C  CG    . ARG A 1 600 ? 130.390 116.885 89.581  1.00 36.23 ?  600 ARG A CG    1 
ATOM   4810  C  CD    . ARG A 1 600 ? 130.451 115.928 88.412  1.00 36.48 ?  600 ARG A CD    1 
ATOM   4811  N  NE    . ARG A 1 600 ? 131.817 115.674 87.972  1.00 35.63 ?  600 ARG A NE    1 
ATOM   4812  C  CZ    . ARG A 1 600 ? 132.631 114.791 88.532  1.00 38.66 ?  600 ARG A CZ    1 
ATOM   4813  N  NH1   . ARG A 1 600 ? 132.256 114.072 89.576  1.00 37.64 1  600 ARG A NH1   1 
ATOM   4814  N  NH2   . ARG A 1 600 ? 133.852 114.627 88.033  1.00 39.46 ?  600 ARG A NH2   1 
ATOM   4815  N  N     . ILE A 1 601 ? 126.522 117.551 91.918  1.00 45.37 ?  601 ILE A N     1 
ATOM   4816  C  CA    . ILE A 1 601 ? 125.125 117.818 92.233  1.00 43.26 ?  601 ILE A CA    1 
ATOM   4817  C  C     . ILE A 1 601 ? 125.009 117.849 93.748  1.00 42.50 ?  601 ILE A C     1 
ATOM   4818  O  O     . ILE A 1 601 ? 125.317 116.857 94.420  1.00 46.73 ?  601 ILE A O     1 
ATOM   4819  C  CB    . ILE A 1 601 ? 124.183 116.767 91.626  1.00 42.87 ?  601 ILE A CB    1 
ATOM   4820  C  CG1   . ILE A 1 601 ? 124.510 116.555 90.147  1.00 43.32 ?  601 ILE A CG1   1 
ATOM   4821  C  CG2   . ILE A 1 601 ? 122.735 117.198 91.791  1.00 42.85 ?  601 ILE A CG2   1 
ATOM   4822  C  CD1   . ILE A 1 601 ? 123.655 115.512 89.474  1.00 43.38 ?  601 ILE A CD1   1 
ATOM   4823  N  N     . GLU A 1 602 ? 124.569 118.980 94.282  1.00 49.62 ?  602 GLU A N     1 
ATOM   4824  C  CA    . GLU A 1 602 ? 124.558 119.216 95.717  1.00 49.44 ?  602 GLU A CA    1 
ATOM   4825  C  C     . GLU A 1 602 ? 123.165 118.922 96.261  1.00 51.45 ?  602 GLU A C     1 
ATOM   4826  O  O     . GLU A 1 602 ? 122.185 119.548 95.844  1.00 53.93 ?  602 GLU A O     1 
ATOM   4827  C  CB    . GLU A 1 602 ? 124.977 120.652 96.025  1.00 49.41 ?  602 GLU A CB    1 
ATOM   4828  C  CG    . GLU A 1 602 ? 124.538 121.163 97.379  1.00 50.26 ?  602 GLU A CG    1 
ATOM   4829  C  CD    . GLU A 1 602 ? 124.807 122.644 97.546  1.00 54.59 ?  602 GLU A CD    1 
ATOM   4830  O  OE1   . GLU A 1 602 ? 125.797 123.138 96.966  1.00 52.32 ?  602 GLU A OE1   1 
ATOM   4831  O  OE2   . GLU A 1 602 ? 124.030 123.313 98.259  1.00 56.03 -1 602 GLU A OE2   1 
ATOM   4832  N  N     . GLU A 1 603 ? 123.082 117.969 97.183  1.00 56.98 ?  603 GLU A N     1 
ATOM   4833  C  CA    . GLU A 1 603 ? 121.822 117.550 97.778  1.00 57.36 ?  603 GLU A CA    1 
ATOM   4834  C  C     . GLU A 1 603 ? 121.660 118.211 99.141  1.00 58.62 ?  603 GLU A C     1 
ATOM   4835  O  O     . GLU A 1 603 ? 122.544 118.104 99.997  1.00 58.60 ?  603 GLU A O     1 
ATOM   4836  C  CB    . GLU A 1 603 ? 121.766 116.028 97.917  1.00 59.38 ?  603 GLU A CB    1 
ATOM   4837  C  CG    . GLU A 1 603 ? 120.475 115.501 98.516  1.00 60.68 ?  603 GLU A CG    1 
ATOM   4838  C  CD    . GLU A 1 603 ? 120.571 114.039 98.911  1.00 61.55 ?  603 GLU A CD    1 
ATOM   4839  O  OE1   . GLU A 1 603 ? 120.572 113.175 98.011  1.00 60.08 ?  603 GLU A OE1   1 
ATOM   4840  O  OE2   . GLU A 1 603 ? 120.647 113.754 100.125 1.00 59.52 -1 603 GLU A OE2   1 
ATOM   4841  N  N     . ARG A 1 604 ? 120.533 118.891 99.336  1.00 61.77 ?  604 ARG A N     1 
ATOM   4842  C  CA    . ARG A 1 604 ? 120.245 119.588 100.579 1.00 61.85 ?  604 ARG A CA    1 
ATOM   4843  C  C     . ARG A 1 604 ? 118.826 119.274 101.025 1.00 62.69 ?  604 ARG A C     1 
ATOM   4844  O  O     . ARG A 1 604 ? 117.960 118.939 100.213 1.00 64.24 ?  604 ARG A O     1 
ATOM   4845  C  CB    . ARG A 1 604 ? 120.409 121.106 100.428 1.00 59.98 ?  604 ARG A CB    1 
ATOM   4846  C  CG    . ARG A 1 604 ? 121.808 121.562 100.055 1.00 61.07 ?  604 ARG A CG    1 
ATOM   4847  C  CD    . ARG A 1 604 ? 122.776 121.379 101.210 1.00 62.30 ?  604 ARG A CD    1 
ATOM   4848  N  NE    . ARG A 1 604 ? 123.754 120.332 100.942 1.00 63.37 ?  604 ARG A NE    1 
ATOM   4849  C  CZ    . ARG A 1 604 ? 125.045 120.552 100.728 1.00 62.57 ?  604 ARG A CZ    1 
ATOM   4850  N  NH1   . ARG A 1 604 ? 125.549 121.774 100.748 1.00 61.28 1  604 ARG A NH1   1 
ATOM   4851  N  NH2   . ARG A 1 604 ? 125.847 119.521 100.487 1.00 60.05 ?  604 ARG A NH2   1 
ATOM   4852  N  N     . THR A 1 605 ? 118.597 119.384 102.331 1.00 68.82 ?  605 THR A N     1 
ATOM   4853  C  CA    . THR A 1 605 ? 117.275 119.215 102.919 1.00 70.06 ?  605 THR A CA    1 
ATOM   4854  C  C     . THR A 1 605 ? 116.887 120.511 103.614 1.00 69.42 ?  605 THR A C     1 
ATOM   4855  O  O     . THR A 1 605 ? 117.557 120.935 104.562 1.00 69.58 ?  605 THR A O     1 
ATOM   4856  C  CB    . THR A 1 605 ? 117.251 118.047 103.909 1.00 70.54 ?  605 THR A CB    1 
ATOM   4857  O  OG1   . THR A 1 605 ? 118.135 117.015 103.456 1.00 71.33 ?  605 THR A OG1   1 
ATOM   4858  C  CG2   . THR A 1 605 ? 115.845 117.482 104.026 1.00 69.20 ?  605 THR A CG2   1 
ATOM   4859  N  N     . TYR A 1 606 ? 115.812 121.137 103.144 1.00 68.76 ?  606 TYR A N     1 
ATOM   4860  C  CA    . TYR A 1 606 ? 115.296 122.373 103.723 1.00 71.10 ?  606 TYR A CA    1 
ATOM   4861  C  C     . TYR A 1 606 ? 113.959 122.056 104.379 1.00 72.93 ?  606 TYR A C     1 
ATOM   4862  O  O     . TYR A 1 606 ? 112.981 121.747 103.689 1.00 70.59 ?  606 TYR A O     1 
ATOM   4863  C  CB    . TYR A 1 606 ? 115.155 123.459 102.659 1.00 69.38 ?  606 TYR A CB    1 
ATOM   4864  C  CG    . TYR A 1 606 ? 116.479 123.920 102.093 1.00 70.30 ?  606 TYR A CG    1 
ATOM   4865  C  CD1   . TYR A 1 606 ? 117.270 124.835 102.776 1.00 68.23 ?  606 TYR A CD1   1 
ATOM   4866  C  CD2   . TYR A 1 606 ? 116.942 123.434 100.880 1.00 69.45 ?  606 TYR A CD2   1 
ATOM   4867  C  CE1   . TYR A 1 606 ? 118.482 125.253 102.263 1.00 68.83 ?  606 TYR A CE1   1 
ATOM   4868  C  CE2   . TYR A 1 606 ? 118.151 123.847 100.358 1.00 67.17 ?  606 TYR A CE2   1 
ATOM   4869  C  CZ    . TYR A 1 606 ? 118.917 124.755 101.054 1.00 70.11 ?  606 TYR A CZ    1 
ATOM   4870  O  OH    . TYR A 1 606 ? 120.122 125.167 100.535 1.00 70.97 ?  606 TYR A OH    1 
ATOM   4871  N  N     . GLY A 1 607 ? 113.917 122.138 105.703 1.00 80.04 ?  607 GLY A N     1 
ATOM   4872  C  CA    . GLY A 1 607 ? 112.733 121.702 106.424 1.00 78.48 ?  607 GLY A CA    1 
ATOM   4873  C  C     . GLY A 1 607 ? 112.527 120.215 106.223 1.00 78.34 ?  607 GLY A C     1 
ATOM   4874  O  O     . GLY A 1 607 ? 113.431 119.401 106.451 1.00 78.36 ?  607 GLY A O     1 
ATOM   4875  N  N     . ASN A 1 608 ? 111.325 119.839 105.786 1.00 79.97 ?  608 ASN A N     1 
ATOM   4876  C  CA    . ASN A 1 608 ? 111.001 118.454 105.469 1.00 81.03 ?  608 ASN A CA    1 
ATOM   4877  C  C     . ASN A 1 608 ? 111.013 118.192 103.967 1.00 80.88 ?  608 ASN A C     1 
ATOM   4878  O  O     . ASN A 1 608 ? 110.358 117.259 103.491 1.00 80.73 ?  608 ASN A O     1 
ATOM   4879  C  CB    . ASN A 1 608 ? 109.645 118.076 106.067 1.00 80.47 ?  608 ASN A CB    1 
ATOM   4880  C  CG    . ASN A 1 608 ? 109.620 118.202 107.579 1.00 81.27 ?  608 ASN A CG    1 
ATOM   4881  O  OD1   . ASN A 1 608 ? 110.664 118.291 108.226 1.00 80.58 ?  608 ASN A OD1   1 
ATOM   4882  N  ND2   . ASN A 1 608 ? 108.421 118.206 108.151 1.00 80.54 ?  608 ASN A ND2   1 
ATOM   4883  N  N     . SER A 1 609 ? 111.751 119.001 103.212 1.00 77.90 ?  609 SER A N     1 
ATOM   4884  C  CA    . SER A 1 609 ? 111.826 118.889 101.763 1.00 77.94 ?  609 SER A CA    1 
ATOM   4885  C  C     . SER A 1 609 ? 113.272 118.679 101.338 1.00 77.93 ?  609 SER A C     1 
ATOM   4886  O  O     . SER A 1 609 ? 114.180 119.347 101.841 1.00 78.15 ?  609 SER A O     1 
ATOM   4887  C  CB    . SER A 1 609 ? 111.262 120.140 101.085 1.00 76.58 ?  609 SER A CB    1 
ATOM   4888  O  OG    . SER A 1 609 ? 112.015 121.290 101.430 1.00 77.68 ?  609 SER A OG    1 
ATOM   4889  N  N     . LYS A 1 610 ? 113.478 117.753 100.406 1.00 66.97 ?  610 LYS A N     1 
ATOM   4890  C  CA    . LYS A 1 610 ? 114.800 117.439 99.881  1.00 66.32 ?  610 LYS A CA    1 
ATOM   4891  C  C     . LYS A 1 610 ? 114.903 117.945 98.449  1.00 66.53 ?  610 LYS A C     1 
ATOM   4892  O  O     . LYS A 1 610 ? 114.040 117.648 97.616  1.00 67.67 ?  610 LYS A O     1 
ATOM   4893  C  CB    . LYS A 1 610 ? 115.066 115.934 99.936  1.00 66.92 ?  610 LYS A CB    1 
ATOM   4894  C  CG    . LYS A 1 610 ? 116.066 115.437 98.905  1.00 66.39 ?  610 LYS A CG    1 
ATOM   4895  C  CD    . LYS A 1 610 ? 116.704 114.129 99.342  1.00 66.95 ?  610 LYS A CD    1 
ATOM   4896  C  CE    . LYS A 1 610 ? 117.212 114.205 100.773 1.00 66.22 ?  610 LYS A CE    1 
ATOM   4897  N  NZ    . LYS A 1 610 ? 118.205 115.298 100.951 1.00 66.39 1  610 LYS A NZ    1 
ATOM   4898  N  N     . THR A 1 611 ? 115.956 118.708 98.168  1.00 64.78 ?  611 THR A N     1 
ATOM   4899  C  CA    . THR A 1 611 ? 116.156 119.305 96.856  1.00 63.63 ?  611 THR A CA    1 
ATOM   4900  C  C     . THR A 1 611 ? 117.619 119.182 96.462  1.00 62.02 ?  611 THR A C     1 
ATOM   4901  O  O     . THR A 1 611 ? 118.504 119.118 97.317  1.00 61.18 ?  611 THR A O     1 
ATOM   4902  C  CB    . THR A 1 611 ? 115.727 120.776 96.837  1.00 64.51 ?  611 THR A CB    1 
ATOM   4903  O  OG1   . THR A 1 611 ? 116.146 121.380 95.607  1.00 68.33 ?  611 THR A OG1   1 
ATOM   4904  C  CG2   . THR A 1 611 ? 116.343 121.520 98.006  1.00 61.51 ?  611 THR A CG2   1 
ATOM   4905  N  N     . TYR A 1 612 ? 117.865 119.151 95.155  1.00 55.17 ?  612 TYR A N     1 
ATOM   4906  C  CA    . TYR A 1 612 ? 119.196 118.929 94.614  1.00 53.75 ?  612 TYR A CA    1 
ATOM   4907  C  C     . TYR A 1 612 ? 119.625 120.124 93.777  1.00 55.99 ?  612 TYR A C     1 
ATOM   4908  O  O     . TYR A 1 612 ? 118.825 120.688 93.023  1.00 55.12 ?  612 TYR A O     1 
ATOM   4909  C  CB    . TYR A 1 612 ? 119.264 117.652 93.762  1.00 56.44 ?  612 TYR A CB    1 
ATOM   4910  C  CG    . TYR A 1 612 ? 118.766 116.394 94.448  1.00 58.31 ?  612 TYR A CG    1 
ATOM   4911  C  CD1   . TYR A 1 612 ? 117.424 116.230 94.769  1.00 57.73 ?  612 TYR A CD1   1 
ATOM   4912  C  CD2   . TYR A 1 612 ? 119.647 115.382 94.797  1.00 57.67 ?  612 TYR A CD2   1 
ATOM   4913  C  CE1   . TYR A 1 612 ? 116.973 115.088 95.397  1.00 58.44 ?  612 TYR A CE1   1 
ATOM   4914  C  CE2   . TYR A 1 612 ? 119.206 114.236 95.426  1.00 58.52 ?  612 TYR A CE2   1 
ATOM   4915  C  CZ    . TYR A 1 612 ? 117.868 114.095 95.725  1.00 60.23 ?  612 TYR A CZ    1 
ATOM   4916  O  OH    . TYR A 1 612 ? 117.425 112.953 96.354  1.00 60.85 ?  612 TYR A OH    1 
ATOM   4917  N  N     . TYR A 1 613 ? 120.892 120.504 93.914  1.00 51.49 ?  613 TYR A N     1 
ATOM   4918  C  CA    . TYR A 1 613 ? 121.460 121.643 93.194  1.00 42.49 ?  613 TYR A CA    1 
ATOM   4919  C  C     . TYR A 1 613 ? 122.632 121.200 92.334  1.00 41.14 ?  613 TYR A C     1 
ATOM   4920  O  O     . TYR A 1 613 ? 123.750 121.018 92.848  1.00 44.64 ?  613 TYR A O     1 
ATOM   4921  C  CB    . TYR A 1 613 ? 121.904 122.732 94.169  1.00 41.40 ?  613 TYR A CB    1 
ATOM   4922  C  CG    . TYR A 1 613 ? 122.523 123.933 93.493  1.00 41.89 ?  613 TYR A CG    1 
ATOM   4923  C  CD1   . TYR A 1 613 ? 121.898 124.547 92.417  1.00 42.79 ?  613 TYR A CD1   1 
ATOM   4924  C  CD2   . TYR A 1 613 ? 123.732 124.454 93.931  1.00 42.04 ?  613 TYR A CD2   1 
ATOM   4925  C  CE1   . TYR A 1 613 ? 122.457 125.645 91.799  1.00 43.12 ?  613 TYR A CE1   1 
ATOM   4926  C  CE2   . TYR A 1 613 ? 124.300 125.551 93.319  1.00 43.78 ?  613 TYR A CE2   1 
ATOM   4927  C  CZ    . TYR A 1 613 ? 123.658 126.144 92.254  1.00 46.61 ?  613 TYR A CZ    1 
ATOM   4928  O  OH    . TYR A 1 613 ? 124.218 127.238 91.640  1.00 46.20 ?  613 TYR A OH    1 
ATOM   4929  N  N     . PRO A 1 614 ? 122.437 121.008 91.034  1.00 40.55 ?  614 PRO A N     1 
ATOM   4930  C  CA    . PRO A 1 614 ? 123.584 120.788 90.150  1.00 40.16 ?  614 PRO A CA    1 
ATOM   4931  C  C     . PRO A 1 614 ? 124.454 122.031 90.086  1.00 40.09 ?  614 PRO A C     1 
ATOM   4932  O  O     . PRO A 1 614 ? 123.980 123.158 90.251  1.00 43.40 ?  614 PRO A O     1 
ATOM   4933  C  CB    . PRO A 1 614 ? 122.942 120.487 88.788  1.00 37.04 ?  614 PRO A CB    1 
ATOM   4934  C  CG    . PRO A 1 614 ? 121.490 120.253 89.068  1.00 43.01 ?  614 PRO A CG    1 
ATOM   4935  C  CD    . PRO A 1 614 ? 121.166 121.031 90.296  1.00 42.07 ?  614 PRO A CD    1 
ATOM   4936  N  N     . MET A 1 615 ? 125.744 121.815 89.855  1.00 37.48 ?  615 MET A N     1 
ATOM   4937  C  CA    . MET A 1 615 ? 126.660 122.934 89.735  1.00 37.01 ?  615 MET A CA    1 
ATOM   4938  C  C     . MET A 1 615 ? 126.282 123.784 88.524  1.00 41.63 ?  615 MET A C     1 
ATOM   4939  O  O     . MET A 1 615 ? 125.770 123.264 87.528  1.00 38.54 ?  615 MET A O     1 
ATOM   4940  C  CB    . MET A 1 615 ? 128.099 122.440 89.613  1.00 33.82 ?  615 MET A CB    1 
ATOM   4941  C  CG    . MET A 1 615 ? 128.772 122.210 90.953  1.00 36.13 ?  615 MET A CG    1 
ATOM   4942  S  SD    . MET A 1 615 ? 128.353 123.479 92.164  1.00 52.76 ?  615 MET A SD    1 
ATOM   4943  C  CE    . MET A 1 615 ? 127.422 122.524 93.359  1.00 35.65 ?  615 MET A CE    1 
ATOM   4944  N  N     . PRO A 1 616 ? 126.490 125.097 88.596  1.00 40.49 ?  616 PRO A N     1 
ATOM   4945  C  CA    . PRO A 1 616 ? 126.060 125.976 87.500  1.00 35.85 ?  616 PRO A CA    1 
ATOM   4946  C  C     . PRO A 1 616 ? 126.702 125.584 86.178  1.00 36.86 ?  616 PRO A C     1 
ATOM   4947  O  O     . PRO A 1 616 ? 127.925 125.490 86.065  1.00 38.67 ?  616 PRO A O     1 
ATOM   4948  C  CB    . PRO A 1 616 ? 126.519 127.361 87.963  1.00 36.67 ?  616 PRO A CB    1 
ATOM   4949  C  CG    . PRO A 1 616 ? 126.586 127.251 89.448  1.00 38.59 ?  616 PRO A CG    1 
ATOM   4950  C  CD    . PRO A 1 616 ? 127.032 125.856 89.734  1.00 35.46 ?  616 PRO A CD    1 
ATOM   4951  N  N     . GLY A 1 617 ? 125.861 125.362 85.173  1.00 36.72 ?  617 GLY A N     1 
ATOM   4952  C  CA    . GLY A 1 617 ? 126.333 124.954 83.869  1.00 31.13 ?  617 GLY A CA    1 
ATOM   4953  C  C     . GLY A 1 617 ? 126.695 123.493 83.744  1.00 38.40 ?  617 GLY A C     1 
ATOM   4954  O  O     . GLY A 1 617 ? 127.243 123.097 82.711  1.00 40.80 ?  617 GLY A O     1 
ATOM   4955  N  N     . LEU A 1 618 ? 126.414 122.681 84.762  1.00 39.29 ?  618 LEU A N     1 
ATOM   4956  C  CA    . LEU A 1 618 ? 126.752 121.266 84.702  1.00 34.62 ?  618 LEU A CA    1 
ATOM   4957  C  C     . LEU A 1 618 ? 125.920 120.564 83.637  1.00 39.88 ?  618 LEU A C     1 
ATOM   4958  O  O     . LEU A 1 618 ? 124.715 120.795 83.508  1.00 40.59 ?  618 LEU A O     1 
ATOM   4959  C  CB    . LEU A 1 618 ? 126.532 120.604 86.061  1.00 34.82 ?  618 LEU A CB    1 
ATOM   4960  C  CG    . LEU A 1 618 ? 126.848 119.111 86.171  1.00 37.41 ?  618 LEU A CG    1 
ATOM   4961  C  CD1   . LEU A 1 618 ? 128.310 118.834 85.862  1.00 34.92 ?  618 LEU A CD1   1 
ATOM   4962  C  CD2   . LEU A 1 618 ? 126.481 118.581 87.547  1.00 35.44 ?  618 LEU A CD2   1 
ATOM   4963  N  N     . ALA A 1 619 ? 126.577 119.701 82.872  1.00 43.40 ?  619 ALA A N     1 
ATOM   4964  C  CA    . ALA A 1 619 ? 125.938 118.939 81.807  1.00 43.12 ?  619 ALA A CA    1 
ATOM   4965  C  C     . ALA A 1 619 ? 126.767 117.682 81.578  1.00 44.84 ?  619 ALA A C     1 
ATOM   4966  O  O     . ALA A 1 619 ? 127.640 117.341 82.382  1.00 50.01 ?  619 ALA A O     1 
ATOM   4967  C  CB    . ALA A 1 619 ? 125.799 119.783 80.535  1.00 41.78 ?  619 ALA A CB    1 
ATOM   4968  N  N     . SER A 1 620 ? 126.491 116.985 80.477  1.00 50.05 ?  620 SER A N     1 
ATOM   4969  C  CA    . SER A 1 620 ? 127.292 115.820 80.127  1.00 50.39 ?  620 SER A CA    1 
ATOM   4970  C  C     . SER A 1 620 ? 128.532 116.205 79.331  1.00 50.52 ?  620 SER A C     1 
ATOM   4971  O  O     . SER A 1 620 ? 129.514 115.456 79.321  1.00 54.16 ?  620 SER A O     1 
ATOM   4972  C  CB    . SER A 1 620 ? 126.449 114.818 79.338  1.00 53.17 ?  620 SER A CB    1 
ATOM   4973  O  OG    . SER A 1 620 ? 125.291 114.448 80.066  1.00 55.31 ?  620 SER A OG    1 
ATOM   4974  N  N     . ASN A 1 621 ? 128.507 117.361 78.665  1.00 48.00 ?  621 ASN A N     1 
ATOM   4975  C  CA    . ASN A 1 621 ? 129.659 117.786 77.879  1.00 48.37 ?  621 ASN A CA    1 
ATOM   4976  C  C     . ASN A 1 621 ? 130.774 118.338 78.760  1.00 51.61 ?  621 ASN A C     1 
ATOM   4977  O  O     . ASN A 1 621 ? 131.926 118.419 78.318  1.00 51.96 ?  621 ASN A O     1 
ATOM   4978  C  CB    . ASN A 1 621 ? 129.232 118.827 76.845  1.00 49.02 ?  621 ASN A CB    1 
ATOM   4979  C  CG    . ASN A 1 621 ? 129.202 120.233 77.409  1.00 51.03 ?  621 ASN A CG    1 
ATOM   4980  O  OD1   . ASN A 1 621 ? 128.332 120.573 78.211  1.00 50.38 ?  621 ASN A OD1   1 
ATOM   4981  N  ND2   . ASN A 1 621 ? 130.152 121.059 76.991  1.00 47.50 ?  621 ASN A ND2   1 
ATOM   4982  N  N     . ASN A 1 622 ? 130.458 118.723 79.996  1.00 44.03 ?  622 ASN A N     1 
ATOM   4983  C  CA    . ASN A 1 622 ? 131.449 119.236 80.936  1.00 40.24 ?  622 ASN A CA    1 
ATOM   4984  C  C     . ASN A 1 622 ? 131.324 118.568 82.301  1.00 42.76 ?  622 ASN A C     1 
ATOM   4985  O  O     . ASN A 1 622 ? 131.637 119.173 83.328  1.00 48.61 ?  622 ASN A O     1 
ATOM   4986  C  CB    . ASN A 1 622 ? 131.344 120.758 81.061  1.00 42.91 ?  622 ASN A CB    1 
ATOM   4987  C  CG    . ASN A 1 622 ? 129.957 121.227 81.476  1.00 42.30 ?  622 ASN A CG    1 
ATOM   4988  O  OD1   . ASN A 1 622 ? 129.244 120.547 82.210  1.00 43.38 ?  622 ASN A OD1   1 
ATOM   4989  N  ND2   . ASN A 1 622 ? 129.575 122.408 81.006  1.00 41.97 ?  622 ASN A ND2   1 
ATOM   4990  N  N     . TRP A 1 623 ? 130.856 117.318 82.323  1.00 37.70 ?  623 TRP A N     1 
ATOM   4991  C  CA    . TRP A 1 623 ? 130.697 116.610 83.589  1.00 38.13 ?  623 TRP A CA    1 
ATOM   4992  C  C     . TRP A 1 623 ? 132.040 116.373 84.268  1.00 38.97 ?  623 TRP A C     1 
ATOM   4993  O  O     . TRP A 1 623 ? 132.171 116.565 85.483  1.00 36.89 ?  623 TRP A O     1 
ATOM   4994  C  CB    . TRP A 1 623 ? 129.975 115.283 83.355  1.00 41.13 ?  623 TRP A CB    1 
ATOM   4995  C  CG    . TRP A 1 623 ? 129.864 114.430 84.580  1.00 37.94 ?  623 TRP A CG    1 
ATOM   4996  C  CD1   . TRP A 1 623 ? 130.744 113.475 84.995  1.00 37.18 ?  623 TRP A CD1   1 
ATOM   4997  C  CD2   . TRP A 1 623 ? 128.807 114.447 85.545  1.00 36.34 ?  623 TRP A CD2   1 
ATOM   4998  N  NE1   . TRP A 1 623 ? 130.304 112.899 86.160  1.00 37.99 ?  623 TRP A NE1   1 
ATOM   4999  C  CE2   . TRP A 1 623 ? 129.115 113.477 86.517  1.00 38.89 ?  623 TRP A CE2   1 
ATOM   5000  C  CE3   . TRP A 1 623 ? 127.630 115.188 85.680  1.00 37.48 ?  623 TRP A CE3   1 
ATOM   5001  C  CZ2   . TRP A 1 623 ? 128.291 113.231 87.613  1.00 37.40 ?  623 TRP A CZ2   1 
ATOM   5002  C  CZ3   . TRP A 1 623 ? 126.813 114.941 86.767  1.00 38.40 ?  623 TRP A CZ3   1 
ATOM   5003  C  CH2   . TRP A 1 623 ? 127.148 113.973 87.719  1.00 37.73 ?  623 TRP A CH2   1 
ATOM   5004  N  N     . PHE A 1 624 ? 133.047 115.955 83.505  1.00 43.16 ?  624 PHE A N     1 
ATOM   5005  C  CA    . PHE A 1 624 ? 134.340 115.622 84.085  1.00 41.82 ?  624 PHE A CA    1 
ATOM   5006  C  C     . PHE A 1 624 ? 135.244 116.832 84.270  1.00 42.59 ?  624 PHE A C     1 
ATOM   5007  O  O     . PHE A 1 624 ? 136.247 116.733 84.985  1.00 50.03 ?  624 PHE A O     1 
ATOM   5008  C  CB    . PHE A 1 624 ? 135.042 114.569 83.226  1.00 41.56 ?  624 PHE A CB    1 
ATOM   5009  C  CG    . PHE A 1 624 ? 134.347 113.238 83.227  1.00 45.32 ?  624 PHE A CG    1 
ATOM   5010  C  CD1   . PHE A 1 624 ? 134.339 112.450 84.365  1.00 42.10 ?  624 PHE A CD1   1 
ATOM   5011  C  CD2   . PHE A 1 624 ? 133.682 112.785 82.099  1.00 44.92 ?  624 PHE A CD2   1 
ATOM   5012  C  CE1   . PHE A 1 624 ? 133.694 111.232 84.376  1.00 41.33 ?  624 PHE A CE1   1 
ATOM   5013  C  CE2   . PHE A 1 624 ? 133.035 111.567 82.106  1.00 42.77 ?  624 PHE A CE2   1 
ATOM   5014  C  CZ    . PHE A 1 624 ? 133.040 110.789 83.244  1.00 45.45 ?  624 PHE A CZ    1 
ATOM   5015  N  N     . PHE A 1 625 ? 134.916 117.967 83.652  1.00 34.98 ?  625 PHE A N     1 
ATOM   5016  C  CA    . PHE A 1 625 ? 135.604 119.207 83.983  1.00 32.84 ?  625 PHE A CA    1 
ATOM   5017  C  C     . PHE A 1 625 ? 135.143 119.769 85.318  1.00 32.46 ?  625 PHE A C     1 
ATOM   5018  O  O     . PHE A 1 625 ? 135.861 120.573 85.921  1.00 36.35 ?  625 PHE A O     1 
ATOM   5019  C  CB    . PHE A 1 625 ? 135.403 120.241 82.877  1.00 31.54 ?  625 PHE A CB    1 
ATOM   5020  C  CG    . PHE A 1 625 ? 136.152 119.930 81.617  1.00 30.72 ?  625 PHE A CG    1 
ATOM   5021  C  CD1   . PHE A 1 625 ? 137.534 119.925 81.605  1.00 33.14 ?  625 PHE A CD1   1 
ATOM   5022  C  CD2   . PHE A 1 625 ? 135.475 119.650 80.443  1.00 34.06 ?  625 PHE A CD2   1 
ATOM   5023  C  CE1   . PHE A 1 625 ? 138.228 119.644 80.448  1.00 36.70 ?  625 PHE A CE1   1 
ATOM   5024  C  CE2   . PHE A 1 625 ? 136.165 119.368 79.283  1.00 32.14 ?  625 PHE A CE2   1 
ATOM   5025  C  CZ    . PHE A 1 625 ? 137.543 119.364 79.286  1.00 36.32 ?  625 PHE A CZ    1 
ATOM   5026  N  N     . TYR A 1 626 ? 133.966 119.367 85.789  1.00 29.43 ?  626 TYR A N     1 
ATOM   5027  C  CA    . TYR A 1 626 ? 133.490 119.729 87.122  1.00 31.49 ?  626 TYR A CA    1 
ATOM   5028  C  C     . TYR A 1 626 ? 133.979 118.731 88.165  1.00 27.64 ?  626 TYR A C     1 
ATOM   5029  O  O     . TYR A 1 626 ? 133.206 118.185 88.948  1.00 30.79 ?  626 TYR A O     1 
ATOM   5030  C  CB    . TYR A 1 626 ? 131.971 119.823 87.124  1.00 32.51 ?  626 TYR A CB    1 
ATOM   5031  C  CG    . TYR A 1 626 ? 131.448 121.207 86.842  1.00 28.67 ?  626 TYR A CG    1 
ATOM   5032  C  CD1   . TYR A 1 626 ? 131.603 122.229 87.767  1.00 32.63 ?  626 TYR A CD1   1 
ATOM   5033  C  CD2   . TYR A 1 626 ? 130.801 121.495 85.649  1.00 30.61 ?  626 TYR A CD2   1 
ATOM   5034  C  CE1   . TYR A 1 626 ? 131.128 123.497 87.513  1.00 29.49 ?  626 TYR A CE1   1 
ATOM   5035  C  CE2   . TYR A 1 626 ? 130.323 122.759 85.386  1.00 28.96 ?  626 TYR A CE2   1 
ATOM   5036  C  CZ    . TYR A 1 626 ? 130.490 123.755 86.322  1.00 27.83 ?  626 TYR A CZ    1 
ATOM   5037  O  OH    . TYR A 1 626 ? 130.017 125.018 86.069  1.00 34.46 ?  626 TYR A OH    1 
ATOM   5038  N  N     . LYS A 1 627 ? 135.287 118.496 88.172  1.00 31.50 ?  627 LYS A N     1 
ATOM   5039  C  CA    . LYS A 1 627 ? 135.880 117.549 89.104  1.00 31.57 ?  627 LYS A CA    1 
ATOM   5040  C  C     . LYS A 1 627 ? 135.690 118.030 90.535  1.00 31.68 ?  627 LYS A C     1 
ATOM   5041  O  O     . LYS A 1 627 ? 135.916 119.203 90.845  1.00 35.85 ?  627 LYS A O     1 
ATOM   5042  C  CB    . LYS A 1 627 ? 137.363 117.374 88.787  1.00 34.95 ?  627 LYS A CB    1 
ATOM   5043  C  CG    . LYS A 1 627 ? 138.062 116.302 89.595  1.00 34.41 ?  627 LYS A CG    1 
ATOM   5044  C  CD    . LYS A 1 627 ? 139.455 116.047 89.053  1.00 32.48 ?  627 LYS A CD    1 
ATOM   5045  C  CE    . LYS A 1 627 ? 140.182 114.997 89.867  1.00 38.41 ?  627 LYS A CE    1 
ATOM   5046  N  NZ    . LYS A 1 627 ? 141.602 114.867 89.446  1.00 39.70 1  627 LYS A NZ    1 
ATOM   5047  N  N     . GLU A 1 628 ? 135.267 117.121 91.408  1.00 35.59 ?  628 GLU A N     1 
ATOM   5048  C  CA    . GLU A 1 628 ? 135.044 117.481 92.800  1.00 36.22 ?  628 GLU A CA    1 
ATOM   5049  C  C     . GLU A 1 628 ? 136.365 117.791 93.493  1.00 39.79 ?  628 GLU A C     1 
ATOM   5050  O  O     . GLU A 1 628 ? 137.419 117.252 93.145  1.00 42.87 ?  628 GLU A O     1 
ATOM   5051  C  CB    . GLU A 1 628 ? 134.311 116.357 93.530  1.00 37.35 ?  628 GLU A CB    1 
ATOM   5052  C  CG    . GLU A 1 628 ? 132.915 116.087 92.994  1.00 39.53 ?  628 GLU A CG    1 
ATOM   5053  C  CD    . GLU A 1 628 ? 132.147 115.093 93.841  1.00 47.64 ?  628 GLU A CD    1 
ATOM   5054  O  OE1   . GLU A 1 628 ? 132.605 114.783 94.960  1.00 43.85 ?  628 GLU A OE1   1 
ATOM   5055  O  OE2   . GLU A 1 628 ? 131.081 114.624 93.388  1.00 44.12 -1 628 GLU A OE2   1 
ATOM   5056  N  N     . ALA A 1 629 ? 136.297 118.683 94.484  1.00 38.57 ?  629 ALA A N     1 
ATOM   5057  C  CA    . ALA A 1 629 ? 137.504 119.137 95.165  1.00 34.48 ?  629 ALA A CA    1 
ATOM   5058  C  C     . ALA A 1 629 ? 138.195 118.007 95.915  1.00 37.29 ?  629 ALA A C     1 
ATOM   5059  O  O     . ALA A 1 629 ? 139.415 118.048 96.109  1.00 44.58 ?  629 ALA A O     1 
ATOM   5060  C  CB    . ALA A 1 629 ? 137.163 120.274 96.124  1.00 35.14 ?  629 ALA A CB    1 
ATOM   5061  N  N     . TYR A 1 630 ? 137.441 117.001 96.355  1.00 42.65 ?  630 TYR A N     1 
ATOM   5062  C  CA    . TYR A 1 630 ? 138.047 115.911 97.111  1.00 41.94 ?  630 TYR A CA    1 
ATOM   5063  C  C     . TYR A 1 630 ? 138.836 114.967 96.214  1.00 44.19 ?  630 TYR A C     1 
ATOM   5064  O  O     . TYR A 1 630 ? 139.783 114.323 96.680  1.00 44.91 ?  630 TYR A O     1 
ATOM   5065  C  CB    . TYR A 1 630 ? 136.969 115.145 97.874  1.00 39.33 ?  630 TYR A CB    1 
ATOM   5066  C  CG    . TYR A 1 630 ? 136.210 115.995 98.863  1.00 40.78 ?  630 TYR A CG    1 
ATOM   5067  C  CD1   . TYR A 1 630 ? 136.771 116.340 100.083 1.00 38.92 ?  630 TYR A CD1   1 
ATOM   5068  C  CD2   . TYR A 1 630 ? 134.932 116.452 98.575  1.00 40.39 ?  630 TYR A CD2   1 
ATOM   5069  C  CE1   . TYR A 1 630 ? 136.081 117.114 100.990 1.00 39.65 ?  630 TYR A CE1   1 
ATOM   5070  C  CE2   . TYR A 1 630 ? 134.235 117.228 99.478  1.00 40.55 ?  630 TYR A CE2   1 
ATOM   5071  C  CZ    . TYR A 1 630 ? 134.815 117.555 100.684 1.00 44.72 ?  630 TYR A CZ    1 
ATOM   5072  O  OH    . TYR A 1 630 ? 134.125 118.328 101.588 1.00 48.31 ?  630 TYR A OH    1 
ATOM   5073  N  N     . ASP A 1 631 ? 138.473 114.873 94.937  1.00 40.74 ?  631 ASP A N     1 
ATOM   5074  C  CA    . ASP A 1 631 ? 139.132 113.947 94.026  1.00 39.43 ?  631 ASP A CA    1 
ATOM   5075  C  C     . ASP A 1 631 ? 140.400 114.513 93.400  1.00 43.72 ?  631 ASP A C     1 
ATOM   5076  O  O     . ASP A 1 631 ? 141.120 113.766 92.729  1.00 46.48 ?  631 ASP A O     1 
ATOM   5077  C  CB    . ASP A 1 631 ? 138.167 113.526 92.913  1.00 42.42 ?  631 ASP A CB    1 
ATOM   5078  C  CG    . ASP A 1 631 ? 136.817 113.092 93.445  1.00 49.41 ?  631 ASP A CG    1 
ATOM   5079  O  OD1   . ASP A 1 631 ? 136.777 112.411 94.490  1.00 48.62 ?  631 ASP A OD1   1 
ATOM   5080  O  OD2   . ASP A 1 631 ? 135.794 113.431 92.814  1.00 51.07 -1 631 ASP A OD2   1 
ATOM   5081  N  N     . MET A 1 632 ? 140.695 115.793 93.596  1.00 39.69 ?  632 MET A N     1 
ATOM   5082  C  CA    . MET A 1 632 ? 141.844 116.416 92.957  1.00 37.62 ?  632 MET A CA    1 
ATOM   5083  C  C     . MET A 1 632 ? 143.015 116.537 93.923  1.00 36.03 ?  632 MET A C     1 
ATOM   5084  O  O     . MET A 1 632 ? 142.862 116.468 95.145  1.00 38.98 ?  632 MET A O     1 
ATOM   5085  C  CB    . MET A 1 632 ? 141.485 117.795 92.401  1.00 37.51 ?  632 MET A CB    1 
ATOM   5086  C  CG    . MET A 1 632 ? 140.546 118.612 93.249  1.00 39.98 ?  632 MET A CG    1 
ATOM   5087  S  SD    . MET A 1 632 ? 140.284 120.248 92.544  1.00 47.46 ?  632 MET A SD    1 
ATOM   5088  C  CE    . MET A 1 632 ? 139.146 119.871 91.218  1.00 33.77 ?  632 MET A CE    1 
ATOM   5089  N  N     . ASP A 1 633 ? 144.200 116.723 93.347  1.00 34.02 ?  633 ASP A N     1 
ATOM   5090  C  CA    . ASP A 1 633 ? 145.419 116.880 94.128  1.00 30.19 ?  633 ASP A CA    1 
ATOM   5091  C  C     . ASP A 1 633 ? 145.414 118.233 94.828  1.00 28.33 ?  633 ASP A C     1 
ATOM   5092  O  O     . ASP A 1 633 ? 145.264 119.275 94.180  1.00 30.74 ?  633 ASP A O     1 
ATOM   5093  C  CB    . ASP A 1 633 ? 146.638 116.751 93.219  1.00 26.25 ?  633 ASP A CB    1 
ATOM   5094  C  CG    . ASP A 1 633 ? 147.931 116.581 93.990  1.00 38.00 ?  633 ASP A CG    1 
ATOM   5095  O  OD1   . ASP A 1 633 ? 147.880 116.466 95.233  1.00 39.38 ?  633 ASP A OD1   1 
ATOM   5096  O  OD2   . ASP A 1 633 ? 149.002 116.568 93.351  1.00 36.15 -1 633 ASP A OD2   1 
ATOM   5097  N  N     . MET A 1 634 ? 145.577 118.221 96.151  1.00 26.57 ?  634 MET A N     1 
ATOM   5098  C  CA    . MET A 1 634 ? 145.643 119.471 96.897  1.00 23.16 ?  634 MET A CA    1 
ATOM   5099  C  C     . MET A 1 634 ? 146.899 120.270 96.578  1.00 25.24 ?  634 MET A C     1 
ATOM   5100  O  O     . MET A 1 634 ? 146.921 121.479 96.817  1.00 26.06 ?  634 MET A O     1 
ATOM   5101  C  CB    . MET A 1 634 ? 145.562 119.202 98.399  1.00 23.97 ?  634 MET A CB    1 
ATOM   5102  C  CG    . MET A 1 634 ? 144.144 119.077 98.922  1.00 29.04 ?  634 MET A CG    1 
ATOM   5103  S  SD    . MET A 1 634 ? 143.127 120.501 98.487  1.00 38.84 ?  634 MET A SD    1 
ATOM   5104  C  CE    . MET A 1 634 ? 141.894 119.725 97.446  1.00 28.17 ?  634 MET A CE    1 
ATOM   5105  N  N     . PHE A 1 635 ? 147.940 119.627 96.045  1.00 24.58 ?  635 PHE A N     1 
ATOM   5106  C  CA    . PHE A 1 635 ? 149.116 120.373 95.613  1.00 21.50 ?  635 PHE A CA    1 
ATOM   5107  C  C     . PHE A 1 635 ? 148.789 121.274 94.428  1.00 21.21 ?  635 PHE A C     1 
ATOM   5108  O  O     . PHE A 1 635 ? 149.243 122.422 94.369  1.00 26.87 ?  635 PHE A O     1 
ATOM   5109  C  CB    . PHE A 1 635 ? 150.252 119.411 95.268  1.00 20.93 ?  635 PHE A CB    1 
ATOM   5110  C  CG    . PHE A 1 635 ? 151.117 119.051 96.442  1.00 27.72 ?  635 PHE A CG    1 
ATOM   5111  C  CD1   . PHE A 1 635 ? 150.560 118.841 97.692  1.00 22.95 ?  635 PHE A CD1   1 
ATOM   5112  C  CD2   . PHE A 1 635 ? 152.487 118.927 96.297  1.00 23.97 ?  635 PHE A CD2   1 
ATOM   5113  C  CE1   . PHE A 1 635 ? 151.353 118.514 98.772  1.00 23.47 ?  635 PHE A CE1   1 
ATOM   5114  C  CE2   . PHE A 1 635 ? 153.283 118.599 97.376  1.00 26.52 ?  635 PHE A CE2   1 
ATOM   5115  C  CZ    . PHE A 1 635 ? 152.714 118.391 98.614  1.00 24.17 ?  635 PHE A CZ    1 
ATOM   5116  N  N     . LYS A 1 636 ? 147.983 120.783 93.486  1.00 26.05 ?  636 LYS A N     1 
ATOM   5117  C  CA    . LYS A 1 636 ? 147.599 121.608 92.346  1.00 24.89 ?  636 LYS A CA    1 
ATOM   5118  C  C     . LYS A 1 636 ? 146.624 122.708 92.752  1.00 23.61 ?  636 LYS A C     1 
ATOM   5119  O  O     . LYS A 1 636 ? 146.669 123.812 92.197  1.00 31.09 ?  636 LYS A O     1 
ATOM   5120  C  CB    . LYS A 1 636 ? 147.004 120.730 91.247  1.00 27.32 ?  636 LYS A CB    1 
ATOM   5121  C  CG    . LYS A 1 636 ? 147.975 119.683 90.723  1.00 27.16 ?  636 LYS A CG    1 
ATOM   5122  C  CD    . LYS A 1 636 ? 148.017 119.661 89.208  1.00 30.50 ?  636 LYS A CD    1 
ATOM   5123  C  CE    . LYS A 1 636 ? 147.843 118.251 88.671  1.00 32.33 ?  636 LYS A CE    1 
ATOM   5124  N  NZ    . LYS A 1 636 ? 147.980 118.206 87.190  1.00 32.76 1  636 LYS A NZ    1 
ATOM   5125  N  N     . VAL A 1 637 ? 145.752 122.438 93.724  1.00 20.12 ?  637 VAL A N     1 
ATOM   5126  C  CA    . VAL A 1 637 ? 144.884 123.487 94.250  1.00 17.76 ?  637 VAL A CA    1 
ATOM   5127  C  C     . VAL A 1 637 ? 145.712 124.547 94.968  1.00 23.34 ?  637 VAL A C     1 
ATOM   5128  O  O     . VAL A 1 637 ? 145.427 125.747 94.873  1.00 26.50 ?  637 VAL A O     1 
ATOM   5129  C  CB    . VAL A 1 637 ? 143.809 122.880 95.169  1.00 21.56 ?  637 VAL A CB    1 
ATOM   5130  C  CG1   . VAL A 1 637 ? 142.842 123.953 95.641  1.00 23.10 ?  637 VAL A CG1   1 
ATOM   5131  C  CG2   . VAL A 1 637 ? 143.064 121.771 94.448  1.00 24.87 ?  637 VAL A CG2   1 
ATOM   5132  N  N     . VAL A 1 638 ? 146.748 124.124 95.697  1.00 26.37 ?  638 VAL A N     1 
ATOM   5133  C  CA    . VAL A 1 638 ? 147.662 125.073 96.323  1.00 21.65 ?  638 VAL A CA    1 
ATOM   5134  C  C     . VAL A 1 638 ? 148.360 125.908 95.260  1.00 18.06 ?  638 VAL A C     1 
ATOM   5135  O  O     . VAL A 1 638 ? 148.531 127.121 95.417  1.00 31.86 ?  638 VAL A O     1 
ATOM   5136  C  CB    . VAL A 1 638 ? 148.679 124.334 97.214  1.00 21.89 ?  638 VAL A CB    1 
ATOM   5137  C  CG1   . VAL A 1 638 ? 149.906 125.196 97.448  1.00 15.98 ?  638 VAL A CG1   1 
ATOM   5138  C  CG2   . VAL A 1 638 ? 148.048 123.940 98.534  1.00 22.01 ?  638 VAL A CG2   1 
ATOM   5139  N  N     . ASP A 1 639 ? 148.778 125.270 94.166  1.00 13.54 ?  639 ASP A N     1 
ATOM   5140  C  CA    . ASP A 1 639 ? 149.400 126.002 93.068  1.00 16.83 ?  639 ASP A CA    1 
ATOM   5141  C  C     . ASP A 1 639 ? 148.452 127.049 92.499  1.00 24.01 ?  639 ASP A C     1 
ATOM   5142  O  O     . ASP A 1 639 ? 148.856 128.186 92.235  1.00 29.17 ?  639 ASP A O     1 
ATOM   5143  C  CB    . ASP A 1 639 ? 149.835 125.027 91.974  1.00 15.86 ?  639 ASP A CB    1 
ATOM   5144  C  CG    . ASP A 1 639 ? 151.085 124.260 92.341  1.00 29.95 ?  639 ASP A CG    1 
ATOM   5145  O  OD1   . ASP A 1 639 ? 151.987 124.851 92.971  1.00 34.26 ?  639 ASP A OD1   1 
ATOM   5146  O  OD2   . ASP A 1 639 ? 151.168 123.060 92.004  1.00 34.71 -1 639 ASP A OD2   1 
ATOM   5147  N  N     . MET A 1 640 ? 147.182 126.686 92.318  1.00 23.60 ?  640 MET A N     1 
ATOM   5148  C  CA    . MET A 1 640 ? 146.204 127.632 91.789  1.00 21.42 ?  640 MET A CA    1 
ATOM   5149  C  C     . MET A 1 640 ? 145.986 128.801 92.744  1.00 22.11 ?  640 MET A C     1 
ATOM   5150  O  O     . MET A 1 640 ? 145.969 129.967 92.328  1.00 25.58 ?  640 MET A O     1 
ATOM   5151  C  CB    . MET A 1 640 ? 144.886 126.909 91.511  1.00 24.83 ?  640 MET A CB    1 
ATOM   5152  C  CG    . MET A 1 640 ? 143.696 127.829 91.321  1.00 24.53 ?  640 MET A CG    1 
ATOM   5153  S  SD    . MET A 1 640 ? 143.745 128.710 89.753  1.00 27.79 ?  640 MET A SD    1 
ATOM   5154  C  CE    . MET A 1 640 ? 142.721 127.651 88.744  1.00 26.13 ?  640 MET A CE    1 
ATOM   5155  N  N     . ILE A 1 641 ? 145.827 128.508 94.036  1.00 21.70 ?  641 ILE A N     1 
ATOM   5156  C  CA    . ILE A 1 641 ? 145.568 129.565 95.008  1.00 16.23 ?  641 ILE A CA    1 
ATOM   5157  C  C     . ILE A 1 641 ? 146.781 130.474 95.148  1.00 18.08 ?  641 ILE A C     1 
ATOM   5158  O  O     . ILE A 1 641 ? 146.645 131.689 95.322  1.00 25.78 ?  641 ILE A O     1 
ATOM   5159  C  CB    . ILE A 1 641 ? 145.140 128.959 96.357  1.00 24.77 ?  641 ILE A CB    1 
ATOM   5160  C  CG1   . ILE A 1 641 ? 143.875 128.118 96.188  1.00 23.13 ?  641 ILE A CG1   1 
ATOM   5161  C  CG2   . ILE A 1 641 ? 144.888 130.049 97.385  1.00 16.45 ?  641 ILE A CG2   1 
ATOM   5162  C  CD1   . ILE A 1 641 ? 142.776 128.814 95.422  1.00 19.77 ?  641 ILE A CD1   1 
ATOM   5163  N  N     . ALA A 1 642 ? 147.986 129.906 95.065  1.00 13.80 ?  642 ALA A N     1 
ATOM   5164  C  CA    . ALA A 1 642 ? 149.196 130.715 95.120  1.00 14.95 ?  642 ALA A CA    1 
ATOM   5165  C  C     . ALA A 1 642 ? 149.360 131.561 93.866  1.00 15.06 ?  642 ALA A C     1 
ATOM   5166  O  O     . ALA A 1 642 ? 149.885 132.677 93.939  1.00 24.85 ?  642 ALA A O     1 
ATOM   5167  C  CB    . ALA A 1 642 ? 150.415 129.819 95.322  1.00 16.20 ?  642 ALA A CB    1 
ATOM   5168  N  N     . THR A 1 643 ? 148.933 131.046 92.712  1.00 17.82 ?  643 THR A N     1 
ATOM   5169  C  CA    . THR A 1 643 ? 148.920 131.861 91.504  1.00 20.13 ?  643 THR A CA    1 
ATOM   5170  C  C     . THR A 1 643 ? 147.965 133.037 91.652  1.00 18.40 ?  643 THR A C     1 
ATOM   5171  O  O     . THR A 1 643 ? 148.290 134.166 91.269  1.00 22.42 ?  643 THR A O     1 
ATOM   5172  C  CB    . THR A 1 643 ? 148.540 131.004 90.298  1.00 22.01 ?  643 THR A CB    1 
ATOM   5173  O  OG1   . THR A 1 643 ? 149.552 130.014 90.079  1.00 28.71 ?  643 THR A OG1   1 
ATOM   5174  C  CG2   . THR A 1 643 ? 148.405 131.861 89.055  1.00 17.65 ?  643 THR A CG2   1 
ATOM   5175  N  N     . ILE A 1 644 ? 146.780 132.793 92.216  1.00 16.05 ?  644 ILE A N     1 
ATOM   5176  C  CA    . ILE A 1 644 ? 145.841 133.885 92.447  1.00 14.62 ?  644 ILE A CA    1 
ATOM   5177  C  C     . ILE A 1 644 ? 146.353 134.812 93.545  1.00 17.27 ?  644 ILE A C     1 
ATOM   5178  O  O     . ILE A 1 644 ? 146.206 136.037 93.457  1.00 22.60 ?  644 ILE A O     1 
ATOM   5179  C  CB    . ILE A 1 644 ? 144.445 133.330 92.780  1.00 15.77 ?  644 ILE A CB    1 
ATOM   5180  C  CG1   . ILE A 1 644 ? 143.920 132.473 91.629  1.00 14.71 ?  644 ILE A CG1   1 
ATOM   5181  C  CG2   . ILE A 1 644 ? 143.480 134.461 93.067  1.00 7.74  ?  644 ILE A CG2   1 
ATOM   5182  C  CD1   . ILE A 1 644 ? 142.745 131.606 92.010  1.00 22.09 ?  644 ILE A CD1   1 
ATOM   5183  N  N     . GLN A 1 645 ? 146.966 134.245 94.589  1.00 11.57 ?  645 GLN A N     1 
ATOM   5184  C  CA    . GLN A 1 645 ? 147.356 135.036 95.753  1.00 11.89 ?  645 GLN A CA    1 
ATOM   5185  C  C     . GLN A 1 645 ? 148.391 136.100 95.410  1.00 18.71 ?  645 GLN A C     1 
ATOM   5186  O  O     . GLN A 1 645 ? 148.447 137.143 96.071  1.00 23.96 ?  645 GLN A O     1 
ATOM   5187  C  CB    . GLN A 1 645 ? 147.889 134.117 96.853  1.00 8.94  ?  645 GLN A CB    1 
ATOM   5188  C  CG    . GLN A 1 645 ? 148.250 134.823 98.150  1.00 10.21 ?  645 GLN A CG    1 
ATOM   5189  C  CD    . GLN A 1 645 ? 147.050 135.447 98.828  1.00 12.21 ?  645 GLN A CD    1 
ATOM   5190  O  OE1   . GLN A 1 645 ? 146.336 134.786 99.578  1.00 18.33 ?  645 GLN A OE1   1 
ATOM   5191  N  NE2   . GLN A 1 645 ? 146.824 136.728 98.570  1.00 4.73  ?  645 GLN A NE2   1 
ATOM   5192  N  N     . GLN A 1 646 ? 149.208 135.869 94.384  1.00 20.94 ?  646 GLN A N     1 
ATOM   5193  C  CA    . GLN A 1 646 ? 150.241 136.836 94.040  1.00 14.79 ?  646 GLN A CA    1 
ATOM   5194  C  C     . GLN A 1 646 ? 149.676 138.141 93.496  1.00 15.69 ?  646 GLN A C     1 
ATOM   5195  O  O     . GLN A 1 646 ? 150.408 139.133 93.436  1.00 20.87 ?  646 GLN A O     1 
ATOM   5196  C  CB    . GLN A 1 646 ? 151.217 136.223 93.035  1.00 20.94 ?  646 GLN A CB    1 
ATOM   5197  C  CG    . GLN A 1 646 ? 150.750 136.258 91.598  1.00 22.21 ?  646 GLN A CG    1 
ATOM   5198  C  CD    . GLN A 1 646 ? 151.681 135.503 90.673  1.00 30.10 ?  646 GLN A CD    1 
ATOM   5199  O  OE1   . GLN A 1 646 ? 151.287 134.523 90.041  1.00 25.03 ?  646 GLN A OE1   1 
ATOM   5200  N  NE2   . GLN A 1 646 ? 152.926 135.954 90.590  1.00 26.74 ?  646 GLN A NE2   1 
ATOM   5201  N  N     . HIS A 1 647 ? 148.401 138.171 93.115  1.00 21.92 ?  647 HIS A N     1 
ATOM   5202  C  CA    . HIS A 1 647 ? 147.746 139.390 92.665  1.00 14.76 ?  647 HIS A CA    1 
ATOM   5203  C  C     . HIS A 1 647 ? 146.742 139.927 93.674  1.00 15.27 ?  647 HIS A C     1 
ATOM   5204  O  O     . HIS A 1 647 ? 146.087 140.937 93.399  1.00 25.12 ?  647 HIS A O     1 
ATOM   5205  C  CB    . HIS A 1 647 ? 147.048 139.147 91.323  1.00 11.36 ?  647 HIS A CB    1 
ATOM   5206  C  CG    . HIS A 1 647 ? 147.938 138.548 90.283  1.00 16.48 ?  647 HIS A CG    1 
ATOM   5207  N  ND1   . HIS A 1 647 ? 149.072 139.180 89.821  1.00 19.03 ?  647 HIS A ND1   1 
ATOM   5208  C  CD2   . HIS A 1 647 ? 147.865 137.374 89.615  1.00 17.59 ?  647 HIS A CD2   1 
ATOM   5209  C  CE1   . HIS A 1 647 ? 149.659 138.421 88.914  1.00 20.83 ?  647 HIS A CE1   1 
ATOM   5210  N  NE2   . HIS A 1 647 ? 148.945 137.319 88.769  1.00 20.71 ?  647 HIS A NE2   1 
ATOM   5211  N  N     . ILE A 1 648 ? 146.601 139.281 94.826  1.00 13.52 ?  648 ILE A N     1 
ATOM   5212  C  CA    . ILE A 1 648 ? 145.649 139.674 95.856  1.00 12.03 ?  648 ILE A CA    1 
ATOM   5213  C  C     . ILE A 1 648 ? 146.442 140.237 97.026  1.00 12.20 ?  648 ILE A C     1 
ATOM   5214  O  O     . ILE A 1 648 ? 147.336 139.565 97.556  1.00 25.66 ?  648 ILE A O     1 
ATOM   5215  C  CB    . ILE A 1 648 ? 144.772 138.490 96.292  1.00 10.19 ?  648 ILE A CB    1 
ATOM   5216  C  CG1   . ILE A 1 648 ? 144.040 137.889 95.090  1.00 11.20 ?  648 ILE A CG1   1 
ATOM   5217  C  CG2   . ILE A 1 648 ? 143.773 138.915 97.350  1.00 5.66  ?  648 ILE A CG2   1 
ATOM   5218  C  CD1   . ILE A 1 648 ? 142.938 138.764 94.542  1.00 5.31  ?  648 ILE A CD1   1 
ATOM   5219  N  N     . ASP A 1 649 ? 146.126 141.471 97.427  1.00 7.57  ?  649 ASP A N     1 
ATOM   5220  C  CA    . ASP A 1 649 ? 146.887 142.103 98.501  1.00 8.07  ?  649 ASP A CA    1 
ATOM   5221  C  C     . ASP A 1 649 ? 146.550 141.501 99.857  1.00 9.20  ?  649 ASP A C     1 
ATOM   5222  O  O     . ASP A 1 649 ? 147.431 141.375 100.714 1.00 27.02 ?  649 ASP A O     1 
ATOM   5223  C  CB    . ASP A 1 649 ? 146.642 143.612 98.512  1.00 18.44 ?  649 ASP A CB    1 
ATOM   5224  C  CG    . ASP A 1 649 ? 145.186 143.968 98.327  1.00 19.25 ?  649 ASP A CG    1 
ATOM   5225  O  OD1   . ASP A 1 649 ? 144.714 143.951 97.175  1.00 24.05 ?  649 ASP A OD1   1 
ATOM   5226  O  OD2   . ASP A 1 649 ? 144.514 144.274 99.332  1.00 20.27 -1 649 ASP A OD2   1 
ATOM   5227  N  N     . GLN A 1 650 ? 145.293 141.145 100.075 1.00 13.71 ?  650 GLN A N     1 
ATOM   5228  C  CA    . GLN A 1 650 ? 144.877 140.425 101.267 1.00 4.37  ?  650 GLN A CA    1 
ATOM   5229  C  C     . GLN A 1 650 ? 144.926 138.925 100.968 1.00 10.77 ?  650 GLN A C     1 
ATOM   5230  O  O     . GLN A 1 650 ? 145.525 138.499 99.979  1.00 20.19 ?  650 GLN A O     1 
ATOM   5231  C  CB    . GLN A 1 650 ? 143.502 140.920 101.716 1.00 6.40  ?  650 GLN A CB    1 
ATOM   5232  C  CG    . GLN A 1 650 ? 143.455 142.411 101.990 1.00 9.80  ?  650 GLN A CG    1 
ATOM   5233  C  CD    . GLN A 1 650 ? 142.127 142.856 102.555 1.00 13.56 ?  650 GLN A CD    1 
ATOM   5234  O  OE1   . GLN A 1 650 ? 141.797 142.553 103.698 1.00 15.64 ?  650 GLN A OE1   1 
ATOM   5235  N  NE2   . GLN A 1 650 ? 141.356 143.582 101.756 1.00 3.67  ?  650 GLN A NE2   1 
ATOM   5236  N  N     . GLY A 1 651 ? 144.331 138.104 101.830 1.00 9.85  ?  651 GLY A N     1 
ATOM   5237  C  CA    . GLY A 1 651 ? 144.384 136.668 101.680 1.00 5.75  ?  651 GLY A CA    1 
ATOM   5238  C  C     . GLY A 1 651 ? 143.196 136.094 100.925 1.00 5.51  ?  651 GLY A C     1 
ATOM   5239  O  O     . GLY A 1 651 ? 142.294 136.793 100.471 1.00 10.85 ?  651 GLY A O     1 
ATOM   5240  N  N     . ILE A 1 652 ? 143.224 134.772 100.794 1.00 13.76 ?  652 ILE A N     1 
ATOM   5241  C  CA    . ILE A 1 652 ? 142.183 133.999 100.132 1.00 2.10  ?  652 ILE A CA    1 
ATOM   5242  C  C     . ILE A 1 652 ? 141.735 132.910 101.093 1.00 12.29 ?  652 ILE A C     1 
ATOM   5243  O  O     . ILE A 1 652 ? 142.570 132.188 101.645 1.00 26.74 ?  652 ILE A O     1 
ATOM   5244  C  CB    . ILE A 1 652 ? 142.685 133.382 98.812  1.00 6.19  ?  652 ILE A CB    1 
ATOM   5245  C  CG1   . ILE A 1 652 ? 143.277 134.459 97.902  1.00 4.30  ?  652 ILE A CG1   1 
ATOM   5246  C  CG2   . ILE A 1 652 ? 141.568 132.634 98.111  1.00 11.90 ?  652 ILE A CG2   1 
ATOM   5247  C  CD1   . ILE A 1 652 ? 143.855 133.916 96.626  1.00 5.06  ?  652 ILE A CD1   1 
ATOM   5248  N  N     . SER A 1 653 ? 140.428 132.793 101.296 1.00 10.56 ?  653 SER A N     1 
ATOM   5249  C  CA    . SER A 1 653 ? 139.884 131.760 102.175 1.00 12.86 ?  653 SER A CA    1 
ATOM   5250  C  C     . SER A 1 653 ? 140.099 130.406 101.515 1.00 18.04 ?  653 SER A C     1 
ATOM   5251  O  O     . SER A 1 653 ? 139.330 129.996 100.647 1.00 20.45 ?  653 SER A O     1 
ATOM   5252  C  CB    . SER A 1 653 ? 138.407 132.013 102.447 1.00 13.46 ?  653 SER A CB    1 
ATOM   5253  O  OG    . SER A 1 653 ? 138.226 132.700 103.668 1.00 20.71 ?  653 SER A OG    1 
ATOM   5254  N  N     . PHE A 1 654 ? 141.139 129.700 101.942 1.00 22.22 ?  654 PHE A N     1 
ATOM   5255  C  CA    . PHE A 1 654 ? 141.610 128.491 101.277 1.00 10.48 ?  654 PHE A CA    1 
ATOM   5256  C  C     . PHE A 1 654 ? 141.200 127.278 102.103 1.00 13.54 ?  654 PHE A C     1 
ATOM   5257  O  O     . PHE A 1 654 ? 141.808 126.988 103.138 1.00 21.98 ?  654 PHE A O     1 
ATOM   5258  C  CB    . PHE A 1 654 ? 143.124 128.549 101.090 1.00 15.97 ?  654 PHE A CB    1 
ATOM   5259  C  CG    . PHE A 1 654 ? 143.687 127.418 100.284 1.00 16.96 ?  654 PHE A CG    1 
ATOM   5260  C  CD1   . PHE A 1 654 ? 142.872 126.634 99.488  1.00 18.84 ?  654 PHE A CD1   1 
ATOM   5261  C  CD2   . PHE A 1 654 ? 145.041 127.145 100.318 1.00 21.85 ?  654 PHE A CD2   1 
ATOM   5262  C  CE1   . PHE A 1 654 ? 143.395 125.599 98.750  1.00 18.09 ?  654 PHE A CE1   1 
ATOM   5263  C  CE2   . PHE A 1 654 ? 145.567 126.113 99.579  1.00 21.06 ?  654 PHE A CE2   1 
ATOM   5264  C  CZ    . PHE A 1 654 ? 144.744 125.338 98.794  1.00 19.78 ?  654 PHE A CZ    1 
ATOM   5265  N  N     . THR A 1 655 ? 140.184 126.563 101.633 1.00 22.24 ?  655 THR A N     1 
ATOM   5266  C  CA    . THR A 1 655 ? 139.730 125.338 102.274 1.00 23.33 ?  655 THR A CA    1 
ATOM   5267  C  C     . THR A 1 655 ? 140.492 124.147 101.709 1.00 26.54 ?  655 THR A C     1 
ATOM   5268  O  O     . THR A 1 655 ? 140.660 124.030 100.491 1.00 26.35 ?  655 THR A O     1 
ATOM   5269  C  CB    . THR A 1 655 ? 138.226 125.149 102.070 1.00 23.96 ?  655 THR A CB    1 
ATOM   5270  O  OG1   . THR A 1 655 ? 137.521 126.224 102.700 1.00 31.72 ?  655 THR A OG1   1 
ATOM   5271  C  CG2   . THR A 1 655 ? 137.766 123.833 102.671 1.00 26.42 ?  655 THR A CG2   1 
ATOM   5272  N  N     . LEU A 1 656 ? 140.958 123.271 102.594 1.00 29.51 ?  656 LEU A N     1 
ATOM   5273  C  CA    . LEU A 1 656 ? 141.613 122.036 102.189 1.00 29.05 ?  656 LEU A CA    1 
ATOM   5274  C  C     . LEU A 1 656 ? 140.596 120.906 102.165 1.00 28.32 ?  656 LEU A C     1 
ATOM   5275  O  O     . LEU A 1 656 ? 139.916 120.650 103.165 1.00 28.78 ?  656 LEU A O     1 
ATOM   5276  C  CB    . LEU A 1 656 ? 142.763 121.690 103.135 1.00 29.85 ?  656 LEU A CB    1 
ATOM   5277  C  CG    . LEU A 1 656 ? 143.963 122.633 103.109 1.00 32.35 ?  656 LEU A CG    1 
ATOM   5278  C  CD1   . LEU A 1 656 ? 145.109 122.049 103.914 1.00 29.79 ?  656 LEU A CD1   1 
ATOM   5279  C  CD2   . LEU A 1 656 ? 144.396 122.924 101.682 1.00 27.79 ?  656 LEU A CD2   1 
ATOM   5280  N  N     . PHE A 1 657 ? 140.498 120.231 101.028 1.00 27.28 ?  657 PHE A N     1 
ATOM   5281  C  CA    . PHE A 1 657 ? 139.530 119.163 100.823 1.00 27.17 ?  657 PHE A CA    1 
ATOM   5282  C  C     . PHE A 1 657 ? 140.266 117.832 100.894 1.00 34.16 ?  657 PHE A C     1 
ATOM   5283  O  O     . PHE A 1 657 ? 141.012 117.476 99.977  1.00 37.77 ?  657 PHE A O     1 
ATOM   5284  C  CB    . PHE A 1 657 ? 138.814 119.344 99.489  1.00 28.61 ?  657 PHE A CB    1 
ATOM   5285  C  CG    . PHE A 1 657 ? 138.186 120.696 99.329  1.00 33.56 ?  657 PHE A CG    1 
ATOM   5286  C  CD1   . PHE A 1 657 ? 136.907 120.940 99.795  1.00 30.41 ?  657 PHE A CD1   1 
ATOM   5287  C  CD2   . PHE A 1 657 ? 138.881 121.733 98.726  1.00 34.59 ?  657 PHE A CD2   1 
ATOM   5288  C  CE1   . PHE A 1 657 ? 136.328 122.183 99.653  1.00 33.52 ?  657 PHE A CE1   1 
ATOM   5289  C  CE2   . PHE A 1 657 ? 138.306 122.978 98.580  1.00 30.81 ?  657 PHE A CE2   1 
ATOM   5290  C  CZ    . PHE A 1 657 ? 137.029 123.203 99.047  1.00 32.22 ?  657 PHE A CZ    1 
ATOM   5291  N  N     . LEU A 1 658 ? 140.051 117.100 101.982 1.00 42.10 ?  658 LEU A N     1 
ATOM   5292  C  CA    . LEU A 1 658 ? 140.825 115.912 102.305 1.00 40.48 ?  658 LEU A CA    1 
ATOM   5293  C  C     . LEU A 1 658 ? 139.961 114.664 102.200 1.00 44.65 ?  658 LEU A C     1 
ATOM   5294  O  O     . LEU A 1 658 ? 138.783 114.677 102.565 1.00 48.50 ?  658 LEU A O     1 
ATOM   5295  C  CB    . LEU A 1 658 ? 141.403 116.016 103.718 1.00 38.92 ?  658 LEU A CB    1 
ATOM   5296  C  CG    . LEU A 1 658 ? 141.859 117.403 104.167 1.00 38.09 ?  658 LEU A CG    1 
ATOM   5297  C  CD1   . LEU A 1 658 ? 142.020 117.434 105.673 1.00 37.57 ?  658 LEU A CD1   1 
ATOM   5298  C  CD2   . LEU A 1 658 ? 143.157 117.789 103.480 1.00 39.85 ?  658 LEU A CD2   1 
ATOM   5299  N  N     . LYS A 1 659 ? 140.551 113.589 101.688 1.00 48.81 ?  659 LYS A N     1 
ATOM   5300  C  CA    . LYS A 1 659 ? 139.902 112.290 101.731 1.00 49.27 ?  659 LYS A CA    1 
ATOM   5301  C  C     . LYS A 1 659 ? 140.139 111.629 103.086 1.00 49.70 ?  659 LYS A C     1 
ATOM   5302  O  O     . LYS A 1 659 ? 141.021 112.021 103.854 1.00 53.26 ?  659 LYS A O     1 
ATOM   5303  C  CB    . LYS A 1 659 ? 140.415 111.388 100.609 1.00 50.47 ?  659 LYS A CB    1 
ATOM   5304  C  CG    . LYS A 1 659 ? 139.926 111.780 99.227  1.00 50.24 ?  659 LYS A CG    1 
ATOM   5305  C  CD    . LYS A 1 659 ? 140.290 110.724 98.198  1.00 50.40 ?  659 LYS A CD    1 
ATOM   5306  C  CE    . LYS A 1 659 ? 139.720 111.067 96.832  1.00 49.54 ?  659 LYS A CE    1 
ATOM   5307  N  NZ    . LYS A 1 659 ? 139.700 109.888 95.925  1.00 49.60 1  659 LYS A NZ    1 
ATOM   5308  N  N     . ASP A 1 660 ? 139.323 110.617 103.381 1.00 56.54 ?  660 ASP A N     1 
ATOM   5309  C  CA    . ASP A 1 660 ? 139.504 109.856 104.611 1.00 56.20 ?  660 ASP A CA    1 
ATOM   5310  C  C     . ASP A 1 660 ? 140.789 109.040 104.603 1.00 56.75 ?  660 ASP A C     1 
ATOM   5311  O  O     . ASP A 1 660 ? 141.338 108.760 105.673 1.00 56.19 ?  660 ASP A O     1 
ATOM   5312  C  CB    . ASP A 1 660 ? 138.306 108.934 104.840 1.00 57.79 ?  660 ASP A CB    1 
ATOM   5313  C  CG    . ASP A 1 660 ? 137.333 109.484 105.862 1.00 58.39 ?  660 ASP A CG    1 
ATOM   5314  O  OD1   . ASP A 1 660 ? 136.274 108.858 106.076 1.00 57.17 ?  660 ASP A OD1   1 
ATOM   5315  O  OD2   . ASP A 1 660 ? 137.629 110.540 106.457 1.00 56.44 -1 660 ASP A OD2   1 
ATOM   5316  N  N     . THR A 1 661 ? 141.279 108.659 103.421 1.00 54.72 ?  661 THR A N     1 
ATOM   5317  C  CA    . THR A 1 661 ? 142.443 107.784 103.341 1.00 54.28 ?  661 THR A CA    1 
ATOM   5318  C  C     . THR A 1 661 ? 143.724 108.482 103.783 1.00 54.79 ?  661 THR A C     1 
ATOM   5319  O  O     . THR A 1 661 ? 144.599 107.841 104.377 1.00 57.02 ?  661 THR A O     1 
ATOM   5320  C  CB    . THR A 1 661 ? 142.604 107.255 101.916 1.00 55.29 ?  661 THR A CB    1 
ATOM   5321  O  OG1   . THR A 1 661 ? 142.232 108.277 100.982 1.00 55.34 ?  661 THR A OG1   1 
ATOM   5322  C  CG2   . THR A 1 661 ? 141.723 106.035 101.702 1.00 54.88 ?  661 THR A CG2   1 
ATOM   5323  N  N     . MET A 1 662 ? 143.861 109.775 103.507 1.00 53.00 ?  662 MET A N     1 
ATOM   5324  C  CA    . MET A 1 662 ? 145.108 110.472 103.787 1.00 52.79 ?  662 MET A CA    1 
ATOM   5325  C  C     . MET A 1 662 ? 145.284 110.691 105.285 1.00 51.88 ?  662 MET A C     1 
ATOM   5326  O  O     . MET A 1 662 ? 144.319 110.939 106.014 1.00 52.12 ?  662 MET A O     1 
ATOM   5327  C  CB    . MET A 1 662 ? 145.161 111.808 103.045 1.00 51.51 ?  662 MET A CB    1 
ATOM   5328  C  CG    . MET A 1 662 ? 144.070 112.794 103.408 1.00 52.69 ?  662 MET A CG    1 
ATOM   5329  S  SD    . MET A 1 662 ? 144.188 114.318 102.449 1.00 60.26 ?  662 MET A SD    1 
ATOM   5330  C  CE    . MET A 1 662 ? 145.037 113.746 100.980 1.00 49.12 ?  662 MET A CE    1 
ATOM   5331  N  N     . THR A 1 663 ? 146.530 110.591 105.739 1.00 44.50 ?  663 THR A N     1 
ATOM   5332  C  CA    . THR A 1 663 ? 146.860 110.655 107.153 1.00 43.95 ?  663 THR A CA    1 
ATOM   5333  C  C     . THR A 1 663 ? 147.108 112.105 107.566 1.00 45.06 ?  663 THR A C     1 
ATOM   5334  O  O     . THR A 1 663 ? 146.886 113.041 106.795 1.00 48.51 ?  663 THR A O     1 
ATOM   5335  C  CB    . THR A 1 663 ? 148.075 109.777 107.447 1.00 43.10 ?  663 THR A CB    1 
ATOM   5336  O  OG1   . THR A 1 663 ? 149.252 110.403 106.920 1.00 41.26 ?  663 THR A OG1   1 
ATOM   5337  C  CG2   . THR A 1 663 ? 147.911 108.415 106.796 1.00 44.67 ?  663 THR A CG2   1 
ATOM   5338  N  N     . THR A 1 664 ? 147.569 112.304 108.803 1.00 39.46 ?  664 THR A N     1 
ATOM   5339  C  CA    . THR A 1 664 ? 147.958 113.645 109.228 1.00 41.82 ?  664 THR A CA    1 
ATOM   5340  C  C     . THR A 1 664 ? 149.238 114.093 108.537 1.00 40.57 ?  664 THR A C     1 
ATOM   5341  O  O     . THR A 1 664 ? 149.473 115.298 108.396 1.00 42.64 ?  664 THR A O     1 
ATOM   5342  C  CB    . THR A 1 664 ? 148.132 113.700 110.745 1.00 41.38 ?  664 THR A CB    1 
ATOM   5343  O  OG1   . THR A 1 664 ? 149.185 112.813 111.142 1.00 40.03 ?  664 THR A OG1   1 
ATOM   5344  C  CG2   . THR A 1 664 ? 146.844 113.304 111.448 1.00 39.88 ?  664 THR A CG2   1 
ATOM   5345  N  N     . ARG A 1 665 ? 150.073 113.145 108.109 1.00 39.85 ?  665 ARG A N     1 
ATOM   5346  C  CA    . ARG A 1 665 ? 151.278 113.503 107.369 1.00 38.49 ?  665 ARG A CA    1 
ATOM   5347  C  C     . ARG A 1 665 ? 150.932 114.154 106.038 1.00 41.53 ?  665 ARG A C     1 
ATOM   5348  O  O     . ARG A 1 665 ? 151.609 115.089 105.606 1.00 42.68 ?  665 ARG A O     1 
ATOM   5349  C  CB    . ARG A 1 665 ? 152.150 112.271 107.143 1.00 39.32 ?  665 ARG A CB    1 
ATOM   5350  C  CG    . ARG A 1 665 ? 153.434 112.567 106.391 1.00 37.71 ?  665 ARG A CG    1 
ATOM   5351  C  CD    . ARG A 1 665 ? 154.341 111.355 106.335 1.00 39.18 ?  665 ARG A CD    1 
ATOM   5352  N  NE    . ARG A 1 665 ? 155.406 111.516 105.354 1.00 41.76 ?  665 ARG A NE    1 
ATOM   5353  C  CZ    . ARG A 1 665 ? 155.242 111.420 104.041 1.00 45.20 ?  665 ARG A CZ    1 
ATOM   5354  N  NH1   . ARG A 1 665 ? 154.059 111.154 103.511 1.00 43.53 1  665 ARG A NH1   1 
ATOM   5355  N  NH2   . ARG A 1 665 ? 156.290 111.593 103.241 1.00 42.18 ?  665 ARG A NH2   1 
ATOM   5356  N  N     . ASP A 1 666 ? 149.887 113.667 105.367 1.00 38.83 ?  666 ASP A N     1 
ATOM   5357  C  CA    . ASP A 1 666 ? 149.478 114.277 104.106 1.00 35.10 ?  666 ASP A CA    1 
ATOM   5358  C  C     . ASP A 1 666 ? 148.959 115.694 104.318 1.00 37.66 ?  666 ASP A C     1 
ATOM   5359  O  O     . ASP A 1 666 ? 149.255 116.596 103.526 1.00 40.48 ?  666 ASP A O     1 
ATOM   5360  C  CB    . ASP A 1 666 ? 148.423 113.409 103.423 1.00 40.83 ?  666 ASP A CB    1 
ATOM   5361  C  CG    . ASP A 1 666 ? 148.961 112.049 103.026 1.00 45.35 ?  666 ASP A CG    1 
ATOM   5362  O  OD1   . ASP A 1 666 ? 150.058 111.993 102.432 1.00 45.48 ?  666 ASP A OD1   1 
ATOM   5363  O  OD2   . ASP A 1 666 ? 148.288 111.036 103.308 1.00 45.22 -1 666 ASP A OD2   1 
ATOM   5364  N  N     . LEU A 1 667 ? 148.183 115.910 105.382 1.00 36.21 ?  667 LEU A N     1 
ATOM   5365  C  CA    . LEU A 1 667 ? 147.715 117.256 105.696 1.00 31.15 ?  667 LEU A CA    1 
ATOM   5366  C  C     . LEU A 1 667 ? 148.888 118.175 106.015 1.00 29.82 ?  667 LEU A C     1 
ATOM   5367  O  O     . LEU A 1 667 ? 148.924 119.331 105.575 1.00 34.82 ?  667 LEU A O     1 
ATOM   5368  C  CB    . LEU A 1 667 ? 146.727 117.194 106.863 1.00 34.82 ?  667 LEU A CB    1 
ATOM   5369  C  CG    . LEU A 1 667 ? 146.093 118.452 107.466 1.00 36.50 ?  667 LEU A CG    1 
ATOM   5370  C  CD1   . LEU A 1 667 ? 145.879 119.544 106.429 1.00 35.38 ?  667 LEU A CD1   1 
ATOM   5371  C  CD2   . LEU A 1 667 ? 144.782 118.099 108.144 1.00 32.66 ?  667 LEU A CD2   1 
ATOM   5372  N  N     . ASN A 1 668 ? 149.867 117.671 106.768 1.00 32.07 ?  668 ASN A N     1 
ATOM   5373  C  CA    . ASN A 1 668 ? 151.053 118.465 107.074 1.00 26.94 ?  668 ASN A CA    1 
ATOM   5374  C  C     . ASN A 1 668 ? 151.847 118.780 105.813 1.00 26.92 ?  668 ASN A C     1 
ATOM   5375  O  O     . ASN A 1 668 ? 152.381 119.883 105.669 1.00 33.03 ?  668 ASN A O     1 
ATOM   5376  C  CB    . ASN A 1 668 ? 151.925 117.729 108.090 1.00 27.90 ?  668 ASN A CB    1 
ATOM   5377  C  CG    . ASN A 1 668 ? 151.644 118.158 109.513 1.00 30.77 ?  668 ASN A CG    1 
ATOM   5378  O  OD1   . ASN A 1 668 ? 151.132 119.248 109.755 1.00 31.97 ?  668 ASN A OD1   1 
ATOM   5379  N  ND2   . ASN A 1 668 ? 151.969 117.294 110.465 1.00 37.76 ?  668 ASN A ND2   1 
ATOM   5380  N  N     . ARG A 1 669 ? 151.946 117.819 104.894 1.00 30.35 ?  669 ARG A N     1 
ATOM   5381  C  CA    . ARG A 1 669 ? 152.634 118.061 103.631 1.00 31.14 ?  669 ARG A CA    1 
ATOM   5382  C  C     . ARG A 1 669 ? 151.919 119.124 102.811 1.00 27.39 ?  669 ARG A C     1 
ATOM   5383  O  O     . ARG A 1 669 ? 152.564 119.975 102.192 1.00 31.90 ?  669 ARG A O     1 
ATOM   5384  C  CB    . ARG A 1 669 ? 152.748 116.762 102.835 1.00 29.28 ?  669 ARG A CB    1 
ATOM   5385  C  CG    . ARG A 1 669 ? 153.854 115.839 103.298 1.00 31.02 ?  669 ARG A CG    1 
ATOM   5386  C  CD    . ARG A 1 669 ? 154.307 114.934 102.168 1.00 34.56 ?  669 ARG A CD    1 
ATOM   5387  N  NE    . ARG A 1 669 ? 155.208 115.615 101.248 1.00 33.91 ?  669 ARG A NE    1 
ATOM   5388  C  CZ    . ARG A 1 669 ? 155.108 115.566 99.927  1.00 33.75 ?  669 ARG A CZ    1 
ATOM   5389  N  NH1   . ARG A 1 669 ? 154.148 114.877 99.332  1.00 34.67 1  669 ARG A NH1   1 
ATOM   5390  N  NH2   . ARG A 1 669 ? 155.992 116.225 99.183  1.00 33.28 ?  669 ARG A NH2   1 
ATOM   5391  N  N     . ILE A 1 670 ? 150.586 119.086 102.788 1.00 23.06 ?  670 ILE A N     1 
ATOM   5392  C  CA    . ILE A 1 670 ? 149.831 120.118 102.082 1.00 27.95 ?  670 ILE A CA    1 
ATOM   5393  C  C     . ILE A 1 670 ? 150.075 121.481 102.716 1.00 30.84 ?  670 ILE A C     1 
ATOM   5394  O  O     . ILE A 1 670 ? 150.268 122.480 102.016 1.00 29.03 ?  670 ILE A O     1 
ATOM   5395  C  CB    . ILE A 1 670 ? 148.332 119.766 102.049 1.00 28.07 ?  670 ILE A CB    1 
ATOM   5396  C  CG1   . ILE A 1 670 ? 148.099 118.488 101.245 1.00 30.56 ?  670 ILE A CG1   1 
ATOM   5397  C  CG2   . ILE A 1 670 ? 147.531 120.906 101.446 1.00 27.64 ?  670 ILE A CG2   1 
ATOM   5398  C  CD1   . ILE A 1 670 ? 146.805 117.788 101.577 1.00 29.61 ?  670 ILE A CD1   1 
ATOM   5399  N  N     . ASP A 1 671 ? 150.079 121.542 104.051 1.00 28.70 ?  671 ASP A N     1 
ATOM   5400  C  CA    . ASP A 1 671 ? 150.333 122.807 104.737 1.00 22.91 ?  671 ASP A CA    1 
ATOM   5401  C  C     . ASP A 1 671 ? 151.733 123.335 104.437 1.00 23.48 ?  671 ASP A C     1 
ATOM   5402  O  O     . ASP A 1 671 ? 151.918 124.535 104.204 1.00 25.79 ?  671 ASP A O     1 
ATOM   5403  C  CB    . ASP A 1 671 ? 150.139 122.636 106.243 1.00 26.10 ?  671 ASP A CB    1 
ATOM   5404  C  CG    . ASP A 1 671 ? 148.727 122.223 106.609 1.00 37.56 ?  671 ASP A CG    1 
ATOM   5405  O  OD1   . ASP A 1 671 ? 147.792 122.565 105.857 1.00 36.26 ?  671 ASP A OD1   1 
ATOM   5406  O  OD2   . ASP A 1 671 ? 148.553 121.554 107.650 1.00 37.09 -1 671 ASP A OD2   1 
ATOM   5407  N  N     . LEU A 1 672 ? 152.730 122.451 104.432 1.00 25.36 ?  672 LEU A N     1 
ATOM   5408  C  CA    . LEU A 1 672 ? 154.101 122.874 104.170 1.00 19.20 ?  672 LEU A CA    1 
ATOM   5409  C  C     . LEU A 1 672 ? 154.301 123.278 102.716 1.00 19.80 ?  672 LEU A C     1 
ATOM   5410  O  O     . LEU A 1 672 ? 155.088 124.185 102.431 1.00 25.70 ?  672 LEU A O     1 
ATOM   5411  C  CB    . LEU A 1 672 ? 155.074 121.761 104.552 1.00 22.76 ?  672 LEU A CB    1 
ATOM   5412  C  CG    . LEU A 1 672 ? 155.182 121.472 106.049 1.00 23.94 ?  672 LEU A CG    1 
ATOM   5413  C  CD1   . LEU A 1 672 ? 155.836 120.121 106.292 1.00 19.57 ?  672 LEU A CD1   1 
ATOM   5414  C  CD2   . LEU A 1 672 ? 155.944 122.581 106.754 1.00 21.82 ?  672 LEU A CD2   1 
ATOM   5415  N  N     . TYR A 1 673 ? 153.606 122.623 101.786 1.00 21.30 ?  673 TYR A N     1 
ATOM   5416  C  CA    . TYR A 1 673 ? 153.678 123.028 100.388 1.00 18.93 ?  673 TYR A CA    1 
ATOM   5417  C  C     . TYR A 1 673 ? 152.974 124.360 100.169 1.00 21.16 ?  673 TYR A C     1 
ATOM   5418  O  O     . TYR A 1 673 ? 153.416 125.177 99.355  1.00 24.42 ?  673 TYR A O     1 
ATOM   5419  C  CB    . TYR A 1 673 ? 153.075 121.943 99.499  1.00 14.92 ?  673 TYR A CB    1 
ATOM   5420  C  CG    . TYR A 1 673 ? 153.165 122.242 98.023  1.00 19.19 ?  673 TYR A CG    1 
ATOM   5421  C  CD1   . TYR A 1 673 ? 154.395 122.349 97.392  1.00 18.76 ?  673 TYR A CD1   1 
ATOM   5422  C  CD2   . TYR A 1 673 ? 152.021 122.411 97.258  1.00 18.36 ?  673 TYR A CD2   1 
ATOM   5423  C  CE1   . TYR A 1 673 ? 154.482 122.620 96.045  1.00 23.48 ?  673 TYR A CE1   1 
ATOM   5424  C  CE2   . TYR A 1 673 ? 152.099 122.681 95.911  1.00 21.21 ?  673 TYR A CE2   1 
ATOM   5425  C  CZ    . TYR A 1 673 ? 153.331 122.784 95.309  1.00 25.20 ?  673 TYR A CZ    1 
ATOM   5426  O  OH    . TYR A 1 673 ? 153.416 123.053 93.964  1.00 24.69 ?  673 TYR A OH    1 
ATOM   5427  N  N     . ALA A 1 674 ? 151.869 124.590 100.880 1.00 23.17 ?  674 ALA A N     1 
ATOM   5428  C  CA    . ALA A 1 674 ? 151.210 125.888 100.828 1.00 16.78 ?  674 ALA A CA    1 
ATOM   5429  C  C     . ALA A 1 674 ? 152.118 126.984 101.368 1.00 17.23 ?  674 ALA A C     1 
ATOM   5430  O  O     . ALA A 1 674 ? 152.216 128.066 100.780 1.00 25.24 ?  674 ALA A O     1 
ATOM   5431  C  CB    . ALA A 1 674 ? 149.899 125.836 101.611 1.00 12.27 ?  674 ALA A CB    1 
ATOM   5432  N  N     . HIS A 1 675 ? 152.804 126.715 102.480 1.00 15.67 ?  675 HIS A N     1 
ATOM   5433  C  CA    . HIS A 1 675 ? 153.760 127.683 103.008 1.00 19.64 ?  675 HIS A CA    1 
ATOM   5434  C  C     . HIS A 1 675 ? 154.901 127.922 102.026 1.00 19.45 ?  675 HIS A C     1 
ATOM   5435  O  O     . HIS A 1 675 ? 155.356 129.058 101.855 1.00 24.55 ?  675 HIS A O     1 
ATOM   5436  C  CB    . HIS A 1 675 ? 154.301 127.205 104.353 1.00 18.08 ?  675 HIS A CB    1 
ATOM   5437  C  CG    . HIS A 1 675 ? 155.437 128.030 104.870 1.00 20.55 ?  675 HIS A CG    1 
ATOM   5438  N  ND1   . HIS A 1 675 ? 156.754 127.649 104.735 1.00 28.37 ?  675 HIS A ND1   1 
ATOM   5439  C  CD2   . HIS A 1 675 ? 155.454 129.218 105.517 1.00 18.60 ?  675 HIS A CD2   1 
ATOM   5440  C  CE1   . HIS A 1 675 ? 157.533 128.567 105.280 1.00 23.86 ?  675 HIS A CE1   1 
ATOM   5441  N  NE2   . HIS A 1 675 ? 156.768 129.529 105.761 1.00 24.59 ?  675 HIS A NE2   1 
ATOM   5442  N  N     . HIS A 1 676 ? 155.380 126.859 101.378 1.00 22.03 ?  676 HIS A N     1 
ATOM   5443  C  CA    . HIS A 1 676 ? 156.461 126.995 100.407 1.00 19.91 ?  676 HIS A CA    1 
ATOM   5444  C  C     . HIS A 1 676 ? 156.024 127.802 99.193  1.00 25.51 ?  676 HIS A C     1 
ATOM   5445  O  O     . HIS A 1 676 ? 156.808 128.581 98.640  1.00 25.79 ?  676 HIS A O     1 
ATOM   5446  C  CB    . HIS A 1 676 ? 156.950 125.611 99.981  1.00 23.94 ?  676 HIS A CB    1 
ATOM   5447  C  CG    . HIS A 1 676 ? 157.872 125.631 98.801  1.00 24.67 ?  676 HIS A CG    1 
ATOM   5448  N  ND1   . HIS A 1 676 ? 159.185 126.035 98.890  1.00 22.61 ?  676 HIS A ND1   1 
ATOM   5449  C  CD2   . HIS A 1 676 ? 157.667 125.297 97.506  1.00 25.58 ?  676 HIS A CD2   1 
ATOM   5450  C  CE1   . HIS A 1 676 ? 159.751 125.949 97.700  1.00 29.10 ?  676 HIS A CE1   1 
ATOM   5451  N  NE2   . HIS A 1 676 ? 158.851 125.504 96.842  1.00 27.74 ?  676 HIS A NE2   1 
ATOM   5452  N  N     . ARG A 1 677 ? 154.777 127.631 98.763  1.00 23.74 ?  677 ARG A N     1 
ATOM   5453  C  CA    . ARG A 1 677 ? 154.285 128.257 97.544  1.00 19.41 ?  677 ARG A CA    1 
ATOM   5454  C  C     . ARG A 1 677 ? 153.765 129.671 97.764  1.00 20.49 ?  677 ARG A C     1 
ATOM   5455  O  O     . ARG A 1 677 ? 153.264 130.284 96.816  1.00 27.52 ?  677 ARG A O     1 
ATOM   5456  C  CB    . ARG A 1 677 ? 153.184 127.396 96.918  1.00 22.31 ?  677 ARG A CB    1 
ATOM   5457  C  CG    . ARG A 1 677 ? 153.708 126.256 96.062  1.00 22.58 ?  677 ARG A CG    1 
ATOM   5458  C  CD    . ARG A 1 677 ? 154.293 126.768 94.757  1.00 18.82 ?  677 ARG A CD    1 
ATOM   5459  N  NE    . ARG A 1 677 ? 153.272 126.940 93.731  1.00 26.67 ?  677 ARG A NE    1 
ATOM   5460  C  CZ    . ARG A 1 677 ? 152.972 128.098 93.158  1.00 31.68 ?  677 ARG A CZ    1 
ATOM   5461  N  NH1   . ARG A 1 677 ? 153.600 129.216 93.486  1.00 29.78 1  677 ARG A NH1   1 
ATOM   5462  N  NH2   . ARG A 1 677 ? 152.017 128.136 92.232  1.00 25.25 ?  677 ARG A NH2   1 
ATOM   5463  N  N     . GLY A 1 678 ? 153.871 130.203 98.976  1.00 18.80 ?  678 GLY A N     1 
ATOM   5464  C  CA    . GLY A 1 678 ? 153.436 131.557 99.245  1.00 11.84 ?  678 GLY A CA    1 
ATOM   5465  C  C     . GLY A 1 678 ? 151.995 131.705 99.665  1.00 17.48 ?  678 GLY A C     1 
ATOM   5466  O  O     . GLY A 1 678 ? 151.457 132.815 99.591  1.00 21.36 ?  678 GLY A O     1 
ATOM   5467  N  N     . ILE A 1 679 ? 151.345 130.625 100.097 1.00 18.57 ?  679 ILE A N     1 
ATOM   5468  C  CA    . ILE A 1 679 ? 149.977 130.721 100.588 1.00 11.37 ?  679 ILE A CA    1 
ATOM   5469  C  C     . ILE A 1 679 ? 149.972 131.499 101.894 1.00 13.32 ?  679 ILE A C     1 
ATOM   5470  O  O     . ILE A 1 679 ? 150.764 131.225 102.804 1.00 29.23 ?  679 ILE A O     1 
ATOM   5471  C  CB    . ILE A 1 679 ? 149.364 129.324 100.763 1.00 16.02 ?  679 ILE A CB    1 
ATOM   5472  C  CG1   . ILE A 1 679 ? 149.166 128.657 99.402  1.00 13.20 ?  679 ILE A CG1   1 
ATOM   5473  C  CG2   . ILE A 1 679 ? 148.055 129.397 101.528 1.00 14.77 ?  679 ILE A CG2   1 
ATOM   5474  C  CD1   . ILE A 1 679 ? 148.278 129.427 98.478  1.00 13.30 ?  679 ILE A CD1   1 
ATOM   5475  N  N     . LYS A 1 680 ? 149.080 132.484 101.990 1.00 9.75  ?  680 LYS A N     1 
ATOM   5476  C  CA    . LYS A 1 680 ? 149.052 133.347 103.164 1.00 6.25  ?  680 LYS A CA    1 
ATOM   5477  C  C     . LYS A 1 680 ? 148.274 132.709 104.309 1.00 5.30  ?  680 LYS A C     1 
ATOM   5478  O  O     . LYS A 1 680 ? 148.732 132.714 105.455 1.00 17.26 ?  680 LYS A O     1 
ATOM   5479  C  CB    . LYS A 1 680 ? 148.453 134.703 102.794 1.00 8.74  ?  680 LYS A CB    1 
ATOM   5480  C  CG    . LYS A 1 680 ? 149.306 135.522 101.845 1.00 0.00  ?  680 LYS A CG    1 
ATOM   5481  C  CD    . LYS A 1 680 ? 148.721 136.906 101.659 1.00 5.72  ?  680 LYS A CD    1 
ATOM   5482  C  CE    . LYS A 1 680 ? 149.441 137.670 100.573 1.00 9.99  ?  680 LYS A CE    1 
ATOM   5483  N  NZ    . LYS A 1 680 ? 148.900 139.043 100.425 1.00 15.99 1  680 LYS A NZ    1 
ATOM   5484  N  N     . THR A 1 681 ? 147.098 132.158 104.020 1.00 10.68 ?  681 THR A N     1 
ATOM   5485  C  CA    . THR A 1 681 ? 146.251 131.557 105.037 1.00 8.05  ?  681 THR A CA    1 
ATOM   5486  C  C     . THR A 1 681 ? 145.643 130.269 104.504 1.00 14.02 ?  681 THR A C     1 
ATOM   5487  O  O     . THR A 1 681 ? 145.442 130.111 103.299 1.00 25.07 ?  681 THR A O     1 
ATOM   5488  C  CB    . THR A 1 681 ? 145.122 132.506 105.482 1.00 14.36 ?  681 THR A CB    1 
ATOM   5489  O  OG1   . THR A 1 681 ? 144.473 133.059 104.331 1.00 21.48 ?  681 THR A OG1   1 
ATOM   5490  C  CG2   . THR A 1 681 ? 145.666 133.636 106.341 1.00 11.98 ?  681 THR A CG2   1 
ATOM   5491  N  N     . ILE A 1 682 ? 145.349 129.350 105.420 1.00 10.50 ?  682 ILE A N     1 
ATOM   5492  C  CA    . ILE A 1 682 ? 144.604 128.134 105.122 1.00 11.42 ?  682 ILE A CA    1 
ATOM   5493  C  C     . ILE A 1 682 ? 143.349 128.136 105.980 1.00 14.42 ?  682 ILE A C     1 
ATOM   5494  O  O     . ILE A 1 682 ? 143.432 128.237 107.208 1.00 15.39 ?  682 ILE A O     1 
ATOM   5495  C  CB    . ILE A 1 682 ? 145.440 126.867 105.377 1.00 16.27 ?  682 ILE A CB    1 
ATOM   5496  C  CG1   . ILE A 1 682 ? 146.806 126.978 104.702 1.00 17.97 ?  682 ILE A CG1   1 
ATOM   5497  C  CG2   . ILE A 1 682 ? 144.707 125.650 104.874 1.00 19.16 ?  682 ILE A CG2   1 
ATOM   5498  C  CD1   . ILE A 1 682 ? 147.667 125.752 104.868 1.00 19.40 ?  682 ILE A CD1   1 
ATOM   5499  N  N     . TYR A 1 683 ? 142.187 128.031 105.334 1.00 16.60 ?  683 TYR A N     1 
ATOM   5500  C  CA    . TYR A 1 683 ? 140.923 128.230 106.045 1.00 11.86 ?  683 TYR A CA    1 
ATOM   5501  C  C     . TYR A 1 683 ? 140.461 126.965 106.763 1.00 23.72 ?  683 TYR A C     1 
ATOM   5502  O  O     . TYR A 1 683 ? 140.427 126.913 107.994 1.00 33.70 ?  683 TYR A O     1 
ATOM   5503  C  CB    . TYR A 1 683 ? 139.852 128.713 105.061 1.00 18.22 ?  683 TYR A CB    1 
ATOM   5504  C  CG    . TYR A 1 683 ? 138.548 129.113 105.706 1.00 15.29 ?  683 TYR A CG    1 
ATOM   5505  C  CD1   . TYR A 1 683 ? 138.504 129.539 107.025 1.00 15.83 ?  683 TYR A CD1   1 
ATOM   5506  C  CD2   . TYR A 1 683 ? 137.359 129.076 104.990 1.00 13.23 ?  683 TYR A CD2   1 
ATOM   5507  C  CE1   . TYR A 1 683 ? 137.319 129.905 107.616 1.00 19.36 ?  683 TYR A CE1   1 
ATOM   5508  C  CE2   . TYR A 1 683 ? 136.166 129.446 105.574 1.00 18.00 ?  683 TYR A CE2   1 
ATOM   5509  C  CZ    . TYR A 1 683 ? 136.153 129.860 106.887 1.00 20.89 ?  683 TYR A CZ    1 
ATOM   5510  O  OH    . TYR A 1 683 ? 134.968 130.229 107.479 1.00 28.35 ?  683 TYR A OH    1 
ATOM   5511  N  N     . TYR A 1 684 ? 140.128 125.927 106.012 1.00 31.22 ?  684 TYR A N     1 
ATOM   5512  C  CA    . TYR A 1 684 ? 139.466 124.768 106.584 1.00 24.27 ?  684 TYR A CA    1 
ATOM   5513  C  C     . TYR A 1 684 ? 140.088 123.493 106.051 1.00 33.98 ?  684 TYR A C     1 
ATOM   5514  O  O     . TYR A 1 684 ? 140.576 123.443 104.919 1.00 35.72 ?  684 TYR A O     1 
ATOM   5515  C  CB    . TYR A 1 684 ? 137.964 124.771 106.278 1.00 27.98 ?  684 TYR A CB    1 
ATOM   5516  C  CG    . TYR A 1 684 ? 137.118 125.374 107.372 1.00 25.86 ?  684 TYR A CG    1 
ATOM   5517  C  CD1   . TYR A 1 684 ? 137.372 125.093 108.706 1.00 28.64 ?  684 TYR A CD1   1 
ATOM   5518  C  CD2   . TYR A 1 684 ? 136.064 126.223 107.071 1.00 27.48 ?  684 TYR A CD2   1 
ATOM   5519  C  CE1   . TYR A 1 684 ? 136.602 125.641 109.710 1.00 32.74 ?  684 TYR A CE1   1 
ATOM   5520  C  CE2   . TYR A 1 684 ? 135.289 126.778 108.066 1.00 26.81 ?  684 TYR A CE2   1 
ATOM   5521  C  CZ    . TYR A 1 684 ? 135.562 126.485 109.383 1.00 33.03 ?  684 TYR A CZ    1 
ATOM   5522  O  OH    . TYR A 1 684 ? 134.791 127.034 110.381 1.00 36.74 ?  684 TYR A OH    1 
ATOM   5523  N  N     . ALA A 1 685 ? 140.069 122.463 106.886 1.00 33.01 ?  685 ALA A N     1 
ATOM   5524  C  CA    . ALA A 1 685 ? 140.461 121.114 106.501 1.00 30.94 ?  685 ALA A CA    1 
ATOM   5525  C  C     . ALA A 1 685 ? 139.176 120.294 106.442 1.00 33.77 ?  685 ALA A C     1 
ATOM   5526  O  O     . ALA A 1 685 ? 138.802 119.627 107.407 1.00 41.20 ?  685 ALA A O     1 
ATOM   5527  C  CB    . ALA A 1 685 ? 141.468 120.533 107.480 1.00 31.56 ?  685 ALA A CB    1 
ATOM   5528  N  N     . ARG A 1 686 ? 138.499 120.355 105.300 1.00 34.12 ?  686 ARG A N     1 
ATOM   5529  C  CA    . ARG A 1 686 ? 137.250 119.636 105.099 1.00 35.47 ?  686 ARG A CA    1 
ATOM   5530  C  C     . ARG A 1 686 ? 137.544 118.219 104.631 1.00 39.33 ?  686 ARG A C     1 
ATOM   5531  O  O     . ARG A 1 686 ? 138.275 118.019 103.657 1.00 41.11 ?  686 ARG A O     1 
ATOM   5532  C  CB    . ARG A 1 686 ? 136.367 120.356 104.079 1.00 38.70 ?  686 ARG A CB    1 
ATOM   5533  C  CG    . ARG A 1 686 ? 135.610 121.541 104.641 1.00 41.76 ?  686 ARG A CG    1 
ATOM   5534  C  CD    . ARG A 1 686 ? 134.342 121.791 103.850 1.00 42.10 ?  686 ARG A CD    1 
ATOM   5535  N  NE    . ARG A 1 686 ? 133.568 120.568 103.674 1.00 43.83 ?  686 ARG A NE    1 
ATOM   5536  C  CZ    . ARG A 1 686 ? 132.270 120.463 103.916 1.00 44.76 ?  686 ARG A CZ    1 
ATOM   5537  N  NH1   . ARG A 1 686 ? 131.561 121.496 104.339 1.00 42.57 1  686 ARG A NH1   1 
ATOM   5538  N  NH2   . ARG A 1 686 ? 131.667 119.292 103.731 1.00 43.63 ?  686 ARG A NH2   1 
ATOM   5539  N  N     . THR A 1 687 ? 136.972 117.242 105.324 1.00 44.90 ?  687 THR A N     1 
ATOM   5540  C  CA    . THR A 1 687 ? 137.204 115.836 105.034 1.00 47.74 ?  687 THR A CA    1 
ATOM   5541  C  C     . THR A 1 687 ? 135.908 115.183 104.572 1.00 46.02 ?  687 THR A C     1 
ATOM   5542  O  O     . THR A 1 687 ? 134.839 115.439 105.133 1.00 49.65 ?  687 THR A O     1 
ATOM   5543  C  CB    . THR A 1 687 ? 137.754 115.109 106.265 1.00 47.73 ?  687 THR A CB    1 
ATOM   5544  O  OG1   . THR A 1 687 ? 138.992 115.712 106.663 1.00 47.03 ?  687 THR A OG1   1 
ATOM   5545  C  CG2   . THR A 1 687 ? 138.004 113.651 105.953 1.00 47.44 ?  687 THR A CG2   1 
ATOM   5546  N  N     . LYS A 1 688 ? 136.008 114.349 103.542 1.00 44.89 ?  688 LYS A N     1 
ATOM   5547  C  CA    . LYS A 1 688 ? 134.850 113.632 103.022 1.00 50.69 ?  688 LYS A CA    1 
ATOM   5548  C  C     . LYS A 1 688 ? 134.860 112.179 103.486 1.00 54.40 ?  688 LYS A C     1 
ATOM   5549  O  O     . LYS A 1 688 ? 135.904 111.643 103.857 1.00 56.78 ?  688 LYS A O     1 
ATOM   5550  C  CB    . LYS A 1 688 ? 134.816 113.697 101.495 1.00 49.89 ?  688 LYS A CB    1 
ATOM   5551  C  CG    . LYS A 1 688 ? 135.690 112.661 100.810 1.00 49.17 ?  688 LYS A CG    1 
ATOM   5552  C  CD    . LYS A 1 688 ? 135.214 112.372 99.396  1.00 51.52 ?  688 LYS A CD    1 
ATOM   5553  C  CE    . LYS A 1 688 ? 133.697 112.323 99.310  1.00 51.01 ?  688 LYS A CE    1 
ATOM   5554  N  NZ    . LYS A 1 688 ? 133.237 111.974 97.938  1.00 50.48 ?  688 LYS A NZ    1 
ATOM   5555  N  N     . VAL B 1 6   ? 153.996 115.676 164.108 1.00 58.06 ?  6   VAL B N     1 
ATOM   5556  C  CA    . VAL B 1 6   ? 152.918 116.440 164.723 1.00 60.47 ?  6   VAL B CA    1 
ATOM   5557  C  C     . VAL B 1 6   ? 153.488 117.518 165.638 1.00 60.85 ?  6   VAL B C     1 
ATOM   5558  O  O     . VAL B 1 6   ? 154.249 117.220 166.558 1.00 56.42 ?  6   VAL B O     1 
ATOM   5559  C  CB    . VAL B 1 6   ? 151.954 115.523 165.493 1.00 59.34 ?  6   VAL B CB    1 
ATOM   5560  C  CG1   . VAL B 1 6   ? 150.774 116.319 166.021 1.00 55.45 ?  6   VAL B CG1   1 
ATOM   5561  C  CG2   . VAL B 1 6   ? 151.479 114.386 164.604 1.00 59.30 ?  6   VAL B CG2   1 
ATOM   5562  N  N     . PRO B 1 7   ? 153.126 118.773 165.374 1.00 59.15 ?  7   PRO B N     1 
ATOM   5563  C  CA    . PRO B 1 7   ? 153.635 119.877 166.197 1.00 53.13 ?  7   PRO B CA    1 
ATOM   5564  C  C     . PRO B 1 7   ? 153.187 119.756 167.644 1.00 55.56 ?  7   PRO B C     1 
ATOM   5565  O  O     . PRO B 1 7   ? 152.136 119.189 167.950 1.00 60.63 ?  7   PRO B O     1 
ATOM   5566  C  CB    . PRO B 1 7   ? 153.040 121.123 165.536 1.00 52.80 ?  7   PRO B CB    1 
ATOM   5567  C  CG    . PRO B 1 7   ? 152.649 120.716 164.169 1.00 56.23 ?  7   PRO B CG    1 
ATOM   5568  C  CD    . PRO B 1 7   ? 152.455 119.235 164.146 1.00 56.88 ?  7   PRO B CD    1 
ATOM   5569  N  N     . LYS B 1 8   ? 154.014 120.295 168.544 1.00 55.11 ?  8   LYS B N     1 
ATOM   5570  C  CA    . LYS B 1 8   ? 153.707 120.233 169.969 1.00 54.87 ?  8   LYS B CA    1 
ATOM   5571  C  C     . LYS B 1 8   ? 152.418 120.975 170.294 1.00 57.26 ?  8   LYS B C     1 
ATOM   5572  O  O     . LYS B 1 8   ? 151.592 120.489 171.077 1.00 59.71 ?  8   LYS B O     1 
ATOM   5573  C  CB    . LYS B 1 8   ? 154.870 120.802 170.781 1.00 55.07 ?  8   LYS B CB    1 
ATOM   5574  C  CG    . LYS B 1 8   ? 154.867 120.384 172.241 1.00 55.73 ?  8   LYS B CG    1 
ATOM   5575  C  CD    . LYS B 1 8   ? 155.410 121.488 173.133 1.00 56.79 ?  8   LYS B CD    1 
ATOM   5576  C  CE    . LYS B 1 8   ? 154.761 121.458 174.506 1.00 58.05 ?  8   LYS B CE    1 
ATOM   5577  N  NZ    . LYS B 1 8   ? 155.622 122.090 175.543 1.00 56.65 1  8   LYS B NZ    1 
ATOM   5578  N  N     . TRP B 1 9   ? 152.226 122.157 169.703 1.00 58.22 ?  9   TRP B N     1 
ATOM   5579  C  CA    . TRP B 1 9   ? 150.993 122.898 169.937 1.00 51.60 ?  9   TRP B CA    1 
ATOM   5580  C  C     . TRP B 1 9   ? 149.786 122.176 169.357 1.00 51.94 ?  9   TRP B C     1 
ATOM   5581  O  O     . TRP B 1 9   ? 148.692 122.254 169.921 1.00 58.14 ?  9   TRP B O     1 
ATOM   5582  C  CB    . TRP B 1 9   ? 151.097 124.307 169.356 1.00 50.43 ?  9   TRP B CB    1 
ATOM   5583  C  CG    . TRP B 1 9   ? 151.455 124.355 167.904 1.00 48.99 ?  9   TRP B CG    1 
ATOM   5584  C  CD1   . TRP B 1 9   ? 150.592 124.364 166.849 1.00 48.05 ?  9   TRP B CD1   1 
ATOM   5585  C  CD2   . TRP B 1 9   ? 152.771 124.429 167.345 1.00 48.63 ?  9   TRP B CD2   1 
ATOM   5586  N  NE1   . TRP B 1 9   ? 151.288 124.427 165.668 1.00 47.61 ?  9   TRP B NE1   1 
ATOM   5587  C  CE2   . TRP B 1 9   ? 152.628 124.470 165.946 1.00 50.20 ?  9   TRP B CE2   1 
ATOM   5588  C  CE3   . TRP B 1 9   ? 154.056 124.458 167.894 1.00 45.96 ?  9   TRP B CE3   1 
ATOM   5589  C  CZ2   . TRP B 1 9   ? 153.721 124.537 165.086 1.00 49.91 ?  9   TRP B CZ2   1 
ATOM   5590  C  CZ3   . TRP B 1 9   ? 155.138 124.526 167.039 1.00 51.15 ?  9   TRP B CZ3   1 
ATOM   5591  C  CH2   . TRP B 1 9   ? 154.964 124.564 165.652 1.00 51.69 ?  9   TRP B CH2   1 
ATOM   5592  N  N     . ILE B 1 10  ? 149.962 121.474 168.237 1.00 52.13 ?  10  ILE B N     1 
ATOM   5593  C  CA    . ILE B 1 10  ? 148.859 120.705 167.672 1.00 53.51 ?  10  ILE B CA    1 
ATOM   5594  C  C     . ILE B 1 10  ? 148.493 119.547 168.593 1.00 54.08 ?  10  ILE B C     1 
ATOM   5595  O  O     . ILE B 1 10  ? 147.309 119.245 168.793 1.00 56.39 ?  10  ILE B O     1 
ATOM   5596  C  CB    . ILE B 1 10  ? 149.215 120.223 166.254 1.00 54.76 ?  10  ILE B CB    1 
ATOM   5597  C  CG1   . ILE B 1 10  ? 149.084 121.371 165.252 1.00 53.72 ?  10  ILE B CG1   1 
ATOM   5598  C  CG2   . ILE B 1 10  ? 148.322 119.069 165.839 1.00 55.30 ?  10  ILE B CG2   1 
ATOM   5599  C  CD1   . ILE B 1 10  ? 147.904 122.283 165.507 1.00 54.18 ?  10  ILE B CD1   1 
ATOM   5600  N  N     . GLN B 1 11  ? 149.496 118.886 169.174 1.00 57.56 ?  11  GLN B N     1 
ATOM   5601  C  CA    . GLN B 1 11  ? 149.218 117.834 170.146 1.00 57.04 ?  11  GLN B CA    1 
ATOM   5602  C  C     . GLN B 1 11  ? 148.495 118.388 171.365 1.00 59.28 ?  11  GLN B C     1 
ATOM   5603  O  O     . GLN B 1 11  ? 147.511 117.802 171.829 1.00 60.20 ?  11  GLN B O     1 
ATOM   5604  C  CB    . GLN B 1 11  ? 150.515 117.145 170.570 1.00 56.99 ?  11  GLN B CB    1 
ATOM   5605  C  CG    . GLN B 1 11  ? 150.954 116.013 169.660 1.00 60.82 ?  11  GLN B CG    1 
ATOM   5606  C  CD    . GLN B 1 11  ? 152.460 115.847 169.632 1.00 62.31 ?  11  GLN B CD    1 
ATOM   5607  O  OE1   . GLN B 1 11  ? 153.050 115.605 168.580 1.00 61.39 ?  11  GLN B OE1   1 
ATOM   5608  N  NE2   . GLN B 1 11  ? 153.091 115.980 170.792 1.00 60.14 ?  11  GLN B NE2   1 
ATOM   5609  N  N     . LEU B 1 12  ? 148.963 119.523 171.891 1.00 58.79 ?  12  LEU B N     1 
ATOM   5610  C  CA    . LEU B 1 12  ? 148.330 120.113 173.068 1.00 54.13 ?  12  LEU B CA    1 
ATOM   5611  C  C     . LEU B 1 12  ? 146.894 120.526 172.776 1.00 57.99 ?  12  LEU B C     1 
ATOM   5612  O  O     . LEU B 1 12  ? 146.003 120.348 173.615 1.00 60.10 ?  12  LEU B O     1 
ATOM   5613  C  CB    . LEU B 1 12  ? 149.142 121.310 173.558 1.00 55.26 ?  12  LEU B CB    1 
ATOM   5614  C  CG    . LEU B 1 12  ? 150.251 121.008 174.564 1.00 58.07 ?  12  LEU B CG    1 
ATOM   5615  C  CD1   . LEU B 1 12  ? 151.147 122.220 174.742 1.00 58.53 ?  12  LEU B CD1   1 
ATOM   5616  C  CD2   . LEU B 1 12  ? 149.663 120.572 175.892 1.00 56.30 ?  12  LEU B CD2   1 
ATOM   5617  N  N     . ASN B 1 13  ? 146.651 121.092 171.592 1.00 53.89 ?  13  ASN B N     1 
ATOM   5618  C  CA    . ASN B 1 13  ? 145.295 121.468 171.210 1.00 52.68 ?  13  ASN B CA    1 
ATOM   5619  C  C     . ASN B 1 13  ? 144.412 120.238 171.041 1.00 56.13 ?  13  ASN B C     1 
ATOM   5620  O  O     . ASN B 1 13  ? 143.198 120.302 171.262 1.00 62.41 ?  13  ASN B O     1 
ATOM   5621  C  CB    . ASN B 1 13  ? 145.332 122.295 169.926 1.00 53.91 ?  13  ASN B CB    1 
ATOM   5622  C  CG    . ASN B 1 13  ? 143.958 122.517 169.333 1.00 53.99 ?  13  ASN B CG    1 
ATOM   5623  O  OD1   . ASN B 1 13  ? 143.522 121.773 168.456 1.00 55.79 ?  13  ASN B OD1   1 
ATOM   5624  N  ND2   . ASN B 1 13  ? 143.267 123.544 169.809 1.00 54.99 ?  13  ASN B ND2   1 
ATOM   5625  N  N     . ASN B 1 14  ? 145.005 119.107 170.652 1.00 59.08 ?  14  ASN B N     1 
ATOM   5626  C  CA    . ASN B 1 14  ? 144.235 117.882 170.483 1.00 55.76 ?  14  ASN B CA    1 
ATOM   5627  C  C     . ASN B 1 14  ? 143.881 117.225 171.811 1.00 58.53 ?  14  ASN B C     1 
ATOM   5628  O  O     . ASN B 1 14  ? 142.999 116.363 171.841 1.00 63.28 ?  14  ASN B O     1 
ATOM   5629  C  CB    . ASN B 1 14  ? 145.004 116.897 169.604 1.00 59.59 ?  14  ASN B CB    1 
ATOM   5630  C  CG    . ASN B 1 14  ? 144.895 117.225 168.130 1.00 59.07 ?  14  ASN B CG    1 
ATOM   5631  O  OD1   . ASN B 1 14  ? 144.632 118.366 167.754 1.00 59.30 ?  14  ASN B OD1   1 
ATOM   5632  N  ND2   . ASN B 1 14  ? 145.097 116.222 167.285 1.00 58.70 ?  14  ASN B ND2   1 
ATOM   5633  N  N     . GLU B 1 15  ? 144.540 117.611 172.905 1.00 59.48 ?  15  GLU B N     1 
ATOM   5634  C  CA    . GLU B 1 15  ? 144.222 117.049 174.212 1.00 59.95 ?  15  GLU B CA    1 
ATOM   5635  C  C     . GLU B 1 15  ? 142.955 117.633 174.818 1.00 61.82 ?  15  GLU B C     1 
ATOM   5636  O  O     . GLU B 1 15  ? 142.542 117.185 175.893 1.00 64.87 ?  15  GLU B O     1 
ATOM   5637  C  CB    . GLU B 1 15  ? 145.386 117.252 175.187 1.00 60.50 ?  15  GLU B CB    1 
ATOM   5638  C  CG    . GLU B 1 15  ? 146.739 116.844 174.643 1.00 62.55 ?  15  GLU B CG    1 
ATOM   5639  C  CD    . GLU B 1 15  ? 147.817 116.841 175.708 1.00 66.42 ?  15  GLU B CD    1 
ATOM   5640  O  OE1   . GLU B 1 15  ? 147.469 116.806 176.906 1.00 64.42 ?  15  GLU B OE1   1 
ATOM   5641  O  OE2   . GLU B 1 15  ? 149.013 116.875 175.346 1.00 66.45 -1 15  GLU B OE2   1 
ATOM   5642  N  N     . ILE B 1 16  ? 142.342 118.626 174.173 1.00 60.94 ?  16  ILE B N     1 
ATOM   5643  C  CA    . ILE B 1 16  ? 141.062 119.140 174.649 1.00 60.27 ?  16  ILE B CA    1 
ATOM   5644  C  C     . ILE B 1 16  ? 139.998 118.053 174.582 1.00 60.83 ?  16  ILE B C     1 
ATOM   5645  O  O     . ILE B 1 16  ? 139.207 117.878 175.516 1.00 61.27 ?  16  ILE B O     1 
ATOM   5646  C  CB    . ILE B 1 16  ? 140.654 120.388 173.845 1.00 61.94 ?  16  ILE B CB    1 
ATOM   5647  C  CG1   . ILE B 1 16  ? 141.775 121.427 173.869 1.00 60.80 ?  16  ILE B CG1   1 
ATOM   5648  C  CG2   . ILE B 1 16  ? 139.361 120.974 174.391 1.00 60.34 ?  16  ILE B CG2   1 
ATOM   5649  C  CD1   . ILE B 1 16  ? 141.331 122.816 173.480 1.00 58.23 ?  16  ILE B CD1   1 
ATOM   5650  N  N     . MET B 1 17  ? 139.966 117.304 173.478 1.00 62.13 ?  17  MET B N     1 
ATOM   5651  C  CA    . MET B 1 17  ? 138.974 116.247 173.322 1.00 63.00 ?  17  MET B CA    1 
ATOM   5652  C  C     . MET B 1 17  ? 139.241 115.056 174.231 1.00 63.88 ?  17  MET B C     1 
ATOM   5653  O  O     . MET B 1 17  ? 138.312 114.291 174.513 1.00 65.86 ?  17  MET B O     1 
ATOM   5654  C  CB    . MET B 1 17  ? 138.920 115.781 171.868 1.00 63.13 ?  17  MET B CB    1 
ATOM   5655  C  CG    . MET B 1 17  ? 138.740 116.870 170.802 1.00 63.32 ?  17  MET B CG    1 
ATOM   5656  S  SD    . MET B 1 17  ? 137.184 117.799 170.705 1.00 70.70 ?  17  MET B SD    1 
ATOM   5657  C  CE    . MET B 1 17  ? 137.212 118.837 172.163 1.00 62.37 ?  17  MET B CE    1 
ATOM   5658  N  N     . ILE B 1 18  ? 140.478 114.874 174.688 1.00 63.36 ?  18  ILE B N     1 
ATOM   5659  C  CA    . ILE B 1 18  ? 140.770 113.812 175.645 1.00 63.14 ?  18  ILE B CA    1 
ATOM   5660  C  C     . ILE B 1 18  ? 140.089 114.188 176.957 1.00 63.69 ?  18  ILE B C     1 
ATOM   5661  O  O     . ILE B 1 18  ? 140.485 115.148 177.624 1.00 64.62 ?  18  ILE B O     1 
ATOM   5662  C  CB    . ILE B 1 18  ? 142.278 113.604 175.829 1.00 63.13 ?  18  ILE B CB    1 
ATOM   5663  C  CG1   . ILE B 1 18  ? 142.856 112.764 174.686 1.00 62.85 ?  18  ILE B CG1   1 
ATOM   5664  C  CG2   . ILE B 1 18  ? 142.567 112.902 177.147 1.00 63.54 ?  18  ILE B CG2   1 
ATOM   5665  C  CD1   . ILE B 1 18  ? 143.021 113.501 173.375 1.00 62.27 ?  18  ILE B CD1   1 
ATOM   5666  N  N     . GLN B 1 19  ? 139.043 113.449 177.315 1.00 68.67 ?  19  GLN B N     1 
ATOM   5667  C  CA    . GLN B 1 19  ? 138.223 113.793 178.468 1.00 69.55 ?  19  GLN B CA    1 
ATOM   5668  C  C     . GLN B 1 19  ? 138.889 113.291 179.740 1.00 70.48 ?  19  GLN B C     1 
ATOM   5669  O  O     . GLN B 1 19  ? 139.075 112.083 179.918 1.00 71.79 ?  19  GLN B O     1 
ATOM   5670  C  CB    . GLN B 1 19  ? 136.823 113.203 178.315 1.00 70.06 ?  19  GLN B CB    1 
ATOM   5671  C  CG    . GLN B 1 19  ? 135.885 114.058 177.480 1.00 69.09 ?  19  GLN B CG    1 
ATOM   5672  C  CD    . GLN B 1 19  ? 134.480 114.103 178.042 1.00 72.31 ?  19  GLN B CD    1 
ATOM   5673  O  OE1   . GLN B 1 19  ? 134.238 113.690 179.175 1.00 72.66 ?  19  GLN B OE1   1 
ATOM   5674  N  NE2   . GLN B 1 19  ? 133.542 114.609 177.249 1.00 69.92 ?  19  GLN B NE2   1 
ATOM   5675  N  N     . LYS B 1 20  ? 139.250 114.218 180.622 1.00 74.71 ?  20  LYS B N     1 
ATOM   5676  C  CA    . LYS B 1 20  ? 139.846 113.899 181.912 1.00 74.45 ?  20  LYS B CA    1 
ATOM   5677  C  C     . LYS B 1 20  ? 138.834 114.218 183.003 1.00 77.20 ?  20  LYS B C     1 
ATOM   5678  O  O     . LYS B 1 20  ? 138.324 115.342 183.069 1.00 74.44 ?  20  LYS B O     1 
ATOM   5679  C  CB    . LYS B 1 20  ? 141.141 114.682 182.125 1.00 71.73 ?  20  LYS B CB    1 
ATOM   5680  C  CG    . LYS B 1 20  ? 141.832 114.392 183.447 1.00 74.91 ?  20  LYS B CG    1 
ATOM   5681  C  CD    . LYS B 1 20  ? 142.668 115.575 183.909 1.00 75.30 ?  20  LYS B CD    1 
ATOM   5682  C  CE    . LYS B 1 20  ? 141.818 116.820 184.094 1.00 76.62 ?  20  LYS B CE    1 
ATOM   5683  N  NZ    . LYS B 1 20  ? 140.552 116.529 184.822 1.00 78.76 1  20  LYS B NZ    1 
ATOM   5684  N  N     . ASP B 1 21  ? 138.544 113.227 183.849 1.00 82.99 ?  21  ASP B N     1 
ATOM   5685  C  CA    . ASP B 1 21  ? 137.573 113.365 184.936 1.00 82.58 ?  21  ASP B CA    1 
ATOM   5686  C  C     . ASP B 1 21  ? 136.195 113.756 184.403 1.00 82.92 ?  21  ASP B C     1 
ATOM   5687  O  O     . ASP B 1 21  ? 135.463 114.532 185.023 1.00 82.22 ?  21  ASP B O     1 
ATOM   5688  C  CB    . ASP B 1 21  ? 138.059 114.366 185.988 1.00 82.38 ?  21  ASP B CB    1 
ATOM   5689  C  CG    . ASP B 1 21  ? 137.334 114.220 187.313 1.00 84.51 ?  21  ASP B CG    1 
ATOM   5690  O  OD1   . ASP B 1 21  ? 137.069 113.070 187.724 1.00 82.89 ?  21  ASP B OD1   1 
ATOM   5691  O  OD2   . ASP B 1 21  ? 137.028 115.255 187.941 1.00 84.64 -1 21  ASP B OD2   1 
ATOM   5692  N  N     . GLY B 1 22  ? 135.837 113.216 183.240 1.00 75.34 ?  22  GLY B N     1 
ATOM   5693  C  CA    . GLY B 1 22  ? 134.530 113.455 182.664 1.00 74.48 ?  22  GLY B CA    1 
ATOM   5694  C  C     . GLY B 1 22  ? 134.328 114.823 182.055 1.00 76.15 ?  22  GLY B C     1 
ATOM   5695  O  O     . GLY B 1 22  ? 133.188 115.174 181.731 1.00 75.95 ?  22  GLY B O     1 
ATOM   5696  N  N     . LYS B 1 23  ? 135.390 115.607 181.889 1.00 72.59 ?  23  LYS B N     1 
ATOM   5697  C  CA    . LYS B 1 23  ? 135.293 116.948 181.336 1.00 69.37 ?  23  LYS B CA    1 
ATOM   5698  C  C     . LYS B 1 23  ? 136.386 117.162 180.300 1.00 70.04 ?  23  LYS B C     1 
ATOM   5699  O  O     . LYS B 1 23  ? 137.470 116.581 180.389 1.00 69.80 ?  23  LYS B O     1 
ATOM   5700  C  CB    . LYS B 1 23  ? 135.408 118.020 182.427 1.00 68.27 ?  23  LYS B CB    1 
ATOM   5701  C  CG    . LYS B 1 23  ? 134.278 118.013 183.439 1.00 68.38 ?  23  LYS B CG    1 
ATOM   5702  C  CD    . LYS B 1 23  ? 134.445 119.145 184.436 1.00 68.60 ?  23  LYS B CD    1 
ATOM   5703  C  CE    . LYS B 1 23  ? 133.404 119.078 185.538 1.00 69.97 ?  23  LYS B CE    1 
ATOM   5704  N  NZ    . LYS B 1 23  ? 133.656 120.101 186.589 1.00 68.39 1  23  LYS B NZ    1 
ATOM   5705  N  N     . PHE B 1 24  ? 136.087 118.004 179.313 1.00 65.61 ?  24  PHE B N     1 
ATOM   5706  C  CA    . PHE B 1 24  ? 137.098 118.396 178.344 1.00 62.62 ?  24  PHE B CA    1 
ATOM   5707  C  C     . PHE B 1 24  ? 138.195 119.203 179.027 1.00 61.66 ?  24  PHE B C     1 
ATOM   5708  O  O     . PHE B 1 24  ? 137.947 119.953 179.974 1.00 61.85 ?  24  PHE B O     1 
ATOM   5709  C  CB    . PHE B 1 24  ? 136.477 119.222 177.216 1.00 61.12 ?  24  PHE B CB    1 
ATOM   5710  C  CG    . PHE B 1 24  ? 135.484 118.469 176.383 1.00 61.30 ?  24  PHE B CG    1 
ATOM   5711  C  CD1   . PHE B 1 24  ? 135.889 117.782 175.253 1.00 64.24 ?  24  PHE B CD1   1 
ATOM   5712  C  CD2   . PHE B 1 24  ? 134.141 118.464 176.717 1.00 61.65 ?  24  PHE B CD2   1 
ATOM   5713  C  CE1   . PHE B 1 24  ? 134.976 117.093 174.480 1.00 64.73 ?  24  PHE B CE1   1 
ATOM   5714  C  CE2   . PHE B 1 24  ? 133.223 117.778 175.947 1.00 62.37 ?  24  PHE B CE2   1 
ATOM   5715  C  CZ    . PHE B 1 24  ? 133.642 117.091 174.826 1.00 61.31 ?  24  PHE B CZ    1 
ATOM   5716  N  N     . GLN B 1 25  ? 139.424 119.041 178.539 1.00 62.73 ?  25  GLN B N     1 
ATOM   5717  C  CA    . GLN B 1 25  ? 140.566 119.784 179.073 1.00 63.64 ?  25  GLN B CA    1 
ATOM   5718  C  C     . GLN B 1 25  ? 140.656 121.113 178.331 1.00 64.69 ?  25  GLN B C     1 
ATOM   5719  O  O     . GLN B 1 25  ? 141.468 121.310 177.424 1.00 64.40 ?  25  GLN B O     1 
ATOM   5720  C  CB    . GLN B 1 25  ? 141.846 118.968 178.949 1.00 64.71 ?  25  GLN B CB    1 
ATOM   5721  C  CG    . GLN B 1 25  ? 141.884 117.744 179.850 1.00 62.14 ?  25  GLN B CG    1 
ATOM   5722  C  CD    . GLN B 1 25  ? 143.052 116.833 179.542 1.00 63.89 ?  25  GLN B CD    1 
ATOM   5723  O  OE1   . GLN B 1 25  ? 144.144 117.001 180.082 1.00 63.37 ?  25  GLN B OE1   1 
ATOM   5724  N  NE2   . GLN B 1 25  ? 142.828 115.861 178.666 1.00 64.37 ?  25  GLN B NE2   1 
ATOM   5725  N  N     . PHE B 1 26  ? 139.787 122.043 178.735 1.00 59.58 ?  26  PHE B N     1 
ATOM   5726  C  CA    . PHE B 1 26  ? 139.743 123.350 178.088 1.00 56.88 ?  26  PHE B CA    1 
ATOM   5727  C  C     . PHE B 1 26  ? 141.005 124.157 178.357 1.00 59.74 ?  26  PHE B C     1 
ATOM   5728  O  O     . PHE B 1 26  ? 141.377 125.010 177.544 1.00 60.98 ?  26  PHE B O     1 
ATOM   5729  C  CB    . PHE B 1 26  ? 138.510 124.122 178.555 1.00 52.78 ?  26  PHE B CB    1 
ATOM   5730  C  CG    . PHE B 1 26  ? 137.219 123.593 178.002 1.00 55.55 ?  26  PHE B CG    1 
ATOM   5731  C  CD1   . PHE B 1 26  ? 137.062 123.400 176.640 1.00 55.27 ?  26  PHE B CD1   1 
ATOM   5732  C  CD2   . PHE B 1 26  ? 136.164 123.285 178.843 1.00 54.50 ?  26  PHE B CD2   1 
ATOM   5733  C  CE1   . PHE B 1 26  ? 135.878 122.912 176.129 1.00 56.32 ?  26  PHE B CE1   1 
ATOM   5734  C  CE2   . PHE B 1 26  ? 134.976 122.797 178.336 1.00 52.70 ?  26  PHE B CE2   1 
ATOM   5735  C  CZ    . PHE B 1 26  ? 134.834 122.610 176.977 1.00 52.96 ?  26  PHE B CZ    1 
ATOM   5736  N  N     . ASP B 1 27  ? 141.673 123.905 179.485 1.00 63.05 ?  27  ASP B N     1 
ATOM   5737  C  CA    . ASP B 1 27  ? 142.896 124.622 179.823 1.00 58.55 ?  27  ASP B CA    1 
ATOM   5738  C  C     . ASP B 1 27  ? 144.068 124.248 178.927 1.00 60.78 ?  27  ASP B C     1 
ATOM   5739  O  O     . ASP B 1 27  ? 145.093 124.936 178.963 1.00 62.31 ?  27  ASP B O     1 
ATOM   5740  C  CB    . ASP B 1 27  ? 143.262 124.364 181.285 1.00 60.43 ?  27  ASP B CB    1 
ATOM   5741  C  CG    . ASP B 1 27  ? 142.069 124.476 182.213 1.00 65.03 ?  27  ASP B CG    1 
ATOM   5742  O  OD1   . ASP B 1 27  ? 141.009 123.899 181.891 1.00 65.00 ?  27  ASP B OD1   1 
ATOM   5743  O  OD2   . ASP B 1 27  ? 142.189 125.142 183.262 1.00 65.17 -1 27  ASP B OD2   1 
ATOM   5744  N  N     . LYS B 1 28  ? 143.949 123.182 178.134 1.00 60.48 ?  28  LYS B N     1 
ATOM   5745  C  CA    . LYS B 1 28  ? 145.029 122.797 177.235 1.00 61.30 ?  28  LYS B CA    1 
ATOM   5746  C  C     . LYS B 1 28  ? 145.210 123.781 176.089 1.00 61.69 ?  28  LYS B C     1 
ATOM   5747  O  O     . LYS B 1 28  ? 146.289 123.823 175.490 1.00 62.22 ?  28  LYS B O     1 
ATOM   5748  C  CB    . LYS B 1 28  ? 144.776 121.396 176.676 1.00 61.12 ?  28  LYS B CB    1 
ATOM   5749  C  CG    . LYS B 1 28  ? 145.031 120.278 177.670 1.00 61.20 ?  28  LYS B CG    1 
ATOM   5750  C  CD    . LYS B 1 28  ? 146.517 120.046 177.863 1.00 61.63 ?  28  LYS B CD    1 
ATOM   5751  C  CE    . LYS B 1 28  ? 146.787 119.194 179.089 1.00 61.66 ?  28  LYS B CE    1 
ATOM   5752  N  NZ    . LYS B 1 28  ? 148.221 118.813 179.187 1.00 59.46 1  28  LYS B NZ    1 
ATOM   5753  N  N     . ASP B 1 29  ? 144.183 124.573 175.770 1.00 58.24 ?  29  ASP B N     1 
ATOM   5754  C  CA    . ASP B 1 29  ? 144.304 125.519 174.668 1.00 55.40 ?  29  ASP B CA    1 
ATOM   5755  C  C     . ASP B 1 29  ? 145.210 126.689 175.031 1.00 55.16 ?  29  ASP B C     1 
ATOM   5756  O  O     . ASP B 1 29  ? 145.877 127.247 174.152 1.00 57.74 ?  29  ASP B O     1 
ATOM   5757  C  CB    . ASP B 1 29  ? 142.922 126.014 174.249 1.00 55.23 ?  29  ASP B CB    1 
ATOM   5758  C  CG    . ASP B 1 29  ? 142.733 126.002 172.745 1.00 58.52 ?  29  ASP B CG    1 
ATOM   5759  O  OD1   . ASP B 1 29  ? 141.896 126.777 172.242 1.00 55.50 ?  29  ASP B OD1   1 
ATOM   5760  O  OD2   . ASP B 1 29  ? 143.423 125.214 172.065 1.00 58.35 -1 29  ASP B OD2   1 
ATOM   5761  N  N     . LYS B 1 30  ? 145.242 127.081 176.307 1.00 55.30 ?  30  LYS B N     1 
ATOM   5762  C  CA    . LYS B 1 30  ? 146.233 128.058 176.748 1.00 56.62 ?  30  LYS B CA    1 
ATOM   5763  C  C     . LYS B 1 30  ? 147.642 127.497 176.619 1.00 56.50 ?  30  LYS B C     1 
ATOM   5764  O  O     . LYS B 1 30  ? 148.556 128.189 176.152 1.00 57.10 ?  30  LYS B O     1 
ATOM   5765  C  CB    . LYS B 1 30  ? 145.955 128.478 178.190 1.00 54.70 ?  30  LYS B CB    1 
ATOM   5766  C  CG    . LYS B 1 30  ? 144.657 129.243 178.376 1.00 56.61 ?  30  LYS B CG    1 
ATOM   5767  C  CD    . LYS B 1 30  ? 144.917 130.685 178.784 1.00 58.11 ?  30  LYS B CD    1 
ATOM   5768  C  CE    . LYS B 1 30  ? 146.000 130.776 179.848 1.00 58.82 ?  30  LYS B CE    1 
ATOM   5769  N  NZ    . LYS B 1 30  ? 146.052 132.124 180.479 1.00 58.06 1  30  LYS B NZ    1 
ATOM   5770  N  N     . GLU B 1 31  ? 147.835 126.239 177.020 1.00 57.78 ?  31  GLU B N     1 
ATOM   5771  C  CA    . GLU B 1 31  ? 149.113 125.580 176.785 1.00 54.53 ?  31  GLU B CA    1 
ATOM   5772  C  C     . GLU B 1 31  ? 149.385 125.446 175.294 1.00 55.31 ?  31  GLU B C     1 
ATOM   5773  O  O     . GLU B 1 31  ? 150.525 125.609 174.847 1.00 57.92 ?  31  GLU B O     1 
ATOM   5774  C  CB    . GLU B 1 31  ? 149.133 124.211 177.462 1.00 55.06 ?  31  GLU B CB    1 
ATOM   5775  C  CG    . GLU B 1 31  ? 149.131 124.268 178.980 1.00 56.40 ?  31  GLU B CG    1 
ATOM   5776  C  CD    . GLU B 1 31  ? 149.206 122.893 179.613 1.00 63.70 ?  31  GLU B CD    1 
ATOM   5777  O  OE1   . GLU B 1 31  ? 149.168 121.892 178.868 1.00 65.30 ?  31  GLU B OE1   1 
ATOM   5778  O  OE2   . GLU B 1 31  ? 149.303 122.813 180.855 1.00 60.64 -1 31  GLU B OE2   1 
ATOM   5779  N  N     . ALA B 1 32  ? 148.347 125.155 174.509 1.00 52.44 ?  32  ALA B N     1 
ATOM   5780  C  CA    . ALA B 1 32  ? 148.525 125.019 173.068 1.00 49.90 ?  32  ALA B CA    1 
ATOM   5781  C  C     . ALA B 1 32  ? 148.987 126.327 172.438 1.00 51.55 ?  32  ALA B C     1 
ATOM   5782  O  O     . ALA B 1 32  ? 149.918 126.333 171.629 1.00 52.12 ?  32  ALA B O     1 
ATOM   5783  C  CB    . ALA B 1 32  ? 147.227 124.542 172.418 1.00 49.16 ?  32  ALA B CB    1 
ATOM   5784  N  N     . VAL B 1 33  ? 148.357 127.447 172.802 1.00 54.60 ?  33  VAL B N     1 
ATOM   5785  C  CA    . VAL B 1 33  ? 148.746 128.726 172.213 1.00 50.88 ?  33  VAL B CA    1 
ATOM   5786  C  C     . VAL B 1 33  ? 150.118 129.160 172.720 1.00 53.80 ?  33  VAL B C     1 
ATOM   5787  O  O     . VAL B 1 33  ? 150.919 129.730 171.968 1.00 55.05 ?  33  VAL B O     1 
ATOM   5788  C  CB    . VAL B 1 33  ? 147.668 129.799 172.465 1.00 45.90 ?  33  VAL B CB    1 
ATOM   5789  C  CG1   . VAL B 1 33  ? 147.533 130.123 173.940 1.00 47.37 ?  33  VAL B CG1   1 
ATOM   5790  C  CG2   . VAL B 1 33  ? 147.976 131.056 171.665 1.00 49.25 ?  33  VAL B CG2   1 
ATOM   5791  N  N     . HIS B 1 34  ? 150.417 128.898 173.997 1.00 51.44 ?  34  HIS B N     1 
ATOM   5792  C  CA    . HIS B 1 34  ? 151.739 129.228 174.521 1.00 47.49 ?  34  HIS B CA    1 
ATOM   5793  C  C     . HIS B 1 34  ? 152.826 128.455 173.788 1.00 48.88 ?  34  HIS B C     1 
ATOM   5794  O  O     . HIS B 1 34  ? 153.860 129.019 173.409 1.00 52.29 ?  34  HIS B O     1 
ATOM   5795  C  CB    . HIS B 1 34  ? 151.796 128.944 176.021 1.00 52.36 ?  34  HIS B CB    1 
ATOM   5796  C  CG    . HIS B 1 34  ? 153.116 129.272 176.645 1.00 53.70 ?  34  HIS B CG    1 
ATOM   5797  N  ND1   . HIS B 1 34  ? 154.134 128.352 176.761 1.00 52.99 ?  34  HIS B ND1   1 
ATOM   5798  C  CD2   . HIS B 1 34  ? 153.584 130.421 177.188 1.00 53.10 ?  34  HIS B CD2   1 
ATOM   5799  C  CE1   . HIS B 1 34  ? 155.173 128.918 177.348 1.00 51.59 ?  34  HIS B CE1   1 
ATOM   5800  N  NE2   . HIS B 1 34  ? 154.864 130.173 177.619 1.00 53.65 ?  34  HIS B NE2   1 
ATOM   5801  N  N     . SER B 1 35  ? 152.607 127.154 173.578 1.00 54.75 ?  35  SER B N     1 
ATOM   5802  C  CA    . SER B 1 35  ? 153.569 126.349 172.837 1.00 52.29 ?  35  SER B CA    1 
ATOM   5803  C  C     . SER B 1 35  ? 153.675 126.816 171.393 1.00 52.81 ?  35  SER B C     1 
ATOM   5804  O  O     . SER B 1 35  ? 154.780 126.916 170.849 1.00 55.62 ?  35  SER B O     1 
ATOM   5805  C  CB    . SER B 1 35  ? 153.176 124.874 172.897 1.00 52.45 ?  35  SER B CB    1 
ATOM   5806  O  OG    . SER B 1 35  ? 154.075 124.080 172.144 1.00 56.52 ?  35  SER B OG    1 
ATOM   5807  N  N     . TYR B 1 36  ? 152.537 127.113 170.760 1.00 49.85 ?  36  TYR B N     1 
ATOM   5808  C  CA    . TYR B 1 36  ? 152.548 127.617 169.392 1.00 50.26 ?  36  TYR B CA    1 
ATOM   5809  C  C     . TYR B 1 36  ? 153.426 128.849 169.278 1.00 47.90 ?  36  TYR B C     1 
ATOM   5810  O  O     . TYR B 1 36  ? 154.339 128.900 168.446 1.00 49.13 ?  36  TYR B O     1 
ATOM   5811  C  CB    . TYR B 1 36  ? 151.122 127.935 168.943 1.00 45.19 ?  36  TYR B CB    1 
ATOM   5812  C  CG    . TYR B 1 36  ? 151.027 128.517 167.552 1.00 43.48 ?  36  TYR B CG    1 
ATOM   5813  C  CD1   . TYR B 1 36  ? 151.673 127.918 166.481 1.00 44.00 ?  36  TYR B CD1   1 
ATOM   5814  C  CD2   . TYR B 1 36  ? 150.292 129.670 167.311 1.00 45.84 ?  36  TYR B CD2   1 
ATOM   5815  C  CE1   . TYR B 1 36  ? 151.587 128.445 165.210 1.00 46.30 ?  36  TYR B CE1   1 
ATOM   5816  C  CE2   . TYR B 1 36  ? 150.201 130.206 166.043 1.00 44.51 ?  36  TYR B CE2   1 
ATOM   5817  C  CZ    . TYR B 1 36  ? 150.851 129.589 164.997 1.00 46.87 ?  36  TYR B CZ    1 
ATOM   5818  O  OH    . TYR B 1 36  ? 150.766 130.119 163.730 1.00 47.50 ?  36  TYR B OH    1 
ATOM   5819  N  N     . PHE B 1 37  ? 153.189 129.841 170.137 1.00 51.88 ?  37  PHE B N     1 
ATOM   5820  C  CA    . PHE B 1 37  ? 154.019 131.038 170.122 1.00 50.44 ?  37  PHE B CA    1 
ATOM   5821  C  C     . PHE B 1 37  ? 155.482 130.686 170.347 1.00 51.90 ?  37  PHE B C     1 
ATOM   5822  O  O     . PHE B 1 37  ? 156.304 130.834 169.437 1.00 55.87 ?  37  PHE B O     1 
ATOM   5823  C  CB    . PHE B 1 37  ? 153.527 132.038 171.166 1.00 52.29 ?  37  PHE B CB    1 
ATOM   5824  C  CG    . PHE B 1 37  ? 152.655 133.111 170.594 1.00 53.14 ?  37  PHE B CG    1 
ATOM   5825  C  CD1   . PHE B 1 37  ? 153.213 134.254 170.054 1.00 51.94 ?  37  PHE B CD1   1 
ATOM   5826  C  CD2   . PHE B 1 37  ? 151.280 132.968 170.574 1.00 52.91 ?  37  PHE B CD2   1 
ATOM   5827  C  CE1   . PHE B 1 37  ? 152.417 135.241 169.518 1.00 53.84 ?  37  PHE B CE1   1 
ATOM   5828  C  CE2   . PHE B 1 37  ? 150.481 133.951 170.040 1.00 51.40 ?  37  PHE B CE2   1 
ATOM   5829  C  CZ    . PHE B 1 37  ? 151.050 135.087 169.510 1.00 51.87 ?  37  PHE B CZ    1 
ATOM   5830  N  N     . VAL B 1 38  ? 155.796 130.127 171.520 1.00 55.94 ?  38  VAL B N     1 
ATOM   5831  C  CA    . VAL B 1 38  ? 157.179 129.954 171.954 1.00 56.74 ?  38  VAL B CA    1 
ATOM   5832  C  C     . VAL B 1 38  ? 157.976 129.083 170.987 1.00 55.35 ?  38  VAL B C     1 
ATOM   5833  O  O     . VAL B 1 38  ? 159.194 129.252 170.854 1.00 57.62 ?  38  VAL B O     1 
ATOM   5834  C  CB    . VAL B 1 38  ? 157.185 129.392 173.394 1.00 54.50 ?  38  VAL B CB    1 
ATOM   5835  C  CG1   . VAL B 1 38  ? 158.431 128.566 173.673 1.00 56.35 ?  38  VAL B CG1   1 
ATOM   5836  C  CG2   . VAL B 1 38  ? 157.058 130.524 174.399 1.00 52.68 ?  38  VAL B CG2   1 
ATOM   5837  N  N     . ASP B 1 39  ? 157.317 128.174 170.268 1.00 53.36 ?  39  ASP B N     1 
ATOM   5838  C  CA    . ASP B 1 39  ? 158.028 127.248 169.398 1.00 52.42 ?  39  ASP B CA    1 
ATOM   5839  C  C     . ASP B 1 39  ? 158.025 127.647 167.930 1.00 57.74 ?  39  ASP B C     1 
ATOM   5840  O  O     . ASP B 1 39  ? 158.950 127.267 167.204 1.00 61.98 ?  39  ASP B O     1 
ATOM   5841  C  CB    . ASP B 1 39  ? 157.436 125.841 169.529 1.00 55.14 ?  39  ASP B CB    1 
ATOM   5842  C  CG    . ASP B 1 39  ? 157.577 125.279 170.928 1.00 60.48 ?  39  ASP B CG    1 
ATOM   5843  O  OD1   . ASP B 1 39  ? 158.187 125.952 171.782 1.00 59.89 ?  39  ASP B OD1   1 
ATOM   5844  O  OD2   . ASP B 1 39  ? 157.078 124.161 171.174 1.00 62.77 -1 39  ASP B OD2   1 
ATOM   5845  N  N     . TYR B 1 40  ? 157.025 128.391 167.457 1.00 58.16 ?  40  TYR B N     1 
ATOM   5846  C  CA    . TYR B 1 40  ? 156.941 128.730 166.044 1.00 55.81 ?  40  TYR B CA    1 
ATOM   5847  C  C     . TYR B 1 40  ? 156.967 130.227 165.792 1.00 59.41 ?  40  TYR B C     1 
ATOM   5848  O  O     . TYR B 1 40  ? 157.715 130.691 164.923 1.00 62.58 ?  40  TYR B O     1 
ATOM   5849  C  CB    . TYR B 1 40  ? 155.664 128.119 165.443 1.00 52.29 ?  40  TYR B CB    1 
ATOM   5850  C  CG    . TYR B 1 40  ? 155.571 128.225 163.941 1.00 56.35 ?  40  TYR B CG    1 
ATOM   5851  C  CD1   . TYR B 1 40  ? 156.289 127.368 163.119 1.00 56.20 ?  40  TYR B CD1   1 
ATOM   5852  C  CD2   . TYR B 1 40  ? 154.758 129.179 163.343 1.00 58.17 ?  40  TYR B CD2   1 
ATOM   5853  C  CE1   . TYR B 1 40  ? 156.205 127.461 161.744 1.00 57.45 ?  40  TYR B CE1   1 
ATOM   5854  C  CE2   . TYR B 1 40  ? 154.667 129.279 161.970 1.00 57.38 ?  40  TYR B CE2   1 
ATOM   5855  C  CZ    . TYR B 1 40  ? 155.392 128.418 161.174 1.00 59.93 ?  40  TYR B CZ    1 
ATOM   5856  O  OH    . TYR B 1 40  ? 155.304 128.515 159.805 1.00 61.60 ?  40  TYR B OH    1 
ATOM   5857  N  N     . ILE B 1 41  ? 156.171 131.003 166.529 1.00 54.61 ?  41  ILE B N     1 
ATOM   5858  C  CA    . ILE B 1 41  ? 155.995 132.411 166.188 1.00 54.22 ?  41  ILE B CA    1 
ATOM   5859  C  C     . ILE B 1 41  ? 157.240 133.205 166.555 1.00 53.52 ?  41  ILE B C     1 
ATOM   5860  O  O     . ILE B 1 41  ? 157.762 133.978 165.746 1.00 56.05 ?  41  ILE B O     1 
ATOM   5861  C  CB    . ILE B 1 41  ? 154.738 132.977 166.872 1.00 52.78 ?  41  ILE B CB    1 
ATOM   5862  C  CG1   . ILE B 1 41  ? 153.490 132.234 166.397 1.00 50.99 ?  41  ILE B CG1   1 
ATOM   5863  C  CG2   . ILE B 1 41  ? 154.606 134.465 166.594 1.00 51.98 ?  41  ILE B CG2   1 
ATOM   5864  C  CD1   . ILE B 1 41  ? 153.343 132.187 164.896 1.00 49.66 ?  41  ILE B CD1   1 
ATOM   5865  N  N     . ASN B 1 42  ? 157.739 133.018 167.779 1.00 52.27 ?  42  ASN B N     1 
ATOM   5866  C  CA    . ASN B 1 42  ? 158.943 133.729 168.196 1.00 54.55 ?  42  ASN B CA    1 
ATOM   5867  C  C     . ASN B 1 42  ? 160.156 133.302 167.381 1.00 56.60 ?  42  ASN B C     1 
ATOM   5868  O  O     . ASN B 1 42  ? 161.105 134.079 167.232 1.00 58.07 ?  42  ASN B O     1 
ATOM   5869  C  CB    . ASN B 1 42  ? 159.193 133.508 169.686 1.00 55.05 ?  42  ASN B CB    1 
ATOM   5870  C  CG    . ASN B 1 42  ? 158.070 134.048 170.551 1.00 56.64 ?  42  ASN B CG    1 
ATOM   5871  O  OD1   . ASN B 1 42  ? 157.072 134.555 170.042 1.00 59.11 ?  42  ASN B OD1   1 
ATOM   5872  N  ND2   . ASN B 1 42  ? 158.233 133.947 171.864 1.00 58.92 ?  42  ASN B ND2   1 
ATOM   5873  N  N     . GLN B 1 43  ? 160.144 132.079 166.849 1.00 59.89 ?  43  GLN B N     1 
ATOM   5874  C  CA    . GLN B 1 43  ? 161.229 131.633 165.981 1.00 57.85 ?  43  GLN B CA    1 
ATOM   5875  C  C     . GLN B 1 43  ? 161.126 132.248 164.591 1.00 58.98 ?  43  GLN B C     1 
ATOM   5876  O  O     . GLN B 1 43  ? 162.146 132.598 163.988 1.00 61.60 ?  43  GLN B O     1 
ATOM   5877  C  CB    . GLN B 1 43  ? 161.230 130.107 165.885 1.00 57.38 ?  43  GLN B CB    1 
ATOM   5878  C  CG    . GLN B 1 43  ? 162.107 129.414 166.918 1.00 60.30 ?  43  GLN B CG    1 
ATOM   5879  C  CD    . GLN B 1 43  ? 161.615 129.623 168.335 1.00 62.50 ?  43  GLN B CD    1 
ATOM   5880  O  OE1   . GLN B 1 43  ? 160.453 129.960 168.556 1.00 62.16 ?  43  GLN B OE1   1 
ATOM   5881  N  NE2   . GLN B 1 43  ? 162.499 129.427 169.305 1.00 60.18 ?  43  GLN B NE2   1 
ATOM   5882  N  N     . ASN B 1 44  ? 159.908 132.389 164.069 1.00 54.48 ?  44  ASN B N     1 
ATOM   5883  C  CA    . ASN B 1 44  ? 159.690 132.856 162.707 1.00 56.91 ?  44  ASN B CA    1 
ATOM   5884  C  C     . ASN B 1 44  ? 159.345 134.337 162.633 1.00 57.23 ?  44  ASN B C     1 
ATOM   5885  O  O     . ASN B 1 44  ? 158.991 134.825 161.555 1.00 55.75 ?  44  ASN B O     1 
ATOM   5886  C  CB    . ASN B 1 44  ? 158.590 132.029 162.037 1.00 54.58 ?  44  ASN B CB    1 
ATOM   5887  C  CG    . ASN B 1 44  ? 158.988 130.579 161.834 1.00 58.80 ?  44  ASN B CG    1 
ATOM   5888  O  OD1   . ASN B 1 44  ? 159.099 130.108 160.702 1.00 62.13 ?  44  ASN B OD1   1 
ATOM   5889  N  ND2   . ASN B 1 44  ? 159.195 129.859 162.931 1.00 57.89 ?  44  ASN B ND2   1 
ATOM   5890  N  N     . THR B 1 45  ? 159.439 135.062 163.743 1.00 57.35 ?  45  THR B N     1 
ATOM   5891  C  CA    . THR B 1 45  ? 159.190 136.497 163.753 1.00 58.16 ?  45  THR B CA    1 
ATOM   5892  C  C     . THR B 1 45  ? 160.503 137.235 163.521 1.00 57.10 ?  45  THR B C     1 
ATOM   5893  O  O     . THR B 1 45  ? 161.437 137.110 164.318 1.00 58.92 ?  45  THR B O     1 
ATOM   5894  C  CB    . THR B 1 45  ? 158.563 136.938 165.074 1.00 56.69 ?  45  THR B CB    1 
ATOM   5895  O  OG1   . THR B 1 45  ? 157.265 136.347 165.212 1.00 60.69 ?  45  THR B OG1   1 
ATOM   5896  C  CG2   . THR B 1 45  ? 158.435 138.452 165.124 1.00 54.98 ?  45  THR B CG2   1 
ATOM   5897  N  N     . VAL B 1 46  ? 160.573 137.995 162.428 1.00 56.57 ?  46  VAL B N     1 
ATOM   5898  C  CA    . VAL B 1 46  ? 161.746 138.820 162.172 1.00 56.20 ?  46  VAL B CA    1 
ATOM   5899  C  C     . VAL B 1 46  ? 161.833 139.897 163.243 1.00 57.03 ?  46  VAL B C     1 
ATOM   5900  O  O     . VAL B 1 46  ? 160.873 140.642 163.477 1.00 58.62 ?  46  VAL B O     1 
ATOM   5901  C  CB    . VAL B 1 46  ? 161.681 139.439 160.770 1.00 54.12 ?  46  VAL B CB    1 
ATOM   5902  C  CG1   . VAL B 1 46  ? 162.931 140.260 160.497 1.00 54.46 ?  46  VAL B CG1   1 
ATOM   5903  C  CG2   . VAL B 1 46  ? 161.515 138.361 159.724 1.00 54.07 ?  46  VAL B CG2   1 
ATOM   5904  N  N     . PHE B 1 47  ? 162.983 139.984 163.898 1.00 61.45 ?  47  PHE B N     1 
ATOM   5905  C  CA    . PHE B 1 47  ? 163.207 140.962 164.948 1.00 63.31 ?  47  PHE B CA    1 
ATOM   5906  C  C     . PHE B 1 47  ? 164.242 141.978 164.493 1.00 64.07 ?  47  PHE B C     1 
ATOM   5907  O  O     . PHE B 1 47  ? 165.207 141.634 163.804 1.00 63.48 ?  47  PHE B O     1 
ATOM   5908  C  CB    . PHE B 1 47  ? 163.664 140.294 166.245 1.00 62.59 ?  47  PHE B CB    1 
ATOM   5909  C  CG    . PHE B 1 47  ? 163.618 141.202 167.440 1.00 64.31 ?  47  PHE B CG    1 
ATOM   5910  C  CD1   . PHE B 1 47  ? 162.410 141.528 168.031 1.00 62.63 ?  47  PHE B CD1   1 
ATOM   5911  C  CD2   . PHE B 1 47  ? 164.782 141.732 167.969 1.00 63.97 ?  47  PHE B CD2   1 
ATOM   5912  C  CE1   . PHE B 1 47  ? 162.363 142.365 169.129 1.00 64.84 ?  47  PHE B CE1   1 
ATOM   5913  C  CE2   . PHE B 1 47  ? 164.743 142.570 169.067 1.00 63.35 ?  47  PHE B CE2   1 
ATOM   5914  C  CZ    . PHE B 1 47  ? 163.531 142.887 169.648 1.00 64.46 ?  47  PHE B CZ    1 
ATOM   5915  N  N     . PHE B 1 48  ? 164.030 143.231 164.881 1.00 61.83 ?  48  PHE B N     1 
ATOM   5916  C  CA    . PHE B 1 48  ? 164.917 144.329 164.546 1.00 57.75 ?  48  PHE B CA    1 
ATOM   5917  C  C     . PHE B 1 48  ? 165.417 144.969 165.833 1.00 60.79 ?  48  PHE B C     1 
ATOM   5918  O  O     . PHE B 1 48  ? 164.759 144.896 166.875 1.00 61.58 ?  48  PHE B O     1 
ATOM   5919  C  CB    . PHE B 1 48  ? 164.213 145.377 163.674 1.00 58.73 ?  48  PHE B CB    1 
ATOM   5920  C  CG    . PHE B 1 48  ? 163.656 144.829 162.387 1.00 57.73 ?  48  PHE B CG    1 
ATOM   5921  C  CD1   . PHE B 1 48  ? 162.489 144.083 162.377 1.00 57.85 ?  48  PHE B CD1   1 
ATOM   5922  C  CD2   . PHE B 1 48  ? 164.297 145.071 161.185 1.00 60.31 ?  48  PHE B CD2   1 
ATOM   5923  C  CE1   . PHE B 1 48  ? 161.977 143.587 161.196 1.00 59.31 ?  48  PHE B CE1   1 
ATOM   5924  C  CE2   . PHE B 1 48  ? 163.788 144.577 160.001 1.00 60.19 ?  48  PHE B CE2   1 
ATOM   5925  C  CZ    . PHE B 1 48  ? 162.627 143.834 160.007 1.00 57.88 ?  48  PHE B CZ    1 
ATOM   5926  N  N     . HIS B 1 49  ? 166.595 145.590 165.754 1.00 65.61 ?  49  HIS B N     1 
ATOM   5927  C  CA    . HIS B 1 49  ? 167.196 146.183 166.945 1.00 65.59 ?  49  HIS B CA    1 
ATOM   5928  C  C     . HIS B 1 49  ? 166.315 147.286 167.517 1.00 67.22 ?  49  HIS B C     1 
ATOM   5929  O  O     . HIS B 1 49  ? 166.180 147.413 168.740 1.00 67.83 ?  49  HIS B O     1 
ATOM   5930  C  CB    . HIS B 1 49  ? 168.589 146.721 166.617 1.00 66.47 ?  49  HIS B CB    1 
ATOM   5931  C  CG    . HIS B 1 49  ? 169.473 146.871 167.816 1.00 70.11 ?  49  HIS B CG    1 
ATOM   5932  N  ND1   . HIS B 1 49  ? 169.234 147.799 168.807 1.00 69.32 ?  49  HIS B ND1   1 
ATOM   5933  C  CD2   . HIS B 1 49  ? 170.597 146.211 168.183 1.00 69.08 ?  49  HIS B CD2   1 
ATOM   5934  C  CE1   . HIS B 1 49  ? 170.171 147.704 169.733 1.00 68.02 ?  49  HIS B CE1   1 
ATOM   5935  N  NE2   . HIS B 1 49  ? 171.011 146.748 169.378 1.00 68.93 ?  49  HIS B NE2   1 
ATOM   5936  N  N     . ASN B 1 50  ? 165.707 148.091 166.651 1.00 65.61 ?  50  ASN B N     1 
ATOM   5937  C  CA    . ASN B 1 50  ? 164.818 149.160 167.078 1.00 63.02 ?  50  ASN B CA    1 
ATOM   5938  C  C     . ASN B 1 50  ? 163.616 149.207 166.147 1.00 61.96 ?  50  ASN B C     1 
ATOM   5939  O  O     . ASN B 1 50  ? 163.623 148.626 165.059 1.00 61.45 ?  50  ASN B O     1 
ATOM   5940  C  CB    . ASN B 1 50  ? 165.534 150.515 167.097 1.00 61.90 ?  50  ASN B CB    1 
ATOM   5941  C  CG    . ASN B 1 50  ? 166.340 150.766 165.840 1.00 63.89 ?  50  ASN B CG    1 
ATOM   5942  O  OD1   . ASN B 1 50  ? 165.784 151.035 164.777 1.00 64.93 ?  50  ASN B OD1   1 
ATOM   5943  N  ND2   . ASN B 1 50  ? 167.659 150.676 165.956 1.00 64.38 ?  50  ASN B ND2   1 
ATOM   5944  N  N     . LEU B 1 51  ? 162.571 149.904 166.597 1.00 58.68 ?  51  LEU B N     1 
ATOM   5945  C  CA    . LEU B 1 51  ? 161.381 150.069 165.769 1.00 58.75 ?  51  LEU B CA    1 
ATOM   5946  C  C     . LEU B 1 51  ? 161.681 150.878 164.514 1.00 60.56 ?  51  LEU B C     1 
ATOM   5947  O  O     . LEU B 1 51  ? 161.048 150.664 163.474 1.00 62.00 ?  51  LEU B O     1 
ATOM   5948  C  CB    . LEU B 1 51  ? 160.267 150.732 166.579 1.00 58.13 ?  51  LEU B CB    1 
ATOM   5949  C  CG    . LEU B 1 51  ? 158.973 151.080 165.842 1.00 57.06 ?  51  LEU B CG    1 
ATOM   5950  C  CD1   . LEU B 1 51  ? 158.347 149.840 165.224 1.00 54.72 ?  51  LEU B CD1   1 
ATOM   5951  C  CD2   . LEU B 1 51  ? 157.998 151.767 166.777 1.00 57.42 ?  51  LEU B CD2   1 
ATOM   5952  N  N     . LYS B 1 52  ? 162.637 151.808 164.590 1.00 59.05 ?  52  LYS B N     1 
ATOM   5953  C  CA    . LYS B 1 52  ? 162.998 152.600 163.418 1.00 57.11 ?  52  LYS B CA    1 
ATOM   5954  C  C     . LYS B 1 52  ? 163.535 151.717 162.300 1.00 60.44 ?  52  LYS B C     1 
ATOM   5955  O  O     . LYS B 1 52  ? 163.174 151.896 161.130 1.00 61.28 ?  52  LYS B O     1 
ATOM   5956  C  CB    . LYS B 1 52  ? 164.027 153.661 163.803 1.00 56.54 ?  52  LYS B CB    1 
ATOM   5957  C  CG    . LYS B 1 52  ? 163.981 154.916 162.952 1.00 60.79 ?  52  LYS B CG    1 
ATOM   5958  C  CD    . LYS B 1 52  ? 165.139 155.843 163.284 1.00 63.71 ?  52  LYS B CD    1 
ATOM   5959  C  CE    . LYS B 1 52  ? 164.857 156.657 164.535 1.00 60.86 ?  52  LYS B CE    1 
ATOM   5960  N  NZ    . LYS B 1 52  ? 166.018 156.671 165.466 1.00 61.13 1  52  LYS B NZ    1 
ATOM   5961  N  N     . GLU B 1 53  ? 164.400 150.759 162.641 1.00 62.10 ?  53  GLU B N     1 
ATOM   5962  C  CA    . GLU B 1 53  ? 164.939 149.855 161.630 1.00 60.79 ?  53  GLU B CA    1 
ATOM   5963  C  C     . GLU B 1 53  ? 163.838 149.007 161.007 1.00 61.00 ?  53  GLU B C     1 
ATOM   5964  O  O     . GLU B 1 53  ? 163.820 148.799 159.788 1.00 61.80 ?  53  GLU B O     1 
ATOM   5965  C  CB    . GLU B 1 53  ? 166.019 148.967 162.244 1.00 60.31 ?  53  GLU B CB    1 
ATOM   5966  C  CG    . GLU B 1 53  ? 166.953 148.334 161.227 1.00 62.43 ?  53  GLU B CG    1 
ATOM   5967  C  CD    . GLU B 1 53  ? 167.230 146.873 161.518 1.00 65.53 ?  53  GLU B CD    1 
ATOM   5968  O  OE1   . GLU B 1 53  ? 167.397 146.523 162.705 1.00 66.13 ?  53  GLU B OE1   1 
ATOM   5969  O  OE2   . GLU B 1 53  ? 167.281 146.075 160.559 1.00 64.07 -1 53  GLU B OE2   1 
ATOM   5970  N  N     . LYS B 1 54  ? 162.909 148.513 161.829 1.00 58.53 ?  54  LYS B N     1 
ATOM   5971  C  CA    . LYS B 1 54  ? 161.803 147.714 161.309 1.00 58.25 ?  54  LYS B CA    1 
ATOM   5972  C  C     . LYS B 1 54  ? 160.936 148.534 160.363 1.00 54.87 ?  54  LYS B C     1 
ATOM   5973  O  O     . LYS B 1 54  ? 160.567 148.069 159.277 1.00 56.61 ?  54  LYS B O     1 
ATOM   5974  C  CB    . LYS B 1 54  ? 160.966 147.169 162.464 1.00 56.86 ?  54  LYS B CB    1 
ATOM   5975  C  CG    . LYS B 1 54  ? 159.644 146.560 162.031 1.00 56.41 ?  54  LYS B CG    1 
ATOM   5976  C  CD    . LYS B 1 54  ? 158.974 145.821 163.172 1.00 57.38 ?  54  LYS B CD    1 
ATOM   5977  C  CE    . LYS B 1 54  ? 157.657 145.211 162.729 1.00 59.39 ?  54  LYS B CE    1 
ATOM   5978  N  NZ    . LYS B 1 54  ? 157.236 144.097 163.623 1.00 59.58 1  54  LYS B NZ    1 
ATOM   5979  N  N     . LEU B 1 55  ? 160.606 149.763 160.760 1.00 55.55 ?  55  LEU B N     1 
ATOM   5980  C  CA    . LEU B 1 55  ? 159.773 150.612 159.916 1.00 56.17 ?  55  LEU B CA    1 
ATOM   5981  C  C     . LEU B 1 55  ? 160.474 150.946 158.608 1.00 59.21 ?  55  LEU B C     1 
ATOM   5982  O  O     . LEU B 1 55  ? 159.847 150.932 157.543 1.00 63.12 ?  55  LEU B O     1 
ATOM   5983  C  CB    . LEU B 1 55  ? 159.397 151.888 160.667 1.00 57.73 ?  55  LEU B CB    1 
ATOM   5984  C  CG    . LEU B 1 55  ? 158.356 151.723 161.773 1.00 57.81 ?  55  LEU B CG    1 
ATOM   5985  C  CD1   . LEU B 1 55  ? 158.193 153.019 162.541 1.00 58.16 ?  55  LEU B CD1   1 
ATOM   5986  C  CD2   . LEU B 1 55  ? 157.025 151.264 161.195 1.00 57.18 ?  55  LEU B CD2   1 
ATOM   5987  N  N     . ASP B 1 56  ? 161.774 151.249 158.669 1.00 60.82 ?  56  ASP B N     1 
ATOM   5988  C  CA    . ASP B 1 56  ? 162.528 151.548 157.457 1.00 60.69 ?  56  ASP B CA    1 
ATOM   5989  C  C     . ASP B 1 56  ? 162.582 150.341 156.530 1.00 59.63 ?  56  ASP B C     1 
ATOM   5990  O  O     . ASP B 1 56  ? 162.406 150.474 155.312 1.00 62.40 ?  56  ASP B O     1 
ATOM   5991  C  CB    . ASP B 1 56  ? 163.939 152.011 157.819 1.00 62.18 ?  56  ASP B CB    1 
ATOM   5992  C  CG    . ASP B 1 56  ? 164.030 153.512 158.000 1.00 64.79 ?  56  ASP B CG    1 
ATOM   5993  O  OD1   . ASP B 1 56  ? 164.980 153.974 158.666 1.00 65.13 ?  56  ASP B OD1   1 
ATOM   5994  O  OD2   . ASP B 1 56  ? 163.153 154.229 157.476 1.00 63.28 -1 56  ASP B OD2   1 
ATOM   5995  N  N     . TYR B 1 57  ? 162.815 149.151 157.091 1.00 55.20 ?  57  TYR B N     1 
ATOM   5996  C  CA    . TYR B 1 57  ? 162.816 147.937 156.284 1.00 56.47 ?  57  TYR B CA    1 
ATOM   5997  C  C     . TYR B 1 57  ? 161.460 147.713 155.631 1.00 57.12 ?  57  TYR B C     1 
ATOM   5998  O  O     . TYR B 1 57  ? 161.384 147.310 154.466 1.00 58.36 ?  57  TYR B O     1 
ATOM   5999  C  CB    . TYR B 1 57  ? 163.199 146.734 157.148 1.00 57.82 ?  57  TYR B CB    1 
ATOM   6000  C  CG    . TYR B 1 57  ? 163.054 145.397 156.451 1.00 57.26 ?  57  TYR B CG    1 
ATOM   6001  C  CD1   . TYR B 1 57  ? 164.072 144.894 155.654 1.00 57.59 ?  57  TYR B CD1   1 
ATOM   6002  C  CD2   . TYR B 1 57  ? 161.903 144.634 156.601 1.00 58.80 ?  57  TYR B CD2   1 
ATOM   6003  C  CE1   . TYR B 1 57  ? 163.944 143.674 155.018 1.00 57.28 ?  57  TYR B CE1   1 
ATOM   6004  C  CE2   . TYR B 1 57  ? 161.766 143.417 155.969 1.00 59.93 ?  57  TYR B CE2   1 
ATOM   6005  C  CZ    . TYR B 1 57  ? 162.790 142.940 155.180 1.00 60.41 ?  57  TYR B CZ    1 
ATOM   6006  O  OH    . TYR B 1 57  ? 162.655 141.724 154.551 1.00 60.67 ?  57  TYR B OH    1 
ATOM   6007  N  N     . LEU B 1 58  ? 160.378 147.968 156.366 1.00 55.53 ?  58  LEU B N     1 
ATOM   6008  C  CA    . LEU B 1 58  ? 159.052 147.703 155.823 1.00 55.09 ?  58  LEU B CA    1 
ATOM   6009  C  C     . LEU B 1 58  ? 158.678 148.702 154.734 1.00 52.51 ?  58  LEU B C     1 
ATOM   6010  O  O     . LEU B 1 58  ? 158.080 148.321 153.722 1.00 54.87 ?  58  LEU B O     1 
ATOM   6011  C  CB    . LEU B 1 58  ? 158.020 147.697 156.950 1.00 53.67 ?  58  LEU B CB    1 
ATOM   6012  C  CG    . LEU B 1 58  ? 158.150 146.479 157.871 1.00 53.10 ?  58  LEU B CG    1 
ATOM   6013  C  CD1   . LEU B 1 58  ? 157.345 146.648 159.145 1.00 53.31 ?  58  LEU B CD1   1 
ATOM   6014  C  CD2   . LEU B 1 58  ? 157.742 145.210 157.142 1.00 51.72 ?  58  LEU B CD2   1 
ATOM   6015  N  N     . VAL B 1 59  ? 159.013 149.983 154.911 1.00 55.94 ?  59  VAL B N     1 
ATOM   6016  C  CA    . VAL B 1 59  ? 158.657 150.955 153.879 1.00 59.41 ?  59  VAL B CA    1 
ATOM   6017  C  C     . VAL B 1 59  ? 159.537 150.777 152.647 1.00 61.68 ?  59  VAL B C     1 
ATOM   6018  O  O     . VAL B 1 59  ? 159.054 150.841 151.511 1.00 58.99 ?  59  VAL B O     1 
ATOM   6019  C  CB    . VAL B 1 59  ? 158.726 152.401 154.409 1.00 58.77 ?  59  VAL B CB    1 
ATOM   6020  C  CG1   . VAL B 1 59  ? 157.509 152.718 155.273 1.00 57.57 ?  59  VAL B CG1   1 
ATOM   6021  C  CG2   . VAL B 1 59  ? 160.035 152.686 155.120 1.00 59.07 ?  59  VAL B CG2   1 
ATOM   6022  N  N     . GLU B 1 60  ? 160.840 150.549 152.846 1.00 62.25 ?  60  GLU B N     1 
ATOM   6023  C  CA    . GLU B 1 60  ? 161.757 150.498 151.712 1.00 60.57 ?  60  GLU B CA    1 
ATOM   6024  C  C     . GLU B 1 60  ? 161.644 149.198 150.926 1.00 61.73 ?  60  GLU B C     1 
ATOM   6025  O  O     . GLU B 1 60  ? 161.957 149.177 149.731 1.00 64.04 ?  60  GLU B O     1 
ATOM   6026  C  CB    . GLU B 1 60  ? 163.196 150.716 152.191 1.00 60.61 ?  60  GLU B CB    1 
ATOM   6027  C  CG    . GLU B 1 60  ? 163.928 149.460 152.625 1.00 61.74 ?  60  GLU B CG    1 
ATOM   6028  C  CD    . GLU B 1 60  ? 165.165 149.764 153.448 1.00 64.83 ?  60  GLU B CD    1 
ATOM   6029  O  OE1   . GLU B 1 60  ? 165.460 150.959 153.663 1.00 64.26 ?  60  GLU B OE1   1 
ATOM   6030  O  OE2   . GLU B 1 60  ? 165.841 148.809 153.883 1.00 61.61 -1 60  GLU B OE2   1 
ATOM   6031  N  N     . ASN B 1 61  ? 161.203 148.111 151.560 1.00 57.46 ?  61  ASN B N     1 
ATOM   6032  C  CA    . ASN B 1 61  ? 161.026 146.836 150.880 1.00 57.98 ?  61  ASN B CA    1 
ATOM   6033  C  C     . ASN B 1 61  ? 159.616 146.653 150.332 1.00 57.86 ?  61  ASN B C     1 
ATOM   6034  O  O     . ASN B 1 61  ? 159.196 145.513 150.099 1.00 59.49 ?  61  ASN B O     1 
ATOM   6035  C  CB    . ASN B 1 61  ? 161.379 145.677 151.815 1.00 59.20 ?  61  ASN B CB    1 
ATOM   6036  C  CG    . ASN B 1 61  ? 162.871 145.449 151.918 1.00 61.20 ?  61  ASN B CG    1 
ATOM   6037  O  OD1   . ASN B 1 61  ? 163.430 144.597 151.227 1.00 60.39 ?  61  ASN B OD1   1 
ATOM   6038  N  ND2   . ASN B 1 61  ? 163.527 146.211 152.784 1.00 60.53 ?  61  ASN B ND2   1 
ATOM   6039  N  N     . GLN B 1 62  ? 158.880 147.747 150.134 1.00 56.47 ?  62  GLN B N     1 
ATOM   6040  C  CA    . GLN B 1 62  ? 157.555 147.722 149.511 1.00 58.76 ?  62  GLN B CA    1 
ATOM   6041  C  C     . GLN B 1 62  ? 156.565 146.882 150.315 1.00 57.86 ?  62  GLN B C     1 
ATOM   6042  O  O     . GLN B 1 62  ? 155.776 146.117 149.757 1.00 59.50 ?  62  GLN B O     1 
ATOM   6043  C  CB    . GLN B 1 62  ? 157.636 147.230 148.063 1.00 58.26 ?  62  GLN B CB    1 
ATOM   6044  C  CG    . GLN B 1 62  ? 158.588 148.028 147.188 1.00 58.23 ?  62  GLN B CG    1 
ATOM   6045  C  CD    . GLN B 1 62  ? 158.254 149.506 147.160 1.00 61.67 ?  62  GLN B CD    1 
ATOM   6046  O  OE1   . GLN B 1 62  ? 158.845 150.303 147.889 1.00 60.56 ?  62  GLN B OE1   1 
ATOM   6047  N  NE2   . GLN B 1 62  ? 157.300 149.880 146.317 1.00 59.67 ?  62  GLN B NE2   1 
ATOM   6048  N  N     . TYR B 1 63  ? 156.602 147.026 151.638 1.00 56.30 ?  63  TYR B N     1 
ATOM   6049  C  CA    . TYR B 1 63  ? 155.630 146.385 152.515 1.00 55.71 ?  63  TYR B CA    1 
ATOM   6050  C  C     . TYR B 1 63  ? 154.591 147.359 153.049 1.00 54.98 ?  63  TYR B C     1 
ATOM   6051  O  O     . TYR B 1 63  ? 153.408 147.015 153.125 1.00 55.89 ?  63  TYR B O     1 
ATOM   6052  C  CB    . TYR B 1 63  ? 156.334 145.706 153.694 1.00 52.99 ?  63  TYR B CB    1 
ATOM   6053  C  CG    . TYR B 1 63  ? 157.051 144.428 153.331 1.00 55.76 ?  63  TYR B CG    1 
ATOM   6054  C  CD1   . TYR B 1 63  ? 156.370 143.372 152.740 1.00 53.23 ?  63  TYR B CD1   1 
ATOM   6055  C  CD2   . TYR B 1 63  ? 158.407 144.274 153.584 1.00 55.99 ?  63  TYR B CD2   1 
ATOM   6056  C  CE1   . TYR B 1 63  ? 157.021 142.203 152.409 1.00 54.08 ?  63  TYR B CE1   1 
ATOM   6057  C  CE2   . TYR B 1 63  ? 159.064 143.109 153.257 1.00 55.25 ?  63  TYR B CE2   1 
ATOM   6058  C  CZ    . TYR B 1 63  ? 158.368 142.076 152.670 1.00 58.33 ?  63  TYR B CZ    1 
ATOM   6059  O  OH    . TYR B 1 63  ? 159.023 140.912 152.342 1.00 61.61 ?  63  TYR B OH    1 
ATOM   6060  N  N     . TYR B 1 64  ? 155.004 148.566 153.415 1.00 51.12 ?  64  TYR B N     1 
ATOM   6061  C  CA    . TYR B 1 64  ? 154.117 149.595 153.933 1.00 49.36 ?  64  TYR B CA    1 
ATOM   6062  C  C     . TYR B 1 64  ? 153.997 150.738 152.935 1.00 51.84 ?  64  TYR B C     1 
ATOM   6063  O  O     . TYR B 1 64  ? 154.666 150.771 151.899 1.00 56.22 ?  64  TYR B O     1 
ATOM   6064  C  CB    . TYR B 1 64  ? 154.626 150.131 155.275 1.00 51.22 ?  64  TYR B CB    1 
ATOM   6065  C  CG    . TYR B 1 64  ? 154.361 149.226 156.450 1.00 49.14 ?  64  TYR B CG    1 
ATOM   6066  C  CD1   . TYR B 1 64  ? 153.612 148.067 156.306 1.00 47.95 ?  64  TYR B CD1   1 
ATOM   6067  C  CD2   . TYR B 1 64  ? 154.858 149.532 157.706 1.00 50.77 ?  64  TYR B CD2   1 
ATOM   6068  C  CE1   . TYR B 1 64  ? 153.370 147.238 157.381 1.00 45.37 ?  64  TYR B CE1   1 
ATOM   6069  C  CE2   . TYR B 1 64  ? 154.621 148.713 158.784 1.00 50.87 ?  64  TYR B CE2   1 
ATOM   6070  C  CZ    . TYR B 1 64  ? 153.877 147.566 158.617 1.00 50.19 ?  64  TYR B CZ    1 
ATOM   6071  O  OH    . TYR B 1 64  ? 153.642 146.749 159.696 1.00 55.95 ?  64  TYR B OH    1 
ATOM   6072  N  N     . GLU B 1 65  ? 153.129 151.686 153.268 1.00 56.36 ?  65  GLU B N     1 
ATOM   6073  C  CA    . GLU B 1 65  ? 152.981 152.918 152.510 1.00 57.07 ?  65  GLU B CA    1 
ATOM   6074  C  C     . GLU B 1 65  ? 153.657 154.052 153.270 1.00 58.36 ?  65  GLU B C     1 
ATOM   6075  O  O     . GLU B 1 65  ? 153.371 154.269 154.451 1.00 59.05 ?  65  GLU B O     1 
ATOM   6076  C  CB    . GLU B 1 65  ? 151.506 153.247 152.273 1.00 54.02 ?  65  GLU B CB    1 
ATOM   6077  C  CG    . GLU B 1 65  ? 150.779 152.253 151.386 1.00 52.75 ?  65  GLU B CG    1 
ATOM   6078  C  CD    . GLU B 1 65  ? 149.280 152.486 151.359 1.00 59.36 ?  65  GLU B CD    1 
ATOM   6079  O  OE1   . GLU B 1 65  ? 148.682 152.650 152.443 1.00 59.54 ?  65  GLU B OE1   1 
ATOM   6080  O  OE2   . GLU B 1 65  ? 148.700 152.508 150.253 1.00 56.85 -1 65  GLU B OE2   1 
ATOM   6081  N  N     . GLU B 1 66  ? 154.558 154.763 152.592 1.00 58.13 ?  66  GLU B N     1 
ATOM   6082  C  CA    . GLU B 1 66  ? 155.250 155.874 153.232 1.00 59.42 ?  66  GLU B CA    1 
ATOM   6083  C  C     . GLU B 1 66  ? 154.338 157.073 153.450 1.00 60.55 ?  66  GLU B C     1 
ATOM   6084  O  O     . GLU B 1 66  ? 154.646 157.926 154.289 1.00 58.82 ?  66  GLU B O     1 
ATOM   6085  C  CB    . GLU B 1 66  ? 156.466 156.283 152.396 1.00 61.14 ?  66  GLU B CB    1 
ATOM   6086  C  CG    . GLU B 1 66  ? 157.482 157.182 153.104 1.00 61.57 ?  66  GLU B CG    1 
ATOM   6087  C  CD    . GLU B 1 66  ? 157.824 156.722 154.512 1.00 65.09 ?  66  GLU B CD    1 
ATOM   6088  O  OE1   . GLU B 1 66  ? 157.070 157.042 155.456 1.00 63.13 ?  66  GLU B OE1   1 
ATOM   6089  O  OE2   . GLU B 1 66  ? 158.857 156.038 154.677 1.00 62.81 -1 66  GLU B OE2   1 
ATOM   6090  N  N     . GLU B 1 67  ? 153.220 157.153 152.724 1.00 58.11 ?  67  GLU B N     1 
ATOM   6091  C  CA    . GLU B 1 67  ? 152.362 158.331 152.801 1.00 55.39 ?  67  GLU B CA    1 
ATOM   6092  C  C     . GLU B 1 67  ? 151.737 158.480 154.183 1.00 59.38 ?  67  GLU B C     1 
ATOM   6093  O  O     . GLU B 1 67  ? 151.800 159.557 154.789 1.00 60.34 ?  67  GLU B O     1 
ATOM   6094  C  CB    . GLU B 1 67  ? 151.276 158.257 151.728 1.00 57.45 ?  67  GLU B CB    1 
ATOM   6095  C  CG    . GLU B 1 67  ? 151.812 158.171 150.310 1.00 58.19 ?  67  GLU B CG    1 
ATOM   6096  C  CD    . GLU B 1 67  ? 151.865 156.748 149.793 1.00 61.21 ?  67  GLU B CD    1 
ATOM   6097  O  OE1   . GLU B 1 67  ? 150.790 156.169 149.531 1.00 62.20 ?  67  GLU B OE1   1 
ATOM   6098  O  OE2   . GLU B 1 67  ? 152.982 156.209 149.647 1.00 62.48 -1 67  GLU B OE2   1 
ATOM   6099  N  N     . PHE B 1 68  ? 151.128 157.412 154.701 1.00 53.85 ?  68  PHE B N     1 
ATOM   6100  C  CA    . PHE B 1 68  ? 150.445 157.513 155.986 1.00 49.12 ?  68  PHE B CA    1 
ATOM   6101  C  C     . PHE B 1 68  ? 151.419 157.543 157.155 1.00 50.48 ?  68  PHE B C     1 
ATOM   6102  O  O     . PHE B 1 68  ? 151.124 158.161 158.183 1.00 54.75 ?  68  PHE B O     1 
ATOM   6103  C  CB    . PHE B 1 68  ? 149.437 156.368 156.143 1.00 49.06 ?  68  PHE B CB    1 
ATOM   6104  C  CG    . PHE B 1 68  ? 150.013 155.112 156.739 1.00 45.75 ?  68  PHE B CG    1 
ATOM   6105  C  CD1   . PHE B 1 68  ? 150.645 154.179 155.938 1.00 48.64 ?  68  PHE B CD1   1 
ATOM   6106  C  CD2   . PHE B 1 68  ? 149.892 154.850 158.094 1.00 45.10 ?  68  PHE B CD2   1 
ATOM   6107  C  CE1   . PHE B 1 68  ? 151.169 153.021 156.480 1.00 48.69 ?  68  PHE B CE1   1 
ATOM   6108  C  CE2   . PHE B 1 68  ? 150.414 153.694 158.640 1.00 47.79 ?  68  PHE B CE2   1 
ATOM   6109  C  CZ    . PHE B 1 68  ? 151.049 152.778 157.830 1.00 48.99 ?  68  PHE B CZ    1 
ATOM   6110  N  N     . LEU B 1 69  ? 152.576 156.890 157.026 1.00 48.84 ?  69  LEU B N     1 
ATOM   6111  C  CA    . LEU B 1 69  ? 153.559 156.916 158.102 1.00 50.00 ?  69  LEU B CA    1 
ATOM   6112  C  C     . LEU B 1 69  ? 154.284 158.253 158.182 1.00 53.07 ?  69  LEU B C     1 
ATOM   6113  O  O     . LEU B 1 69  ? 154.737 158.642 159.264 1.00 50.57 ?  69  LEU B O     1 
ATOM   6114  C  CB    . LEU B 1 69  ? 154.567 155.782 157.927 1.00 50.19 ?  69  LEU B CB    1 
ATOM   6115  C  CG    . LEU B 1 69  ? 154.112 154.415 158.438 1.00 49.96 ?  69  LEU B CG    1 
ATOM   6116  C  CD1   . LEU B 1 69  ? 155.101 153.331 158.044 1.00 50.10 ?  69  LEU B CD1   1 
ATOM   6117  C  CD2   . LEU B 1 69  ? 153.916 154.448 159.944 1.00 50.65 ?  69  LEU B CD2   1 
ATOM   6118  N  N     . SER B 1 70  ? 154.401 158.966 157.060 1.00 57.68 ?  70  SER B N     1 
ATOM   6119  C  CA    . SER B 1 70  ? 155.047 160.274 157.071 1.00 54.92 ?  70  SER B CA    1 
ATOM   6120  C  C     . SER B 1 70  ? 154.223 161.320 157.806 1.00 51.98 ?  70  SER B C     1 
ATOM   6121  O  O     . SER B 1 70  ? 154.750 162.390 158.129 1.00 53.93 ?  70  SER B O     1 
ATOM   6122  C  CB    . SER B 1 70  ? 155.316 160.743 155.641 1.00 53.34 ?  70  SER B CB    1 
ATOM   6123  O  OG    . SER B 1 70  ? 154.136 160.694 154.861 1.00 54.26 ?  70  SER B OG    1 
ATOM   6124  N  N     . LEU B 1 71  ? 152.947 161.040 158.072 1.00 46.56 ?  71  LEU B N     1 
ATOM   6125  C  CA    . LEU B 1 71  ? 152.088 161.985 158.773 1.00 46.13 ?  71  LEU B CA    1 
ATOM   6126  C  C     . LEU B 1 71  ? 152.448 162.128 160.244 1.00 47.72 ?  71  LEU B C     1 
ATOM   6127  O  O     . LEU B 1 71  ? 151.949 163.050 160.897 1.00 50.28 ?  71  LEU B O     1 
ATOM   6128  C  CB    . LEU B 1 71  ? 150.627 161.556 158.638 1.00 46.23 ?  71  LEU B CB    1 
ATOM   6129  C  CG    . LEU B 1 71  ? 149.981 161.801 157.273 1.00 50.87 ?  71  LEU B CG    1 
ATOM   6130  C  CD1   . LEU B 1 71  ? 148.471 161.783 157.388 1.00 48.61 ?  71  LEU B CD1   1 
ATOM   6131  C  CD2   . LEU B 1 71  ? 150.459 163.115 156.680 1.00 49.17 ?  71  LEU B CD2   1 
ATOM   6132  N  N     . TYR B 1 72  ? 153.293 161.251 160.776 1.00 45.28 ?  72  TYR B N     1 
ATOM   6133  C  CA    . TYR B 1 72  ? 153.706 161.291 162.169 1.00 44.42 ?  72  TYR B CA    1 
ATOM   6134  C  C     . TYR B 1 72  ? 155.219 161.416 162.255 1.00 48.54 ?  72  TYR B C     1 
ATOM   6135  O  O     . TYR B 1 72  ? 155.945 160.865 161.421 1.00 50.77 ?  72  TYR B O     1 
ATOM   6136  C  CB    . TYR B 1 72  ? 153.274 160.029 162.927 1.00 46.60 ?  72  TYR B CB    1 
ATOM   6137  C  CG    . TYR B 1 72  ? 151.838 159.614 162.722 1.00 44.13 ?  72  TYR B CG    1 
ATOM   6138  C  CD1   . TYR B 1 72  ? 151.474 158.813 161.649 1.00 40.51 ?  72  TYR B CD1   1 
ATOM   6139  C  CD2   . TYR B 1 72  ? 150.850 160.001 163.615 1.00 45.33 ?  72  TYR B CD2   1 
ATOM   6140  C  CE1   . TYR B 1 72  ? 150.168 158.428 161.460 1.00 40.64 ?  72  TYR B CE1   1 
ATOM   6141  C  CE2   . TYR B 1 72  ? 149.539 159.616 163.436 1.00 41.64 ?  72  TYR B CE2   1 
ATOM   6142  C  CZ    . TYR B 1 72  ? 149.204 158.829 162.356 1.00 42.12 ?  72  TYR B CZ    1 
ATOM   6143  O  OH    . TYR B 1 72  ? 147.900 158.443 162.171 1.00 47.11 ?  72  TYR B OH    1 
ATOM   6144  N  N     . SER B 1 73  ? 155.689 162.142 163.263 1.00 54.10 ?  73  SER B N     1 
ATOM   6145  C  CA    . SER B 1 73  ? 157.082 162.021 163.657 1.00 54.69 ?  73  SER B CA    1 
ATOM   6146  C  C     . SER B 1 73  ? 157.323 160.626 164.218 1.00 54.99 ?  73  SER B C     1 
ATOM   6147  O  O     . SER B 1 73  ? 156.410 159.983 164.744 1.00 58.63 ?  73  SER B O     1 
ATOM   6148  C  CB    . SER B 1 73  ? 157.444 163.083 164.694 1.00 53.07 ?  73  SER B CB    1 
ATOM   6149  O  OG    . SER B 1 73  ? 156.825 162.809 165.938 1.00 51.89 ?  73  SER B OG    1 
ATOM   6150  N  N     . PHE B 1 74  ? 158.562 160.146 164.090 1.00 56.10 ?  74  PHE B N     1 
ATOM   6151  C  CA    . PHE B 1 74  ? 158.850 158.788 164.539 1.00 55.84 ?  74  PHE B CA    1 
ATOM   6152  C  C     . PHE B 1 74  ? 158.601 158.620 166.033 1.00 55.08 ?  74  PHE B C     1 
ATOM   6153  O  O     . PHE B 1 74  ? 158.317 157.509 166.490 1.00 60.39 ?  74  PHE B O     1 
ATOM   6154  C  CB    . PHE B 1 74  ? 160.286 158.391 164.209 1.00 56.32 ?  74  PHE B CB    1 
ATOM   6155  C  CG    . PHE B 1 74  ? 160.681 157.066 164.791 1.00 57.06 ?  74  PHE B CG    1 
ATOM   6156  C  CD1   . PHE B 1 74  ? 160.130 155.894 164.302 1.00 56.22 ?  74  PHE B CD1   1 
ATOM   6157  C  CD2   . PHE B 1 74  ? 161.571 156.992 165.849 1.00 57.99 ?  74  PHE B CD2   1 
ATOM   6158  C  CE1   . PHE B 1 74  ? 160.475 154.674 164.841 1.00 58.61 ?  74  PHE B CE1   1 
ATOM   6159  C  CE2   . PHE B 1 74  ? 161.920 155.774 166.392 1.00 57.74 ?  74  PHE B CE2   1 
ATOM   6160  C  CZ    . PHE B 1 74  ? 161.370 154.613 165.888 1.00 59.91 ?  74  PHE B CZ    1 
ATOM   6161  N  N     . GLU B 1 75  ? 158.702 159.702 166.808 1.00 54.53 ?  75  GLU B N     1 
ATOM   6162  C  CA    . GLU B 1 75  ? 158.395 159.611 168.231 1.00 58.15 ?  75  GLU B CA    1 
ATOM   6163  C  C     . GLU B 1 75  ? 156.935 159.238 168.452 1.00 60.11 ?  75  GLU B C     1 
ATOM   6164  O  O     . GLU B 1 75  ? 156.618 158.423 169.326 1.00 60.42 ?  75  GLU B O     1 
ATOM   6165  C  CB    . GLU B 1 75  ? 158.726 160.931 168.925 1.00 56.36 ?  75  GLU B CB    1 
ATOM   6166  C  CG    . GLU B 1 75  ? 160.211 161.245 168.972 1.00 56.59 ?  75  GLU B CG    1 
ATOM   6167  C  CD    . GLU B 1 75  ? 161.034 160.084 169.496 1.00 63.42 ?  75  GLU B CD    1 
ATOM   6168  O  OE1   . GLU B 1 75  ? 160.806 159.666 170.651 1.00 63.49 ?  75  GLU B OE1   1 
ATOM   6169  O  OE2   . GLU B 1 75  ? 161.907 159.589 168.754 1.00 62.13 -1 75  GLU B OE2   1 
ATOM   6170  N  N     . ASP B 1 76  ? 156.030 159.820 167.664 1.00 55.72 ?  76  ASP B N     1 
ATOM   6171  C  CA    . ASP B 1 76  ? 154.613 159.498 167.795 1.00 54.37 ?  76  ASP B CA    1 
ATOM   6172  C  C     . ASP B 1 76  ? 154.338 158.044 167.431 1.00 55.43 ?  76  ASP B C     1 
ATOM   6173  O  O     . ASP B 1 76  ? 153.559 157.363 168.108 1.00 58.92 ?  76  ASP B O     1 
ATOM   6174  C  CB    . ASP B 1 76  ? 153.784 160.438 166.922 1.00 55.73 ?  76  ASP B CB    1 
ATOM   6175  C  CG    . ASP B 1 76  ? 153.892 161.883 167.360 1.00 58.99 ?  76  ASP B CG    1 
ATOM   6176  O  OD1   . ASP B 1 76  ? 153.925 162.134 168.583 1.00 59.14 ?  76  ASP B OD1   1 
ATOM   6177  O  OD2   . ASP B 1 76  ? 153.939 162.770 166.483 1.00 58.03 -1 76  ASP B OD2   1 
ATOM   6178  N  N     . ILE B 1 77  ? 154.965 157.552 166.360 1.00 48.13 ?  77  ILE B N     1 
ATOM   6179  C  CA    . ILE B 1 77  ? 154.793 156.153 165.974 1.00 49.21 ?  77  ILE B CA    1 
ATOM   6180  C  C     . ILE B 1 77  ? 155.347 155.233 167.054 1.00 50.79 ?  77  ILE B C     1 
ATOM   6181  O  O     . ILE B 1 77  ? 154.763 154.187 167.363 1.00 54.21 ?  77  ILE B O     1 
ATOM   6182  C  CB    . ILE B 1 77  ? 155.458 155.892 164.610 1.00 49.26 ?  77  ILE B CB    1 
ATOM   6183  C  CG1   . ILE B 1 77  ? 154.820 156.768 163.533 1.00 49.08 ?  77  ILE B CG1   1 
ATOM   6184  C  CG2   . ILE B 1 77  ? 155.341 154.427 164.232 1.00 49.31 ?  77  ILE B CG2   1 
ATOM   6185  C  CD1   . ILE B 1 77  ? 155.614 156.829 162.255 1.00 50.74 ?  77  ILE B CD1   1 
ATOM   6186  N  N     . LYS B 1 78  ? 156.487 155.606 167.636 1.00 52.56 ?  78  LYS B N     1 
ATOM   6187  C  CA    . LYS B 1 78  ? 157.066 154.814 168.714 1.00 51.80 ?  78  LYS B CA    1 
ATOM   6188  C  C     . LYS B 1 78  ? 156.139 154.769 169.919 1.00 52.98 ?  78  LYS B C     1 
ATOM   6189  O  O     . LYS B 1 78  ? 155.979 153.719 170.546 1.00 56.49 ?  78  LYS B O     1 
ATOM   6190  C  CB    . LYS B 1 78  ? 158.432 155.379 169.101 1.00 55.18 ?  78  LYS B CB    1 
ATOM   6191  C  CG    . LYS B 1 78  ? 159.163 154.569 170.154 1.00 54.95 ?  78  LYS B CG    1 
ATOM   6192  C  CD    . LYS B 1 78  ? 160.586 154.268 169.721 1.00 55.76 ?  78  LYS B CD    1 
ATOM   6193  C  CE    . LYS B 1 78  ? 161.593 154.766 170.742 1.00 57.25 ?  78  LYS B CE    1 
ATOM   6194  N  NZ    . LYS B 1 78  ? 162.995 154.575 170.279 1.00 55.90 1  78  LYS B NZ    1 
ATOM   6195  N  N     . GLU B 1 79  ? 155.514 155.899 170.257 1.00 53.27 ?  79  GLU B N     1 
ATOM   6196  C  CA    . GLU B 1 79  ? 154.572 155.905 171.374 1.00 52.11 ?  79  GLU B CA    1 
ATOM   6197  C  C     . GLU B 1 79  ? 153.317 155.100 171.060 1.00 51.11 ?  79  GLU B C     1 
ATOM   6198  O  O     . GLU B 1 79  ? 152.752 154.465 171.957 1.00 52.30 ?  79  GLU B O     1 
ATOM   6199  C  CB    . GLU B 1 79  ? 154.208 157.341 171.753 1.00 52.64 ?  79  GLU B CB    1 
ATOM   6200  C  CG    . GLU B 1 79  ? 155.380 158.204 172.225 1.00 56.29 ?  79  GLU B CG    1 
ATOM   6201  C  CD    . GLU B 1 79  ? 156.437 157.439 173.015 1.00 58.47 ?  79  GLU B CD    1 
ATOM   6202  O  OE1   . GLU B 1 79  ? 157.639 157.707 172.801 1.00 56.16 ?  79  GLU B OE1   1 
ATOM   6203  O  OE2   . GLU B 1 79  ? 156.080 156.612 173.882 1.00 57.13 -1 79  GLU B OE2   1 
ATOM   6204  N  N     . VAL B 1 80  ? 152.870 155.106 169.804 1.00 48.64 ?  80  VAL B N     1 
ATOM   6205  C  CA    . VAL B 1 80  ? 151.730 154.279 169.418 1.00 45.07 ?  80  VAL B CA    1 
ATOM   6206  C  C     . VAL B 1 80  ? 152.066 152.799 169.576 1.00 48.97 ?  80  VAL B C     1 
ATOM   6207  O  O     . VAL B 1 80  ? 151.276 152.016 170.124 1.00 51.77 ?  80  VAL B O     1 
ATOM   6208  C  CB    . VAL B 1 80  ? 151.297 154.619 167.979 1.00 44.98 ?  80  VAL B CB    1 
ATOM   6209  C  CG1   . VAL B 1 80  ? 150.376 153.555 167.425 1.00 46.55 ?  80  VAL B CG1   1 
ATOM   6210  C  CG2   . VAL B 1 80  ? 150.617 155.978 167.944 1.00 45.90 ?  80  VAL B CG2   1 
ATOM   6211  N  N     . PHE B 1 81  ? 153.252 152.395 169.114 1.00 47.44 ?  81  PHE B N     1 
ATOM   6212  C  CA    . PHE B 1 81  ? 153.684 151.011 169.291 1.00 44.10 ?  81  PHE B CA    1 
ATOM   6213  C  C     . PHE B 1 81  ? 153.855 150.672 170.768 1.00 45.61 ?  81  PHE B C     1 
ATOM   6214  O  O     . PHE B 1 81  ? 153.575 149.544 171.189 1.00 51.04 ?  81  PHE B O     1 
ATOM   6215  C  CB    . PHE B 1 81  ? 154.982 150.764 168.525 1.00 43.36 ?  81  PHE B CB    1 
ATOM   6216  C  CG    . PHE B 1 81  ? 154.775 150.343 167.099 1.00 43.48 ?  81  PHE B CG    1 
ATOM   6217  C  CD1   . PHE B 1 81  ? 154.459 151.274 166.125 1.00 44.24 ?  81  PHE B CD1   1 
ATOM   6218  C  CD2   . PHE B 1 81  ? 154.900 149.015 166.732 1.00 43.71 ?  81  PHE B CD2   1 
ATOM   6219  C  CE1   . PHE B 1 81  ? 154.268 150.887 164.813 1.00 44.16 ?  81  PHE B CE1   1 
ATOM   6220  C  CE2   . PHE B 1 81  ? 154.710 148.623 165.423 1.00 45.21 ?  81  PHE B CE2   1 
ATOM   6221  C  CZ    . PHE B 1 81  ? 154.395 149.561 164.462 1.00 43.39 ?  81  PHE B CZ    1 
ATOM   6222  N  N     . LYS B 1 82  ? 154.319 151.633 171.566 1.00 47.11 ?  82  LYS B N     1 
ATOM   6223  C  CA    . LYS B 1 82  ? 154.402 151.439 173.010 1.00 51.39 ?  82  LYS B CA    1 
ATOM   6224  C  C     . LYS B 1 82  ? 153.026 151.172 173.600 1.00 51.71 ?  82  LYS B C     1 
ATOM   6225  O  O     . LYS B 1 82  ? 152.857 150.288 174.446 1.00 51.17 ?  82  LYS B O     1 
ATOM   6226  C  CB    . LYS B 1 82  ? 155.026 152.671 173.666 1.00 53.58 ?  82  LYS B CB    1 
ATOM   6227  C  CG    . LYS B 1 82  ? 156.360 152.439 174.348 1.00 53.04 ?  82  LYS B CG    1 
ATOM   6228  C  CD    . LYS B 1 82  ? 157.497 152.346 173.351 1.00 54.24 ?  82  LYS B CD    1 
ATOM   6229  C  CE    . LYS B 1 82  ? 158.836 152.478 174.057 1.00 55.14 ?  82  LYS B CE    1 
ATOM   6230  N  NZ    . LYS B 1 82  ? 159.864 151.557 173.506 1.00 56.03 1  82  LYS B NZ    1 
ATOM   6231  N  N     . THR B 1 83  ? 152.028 151.941 173.162 1.00 47.16 ?  83  THR B N     1 
ATOM   6232  C  CA    . THR B 1 83  ? 150.665 151.744 173.641 1.00 45.62 ?  83  THR B CA    1 
ATOM   6233  C  C     . THR B 1 83  ? 150.143 150.366 173.257 1.00 47.50 ?  83  THR B C     1 
ATOM   6234  O  O     . THR B 1 83  ? 149.452 149.713 174.048 1.00 51.83 ?  83  THR B O     1 
ATOM   6235  C  CB    . THR B 1 83  ? 149.752 152.838 173.091 1.00 45.08 ?  83  THR B CB    1 
ATOM   6236  O  OG1   . THR B 1 83  ? 150.328 154.121 173.366 1.00 51.98 ?  83  THR B OG1   1 
ATOM   6237  C  CG2   . THR B 1 83  ? 148.382 152.764 173.736 1.00 47.96 ?  83  THR B CG2   1 
ATOM   6238  N  N     . ALA B 1 84  ? 150.457 149.909 172.042 1.00 41.73 ?  84  ALA B N     1 
ATOM   6239  C  CA    . ALA B 1 84  ? 150.026 148.574 171.636 1.00 38.19 ?  84  ALA B CA    1 
ATOM   6240  C  C     . ALA B 1 84  ? 150.673 147.491 172.489 1.00 41.93 ?  84  ALA B C     1 
ATOM   6241  O  O     . ALA B 1 84  ? 150.003 146.537 172.902 1.00 50.02 ?  84  ALA B O     1 
ATOM   6242  C  CB    . ALA B 1 84  ? 150.337 148.346 170.161 1.00 41.37 ?  84  ALA B CB    1 
ATOM   6243  N  N     . TYR B 1 85  ? 151.972 147.614 172.762 1.00 48.73 ?  85  TYR B N     1 
ATOM   6244  C  CA    . TYR B 1 85  ? 152.671 146.605 173.547 1.00 44.08 ?  85  TYR B CA    1 
ATOM   6245  C  C     . TYR B 1 85  ? 152.497 146.795 175.046 1.00 45.71 ?  85  TYR B C     1 
ATOM   6246  O  O     . TYR B 1 85  ? 152.830 145.886 175.813 1.00 48.79 ?  85  TYR B O     1 
ATOM   6247  C  CB    . TYR B 1 85  ? 154.161 146.601 173.197 1.00 45.03 ?  85  TYR B CB    1 
ATOM   6248  C  CG    . TYR B 1 85  ? 154.478 145.943 171.873 1.00 45.73 ?  85  TYR B CG    1 
ATOM   6249  C  CD1   . TYR B 1 85  ? 154.444 146.666 170.690 1.00 45.47 ?  85  TYR B CD1   1 
ATOM   6250  C  CD2   . TYR B 1 85  ? 154.814 144.599 171.809 1.00 45.37 ?  85  TYR B CD2   1 
ATOM   6251  C  CE1   . TYR B 1 85  ? 154.733 146.071 169.481 1.00 45.26 ?  85  TYR B CE1   1 
ATOM   6252  C  CE2   . TYR B 1 85  ? 155.104 143.994 170.604 1.00 45.88 ?  85  TYR B CE2   1 
ATOM   6253  C  CZ    . TYR B 1 85  ? 155.062 144.734 169.444 1.00 47.44 ?  85  TYR B CZ    1 
ATOM   6254  O  OH    . TYR B 1 85  ? 155.351 144.135 168.242 1.00 49.52 ?  85  TYR B OH    1 
ATOM   6255  N  N     . ALA B 1 86  ? 151.988 147.949 175.485 1.00 48.77 ?  86  ALA B N     1 
ATOM   6256  C  CA    . ALA B 1 86  ? 151.752 148.157 176.908 1.00 49.11 ?  86  ALA B CA    1 
ATOM   6257  C  C     . ALA B 1 86  ? 150.640 147.267 177.444 1.00 51.18 ?  86  ALA B C     1 
ATOM   6258  O  O     . ALA B 1 86  ? 150.615 146.985 178.647 1.00 50.07 ?  86  ALA B O     1 
ATOM   6259  C  CB    . ALA B 1 86  ? 151.416 149.622 177.185 1.00 45.01 ?  86  ALA B CB    1 
ATOM   6260  N  N     . LYS B 1 87  ? 149.722 146.826 176.585 1.00 43.59 ?  87  LYS B N     1 
ATOM   6261  C  CA    . LYS B 1 87  ? 148.630 145.968 177.022 1.00 43.37 ?  87  LYS B CA    1 
ATOM   6262  C  C     . LYS B 1 87  ? 149.076 144.540 177.300 1.00 46.64 ?  87  LYS B C     1 
ATOM   6263  O  O     . LYS B 1 87  ? 148.388 143.828 178.038 1.00 46.53 ?  87  LYS B O     1 
ATOM   6264  C  CB    . LYS B 1 87  ? 147.515 145.959 175.975 1.00 46.41 ?  87  LYS B CB    1 
ATOM   6265  C  CG    . LYS B 1 87  ? 146.126 145.754 176.551 1.00 47.31 ?  87  LYS B CG    1 
ATOM   6266  C  CD    . LYS B 1 87  ? 145.424 144.581 175.889 1.00 43.91 ?  87  LYS B CD    1 
ATOM   6267  C  CE    . LYS B 1 87  ? 144.167 144.193 176.648 1.00 43.53 ?  87  LYS B CE    1 
ATOM   6268  N  NZ    . LYS B 1 87  ? 143.433 143.084 175.978 1.00 41.20 1  87  LYS B NZ    1 
ATOM   6269  N  N     . LYS B 1 88  ? 150.208 144.114 176.735 1.00 51.97 ?  88  LYS B N     1 
ATOM   6270  C  CA    . LYS B 1 88  ? 150.694 142.741 176.860 1.00 47.74 ?  88  LYS B CA    1 
ATOM   6271  C  C     . LYS B 1 88  ? 149.608 141.747 176.456 1.00 46.69 ?  88  LYS B C     1 
ATOM   6272  O  O     . LYS B 1 88  ? 149.294 140.799 177.178 1.00 49.88 ?  88  LYS B O     1 
ATOM   6273  C  CB    . LYS B 1 88  ? 151.200 142.460 178.276 1.00 48.98 ?  88  LYS B CB    1 
ATOM   6274  C  CG    . LYS B 1 88  ? 152.069 143.563 178.857 1.00 47.10 ?  88  LYS B CG    1 
ATOM   6275  C  CD    . LYS B 1 88  ? 153.398 143.019 179.348 1.00 50.61 ?  88  LYS B CD    1 
ATOM   6276  C  CE    . LYS B 1 88  ? 153.224 142.203 180.617 1.00 52.66 ?  88  LYS B CE    1 
ATOM   6277  N  NZ    . LYS B 1 88  ? 154.403 141.333 180.885 1.00 51.45 1  88  LYS B NZ    1 
ATOM   6278  N  N     . PHE B 1 89  ? 149.023 141.984 175.283 1.00 45.43 ?  89  PHE B N     1 
ATOM   6279  C  CA    . PHE B 1 89  ? 147.904 141.172 174.827 1.00 40.04 ?  89  PHE B CA    1 
ATOM   6280  C  C     . PHE B 1 89  ? 148.341 139.732 174.599 1.00 42.32 ?  89  PHE B C     1 
ATOM   6281  O  O     . PHE B 1 89  ? 149.380 139.471 173.987 1.00 43.62 ?  89  PHE B O     1 
ATOM   6282  C  CB    . PHE B 1 89  ? 147.317 141.750 173.539 1.00 39.99 ?  89  PHE B CB    1 
ATOM   6283  C  CG    . PHE B 1 89  ? 146.273 140.875 172.908 1.00 38.98 ?  89  PHE B CG    1 
ATOM   6284  C  CD1   . PHE B 1 89  ? 144.975 140.877 173.384 1.00 37.21 ?  89  PHE B CD1   1 
ATOM   6285  C  CD2   . PHE B 1 89  ? 146.592 140.044 171.849 1.00 39.03 ?  89  PHE B CD2   1 
ATOM   6286  C  CE1   . PHE B 1 89  ? 144.014 140.072 172.813 1.00 39.04 ?  89  PHE B CE1   1 
ATOM   6287  C  CE2   . PHE B 1 89  ? 145.634 139.236 171.275 1.00 35.00 ?  89  PHE B CE2   1 
ATOM   6288  C  CZ    . PHE B 1 89  ? 144.345 139.250 171.756 1.00 38.35 ?  89  PHE B CZ    1 
ATOM   6289  N  N     . ARG B 1 90  ? 147.535 138.796 175.088 1.00 43.49 ?  90  ARG B N     1 
ATOM   6290  C  CA    . ARG B 1 90  ? 147.778 137.373 174.914 1.00 43.41 ?  90  ARG B CA    1 
ATOM   6291  C  C     . ARG B 1 90  ? 146.583 136.748 174.214 1.00 43.90 ?  90  ARG B C     1 
ATOM   6292  O  O     . ARG B 1 90  ? 145.437 136.976 174.613 1.00 47.64 ?  90  ARG B O     1 
ATOM   6293  C  CB    . ARG B 1 90  ? 148.023 136.684 176.259 1.00 46.45 ?  90  ARG B CB    1 
ATOM   6294  C  CG    . ARG B 1 90  ? 149.212 137.229 177.024 1.00 46.45 ?  90  ARG B CG    1 
ATOM   6295  C  CD    . ARG B 1 90  ? 150.493 136.527 176.616 1.00 48.43 ?  90  ARG B CD    1 
ATOM   6296  N  NE    . ARG B 1 90  ? 151.302 137.352 175.729 1.00 51.01 ?  90  ARG B NE    1 
ATOM   6297  C  CZ    . ARG B 1 90  ? 152.066 138.359 176.129 1.00 49.77 ?  90  ARG B CZ    1 
ATOM   6298  N  NH1   . ARG B 1 90  ? 152.168 138.685 177.407 1.00 47.15 1  90  ARG B NH1   1 
ATOM   6299  N  NH2   . ARG B 1 90  ? 152.747 139.057 175.225 1.00 51.52 ?  90  ARG B NH2   1 
ATOM   6300  N  N     . PHE B 1 91  ? 146.851 135.974 173.174 1.00 36.62 ?  91  PHE B N     1 
ATOM   6301  C  CA    . PHE B 1 91  ? 145.792 135.219 172.525 1.00 39.12 ?  91  PHE B CA    1 
ATOM   6302  C  C     . PHE B 1 91  ? 145.300 134.133 173.476 1.00 44.74 ?  91  PHE B C     1 
ATOM   6303  O  O     . PHE B 1 91  ? 146.105 133.330 173.960 1.00 45.97 ?  91  PHE B O     1 
ATOM   6304  C  CB    . PHE B 1 91  ? 146.294 134.601 171.224 1.00 39.16 ?  91  PHE B CB    1 
ATOM   6305  C  CG    . PHE B 1 91  ? 146.427 135.585 170.098 1.00 40.47 ?  91  PHE B CG    1 
ATOM   6306  C  CD1   . PHE B 1 91  ? 145.307 136.065 169.441 1.00 43.58 ?  91  PHE B CD1   1 
ATOM   6307  C  CD2   . PHE B 1 91  ? 147.673 136.028 169.694 1.00 42.01 ?  91  PHE B CD2   1 
ATOM   6308  C  CE1   . PHE B 1 91  ? 145.428 136.966 168.404 1.00 40.28 ?  91  PHE B CE1   1 
ATOM   6309  C  CE2   . PHE B 1 91  ? 147.799 136.929 168.657 1.00 40.89 ?  91  PHE B CE2   1 
ATOM   6310  C  CZ    . PHE B 1 91  ? 146.675 137.398 168.011 1.00 36.90 ?  91  PHE B CZ    1 
ATOM   6311  N  N     . PRO B 1 92  ? 144.000 134.075 173.774 1.00 44.11 ?  92  PRO B N     1 
ATOM   6312  C  CA    . PRO B 1 92  ? 143.529 133.090 174.757 1.00 40.42 ?  92  PRO B CA    1 
ATOM   6313  C  C     . PRO B 1 92  ? 143.541 131.667 174.236 1.00 39.94 ?  92  PRO B C     1 
ATOM   6314  O  O     . PRO B 1 92  ? 143.706 130.730 175.028 1.00 43.37 ?  92  PRO B O     1 
ATOM   6315  C  CB    . PRO B 1 92  ? 142.106 133.568 175.068 1.00 40.58 ?  92  PRO B CB    1 
ATOM   6316  C  CG    . PRO B 1 92  ? 141.670 134.238 173.814 1.00 40.82 ?  92  PRO B CG    1 
ATOM   6317  C  CD    . PRO B 1 92  ? 142.897 134.877 173.219 1.00 42.53 ?  92  PRO B CD    1 
ATOM   6318  N  N     . SER B 1 93  ? 143.377 131.474 172.933 1.00 38.53 ?  93  SER B N     1 
ATOM   6319  C  CA    . SER B 1 93  ? 143.280 130.151 172.342 1.00 40.38 ?  93  SER B CA    1 
ATOM   6320  C  C     . SER B 1 93  ? 144.295 130.026 171.216 1.00 42.60 ?  93  SER B C     1 
ATOM   6321  O  O     . SER B 1 93  ? 144.772 131.022 170.668 1.00 47.55 ?  93  SER B O     1 
ATOM   6322  C  CB    . SER B 1 93  ? 141.866 129.882 171.813 1.00 44.04 ?  93  SER B CB    1 
ATOM   6323  O  OG    . SER B 1 93  ? 141.792 130.111 170.418 1.00 50.00 ?  93  SER B OG    1 
ATOM   6324  N  N     . PHE B 1 94  ? 144.634 128.779 170.884 1.00 41.90 ?  94  PHE B N     1 
ATOM   6325  C  CA    . PHE B 1 94  ? 145.568 128.545 169.790 1.00 40.14 ?  94  PHE B CA    1 
ATOM   6326  C  C     . PHE B 1 94  ? 144.988 128.998 168.458 1.00 42.76 ?  94  PHE B C     1 
ATOM   6327  O  O     . PHE B 1 94  ? 145.718 129.505 167.600 1.00 47.43 ?  94  PHE B O     1 
ATOM   6328  C  CB    . PHE B 1 94  ? 145.957 127.069 169.723 1.00 40.16 ?  94  PHE B CB    1 
ATOM   6329  C  CG    . PHE B 1 94  ? 146.530 126.664 168.399 1.00 41.76 ?  94  PHE B CG    1 
ATOM   6330  C  CD1   . PHE B 1 94  ? 147.780 127.107 168.010 1.00 42.32 ?  94  PHE B CD1   1 
ATOM   6331  C  CD2   . PHE B 1 94  ? 145.813 125.859 167.533 1.00 43.73 ?  94  PHE B CD2   1 
ATOM   6332  C  CE1   . PHE B 1 94  ? 148.306 126.749 166.788 1.00 42.88 ?  94  PHE B CE1   1 
ATOM   6333  C  CE2   . PHE B 1 94  ? 146.338 125.498 166.309 1.00 41.04 ?  94  PHE B CE2   1 
ATOM   6334  C  CZ    . PHE B 1 94  ? 147.585 125.943 165.938 1.00 40.39 ?  94  PHE B CZ    1 
ATOM   6335  N  N     . MET B 1 95  ? 143.681 128.813 168.262 1.00 38.81 ?  95  MET B N     1 
ATOM   6336  C  CA    . MET B 1 95  ? 143.078 129.142 166.975 1.00 34.84 ?  95  MET B CA    1 
ATOM   6337  C  C     . MET B 1 95  ? 143.100 130.639 166.698 1.00 41.06 ?  95  MET B C     1 
ATOM   6338  O  O     . MET B 1 95  ? 143.241 131.041 165.541 1.00 43.38 ?  95  MET B O     1 
ATOM   6339  C  CB    . MET B 1 95  ? 141.648 128.607 166.907 1.00 41.10 ?  95  MET B CB    1 
ATOM   6340  C  CG    . MET B 1 95  ? 140.946 128.783 165.556 1.00 45.93 ?  95  MET B CG    1 
ATOM   6341  S  SD    . MET B 1 95  ? 141.663 128.086 164.041 1.00 55.90 ?  95  MET B SD    1 
ATOM   6342  C  CE    . MET B 1 95  ? 142.692 126.744 164.628 1.00 43.07 ?  95  MET B CE    1 
ATOM   6343  N  N     . SER B 1 96  ? 142.977 131.474 167.730 1.00 36.73 ?  96  SER B N     1 
ATOM   6344  C  CA    . SER B 1 96  ? 143.060 132.918 167.522 1.00 33.30 ?  96  SER B CA    1 
ATOM   6345  C  C     . SER B 1 96  ? 144.409 133.310 166.931 1.00 36.80 ?  96  SER B C     1 
ATOM   6346  O  O     . SER B 1 96  ? 144.481 133.974 165.885 1.00 32.79 ?  96  SER B O     1 
ATOM   6347  C  CB    . SER B 1 96  ? 142.828 133.644 168.846 1.00 36.01 ?  96  SER B CB    1 
ATOM   6348  O  OG    . SER B 1 96  ? 141.826 133.001 169.609 1.00 42.95 ?  96  SER B OG    1 
ATOM   6349  N  N     . ALA B 1 97  ? 145.493 132.889 167.585 1.00 36.06 ?  97  ALA B N     1 
ATOM   6350  C  CA    . ALA B 1 97  ? 146.833 133.209 167.110 1.00 32.56 ?  97  ALA B CA    1 
ATOM   6351  C  C     . ALA B 1 97  ? 147.108 132.569 165.758 1.00 34.38 ?  97  ALA B C     1 
ATOM   6352  O  O     . ALA B 1 97  ? 147.726 133.190 164.888 1.00 40.22 ?  97  ALA B O     1 
ATOM   6353  C  CB    . ALA B 1 97  ? 147.870 132.761 168.135 1.00 38.51 ?  97  ALA B CB    1 
ATOM   6354  N  N     . PHE B 1 98  ? 146.671 131.323 165.571 1.00 37.04 ?  98  PHE B N     1 
ATOM   6355  C  CA    . PHE B 1 98  ? 146.886 130.645 164.299 1.00 34.05 ?  98  PHE B CA    1 
ATOM   6356  C  C     . PHE B 1 98  ? 146.193 131.384 163.163 1.00 36.17 ?  98  PHE B C     1 
ATOM   6357  O  O     . PHE B 1 98  ? 146.789 131.622 162.108 1.00 48.45 ?  98  PHE B O     1 
ATOM   6358  C  CB    . PHE B 1 98  ? 146.392 129.202 164.384 1.00 39.75 ?  98  PHE B CB    1 
ATOM   6359  C  CG    . PHE B 1 98  ? 146.473 128.457 163.083 1.00 39.93 ?  98  PHE B CG    1 
ATOM   6360  C  CD1   . PHE B 1 98  ? 147.666 127.893 162.667 1.00 39.71 ?  98  PHE B CD1   1 
ATOM   6361  C  CD2   . PHE B 1 98  ? 145.357 128.322 162.276 1.00 41.60 ?  98  PHE B CD2   1 
ATOM   6362  C  CE1   . PHE B 1 98  ? 147.744 127.210 161.472 1.00 39.50 ?  98  PHE B CE1   1 
ATOM   6363  C  CE2   . PHE B 1 98  ? 145.431 127.641 161.078 1.00 44.69 ?  98  PHE B CE2   1 
ATOM   6364  C  CZ    . PHE B 1 98  ? 146.625 127.084 160.677 1.00 43.40 ?  98  PHE B CZ    1 
ATOM   6365  N  N     . LYS B 1 99  ? 144.932 131.768 163.367 1.00 41.42 ?  99  LYS B N     1 
ATOM   6366  C  CA    . LYS B 1 99  ? 144.196 132.479 162.332 1.00 39.05 ?  99  LYS B CA    1 
ATOM   6367  C  C     . LYS B 1 99  ? 144.832 133.827 162.035 1.00 37.72 ?  99  LYS B C     1 
ATOM   6368  O  O     . LYS B 1 99  ? 144.972 134.207 160.868 1.00 42.56 ?  99  LYS B O     1 
ATOM   6369  C  CB    . LYS B 1 99  ? 142.736 132.649 162.749 1.00 37.97 ?  99  LYS B CB    1 
ATOM   6370  C  CG    . LYS B 1 99  ? 141.882 131.415 162.524 1.00 42.93 ?  99  LYS B CG    1 
ATOM   6371  C  CD    . LYS B 1 99  ? 141.976 130.928 161.091 1.00 42.94 ?  99  LYS B CD    1 
ATOM   6372  C  CE    . LYS B 1 99  ? 140.719 130.184 160.681 1.00 42.46 ?  99  LYS B CE    1 
ATOM   6373  N  NZ    . LYS B 1 99  ? 140.246 130.603 159.335 1.00 47.99 1  99  LYS B NZ    1 
ATOM   6374  N  N     . PHE B 1 100 ? 145.247 134.560 163.072 1.00 36.96 ?  100 PHE B N     1 
ATOM   6375  C  CA    . PHE B 1 100 ? 145.875 135.852 162.818 1.00 34.43 ?  100 PHE B CA    1 
ATOM   6376  C  C     . PHE B 1 100 ? 147.178 135.689 162.046 1.00 37.14 ?  100 PHE B C     1 
ATOM   6377  O  O     . PHE B 1 100 ? 147.385 136.334 161.014 1.00 41.84 ?  100 PHE B O     1 
ATOM   6378  C  CB    . PHE B 1 100 ? 146.134 136.612 164.116 1.00 34.19 ?  100 PHE B CB    1 
ATOM   6379  C  CG    . PHE B 1 100 ? 146.876 137.896 163.898 1.00 37.70 ?  100 PHE B CG    1 
ATOM   6380  C  CD1   . PHE B 1 100 ? 146.243 138.981 163.316 1.00 37.53 ?  100 PHE B CD1   1 
ATOM   6381  C  CD2   . PHE B 1 100 ? 148.214 138.003 164.223 1.00 34.09 ?  100 PHE B CD2   1 
ATOM   6382  C  CE1   . PHE B 1 100 ? 146.926 140.157 163.091 1.00 37.84 ?  100 PHE B CE1   1 
ATOM   6383  C  CE2   . PHE B 1 100 ? 148.900 139.175 163.997 1.00 35.09 ?  100 PHE B CE2   1 
ATOM   6384  C  CZ    . PHE B 1 100 ? 148.256 140.254 163.433 1.00 37.50 ?  100 PHE B CZ    1 
ATOM   6385  N  N     . TYR B 1 101 ? 148.063 134.817 162.520 1.00 40.14 ?  101 TYR B N     1 
ATOM   6386  C  CA    . TYR B 1 101 ? 149.374 134.676 161.905 1.00 36.34 ?  101 TYR B CA    1 
ATOM   6387  C  C     . TYR B 1 101 ? 149.342 133.876 160.611 1.00 35.53 ?  101 TYR B C     1 
ATOM   6388  O  O     . TYR B 1 101 ? 150.379 133.759 159.953 1.00 44.77 ?  101 TYR B O     1 
ATOM   6389  C  CB    . TYR B 1 101 ? 150.350 134.046 162.901 1.00 35.64 ?  101 TYR B CB    1 
ATOM   6390  C  CG    . TYR B 1 101 ? 150.785 135.018 163.971 1.00 33.35 ?  101 TYR B CG    1 
ATOM   6391  C  CD1   . TYR B 1 101 ? 151.654 136.059 163.679 1.00 34.17 ?  101 TYR B CD1   1 
ATOM   6392  C  CD2   . TYR B 1 101 ? 150.304 134.912 165.266 1.00 37.40 ?  101 TYR B CD2   1 
ATOM   6393  C  CE1   . TYR B 1 101 ? 152.043 136.956 164.650 1.00 36.52 ?  101 TYR B CE1   1 
ATOM   6394  C  CE2   . TYR B 1 101 ? 150.686 135.805 166.242 1.00 39.90 ?  101 TYR B CE2   1 
ATOM   6395  C  CZ    . TYR B 1 101 ? 151.556 136.825 165.930 1.00 40.02 ?  101 TYR B CZ    1 
ATOM   6396  O  OH    . TYR B 1 101 ? 151.937 137.714 166.905 1.00 39.82 ?  101 TYR B OH    1 
ATOM   6397  N  N     . ASN B 1 102 ? 148.190 133.322 160.233 1.00 38.82 ?  102 ASN B N     1 
ATOM   6398  C  CA    . ASN B 1 102 ? 148.056 132.679 158.936 1.00 41.96 ?  102 ASN B CA    1 
ATOM   6399  C  C     . ASN B 1 102 ? 147.258 133.499 157.931 1.00 43.72 ?  102 ASN B C     1 
ATOM   6400  O  O     . ASN B 1 102 ? 147.376 133.247 156.727 1.00 48.13 ?  102 ASN B O     1 
ATOM   6401  C  CB    . ASN B 1 102 ? 147.394 131.304 159.092 1.00 40.56 ?  102 ASN B CB    1 
ATOM   6402  C  CG    . ASN B 1 102 ? 148.400 130.200 159.350 1.00 44.81 ?  102 ASN B CG    1 
ATOM   6403  O  OD1   . ASN B 1 102 ? 149.269 130.324 160.213 1.00 48.40 ?  102 ASN B OD1   1 
ATOM   6404  N  ND2   . ASN B 1 102 ? 148.287 129.113 158.598 1.00 43.12 ?  102 ASN B ND2   1 
ATOM   6405  N  N     . ASP B 1 103 ? 146.456 134.463 158.379 1.00 42.99 ?  103 ASP B N     1 
ATOM   6406  C  CA    . ASP B 1 103 ? 145.616 135.223 157.462 1.00 42.91 ?  103 ASP B CA    1 
ATOM   6407  C  C     . ASP B 1 103 ? 145.937 136.708 157.414 1.00 42.58 ?  103 ASP B C     1 
ATOM   6408  O  O     . ASP B 1 103 ? 145.848 137.312 156.343 1.00 46.97 ?  103 ASP B O     1 
ATOM   6409  C  CB    . ASP B 1 103 ? 144.135 135.046 157.838 1.00 45.28 ?  103 ASP B CB    1 
ATOM   6410  C  CG    . ASP B 1 103 ? 143.655 133.618 157.668 1.00 50.09 ?  103 ASP B CG    1 
ATOM   6411  O  OD1   . ASP B 1 103 ? 144.437 132.775 157.183 1.00 50.18 ?  103 ASP B OD1   1 
ATOM   6412  O  OD2   . ASP B 1 103 ? 142.492 133.337 158.025 1.00 53.52 -1 103 ASP B OD2   1 
ATOM   6413  N  N     . TYR B 1 104 ? 146.306 137.318 158.538 1.00 36.66 ?  104 TYR B N     1 
ATOM   6414  C  CA    . TYR B 1 104 ? 146.423 138.766 158.627 1.00 41.43 ?  104 TYR B CA    1 
ATOM   6415  C  C     . TYR B 1 104 ? 147.826 139.264 158.931 1.00 39.97 ?  104 TYR B C     1 
ATOM   6416  O  O     . TYR B 1 104 ? 148.141 140.404 158.587 1.00 45.56 ?  104 TYR B O     1 
ATOM   6417  C  CB    . TYR B 1 104 ? 145.468 139.309 159.701 1.00 37.76 ?  104 TYR B CB    1 
ATOM   6418  C  CG    . TYR B 1 104 ? 144.034 138.888 159.493 1.00 41.00 ?  104 TYR B CG    1 
ATOM   6419  C  CD1   . TYR B 1 104 ? 143.195 139.610 158.658 1.00 40.31 ?  104 TYR B CD1   1 
ATOM   6420  C  CD2   . TYR B 1 104 ? 143.522 137.763 160.123 1.00 35.66 ?  104 TYR B CD2   1 
ATOM   6421  C  CE1   . TYR B 1 104 ? 141.887 139.228 158.460 1.00 39.93 ?  104 TYR B CE1   1 
ATOM   6422  C  CE2   . TYR B 1 104 ? 142.215 137.371 159.930 1.00 36.77 ?  104 TYR B CE2   1 
ATOM   6423  C  CZ    . TYR B 1 104 ? 141.401 138.109 159.098 1.00 41.95 ?  104 TYR B CZ    1 
ATOM   6424  O  OH    . TYR B 1 104 ? 140.097 137.726 158.901 1.00 41.50 ?  104 TYR B OH    1 
ATOM   6425  N  N     . ALA B 1 105 ? 148.669 138.458 159.570 1.00 42.71 ?  105 ALA B N     1 
ATOM   6426  C  CA    . ALA B 1 105 ? 150.018 138.900 159.890 1.00 42.57 ?  105 ALA B CA    1 
ATOM   6427  C  C     . ALA B 1 105 ? 150.837 139.082 158.620 1.00 45.88 ?  105 ALA B C     1 
ATOM   6428  O  O     . ALA B 1 105 ? 150.775 138.262 157.699 1.00 44.64 ?  105 ALA B O     1 
ATOM   6429  C  CB    . ALA B 1 105 ? 150.704 137.899 160.815 1.00 38.01 ?  105 ALA B CB    1 
ATOM   6430  N  N     . LEU B 1 106 ? 151.604 140.167 158.573 1.00 47.08 ?  106 LEU B N     1 
ATOM   6431  C  CA    . LEU B 1 106 ? 152.435 140.443 157.411 1.00 44.38 ?  106 LEU B CA    1 
ATOM   6432  C  C     . LEU B 1 106 ? 153.600 139.465 157.355 1.00 47.36 ?  106 LEU B C     1 
ATOM   6433  O  O     . LEU B 1 106 ? 154.318 139.278 158.341 1.00 47.74 ?  106 LEU B O     1 
ATOM   6434  C  CB    . LEU B 1 106 ? 152.950 141.881 157.453 1.00 48.24 ?  106 LEU B CB    1 
ATOM   6435  C  CG    . LEU B 1 106 ? 153.725 142.370 156.229 1.00 44.94 ?  106 LEU B CG    1 
ATOM   6436  C  CD1   . LEU B 1 106 ? 152.813 142.460 155.018 1.00 44.16 ?  106 LEU B CD1   1 
ATOM   6437  C  CD2   . LEU B 1 106 ? 154.377 143.712 156.510 1.00 44.60 ?  106 LEU B CD2   1 
ATOM   6438  N  N     . LYS B 1 107 ? 153.786 138.845 156.196 1.00 55.35 ?  107 LYS B N     1 
ATOM   6439  C  CA    . LYS B 1 107 ? 154.855 137.889 155.972 1.00 55.18 ?  107 LYS B CA    1 
ATOM   6440  C  C     . LYS B 1 107 ? 155.793 138.408 154.894 1.00 56.71 ?  107 LYS B C     1 
ATOM   6441  O  O     . LYS B 1 107 ? 155.471 139.344 154.155 1.00 55.21 ?  107 LYS B O     1 
ATOM   6442  C  CB    . LYS B 1 107 ? 154.303 136.518 155.566 1.00 54.68 ?  107 LYS B CB    1 
ATOM   6443  C  CG    . LYS B 1 107 ? 153.854 135.660 156.730 1.00 52.82 ?  107 LYS B CG    1 
ATOM   6444  C  CD    . LYS B 1 107 ? 153.005 134.497 156.256 1.00 55.63 ?  107 LYS B CD    1 
ATOM   6445  C  CE    . LYS B 1 107 ? 152.236 133.882 157.408 1.00 57.28 ?  107 LYS B CE    1 
ATOM   6446  N  NZ    . LYS B 1 107 ? 151.850 134.904 158.419 1.00 56.18 1  107 LYS B NZ    1 
ATOM   6447  N  N     . THR B 1 108 ? 156.970 137.791 154.815 1.00 60.92 ?  108 THR B N     1 
ATOM   6448  C  CA    . THR B 1 108 ? 157.932 138.143 153.786 1.00 60.71 ?  108 THR B CA    1 
ATOM   6449  C  C     . THR B 1 108 ? 157.363 137.829 152.403 1.00 62.10 ?  108 THR B C     1 
ATOM   6450  O  O     . THR B 1 108 ? 156.359 137.128 152.256 1.00 62.89 ?  108 THR B O     1 
ATOM   6451  C  CB    . THR B 1 108 ? 159.246 137.393 154.001 1.00 59.88 ?  108 THR B CB    1 
ATOM   6452  O  OG1   . THR B 1 108 ? 158.974 135.999 154.195 1.00 62.05 ?  108 THR B OG1   1 
ATOM   6453  C  CG2   . THR B 1 108 ? 159.978 137.929 155.218 1.00 57.02 ?  108 THR B CG2   1 
ATOM   6454  N  N     . ASN B 1 109 ? 158.025 138.366 151.374 1.00 63.27 ?  109 ASN B N     1 
ATOM   6455  C  CA    . ASN B 1 109 ? 157.551 138.166 150.008 1.00 63.09 ?  109 ASN B CA    1 
ATOM   6456  C  C     . ASN B 1 109 ? 157.537 136.693 149.620 1.00 66.07 ?  109 ASN B C     1 
ATOM   6457  O  O     . ASN B 1 109 ? 156.748 136.287 148.759 1.00 65.99 ?  109 ASN B O     1 
ATOM   6458  C  CB    . ASN B 1 109 ? 158.411 138.965 149.029 1.00 61.80 ?  109 ASN B CB    1 
ATOM   6459  C  CG    . ASN B 1 109 ? 158.442 140.444 149.357 1.00 64.04 ?  109 ASN B CG    1 
ATOM   6460  O  OD1   . ASN B 1 109 ? 157.423 141.129 149.279 1.00 66.19 ?  109 ASN B OD1   1 
ATOM   6461  N  ND2   . ASN B 1 109 ? 159.615 140.943 149.726 1.00 63.88 ?  109 ASN B ND2   1 
ATOM   6462  N  N     . ASP B 1 110 ? 158.394 135.881 150.235 1.00 66.04 ?  110 ASP B N     1 
ATOM   6463  C  CA    . ASP B 1 110 ? 158.381 134.440 150.025 1.00 67.63 ?  110 ASP B CA    1 
ATOM   6464  C  C     . ASP B 1 110 ? 157.508 133.710 151.039 1.00 66.77 ?  110 ASP B C     1 
ATOM   6465  O  O     . ASP B 1 110 ? 157.478 132.475 151.035 1.00 67.18 ?  110 ASP B O     1 
ATOM   6466  C  CB    . ASP B 1 110 ? 159.807 133.881 150.057 1.00 68.15 ?  110 ASP B CB    1 
ATOM   6467  C  CG    . ASP B 1 110 ? 160.482 134.075 151.398 1.00 69.90 ?  110 ASP B CG    1 
ATOM   6468  O  OD1   . ASP B 1 110 ? 160.108 135.017 152.122 1.00 69.54 ?  110 ASP B OD1   1 
ATOM   6469  O  OD2   . ASP B 1 110 ? 161.390 133.284 151.728 1.00 69.81 -1 110 ASP B OD2   1 
ATOM   6470  N  N     . LYS B 1 111 ? 156.798 134.449 151.897 1.00 64.62 ?  111 LYS B N     1 
ATOM   6471  C  CA    . LYS B 1 111 ? 155.886 133.875 152.889 1.00 64.06 ?  111 LYS B CA    1 
ATOM   6472  C  C     . LYS B 1 111 ? 156.599 132.869 153.789 1.00 66.24 ?  111 LYS B C     1 
ATOM   6473  O  O     . LYS B 1 111 ? 156.066 131.806 154.109 1.00 67.00 ?  111 LYS B O     1 
ATOM   6474  C  CB    . LYS B 1 111 ? 154.667 133.235 152.220 1.00 64.89 ?  111 LYS B CB    1 
ATOM   6475  C  CG    . LYS B 1 111 ? 154.030 134.081 151.127 1.00 64.51 ?  111 LYS B CG    1 
ATOM   6476  C  CD    . LYS B 1 111 ? 153.681 135.478 151.623 1.00 66.11 ?  111 LYS B CD    1 
ATOM   6477  C  CE    . LYS B 1 111 ? 152.488 135.452 152.564 1.00 67.79 ?  111 LYS B CE    1 
ATOM   6478  N  NZ    . LYS B 1 111 ? 151.265 134.919 151.905 1.00 68.04 1  111 LYS B NZ    1 
ATOM   6479  N  N     . LYS B 1 112 ? 157.817 133.210 154.203 1.00 65.24 ?  112 LYS B N     1 
ATOM   6480  C  CA    . LYS B 1 112 ? 158.634 132.346 155.048 1.00 64.41 ?  112 LYS B CA    1 
ATOM   6481  C  C     . LYS B 1 112 ? 158.725 132.824 156.488 1.00 64.17 ?  112 LYS B C     1 
ATOM   6482  O  O     . LYS B 1 112 ? 158.616 132.011 157.408 1.00 65.83 ?  112 LYS B O     1 
ATOM   6483  C  CB    . LYS B 1 112 ? 160.046 132.225 154.460 1.00 63.97 ?  112 LYS B CB    1 
ATOM   6484  C  CG    . LYS B 1 112 ? 161.134 131.880 155.467 1.00 67.04 ?  112 LYS B CG    1 
ATOM   6485  C  CD    . LYS B 1 112 ? 161.104 130.405 155.837 1.00 65.11 ?  112 LYS B CD    1 
ATOM   6486  C  CE    . LYS B 1 112 ? 161.677 130.174 157.226 1.00 65.22 ?  112 LYS B CE    1 
ATOM   6487  N  NZ    . LYS B 1 112 ? 160.829 130.787 158.286 1.00 64.88 1  112 LYS B NZ    1 
ATOM   6488  N  N     . LYS B 1 113 ? 158.909 134.118 156.707 1.00 60.20 ?  113 LYS B N     1 
ATOM   6489  C  CA    . LYS B 1 113 ? 159.051 134.693 158.037 1.00 59.08 ?  113 LYS B CA    1 
ATOM   6490  C  C     . LYS B 1 113 ? 157.878 135.627 158.323 1.00 59.43 ?  113 LYS B C     1 
ATOM   6491  O  O     . LYS B 1 113 ? 157.031 135.881 157.465 1.00 57.53 ?  113 LYS B O     1 
ATOM   6492  C  CB    . LYS B 1 113 ? 160.389 135.425 158.165 1.00 57.33 ?  113 LYS B CB    1 
ATOM   6493  C  CG    . LYS B 1 113 ? 161.584 134.511 158.376 1.00 57.95 ?  113 LYS B CG    1 
ATOM   6494  C  CD    . LYS B 1 113 ? 161.623 133.970 159.793 1.00 59.48 ?  113 LYS B CD    1 
ATOM   6495  C  CE    . LYS B 1 113 ? 163.022 133.524 160.175 1.00 57.00 ?  113 LYS B CE    1 
ATOM   6496  N  NZ    . LYS B 1 113 ? 163.105 132.046 160.332 1.00 58.77 1  113 LYS B NZ    1 
ATOM   6497  N  N     . ILE B 1 114 ? 157.840 136.144 159.549 1.00 52.83 ?  114 ILE B N     1 
ATOM   6498  C  CA    . ILE B 1 114 ? 156.751 136.992 160.023 1.00 49.84 ?  114 ILE B CA    1 
ATOM   6499  C  C     . ILE B 1 114 ? 157.320 138.363 160.357 1.00 51.40 ?  114 ILE B C     1 
ATOM   6500  O  O     . ILE B 1 114 ? 158.241 138.475 161.177 1.00 54.24 ?  114 ILE B O     1 
ATOM   6501  C  CB    . ILE B 1 114 ? 156.047 136.379 161.246 1.00 51.19 ?  114 ILE B CB    1 
ATOM   6502  C  CG1   . ILE B 1 114 ? 155.188 135.184 160.830 1.00 49.80 ?  114 ILE B CG1   1 
ATOM   6503  C  CG2   . ILE B 1 114 ? 155.201 137.418 161.956 1.00 51.04 ?  114 ILE B CG2   1 
ATOM   6504  C  CD1   . ILE B 1 114 ? 154.773 134.308 161.987 1.00 46.81 ?  114 ILE B CD1   1 
ATOM   6505  N  N     . LEU B 1 115 ? 156.774 139.404 159.727 1.00 48.43 ?  115 LEU B N     1 
ATOM   6506  C  CA    . LEU B 1 115 ? 157.184 140.771 160.026 1.00 47.70 ?  115 LEU B CA    1 
ATOM   6507  C  C     . LEU B 1 115 ? 156.328 141.415 161.106 1.00 50.04 ?  115 LEU B C     1 
ATOM   6508  O  O     . LEU B 1 115 ? 156.841 142.183 161.926 1.00 51.35 ?  115 LEU B O     1 
ATOM   6509  C  CB    . LEU B 1 115 ? 157.129 141.639 158.766 1.00 49.26 ?  115 LEU B CB    1 
ATOM   6510  C  CG    . LEU B 1 115 ? 158.223 141.500 157.707 1.00 47.40 ?  115 LEU B CG    1 
ATOM   6511  C  CD1   . LEU B 1 115 ? 159.590 141.323 158.349 1.00 49.77 ?  115 LEU B CD1   1 
ATOM   6512  C  CD2   . LEU B 1 115 ? 157.910 140.363 156.765 1.00 48.91 ?  115 LEU B CD2   1 
ATOM   6513  N  N     . GLU B 1 116 ? 155.032 141.119 161.126 1.00 46.96 ?  116 GLU B N     1 
ATOM   6514  C  CA    . GLU B 1 116 ? 154.078 141.813 161.980 1.00 46.21 ?  116 GLU B CA    1 
ATOM   6515  C  C     . GLU B 1 116 ? 153.565 140.885 163.070 1.00 44.69 ?  116 GLU B C     1 
ATOM   6516  O  O     . GLU B 1 116 ? 153.116 139.771 162.785 1.00 49.18 ?  116 GLU B O     1 
ATOM   6517  C  CB    . GLU B 1 116 ? 152.900 142.343 161.162 1.00 43.45 ?  116 GLU B CB    1 
ATOM   6518  C  CG    . GLU B 1 116 ? 153.002 143.808 160.800 1.00 44.40 ?  116 GLU B CG    1 
ATOM   6519  C  CD    . GLU B 1 116 ? 151.846 144.270 159.937 1.00 47.71 ?  116 GLU B CD    1 
ATOM   6520  O  OE1   . GLU B 1 116 ? 151.023 143.418 159.542 1.00 49.39 ?  116 GLU B OE1   1 
ATOM   6521  O  OE2   . GLU B 1 116 ? 151.760 145.482 159.656 1.00 50.22 -1 116 GLU B OE2   1 
ATOM   6522  N  N     . ARG B 1 117 ? 153.626 141.353 164.312 1.00 39.36 ?  117 ARG B N     1 
ATOM   6523  C  CA    . ARG B 1 117 ? 152.896 140.730 165.398 1.00 41.72 ?  117 ARG B CA    1 
ATOM   6524  C  C     . ARG B 1 117 ? 151.481 141.303 165.427 1.00 41.09 ?  117 ARG B C     1 
ATOM   6525  O  O     . ARG B 1 117 ? 151.104 142.130 164.595 1.00 39.45 ?  117 ARG B O     1 
ATOM   6526  C  CB    . ARG B 1 117 ? 153.614 140.951 166.728 1.00 42.00 ?  117 ARG B CB    1 
ATOM   6527  C  CG    . ARG B 1 117 ? 155.012 140.365 166.787 1.00 40.80 ?  117 ARG B CG    1 
ATOM   6528  C  CD    . ARG B 1 117 ? 155.022 138.901 166.376 1.00 46.77 ?  117 ARG B CD    1 
ATOM   6529  N  NE    . ARG B 1 117 ? 154.824 138.008 167.512 1.00 44.38 ?  117 ARG B NE    1 
ATOM   6530  C  CZ    . ARG B 1 117 ? 155.715 137.797 168.472 1.00 45.70 ?  117 ARG B CZ    1 
ATOM   6531  N  NH1   . ARG B 1 117 ? 156.899 138.385 168.459 1.00 43.54 1  117 ARG B NH1   1 
ATOM   6532  N  NH2   . ARG B 1 117 ? 155.411 136.969 169.467 1.00 47.75 ?  117 ARG B NH2   1 
ATOM   6533  N  N     . TYR B 1 118 ? 150.678 140.854 166.391 1.00 41.03 ?  118 TYR B N     1 
ATOM   6534  C  CA    . TYR B 1 118 ? 149.347 141.429 166.549 1.00 35.12 ?  118 TYR B CA    1 
ATOM   6535  C  C     . TYR B 1 118 ? 149.436 142.908 166.901 1.00 38.01 ?  118 TYR B C     1 
ATOM   6536  O  O     . TYR B 1 118 ? 148.689 143.733 166.360 1.00 40.88 ?  118 TYR B O     1 
ATOM   6537  C  CB    . TYR B 1 118 ? 148.568 140.662 167.615 1.00 36.39 ?  118 TYR B CB    1 
ATOM   6538  C  CG    . TYR B 1 118 ? 147.087 140.959 167.620 1.00 38.14 ?  118 TYR B CG    1 
ATOM   6539  C  CD1   . TYR B 1 118 ? 146.326 140.810 166.470 1.00 33.51 ?  118 TYR B CD1   1 
ATOM   6540  C  CD2   . TYR B 1 118 ? 146.452 141.391 168.774 1.00 36.95 ?  118 TYR B CD2   1 
ATOM   6541  C  CE1   . TYR B 1 118 ? 144.976 141.079 166.471 1.00 33.42 ?  118 TYR B CE1   1 
ATOM   6542  C  CE2   . TYR B 1 118 ? 145.100 141.659 168.785 1.00 33.77 ?  118 TYR B CE2   1 
ATOM   6543  C  CZ    . TYR B 1 118 ? 144.367 141.503 167.629 1.00 35.25 ?  118 TYR B CZ    1 
ATOM   6544  O  OH    . TYR B 1 118 ? 143.020 141.774 167.634 1.00 45.00 ?  118 TYR B OH    1 
ATOM   6545  N  N     . GLU B 1 119 ? 150.362 143.260 167.794 1.00 44.44 ?  119 GLU B N     1 
ATOM   6546  C  CA    . GLU B 1 119 ? 150.526 144.653 168.188 1.00 38.64 ?  119 GLU B CA    1 
ATOM   6547  C  C     . GLU B 1 119 ? 150.998 145.513 167.022 1.00 38.45 ?  119 GLU B C     1 
ATOM   6548  O  O     . GLU B 1 119 ? 150.553 146.653 166.874 1.00 49.14 ?  119 GLU B O     1 
ATOM   6549  C  CB    . GLU B 1 119 ? 151.497 144.752 169.362 1.00 38.99 ?  119 GLU B CB    1 
ATOM   6550  C  CG    . GLU B 1 119 ? 150.972 144.134 170.646 1.00 39.79 ?  119 GLU B CG    1 
ATOM   6551  C  CD    . GLU B 1 119 ? 151.417 142.697 170.827 1.00 45.71 ?  119 GLU B CD    1 
ATOM   6552  O  OE1   . GLU B 1 119 ? 151.647 142.010 169.809 1.00 45.33 ?  119 GLU B OE1   1 
ATOM   6553  O  OE2   . GLU B 1 119 ? 151.535 142.250 171.988 1.00 46.42 -1 119 GLU B OE2   1 
ATOM   6554  N  N     . ASP B 1 120 ? 151.901 144.993 166.187 1.00 40.96 ?  120 ASP B N     1 
ATOM   6555  C  CA    . ASP B 1 120 ? 152.370 145.769 165.040 1.00 39.84 ?  120 ASP B CA    1 
ATOM   6556  C  C     . ASP B 1 120 ? 151.244 146.018 164.045 1.00 39.51 ?  120 ASP B C     1 
ATOM   6557  O  O     . ASP B 1 120 ? 151.086 147.135 163.537 1.00 44.82 ?  120 ASP B O     1 
ATOM   6558  C  CB    . ASP B 1 120 ? 153.539 145.059 164.357 1.00 45.29 ?  120 ASP B CB    1 
ATOM   6559  C  CG    . ASP B 1 120 ? 154.551 144.524 165.342 1.00 47.85 ?  120 ASP B CG    1 
ATOM   6560  O  OD1   . ASP B 1 120 ? 154.965 143.358 165.190 1.00 51.60 ?  120 ASP B OD1   1 
ATOM   6561  O  OD2   . ASP B 1 120 ? 154.927 145.267 166.272 1.00 46.55 -1 120 ASP B OD2   1 
ATOM   6562  N  N     . ARG B 1 121 ? 150.456 144.983 163.749 1.00 34.52 ?  121 ARG B N     1 
ATOM   6563  C  CA    . ARG B 1 121 ? 149.323 145.144 162.844 1.00 31.09 ?  121 ARG B CA    1 
ATOM   6564  C  C     . ARG B 1 121 ? 148.320 146.147 163.395 1.00 35.79 ?  121 ARG B C     1 
ATOM   6565  O  O     . ARG B 1 121 ? 147.823 147.010 162.661 1.00 45.87 ?  121 ARG B O     1 
ATOM   6566  C  CB    . ARG B 1 121 ? 148.659 143.789 162.600 1.00 35.38 ?  121 ARG B CB    1 
ATOM   6567  C  CG    . ARG B 1 121 ? 147.398 143.837 161.757 1.00 32.93 ?  121 ARG B CG    1 
ATOM   6568  C  CD    . ARG B 1 121 ? 147.712 143.736 160.280 1.00 32.41 ?  121 ARG B CD    1 
ATOM   6569  N  NE    . ARG B 1 121 ? 147.518 145.013 159.605 1.00 43.28 ?  121 ARG B NE    1 
ATOM   6570  C  CZ    . ARG B 1 121 ? 148.298 145.476 158.640 1.00 39.89 ?  121 ARG B CZ    1 
ATOM   6571  N  NH1   . ARG B 1 121 ? 149.341 144.789 158.206 1.00 42.44 1  121 ARG B NH1   1 
ATOM   6572  N  NH2   . ARG B 1 121 ? 148.027 146.659 158.100 1.00 32.92 ?  121 ARG B NH2   1 
ATOM   6573  N  N     . ILE B 1 122 ? 148.024 146.061 164.693 1.00 35.39 ?  122 ILE B N     1 
ATOM   6574  C  CA    . ILE B 1 122 ? 147.068 146.982 165.297 1.00 29.58 ?  122 ILE B CA    1 
ATOM   6575  C  C     . ILE B 1 122 ? 147.610 148.407 165.288 1.00 30.42 ?  122 ILE B C     1 
ATOM   6576  O  O     . ILE B 1 122 ? 146.873 149.361 165.019 1.00 37.63 ?  122 ILE B O     1 
ATOM   6577  C  CB    . ILE B 1 122 ? 146.699 146.507 166.712 1.00 35.40 ?  122 ILE B CB    1 
ATOM   6578  C  CG1   . ILE B 1 122 ? 145.640 145.408 166.620 1.00 32.27 ?  122 ILE B CG1   1 
ATOM   6579  C  CG2   . ILE B 1 122 ? 146.202 147.661 167.570 1.00 31.89 ?  122 ILE B CG2   1 
ATOM   6580  C  CD1   . ILE B 1 122 ? 145.032 145.037 167.933 1.00 32.92 ?  122 ILE B CD1   1 
ATOM   6581  N  N     . SER B 1 123 ? 148.904 148.578 165.568 1.00 33.76 ?  123 SER B N     1 
ATOM   6582  C  CA    . SER B 1 123 ? 149.501 149.908 165.539 1.00 32.60 ?  123 SER B CA    1 
ATOM   6583  C  C     . SER B 1 123 ? 149.456 150.507 164.143 1.00 36.18 ?  123 SER B C     1 
ATOM   6584  O  O     . SER B 1 123 ? 149.157 151.694 163.978 1.00 36.84 ?  123 SER B O     1 
ATOM   6585  C  CB    . SER B 1 123 ? 150.944 149.850 166.036 1.00 32.05 ?  123 SER B CB    1 
ATOM   6586  O  OG    . SER B 1 123 ? 151.018 149.278 167.322 1.00 37.98 ?  123 SER B OG    1 
ATOM   6587  N  N     . ILE B 1 124 ? 149.758 149.704 163.122 1.00 36.71 ?  124 ILE B N     1 
ATOM   6588  C  CA    . ILE B 1 124 ? 149.725 150.212 161.755 1.00 34.76 ?  124 ILE B CA    1 
ATOM   6589  C  C     . ILE B 1 124 ? 148.303 150.582 161.355 1.00 39.62 ?  124 ILE B C     1 
ATOM   6590  O  O     . ILE B 1 124 ? 148.071 151.631 160.739 1.00 39.84 ?  124 ILE B O     1 
ATOM   6591  C  CB    . ILE B 1 124 ? 150.347 149.185 160.793 1.00 39.41 ?  124 ILE B CB    1 
ATOM   6592  C  CG1   . ILE B 1 124 ? 151.870 149.210 160.925 1.00 41.25 ?  124 ILE B CG1   1 
ATOM   6593  C  CG2   . ILE B 1 124 ? 149.933 149.468 159.359 1.00 36.46 ?  124 ILE B CG2   1 
ATOM   6594  C  CD1   . ILE B 1 124 ? 152.470 150.594 160.797 1.00 36.63 ?  124 ILE B CD1   1 
ATOM   6595  N  N     . VAL B 1 125 ? 147.327 149.744 161.715 1.00 32.40 ?  125 VAL B N     1 
ATOM   6596  C  CA    . VAL B 1 125 ? 145.935 150.046 161.393 1.00 30.50 ?  125 VAL B CA    1 
ATOM   6597  C  C     . VAL B 1 125 ? 145.488 151.322 162.098 1.00 25.65 ?  125 VAL B C     1 
ATOM   6598  O  O     . VAL B 1 125 ? 144.799 152.164 161.510 1.00 35.98 ?  125 VAL B O     1 
ATOM   6599  C  CB    . VAL B 1 125 ? 145.035 148.847 161.745 1.00 37.24 ?  125 VAL B CB    1 
ATOM   6600  C  CG1   . VAL B 1 125 ? 143.574 149.238 161.687 1.00 32.65 ?  125 VAL B CG1   1 
ATOM   6601  C  CG2   . VAL B 1 125 ? 145.304 147.692 160.796 1.00 27.59 ?  125 VAL B CG2   1 
ATOM   6602  N  N     . ALA B 1 126 ? 145.882 151.494 163.360 1.00 24.10 ?  126 ALA B N     1 
ATOM   6603  C  CA    . ALA B 1 126 ? 145.506 152.692 164.105 1.00 26.21 ?  126 ALA B CA    1 
ATOM   6604  C  C     . ALA B 1 126 ? 146.163 153.942 163.533 1.00 31.08 ?  126 ALA B C     1 
ATOM   6605  O  O     . ALA B 1 126 ? 145.530 155.001 163.455 1.00 34.62 ?  126 ALA B O     1 
ATOM   6606  C  CB    . ALA B 1 126 ? 145.877 152.526 165.576 1.00 29.96 ?  126 ALA B CB    1 
ATOM   6607  N  N     . LEU B 1 127 ? 147.436 153.843 163.146 1.00 36.91 ?  127 LEU B N     1 
ATOM   6608  C  CA    . LEU B 1 127 ? 148.124 154.988 162.562 1.00 26.42 ?  127 LEU B CA    1 
ATOM   6609  C  C     . LEU B 1 127 ? 147.519 155.359 161.217 1.00 26.74 ?  127 LEU B C     1 
ATOM   6610  O  O     . LEU B 1 127 ? 147.476 156.539 160.852 1.00 33.01 ?  127 LEU B O     1 
ATOM   6611  C  CB    . LEU B 1 127 ? 149.616 154.689 162.417 1.00 28.93 ?  127 LEU B CB    1 
ATOM   6612  C  CG    . LEU B 1 127 ? 150.448 154.675 163.699 1.00 32.83 ?  127 LEU B CG    1 
ATOM   6613  C  CD1   . LEU B 1 127 ? 151.753 153.932 163.481 1.00 38.52 ?  127 LEU B CD1   1 
ATOM   6614  C  CD2   . LEU B 1 127 ? 150.715 156.086 164.187 1.00 33.35 ?  127 LEU B CD2   1 
ATOM   6615  N  N     . PHE B 1 128 ? 147.056 154.364 160.459 1.00 32.50 ?  128 PHE B N     1 
ATOM   6616  C  CA    . PHE B 1 128 ? 146.354 154.654 159.214 1.00 33.27 ?  128 PHE B CA    1 
ATOM   6617  C  C     . PHE B 1 128 ? 144.996 155.293 159.487 1.00 30.13 ?  128 PHE B C     1 
ATOM   6618  O  O     . PHE B 1 128 ? 144.574 156.199 158.761 1.00 40.74 ?  128 PHE B O     1 
ATOM   6619  C  CB    . PHE B 1 128 ? 146.219 153.372 158.388 1.00 29.67 ?  128 PHE B CB    1 
ATOM   6620  C  CG    . PHE B 1 128 ? 145.223 153.460 157.265 1.00 35.44 ?  128 PHE B CG    1 
ATOM   6621  C  CD1   . PHE B 1 128 ? 143.880 153.186 157.475 1.00 33.75 ?  128 PHE B CD1   1 
ATOM   6622  C  CD2   . PHE B 1 128 ? 145.633 153.823 155.995 1.00 37.02 ?  128 PHE B CD2   1 
ATOM   6623  C  CE1   . PHE B 1 128 ? 142.973 153.275 156.442 1.00 34.62 ?  128 PHE B CE1   1 
ATOM   6624  C  CE2   . PHE B 1 128 ? 144.729 153.911 154.959 1.00 36.99 ?  128 PHE B CE2   1 
ATOM   6625  C  CZ    . PHE B 1 128 ? 143.398 153.638 155.183 1.00 34.68 ?  128 PHE B CZ    1 
ATOM   6626  N  N     . PHE B 1 129 ? 144.296 154.826 160.524 1.00 27.70 ?  129 PHE B N     1 
ATOM   6627  C  CA    . PHE B 1 129 ? 142.991 155.385 160.863 1.00 21.42 ?  129 PHE B CA    1 
ATOM   6628  C  C     . PHE B 1 129 ? 143.097 156.840 161.298 1.00 30.37 ?  129 PHE B C     1 
ATOM   6629  O  O     . PHE B 1 129 ? 142.280 157.675 160.894 1.00 33.81 ?  129 PHE B O     1 
ATOM   6630  C  CB    . PHE B 1 129 ? 142.336 154.565 161.973 1.00 24.55 ?  129 PHE B CB    1 
ATOM   6631  C  CG    . PHE B 1 129 ? 141.680 153.306 161.500 1.00 26.58 ?  129 PHE B CG    1 
ATOM   6632  C  CD1   . PHE B 1 129 ? 141.425 153.100 160.157 1.00 26.21 ?  129 PHE B CD1   1 
ATOM   6633  C  CD2   . PHE B 1 129 ? 141.308 152.330 162.407 1.00 28.07 ?  129 PHE B CD2   1 
ATOM   6634  C  CE1   . PHE B 1 129 ? 140.818 151.939 159.729 1.00 25.06 ?  129 PHE B CE1   1 
ATOM   6635  C  CE2   . PHE B 1 129 ? 140.696 151.169 161.984 1.00 30.63 ?  129 PHE B CE2   1 
ATOM   6636  C  CZ    . PHE B 1 129 ? 140.453 150.973 160.644 1.00 30.17 ?  129 PHE B CZ    1 
ATOM   6637  N  N     . ALA B 1 130 ? 144.090 157.160 162.131 1.00 35.74 ?  130 ALA B N     1 
ATOM   6638  C  CA    . ALA B 1 130 ? 144.154 158.490 162.727 1.00 35.44 ?  130 ALA B CA    1 
ATOM   6639  C  C     . ALA B 1 130 ? 144.504 159.562 161.704 1.00 42.14 ?  130 ALA B C     1 
ATOM   6640  O  O     . ALA B 1 130 ? 144.074 160.712 161.848 1.00 47.31 ?  130 ALA B O     1 
ATOM   6641  C  CB    . ALA B 1 130 ? 145.161 158.501 163.870 1.00 33.44 ?  130 ALA B CB    1 
ATOM   6642  N  N     . ASN B 1 131 ? 145.284 159.212 160.680 1.00 41.73 ?  131 ASN B N     1 
ATOM   6643  C  CA    . ASN B 1 131 ? 145.628 160.128 159.591 1.00 41.38 ?  131 ASN B CA    1 
ATOM   6644  C  C     . ASN B 1 131 ? 146.349 161.373 160.110 1.00 42.82 ?  131 ASN B C     1 
ATOM   6645  O  O     . ASN B 1 131 ? 146.040 162.503 159.728 1.00 46.71 ?  131 ASN B O     1 
ATOM   6646  C  CB    . ASN B 1 131 ? 144.381 160.509 158.787 1.00 40.39 ?  131 ASN B CB    1 
ATOM   6647  C  CG    . ASN B 1 131 ? 144.706 160.931 157.371 1.00 46.02 ?  131 ASN B CG    1 
ATOM   6648  O  OD1   . ASN B 1 131 ? 145.552 160.331 156.709 1.00 45.99 ?  131 ASN B OD1   1 
ATOM   6649  N  ND2   . ASN B 1 131 ? 144.032 161.970 156.894 1.00 44.13 ?  131 ASN B ND2   1 
ATOM   6650  N  N     . GLY B 1 132 ? 147.323 161.157 160.992 1.00 42.48 ?  132 GLY B N     1 
ATOM   6651  C  CA    . GLY B 1 132 ? 148.180 162.222 161.475 1.00 39.49 ?  132 GLY B CA    1 
ATOM   6652  C  C     . GLY B 1 132 ? 147.963 162.630 162.916 1.00 44.84 ?  132 GLY B C     1 
ATOM   6653  O  O     . GLY B 1 132 ? 148.739 163.448 163.427 1.00 50.55 ?  132 GLY B O     1 
ATOM   6654  N  N     . ASP B 1 133 ? 146.950 162.098 163.592 1.00 46.99 ?  133 ASP B N     1 
ATOM   6655  C  CA    . ASP B 1 133 ? 146.659 162.452 164.975 1.00 47.34 ?  133 ASP B CA    1 
ATOM   6656  C  C     . ASP B 1 133 ? 147.233 161.382 165.897 1.00 48.68 ?  133 ASP B C     1 
ATOM   6657  O  O     . ASP B 1 133 ? 146.857 160.210 165.806 1.00 48.93 ?  133 ASP B O     1 
ATOM   6658  C  CB    . ASP B 1 133 ? 145.153 162.601 165.190 1.00 47.18 ?  133 ASP B CB    1 
ATOM   6659  C  CG    . ASP B 1 133 ? 144.813 163.335 166.474 1.00 52.90 ?  133 ASP B CG    1 
ATOM   6660  O  OD1   . ASP B 1 133 ? 145.716 163.530 167.313 1.00 54.28 ?  133 ASP B OD1   1 
ATOM   6661  O  OD2   . ASP B 1 133 ? 143.634 163.711 166.646 1.00 50.36 -1 133 ASP B OD2   1 
ATOM   6662  N  N     . THR B 1 134 ? 148.142 161.787 166.786 1.00 49.26 ?  134 THR B N     1 
ATOM   6663  C  CA    . THR B 1 134 ? 148.791 160.819 167.665 1.00 45.20 ?  134 THR B CA    1 
ATOM   6664  C  C     . THR B 1 134 ? 147.849 160.344 168.765 1.00 47.30 ?  134 THR B C     1 
ATOM   6665  O  O     . THR B 1 134 ? 147.805 159.149 169.078 1.00 50.75 ?  134 THR B O     1 
ATOM   6666  C  CB    . THR B 1 134 ? 150.055 161.426 168.268 1.00 53.73 ?  134 THR B CB    1 
ATOM   6667  O  OG1   . THR B 1 134 ? 150.908 161.882 167.212 1.00 55.93 ?  134 THR B OG1   1 
ATOM   6668  C  CG2   . THR B 1 134 ? 150.795 160.394 169.101 1.00 50.56 ?  134 THR B CG2   1 
ATOM   6669  N  N     . GLU B 1 135 ? 147.092 161.263 169.368 1.00 46.01 ?  135 GLU B N     1 
ATOM   6670  C  CA    . GLU B 1 135 ? 146.138 160.870 170.398 1.00 45.42 ?  135 GLU B CA    1 
ATOM   6671  C  C     . GLU B 1 135 ? 145.035 159.992 169.819 1.00 50.14 ?  135 GLU B C     1 
ATOM   6672  O  O     . GLU B 1 135 ? 144.614 159.017 170.451 1.00 51.83 ?  135 GLU B O     1 
ATOM   6673  C  CB    . GLU B 1 135 ? 145.547 162.108 171.068 1.00 47.74 ?  135 GLU B CB    1 
ATOM   6674  C  CG    . GLU B 1 135 ? 146.588 163.059 171.629 1.00 48.68 ?  135 GLU B CG    1 
ATOM   6675  C  CD    . GLU B 1 135 ? 147.705 162.338 172.354 1.00 55.32 ?  135 GLU B CD    1 
ATOM   6676  O  OE1   . GLU B 1 135 ? 147.421 161.658 173.363 1.00 54.01 ?  135 GLU B OE1   1 
ATOM   6677  O  OE2   . GLU B 1 135 ? 148.869 162.449 171.915 1.00 55.95 -1 135 GLU B OE2   1 
ATOM   6678  N  N     . LYS B 1 136 ? 144.557 160.325 168.619 1.00 40.63 ?  136 LYS B N     1 
ATOM   6679  C  CA    . LYS B 1 136 ? 143.564 159.485 167.959 1.00 38.65 ?  136 LYS B CA    1 
ATOM   6680  C  C     . LYS B 1 136 ? 144.132 158.107 167.645 1.00 39.71 ?  136 LYS B C     1 
ATOM   6681  O  O     . LYS B 1 136 ? 143.438 157.093 167.786 1.00 46.00 ?  136 LYS B O     1 
ATOM   6682  C  CB    . LYS B 1 136 ? 143.068 160.170 166.686 1.00 46.29 ?  136 LYS B CB    1 
ATOM   6683  C  CG    . LYS B 1 136 ? 141.775 159.612 166.127 1.00 41.83 ?  136 LYS B CG    1 
ATOM   6684  C  CD    . LYS B 1 136 ? 140.570 160.198 166.833 1.00 43.62 ?  136 LYS B CD    1 
ATOM   6685  C  CE    . LYS B 1 136 ? 139.288 159.886 166.080 1.00 46.52 ?  136 LYS B CE    1 
ATOM   6686  N  NZ    . LYS B 1 136 ? 138.139 160.677 166.598 1.00 49.13 1  136 LYS B NZ    1 
ATOM   6687  N  N     . ALA B 1 137 ? 145.393 158.048 167.208 1.00 34.81 ?  137 ALA B N     1 
ATOM   6688  C  CA    . ALA B 1 137 ? 146.025 156.761 166.942 1.00 31.55 ?  137 ALA B CA    1 
ATOM   6689  C  C     . ALA B 1 137 ? 146.142 155.931 168.213 1.00 35.22 ?  137 ALA B C     1 
ATOM   6690  O  O     . ALA B 1 137 ? 145.918 154.717 168.193 1.00 38.48 ?  137 ALA B O     1 
ATOM   6691  C  CB    . ALA B 1 137 ? 147.401 156.967 166.308 1.00 31.27 ?  137 ALA B CB    1 
ATOM   6692  N  N     . LYS B 1 138 ? 146.496 156.570 169.330 1.00 39.95 ?  138 LYS B N     1 
ATOM   6693  C  CA    . LYS B 1 138 ? 146.563 155.855 170.601 1.00 38.43 ?  138 LYS B CA    1 
ATOM   6694  C  C     . LYS B 1 138 ? 145.185 155.372 171.033 1.00 38.29 ?  138 LYS B C     1 
ATOM   6695  O  O     . LYS B 1 138 ? 145.049 154.281 171.597 1.00 41.57 ?  138 LYS B O     1 
ATOM   6696  C  CB    . LYS B 1 138 ? 147.185 156.748 171.673 1.00 46.55 ?  138 LYS B CB    1 
ATOM   6697  C  CG    . LYS B 1 138 ? 148.658 156.474 171.922 1.00 45.57 ?  138 LYS B CG    1 
ATOM   6698  C  CD    . LYS B 1 138 ? 149.471 157.755 171.933 1.00 42.75 ?  138 LYS B CD    1 
ATOM   6699  C  CE    . LYS B 1 138 ? 148.963 158.725 172.982 1.00 41.41 ?  138 LYS B CE    1 
ATOM   6700  N  NZ    . LYS B 1 138 ? 149.832 159.930 173.082 1.00 45.27 1  138 LYS B NZ    1 
ATOM   6701  N  N     . GLU B 1 139 ? 144.148 156.176 170.786 1.00 42.21 ?  139 GLU B N     1 
ATOM   6702  C  CA    . GLU B 1 139 ? 142.788 155.748 171.095 1.00 37.82 ?  139 GLU B CA    1 
ATOM   6703  C  C     . GLU B 1 139 ? 142.389 154.535 170.265 1.00 34.72 ?  139 GLU B C     1 
ATOM   6704  O  O     . GLU B 1 139 ? 141.774 153.596 170.783 1.00 43.86 ?  139 GLU B O     1 
ATOM   6705  C  CB    . GLU B 1 139 ? 141.811 156.900 170.868 1.00 36.39 ?  139 GLU B CB    1 
ATOM   6706  C  CG    . GLU B 1 139 ? 141.361 157.584 172.143 1.00 41.29 ?  139 GLU B CG    1 
ATOM   6707  C  CD    . GLU B 1 139 ? 141.177 159.078 171.971 1.00 49.30 ?  139 GLU B CD    1 
ATOM   6708  O  OE1   . GLU B 1 139 ? 140.640 159.495 170.922 1.00 46.90 ?  139 GLU B OE1   1 
ATOM   6709  O  OE2   . GLU B 1 139 ? 141.566 159.835 172.883 1.00 47.07 -1 139 GLU B OE2   1 
ATOM   6710  N  N     . TYR B 1 140 ? 142.728 154.537 168.975 1.00 27.13 ?  140 TYR B N     1 
ATOM   6711  C  CA    . TYR B 1 140 ? 142.445 153.377 168.133 1.00 28.57 ?  140 TYR B CA    1 
ATOM   6712  C  C     . TYR B 1 140 ? 143.227 152.156 168.601 1.00 32.48 ?  140 TYR B C     1 
ATOM   6713  O  O     . TYR B 1 140 ? 142.712 151.030 168.578 1.00 35.20 ?  140 TYR B O     1 
ATOM   6714  C  CB    . TYR B 1 140 ? 142.775 153.685 166.675 1.00 31.21 ?  140 TYR B CB    1 
ATOM   6715  C  CG    . TYR B 1 140 ? 141.784 154.574 165.966 1.00 33.68 ?  140 TYR B CG    1 
ATOM   6716  C  CD1   . TYR B 1 140 ? 140.437 154.246 165.908 1.00 36.18 ?  140 TYR B CD1   1 
ATOM   6717  C  CD2   . TYR B 1 140 ? 142.202 155.735 165.335 1.00 34.26 ?  140 TYR B CD2   1 
ATOM   6718  C  CE1   . TYR B 1 140 ? 139.536 155.057 165.250 1.00 34.00 ?  140 TYR B CE1   1 
ATOM   6719  C  CE2   . TYR B 1 140 ? 141.312 156.548 164.679 1.00 32.61 ?  140 TYR B CE2   1 
ATOM   6720  C  CZ    . TYR B 1 140 ? 139.981 156.208 164.639 1.00 30.34 ?  140 TYR B CZ    1 
ATOM   6721  O  OH    . TYR B 1 140 ? 139.100 157.030 163.979 1.00 37.65 ?  140 TYR B OH    1 
ATOM   6722  N  N     . VAL B 1 141 ? 144.481 152.357 169.014 1.00 36.80 ?  141 VAL B N     1 
ATOM   6723  C  CA    . VAL B 1 141 ? 145.287 151.259 169.539 1.00 34.60 ?  141 VAL B CA    1 
ATOM   6724  C  C     . VAL B 1 141 ? 144.636 150.668 170.780 1.00 31.82 ?  141 VAL B C     1 
ATOM   6725  O  O     . VAL B 1 141 ? 144.551 149.448 170.931 1.00 38.24 ?  141 VAL B O     1 
ATOM   6726  C  CB    . VAL B 1 141 ? 146.721 151.735 169.833 1.00 36.80 ?  141 VAL B CB    1 
ATOM   6727  C  CG1   . VAL B 1 141 ? 147.387 150.810 170.823 1.00 35.04 ?  141 VAL B CG1   1 
ATOM   6728  C  CG2   . VAL B 1 141 ? 147.529 151.774 168.564 1.00 35.06 ?  141 VAL B CG2   1 
ATOM   6729  N  N     . ASN B 1 142 ? 144.176 151.524 171.691 1.00 33.90 ?  142 ASN B N     1 
ATOM   6730  C  CA    . ASN B 1 142 ? 143.511 151.027 172.891 1.00 33.04 ?  142 ASN B CA    1 
ATOM   6731  C  C     . ASN B 1 142 ? 142.214 150.312 172.541 1.00 34.96 ?  142 ASN B C     1 
ATOM   6732  O  O     . ASN B 1 142 ? 141.871 149.300 173.160 1.00 41.23 ?  142 ASN B O     1 
ATOM   6733  C  CB    . ASN B 1 142 ? 143.250 152.177 173.861 1.00 30.82 ?  142 ASN B CB    1 
ATOM   6734  C  CG    . ASN B 1 142 ? 144.498 152.603 174.603 1.00 36.66 ?  142 ASN B CG    1 
ATOM   6735  O  OD1   . ASN B 1 142 ? 145.231 151.770 175.135 1.00 37.28 ?  142 ASN B OD1   1 
ATOM   6736  N  ND2   . ASN B 1 142 ? 144.750 153.905 174.640 1.00 38.79 ?  142 ASN B ND2   1 
ATOM   6737  N  N     . LEU B 1 143 ? 141.479 150.826 171.554 1.00 34.18 ?  143 LEU B N     1 
ATOM   6738  C  CA    . LEU B 1 143 ? 140.221 150.205 171.160 1.00 28.75 ?  143 LEU B CA    1 
ATOM   6739  C  C     . LEU B 1 143 ? 140.439 148.819 170.565 1.00 32.78 ?  143 LEU B C     1 
ATOM   6740  O  O     . LEU B 1 143 ? 139.670 147.892 170.842 1.00 36.15 ?  143 LEU B O     1 
ATOM   6741  C  CB    . LEU B 1 143 ? 139.486 151.104 170.169 1.00 28.80 ?  143 LEU B CB    1 
ATOM   6742  C  CG    . LEU B 1 143 ? 137.975 150.917 170.100 1.00 34.07 ?  143 LEU B CG    1 
ATOM   6743  C  CD1   . LEU B 1 143 ? 137.330 151.474 171.355 1.00 32.88 ?  143 LEU B CD1   1 
ATOM   6744  C  CD2   . LEU B 1 143 ? 137.419 151.589 168.863 1.00 33.46 ?  143 LEU B CD2   1 
ATOM   6745  N  N     . MET B 1 144 ? 141.474 148.657 169.742 1.00 34.58 ?  144 MET B N     1 
ATOM   6746  C  CA    . MET B 1 144 ? 141.688 147.393 169.048 1.00 24.95 ?  144 MET B CA    1 
ATOM   6747  C  C     . MET B 1 144 ? 142.488 146.382 169.860 1.00 25.64 ?  144 MET B C     1 
ATOM   6748  O  O     . MET B 1 144 ? 142.225 145.179 169.760 1.00 34.30 ?  144 MET B O     1 
ATOM   6749  C  CB    . MET B 1 144 ? 142.381 147.642 167.706 1.00 27.95 ?  144 MET B CB    1 
ATOM   6750  C  CG    . MET B 1 144 ? 141.528 148.424 166.721 1.00 28.00 ?  144 MET B CG    1 
ATOM   6751  S  SD    . MET B 1 144 ? 142.227 148.455 165.063 1.00 45.60 ?  144 MET B SD    1 
ATOM   6752  C  CE    . MET B 1 144 ? 143.665 149.480 165.338 1.00 26.96 ?  144 MET B CE    1 
ATOM   6753  N  N     . ILE B 1 145 ? 143.464 146.830 170.653 1.00 28.38 ?  145 ILE B N     1 
ATOM   6754  C  CA    . ILE B 1 145 ? 144.217 145.903 171.493 1.00 29.34 ?  145 ILE B CA    1 
ATOM   6755  C  C     . ILE B 1 145 ? 143.349 145.398 172.638 1.00 35.80 ?  145 ILE B C     1 
ATOM   6756  O  O     . ILE B 1 145 ? 143.517 144.262 173.096 1.00 39.90 ?  145 ILE B O     1 
ATOM   6757  C  CB    . ILE B 1 145 ? 145.521 146.559 171.989 1.00 31.03 ?  145 ILE B CB    1 
ATOM   6758  C  CG1   . ILE B 1 145 ? 146.610 145.502 172.186 1.00 32.44 ?  145 ILE B CG1   1 
ATOM   6759  C  CG2   . ILE B 1 145 ? 145.305 147.343 173.276 1.00 33.30 ?  145 ILE B CG2   1 
ATOM   6760  C  CD1   . ILE B 1 145 ? 147.108 144.887 170.901 1.00 35.50 ?  145 ILE B CD1   1 
ATOM   6761  N  N     . ASN B 1 146 ? 142.408 146.218 173.115 1.00 33.84 ?  146 ASN B N     1 
ATOM   6762  C  CA    . ASN B 1 146 ? 141.379 145.727 174.019 1.00 27.26 ?  146 ASN B CA    1 
ATOM   6763  C  C     . ASN B 1 146 ? 140.354 144.872 173.294 1.00 29.59 ?  146 ASN B C     1 
ATOM   6764  O  O     . ASN B 1 146 ? 139.510 144.254 173.951 1.00 38.22 ?  146 ASN B O     1 
ATOM   6765  C  CB    . ASN B 1 146 ? 140.678 146.891 174.717 1.00 27.33 ?  146 ASN B CB    1 
ATOM   6766  C  CG    . ASN B 1 146 ? 141.567 147.587 175.722 1.00 33.18 ?  146 ASN B CG    1 
ATOM   6767  O  OD1   . ASN B 1 146 ? 142.569 147.033 176.171 1.00 41.26 ?  146 ASN B OD1   1 
ATOM   6768  N  ND2   . ASN B 1 146 ? 141.206 148.813 176.081 1.00 34.54 ?  146 ASN B ND2   1 
ATOM   6769  N  N     . GLN B 1 147 ? 140.413 144.838 171.963 1.00 33.55 ?  147 GLN B N     1 
ATOM   6770  C  CA    . GLN B 1 147 ? 139.536 144.013 171.137 1.00 24.10 ?  147 GLN B CA    1 
ATOM   6771  C  C     . GLN B 1 147 ? 138.072 144.382 171.343 1.00 23.97 ?  147 GLN B C     1 
ATOM   6772  O  O     . GLN B 1 147 ? 137.193 143.521 171.353 1.00 38.00 ?  147 GLN B O     1 
ATOM   6773  C  CB    . GLN B 1 147 ? 139.774 142.525 171.400 1.00 23.94 ?  147 GLN B CB    1 
ATOM   6774  C  CG    . GLN B 1 147 ? 141.127 142.038 170.918 1.00 24.48 ?  147 GLN B CG    1 
ATOM   6775  C  CD    . GLN B 1 147 ? 141.193 140.537 170.791 1.00 31.06 ?  147 GLN B CD    1 
ATOM   6776  O  OE1   . GLN B 1 147 ? 140.733 139.808 171.669 1.00 41.78 ?  147 GLN B OE1   1 
ATOM   6777  N  NE2   . GLN B 1 147 ? 141.770 140.061 169.696 1.00 31.16 ?  147 GLN B NE2   1 
ATOM   6778  N  N     . GLU B 1 148 ? 137.811 145.676 171.523 1.00 25.67 ?  148 GLU B N     1 
ATOM   6779  C  CA    . GLU B 1 148 ? 136.437 146.161 171.558 1.00 23.25 ?  148 GLU B CA    1 
ATOM   6780  C  C     . GLU B 1 148 ? 135.880 146.375 170.160 1.00 29.08 ?  148 GLU B C     1 
ATOM   6781  O  O     . GLU B 1 148 ? 134.680 146.183 169.937 1.00 35.96 ?  148 GLU B O     1 
ATOM   6782  C  CB    . GLU B 1 148 ? 136.353 147.465 172.348 1.00 18.14 ?  148 GLU B CB    1 
ATOM   6783  C  CG    . GLU B 1 148 ? 136.742 147.345 173.804 1.00 21.97 ?  148 GLU B CG    1 
ATOM   6784  C  CD    . GLU B 1 148 ? 137.128 148.680 174.404 1.00 35.44 ?  148 GLU B CD    1 
ATOM   6785  O  OE1   . GLU B 1 148 ? 138.260 149.139 174.155 1.00 35.25 ?  148 GLU B OE1   1 
ATOM   6786  O  OE2   . GLU B 1 148 ? 136.298 149.275 175.121 1.00 42.82 -1 148 GLU B OE2   1 
ATOM   6787  N  N     . TYR B 1 149 ? 136.729 146.772 169.217 1.00 26.98 ?  149 TYR B N     1 
ATOM   6788  C  CA    . TYR B 1 149 ? 136.329 147.000 167.836 1.00 19.69 ?  149 TYR B CA    1 
ATOM   6789  C  C     . TYR B 1 149 ? 137.292 146.272 166.916 1.00 24.35 ?  149 TYR B C     1 
ATOM   6790  O  O     . TYR B 1 149 ? 138.511 146.373 167.080 1.00 32.74 ?  149 TYR B O     1 
ATOM   6791  C  CB    . TYR B 1 149 ? 136.312 148.492 167.501 1.00 22.94 ?  149 TYR B CB    1 
ATOM   6792  C  CG    . TYR B 1 149 ? 136.171 148.781 166.027 1.00 24.46 ?  149 TYR B CG    1 
ATOM   6793  C  CD1   . TYR B 1 149 ? 135.031 148.402 165.332 1.00 19.89 ?  149 TYR B CD1   1 
ATOM   6794  C  CD2   . TYR B 1 149 ? 137.180 149.428 165.327 1.00 17.39 ?  149 TYR B CD2   1 
ATOM   6795  C  CE1   . TYR B 1 149 ? 134.899 148.661 163.985 1.00 19.99 ?  149 TYR B CE1   1 
ATOM   6796  C  CE2   . TYR B 1 149 ? 137.056 149.690 163.981 1.00 24.90 ?  149 TYR B CE2   1 
ATOM   6797  C  CZ    . TYR B 1 149 ? 135.913 149.307 163.315 1.00 20.08 ?  149 TYR B CZ    1 
ATOM   6798  O  OH    . TYR B 1 149 ? 135.784 149.566 161.971 1.00 16.11 ?  149 TYR B OH    1 
ATOM   6799  N  N     . GLN B 1 150 ? 136.743 145.542 165.955 1.00 19.57 ?  150 GLN B N     1 
ATOM   6800  C  CA    . GLN B 1 150 ? 137.540 144.835 164.956 1.00 12.37 ?  150 GLN B CA    1 
ATOM   6801  C  C     . GLN B 1 150 ? 137.218 145.378 163.576 1.00 20.86 ?  150 GLN B C     1 
ATOM   6802  O  O     . GLN B 1 150 ? 136.083 145.200 163.094 1.00 32.26 ?  150 GLN B O     1 
ATOM   6803  C  CB    . GLN B 1 150 ? 137.272 143.332 165.017 1.00 19.69 ?  150 GLN B CB    1 
ATOM   6804  C  CG    . GLN B 1 150 ? 137.917 142.519 163.907 1.00 20.88 ?  150 GLN B CG    1 
ATOM   6805  C  CD    . GLN B 1 150 ? 139.417 142.708 163.835 1.00 20.38 ?  150 GLN B CD    1 
ATOM   6806  O  OE1   . GLN B 1 150 ? 140.147 142.319 164.743 1.00 27.08 ?  150 GLN B OE1   1 
ATOM   6807  N  NE2   . GLN B 1 150 ? 139.884 143.301 162.746 1.00 15.99 ?  150 GLN B NE2   1 
ATOM   6808  N  N     . PRO B 1 151 ? 138.152 146.049 162.907 1.00 27.09 ?  151 PRO B N     1 
ATOM   6809  C  CA    . PRO B 1 151 ? 137.934 146.402 161.502 1.00 14.54 ?  151 PRO B CA    1 
ATOM   6810  C  C     . PRO B 1 151 ? 137.776 145.146 160.662 1.00 20.56 ?  151 PRO B C     1 
ATOM   6811  O  O     . PRO B 1 151 ? 138.298 144.079 160.997 1.00 29.40 ?  151 PRO B O     1 
ATOM   6812  C  CB    . PRO B 1 151 ? 139.200 147.179 161.125 1.00 18.53 ?  151 PRO B CB    1 
ATOM   6813  C  CG    . PRO B 1 151 ? 139.790 147.612 162.423 1.00 20.87 ?  151 PRO B CG    1 
ATOM   6814  C  CD    . PRO B 1 151 ? 139.436 146.556 163.415 1.00 17.91 ?  151 PRO B CD    1 
ATOM   6815  N  N     . SER B 1 152 ? 137.032 145.276 159.569 1.00 24.85 ?  152 SER B N     1 
ATOM   6816  C  CA    . SER B 1 152 ? 136.743 144.128 158.724 1.00 18.45 ?  152 SER B CA    1 
ATOM   6817  C  C     . SER B 1 152 ? 138.030 143.520 158.174 1.00 24.70 ?  152 SER B C     1 
ATOM   6818  O  O     . SER B 1 152 ? 139.103 144.126 158.210 1.00 25.54 ?  152 SER B O     1 
ATOM   6819  C  CB    . SER B 1 152 ? 135.822 144.529 157.574 1.00 21.43 ?  152 SER B CB    1 
ATOM   6820  O  OG    . SER B 1 152 ? 136.468 145.433 156.697 1.00 26.76 ?  152 SER B OG    1 
ATOM   6821  N  N     . THR B 1 153 ? 137.906 142.295 157.668 1.00 32.55 ?  153 THR B N     1 
ATOM   6822  C  CA    . THR B 1 153 ? 139.051 141.605 157.081 1.00 20.41 ?  153 THR B CA    1 
ATOM   6823  C  C     . THR B 1 153 ? 139.773 142.430 156.019 1.00 31.50 ?  153 THR B C     1 
ATOM   6824  O  O     . THR B 1 153 ? 141.012 142.490 156.072 1.00 34.82 ?  153 THR B O     1 
ATOM   6825  C  CB    . THR B 1 153 ? 138.598 140.252 156.509 1.00 27.31 ?  153 THR B CB    1 
ATOM   6826  O  OG1   . THR B 1 153 ? 138.305 139.351 157.583 1.00 33.85 ?  153 THR B OG1   1 
ATOM   6827  C  CG2   . THR B 1 153 ? 139.678 139.646 155.631 1.00 30.48 ?  153 THR B CG2   1 
ATOM   6828  N  N     . PRO B 1 154 ? 139.101 143.087 155.065 1.00 33.93 ?  154 PRO B N     1 
ATOM   6829  C  CA    . PRO B 1 154 ? 139.852 143.949 154.134 1.00 21.38 ?  154 PRO B CA    1 
ATOM   6830  C  C     . PRO B 1 154 ? 140.597 145.074 154.829 1.00 22.56 ?  154 PRO B C     1 
ATOM   6831  O  O     . PRO B 1 154 ? 141.790 145.277 154.570 1.00 31.19 ?  154 PRO B O     1 
ATOM   6832  C  CB    . PRO B 1 154 ? 138.758 144.480 153.197 1.00 24.01 ?  154 PRO B CB    1 
ATOM   6833  C  CG    . PRO B 1 154 ? 137.661 143.508 153.311 1.00 22.70 ?  154 PRO B CG    1 
ATOM   6834  C  CD    . PRO B 1 154 ? 137.671 143.041 154.715 1.00 25.54 ?  154 PRO B CD    1 
ATOM   6835  N  N     . THR B 1 155 ? 139.927 145.808 155.718 1.00 25.99 ?  155 THR B N     1 
ATOM   6836  C  CA    . THR B 1 155 ? 140.574 146.924 156.399 1.00 22.14 ?  155 THR B CA    1 
ATOM   6837  C  C     . THR B 1 155 ? 141.708 146.442 157.294 1.00 25.99 ?  155 THR B C     1 
ATOM   6838  O  O     . THR B 1 155 ? 142.826 146.963 157.233 1.00 25.30 ?  155 THR B O     1 
ATOM   6839  C  CB    . THR B 1 155 ? 139.547 147.708 157.215 1.00 23.99 ?  155 THR B CB    1 
ATOM   6840  O  OG1   . THR B 1 155 ? 138.423 148.031 156.389 1.00 26.39 ?  155 THR B OG1   1 
ATOM   6841  C  CG2   . THR B 1 155 ? 140.162 148.987 157.745 1.00 20.80 ?  155 THR B CG2   1 
ATOM   6842  N  N     . PHE B 1 156 ? 141.440 145.438 158.130 1.00 30.04 ?  156 PHE B N     1 
ATOM   6843  C  CA    . PHE B 1 156 ? 142.457 144.953 159.056 1.00 21.34 ?  156 PHE B CA    1 
ATOM   6844  C  C     . PHE B 1 156 ? 143.652 144.371 158.313 1.00 29.13 ?  156 PHE B C     1 
ATOM   6845  O  O     . PHE B 1 156 ? 144.803 144.581 158.710 1.00 32.96 ?  156 PHE B O     1 
ATOM   6846  C  CB    . PHE B 1 156 ? 141.852 143.915 160.000 1.00 26.41 ?  156 PHE B CB    1 
ATOM   6847  C  CG    . PHE B 1 156 ? 142.654 143.692 161.249 1.00 30.29 ?  156 PHE B CG    1 
ATOM   6848  C  CD1   . PHE B 1 156 ? 142.950 144.746 162.093 1.00 28.22 ?  156 PHE B CD1   1 
ATOM   6849  C  CD2   . PHE B 1 156 ? 143.110 142.427 161.578 1.00 23.06 ?  156 PHE B CD2   1 
ATOM   6850  C  CE1   . PHE B 1 156 ? 143.687 144.546 163.241 1.00 30.39 ?  156 PHE B CE1   1 
ATOM   6851  C  CE2   . PHE B 1 156 ? 143.846 142.221 162.726 1.00 25.10 ?  156 PHE B CE2   1 
ATOM   6852  C  CZ    . PHE B 1 156 ? 144.135 143.282 163.557 1.00 30.21 ?  156 PHE B CZ    1 
ATOM   6853  N  N     . LEU B 1 157 ? 143.399 143.633 157.233 1.00 32.80 ?  157 LEU B N     1 
ATOM   6854  C  CA    . LEU B 1 157 ? 144.478 142.977 156.506 1.00 27.12 ?  157 LEU B CA    1 
ATOM   6855  C  C     . LEU B 1 157 ? 145.292 143.968 155.682 1.00 33.90 ?  157 LEU B C     1 
ATOM   6856  O  O     . LEU B 1 157 ? 146.521 143.857 155.611 1.00 41.74 ?  157 LEU B O     1 
ATOM   6857  C  CB    . LEU B 1 157 ? 143.900 141.883 155.611 1.00 32.38 ?  157 LEU B CB    1 
ATOM   6858  C  CG    . LEU B 1 157 ? 144.839 141.238 154.593 1.00 33.14 ?  157 LEU B CG    1 
ATOM   6859  C  CD1   . LEU B 1 157 ? 145.876 140.386 155.296 1.00 33.58 ?  157 LEU B CD1   1 
ATOM   6860  C  CD2   . LEU B 1 157 ? 144.051 140.412 153.594 1.00 30.09 ?  157 LEU B CD2   1 
ATOM   6861  N  N     . ASN B 1 158 ? 144.635 144.946 155.059 1.00 35.49 ?  158 ASN B N     1 
ATOM   6862  C  CA    . ASN B 1 158 ? 145.275 145.731 154.014 1.00 28.83 ?  158 ASN B CA    1 
ATOM   6863  C  C     . ASN B 1 158 ? 145.686 147.134 154.440 1.00 32.73 ?  158 ASN B C     1 
ATOM   6864  O  O     . ASN B 1 158 ? 146.490 147.754 153.737 1.00 39.64 ?  158 ASN B O     1 
ATOM   6865  C  CB    . ASN B 1 158 ? 144.345 145.837 152.799 1.00 33.04 ?  158 ASN B CB    1 
ATOM   6866  C  CG    . ASN B 1 158 ? 144.142 144.509 152.105 1.00 38.50 ?  158 ASN B CG    1 
ATOM   6867  O  OD1   . ASN B 1 158 ? 145.090 143.752 151.900 1.00 39.97 ?  158 ASN B OD1   1 
ATOM   6868  N  ND2   . ASN B 1 158 ? 142.901 144.215 151.742 1.00 36.86 ?  158 ASN B ND2   1 
ATOM   6869  N  N     . ALA B 1 159 ? 145.171 147.650 155.554 1.00 32.24 ?  159 ALA B N     1 
ATOM   6870  C  CA    . ALA B 1 159 ? 145.463 149.029 155.930 1.00 32.52 ?  159 ALA B CA    1 
ATOM   6871  C  C     . ALA B 1 159 ? 146.958 149.228 156.142 1.00 38.45 ?  159 ALA B C     1 
ATOM   6872  O  O     . ALA B 1 159 ? 147.602 148.471 156.874 1.00 44.26 ?  159 ALA B O     1 
ATOM   6873  C  CB    . ALA B 1 159 ? 144.698 149.412 157.194 1.00 33.14 ?  159 ALA B CB    1 
ATOM   6874  N  N     . GLY B 1 160 ? 147.506 150.254 155.499 1.00 43.15 ?  160 GLY B N     1 
ATOM   6875  C  CA    . GLY B 1 160 ? 148.917 150.550 155.622 1.00 38.96 ?  160 GLY B CA    1 
ATOM   6876  C  C     . GLY B 1 160 ? 149.846 149.623 154.876 1.00 41.97 ?  160 GLY B C     1 
ATOM   6877  O  O     . GLY B 1 160 ? 151.022 149.527 155.236 1.00 50.62 ?  160 GLY B O     1 
ATOM   6878  N  N     . ARG B 1 161 ? 149.362 148.934 153.847 1.00 44.25 ?  161 ARG B N     1 
ATOM   6879  C  CA    . ARG B 1 161 ? 150.175 148.023 153.058 1.00 44.56 ?  161 ARG B CA    1 
ATOM   6880  C  C     . ARG B 1 161 ? 150.305 148.539 151.631 1.00 48.02 ?  161 ARG B C     1 
ATOM   6881  O  O     . ARG B 1 161 ? 149.320 148.975 151.028 1.00 49.36 ?  161 ARG B O     1 
ATOM   6882  C  CB    . ARG B 1 161 ? 149.577 146.614 153.049 1.00 41.42 ?  161 ARG B CB    1 
ATOM   6883  C  CG    . ARG B 1 161 ? 149.671 145.895 154.382 1.00 41.80 ?  161 ARG B CG    1 
ATOM   6884  C  CD    . ARG B 1 161 ? 149.618 144.391 154.195 1.00 42.34 ?  161 ARG B CD    1 
ATOM   6885  N  NE    . ARG B 1 161 ? 149.584 143.687 155.469 1.00 44.00 ?  161 ARG B NE    1 
ATOM   6886  C  CZ    . ARG B 1 161 ? 149.245 142.414 155.614 1.00 46.38 ?  161 ARG B CZ    1 
ATOM   6887  N  NH1   . ARG B 1 161 ? 148.916 141.665 154.574 1.00 49.01 1  161 ARG B NH1   1 
ATOM   6888  N  NH2   . ARG B 1 161 ? 149.236 141.878 156.830 1.00 45.53 ?  161 ARG B NH2   1 
ATOM   6889  N  N     . LYS B 1 162 ? 151.528 148.491 151.101 1.00 57.73 ?  162 LYS B N     1 
ATOM   6890  C  CA    . LYS B 1 162 ? 151.771 148.974 149.745 1.00 57.20 ?  162 LYS B CA    1 
ATOM   6891  C  C     . LYS B 1 162 ? 151.109 148.071 148.711 1.00 58.40 ?  162 LYS B C     1 
ATOM   6892  O  O     . LYS B 1 162 ? 150.410 148.550 147.810 1.00 60.39 ?  162 LYS B O     1 
ATOM   6893  C  CB    . LYS B 1 162 ? 153.274 149.074 149.489 1.00 57.41 ?  162 LYS B CB    1 
ATOM   6894  C  CG    . LYS B 1 162 ? 153.648 149.295 148.036 1.00 59.42 ?  162 LYS B CG    1 
ATOM   6895  C  CD    . LYS B 1 162 ? 153.588 150.767 147.671 1.00 58.54 ?  162 LYS B CD    1 
ATOM   6896  C  CE    . LYS B 1 162 ? 154.654 151.559 148.410 1.00 57.34 ?  162 LYS B CE    1 
ATOM   6897  N  NZ    . LYS B 1 162 ? 154.340 153.014 148.445 1.00 58.40 1  162 LYS B NZ    1 
ATOM   6898  N  N     . ARG B 1 163 ? 151.316 146.760 148.825 1.00 57.99 ?  163 ARG B N     1 
ATOM   6899  C  CA    . ARG B 1 163 ? 150.710 145.796 147.907 1.00 60.65 ?  163 ARG B CA    1 
ATOM   6900  C  C     . ARG B 1 163 ? 149.414 145.244 148.502 1.00 62.84 ?  163 ARG B C     1 
ATOM   6901  O  O     . ARG B 1 163 ? 149.297 144.071 148.854 1.00 61.14 ?  163 ARG B O     1 
ATOM   6902  C  CB    . ARG B 1 163 ? 151.695 144.679 147.583 1.00 61.32 ?  163 ARG B CB    1 
ATOM   6903  C  CG    . ARG B 1 163 ? 152.766 145.069 146.579 1.00 62.25 ?  163 ARG B CG    1 
ATOM   6904  C  CD    . ARG B 1 163 ? 153.924 144.089 146.610 1.00 61.92 ?  163 ARG B CD    1 
ATOM   6905  N  NE    . ARG B 1 163 ? 154.818 144.337 147.734 1.00 64.82 ?  163 ARG B NE    1 
ATOM   6906  C  CZ    . ARG B 1 163 ? 155.573 143.410 148.307 1.00 66.36 ?  163 ARG B CZ    1 
ATOM   6907  N  NH1   . ARG B 1 163 ? 155.566 142.155 147.887 1.00 63.10 1  163 ARG B NH1   1 
ATOM   6908  N  NH2   . ARG B 1 163 ? 156.356 143.751 149.327 1.00 62.68 ?  163 ARG B NH2   1 
ATOM   6909  N  N     . ARG B 1 164 ? 148.430 146.129 148.607 1.00 56.69 ?  164 ARG B N     1 
ATOM   6910  C  CA    . ARG B 1 164 ? 147.168 145.830 149.261 1.00 53.92 ?  164 ARG B CA    1 
ATOM   6911  C  C     . ARG B 1 164 ? 146.026 145.842 148.256 1.00 53.28 ?  164 ARG B C     1 
ATOM   6912  O  O     . ARG B 1 164 ? 146.092 146.508 147.218 1.00 52.80 ?  164 ARG B O     1 
ATOM   6913  C  CB    . ARG B 1 164 ? 146.874 146.840 150.375 1.00 52.22 ?  164 ARG B CB    1 
ATOM   6914  C  CG    . ARG B 1 164 ? 146.391 148.194 149.870 1.00 51.00 ?  164 ARG B CG    1 
ATOM   6915  C  CD    . ARG B 1 164 ? 145.899 149.072 151.008 1.00 53.16 ?  164 ARG B CD    1 
ATOM   6916  N  NE    . ARG B 1 164 ? 145.639 150.444 150.588 1.00 53.94 ?  164 ARG B NE    1 
ATOM   6917  C  CZ    . ARG B 1 164 ? 144.555 150.834 149.930 1.00 56.41 ?  164 ARG B CZ    1 
ATOM   6918  N  NH1   . ARG B 1 164 ? 143.604 149.978 149.593 1.00 51.21 1  164 ARG B NH1   1 
ATOM   6919  N  NH2   . ARG B 1 164 ? 144.423 152.116 149.602 1.00 56.21 ?  164 ARG B NH2   1 
ATOM   6920  N  N     . GLY B 1 165 ? 144.981 145.082 148.570 1.00 50.68 ?  165 GLY B N     1 
ATOM   6921  C  CA    . GLY B 1 165 ? 143.716 145.223 147.889 1.00 47.35 ?  165 GLY B CA    1 
ATOM   6922  C  C     . GLY B 1 165 ? 142.930 146.389 148.450 1.00 51.38 ?  165 GLY B C     1 
ATOM   6923  O  O     . GLY B 1 165 ? 143.390 147.139 149.310 1.00 52.32 ?  165 GLY B O     1 
ATOM   6924  N  N     . GLU B 1 166 ? 141.713 146.544 147.945 1.00 48.09 ?  166 GLU B N     1 
ATOM   6925  C  CA    . GLU B 1 166 ? 140.847 147.601 148.442 1.00 42.72 ?  166 GLU B CA    1 
ATOM   6926  C  C     . GLU B 1 166 ? 140.415 147.304 149.874 1.00 42.86 ?  166 GLU B C     1 
ATOM   6927  O  O     . GLU B 1 166 ? 140.343 146.149 150.301 1.00 39.32 ?  166 GLU B O     1 
ATOM   6928  C  CB    . GLU B 1 166 ? 139.624 147.760 147.541 1.00 41.35 ?  166 GLU B CB    1 
ATOM   6929  C  CG    . GLU B 1 166 ? 139.232 149.206 147.278 1.00 45.08 ?  166 GLU B CG    1 
ATOM   6930  C  CD    . GLU B 1 166 ? 140.295 149.976 146.514 1.00 49.94 ?  166 GLU B CD    1 
ATOM   6931  O  OE1   . GLU B 1 166 ? 141.083 149.343 145.780 1.00 49.58 ?  166 GLU B OE1   1 
ATOM   6932  O  OE2   . GLU B 1 166 ? 140.344 151.216 146.650 1.00 48.28 -1 166 GLU B OE2   1 
ATOM   6933  N  N     . LEU B 1 167 ? 140.133 148.369 150.624 1.00 38.04 ?  167 LEU B N     1 
ATOM   6934  C  CA    . LEU B 1 167 ? 139.640 148.224 151.986 1.00 32.21 ?  167 LEU B CA    1 
ATOM   6935  C  C     . LEU B 1 167 ? 138.154 147.895 152.037 1.00 35.31 ?  167 LEU B C     1 
ATOM   6936  O  O     . LEU B 1 167 ? 137.639 147.597 153.119 1.00 38.65 ?  167 LEU B O     1 
ATOM   6937  C  CB    . LEU B 1 167 ? 139.916 149.501 152.784 1.00 33.90 ?  167 LEU B CB    1 
ATOM   6938  C  CG    . LEU B 1 167 ? 141.165 149.524 153.670 1.00 34.71 ?  167 LEU B CG    1 
ATOM   6939  C  CD1   . LEU B 1 167 ? 142.359 148.910 152.961 1.00 31.87 ?  167 LEU B CD1   1 
ATOM   6940  C  CD2   . LEU B 1 167 ? 141.475 150.943 154.098 1.00 32.27 ?  167 LEU B CD2   1 
ATOM   6941  N  N     . VAL B 1 168 ? 137.466 147.942 150.901 1.00 36.93 ?  168 VAL B N     1 
ATOM   6942  C  CA    . VAL B 1 168 ? 136.062 147.570 150.793 1.00 28.61 ?  168 VAL B CA    1 
ATOM   6943  C  C     . VAL B 1 168 ? 135.979 146.281 149.989 1.00 33.31 ?  168 VAL B C     1 
ATOM   6944  O  O     . VAL B 1 168 ? 136.681 146.122 148.985 1.00 39.76 ?  168 VAL B O     1 
ATOM   6945  C  CB    . VAL B 1 168 ? 135.233 148.689 150.130 1.00 27.73 ?  168 VAL B CB    1 
ATOM   6946  C  CG1   . VAL B 1 168 ? 133.761 148.313 150.082 1.00 34.50 ?  168 VAL B CG1   1 
ATOM   6947  C  CG2   . VAL B 1 168 ? 135.428 149.999 150.868 1.00 31.65 ?  168 VAL B CG2   1 
ATOM   6948  N  N     . SER B 1 169 ? 135.130 145.356 150.437 1.00 29.47 ?  169 SER B N     1 
ATOM   6949  C  CA    . SER B 1 169 ? 134.963 144.088 149.744 1.00 29.73 ?  169 SER B CA    1 
ATOM   6950  C  C     . SER B 1 169 ? 133.523 143.766 149.374 1.00 31.28 ?  169 SER B C     1 
ATOM   6951  O  O     . SER B 1 169 ? 133.285 142.721 148.761 1.00 40.22 ?  169 SER B O     1 
ATOM   6952  C  CB    . SER B 1 169 ? 135.532 142.934 150.582 1.00 36.48 ?  169 SER B CB    1 
ATOM   6953  O  OG    . SER B 1 169 ? 136.917 142.768 150.337 1.00 43.76 ?  169 SER B OG    1 
ATOM   6954  N  N     . CYS B 1 170 ? 132.562 144.612 149.726 1.00 25.02 ?  170 CYS B N     1 
ATOM   6955  C  CA    . CYS B 1 170 ? 131.172 144.411 149.340 1.00 23.57 ?  170 CYS B CA    1 
ATOM   6956  C  C     . CYS B 1 170 ? 130.759 145.535 148.405 1.00 23.82 ?  170 CYS B C     1 
ATOM   6957  O  O     . CYS B 1 170 ? 130.864 146.714 148.759 1.00 31.72 ?  170 CYS B O     1 
ATOM   6958  C  CB    . CYS B 1 170 ? 130.253 144.344 150.564 1.00 34.88 ?  170 CYS B CB    1 
ATOM   6959  S  SG    . CYS B 1 170 ? 130.351 145.743 151.700 1.00 46.19 ?  170 CYS B SG    1 
ATOM   6960  N  N     . PHE B 1 171 ? 130.304 145.169 147.211 1.00 25.86 ?  171 PHE B N     1 
ATOM   6961  C  CA    . PHE B 1 171 ? 129.837 146.119 146.214 1.00 11.61 ?  171 PHE B CA    1 
ATOM   6962  C  C     . PHE B 1 171 ? 128.499 145.651 145.671 1.00 16.26 ?  171 PHE B C     1 
ATOM   6963  O  O     . PHE B 1 171 ? 128.262 144.447 145.536 1.00 24.49 ?  171 PHE B O     1 
ATOM   6964  C  CB    . PHE B 1 171 ? 130.847 146.277 145.073 1.00 17.72 ?  171 PHE B CB    1 
ATOM   6965  C  CG    . PHE B 1 171 ? 132.236 146.585 145.539 1.00 17.83 ?  171 PHE B CG    1 
ATOM   6966  C  CD1   . PHE B 1 171 ? 132.595 147.876 145.874 1.00 19.98 ?  171 PHE B CD1   1 
ATOM   6967  C  CD2   . PHE B 1 171 ? 133.184 145.584 145.640 1.00 19.73 ?  171 PHE B CD2   1 
ATOM   6968  C  CE1   . PHE B 1 171 ? 133.869 148.162 146.309 1.00 13.29 ?  171 PHE B CE1   1 
ATOM   6969  C  CE2   . PHE B 1 171 ? 134.460 145.866 146.073 1.00 17.80 ?  171 PHE B CE2   1 
ATOM   6970  C  CZ    . PHE B 1 171 ? 134.803 147.157 146.406 1.00 10.83 ?  171 PHE B CZ    1 
ATOM   6971  N  N     . LEU B 1 172 ? 127.626 146.606 145.370 1.00 14.93 ?  172 LEU B N     1 
ATOM   6972  C  CA    . LEU B 1 172 ? 126.293 146.324 144.854 1.00 7.54  ?  172 LEU B CA    1 
ATOM   6973  C  C     . LEU B 1 172 ? 126.091 147.142 143.592 1.00 13.54 ?  172 LEU B C     1 
ATOM   6974  O  O     . LEU B 1 172 ? 126.083 148.376 143.647 1.00 21.70 ?  172 LEU B O     1 
ATOM   6975  C  CB    . LEU B 1 172 ? 125.212 146.653 145.886 1.00 8.45  ?  172 LEU B CB    1 
ATOM   6976  C  CG    . LEU B 1 172 ? 125.117 145.812 147.157 1.00 2.85  ?  172 LEU B CG    1 
ATOM   6977  C  CD1   . LEU B 1 172 ? 126.162 146.231 148.176 1.00 11.18 ?  172 LEU B CD1   1 
ATOM   6978  C  CD2   . LEU B 1 172 ? 123.730 145.945 147.741 1.00 16.09 ?  172 LEU B CD2   1 
ATOM   6979  N  N     . LEU B 1 173 ? 125.913 146.462 142.465 1.00 20.16 ?  173 LEU B N     1 
ATOM   6980  C  CA    . LEU B 1 173 ? 125.785 147.109 141.169 1.00 8.80  ?  173 LEU B CA    1 
ATOM   6981  C  C     . LEU B 1 173 ? 124.373 146.948 140.628 1.00 18.02 ?  173 LEU B C     1 
ATOM   6982  O  O     . LEU B 1 173 ? 123.791 145.861 140.692 1.00 29.94 ?  173 LEU B O     1 
ATOM   6983  C  CB    . LEU B 1 173 ? 126.780 146.527 140.164 1.00 13.72 ?  173 LEU B CB    1 
ATOM   6984  C  CG    . LEU B 1 173 ? 128.242 146.402 140.586 1.00 19.57 ?  173 LEU B CG    1 
ATOM   6985  C  CD1   . LEU B 1 173 ? 129.060 145.906 139.410 1.00 22.40 ?  173 LEU B CD1   1 
ATOM   6986  C  CD2   . LEU B 1 173 ? 128.776 147.727 141.093 1.00 25.38 ?  173 LEU B CD2   1 
ATOM   6987  N  N     . GLU B 1 174 ? 123.826 148.037 140.104 1.00 26.42 ?  174 GLU B N     1 
ATOM   6988  C  CA    . GLU B 1 174 ? 122.603 147.988 139.319 1.00 22.09 ?  174 GLU B CA    1 
ATOM   6989  C  C     . GLU B 1 174 ? 122.959 147.773 137.856 1.00 20.40 ?  174 GLU B C     1 
ATOM   6990  O  O     . GLU B 1 174 ? 123.872 148.412 137.329 1.00 31.33 ?  174 GLU B O     1 
ATOM   6991  C  CB    . GLU B 1 174 ? 121.804 149.282 139.474 1.00 26.22 ?  174 GLU B CB    1 
ATOM   6992  C  CG    . GLU B 1 174 ? 121.240 149.523 140.857 1.00 22.93 ?  174 GLU B CG    1 
ATOM   6993  C  CD    . GLU B 1 174 ? 119.749 149.283 140.920 1.00 27.60 ?  174 GLU B CD    1 
ATOM   6994  O  OE1   . GLU B 1 174 ? 119.179 148.816 139.913 1.00 31.09 ?  174 GLU B OE1   1 
ATOM   6995  O  OE2   . GLU B 1 174 ? 119.144 149.568 141.973 1.00 26.84 -1 174 GLU B OE2   1 
ATOM   6996  N  N     . VAL B 1 175 ? 122.235 146.870 137.202 1.00 17.81 ?  175 VAL B N     1 
ATOM   6997  C  CA    . VAL B 1 175 ? 122.447 146.565 135.793 1.00 17.01 ?  175 VAL B CA    1 
ATOM   6998  C  C     . VAL B 1 175 ? 121.226 147.042 135.021 1.00 21.62 ?  175 VAL B C     1 
ATOM   6999  O  O     . VAL B 1 175 ? 120.100 146.611 135.297 1.00 24.85 ?  175 VAL B O     1 
ATOM   7000  C  CB    . VAL B 1 175 ? 122.697 145.066 135.566 1.00 18.44 ?  175 VAL B CB    1 
ATOM   7001  C  CG1   . VAL B 1 175 ? 123.192 144.819 134.152 1.00 7.81  ?  175 VAL B CG1   1 
ATOM   7002  C  CG2   . VAL B 1 175 ? 123.689 144.533 136.588 1.00 18.22 ?  175 VAL B CG2   1 
ATOM   7003  N  N     . ASN B 1 176 ? 121.447 147.929 134.059 1.00 17.07 ?  176 ASN B N     1 
ATOM   7004  C  CA    . ASN B 1 176 ? 120.373 148.448 133.229 1.00 18.01 ?  176 ASN B CA    1 
ATOM   7005  C  C     . ASN B 1 176 ? 120.103 147.512 132.056 1.00 22.69 ?  176 ASN B C     1 
ATOM   7006  O  O     . ASN B 1 176 ? 120.949 146.706 131.661 1.00 27.73 ?  176 ASN B O     1 
ATOM   7007  C  CB    . ASN B 1 176 ? 120.712 149.848 132.721 1.00 19.42 ?  176 ASN B CB    1 
ATOM   7008  C  CG    . ASN B 1 176 ? 119.514 150.766 132.694 1.00 17.10 ?  176 ASN B CG    1 
ATOM   7009  O  OD1   . ASN B 1 176 ? 118.372 150.314 132.676 1.00 26.13 ?  176 ASN B OD1   1 
ATOM   7010  N  ND2   . ASN B 1 176 ? 119.769 152.066 132.693 1.00 18.44 ?  176 ASN B ND2   1 
ATOM   7011  N  N     . ASP B 1 177 ? 118.901 147.635 131.493 1.00 27.31 ?  177 ASP B N     1 
ATOM   7012  C  CA    . ASP B 1 177 ? 118.437 146.741 130.434 1.00 23.71 ?  177 ASP B CA    1 
ATOM   7013  C  C     . ASP B 1 177 ? 118.980 147.229 129.092 1.00 24.80 ?  177 ASP B C     1 
ATOM   7014  O  O     . ASP B 1 177 ? 118.287 147.861 128.291 1.00 31.45 ?  177 ASP B O     1 
ATOM   7015  C  CB    . ASP B 1 177 ? 116.917 146.666 130.437 1.00 20.34 ?  177 ASP B CB    1 
ATOM   7016  C  CG    . ASP B 1 177 ? 116.391 145.527 129.600 1.00 26.79 ?  177 ASP B CG    1 
ATOM   7017  O  OD1   . ASP B 1 177 ? 117.046 144.465 129.561 1.00 34.35 ?  177 ASP B OD1   1 
ATOM   7018  O  OD2   . ASP B 1 177 ? 115.317 145.692 128.986 1.00 33.24 -1 177 ASP B OD2   1 
ATOM   7019  N  N     . SER B 1 178 ? 120.248 146.914 128.848 1.00 19.77 ?  178 SER B N     1 
ATOM   7020  C  CA    . SER B 1 178 ? 120.919 147.279 127.608 1.00 17.17 ?  178 SER B CA    1 
ATOM   7021  C  C     . SER B 1 178 ? 122.217 146.493 127.515 1.00 21.75 ?  178 SER B C     1 
ATOM   7022  O  O     . SER B 1 178 ? 122.794 146.097 128.531 1.00 34.49 ?  178 SER B O     1 
ATOM   7023  C  CB    . SER B 1 178 ? 121.194 148.785 127.534 1.00 14.65 ?  178 SER B CB    1 
ATOM   7024  O  OG    . SER B 1 178 ? 122.443 149.105 128.112 1.00 27.93 ?  178 SER B OG    1 
ATOM   7025  N  N     . LEU B 1 179 ? 122.666 146.264 126.278 1.00 32.35 ?  179 LEU B N     1 
ATOM   7026  C  CA    . LEU B 1 179 ? 123.922 145.550 126.072 1.00 19.98 ?  179 LEU B CA    1 
ATOM   7027  C  C     . LEU B 1 179 ? 125.109 146.373 126.552 1.00 17.04 ?  179 LEU B C     1 
ATOM   7028  O  O     . LEU B 1 179 ? 126.074 145.823 127.093 1.00 26.29 ?  179 LEU B O     1 
ATOM   7029  C  CB    . LEU B 1 179 ? 124.088 145.182 124.598 1.00 23.05 ?  179 LEU B CB    1 
ATOM   7030  C  CG    . LEU B 1 179 ? 125.286 144.287 124.274 1.00 23.10 ?  179 LEU B CG    1 
ATOM   7031  C  CD1   . LEU B 1 179 ? 125.082 142.895 124.847 1.00 20.90 ?  179 LEU B CD1   1 
ATOM   7032  C  CD2   . LEU B 1 179 ? 125.523 144.224 122.776 1.00 21.71 ?  179 LEU B CD2   1 
ATOM   7033  N  N     . ASN B 1 180 ? 125.059 147.693 126.356 1.00 19.32 ?  180 ASN B N     1 
ATOM   7034  C  CA    . ASN B 1 180 ? 126.112 148.563 126.869 1.00 14.81 ?  180 ASN B CA    1 
ATOM   7035  C  C     . ASN B 1 180 ? 126.224 148.440 128.382 1.00 22.05 ?  180 ASN B C     1 
ATOM   7036  O  O     . ASN B 1 180 ? 127.323 148.281 128.930 1.00 30.45 ?  180 ASN B O     1 
ATOM   7037  C  CB    . ASN B 1 180 ? 125.830 150.012 126.472 1.00 23.77 ?  180 ASN B CB    1 
ATOM   7038  C  CG    . ASN B 1 180 ? 126.280 150.332 125.063 1.00 29.53 ?  180 ASN B CG    1 
ATOM   7039  O  OD1   . ASN B 1 180 ? 127.108 149.631 124.489 1.00 34.41 ?  180 ASN B OD1   1 
ATOM   7040  N  ND2   . ASN B 1 180 ? 125.732 151.401 124.499 1.00 27.63 ?  180 ASN B ND2   1 
ATOM   7041  N  N     . ASP B 1 181 ? 125.085 148.488 129.072 1.00 24.53 ?  181 ASP B N     1 
ATOM   7042  C  CA    . ASP B 1 181 ? 125.086 148.404 130.526 1.00 15.71 ?  181 ASP B CA    1 
ATOM   7043  C  C     . ASP B 1 181 ? 125.473 147.013 131.011 1.00 20.15 ?  181 ASP B C     1 
ATOM   7044  O  O     . ASP B 1 181 ? 126.135 146.888 132.041 1.00 30.36 ?  181 ASP B O     1 
ATOM   7045  C  CB    . ASP B 1 181 ? 123.718 148.805 131.066 1.00 27.99 ?  181 ASP B CB    1 
ATOM   7046  C  CG    . ASP B 1 181 ? 123.426 150.280 130.865 1.00 31.71 ?  181 ASP B CG    1 
ATOM   7047  O  OD1   . ASP B 1 181 ? 124.044 151.110 131.562 1.00 32.18 ?  181 ASP B OD1   1 
ATOM   7048  O  OD2   . ASP B 1 181 ? 122.577 150.610 130.012 1.00 26.06 -1 181 ASP B OD2   1 
ATOM   7049  N  N     . ILE B 1 182 ? 125.084 145.963 130.287 1.00 21.62 ?  182 ILE B N     1 
ATOM   7050  C  CA    . ILE B 1 182 ? 125.470 144.610 130.677 1.00 21.44 ?  182 ILE B CA    1 
ATOM   7051  C  C     . ILE B 1 182 ? 126.974 144.411 130.521 1.00 19.32 ?  182 ILE B C     1 
ATOM   7052  O  O     . ILE B 1 182 ? 127.633 143.827 131.392 1.00 22.73 ?  182 ILE B O     1 
ATOM   7053  C  CB    . ILE B 1 182 ? 124.665 143.576 129.869 1.00 19.85 ?  182 ILE B CB    1 
ATOM   7054  C  CG1   . ILE B 1 182 ? 123.243 143.472 130.421 1.00 20.49 ?  182 ILE B CG1   1 
ATOM   7055  C  CG2   . ILE B 1 182 ? 125.344 142.219 129.891 1.00 22.79 ?  182 ILE B CG2   1 
ATOM   7056  C  CD1   . ILE B 1 182 ? 122.283 142.782 129.496 1.00 23.22 ?  182 ILE B CD1   1 
ATOM   7057  N  N     . SER B 1 183 ? 127.542 144.893 129.415 1.00 26.18 ?  183 SER B N     1 
ATOM   7058  C  CA    . SER B 1 183 ? 128.986 144.802 129.227 1.00 16.94 ?  183 SER B CA    1 
ATOM   7059  C  C     . SER B 1 183 ? 129.728 145.611 130.281 1.00 19.44 ?  183 SER B C     1 
ATOM   7060  O  O     . SER B 1 183 ? 130.753 145.164 130.812 1.00 27.79 ?  183 SER B O     1 
ATOM   7061  C  CB    . SER B 1 183 ? 129.362 145.274 127.826 1.00 17.25 ?  183 SER B CB    1 
ATOM   7062  O  OG    . SER B 1 183 ? 128.839 146.561 127.566 1.00 33.98 ?  183 SER B OG    1 
ATOM   7063  N  N     . ARG B 1 184 ? 129.225 146.806 130.602 1.00 25.39 ?  184 ARG B N     1 
ATOM   7064  C  CA    . ARG B 1 184 ? 129.847 147.602 131.652 1.00 17.87 ?  184 ARG B CA    1 
ATOM   7065  C  C     . ARG B 1 184 ? 129.736 146.914 133.006 1.00 26.39 ?  184 ARG B C     1 
ATOM   7066  O  O     . ARG B 1 184 ? 130.657 146.992 133.823 1.00 31.50 ?  184 ARG B O     1 
ATOM   7067  C  CB    . ARG B 1 184 ? 129.217 148.991 131.702 1.00 16.95 ?  184 ARG B CB    1 
ATOM   7068  C  CG    . ARG B 1 184 ? 129.923 149.943 132.648 1.00 27.61 ?  184 ARG B CG    1 
ATOM   7069  C  CD    . ARG B 1 184 ? 131.420 149.943 132.424 1.00 26.09 ?  184 ARG B CD    1 
ATOM   7070  N  NE    . ARG B 1 184 ? 131.812 150.912 131.411 1.00 34.37 ?  184 ARG B NE    1 
ATOM   7071  C  CZ    . ARG B 1 184 ? 132.977 150.905 130.778 1.00 34.93 ?  184 ARG B CZ    1 
ATOM   7072  N  NH1   . ARG B 1 184 ? 133.893 149.984 131.028 1.00 25.59 1  184 ARG B NH1   1 
ATOM   7073  N  NH2   . ARG B 1 184 ? 133.229 151.847 129.874 1.00 32.42 ?  184 ARG B NH2   1 
ATOM   7074  N  N     . ALA B 1 185 ? 128.612 146.246 133.268 1.00 31.15 ?  185 ALA B N     1 
ATOM   7075  C  CA    . ALA B 1 185 ? 128.458 145.505 134.513 1.00 8.29  ?  185 ALA B CA    1 
ATOM   7076  C  C     . ALA B 1 185 ? 129.459 144.366 134.600 1.00 12.71 ?  185 ALA B C     1 
ATOM   7077  O  O     . ALA B 1 185 ? 130.047 144.130 135.660 1.00 22.32 ?  185 ALA B O     1 
ATOM   7078  C  CB    . ALA B 1 185 ? 127.031 144.973 134.636 1.00 9.14  ?  185 ALA B CB    1 
ATOM   7079  N  N     . ILE B 1 186 ? 129.670 143.648 133.496 1.00 22.82 ?  186 ILE B N     1 
ATOM   7080  C  CA    . ILE B 1 186 ? 130.670 142.582 133.484 1.00 23.20 ?  186 ILE B CA    1 
ATOM   7081  C  C     . ILE B 1 186 ? 132.059 143.156 133.736 1.00 17.77 ?  186 ILE B C     1 
ATOM   7082  O  O     . ILE B 1 186 ? 132.843 142.612 134.528 1.00 26.42 ?  186 ILE B O     1 
ATOM   7083  C  CB    . ILE B 1 186 ? 130.608 141.806 132.154 1.00 27.87 ?  186 ILE B CB    1 
ATOM   7084  C  CG1   . ILE B 1 186 ? 129.426 140.838 132.158 1.00 21.95 ?  186 ILE B CG1   1 
ATOM   7085  C  CG2   . ILE B 1 186 ? 131.905 141.052 131.901 1.00 23.79 ?  186 ILE B CG2   1 
ATOM   7086  C  CD1   . ILE B 1 186 ? 128.761 140.695 130.813 1.00 27.46 ?  186 ILE B CD1   1 
ATOM   7087  N  N     . ASP B 1 187 ? 132.379 144.273 133.080 1.00 23.35 ?  187 ASP B N     1 
ATOM   7088  C  CA    . ASP B 1 187 ? 133.680 144.906 133.267 1.00 18.17 ?  187 ASP B CA    1 
ATOM   7089  C  C     . ASP B 1 187 ? 133.886 145.333 134.716 1.00 28.09 ?  187 ASP B C     1 
ATOM   7090  O  O     . ASP B 1 187 ? 134.933 145.063 135.311 1.00 34.35 ?  187 ASP B O     1 
ATOM   7091  C  CB    . ASP B 1 187 ? 133.813 146.106 132.330 1.00 17.20 ?  187 ASP B CB    1 
ATOM   7092  C  CG    . ASP B 1 187 ? 134.893 147.073 132.769 1.00 35.28 ?  187 ASP B CG    1 
ATOM   7093  O  OD1   . ASP B 1 187 ? 136.051 146.640 132.941 1.00 34.32 ?  187 ASP B OD1   1 
ATOM   7094  O  OD2   . ASP B 1 187 ? 134.583 148.269 132.948 1.00 41.83 -1 187 ASP B OD2   1 
ATOM   7095  N  N     . ILE B 1 188 ? 132.889 146.000 135.299 1.00 23.60 ?  188 ILE B N     1 
ATOM   7096  C  CA    . ILE B 1 188 ? 133.015 146.495 136.665 1.00 22.56 ?  188 ILE B CA    1 
ATOM   7097  C  C     . ILE B 1 188 ? 133.070 145.338 137.652 1.00 25.27 ?  188 ILE B C     1 
ATOM   7098  O  O     . ILE B 1 188 ? 133.793 145.393 138.652 1.00 27.77 ?  188 ILE B O     1 
ATOM   7099  C  CB    . ILE B 1 188 ? 131.867 147.468 136.988 1.00 26.73 ?  188 ILE B CB    1 
ATOM   7100  C  CG1   . ILE B 1 188 ? 131.967 148.720 136.121 1.00 25.52 ?  188 ILE B CG1   1 
ATOM   7101  C  CG2   . ILE B 1 188 ? 131.901 147.875 138.444 1.00 26.77 ?  188 ILE B CG2   1 
ATOM   7102  C  CD1   . ILE B 1 188 ? 130.793 149.652 136.281 1.00 21.59 ?  188 ILE B CD1   1 
ATOM   7103  N  N     . SER B 1 189 ? 132.310 144.273 137.394 1.00 19.85 ?  189 SER B N     1 
ATOM   7104  C  CA    . SER B 1 189 ? 132.373 143.095 138.248 1.00 13.40 ?  189 SER B CA    1 
ATOM   7105  C  C     . SER B 1 189 ? 133.763 142.480 138.228 1.00 20.94 ?  189 SER B C     1 
ATOM   7106  O  O     . SER B 1 189 ? 134.298 142.112 139.278 1.00 25.83 ?  189 SER B O     1 
ATOM   7107  C  CB    . SER B 1 189 ? 131.327 142.072 137.806 1.00 20.14 ?  189 SER B CB    1 
ATOM   7108  O  OG    . SER B 1 189 ? 130.032 142.640 137.811 1.00 29.91 ?  189 SER B OG    1 
ATOM   7109  N  N     . MET B 1 190 ? 134.370 142.369 137.044 1.00 30.19 ?  190 MET B N     1 
ATOM   7110  C  CA    . MET B 1 190 ? 135.727 141.835 136.972 1.00 22.37 ?  190 MET B CA    1 
ATOM   7111  C  C     . MET B 1 190 ? 136.727 142.763 137.652 1.00 16.93 ?  190 MET B C     1 
ATOM   7112  O  O     . MET B 1 190 ? 137.654 142.297 138.320 1.00 21.26 ?  190 MET B O     1 
ATOM   7113  C  CB    . MET B 1 190 ? 136.126 141.581 135.519 1.00 21.58 ?  190 MET B CB    1 
ATOM   7114  C  CG    . MET B 1 190 ? 135.324 140.483 134.855 1.00 27.32 ?  190 MET B CG    1 
ATOM   7115  S  SD    . MET B 1 190 ? 136.163 139.725 133.454 1.00 35.79 ?  190 MET B SD    1 
ATOM   7116  C  CE    . MET B 1 190 ? 136.143 141.078 132.285 1.00 25.79 ?  190 MET B CE    1 
ATOM   7117  N  N     . GLN B 1 191 ? 136.554 144.077 137.500 1.00 21.42 ?  191 GLN B N     1 
ATOM   7118  C  CA    . GLN B 1 191 ? 137.473 145.019 138.133 1.00 23.07 ?  191 GLN B CA    1 
ATOM   7119  C  C     . GLN B 1 191 ? 137.374 144.963 139.653 1.00 25.57 ?  191 GLN B C     1 
ATOM   7120  O  O     . GLN B 1 191 ? 138.392 145.052 140.349 1.00 32.40 ?  191 GLN B O     1 
ATOM   7121  C  CB    . GLN B 1 191 ? 137.209 146.440 137.633 1.00 24.32 ?  191 GLN B CB    1 
ATOM   7122  C  CG    . GLN B 1 191 ? 137.441 146.634 136.146 1.00 23.68 ?  191 GLN B CG    1 
ATOM   7123  C  CD    . GLN B 1 191 ? 138.909 146.649 135.772 1.00 27.63 ?  191 GLN B CD    1 
ATOM   7124  O  OE1   . GLN B 1 191 ? 139.786 146.645 136.634 1.00 30.80 ?  191 GLN B OE1   1 
ATOM   7125  N  NE2   . GLN B 1 191 ? 139.183 146.661 134.475 1.00 28.81 ?  191 GLN B NE2   1 
ATOM   7126  N  N     . LEU B 1 192 ? 136.160 144.829 140.187 1.00 24.98 ?  192 LEU B N     1 
ATOM   7127  C  CA    . LEU B 1 192 ? 135.986 144.790 141.634 1.00 16.38 ?  192 LEU B CA    1 
ATOM   7128  C  C     . LEU B 1 192 ? 136.394 143.441 142.213 1.00 23.84 ?  192 LEU B C     1 
ATOM   7129  O  O     . LEU B 1 192 ? 136.957 143.383 143.310 1.00 36.16 ?  192 LEU B O     1 
ATOM   7130  C  CB    . LEU B 1 192 ? 134.538 145.116 141.998 1.00 18.21 ?  192 LEU B CB    1 
ATOM   7131  C  CG    . LEU B 1 192 ? 134.076 146.539 141.678 1.00 19.83 ?  192 LEU B CG    1 
ATOM   7132  C  CD1   . LEU B 1 192 ? 132.571 146.654 141.820 1.00 19.10 ?  192 LEU B CD1   1 
ATOM   7133  C  CD2   . LEU B 1 192 ? 134.782 147.549 142.564 1.00 17.33 ?  192 LEU B CD2   1 
ATOM   7134  N  N     . SER B 1 193 ? 136.117 142.349 141.497 1.00 27.70 ?  193 SER B N     1 
ATOM   7135  C  CA    . SER B 1 193 ? 136.600 141.043 141.925 1.00 20.19 ?  193 SER B CA    1 
ATOM   7136  C  C     . SER B 1 193 ? 138.118 140.975 141.868 1.00 28.24 ?  193 SER B C     1 
ATOM   7137  O  O     . SER B 1 193 ? 138.738 140.277 142.675 1.00 36.87 ?  193 SER B O     1 
ATOM   7138  C  CB    . SER B 1 193 ? 135.980 139.949 141.057 1.00 25.64 ?  193 SER B CB    1 
ATOM   7139  O  OG    . SER B 1 193 ? 136.288 138.663 141.562 1.00 42.27 ?  193 SER B OG    1 
ATOM   7140  N  N     . LYS B 1 194 ? 138.729 141.693 140.924 1.00 34.56 ?  194 LYS B N     1 
ATOM   7141  C  CA    . LYS B 1 194 ? 140.183 141.796 140.883 1.00 32.01 ?  194 LYS B CA    1 
ATOM   7142  C  C     . LYS B 1 194 ? 140.721 142.433 142.158 1.00 35.73 ?  194 LYS B C     1 
ATOM   7143  O  O     . LYS B 1 194 ? 141.742 141.995 142.699 1.00 43.69 ?  194 LYS B O     1 
ATOM   7144  C  CB    . LYS B 1 194 ? 140.604 142.598 139.652 1.00 27.19 ?  194 LYS B CB    1 
ATOM   7145  C  CG    . LYS B 1 194 ? 142.010 143.151 139.707 1.00 36.44 ?  194 LYS B CG    1 
ATOM   7146  C  CD    . LYS B 1 194 ? 142.236 144.182 138.616 1.00 38.23 ?  194 LYS B CD    1 
ATOM   7147  C  CE    . LYS B 1 194 ? 143.719 144.418 138.380 1.00 36.81 ?  194 LYS B CE    1 
ATOM   7148  N  NZ    . LYS B 1 194 ? 143.953 145.431 137.315 1.00 37.91 1  194 LYS B NZ    1 
ATOM   7149  N  N     . LEU B 1 195 ? 140.036 143.462 142.660 1.00 34.15 ?  195 LEU B N     1 
ATOM   7150  C  CA    . LEU B 1 195 ? 140.409 144.088 143.922 1.00 35.73 ?  195 LEU B CA    1 
ATOM   7151  C  C     . LEU B 1 195 ? 140.148 143.191 145.124 1.00 35.64 ?  195 LEU B C     1 
ATOM   7152  O  O     . LEU B 1 195 ? 140.579 143.531 146.231 1.00 42.62 ?  195 LEU B O     1 
ATOM   7153  C  CB    . LEU B 1 195 ? 139.655 145.407 144.095 1.00 38.37 ?  195 LEU B CB    1 
ATOM   7154  C  CG    . LEU B 1 195 ? 139.884 146.455 143.007 1.00 37.71 ?  195 LEU B CG    1 
ATOM   7155  C  CD1   . LEU B 1 195 ? 139.092 147.719 143.306 1.00 32.38 ?  195 LEU B CD1   1 
ATOM   7156  C  CD2   . LEU B 1 195 ? 141.364 146.759 142.859 1.00 34.65 ?  195 LEU B CD2   1 
ATOM   7157  N  N     . GLY B 1 196 ? 139.456 142.073 144.940 1.00 31.06 ?  196 GLY B N     1 
ATOM   7158  C  CA    . GLY B 1 196 ? 139.170 141.157 146.020 1.00 30.00 ?  196 GLY B CA    1 
ATOM   7159  C  C     . GLY B 1 196 ? 137.815 141.317 146.666 1.00 36.77 ?  196 GLY B C     1 
ATOM   7160  O  O     . GLY B 1 196 ? 137.569 140.696 147.705 1.00 39.00 ?  196 GLY B O     1 
ATOM   7161  N  N     . GLY B 1 197 ? 136.929 142.120 146.088 1.00 30.42 ?  197 GLY B N     1 
ATOM   7162  C  CA    . GLY B 1 197 ? 135.635 142.403 146.682 1.00 25.49 ?  197 GLY B CA    1 
ATOM   7163  C  C     . GLY B 1 197 ? 134.524 141.557 146.085 1.00 27.37 ?  197 GLY B C     1 
ATOM   7164  O  O     . GLY B 1 197 ? 134.518 141.276 144.886 1.00 31.59 ?  197 GLY B O     1 
ATOM   7165  N  N     . GLY B 1 198 ? 133.588 141.156 146.939 1.00 25.08 ?  198 GLY B N     1 
ATOM   7166  C  CA    . GLY B 1 198 ? 132.392 140.492 146.457 1.00 14.95 ?  198 GLY B CA    1 
ATOM   7167  C  C     . GLY B 1 198 ? 131.446 141.488 145.812 1.00 14.13 ?  198 GLY B C     1 
ATOM   7168  O  O     . GLY B 1 198 ? 131.242 142.595 146.307 1.00 24.21 ?  198 GLY B O     1 
ATOM   7169  N  N     . VAL B 1 199 ? 130.867 141.086 144.685 1.00 22.61 ?  199 VAL B N     1 
ATOM   7170  C  CA    . VAL B 1 199 ? 130.051 141.967 143.860 1.00 17.88 ?  199 VAL B CA    1 
ATOM   7171  C  C     . VAL B 1 199 ? 128.643 141.398 143.783 1.00 8.99  ?  199 VAL B C     1 
ATOM   7172  O  O     . VAL B 1 199 ? 128.461 140.219 143.458 1.00 18.81 ?  199 VAL B O     1 
ATOM   7173  C  CB    . VAL B 1 199 ? 130.648 142.137 142.451 1.00 12.95 ?  199 VAL B CB    1 
ATOM   7174  C  CG1   . VAL B 1 199 ? 129.891 143.202 141.681 1.00 18.72 ?  199 VAL B CG1   1 
ATOM   7175  C  CG2   . VAL B 1 199 ? 132.122 142.480 142.540 1.00 17.15 ?  199 VAL B CG2   1 
ATOM   7176  N  N     . SER B 1 200 ? 127.655 142.231 144.084 1.00 18.60 ?  200 SER B N     1 
ATOM   7177  C  CA    . SER B 1 200 ? 126.251 141.871 143.968 1.00 7.07  ?  200 SER B CA    1 
ATOM   7178  C  C     . SER B 1 200 ? 125.633 142.663 142.828 1.00 13.22 ?  200 SER B C     1 
ATOM   7179  O  O     . SER B 1 200 ? 125.839 143.877 142.728 1.00 22.94 ?  200 SER B O     1 
ATOM   7180  C  CB    . SER B 1 200 ? 125.504 142.141 145.273 1.00 13.11 ?  200 SER B CB    1 
ATOM   7181  O  OG    . SER B 1 200 ? 124.317 141.373 145.343 1.00 22.00 ?  200 SER B OG    1 
ATOM   7182  N  N     . LEU B 1 201 ? 124.884 141.979 141.970 1.00 20.67 ?  201 LEU B N     1 
ATOM   7183  C  CA    . LEU B 1 201 ? 124.297 142.587 140.786 1.00 7.80  ?  201 LEU B CA    1 
ATOM   7184  C  C     . LEU B 1 201 ? 122.784 142.445 140.834 1.00 10.12 ?  201 LEU B C     1 
ATOM   7185  O  O     . LEU B 1 201 ? 122.266 141.361 141.124 1.00 14.11 ?  201 LEU B O     1 
ATOM   7186  C  CB    . LEU B 1 201 ? 124.856 141.946 139.514 1.00 20.30 ?  201 LEU B CB    1 
ATOM   7187  C  CG    . LEU B 1 201 ? 126.369 142.084 139.353 1.00 18.96 ?  201 LEU B CG    1 
ATOM   7188  C  CD1   . LEU B 1 201 ? 127.060 140.751 139.584 1.00 22.23 ?  201 LEU B CD1   1 
ATOM   7189  C  CD2   . LEU B 1 201 ? 126.712 142.641 137.985 1.00 16.03 ?  201 LEU B CD2   1 
ATOM   7190  N  N     . ASN B 1 202 ? 122.085 143.541 140.560 1.00 15.66 ?  202 ASN B N     1 
ATOM   7191  C  CA    . ASN B 1 202 ? 120.631 143.539 140.460 1.00 7.09  ?  202 ASN B CA    1 
ATOM   7192  C  C     . ASN B 1 202 ? 120.254 143.257 139.011 1.00 22.09 ?  202 ASN B C     1 
ATOM   7193  O  O     . ASN B 1 202 ? 120.541 144.062 138.119 1.00 34.99 ?  202 ASN B O     1 
ATOM   7194  C  CB    . ASN B 1 202 ? 120.056 144.871 140.929 1.00 9.23  ?  202 ASN B CB    1 
ATOM   7195  C  CG    . ASN B 1 202 ? 118.580 144.788 141.249 1.00 13.69 ?  202 ASN B CG    1 
ATOM   7196  O  OD1   . ASN B 1 202 ? 118.053 143.714 141.533 1.00 23.02 ?  202 ASN B OD1   1 
ATOM   7197  N  ND2   . ASN B 1 202 ? 117.904 145.928 141.208 1.00 13.77 ?  202 ASN B ND2   1 
ATOM   7198  N  N     . LEU B 1 203 ? 119.613 142.116 138.775 1.00 13.13 ?  203 LEU B N     1 
ATOM   7199  C  CA    . LEU B 1 203 ? 119.224 141.702 137.436 1.00 10.38 ?  203 LEU B CA    1 
ATOM   7200  C  C     . LEU B 1 203 ? 117.744 141.925 137.158 1.00 11.78 ?  203 LEU B C     1 
ATOM   7201  O  O     . LEU B 1 203 ? 117.236 141.443 136.142 1.00 20.55 ?  203 LEU B O     1 
ATOM   7202  C  CB    . LEU B 1 203 ? 119.581 140.229 137.220 1.00 19.25 ?  203 LEU B CB    1 
ATOM   7203  C  CG    . LEU B 1 203 ? 121.052 139.842 137.382 1.00 19.16 ?  203 LEU B CG    1 
ATOM   7204  C  CD1   . LEU B 1 203 ? 121.317 138.490 136.746 1.00 15.97 ?  203 LEU B CD1   1 
ATOM   7205  C  CD2   . LEU B 1 203 ? 121.968 140.900 136.788 1.00 18.43 ?  203 LEU B CD2   1 
ATOM   7206  N  N     . SER B 1 204 ? 117.043 142.649 138.034 1.00 16.09 ?  204 SER B N     1 
ATOM   7207  C  CA    . SER B 1 204 ? 115.598 142.790 137.890 1.00 17.71 ?  204 SER B CA    1 
ATOM   7208  C  C     . SER B 1 204 ? 115.224 143.712 136.738 1.00 20.50 ?  204 SER B C     1 
ATOM   7209  O  O     . SER B 1 204 ? 114.139 143.572 136.165 1.00 27.93 ?  204 SER B O     1 
ATOM   7210  C  CB    . SER B 1 204 ? 114.992 143.302 139.195 1.00 12.46 ?  204 SER B CB    1 
ATOM   7211  O  OG    . SER B 1 204 ? 115.205 142.376 140.242 1.00 24.39 ?  204 SER B OG    1 
ATOM   7212  N  N     . LYS B 1 205 ? 116.092 144.661 136.390 1.00 17.96 ?  205 LYS B N     1 
ATOM   7213  C  CA    . LYS B 1 205 ? 115.807 145.557 135.278 1.00 16.97 ?  205 LYS B CA    1 
ATOM   7214  C  C     . LYS B 1 205 ? 115.987 144.889 133.924 1.00 21.08 ?  205 LYS B C     1 
ATOM   7215  O  O     . LYS B 1 205 ? 115.370 145.328 132.949 1.00 30.01 ?  205 LYS B O     1 
ATOM   7216  C  CB    . LYS B 1 205 ? 116.689 146.801 135.359 1.00 17.17 ?  205 LYS B CB    1 
ATOM   7217  C  CG    . LYS B 1 205 ? 116.341 147.714 136.509 1.00 13.29 ?  205 LYS B CG    1 
ATOM   7218  C  CD    . LYS B 1 205 ? 117.190 148.964 136.488 1.00 19.85 ?  205 LYS B CD    1 
ATOM   7219  C  CE    . LYS B 1 205 ? 116.684 149.981 137.487 1.00 24.37 ?  205 LYS B CE    1 
ATOM   7220  N  NZ    . LYS B 1 205 ? 116.843 149.517 138.889 1.00 17.22 1  205 LYS B NZ    1 
ATOM   7221  N  N     . LEU B 1 206 ? 116.814 143.851 133.843 1.00 17.26 ?  206 LEU B N     1 
ATOM   7222  C  CA    . LEU B 1 206 ? 116.998 143.136 132.590 1.00 11.29 ?  206 LEU B CA    1 
ATOM   7223  C  C     . LEU B 1 206 ? 115.694 142.481 132.157 1.00 19.76 ?  206 LEU B C     1 
ATOM   7224  O  O     . LEU B 1 206 ? 115.014 141.836 132.958 1.00 25.80 ?  206 LEU B O     1 
ATOM   7225  C  CB    . LEU B 1 206 ? 118.090 142.080 132.741 1.00 19.80 ?  206 LEU B CB    1 
ATOM   7226  C  CG    . LEU B 1 206 ? 119.432 142.576 133.273 1.00 22.20 ?  206 LEU B CG    1 
ATOM   7227  C  CD1   . LEU B 1 206 ? 120.375 141.409 133.474 1.00 17.52 ?  206 LEU B CD1   1 
ATOM   7228  C  CD2   . LEU B 1 206 ? 120.029 143.598 132.328 1.00 26.19 ?  206 LEU B CD2   1 
ATOM   7229  N  N     . ARG B 1 207 ? 115.350 142.646 130.884 1.00 26.99 ?  207 ARG B N     1 
ATOM   7230  C  CA    . ARG B 1 207 ? 114.117 142.070 130.376 1.00 22.95 ?  207 ARG B CA    1 
ATOM   7231  C  C     . ARG B 1 207 ? 114.227 140.551 130.296 1.00 26.41 ?  207 ARG B C     1 
ATOM   7232  O  O     . ARG B 1 207 ? 115.312 139.988 130.125 1.00 30.49 ?  207 ARG B O     1 
ATOM   7233  C  CB    . ARG B 1 207 ? 113.766 142.659 129.009 1.00 23.26 ?  207 ARG B CB    1 
ATOM   7234  C  CG    . ARG B 1 207 ? 114.763 142.385 127.905 1.00 24.90 ?  207 ARG B CG    1 
ATOM   7235  C  CD    . ARG B 1 207 ? 114.428 143.216 126.678 1.00 22.50 ?  207 ARG B CD    1 
ATOM   7236  N  NE    . ARG B 1 207 ? 114.810 144.611 126.851 1.00 27.64 ?  207 ARG B NE    1 
ATOM   7237  C  CZ    . ARG B 1 207 ? 115.011 145.465 125.857 1.00 21.97 ?  207 ARG B CZ    1 
ATOM   7238  N  NH1   . ARG B 1 207 ? 114.840 145.110 124.595 1.00 28.60 1  207 ARG B NH1   1 
ATOM   7239  N  NH2   . ARG B 1 207 ? 115.397 146.706 126.137 1.00 18.36 ?  207 ARG B NH2   1 
ATOM   7240  N  N     . ALA B 1 208 ? 113.082 139.891 130.430 1.00 30.71 ?  208 ALA B N     1 
ATOM   7241  C  CA    . ALA B 1 208 ? 113.042 138.447 130.566 1.00 29.17 ?  208 ALA B CA    1 
ATOM   7242  C  C     . ALA B 1 208 ? 113.370 137.756 129.244 1.00 33.52 ?  208 ALA B C     1 
ATOM   7243  O  O     . ALA B 1 208 ? 113.563 138.387 128.202 1.00 35.30 ?  208 ALA B O     1 
ATOM   7244  C  CB    . ALA B 1 208 ? 111.670 138.000 131.062 1.00 26.41 ?  208 ALA B CB    1 
ATOM   7245  N  N     . LYS B 1 209 ? 113.438 136.430 129.309 1.00 26.37 ?  209 LYS B N     1 
ATOM   7246  C  CA    . LYS B 1 209 ? 113.669 135.623 128.123 1.00 22.11 ?  209 LYS B CA    1 
ATOM   7247  C  C     . LYS B 1 209 ? 112.461 135.686 127.196 1.00 33.53 ?  209 LYS B C     1 
ATOM   7248  O  O     . LYS B 1 209 ? 111.312 135.661 127.643 1.00 35.56 ?  209 LYS B O     1 
ATOM   7249  C  CB    . LYS B 1 209 ? 113.956 134.175 128.517 1.00 27.44 ?  209 LYS B CB    1 
ATOM   7250  C  CG    . LYS B 1 209 ? 114.752 133.389 127.490 1.00 33.01 ?  209 LYS B CG    1 
ATOM   7251  C  CD    . LYS B 1 209 ? 114.194 131.986 127.312 1.00 31.98 ?  209 LYS B CD    1 
ATOM   7252  C  CE    . LYS B 1 209 ? 113.659 131.427 128.619 1.00 36.48 ?  209 LYS B CE    1 
ATOM   7253  N  NZ    . LYS B 1 209 ? 112.954 130.131 128.425 1.00 35.63 1  209 LYS B NZ    1 
ATOM   7254  N  N     . GLY B 1 210 ? 112.729 135.759 125.895 1.00 36.34 ?  210 GLY B N     1 
ATOM   7255  C  CA    . GLY B 1 210 ? 111.659 135.877 124.928 1.00 32.08 ?  210 GLY B CA    1 
ATOM   7256  C  C     . GLY B 1 210 ? 111.057 137.258 124.818 1.00 36.40 ?  210 GLY B C     1 
ATOM   7257  O  O     . GLY B 1 210 ? 109.858 137.382 124.549 1.00 38.93 ?  210 GLY B O     1 
ATOM   7258  N  N     . GLU B 1 211 ? 111.847 138.302 125.031 1.00 39.33 ?  211 GLU B N     1 
ATOM   7259  C  CA    . GLU B 1 211 ? 111.405 139.675 124.857 1.00 33.16 ?  211 GLU B CA    1 
ATOM   7260  C  C     . GLU B 1 211 ? 112.001 140.256 123.582 1.00 36.67 ?  211 GLU B C     1 
ATOM   7261  O  O     . GLU B 1 211 ? 112.968 139.736 123.020 1.00 39.90 ?  211 GLU B O     1 
ATOM   7262  C  CB    . GLU B 1 211 ? 111.785 140.531 126.070 1.00 34.62 ?  211 GLU B CB    1 
ATOM   7263  C  CG    . GLU B 1 211 ? 110.949 140.247 127.301 1.00 35.76 ?  211 GLU B CG    1 
ATOM   7264  C  CD    . GLU B 1 211 ? 110.384 141.505 127.925 1.00 41.33 ?  211 GLU B CD    1 
ATOM   7265  O  OE1   . GLU B 1 211 ? 109.600 142.202 127.248 1.00 43.31 ?  211 GLU B OE1   1 
ATOM   7266  O  OE2   . GLU B 1 211 ? 110.710 141.792 129.094 1.00 41.92 -1 211 GLU B OE2   1 
ATOM   7267  N  N     . ALA B 1 212 ? 111.404 141.351 123.125 1.00 37.07 ?  212 ALA B N     1 
ATOM   7268  C  CA    . ALA B 1 212 ? 111.787 141.971 121.867 1.00 33.37 ?  212 ALA B CA    1 
ATOM   7269  C  C     . ALA B 1 212 ? 113.008 142.863 122.047 1.00 38.75 ?  212 ALA B C     1 
ATOM   7270  O  O     . ALA B 1 212 ? 113.143 143.557 123.058 1.00 40.21 ?  212 ALA B O     1 
ATOM   7271  C  CB    . ALA B 1 212 ? 110.628 142.787 121.295 1.00 37.58 ?  212 ALA B CB    1 
ATOM   7272  N  N     . ILE B 1 213 ? 113.896 142.836 121.058 1.00 35.60 ?  213 ILE B N     1 
ATOM   7273  C  CA    . ILE B 1 213 ? 115.042 143.735 120.990 1.00 35.47 ?  213 ILE B CA    1 
ATOM   7274  C  C     . ILE B 1 213 ? 114.853 144.587 119.742 1.00 35.53 ?  213 ILE B C     1 
ATOM   7275  O  O     . ILE B 1 213 ? 115.117 144.127 118.625 1.00 42.01 ?  213 ILE B O     1 
ATOM   7276  C  CB    . ILE B 1 213 ? 116.377 142.983 120.957 1.00 37.16 ?  213 ILE B CB    1 
ATOM   7277  C  CG1   . ILE B 1 213 ? 116.483 142.018 122.137 1.00 36.22 ?  213 ILE B CG1   1 
ATOM   7278  C  CG2   . ILE B 1 213 ? 117.540 143.962 120.970 1.00 33.09 ?  213 ILE B CG2   1 
ATOM   7279  C  CD1   . ILE B 1 213 ? 117.655 141.071 122.045 1.00 31.45 ?  213 ILE B CD1   1 
ATOM   7280  N  N     . LYS B 1 214 ? 114.389 145.826 119.933 1.00 40.21 ?  214 LYS B N     1 
ATOM   7281  C  CA    . LYS B 1 214 ? 114.142 146.807 118.875 1.00 39.89 ?  214 LYS B CA    1 
ATOM   7282  C  C     . LYS B 1 214 ? 113.449 146.192 117.661 1.00 45.59 ?  214 LYS B C     1 
ATOM   7283  O  O     . LYS B 1 214 ? 114.038 146.101 116.579 1.00 45.66 ?  214 LYS B O     1 
ATOM   7284  C  CB    . LYS B 1 214 ? 115.432 147.544 118.463 1.00 39.26 ?  214 LYS B CB    1 
ATOM   7285  C  CG    . LYS B 1 214 ? 116.661 146.710 118.132 1.00 41.69 ?  214 LYS B CG    1 
ATOM   7286  C  CD    . LYS B 1 214 ? 117.692 147.544 117.395 1.00 40.17 ?  214 LYS B CD    1 
ATOM   7287  C  CE    . LYS B 1 214 ? 119.030 146.835 117.323 1.00 42.26 ?  214 LYS B CE    1 
ATOM   7288  N  NZ    . LYS B 1 214 ? 120.162 147.801 117.356 1.00 44.06 1  214 LYS B NZ    1 
ATOM   7289  N  N     . ASP B 1 215 ? 112.205 145.752 117.852 1.00 52.33 ?  215 ASP B N     1 
ATOM   7290  C  CA    . ASP B 1 215 ? 111.267 145.219 116.869 1.00 53.60 ?  215 ASP B CA    1 
ATOM   7291  C  C     . ASP B 1 215 ? 111.543 143.760 116.514 1.00 54.25 ?  215 ASP B C     1 
ATOM   7292  O  O     . ASP B 1 215 ? 110.806 143.195 115.706 1.00 56.29 ?  215 ASP B O     1 
ATOM   7293  C  CB    . ASP B 1 215 ? 111.217 146.040 115.564 1.00 52.06 ?  215 ASP B CB    1 
ATOM   7294  C  CG    . ASP B 1 215 ? 110.547 147.385 115.750 1.00 59.18 ?  215 ASP B CG    1 
ATOM   7295  O  OD1   . ASP B 1 215 ? 109.317 147.414 115.965 1.00 56.38 ?  215 ASP B OD1   1 
ATOM   7296  O  OD2   . ASP B 1 215 ? 111.251 148.415 115.678 1.00 56.99 -1 215 ASP B OD2   1 
ATOM   7297  N  N     . VAL B 1 216 ? 112.566 143.129 117.078 1.00 48.01 ?  216 VAL B N     1 
ATOM   7298  C  CA    . VAL B 1 216 ? 112.786 141.702 116.868 1.00 43.71 ?  216 VAL B CA    1 
ATOM   7299  C  C     . VAL B 1 216 ? 112.298 140.959 118.105 1.00 48.49 ?  216 VAL B C     1 
ATOM   7300  O  O     . VAL B 1 216 ? 113.005 140.879 119.114 1.00 51.75 ?  216 VAL B O     1 
ATOM   7301  C  CB    . VAL B 1 216 ? 114.265 141.404 116.584 1.00 45.75 ?  216 VAL B CB    1 
ATOM   7302  C  CG1   . VAL B 1 216 ? 114.488 139.907 116.436 1.00 45.61 ?  216 VAL B CG1   1 
ATOM   7303  C  CG2   . VAL B 1 216 ? 114.720 142.142 115.338 1.00 43.69 ?  216 VAL B CG2   1 
ATOM   7304  N  N     . GLU B 1 217 ? 111.089 140.412 118.026 1.00 49.70 ?  217 GLU B N     1 
ATOM   7305  C  CA    . GLU B 1 217 ? 110.442 139.780 119.165 1.00 50.06 ?  217 GLU B CA    1 
ATOM   7306  C  C     . GLU B 1 217 ? 111.118 138.462 119.517 1.00 45.18 ?  217 GLU B C     1 
ATOM   7307  O  O     . GLU B 1 217 ? 111.753 137.821 118.680 1.00 45.39 ?  217 GLU B O     1 
ATOM   7308  C  CB    . GLU B 1 217 ? 108.961 139.538 118.873 1.00 46.34 ?  217 GLU B CB    1 
ATOM   7309  C  CG    . GLU B 1 217 ? 108.350 140.532 117.906 1.00 49.31 ?  217 GLU B CG    1 
ATOM   7310  C  CD    . GLU B 1 217 ? 108.010 141.849 118.572 1.00 52.31 ?  217 GLU B CD    1 
ATOM   7311  O  OE1   . GLU B 1 217 ? 107.417 141.824 119.670 1.00 50.98 ?  217 GLU B OE1   1 
ATOM   7312  O  OE2   . GLU B 1 217 ? 108.335 142.908 117.996 1.00 54.93 -1 217 GLU B OE2   1 
ATOM   7313  N  N     . ASN B 1 218 ? 110.973 138.068 120.784 1.00 42.09 ?  218 ASN B N     1 
ATOM   7314  C  CA    . ASN B 1 218 ? 111.454 136.777 121.279 1.00 43.42 ?  218 ASN B CA    1 
ATOM   7315  C  C     . ASN B 1 218 ? 112.947 136.591 121.017 1.00 46.69 ?  218 ASN B C     1 
ATOM   7316  O  O     . ASN B 1 218 ? 113.398 135.522 120.602 1.00 48.20 ?  218 ASN B O     1 
ATOM   7317  C  CB    . ASN B 1 218 ? 110.645 135.630 120.671 1.00 42.39 ?  218 ASN B CB    1 
ATOM   7318  C  CG    . ASN B 1 218 ? 110.597 134.413 121.566 1.00 46.35 ?  218 ASN B CG    1 
ATOM   7319  O  OD1   . ASN B 1 218 ? 109.727 134.297 122.428 1.00 49.47 ?  218 ASN B OD1   1 
ATOM   7320  N  ND2   . ASN B 1 218 ? 111.534 133.495 121.367 1.00 47.74 ?  218 ASN B ND2   1 
ATOM   7321  N  N     . ALA B 1 219 ? 113.728 137.643 121.268 1.00 35.88 ?  219 ALA B N     1 
ATOM   7322  C  CA    . ALA B 1 219 ? 115.152 137.633 120.965 1.00 33.97 ?  219 ALA B CA    1 
ATOM   7323  C  C     . ALA B 1 219 ? 116.055 137.680 122.189 1.00 37.71 ?  219 ALA B C     1 
ATOM   7324  O  O     . ALA B 1 219 ? 117.262 137.462 122.049 1.00 37.78 ?  219 ALA B O     1 
ATOM   7325  C  CB    . ALA B 1 219 ? 115.509 138.812 120.048 1.00 34.85 ?  219 ALA B CB    1 
ATOM   7326  N  N     . THR B 1 220 ? 115.513 137.956 123.369 1.00 34.96 ?  220 THR B N     1 
ATOM   7327  C  CA    . THR B 1 220 ? 116.319 138.126 124.570 1.00 33.11 ?  220 THR B CA    1 
ATOM   7328  C  C     . THR B 1 220 ? 116.498 136.788 125.276 1.00 35.08 ?  220 THR B C     1 
ATOM   7329  O  O     . THR B 1 220 ? 115.535 136.036 125.449 1.00 33.67 ?  220 THR B O     1 
ATOM   7330  C  CB    . THR B 1 220 ? 115.668 139.141 125.510 1.00 28.35 ?  220 THR B CB    1 
ATOM   7331  O  OG1   . THR B 1 220 ? 115.498 140.387 124.825 1.00 34.03 ?  220 THR B OG1   1 
ATOM   7332  C  CG2   . THR B 1 220 ? 116.531 139.367 126.738 1.00 33.35 ?  220 THR B CG2   1 
ATOM   7333  N  N     . LYS B 1 221 ? 117.738 136.493 125.675 1.00 35.88 ?  221 LYS B N     1 
ATOM   7334  C  CA    . LYS B 1 221 ? 118.027 135.289 126.443 1.00 32.46 ?  221 LYS B CA    1 
ATOM   7335  C  C     . LYS B 1 221 ? 117.610 135.405 127.901 1.00 36.33 ?  221 LYS B C     1 
ATOM   7336  O  O     . LYS B 1 221 ? 117.648 134.401 128.620 1.00 40.45 ?  221 LYS B O     1 
ATOM   7337  C  CB    . LYS B 1 221 ? 119.518 134.956 126.376 1.00 33.12 ?  221 LYS B CB    1 
ATOM   7338  C  CG    . LYS B 1 221 ? 120.227 135.497 125.155 1.00 31.06 ?  221 LYS B CG    1 
ATOM   7339  C  CD    . LYS B 1 221 ? 121.563 134.807 124.964 1.00 36.10 ?  221 LYS B CD    1 
ATOM   7340  C  CE    . LYS B 1 221 ? 121.387 133.377 124.493 1.00 37.98 ?  221 LYS B CE    1 
ATOM   7341  N  NZ    . LYS B 1 221 ? 120.640 133.314 123.211 1.00 37.38 1  221 LYS B NZ    1 
ATOM   7342  N  N     . GLY B 1 222 ? 117.228 136.590 128.352 1.00 34.14 ?  222 GLY B N     1 
ATOM   7343  C  CA    . GLY B 1 222 ? 116.785 136.773 129.714 1.00 32.70 ?  222 GLY B CA    1 
ATOM   7344  C  C     . GLY B 1 222 ? 117.932 137.028 130.670 1.00 31.75 ?  222 GLY B C     1 
ATOM   7345  O  O     . GLY B 1 222 ? 119.059 137.347 130.285 1.00 34.90 ?  222 GLY B O     1 
ATOM   7346  N  N     . VAL B 1 223 ? 117.621 136.884 131.961 1.00 26.93 ?  223 VAL B N     1 
ATOM   7347  C  CA    . VAL B 1 223 ? 118.625 137.105 132.997 1.00 30.96 ?  223 VAL B CA    1 
ATOM   7348  C  C     . VAL B 1 223 ? 119.610 135.957 133.115 1.00 22.59 ?  223 VAL B C     1 
ATOM   7349  O  O     . VAL B 1 223 ? 120.667 136.130 133.727 1.00 25.89 ?  223 VAL B O     1 
ATOM   7350  C  CB    . VAL B 1 223 ? 117.972 137.352 134.370 1.00 27.74 ?  223 VAL B CB    1 
ATOM   7351  C  CG1   . VAL B 1 223 ? 116.880 138.398 134.255 1.00 21.69 ?  223 VAL B CG1   1 
ATOM   7352  C  CG2   . VAL B 1 223 ? 117.423 136.057 134.948 1.00 26.44 ?  223 VAL B CG2   1 
ATOM   7353  N  N     . VAL B 1 224 ? 119.309 134.794 132.534 1.00 26.79 ?  224 VAL B N     1 
ATOM   7354  C  CA    . VAL B 1 224 ? 120.199 133.647 132.685 1.00 26.01 ?  224 VAL B CA    1 
ATOM   7355  C  C     . VAL B 1 224 ? 121.419 133.762 131.774 1.00 31.64 ?  224 VAL B C     1 
ATOM   7356  O  O     . VAL B 1 224 ? 122.510 133.309 132.136 1.00 37.19 ?  224 VAL B O     1 
ATOM   7357  C  CB    . VAL B 1 224 ? 119.427 132.342 132.440 1.00 32.12 ?  224 VAL B CB    1 
ATOM   7358  C  CG1   . VAL B 1 224 ? 120.312 131.141 132.721 1.00 28.23 ?  224 VAL B CG1   1 
ATOM   7359  C  CG2   . VAL B 1 224 ? 118.188 132.301 133.312 1.00 32.42 ?  224 VAL B CG2   1 
ATOM   7360  N  N     . GLY B 1 225 ? 121.275 134.361 130.591 1.00 20.31 ?  225 GLY B N     1 
ATOM   7361  C  CA    . GLY B 1 225 ? 122.447 134.627 129.772 1.00 17.94 ?  225 GLY B CA    1 
ATOM   7362  C  C     . GLY B 1 225 ? 123.406 135.593 130.441 1.00 20.10 ?  225 GLY B C     1 
ATOM   7363  O  O     . GLY B 1 225 ? 124.623 135.382 130.444 1.00 30.82 ?  225 GLY B O     1 
ATOM   7364  N  N     . VAL B 1 226 ? 122.866 136.660 131.033 1.00 18.63 ?  226 VAL B N     1 
ATOM   7365  C  CA    . VAL B 1 226 ? 123.685 137.580 131.812 1.00 21.71 ?  226 VAL B CA    1 
ATOM   7366  C  C     . VAL B 1 226 ? 124.271 136.873 133.024 1.00 18.90 ?  226 VAL B C     1 
ATOM   7367  O  O     . VAL B 1 226 ? 125.395 137.165 133.439 1.00 23.94 ?  226 VAL B O     1 
ATOM   7368  C  CB    . VAL B 1 226 ? 122.858 138.816 132.219 1.00 21.28 ?  226 VAL B CB    1 
ATOM   7369  C  CG1   . VAL B 1 226 ? 123.727 139.823 132.952 1.00 29.21 ?  226 VAL B CG1   1 
ATOM   7370  C  CG2   . VAL B 1 226 ? 122.224 139.446 130.995 1.00 23.54 ?  226 VAL B CG2   1 
ATOM   7371  N  N     . MET B 1 227 ? 123.523 135.938 133.610 1.00 22.86 ?  227 MET B N     1 
ATOM   7372  C  CA    . MET B 1 227 ? 124.037 135.160 134.733 1.00 23.74 ?  227 MET B CA    1 
ATOM   7373  C  C     . MET B 1 227 ? 125.247 134.333 134.327 1.00 25.47 ?  227 MET B C     1 
ATOM   7374  O  O     . MET B 1 227 ? 126.234 134.265 135.064 1.00 28.53 ?  227 MET B O     1 
ATOM   7375  C  CB    . MET B 1 227 ? 122.934 134.257 135.279 1.00 17.04 ?  227 MET B CB    1 
ATOM   7376  C  CG    . MET B 1 227 ? 122.020 134.918 136.285 1.00 18.35 ?  227 MET B CG    1 
ATOM   7377  S  SD    . MET B 1 227 ? 120.958 133.707 137.077 1.00 33.72 ?  227 MET B SD    1 
ATOM   7378  C  CE    . MET B 1 227 ? 122.030 133.166 138.393 1.00 30.40 ?  227 MET B CE    1 
ATOM   7379  N  N     . LYS B 1 228 ? 125.185 133.688 133.161 1.00 23.81 ?  228 LYS B N     1 
ATOM   7380  C  CA    . LYS B 1 228 ? 126.330 132.930 132.662 1.00 19.93 ?  228 LYS B CA    1 
ATOM   7381  C  C     . LYS B 1 228 ? 127.513 133.845 132.377 1.00 20.40 ?  228 LYS B C     1 
ATOM   7382  O  O     . LYS B 1 228 ? 128.664 133.509 132.697 1.00 26.34 ?  228 LYS B O     1 
ATOM   7383  C  CB    . LYS B 1 228 ? 125.944 132.160 131.402 1.00 22.60 ?  228 LYS B CB    1 
ATOM   7384  C  CG    . LYS B 1 228 ? 124.817 131.172 131.591 1.00 24.65 ?  228 LYS B CG    1 
ATOM   7385  C  CD    . LYS B 1 228 ? 124.790 130.169 130.455 1.00 33.66 ?  228 LYS B CD    1 
ATOM   7386  C  CE    . LYS B 1 228 ? 123.844 130.606 129.349 1.00 38.31 ?  228 LYS B CE    1 
ATOM   7387  N  NZ    . LYS B 1 228 ? 122.424 130.311 129.685 1.00 36.29 1  228 LYS B NZ    1 
ATOM   7388  N  N     . LEU B 1 229 ? 127.250 135.002 131.766 1.00 22.70 ?  229 LEU B N     1 
ATOM   7389  C  CA    . LEU B 1 229 ? 128.317 135.963 131.508 1.00 20.74 ?  229 LEU B CA    1 
ATOM   7390  C  C     . LEU B 1 229 ? 128.990 136.392 132.804 1.00 24.12 ?  229 LEU B C     1 
ATOM   7391  O  O     . LEU B 1 229 ? 130.221 136.442 132.893 1.00 29.02 ?  229 LEU B O     1 
ATOM   7392  C  CB    . LEU B 1 229 ? 127.764 137.184 130.776 1.00 23.24 ?  229 LEU B CB    1 
ATOM   7393  C  CG    . LEU B 1 229 ? 127.503 137.100 129.276 1.00 19.83 ?  229 LEU B CG    1 
ATOM   7394  C  CD1   . LEU B 1 229 ? 126.617 138.254 128.859 1.00 24.18 ?  229 LEU B CD1   1 
ATOM   7395  C  CD2   . LEU B 1 229 ? 128.808 137.119 128.506 1.00 19.50 ?  229 LEU B CD2   1 
ATOM   7396  N  N     . LEU B 1 230 ? 128.191 136.695 133.828 1.00 27.00 ?  230 LEU B N     1 
ATOM   7397  C  CA    . LEU B 1 230 ? 128.737 137.138 135.106 1.00 18.28 ?  230 LEU B CA    1 
ATOM   7398  C  C     . LEU B 1 230 ? 129.471 136.011 135.816 1.00 13.47 ?  230 LEU B C     1 
ATOM   7399  O  O     . LEU B 1 230 ? 130.491 136.246 136.467 1.00 32.34 ?  230 LEU B O     1 
ATOM   7400  C  CB    . LEU B 1 230 ? 127.620 137.691 135.988 1.00 19.19 ?  230 LEU B CB    1 
ATOM   7401  C  CG    . LEU B 1 230 ? 126.984 138.999 135.524 1.00 23.66 ?  230 LEU B CG    1 
ATOM   7402  C  CD1   . LEU B 1 230 ? 125.764 139.322 136.367 1.00 28.79 ?  230 LEU B CD1   1 
ATOM   7403  C  CD2   . LEU B 1 230 ? 127.993 140.135 135.570 1.00 24.41 ?  230 LEU B CD2   1 
ATOM   7404  N  N     . ASP B 1 231 ? 128.963 134.782 135.715 1.00 22.77 ?  231 ASP B N     1 
ATOM   7405  C  CA    . ASP B 1 231 ? 129.643 133.651 136.334 1.00 25.27 ?  231 ASP B CA    1 
ATOM   7406  C  C     . ASP B 1 231 ? 131.017 133.437 135.718 1.00 29.78 ?  231 ASP B C     1 
ATOM   7407  O  O     . ASP B 1 231 ? 132.004 133.233 136.436 1.00 33.95 ?  231 ASP B O     1 
ATOM   7408  C  CB    . ASP B 1 231 ? 128.790 132.391 136.199 1.00 24.32 ?  231 ASP B CB    1 
ATOM   7409  C  CG    . ASP B 1 231 ? 129.341 131.226 136.992 1.00 40.21 ?  231 ASP B CG    1 
ATOM   7410  O  OD1   . ASP B 1 231 ? 129.185 131.223 138.230 1.00 44.23 ?  231 ASP B OD1   1 
ATOM   7411  O  OD2   . ASP B 1 231 ? 129.931 130.311 136.380 1.00 39.45 -1 231 ASP B OD2   1 
ATOM   7412  N  N     . ASN B 1 232 ? 131.110 133.507 134.389 1.00 30.21 ?  232 ASN B N     1 
ATOM   7413  C  CA    . ASN B 1 232 ? 132.415 133.381 133.747 1.00 28.77 ?  232 ASN B CA    1 
ATOM   7414  C  C     . ASN B 1 232 ? 133.307 134.582 134.043 1.00 23.15 ?  232 ASN B C     1 
ATOM   7415  O  O     . ASN B 1 232 ? 134.528 134.435 134.168 1.00 31.63 ?  232 ASN B O     1 
ATOM   7416  C  CB    . ASN B 1 232 ? 132.240 133.177 132.246 1.00 26.34 ?  232 ASN B CB    1 
ATOM   7417  C  CG    . ASN B 1 232 ? 132.187 131.715 131.874 1.00 31.22 ?  232 ASN B CG    1 
ATOM   7418  O  OD1   . ASN B 1 232 ? 132.986 130.914 132.356 1.00 36.86 ?  232 ASN B OD1   1 
ATOM   7419  N  ND2   . ASN B 1 232 ? 131.217 131.348 131.061 1.00 35.04 ?  232 ASN B ND2   1 
ATOM   7420  N  N     . ALA B 1 233 ? 132.721 135.774 134.161 1.00 18.47 ?  233 ALA B N     1 
ATOM   7421  C  CA    . ALA B 1 233 ? 133.507 136.950 134.513 1.00 15.26 ?  233 ALA B CA    1 
ATOM   7422  C  C     . ALA B 1 233 ? 134.108 136.817 135.907 1.00 26.94 ?  233 ALA B C     1 
ATOM   7423  O  O     . ALA B 1 233 ? 135.262 137.196 136.133 1.00 30.67 ?  233 ALA B O     1 
ATOM   7424  C  CB    . ALA B 1 233 ? 132.637 138.202 134.415 1.00 20.26 ?  233 ALA B CB    1 
ATOM   7425  N  N     . PHE B 1 234 ? 133.332 136.290 136.857 1.00 30.52 ?  234 PHE B N     1 
ATOM   7426  C  CA    . PHE B 1 234 ? 133.839 136.092 138.210 1.00 24.01 ?  234 PHE B CA    1 
ATOM   7427  C  C     . PHE B 1 234 ? 134.835 134.943 138.272 1.00 24.34 ?  234 PHE B C     1 
ATOM   7428  O  O     . PHE B 1 234 ? 135.779 134.988 139.069 1.00 29.06 ?  234 PHE B O     1 
ATOM   7429  C  CB    . PHE B 1 234 ? 132.682 135.845 139.176 1.00 21.79 ?  234 PHE B CB    1 
ATOM   7430  C  CG    . PHE B 1 234 ? 131.949 137.093 139.567 1.00 21.25 ?  234 PHE B CG    1 
ATOM   7431  C  CD1   . PHE B 1 234 ? 132.617 138.146 140.162 1.00 24.86 ?  234 PHE B CD1   1 
ATOM   7432  C  CD2   . PHE B 1 234 ? 130.591 137.212 139.340 1.00 23.68 ?  234 PHE B CD2   1 
ATOM   7433  C  CE1   . PHE B 1 234 ? 131.943 139.295 140.518 1.00 24.28 ?  234 PHE B CE1   1 
ATOM   7434  C  CE2   . PHE B 1 234 ? 129.915 138.359 139.691 1.00 23.92 ?  234 PHE B CE2   1 
ATOM   7435  C  CZ    . PHE B 1 234 ? 130.591 139.398 140.283 1.00 24.77 ?  234 PHE B CZ    1 
ATOM   7436  N  N     . ARG B 1 235 ? 134.638 133.906 137.455 1.00 31.14 ?  235 ARG B N     1 
ATOM   7437  C  CA    . ARG B 1 235 ? 135.618 132.827 137.385 1.00 25.16 ?  235 ARG B CA    1 
ATOM   7438  C  C     . ARG B 1 235 ? 136.944 133.321 136.821 1.00 31.81 ?  235 ARG B C     1 
ATOM   7439  O  O     . ARG B 1 235 ? 138.012 132.897 137.274 1.00 40.91 ?  235 ARG B O     1 
ATOM   7440  C  CB    . ARG B 1 235 ? 135.072 131.671 136.548 1.00 28.01 ?  235 ARG B CB    1 
ATOM   7441  C  CG    . ARG B 1 235 ? 134.337 130.627 137.367 1.00 38.67 ?  235 ARG B CG    1 
ATOM   7442  C  CD    . ARG B 1 235 ? 134.064 129.360 136.576 1.00 33.71 ?  235 ARG B CD    1 
ATOM   7443  N  NE    . ARG B 1 235 ? 132.706 129.331 136.047 1.00 37.92 ?  235 ARG B NE    1 
ATOM   7444  C  CZ    . ARG B 1 235 ? 132.408 129.251 134.758 1.00 40.90 ?  235 ARG B CZ    1 
ATOM   7445  N  NH1   . ARG B 1 235 ? 133.352 129.172 133.835 1.00 42.51 1  235 ARG B NH1   1 
ATOM   7446  N  NH2   . ARG B 1 235 ? 131.132 129.251 134.387 1.00 36.14 ?  235 ARG B NH2   1 
ATOM   7447  N  N     . TYR B 1 236 ? 136.899 134.205 135.824 1.00 22.81 ?  236 TYR B N     1 
ATOM   7448  C  CA    . TYR B 1 236 ? 138.136 134.732 135.259 1.00 24.99 ?  236 TYR B CA    1 
ATOM   7449  C  C     . TYR B 1 236 ? 138.832 135.668 136.238 1.00 24.34 ?  236 TYR B C     1 
ATOM   7450  O  O     . TYR B 1 236 ? 140.041 135.554 136.470 1.00 26.55 ?  236 TYR B O     1 
ATOM   7451  C  CB    . TYR B 1 236 ? 137.853 135.453 133.943 1.00 24.45 ?  236 TYR B CB    1 
ATOM   7452  C  CG    . TYR B 1 236 ? 139.101 135.967 133.274 1.00 22.08 ?  236 TYR B CG    1 
ATOM   7453  C  CD1   . TYR B 1 236 ? 139.979 135.092 132.654 1.00 18.62 ?  236 TYR B CD1   1 
ATOM   7454  C  CD2   . TYR B 1 236 ? 139.412 137.319 133.274 1.00 18.79 ?  236 TYR B CD2   1 
ATOM   7455  C  CE1   . TYR B 1 236 ? 141.121 135.545 132.046 1.00 23.08 ?  236 TYR B CE1   1 
ATOM   7456  C  CE2   . TYR B 1 236 ? 140.555 137.782 132.665 1.00 13.61 ?  236 TYR B CE2   1 
ATOM   7457  C  CZ    . TYR B 1 236 ? 141.406 136.889 132.054 1.00 20.82 ?  236 TYR B CZ    1 
ATOM   7458  O  OH    . TYR B 1 236 ? 142.549 137.333 131.442 1.00 30.55 ?  236 TYR B OH    1 
ATOM   7459  N  N     . ALA B 1 237 ? 138.085 136.606 136.821 1.00 29.80 ?  237 ALA B N     1 
ATOM   7460  C  CA    . ALA B 1 237 ? 138.638 137.558 137.784 1.00 29.51 ?  237 ALA B CA    1 
ATOM   7461  C  C     . ALA B 1 237 ? 138.686 136.893 139.160 1.00 36.56 ?  237 ALA B C     1 
ATOM   7462  O  O     . ALA B 1 237 ? 137.928 137.208 140.079 1.00 36.35 ?  237 ALA B O     1 
ATOM   7463  C  CB    . ALA B 1 237 ? 137.821 138.841 137.802 1.00 30.47 ?  237 ALA B CB    1 
ATOM   7464  N  N     . ASP B 1 238 ? 139.616 135.945 139.286 1.00 51.59 ?  238 ASP B N     1 
ATOM   7465  C  CA    . ASP B 1 238 ? 139.723 135.100 140.466 1.00 51.32 ?  238 ASP B CA    1 
ATOM   7466  C  C     . ASP B 1 238 ? 140.738 135.623 141.474 1.00 55.56 ?  238 ASP B C     1 
ATOM   7467  O  O     . ASP B 1 238 ? 141.377 134.824 142.172 1.00 57.66 ?  238 ASP B O     1 
ATOM   7468  C  CB    . ASP B 1 238 ? 140.073 133.670 140.054 1.00 49.85 ?  238 ASP B CB    1 
ATOM   7469  C  CG    . ASP B 1 238 ? 138.925 132.708 140.266 1.00 54.08 ?  238 ASP B CG    1 
ATOM   7470  O  OD1   . ASP B 1 238 ? 138.911 131.645 139.612 1.00 53.16 ?  238 ASP B OD1   1 
ATOM   7471  O  OD2   . ASP B 1 238 ? 138.025 133.025 141.069 1.00 53.25 -1 238 ASP B OD2   1 
ATOM   7472  N  N     . GLN B 1 239 ? 140.913 136.944 141.553 1.00 64.45 ?  239 GLN B N     1 
ATOM   7473  C  CA    . GLN B 1 239 ? 141.813 137.575 142.520 1.00 65.28 ?  239 GLN B CA    1 
ATOM   7474  C  C     . GLN B 1 239 ? 143.241 137.051 142.374 1.00 67.16 ?  239 GLN B C     1 
ATOM   7475  O  O     . GLN B 1 239 ? 143.862 136.595 143.337 1.00 64.76 ?  239 GLN B O     1 
ATOM   7476  C  CB    . GLN B 1 239 ? 141.302 137.381 143.951 1.00 64.30 ?  239 GLN B CB    1 
ATOM   7477  C  CG    . GLN B 1 239 ? 139.856 137.791 144.151 1.00 63.46 ?  239 GLN B CG    1 
ATOM   7478  C  CD    . GLN B 1 239 ? 139.325 137.406 145.514 1.00 66.62 ?  239 GLN B CD    1 
ATOM   7479  O  OE1   . GLN B 1 239 ? 138.134 137.142 145.676 1.00 64.72 ?  239 GLN B OE1   1 
ATOM   7480  N  NE2   . GLN B 1 239 ? 140.207 137.373 146.504 1.00 66.44 ?  239 GLN B NE2   1 
ATOM   7481  N  N     . MET B 1 240 ? 143.757 137.115 141.144 1.00 68.36 ?  240 MET B N     1 
ATOM   7482  C  CA    . MET B 1 240 ? 145.115 136.674 140.823 1.00 67.11 ?  240 MET B CA    1 
ATOM   7483  C  C     . MET B 1 240 ? 145.350 135.218 141.212 1.00 67.96 ?  240 MET B C     1 
ATOM   7484  O  O     . MET B 1 240 ? 146.447 134.846 141.636 1.00 68.29 ?  240 MET B O     1 
ATOM   7485  C  CB    . MET B 1 240 ? 146.164 137.575 141.483 1.00 67.19 ?  240 MET B CB    1 
ATOM   7486  C  CG    . MET B 1 240 ? 146.230 138.983 140.918 1.00 68.64 ?  240 MET B CG    1 
ATOM   7487  S  SD    . MET B 1 240 ? 144.619 139.685 140.525 1.00 76.69 ?  240 MET B SD    1 
ATOM   7488  C  CE    . MET B 1 240 ? 145.058 141.411 140.358 1.00 66.55 ?  240 MET B CE    1 
ATOM   7489  N  N     . GLY B 1 241 ? 144.323 134.382 141.077 1.00 70.46 ?  241 GLY B N     1 
ATOM   7490  C  CA    . GLY B 1 241 ? 144.452 132.980 141.422 1.00 69.56 ?  241 GLY B CA    1 
ATOM   7491  C  C     . GLY B 1 241 ? 144.626 132.693 142.894 1.00 72.28 ?  241 GLY B C     1 
ATOM   7492  O  O     . GLY B 1 241 ? 145.066 131.595 143.247 1.00 72.91 ?  241 GLY B O     1 
ATOM   7493  N  N     . GLN B 1 242 ? 144.297 133.644 143.768 1.00 73.68 ?  242 GLN B N     1 
ATOM   7494  C  CA    . GLN B 1 242 ? 144.459 133.459 145.206 1.00 73.00 ?  242 GLN B CA    1 
ATOM   7495  C  C     . GLN B 1 242 ? 143.181 132.925 145.848 1.00 73.64 ?  242 GLN B C     1 
ATOM   7496  O  O     . GLN B 1 242 ? 143.183 131.853 146.461 1.00 71.98 ?  242 GLN B O     1 
ATOM   7497  C  CB    . GLN B 1 242 ? 144.876 134.780 145.862 1.00 71.35 ?  242 GLN B CB    1 
ATOM   7498  C  CG    . GLN B 1 242 ? 146.252 135.278 145.448 1.00 73.43 ?  242 GLN B CG    1 
ATOM   7499  C  CD    . GLN B 1 242 ? 146.814 136.308 146.411 1.00 75.32 ?  242 GLN B CD    1 
ATOM   7500  O  OE1   . GLN B 1 242 ? 146.261 136.537 147.486 1.00 75.18 ?  242 GLN B OE1   1 
ATOM   7501  N  NE2   . GLN B 1 242 ? 147.922 136.933 146.028 1.00 72.12 ?  242 GLN B NE2   1 
ATOM   7502  N  N     . ARG B 1 243 ? 142.084 133.665 145.709 1.00 68.25 ?  243 ARG B N     1 
ATOM   7503  C  CA    . ARG B 1 243 ? 140.797 133.293 146.275 1.00 66.93 ?  243 ARG B CA    1 
ATOM   7504  C  C     . ARG B 1 243 ? 139.743 133.348 145.181 1.00 66.24 ?  243 ARG B C     1 
ATOM   7505  O  O     . ARG B 1 243 ? 139.741 134.267 144.357 1.00 65.42 ?  243 ARG B O     1 
ATOM   7506  C  CB    . ARG B 1 243 ? 140.419 134.221 147.438 1.00 66.32 ?  243 ARG B CB    1 
ATOM   7507  C  CG    . ARG B 1 243 ? 139.065 133.942 148.069 1.00 66.93 ?  243 ARG B CG    1 
ATOM   7508  C  CD    . ARG B 1 243 ? 138.586 135.146 148.868 1.00 67.50 ?  243 ARG B CD    1 
ATOM   7509  N  NE    . ARG B 1 243 ? 137.859 136.103 148.043 1.00 69.40 ?  243 ARG B NE    1 
ATOM   7510  C  CZ    . ARG B 1 243 ? 136.696 136.650 148.376 1.00 69.52 ?  243 ARG B CZ    1 
ATOM   7511  N  NH1   . ARG B 1 243 ? 136.099 136.360 149.519 1.00 66.61 1  243 ARG B NH1   1 
ATOM   7512  N  NH2   . ARG B 1 243 ? 136.122 137.511 147.542 1.00 64.05 ?  243 ARG B NH2   1 
ATOM   7513  N  N     . GLN B 1 244 ? 138.854 132.357 145.174 1.00 64.22 ?  244 GLN B N     1 
ATOM   7514  C  CA    . GLN B 1 244 ? 137.867 132.236 144.109 1.00 63.23 ?  244 GLN B CA    1 
ATOM   7515  C  C     . GLN B 1 244 ? 136.960 133.460 144.063 1.00 63.95 ?  244 GLN B C     1 
ATOM   7516  O  O     . GLN B 1 244 ? 136.477 133.931 145.096 1.00 61.87 ?  244 GLN B O     1 
ATOM   7517  C  CB    . GLN B 1 244 ? 137.037 130.968 144.303 1.00 61.27 ?  244 GLN B CB    1 
ATOM   7518  C  CG    . GLN B 1 244 ? 137.855 129.686 144.278 1.00 62.33 ?  244 GLN B CG    1 
ATOM   7519  C  CD    . GLN B 1 244 ? 136.989 128.442 144.299 1.00 62.46 ?  244 GLN B CD    1 
ATOM   7520  O  OE1   . GLN B 1 244 ? 135.976 128.386 144.996 1.00 60.44 ?  244 GLN B OE1   1 
ATOM   7521  N  NE2   . GLN B 1 244 ? 137.385 127.433 143.531 1.00 60.00 ?  244 GLN B NE2   1 
ATOM   7522  N  N     . GLY B 1 245 ? 136.737 133.975 142.854 1.00 49.21 ?  245 GLY B N     1 
ATOM   7523  C  CA    . GLY B 1 245 ? 135.880 135.127 142.658 1.00 44.50 ?  245 GLY B CA    1 
ATOM   7524  C  C     . GLY B 1 245 ? 134.438 134.855 143.028 1.00 44.34 ?  245 GLY B C     1 
ATOM   7525  O  O     . GLY B 1 245 ? 133.812 133.940 142.486 1.00 41.39 ?  245 GLY B O     1 
ATOM   7526  N  N     . SER B 1 246 ? 133.898 135.647 143.949 1.00 39.46 ?  246 SER B N     1 
ATOM   7527  C  CA    . SER B 1 246 ? 132.557 135.445 144.476 1.00 33.42 ?  246 SER B CA    1 
ATOM   7528  C  C     . SER B 1 246 ? 131.664 136.603 144.060 1.00 30.07 ?  246 SER B C     1 
ATOM   7529  O  O     . SER B 1 246 ? 132.019 137.770 144.252 1.00 23.53 ?  246 SER B O     1 
ATOM   7530  C  CB    . SER B 1 246 ? 132.583 135.316 146.000 1.00 31.88 ?  246 SER B CB    1 
ATOM   7531  O  OG    . SER B 1 246 ? 133.256 136.412 146.594 1.00 38.37 ?  246 SER B OG    1 
ATOM   7532  N  N     . GLY B 1 247 ? 130.508 136.274 143.490 1.00 26.03 ?  247 GLY B N     1 
ATOM   7533  C  CA    . GLY B 1 247 ? 129.547 137.280 143.102 1.00 10.12 ?  247 GLY B CA    1 
ATOM   7534  C  C     . GLY B 1 247 ? 128.140 136.809 143.407 1.00 12.49 ?  247 GLY B C     1 
ATOM   7535  O  O     . GLY B 1 247 ? 127.886 135.620 143.599 1.00 22.70 ?  247 GLY B O     1 
ATOM   7536  N  N     . ALA B 1 248 ? 127.226 137.772 143.452 1.00 17.14 ?  248 ALA B N     1 
ATOM   7537  C  CA    . ALA B 1 248 ? 125.829 137.497 143.737 1.00 17.75 ?  248 ALA B CA    1 
ATOM   7538  C  C     . ALA B 1 248 ? 124.953 138.179 142.700 1.00 16.83 ?  248 ALA B C     1 
ATOM   7539  O  O     . ALA B 1 248 ? 125.278 139.257 142.197 1.00 23.25 ?  248 ALA B O     1 
ATOM   7540  C  CB    . ALA B 1 248 ? 125.434 137.967 145.144 1.00 4.65  ?  248 ALA B CB    1 
ATOM   7541  N  N     . ALA B 1 249 ? 123.838 137.531 142.379 1.00 16.18 ?  249 ALA B N     1 
ATOM   7542  C  CA    . ALA B 1 249 ? 122.840 138.075 141.473 1.00 14.30 ?  249 ALA B CA    1 
ATOM   7543  C  C     . ALA B 1 249 ? 121.501 138.110 142.191 1.00 16.37 ?  249 ALA B C     1 
ATOM   7544  O  O     . ALA B 1 249 ? 121.119 137.135 142.843 1.00 24.63 ?  249 ALA B O     1 
ATOM   7545  C  CB    . ALA B 1 249 ? 122.741 137.246 140.192 1.00 11.62 ?  249 ALA B CB    1 
ATOM   7546  N  N     . TYR B 1 250 ? 120.797 139.228 142.077 1.00 17.18 ?  250 TYR B N     1 
ATOM   7547  C  CA    . TYR B 1 250 ? 119.508 139.399 142.723 1.00 5.89  ?  250 TYR B CA    1 
ATOM   7548  C  C     . TYR B 1 250 ? 118.432 139.612 141.672 1.00 7.44  ?  250 TYR B C     1 
ATOM   7549  O  O     . TYR B 1 250 ? 118.629 140.357 140.708 1.00 21.34 ?  250 TYR B O     1 
ATOM   7550  C  CB    . TYR B 1 250 ? 119.527 140.576 143.700 1.00 12.37 ?  250 TYR B CB    1 
ATOM   7551  C  CG    . TYR B 1 250 ? 120.029 140.213 145.075 1.00 15.54 ?  250 TYR B CG    1 
ATOM   7552  C  CD1   . TYR B 1 250 ? 121.376 139.976 145.302 1.00 8.40  ?  250 TYR B CD1   1 
ATOM   7553  C  CD2   . TYR B 1 250 ? 119.154 140.093 146.146 1.00 12.52 ?  250 TYR B CD2   1 
ATOM   7554  C  CE1   . TYR B 1 250 ? 121.839 139.637 146.554 1.00 1.20  ?  250 TYR B CE1   1 
ATOM   7555  C  CE2   . TYR B 1 250 ? 119.609 139.755 147.403 1.00 7.97  ?  250 TYR B CE2   1 
ATOM   7556  C  CZ    . TYR B 1 250 ? 120.953 139.529 147.600 1.00 11.67 ?  250 TYR B CZ    1 
ATOM   7557  O  OH    . TYR B 1 250 ? 121.414 139.196 148.851 1.00 21.15 ?  250 TYR B OH    1 
ATOM   7558  N  N     . LEU B 1 251 ? 117.299 138.945 141.861 1.00 14.84 ?  251 LEU B N     1 
ATOM   7559  C  CA    . LEU B 1 251 ? 116.158 139.090 140.973 1.00 15.67 ?  251 LEU B CA    1 
ATOM   7560  C  C     . LEU B 1 251 ? 114.895 139.230 141.803 1.00 10.15 ?  251 LEU B C     1 
ATOM   7561  O  O     . LEU B 1 251 ? 114.728 138.541 142.812 1.00 19.07 ?  251 LEU B O     1 
ATOM   7562  C  CB    . LEU B 1 251 ? 116.027 137.894 140.025 1.00 14.63 ?  251 LEU B CB    1 
ATOM   7563  C  CG    . LEU B 1 251 ? 115.179 138.132 138.777 1.00 14.48 ?  251 LEU B CG    1 
ATOM   7564  C  CD1   . LEU B 1 251 ? 115.892 139.055 137.812 1.00 6.94  ?  251 LEU B CD1   1 
ATOM   7565  C  CD2   . LEU B 1 251 ? 114.832 136.818 138.110 1.00 10.11 ?  251 LEU B CD2   1 
ATOM   7566  N  N     . ASN B 1 252 ? 114.012 140.127 141.376 1.00 12.31 ?  252 ASN B N     1 
ATOM   7567  C  CA    . ASN B 1 252 ? 112.713 140.255 142.018 1.00 10.56 ?  252 ASN B CA    1 
ATOM   7568  C  C     . ASN B 1 252 ? 111.880 139.004 141.773 1.00 17.18 ?  252 ASN B C     1 
ATOM   7569  O  O     . ASN B 1 252 ? 111.945 138.394 140.704 1.00 27.97 ?  252 ASN B O     1 
ATOM   7570  C  CB    . ASN B 1 252 ? 111.982 141.489 141.496 1.00 13.51 ?  252 ASN B CB    1 
ATOM   7571  C  CG    . ASN B 1 252 ? 111.018 142.065 142.511 1.00 20.90 ?  252 ASN B CG    1 
ATOM   7572  O  OD1   . ASN B 1 252 ? 109.963 141.492 142.777 1.00 31.96 ?  252 ASN B OD1   1 
ATOM   7573  N  ND2   . ASN B 1 252 ? 111.379 143.204 143.087 1.00 16.81 ?  252 ASN B ND2   1 
ATOM   7574  N  N     . ILE B 1 253 ? 111.093 138.617 142.780 1.00 12.04 ?  253 ILE B N     1 
ATOM   7575  C  CA    . ILE B 1 253 ? 110.259 137.431 142.645 1.00 17.59 ?  253 ILE B CA    1 
ATOM   7576  C  C     . ILE B 1 253 ? 109.158 137.625 141.609 1.00 23.32 ?  253 ILE B C     1 
ATOM   7577  O  O     . ILE B 1 253 ? 108.625 136.641 141.085 1.00 24.82 ?  253 ILE B O     1 
ATOM   7578  C  CB    . ILE B 1 253 ? 109.671 137.035 144.014 1.00 20.99 ?  253 ILE B CB    1 
ATOM   7579  C  CG1   . ILE B 1 253 ? 109.270 135.559 144.013 1.00 16.36 ?  253 ILE B CG1   1 
ATOM   7580  C  CG2   . ILE B 1 253 ? 108.499 137.930 144.381 1.00 14.57 ?  253 ILE B CG2   1 
ATOM   7581  C  CD1   . ILE B 1 253 ? 109.421 134.886 145.348 1.00 18.96 ?  253 ILE B CD1   1 
ATOM   7582  N  N     . PHE B 1 254 ? 108.808 138.868 141.288 1.00 30.33 ?  254 PHE B N     1 
ATOM   7583  C  CA    . PHE B 1 254 ? 107.815 139.154 140.263 1.00 18.12 ?  254 PHE B CA    1 
ATOM   7584  C  C     . PHE B 1 254 ? 108.427 139.280 138.875 1.00 20.80 ?  254 PHE B C     1 
ATOM   7585  O  O     . PHE B 1 254 ? 107.698 139.522 137.908 1.00 27.34 ?  254 PHE B O     1 
ATOM   7586  C  CB    . PHE B 1 254 ? 107.044 140.429 140.616 1.00 21.69 ?  254 PHE B CB    1 
ATOM   7587  C  CG    . PHE B 1 254 ? 105.981 140.221 141.656 1.00 26.47 ?  254 PHE B CG    1 
ATOM   7588  C  CD1   . PHE B 1 254 ? 104.883 139.424 141.388 1.00 25.87 ?  254 PHE B CD1   1 
ATOM   7589  C  CD2   . PHE B 1 254 ? 106.085 140.810 142.903 1.00 25.47 ?  254 PHE B CD2   1 
ATOM   7590  C  CE1   . PHE B 1 254 ? 103.904 139.227 142.339 1.00 29.44 ?  254 PHE B CE1   1 
ATOM   7591  C  CE2   . PHE B 1 254 ? 105.108 140.615 143.859 1.00 26.38 ?  254 PHE B CE2   1 
ATOM   7592  C  CZ    . PHE B 1 254 ? 104.017 139.822 143.576 1.00 25.35 ?  254 PHE B CZ    1 
ATOM   7593  N  N     . HIS B 1 255 ? 109.741 139.128 138.759 1.00 27.15 ?  255 HIS B N     1 
ATOM   7594  C  CA    . HIS B 1 255 ? 110.379 139.049 137.454 1.00 20.76 ?  255 HIS B CA    1 
ATOM   7595  C  C     . HIS B 1 255 ? 109.954 137.771 136.747 1.00 23.58 ?  255 HIS B C     1 
ATOM   7596  O  O     . HIS B 1 255 ? 109.781 136.722 137.371 1.00 30.47 ?  255 HIS B O     1 
ATOM   7597  C  CB    . HIS B 1 255 ? 111.898 139.095 137.603 1.00 17.98 ?  255 HIS B CB    1 
ATOM   7598  C  CG    . HIS B 1 255 ? 112.625 139.450 136.343 1.00 22.26 ?  255 HIS B CG    1 
ATOM   7599  N  ND1   . HIS B 1 255 ? 112.800 138.558 135.308 1.00 14.82 ?  255 HIS B ND1   1 
ATOM   7600  C  CD2   . HIS B 1 255 ? 113.234 140.596 135.959 1.00 20.06 ?  255 HIS B CD2   1 
ATOM   7601  C  CE1   . HIS B 1 255 ? 113.480 139.142 134.337 1.00 12.90 ?  255 HIS B CE1   1 
ATOM   7602  N  NE2   . HIS B 1 255 ? 113.758 140.378 134.708 1.00 12.09 ?  255 HIS B NE2   1 
ATOM   7603  N  N     . ARG B 1 256 ? 109.787 137.870 135.429 1.00 26.39 ?  256 ARG B N     1 
ATOM   7604  C  CA    . ARG B 1 256 ? 109.315 136.732 134.651 1.00 22.29 ?  256 ARG B CA    1 
ATOM   7605  C  C     . ARG B 1 256 ? 110.301 135.572 134.701 1.00 24.96 ?  256 ARG B C     1 
ATOM   7606  O  O     . ARG B 1 256 ? 109.899 134.404 134.727 1.00 32.64 ?  256 ARG B O     1 
ATOM   7607  C  CB    . ARG B 1 256 ? 109.066 137.170 133.211 1.00 26.13 ?  256 ARG B CB    1 
ATOM   7608  C  CG    . ARG B 1 256 ? 107.880 136.514 132.565 1.00 35.87 ?  256 ARG B CG    1 
ATOM   7609  C  CD    . ARG B 1 256 ? 108.222 135.136 132.055 1.00 31.95 ?  256 ARG B CD    1 
ATOM   7610  N  NE    . ARG B 1 256 ? 109.594 135.026 131.578 1.00 30.96 ?  256 ARG B NE    1 
ATOM   7611  C  CZ    . ARG B 1 256 ? 110.131 133.905 131.120 1.00 33.29 ?  256 ARG B CZ    1 
ATOM   7612  N  NH1   . ARG B 1 256 ? 109.441 132.776 131.075 1.00 30.55 1  256 ARG B NH1   1 
ATOM   7613  N  NH2   . ARG B 1 256 ? 111.392 133.913 130.701 1.00 34.33 ?  256 ARG B NH2   1 
ATOM   7614  N  N     . ASP B 1 257 ? 111.596 135.873 134.724 1.00 26.22 ?  257 ASP B N     1 
ATOM   7615  C  CA    . ASP B 1 257 ? 112.640 134.859 134.722 1.00 21.49 ?  257 ASP B CA    1 
ATOM   7616  C  C     . ASP B 1 257 ? 112.931 134.292 136.102 1.00 22.72 ?  257 ASP B C     1 
ATOM   7617  O  O     . ASP B 1 257 ? 114.007 133.715 136.290 1.00 27.09 ?  257 ASP B O     1 
ATOM   7618  C  CB    . ASP B 1 257 ? 113.925 135.432 134.127 1.00 25.70 ?  257 ASP B CB    1 
ATOM   7619  C  CG    . ASP B 1 257 ? 113.915 135.439 132.619 1.00 32.76 ?  257 ASP B CG    1 
ATOM   7620  O  OD1   . ASP B 1 257 ? 113.018 134.808 132.024 1.00 31.80 ?  257 ASP B OD1   1 
ATOM   7621  O  OD2   . ASP B 1 257 ? 114.804 136.081 132.028 1.00 36.44 -1 257 ASP B OD2   1 
ATOM   7622  N  N     . ILE B 1 258 ? 112.019 134.436 137.065 1.00 26.47 ?  258 ILE B N     1 
ATOM   7623  C  CA    . ILE B 1 258 ? 112.314 134.011 138.431 1.00 23.00 ?  258 ILE B CA    1 
ATOM   7624  C  C     . ILE B 1 258 ? 112.508 132.501 138.499 1.00 22.75 ?  258 ILE B C     1 
ATOM   7625  O  O     . ILE B 1 258 ? 113.378 132.009 139.225 1.00 34.15 ?  258 ILE B O     1 
ATOM   7626  C  CB    . ILE B 1 258 ? 111.217 134.500 139.395 1.00 27.55 ?  258 ILE B CB    1 
ATOM   7627  C  CG1   . ILE B 1 258 ? 111.577 134.147 140.841 1.00 24.90 ?  258 ILE B CG1   1 
ATOM   7628  C  CG2   . ILE B 1 258 ? 109.852 133.946 139.010 1.00 19.92 ?  258 ILE B CG2   1 
ATOM   7629  C  CD1   . ILE B 1 258 ? 112.887 134.745 141.302 1.00 17.22 ?  258 ILE B CD1   1 
ATOM   7630  N  N     . ASN B 1 259 ? 111.720 131.739 137.737 1.00 31.64 ?  259 ASN B N     1 
ATOM   7631  C  CA    . ASN B 1 259 ? 111.864 130.286 137.762 1.00 28.34 ?  259 ASN B CA    1 
ATOM   7632  C  C     . ASN B 1 259 ? 113.157 129.849 137.083 1.00 28.53 ?  259 ASN B C     1 
ATOM   7633  O  O     . ASN B 1 259 ? 113.848 128.953 137.575 1.00 30.84 ?  259 ASN B O     1 
ATOM   7634  C  CB    . ASN B 1 259 ? 110.653 129.625 137.109 1.00 29.00 ?  259 ASN B CB    1 
ATOM   7635  C  CG    . ASN B 1 259 ? 109.457 129.564 138.035 1.00 33.29 ?  259 ASN B CG    1 
ATOM   7636  O  OD1   . ASN B 1 259 ? 109.526 128.985 139.118 1.00 34.36 ?  259 ASN B OD1   1 
ATOM   7637  N  ND2   . ASN B 1 259 ? 108.352 130.164 137.615 1.00 34.97 ?  259 ASN B ND2   1 
ATOM   7638  N  N     . ASP B 1 260 ? 113.500 130.475 135.956 1.00 31.47 ?  260 ASP B N     1 
ATOM   7639  C  CA    . ASP B 1 260 ? 114.800 130.230 135.340 1.00 24.64 ?  260 ASP B CA    1 
ATOM   7640  C  C     . ASP B 1 260 ? 115.930 130.662 136.264 1.00 28.75 ?  260 ASP B C     1 
ATOM   7641  O  O     . ASP B 1 260 ? 116.971 129.998 136.342 1.00 33.75 ?  260 ASP B O     1 
ATOM   7642  C  CB    . ASP B 1 260 ? 114.892 130.963 134.003 1.00 27.87 ?  260 ASP B CB    1 
ATOM   7643  C  CG    . ASP B 1 260 ? 113.802 130.554 133.037 1.00 40.56 ?  260 ASP B CG    1 
ATOM   7644  O  OD1   . ASP B 1 260 ? 113.693 131.181 131.963 1.00 37.76 ?  260 ASP B OD1   1 
ATOM   7645  O  OD2   . ASP B 1 260 ? 113.052 129.606 133.352 1.00 42.90 -1 260 ASP B OD2   1 
ATOM   7646  N  N     . PHE B 1 261 ? 115.742 131.783 136.962 1.00 33.42 ?  261 PHE B N     1 
ATOM   7647  C  CA    . PHE B 1 261 ? 116.729 132.259 137.926 1.00 20.73 ?  261 PHE B CA    1 
ATOM   7648  C  C     . PHE B 1 261 ? 116.981 131.223 139.014 1.00 23.47 ?  261 PHE B C     1 
ATOM   7649  O  O     . PHE B 1 261 ? 118.129 130.985 139.405 1.00 26.79 ?  261 PHE B O     1 
ATOM   7650  C  CB    . PHE B 1 261 ? 116.238 133.574 138.529 1.00 14.21 ?  261 PHE B CB    1 
ATOM   7651  C  CG    . PHE B 1 261 ? 117.225 134.252 139.431 1.00 27.64 ?  261 PHE B CG    1 
ATOM   7652  C  CD1   . PHE B 1 261 ? 118.298 134.945 138.906 1.00 22.13 ?  261 PHE B CD1   1 
ATOM   7653  C  CD2   . PHE B 1 261 ? 117.055 134.230 140.804 1.00 21.15 ?  261 PHE B CD2   1 
ATOM   7654  C  CE1   . PHE B 1 261 ? 119.197 135.580 139.731 1.00 14.29 ?  261 PHE B CE1   1 
ATOM   7655  C  CE2   . PHE B 1 261 ? 117.952 134.865 141.633 1.00 12.58 ?  261 PHE B CE2   1 
ATOM   7656  C  CZ    . PHE B 1 261 ? 119.024 135.540 141.095 1.00 17.93 ?  261 PHE B CZ    1 
ATOM   7657  N  N     . LEU B 1 262 ? 115.915 130.595 139.515 1.00 31.41 ?  262 LEU B N     1 
ATOM   7658  C  CA    . LEU B 1 262 ? 116.061 129.599 140.568 1.00 25.47 ?  262 LEU B CA    1 
ATOM   7659  C  C     . LEU B 1 262 ? 116.602 128.279 140.039 1.00 30.04 ?  262 LEU B C     1 
ATOM   7660  O  O     . LEU B 1 262 ? 117.305 127.567 140.765 1.00 32.42 ?  262 LEU B O     1 
ATOM   7661  C  CB    . LEU B 1 262 ? 114.720 129.378 141.263 1.00 32.20 ?  262 LEU B CB    1 
ATOM   7662  C  CG    . LEU B 1 262 ? 114.092 130.612 141.904 1.00 22.35 ?  262 LEU B CG    1 
ATOM   7663  C  CD1   . LEU B 1 262 ? 112.723 130.280 142.465 1.00 29.16 ?  262 LEU B CD1   1 
ATOM   7664  C  CD2   . LEU B 1 262 ? 115.006 131.163 142.976 1.00 22.81 ?  262 LEU B CD2   1 
ATOM   7665  N  N     . ASP B 1 263 ? 116.292 127.931 138.788 1.00 42.45 ?  263 ASP B N     1 
ATOM   7666  C  CA    . ASP B 1 263 ? 116.744 126.665 138.224 1.00 31.66 ?  263 ASP B CA    1 
ATOM   7667  C  C     . ASP B 1 263 ? 118.251 126.605 138.031 1.00 34.41 ?  263 ASP B C     1 
ATOM   7668  O  O     . ASP B 1 263 ? 118.785 125.514 137.809 1.00 47.73 ?  263 ASP B O     1 
ATOM   7669  C  CB    . ASP B 1 263 ? 116.048 126.403 136.888 1.00 37.05 ?  263 ASP B CB    1 
ATOM   7670  C  CG    . ASP B 1 263 ? 114.572 126.115 137.046 1.00 46.24 ?  263 ASP B CG    1 
ATOM   7671  O  OD1   . ASP B 1 263 ? 114.127 125.891 138.190 1.00 42.48 ?  263 ASP B OD1   1 
ATOM   7672  O  OD2   . ASP B 1 263 ? 113.852 126.115 136.025 1.00 47.80 -1 263 ASP B OD2   1 
ATOM   7673  N  N     . THR B 1 264 ? 118.948 127.740 138.100 1.00 38.94 ?  264 THR B N     1 
ATOM   7674  C  CA    . THR B 1 264 ? 120.400 127.740 137.984 1.00 37.20 ?  264 THR B CA    1 
ATOM   7675  C  C     . THR B 1 264 ? 121.088 127.112 139.189 1.00 40.49 ?  264 THR B C     1 
ATOM   7676  O  O     . THR B 1 264 ? 122.285 126.820 139.112 1.00 41.51 ?  264 THR B O     1 
ATOM   7677  C  CB    . THR B 1 264 ? 120.914 129.168 137.788 1.00 34.86 ?  264 THR B CB    1 
ATOM   7678  O  OG1   . THR B 1 264 ? 120.539 129.974 138.912 1.00 37.84 ?  264 THR B OG1   1 
ATOM   7679  C  CG2   . THR B 1 264 ? 120.331 129.774 136.526 1.00 35.27 ?  264 THR B CG2   1 
ATOM   7680  N  N     . LYS B 1 265 ? 120.369 126.895 140.289 1.00 34.45 ?  265 LYS B N     1 
ATOM   7681  C  CA    . LYS B 1 265 ? 120.944 126.330 141.501 1.00 36.43 ?  265 LYS B CA    1 
ATOM   7682  C  C     . LYS B 1 265 ? 120.504 124.899 141.770 1.00 41.95 ?  265 LYS B C     1 
ATOM   7683  O  O     . LYS B 1 265 ? 120.906 124.327 142.788 1.00 44.94 ?  265 LYS B O     1 
ATOM   7684  C  CB    . LYS B 1 265 ? 120.597 127.209 142.706 1.00 35.53 ?  265 LYS B CB    1 
ATOM   7685  C  CG    . LYS B 1 265 ? 121.410 128.480 142.785 1.00 38.41 ?  265 LYS B CG    1 
ATOM   7686  C  CD    . LYS B 1 265 ? 122.888 128.181 142.658 1.00 42.43 ?  265 LYS B CD    1 
ATOM   7687  C  CE    . LYS B 1 265 ? 123.698 129.453 142.610 1.00 39.18 ?  265 LYS B CE    1 
ATOM   7688  N  NZ    . LYS B 1 265 ? 125.118 129.183 142.270 1.00 43.31 1  265 LYS B NZ    1 
ATOM   7689  N  N     . LYS B 1 266 ? 119.693 124.307 140.900 1.00 46.48 ?  266 LYS B N     1 
ATOM   7690  C  CA    . LYS B 1 266 ? 119.299 122.919 141.082 1.00 48.96 ?  266 LYS B CA    1 
ATOM   7691  C  C     . LYS B 1 266 ? 120.483 121.991 140.839 1.00 55.08 ?  266 LYS B C     1 
ATOM   7692  O  O     . LYS B 1 266 ? 121.364 122.271 140.022 1.00 56.31 ?  266 LYS B O     1 
ATOM   7693  C  CB    . LYS B 1 266 ? 118.147 122.561 140.145 1.00 48.89 ?  266 LYS B CB    1 
ATOM   7694  C  CG    . LYS B 1 266 ? 116.797 123.086 140.596 1.00 50.80 ?  266 LYS B CG    1 
ATOM   7695  C  CD    . LYS B 1 266 ? 115.717 122.771 139.576 1.00 51.90 ?  266 LYS B CD    1 
ATOM   7696  C  CE    . LYS B 1 266 ? 114.337 123.129 140.104 1.00 50.94 ?  266 LYS B CE    1 
ATOM   7697  N  NZ    . LYS B 1 266 ? 113.299 123.049 139.039 1.00 50.51 1  266 LYS B NZ    1 
ATOM   7698  N  N     . ILE B 1 267 ? 120.504 120.876 141.572 1.00 58.24 ?  267 ILE B N     1 
ATOM   7699  C  CA    . ILE B 1 267 ? 121.585 119.910 141.414 1.00 60.88 ?  267 ILE B CA    1 
ATOM   7700  C  C     . ILE B 1 267 ? 121.527 119.254 140.042 1.00 62.41 ?  267 ILE B C     1 
ATOM   7701  O  O     . ILE B 1 267 ? 122.559 118.846 139.495 1.00 61.60 ?  267 ILE B O     1 
ATOM   7702  C  CB    . ILE B 1 267 ? 121.544 118.859 142.539 1.00 62.07 ?  267 ILE B CB    1 
ATOM   7703  C  CG1   . ILE B 1 267 ? 121.815 119.505 143.900 1.00 61.89 ?  267 ILE B CG1   1 
ATOM   7704  C  CG2   . ILE B 1 267 ? 122.549 117.751 142.272 1.00 58.67 ?  267 ILE B CG2   1 
ATOM   7705  C  CD1   . ILE B 1 267 ? 120.566 119.775 144.715 1.00 60.76 ?  267 ILE B CD1   1 
ATOM   7706  N  N     . SER B 1 268 ? 120.334 119.143 139.463 1.00 63.05 ?  268 SER B N     1 
ATOM   7707  C  CA    . SER B 1 268 ? 120.141 118.549 138.149 1.00 64.65 ?  268 SER B CA    1 
ATOM   7708  C  C     . SER B 1 268 ? 120.213 119.571 137.021 1.00 65.97 ?  268 SER B C     1 
ATOM   7709  O  O     . SER B 1 268 ? 119.835 119.253 135.890 1.00 65.58 ?  268 SER B O     1 
ATOM   7710  C  CB    . SER B 1 268 ? 118.796 117.819 138.096 1.00 66.48 ?  268 SER B CB    1 
ATOM   7711  O  OG    . SER B 1 268 ? 117.739 118.682 138.475 1.00 61.93 ?  268 SER B OG    1 
ATOM   7712  N  N     . ALA B 1 269 ? 120.678 120.786 137.306 1.00 70.03 ?  269 ALA B N     1 
ATOM   7713  C  CA    . ALA B 1 269 ? 120.681 121.841 136.302 1.00 70.26 ?  269 ALA B CA    1 
ATOM   7714  C  C     . ALA B 1 269 ? 121.626 121.505 135.155 1.00 71.13 ?  269 ALA B C     1 
ATOM   7715  O  O     . ALA B 1 269 ? 122.715 120.961 135.361 1.00 68.97 ?  269 ALA B O     1 
ATOM   7716  C  CB    . ALA B 1 269 ? 121.079 123.174 136.935 1.00 66.54 ?  269 ALA B CB    1 
ATOM   7717  N  N     . ASP B 1 270 ? 121.197 121.831 133.940 1.00 74.02 ?  270 ASP B N     1 
ATOM   7718  C  CA    . ASP B 1 270 ? 122.029 121.635 132.762 1.00 74.33 ?  270 ASP B CA    1 
ATOM   7719  C  C     . ASP B 1 270 ? 123.242 122.558 132.809 1.00 73.93 ?  270 ASP B C     1 
ATOM   7720  O  O     . ASP B 1 270 ? 123.200 123.649 133.385 1.00 75.43 ?  270 ASP B O     1 
ATOM   7721  C  CB    . ASP B 1 270 ? 121.220 121.890 131.491 1.00 73.65 ?  270 ASP B CB    1 
ATOM   7722  C  CG    . ASP B 1 270 ? 121.814 121.212 130.272 1.00 76.84 ?  270 ASP B CG    1 
ATOM   7723  O  OD1   . ASP B 1 270 ? 122.995 121.468 129.960 1.00 75.94 ?  270 ASP B OD1   1 
ATOM   7724  O  OD2   . ASP B 1 270 ? 121.096 120.422 129.622 1.00 75.61 -1 270 ASP B OD2   1 
ATOM   7725  N  N     . GLU B 1 271 ? 124.337 122.106 132.194 1.00 74.27 ?  271 GLU B N     1 
ATOM   7726  C  CA    . GLU B 1 271 ? 125.575 122.876 132.218 1.00 75.67 ?  271 GLU B CA    1 
ATOM   7727  C  C     . GLU B 1 271 ? 125.464 124.192 131.459 1.00 73.53 ?  271 GLU B C     1 
ATOM   7728  O  O     . GLU B 1 271 ? 126.268 125.099 131.698 1.00 73.03 ?  271 GLU B O     1 
ATOM   7729  C  CB    . GLU B 1 271 ? 126.725 122.043 131.650 1.00 73.87 ?  271 GLU B CB    1 
ATOM   7730  C  CG    . GLU B 1 271 ? 127.151 120.891 132.545 1.00 73.21 ?  271 GLU B CG    1 
ATOM   7731  C  CD    . GLU B 1 271 ? 127.700 121.360 133.878 1.00 75.05 ?  271 GLU B CD    1 
ATOM   7732  O  OE1   . GLU B 1 271 ? 128.399 122.395 133.907 1.00 75.43 ?  271 GLU B OE1   1 
ATOM   7733  O  OE2   . GLU B 1 271 ? 127.430 120.696 134.901 1.00 74.89 -1 271 GLU B OE2   1 
ATOM   7734  N  N     . ASP B 1 272 ? 124.496 124.321 130.553 1.00 69.75 ?  272 ASP B N     1 
ATOM   7735  C  CA    . ASP B 1 272 ? 124.243 125.587 129.879 1.00 71.73 ?  272 ASP B CA    1 
ATOM   7736  C  C     . ASP B 1 272 ? 123.296 126.486 130.663 1.00 70.44 ?  272 ASP B C     1 
ATOM   7737  O  O     . ASP B 1 272 ? 122.990 127.591 130.205 1.00 66.88 ?  272 ASP B O     1 
ATOM   7738  C  CB    . ASP B 1 272 ? 123.690 125.342 128.468 1.00 70.85 ?  272 ASP B CB    1 
ATOM   7739  C  CG    . ASP B 1 272 ? 122.237 124.901 128.472 1.00 73.30 ?  272 ASP B CG    1 
ATOM   7740  O  OD1   . ASP B 1 272 ? 121.805 124.254 129.447 1.00 72.91 ?  272 ASP B OD1   1 
ATOM   7741  O  OD2   . ASP B 1 272 ? 121.524 125.206 127.492 1.00 70.51 -1 272 ASP B OD2   1 
ATOM   7742  N  N     . VAL B 1 273 ? 122.814 126.029 131.820 1.00 66.23 ?  273 VAL B N     1 
ATOM   7743  C  CA    . VAL B 1 273 ? 121.975 126.826 132.702 1.00 66.52 ?  273 VAL B CA    1 
ATOM   7744  C  C     . VAL B 1 273 ? 122.632 127.044 134.060 1.00 64.95 ?  273 VAL B C     1 
ATOM   7745  O  O     . VAL B 1 273 ? 122.546 128.139 134.627 1.00 66.14 ?  273 VAL B O     1 
ATOM   7746  C  CB    . VAL B 1 273 ? 120.582 126.182 132.873 1.00 68.18 ?  273 VAL B CB    1 
ATOM   7747  C  CG1   . VAL B 1 273 ? 119.720 127.004 133.822 1.00 62.76 ?  273 VAL B CG1   1 
ATOM   7748  C  CG2   . VAL B 1 273 ? 119.901 126.026 131.523 1.00 65.62 ?  273 VAL B CG2   1 
ATOM   7749  N  N     . ARG B 1 274 ? 123.299 126.021 134.589 1.00 62.96 ?  274 ARG B N     1 
ATOM   7750  C  CA    . ARG B 1 274 ? 123.862 126.087 135.930 1.00 61.76 ?  274 ARG B CA    1 
ATOM   7751  C  C     . ARG B 1 274 ? 124.965 127.137 136.018 1.00 62.60 ?  274 ARG B C     1 
ATOM   7752  O  O     . ARG B 1 274 ? 125.789 127.278 135.112 1.00 62.96 ?  274 ARG B O     1 
ATOM   7753  C  CB    . ARG B 1 274 ? 124.411 124.715 136.329 1.00 65.11 ?  274 ARG B CB    1 
ATOM   7754  C  CG    . ARG B 1 274 ? 125.567 124.753 137.317 1.00 62.82 ?  274 ARG B CG    1 
ATOM   7755  C  CD    . ARG B 1 274 ? 125.603 123.507 138.185 1.00 63.74 ?  274 ARG B CD    1 
ATOM   7756  N  NE    . ARG B 1 274 ? 126.005 122.327 137.428 1.00 66.77 ?  274 ARG B NE    1 
ATOM   7757  C  CZ    . ARG B 1 274 ? 125.226 121.277 137.207 1.00 68.61 ?  274 ARG B CZ    1 
ATOM   7758  N  NH1   . ARG B 1 274 ? 123.991 121.220 137.678 1.00 67.06 1  274 ARG B NH1   1 
ATOM   7759  N  NH2   . ARG B 1 274 ? 125.698 120.257 136.495 1.00 66.55 ?  274 ARG B NH2   1 
ATOM   7760  N  N     . VAL B 1 275 ? 124.967 127.880 137.123 1.00 49.50 ?  275 VAL B N     1 
ATOM   7761  C  CA    . VAL B 1 275 ? 126.033 128.814 137.464 1.00 46.65 ?  275 VAL B CA    1 
ATOM   7762  C  C     . VAL B 1 275 ? 126.684 128.330 138.753 1.00 49.29 ?  275 VAL B C     1 
ATOM   7763  O  O     . VAL B 1 275 ? 125.995 127.873 139.673 1.00 54.55 ?  275 VAL B O     1 
ATOM   7764  C  CB    . VAL B 1 275 ? 125.511 130.258 137.610 1.00 45.30 ?  275 VAL B CB    1 
ATOM   7765  C  CG1   . VAL B 1 275 ? 125.109 130.815 136.254 1.00 41.64 ?  275 VAL B CG1   1 
ATOM   7766  C  CG2   . VAL B 1 275 ? 124.339 130.311 138.572 1.00 48.00 ?  275 VAL B CG2   1 
ATOM   7767  N  N     . LYS B 1 276 ? 128.011 128.411 138.812 1.00 43.13 ?  276 LYS B N     1 
ATOM   7768  C  CA    . LYS B 1 276 ? 128.778 127.817 139.902 1.00 44.19 ?  276 LYS B CA    1 
ATOM   7769  C  C     . LYS B 1 276 ? 129.235 128.838 140.937 1.00 42.13 ?  276 LYS B C     1 
ATOM   7770  O  O     . LYS B 1 276 ? 129.067 128.616 142.139 1.00 48.13 ?  276 LYS B O     1 
ATOM   7771  C  CB    . LYS B 1 276 ? 130.002 127.059 139.359 1.00 45.94 ?  276 LYS B CB    1 
ATOM   7772  C  CG    . LYS B 1 276 ? 129.716 125.736 138.629 1.00 47.42 ?  276 LYS B CG    1 
ATOM   7773  C  CD    . LYS B 1 276 ? 129.050 125.876 137.258 1.00 48.40 ?  276 LYS B CD    1 
ATOM   7774  C  CE    . LYS B 1 276 ? 129.562 127.076 136.475 1.00 45.33 ?  276 LYS B CE    1 
ATOM   7775  N  NZ    . LYS B 1 276 ? 129.227 126.971 135.028 1.00 49.22 1  276 LYS B NZ    1 
ATOM   7776  N  N     . THR B 1 277 ? 129.816 129.951 140.499 1.00 38.02 ?  277 THR B N     1 
ATOM   7777  C  CA    . THR B 1 277 ? 130.399 130.934 141.400 1.00 39.22 ?  277 THR B CA    1 
ATOM   7778  C  C     . THR B 1 277 ? 129.500 132.140 141.627 1.00 38.73 ?  277 THR B C     1 
ATOM   7779  O  O     . THR B 1 277 ? 129.960 133.148 142.171 1.00 39.15 ?  277 THR B O     1 
ATOM   7780  C  CB    . THR B 1 277 ? 131.757 131.396 140.870 1.00 41.69 ?  277 THR B CB    1 
ATOM   7781  O  OG1   . THR B 1 277 ? 131.563 132.273 139.752 1.00 33.70 ?  277 THR B OG1   1 
ATOM   7782  C  CG2   . THR B 1 277 ? 132.589 130.200 140.438 1.00 39.64 ?  277 THR B CG2   1 
ATOM   7783  N  N     . LEU B 1 278 ? 128.235 132.063 141.225 1.00 34.18 ?  278 LEU B N     1 
ATOM   7784  C  CA    . LEU B 1 278 ? 127.305 133.182 141.322 1.00 28.24 ?  278 LEU B CA    1 
ATOM   7785  C  C     . LEU B 1 278 ? 126.204 132.821 142.310 1.00 24.52 ?  278 LEU B C     1 
ATOM   7786  O  O     . LEU B 1 278 ? 125.311 132.034 141.986 1.00 36.61 ?  278 LEU B O     1 
ATOM   7787  C  CB    . LEU B 1 278 ? 126.721 133.523 139.953 1.00 30.67 ?  278 LEU B CB    1 
ATOM   7788  C  CG    . LEU B 1 278 ? 126.187 134.942 139.760 1.00 28.70 ?  278 LEU B CG    1 
ATOM   7789  C  CD1   . LEU B 1 278 ? 127.326 135.915 139.546 1.00 24.89 ?  278 LEU B CD1   1 
ATOM   7790  C  CD2   . LEU B 1 278 ? 125.221 134.988 138.592 1.00 27.96 ?  278 LEU B CD2   1 
ATOM   7791  N  N     . SER B 1 279 ? 126.272 133.392 143.508 1.00 24.89 ?  279 SER B N     1 
ATOM   7792  C  CA    . SER B 1 279 ? 125.184 133.258 144.464 1.00 17.98 ?  279 SER B CA    1 
ATOM   7793  C  C     . SER B 1 279 ? 123.954 133.996 143.954 1.00 21.42 ?  279 SER B C     1 
ATOM   7794  O  O     . SER B 1 279 ? 124.051 134.944 143.172 1.00 30.82 ?  279 SER B O     1 
ATOM   7795  C  CB    . SER B 1 279 ? 125.596 133.810 145.826 1.00 18.46 ?  279 SER B CB    1 
ATOM   7796  O  OG    . SER B 1 279 ? 126.788 133.200 146.284 1.00 31.78 ?  279 SER B OG    1 
ATOM   7797  N  N     . ILE B 1 280 ? 122.782 133.549 144.392 1.00 19.86 ?  280 ILE B N     1 
ATOM   7798  C  CA    . ILE B 1 280 ? 121.525 134.132 143.948 1.00 20.27 ?  280 ILE B CA    1 
ATOM   7799  C  C     . ILE B 1 280 ? 120.727 134.584 145.159 1.00 12.37 ?  280 ILE B C     1 
ATOM   7800  O  O     . ILE B 1 280 ? 120.719 133.919 146.200 1.00 25.03 ?  280 ILE B O     1 
ATOM   7801  C  CB    . ILE B 1 280 ? 120.705 133.154 143.080 1.00 15.42 ?  280 ILE B CB    1 
ATOM   7802  C  CG1   . ILE B 1 280 ? 120.349 131.883 143.848 1.00 21.88 ?  280 ILE B CG1   1 
ATOM   7803  C  CG2   . ILE B 1 280 ? 121.465 132.803 141.827 1.00 16.03 ?  280 ILE B CG2   1 
ATOM   7804  C  CD1   . ILE B 1 280 ? 119.119 131.190 143.308 1.00 15.40 ?  280 ILE B CD1   1 
ATOM   7805  N  N     . GLY B 1 281 ? 120.088 135.732 145.029 1.00 6.93  ?  281 GLY B N     1 
ATOM   7806  C  CA    . GLY B 1 281 ? 119.165 136.212 146.043 1.00 6.77  ?  281 GLY B CA    1 
ATOM   7807  C  C     . GLY B 1 281 ? 117.864 136.635 145.403 1.00 4.21  ?  281 GLY B C     1 
ATOM   7808  O  O     . GLY B 1 281 ? 117.853 137.216 144.322 1.00 20.89 ?  281 GLY B O     1 
ATOM   7809  N  N     . VAL B 1 282 ? 116.764 136.328 146.081 1.00 13.07 ?  282 VAL B N     1 
ATOM   7810  C  CA    . VAL B 1 282 ? 115.427 136.648 145.597 1.00 16.12 ?  282 VAL B CA    1 
ATOM   7811  C  C     . VAL B 1 282 ? 114.865 137.778 146.446 1.00 12.86 ?  282 VAL B C     1 
ATOM   7812  O  O     . VAL B 1 282 ? 114.910 137.720 147.680 1.00 21.68 ?  282 VAL B O     1 
ATOM   7813  C  CB    . VAL B 1 282 ? 114.505 135.417 145.623 1.00 16.31 ?  282 VAL B CB    1 
ATOM   7814  C  CG1   . VAL B 1 282 ? 113.064 135.826 145.400 1.00 20.40 ?  282 VAL B CG1   1 
ATOM   7815  C  CG2   . VAL B 1 282 ? 114.931 134.434 144.558 1.00 22.87 ?  282 VAL B CG2   1 
ATOM   7816  N  N     . VAL B 1 283 ? 114.350 138.806 145.782 1.00 2.61  ?  283 VAL B N     1 
ATOM   7817  C  CA    . VAL B 1 283 ? 113.705 139.933 146.441 1.00 9.73  ?  283 VAL B CA    1 
ATOM   7818  C  C     . VAL B 1 283 ? 112.204 139.698 146.425 1.00 12.01 ?  283 VAL B C     1 
ATOM   7819  O  O     . VAL B 1 283 ? 111.610 139.498 145.359 1.00 22.77 ?  283 VAL B O     1 
ATOM   7820  C  CB    . VAL B 1 283 ? 114.068 141.258 145.752 1.00 8.36  ?  283 VAL B CB    1 
ATOM   7821  C  CG1   . VAL B 1 283 ? 113.627 142.427 146.602 1.00 10.05 ?  283 VAL B CG1   1 
ATOM   7822  C  CG2   . VAL B 1 283 ? 115.561 141.316 145.488 1.00 9.21  ?  283 VAL B CG2   1 
ATOM   7823  N  N     . ILE B 1 284 ? 111.590 139.712 147.603 1.00 16.01 ?  284 ILE B N     1 
ATOM   7824  C  CA    . ILE B 1 284 ? 110.173 139.389 147.736 1.00 17.63 ?  284 ILE B CA    1 
ATOM   7825  C  C     . ILE B 1 284 ? 109.419 140.578 148.318 1.00 21.20 ?  284 ILE B C     1 
ATOM   7826  O  O     . ILE B 1 284 ? 109.589 140.899 149.504 1.00 24.03 ?  284 ILE B O     1 
ATOM   7827  C  CB    . ILE B 1 284 ? 109.968 138.137 148.603 1.00 14.12 ?  284 ILE B CB    1 
ATOM   7828  C  CG1   . ILE B 1 284 ? 110.811 136.979 148.075 1.00 17.29 ?  284 ILE B CG1   1 
ATOM   7829  C  CG2   . ILE B 1 284 ? 108.499 137.757 148.645 1.00 15.92 ?  284 ILE B CG2   1 
ATOM   7830  C  CD1   . ILE B 1 284 ? 110.595 135.685 148.814 1.00 20.09 ?  284 ILE B CD1   1 
ATOM   7831  N  N     . PRO B 1 285 ? 108.591 141.259 147.534 1.00 20.06 ?  285 PRO B N     1 
ATOM   7832  C  CA    . PRO B 1 285 ? 107.715 142.287 148.103 1.00 29.69 ?  285 PRO B CA    1 
ATOM   7833  C  C     . PRO B 1 285 ? 106.596 141.665 148.923 1.00 28.16 ?  285 PRO B C     1 
ATOM   7834  O  O     . PRO B 1 285 ? 106.326 140.464 148.855 1.00 23.12 ?  285 PRO B O     1 
ATOM   7835  C  CB    . PRO B 1 285 ? 107.160 143.010 146.870 1.00 22.68 ?  285 PRO B CB    1 
ATOM   7836  C  CG    . PRO B 1 285 ? 108.069 142.631 145.749 1.00 20.66 ?  285 PRO B CG    1 
ATOM   7837  C  CD    . PRO B 1 285 ? 108.553 141.256 146.065 1.00 14.72 ?  285 PRO B CD    1 
ATOM   7838  N  N     . ASP B 1 286 ? 105.939 142.512 149.718 1.00 31.68 ?  286 ASP B N     1 
ATOM   7839  C  CA    . ASP B 1 286 ? 104.804 142.053 150.512 1.00 25.85 ?  286 ASP B CA    1 
ATOM   7840  C  C     . ASP B 1 286 ? 103.656 141.565 149.641 1.00 32.58 ?  286 ASP B C     1 
ATOM   7841  O  O     . ASP B 1 286 ? 102.832 140.772 150.109 1.00 36.13 ?  286 ASP B O     1 
ATOM   7842  C  CB    . ASP B 1 286 ? 104.309 143.170 151.430 1.00 27.89 ?  286 ASP B CB    1 
ATOM   7843  C  CG    . ASP B 1 286 ? 104.903 143.090 152.820 1.00 42.45 ?  286 ASP B CG    1 
ATOM   7844  O  OD1   . ASP B 1 286 ? 105.815 142.265 153.034 1.00 38.68 ?  286 ASP B OD1   1 
ATOM   7845  O  OD2   . ASP B 1 286 ? 104.461 143.858 153.699 1.00 45.98 -1 286 ASP B OD2   1 
ATOM   7846  N  N     . LYS B 1 287 ? 103.581 142.026 148.391 1.00 35.56 ?  287 LYS B N     1 
ATOM   7847  C  CA    . LYS B 1 287 ? 102.513 141.591 147.498 1.00 29.84 ?  287 LYS B CA    1 
ATOM   7848  C  C     . LYS B 1 287 ? 102.587 140.094 147.231 1.00 31.94 ?  287 LYS B C     1 
ATOM   7849  O  O     . LYS B 1 287 ? 101.559 139.411 147.197 1.00 37.47 ?  287 LYS B O     1 
ATOM   7850  C  CB    . LYS B 1 287 ? 102.577 142.372 146.185 1.00 29.52 ?  287 LYS B CB    1 
ATOM   7851  C  CG    . LYS B 1 287 ? 101.330 142.240 145.330 1.00 27.75 ?  287 LYS B CG    1 
ATOM   7852  C  CD    . LYS B 1 287 ? 100.095 142.643 146.114 1.00 34.61 ?  287 LYS B CD    1 
ATOM   7853  C  CE    . LYS B 1 287 ? 98.861  142.659 145.235 1.00 35.33 ?  287 LYS B CE    1 
ATOM   7854  N  NZ    . LYS B 1 287 ? 97.704  143.287 145.927 1.00 36.98 1  287 LYS B NZ    1 
ATOM   7855  N  N     . PHE B 1 288 ? 103.796 139.565 147.032 1.00 31.64 ?  288 PHE B N     1 
ATOM   7856  C  CA    . PHE B 1 288 ? 103.943 138.133 146.789 1.00 25.08 ?  288 PHE B CA    1 
ATOM   7857  C  C     . PHE B 1 288 ? 103.518 137.318 148.002 1.00 26.26 ?  288 PHE B C     1 
ATOM   7858  O  O     . PHE B 1 288 ? 102.848 136.287 147.862 1.00 36.76 ?  288 PHE B O     1 
ATOM   7859  C  CB    . PHE B 1 288 ? 105.386 137.811 146.407 1.00 26.32 ?  288 PHE B CB    1 
ATOM   7860  C  CG    . PHE B 1 288 ? 105.585 136.402 145.935 1.00 26.81 ?  288 PHE B CG    1 
ATOM   7861  C  CD1   . PHE B 1 288 ? 105.885 135.394 146.835 1.00 23.51 ?  288 PHE B CD1   1 
ATOM   7862  C  CD2   . PHE B 1 288 ? 105.467 136.084 144.595 1.00 24.59 ?  288 PHE B CD2   1 
ATOM   7863  C  CE1   . PHE B 1 288 ? 106.066 134.099 146.406 1.00 23.18 ?  288 PHE B CE1   1 
ATOM   7864  C  CE2   . PHE B 1 288 ? 105.650 134.790 144.161 1.00 30.28 ?  288 PHE B CE2   1 
ATOM   7865  C  CZ    . PHE B 1 288 ? 105.949 133.797 145.068 1.00 29.49 ?  288 PHE B CZ    1 
ATOM   7866  N  N     . VAL B 1 289 ? 103.903 137.756 149.201 1.00 33.44 ?  289 VAL B N     1 
ATOM   7867  C  CA    . VAL B 1 289 ? 103.519 137.039 150.409 1.00 30.03 ?  289 VAL B CA    1 
ATOM   7868  C  C     . VAL B 1 289 ? 102.013 137.113 150.614 1.00 32.62 ?  289 VAL B C     1 
ATOM   7869  O  O     . VAL B 1 289 ? 101.388 136.154 151.079 1.00 35.56 ?  289 VAL B O     1 
ATOM   7870  C  CB    . VAL B 1 289 ? 104.291 137.589 151.623 1.00 32.52 ?  289 VAL B CB    1 
ATOM   7871  C  CG1   . VAL B 1 289 ? 103.901 136.843 152.887 1.00 31.58 ?  289 VAL B CG1   1 
ATOM   7872  C  CG2   . VAL B 1 289 ? 105.787 137.490 151.383 1.00 25.79 ?  289 VAL B CG2   1 
ATOM   7873  N  N     . GLU B 1 290 ? 101.403 138.248 150.268 1.00 36.62 ?  290 GLU B N     1 
ATOM   7874  C  CA    . GLU B 1 290 ? 99.954  138.370 150.367 1.00 33.24 ?  290 GLU B CA    1 
ATOM   7875  C  C     . GLU B 1 290 ? 99.250  137.449 149.378 1.00 37.81 ?  290 GLU B C     1 
ATOM   7876  O  O     . GLU B 1 290 ? 98.229  136.836 149.712 1.00 45.39 ?  290 GLU B O     1 
ATOM   7877  C  CB    . GLU B 1 290 ? 99.538  139.824 150.143 1.00 36.09 ?  290 GLU B CB    1 
ATOM   7878  C  CG    . GLU B 1 290 ? 98.040  140.060 150.184 1.00 39.32 ?  290 GLU B CG    1 
ATOM   7879  C  CD    . GLU B 1 290 ? 97.683  141.532 150.132 1.00 48.27 ?  290 GLU B CD    1 
ATOM   7880  O  OE1   . GLU B 1 290 ? 98.113  142.215 149.179 1.00 46.35 ?  290 GLU B OE1   1 
ATOM   7881  O  OE2   . GLU B 1 290 ? 96.969  142.005 151.041 1.00 49.09 -1 290 GLU B OE2   1 
ATOM   7882  N  N     . LEU B 1 291 ? 99.775  137.343 148.156 1.00 30.84 ?  291 LEU B N     1 
ATOM   7883  C  CA    . LEU B 1 291 ? 99.177  136.455 147.164 1.00 27.61 ?  291 LEU B CA    1 
ATOM   7884  C  C     . LEU B 1 291 ? 99.316  134.995 147.571 1.00 34.77 ?  291 LEU B C     1 
ATOM   7885  O  O     . LEU B 1 291 ? 98.381  134.205 147.400 1.00 38.54 ?  291 LEU B O     1 
ATOM   7886  C  CB    . LEU B 1 291 ? 99.811  136.689 145.793 1.00 32.42 ?  291 LEU B CB    1 
ATOM   7887  C  CG    . LEU B 1 291 ? 99.551  138.045 145.137 1.00 33.84 ?  291 LEU B CG    1 
ATOM   7888  C  CD1   . LEU B 1 291 ? 100.534 138.278 144.007 1.00 26.96 ?  291 LEU B CD1   1 
ATOM   7889  C  CD2   . LEU B 1 291 ? 98.121  138.138 144.640 1.00 31.97 ?  291 LEU B CD2   1 
ATOM   7890  N  N     . ALA B 1 292 ? 100.480 134.613 148.103 1.00 41.06 ?  292 ALA B N     1 
ATOM   7891  C  CA    . ALA B 1 292 ? 100.673 133.241 148.557 1.00 31.29 ?  292 ALA B CA    1 
ATOM   7892  C  C     . ALA B 1 292 ? 99.831  132.932 149.787 1.00 31.33 ?  292 ALA B C     1 
ATOM   7893  O  O     . ALA B 1 292 ? 99.362  131.800 149.949 1.00 38.52 ?  292 ALA B O     1 
ATOM   7894  C  CB    . ALA B 1 292 ? 102.151 132.986 148.849 1.00 27.35 ?  292 ALA B CB    1 
ATOM   7895  N  N     . ARG B 1 293 ? 99.634  133.919 150.663 1.00 36.05 ?  293 ARG B N     1 
ATOM   7896  C  CA    . ARG B 1 293 ? 98.839  133.709 151.867 1.00 36.19 ?  293 ARG B CA    1 
ATOM   7897  C  C     . ARG B 1 293 ? 97.396  133.365 151.525 1.00 41.29 ?  293 ARG B C     1 
ATOM   7898  O  O     . ARG B 1 293 ? 96.799  132.472 152.137 1.00 47.95 ?  293 ARG B O     1 
ATOM   7899  C  CB    . ARG B 1 293 ? 98.905  134.957 152.747 1.00 37.33 ?  293 ARG B CB    1 
ATOM   7900  C  CG    . ARG B 1 293 ? 97.953  134.970 153.923 1.00 37.72 ?  293 ARG B CG    1 
ATOM   7901  C  CD    . ARG B 1 293 ? 97.933  136.344 154.562 1.00 38.99 ?  293 ARG B CD    1 
ATOM   7902  N  NE    . ARG B 1 293 ? 99.282  136.870 154.731 1.00 45.33 ?  293 ARG B NE    1 
ATOM   7903  C  CZ    . ARG B 1 293 ? 99.665  138.086 154.363 1.00 43.13 ?  293 ARG B CZ    1 
ATOM   7904  N  NH1   . ARG B 1 293 ? 98.820  138.940 153.811 1.00 42.09 1  293 ARG B NH1   1 
ATOM   7905  N  NH2   . ARG B 1 293 ? 100.929 138.452 154.555 1.00 40.00 ?  293 ARG B NH2   1 
ATOM   7906  N  N     . GLU B 1 294 ? 96.822  134.059 150.548 1.00 48.58 ?  294 GLU B N     1 
ATOM   7907  C  CA    . GLU B 1 294 ? 95.447  133.829 150.129 1.00 47.69 ?  294 GLU B CA    1 
ATOM   7908  C  C     . GLU B 1 294 ? 95.334  132.802 149.011 1.00 45.66 ?  294 GLU B C     1 
ATOM   7909  O  O     . GLU B 1 294 ? 94.226  132.564 148.521 1.00 48.04 ?  294 GLU B O     1 
ATOM   7910  C  CB    . GLU B 1 294 ? 94.808  135.147 149.689 1.00 44.43 ?  294 GLU B CB    1 
ATOM   7911  C  CG    . GLU B 1 294 ? 94.721  136.187 150.791 1.00 48.49 ?  294 GLU B CG    1 
ATOM   7912  C  CD    . GLU B 1 294 ? 94.792  137.602 150.258 1.00 55.04 ?  294 GLU B CD    1 
ATOM   7913  O  OE1   . GLU B 1 294 ? 94.942  137.765 149.029 1.00 56.38 ?  294 GLU B OE1   1 
ATOM   7914  O  OE2   . GLU B 1 294 ? 94.702  138.550 151.067 1.00 54.30 -1 294 GLU B OE2   1 
ATOM   7915  N  N     . ASP B 1 295 ? 96.451  132.204 148.594 1.00 44.07 ?  295 ASP B N     1 
ATOM   7916  C  CA    . ASP B 1 295 ? 96.497  131.162 147.570 1.00 43.93 ?  295 ASP B CA    1 
ATOM   7917  C  C     . ASP B 1 295 ? 95.985  131.643 146.216 1.00 49.15 ?  295 ASP B C     1 
ATOM   7918  O  O     . ASP B 1 295 ? 95.667  130.826 145.346 1.00 47.46 ?  295 ASP B O     1 
ATOM   7919  C  CB    . ASP B 1 295 ? 95.726  129.910 148.007 1.00 45.64 ?  295 ASP B CB    1 
ATOM   7920  C  CG    . ASP B 1 295 ? 96.447  128.625 147.644 1.00 52.77 ?  295 ASP B CG    1 
ATOM   7921  O  OD1   . ASP B 1 295 ? 97.352  128.672 146.786 1.00 54.24 ?  295 ASP B OD1   1 
ATOM   7922  O  OD2   . ASP B 1 295 ? 96.105  127.568 148.212 1.00 50.23 -1 295 ASP B OD2   1 
ATOM   7923  N  N     . LYS B 1 296 ? 95.895  132.955 146.016 1.00 49.66 ?  296 LYS B N     1 
ATOM   7924  C  CA    . LYS B 1 296 ? 95.542  133.481 144.705 1.00 47.19 ?  296 LYS B CA    1 
ATOM   7925  C  C     . LYS B 1 296 ? 96.681  133.242 143.725 1.00 45.50 ?  296 LYS B C     1 
ATOM   7926  O  O     . LYS B 1 296 ? 97.856  133.385 144.071 1.00 51.87 ?  296 LYS B O     1 
ATOM   7927  C  CB    . LYS B 1 296 ? 95.234  134.976 144.790 1.00 46.04 ?  296 LYS B CB    1 
ATOM   7928  C  CG    . LYS B 1 296 ? 94.708  135.431 146.136 1.00 47.76 ?  296 LYS B CG    1 
ATOM   7929  C  CD    . LYS B 1 296 ? 93.716  136.570 145.987 1.00 49.04 ?  296 LYS B CD    1 
ATOM   7930  C  CE    . LYS B 1 296 ? 92.325  136.052 145.660 1.00 51.74 ?  296 LYS B CE    1 
ATOM   7931  N  NZ    . LYS B 1 296 ? 91.783  135.188 146.745 1.00 50.32 1  296 LYS B NZ    1 
ATOM   7932  N  N     . ALA B 1 297 ? 96.332  132.874 142.497 1.00 45.38 ?  297 ALA B N     1 
ATOM   7933  C  CA    . ALA B 1 297 ? 97.345  132.660 141.474 1.00 46.15 ?  297 ALA B CA    1 
ATOM   7934  C  C     . ALA B 1 297 ? 97.988  133.988 141.096 1.00 45.62 ?  297 ALA B C     1 
ATOM   7935  O  O     . ALA B 1 297 ? 97.293  134.964 140.795 1.00 53.38 ?  297 ALA B O     1 
ATOM   7936  C  CB    . ALA B 1 297 ? 96.729  131.992 140.248 1.00 44.20 ?  297 ALA B CB    1 
ATOM   7937  N  N     . ALA B 1 298 ? 99.315  134.025 141.112 1.00 38.81 ?  298 ALA B N     1 
ATOM   7938  C  CA    . ALA B 1 298 ? 100.068 135.253 140.915 1.00 39.74 ?  298 ALA B CA    1 
ATOM   7939  C  C     . ALA B 1 298 ? 100.583 135.352 139.485 1.00 37.91 ?  298 ALA B C     1 
ATOM   7940  O  O     . ALA B 1 298 ? 100.533 134.400 138.705 1.00 41.21 ?  298 ALA B O     1 
ATOM   7941  C  CB    . ALA B 1 298 ? 101.233 135.331 141.907 1.00 42.58 ?  298 ALA B CB    1 
ATOM   7942  N  N     . TYR B 1 299 ? 101.089 136.535 139.151 1.00 38.47 ?  299 TYR B N     1 
ATOM   7943  C  CA    . TYR B 1 299 ? 101.611 136.833 137.825 1.00 31.67 ?  299 TYR B CA    1 
ATOM   7944  C  C     . TYR B 1 299 ? 103.040 137.339 137.941 1.00 33.77 ?  299 TYR B C     1 
ATOM   7945  O  O     . TYR B 1 299 ? 103.329 138.209 138.768 1.00 41.45 ?  299 TYR B O     1 
ATOM   7946  C  CB    . TYR B 1 299 ? 100.749 137.882 137.120 1.00 32.93 ?  299 TYR B CB    1 
ATOM   7947  C  CG    . TYR B 1 299 ? 99.467  137.343 136.531 1.00 35.07 ?  299 TYR B CG    1 
ATOM   7948  C  CD1   . TYR B 1 299 ? 99.488  136.519 135.416 1.00 37.58 ?  299 TYR B CD1   1 
ATOM   7949  C  CD2   . TYR B 1 299 ? 98.238  137.665 137.088 1.00 36.23 ?  299 TYR B CD2   1 
ATOM   7950  C  CE1   . TYR B 1 299 ? 98.320  136.029 134.874 1.00 41.02 ?  299 TYR B CE1   1 
ATOM   7951  C  CE2   . TYR B 1 299 ? 97.066  137.178 136.553 1.00 39.48 ?  299 TYR B CE2   1 
ATOM   7952  C  CZ    . TYR B 1 299 ? 97.111  136.361 135.446 1.00 44.62 ?  299 TYR B CZ    1 
ATOM   7953  O  OH    . TYR B 1 299 ? 95.942  135.875 134.908 1.00 45.44 ?  299 TYR B OH    1 
ATOM   7954  N  N     . VAL B 1 300 ? 103.927 136.793 137.117 1.00 32.57 ?  300 VAL B N     1 
ATOM   7955  C  CA    . VAL B 1 300 ? 105.259 137.349 136.917 1.00 28.85 ?  300 VAL B CA    1 
ATOM   7956  C  C     . VAL B 1 300 ? 105.241 138.119 135.608 1.00 27.75 ?  300 VAL B C     1 
ATOM   7957  O  O     . VAL B 1 300 ? 104.595 137.702 134.640 1.00 32.37 ?  300 VAL B O     1 
ATOM   7958  C  CB    . VAL B 1 300 ? 106.342 136.254 136.914 1.00 24.24 ?  300 VAL B CB    1 
ATOM   7959  C  CG1   . VAL B 1 300 ? 106.608 135.776 138.329 1.00 26.78 ?  300 VAL B CG1   1 
ATOM   7960  C  CG2   . VAL B 1 300 ? 105.930 135.098 136.022 1.00 31.98 ?  300 VAL B CG2   1 
ATOM   7961  N  N     . PHE B 1 301 ? 105.939 139.247 135.572 1.00 30.11 ?  301 PHE B N     1 
ATOM   7962  C  CA    . PHE B 1 301 ? 105.796 140.205 134.489 1.00 23.39 ?  301 PHE B CA    1 
ATOM   7963  C  C     . PHE B 1 301 ? 107.081 140.316 133.686 1.00 31.95 ?  301 PHE B C     1 
ATOM   7964  O  O     . PHE B 1 301 ? 108.183 140.152 134.215 1.00 33.95 ?  301 PHE B O     1 
ATOM   7965  C  CB    . PHE B 1 301 ? 105.407 141.581 135.030 1.00 24.46 ?  301 PHE B CB    1 
ATOM   7966  C  CG    . PHE B 1 301 ? 104.238 141.550 135.966 1.00 31.13 ?  301 PHE B CG    1 
ATOM   7967  C  CD1   . PHE B 1 301 ? 102.944 141.572 135.479 1.00 28.85 ?  301 PHE B CD1   1 
ATOM   7968  C  CD2   . PHE B 1 301 ? 104.434 141.484 137.334 1.00 27.61 ?  301 PHE B CD2   1 
ATOM   7969  C  CE1   . PHE B 1 301 ? 101.868 141.536 136.338 1.00 30.97 ?  301 PHE B CE1   1 
ATOM   7970  C  CE2   . PHE B 1 301 ? 103.361 141.448 138.196 1.00 28.61 ?  301 PHE B CE2   1 
ATOM   7971  C  CZ    . PHE B 1 301 ? 102.076 141.476 137.697 1.00 33.66 ?  301 PHE B CZ    1 
ATOM   7972  N  N     . TYR B 1 302 ? 106.922 140.591 132.396 1.00 31.27 ?  302 TYR B N     1 
ATOM   7973  C  CA    . TYR B 1 302 ? 108.059 140.903 131.546 1.00 28.12 ?  302 TYR B CA    1 
ATOM   7974  C  C     . TYR B 1 302 ? 108.461 142.354 131.780 1.00 29.09 ?  302 TYR B C     1 
ATOM   7975  O  O     . TYR B 1 302 ? 107.660 143.256 131.512 1.00 32.21 ?  302 TYR B O     1 
ATOM   7976  C  CB    . TYR B 1 302 ? 107.714 140.678 130.080 1.00 29.30 ?  302 TYR B CB    1 
ATOM   7977  C  CG    . TYR B 1 302 ? 107.509 139.226 129.702 1.00 31.34 ?  302 TYR B CG    1 
ATOM   7978  C  CD1   . TYR B 1 302 ? 106.347 138.554 130.054 1.00 30.03 ?  302 TYR B CD1   1 
ATOM   7979  C  CD2   . TYR B 1 302 ? 108.475 138.530 128.991 1.00 29.42 ?  302 TYR B CD2   1 
ATOM   7980  C  CE1   . TYR B 1 302 ? 106.154 137.233 129.709 1.00 30.43 ?  302 TYR B CE1   1 
ATOM   7981  C  CE2   . TYR B 1 302 ? 108.291 137.208 128.644 1.00 31.36 ?  302 TYR B CE2   1 
ATOM   7982  C  CZ    . TYR B 1 302 ? 107.129 136.565 129.005 1.00 34.48 ?  302 TYR B CZ    1 
ATOM   7983  O  OH    . TYR B 1 302 ? 106.939 135.246 128.662 1.00 34.45 ?  302 TYR B OH    1 
ATOM   7984  N  N     . PRO B 1 303 ? 109.664 142.621 132.291 1.00 26.70 ?  303 PRO B N     1 
ATOM   7985  C  CA    . PRO B 1 303 ? 110.004 143.998 132.686 1.00 30.11 ?  303 PRO B CA    1 
ATOM   7986  C  C     . PRO B 1 303 ? 109.986 145.002 131.548 1.00 28.10 ?  303 PRO B C     1 
ATOM   7987  O  O     . PRO B 1 303 ? 109.648 146.171 131.778 1.00 33.19 ?  303 PRO B O     1 
ATOM   7988  C  CB    . PRO B 1 303 ? 111.412 143.848 133.278 1.00 29.93 ?  303 PRO B CB    1 
ATOM   7989  C  CG    . PRO B 1 303 ? 111.485 142.433 133.705 1.00 27.96 ?  303 PRO B CG    1 
ATOM   7990  C  CD    . PRO B 1 303 ? 110.707 141.663 132.687 1.00 23.22 ?  303 PRO B CD    1 
ATOM   7991  N  N     . HIS B 1 304 ? 110.346 144.596 130.330 1.00 29.44 ?  304 HIS B N     1 
ATOM   7992  C  CA    . HIS B 1 304 ? 110.417 145.565 129.242 1.00 27.98 ?  304 HIS B CA    1 
ATOM   7993  C  C     . HIS B 1 304 ? 109.037 146.054 128.830 1.00 34.11 ?  304 HIS B C     1 
ATOM   7994  O  O     . HIS B 1 304 ? 108.889 147.213 128.437 1.00 41.97 ?  304 HIS B O     1 
ATOM   7995  C  CB    . HIS B 1 304 ? 111.151 144.976 128.040 1.00 29.58 ?  304 HIS B CB    1 
ATOM   7996  C  CG    . HIS B 1 304 ? 111.520 145.997 127.010 1.00 33.21 ?  304 HIS B CG    1 
ATOM   7997  N  ND1   . HIS B 1 304 ? 112.143 147.183 127.331 1.00 33.55 ?  304 HIS B ND1   1 
ATOM   7998  C  CD2   . HIS B 1 304 ? 111.345 146.015 125.668 1.00 34.93 ?  304 HIS B CD2   1 
ATOM   7999  C  CE1   . HIS B 1 304 ? 112.342 147.886 126.231 1.00 32.26 ?  304 HIS B CE1   1 
ATOM   8000  N  NE2   . HIS B 1 304 ? 111.866 147.200 125.208 1.00 34.44 ?  304 HIS B NE2   1 
ATOM   8001  N  N     . THR B 1 305 ? 108.018 145.196 128.914 1.00 33.07 ?  305 THR B N     1 
ATOM   8002  C  CA    . THR B 1 305 ? 106.658 145.649 128.642 1.00 32.53 ?  305 THR B CA    1 
ATOM   8003  C  C     . THR B 1 305 ? 106.225 146.709 129.645 1.00 29.67 ?  305 THR B C     1 
ATOM   8004  O  O     . THR B 1 305 ? 105.607 147.713 129.273 1.00 35.87 ?  305 THR B O     1 
ATOM   8005  C  CB    . THR B 1 305 ? 105.695 144.464 128.661 1.00 31.15 ?  305 THR B CB    1 
ATOM   8006  O  OG1   . THR B 1 305 ? 105.571 143.969 129.999 1.00 29.56 ?  305 THR B OG1   1 
ATOM   8007  C  CG2   . THR B 1 305 ? 106.210 143.355 127.763 1.00 31.52 ?  305 THR B CG2   1 
ATOM   8008  N  N     . ILE B 1 306 ? 106.552 146.508 130.923 1.00 35.97 ?  306 ILE B N     1 
ATOM   8009  C  CA    . ILE B 1 306 ? 106.224 147.495 131.945 1.00 29.61 ?  306 ILE B CA    1 
ATOM   8010  C  C     . ILE B 1 306 ? 106.979 148.794 131.696 1.00 28.38 ?  306 ILE B C     1 
ATOM   8011  O  O     . ILE B 1 306 ? 106.418 149.889 131.827 1.00 35.85 ?  306 ILE B O     1 
ATOM   8012  C  CB    . ILE B 1 306 ? 106.518 146.922 133.343 1.00 27.13 ?  306 ILE B CB    1 
ATOM   8013  C  CG1   . ILE B 1 306 ? 105.448 145.902 133.728 1.00 27.32 ?  306 ILE B CG1   1 
ATOM   8014  C  CG2   . ILE B 1 306 ? 106.601 148.033 134.379 1.00 30.70 ?  306 ILE B CG2   1 
ATOM   8015  C  CD1   . ILE B 1 306 ? 105.732 145.179 135.008 1.00 29.91 ?  306 ILE B CD1   1 
ATOM   8016  N  N     . TYR B 1 307 ? 108.258 148.695 131.332 1.00 30.49 ?  307 TYR B N     1 
ATOM   8017  C  CA    . TYR B 1 307 ? 109.042 149.893 131.051 1.00 31.96 ?  307 TYR B CA    1 
ATOM   8018  C  C     . TYR B 1 307 ? 108.481 150.656 129.858 1.00 35.66 ?  307 TYR B C     1 
ATOM   8019  O  O     . TYR B 1 307 ? 108.442 151.891 129.864 1.00 39.51 ?  307 TYR B O     1 
ATOM   8020  C  CB    . TYR B 1 307 ? 110.504 149.518 130.809 1.00 26.23 ?  307 TYR B CB    1 
ATOM   8021  C  CG    . TYR B 1 307 ? 111.401 150.708 130.581 1.00 35.96 ?  307 TYR B CG    1 
ATOM   8022  C  CD1   . TYR B 1 307 ? 111.843 151.479 131.647 1.00 31.13 ?  307 TYR B CD1   1 
ATOM   8023  C  CD2   . TYR B 1 307 ? 111.801 151.066 129.302 1.00 37.14 ?  307 TYR B CD2   1 
ATOM   8024  C  CE1   . TYR B 1 307 ? 112.662 152.570 131.444 1.00 31.45 ?  307 TYR B CE1   1 
ATOM   8025  C  CE2   . TYR B 1 307 ? 112.618 152.155 129.090 1.00 36.70 ?  307 TYR B CE2   1 
ATOM   8026  C  CZ    . TYR B 1 307 ? 113.046 152.904 130.164 1.00 37.64 ?  307 TYR B CZ    1 
ATOM   8027  O  OH    . TYR B 1 307 ? 113.862 153.990 129.956 1.00 40.14 ?  307 TYR B OH    1 
ATOM   8028  N  N     . LYS B 1 308 ? 108.055 149.937 128.819 1.00 39.05 ?  308 LYS B N     1 
ATOM   8029  C  CA    . LYS B 1 308 ? 107.476 150.590 127.651 1.00 32.40 ?  308 LYS B CA    1 
ATOM   8030  C  C     . LYS B 1 308 ? 106.132 151.228 127.979 1.00 28.74 ?  308 LYS B C     1 
ATOM   8031  O  O     . LYS B 1 308 ? 105.813 152.311 127.474 1.00 37.26 ?  308 LYS B O     1 
ATOM   8032  C  CB    . LYS B 1 308 ? 107.324 149.581 126.514 1.00 32.55 ?  308 LYS B CB    1 
ATOM   8033  C  CG    . LYS B 1 308 ? 108.537 149.478 125.607 1.00 33.55 ?  308 LYS B CG    1 
ATOM   8034  C  CD    . LYS B 1 308 ? 108.612 148.123 124.915 1.00 37.52 ?  308 LYS B CD    1 
ATOM   8035  C  CE    . LYS B 1 308 ? 107.238 147.492 124.748 1.00 38.18 ?  308 LYS B CE    1 
ATOM   8036  N  NZ    . LYS B 1 308 ? 107.310 146.008 124.658 1.00 39.44 1  308 LYS B NZ    1 
ATOM   8037  N  N     . GLU B 1 309 ? 105.332 150.573 128.821 1.00 30.88 ?  309 GLU B N     1 
ATOM   8038  C  CA    . GLU B 1 309 ? 104.000 151.087 129.118 1.00 35.01 ?  309 GLU B CA    1 
ATOM   8039  C  C     . GLU B 1 309 ? 104.050 152.290 130.051 1.00 39.29 ?  309 GLU B C     1 
ATOM   8040  O  O     . GLU B 1 309 ? 103.296 153.252 129.870 1.00 42.53 ?  309 GLU B O     1 
ATOM   8041  C  CB    . GLU B 1 309 ? 103.138 149.976 129.718 1.00 31.66 ?  309 GLU B CB    1 
ATOM   8042  C  CG    . GLU B 1 309 ? 101.756 150.426 130.158 1.00 37.92 ?  309 GLU B CG    1 
ATOM   8043  C  CD    . GLU B 1 309 ? 100.875 150.845 128.999 1.00 44.26 ?  309 GLU B CD    1 
ATOM   8044  O  OE1   . GLU B 1 309 ? 101.217 150.532 127.839 1.00 44.90 ?  309 GLU B OE1   1 
ATOM   8045  O  OE2   . GLU B 1 309 ? 99.837  151.493 129.249 1.00 42.88 -1 309 GLU B OE2   1 
ATOM   8046  N  N     . TYR B 1 310 ? 104.926 152.259 131.055 1.00 38.41 ?  310 TYR B N     1 
ATOM   8047  C  CA    . TYR B 1 310 ? 104.921 153.269 132.103 1.00 32.71 ?  310 TYR B CA    1 
ATOM   8048  C  C     . TYR B 1 310 ? 106.144 154.173 132.102 1.00 31.48 ?  310 TYR B C     1 
ATOM   8049  O  O     . TYR B 1 310 ? 106.157 155.161 132.843 1.00 37.24 ?  310 TYR B O     1 
ATOM   8050  C  CB    . TYR B 1 310 ? 104.794 152.598 133.478 1.00 34.92 ?  310 TYR B CB    1 
ATOM   8051  C  CG    . TYR B 1 310 ? 103.550 151.755 133.623 1.00 35.19 ?  310 TYR B CG    1 
ATOM   8052  C  CD1   . TYR B 1 310 ? 102.331 152.333 133.950 1.00 31.87 ?  310 TYR B CD1   1 
ATOM   8053  C  CD2   . TYR B 1 310 ? 103.588 150.384 133.417 1.00 30.33 ?  310 TYR B CD2   1 
ATOM   8054  C  CE1   . TYR B 1 310 ? 101.192 151.569 134.077 1.00 34.98 ?  310 TYR B CE1   1 
ATOM   8055  C  CE2   . TYR B 1 310 ? 102.453 149.613 133.539 1.00 31.20 ?  310 TYR B CE2   1 
ATOM   8056  C  CZ    . TYR B 1 310 ? 101.258 150.210 133.871 1.00 35.71 ?  310 TYR B CZ    1 
ATOM   8057  O  OH    . TYR B 1 310 ? 100.123 149.445 133.995 1.00 36.16 ?  310 TYR B OH    1 
ATOM   8058  N  N     . GLY B 1 311 ? 107.164 153.871 131.304 1.00 27.99 ?  311 GLY B N     1 
ATOM   8059  C  CA    . GLY B 1 311 ? 108.379 154.654 131.325 1.00 30.48 ?  311 GLY B CA    1 
ATOM   8060  C  C     . GLY B 1 311 ? 109.247 154.443 132.543 1.00 31.62 ?  311 GLY B C     1 
ATOM   8061  O  O     . GLY B 1 311 ? 110.270 155.124 132.678 1.00 40.98 ?  311 GLY B O     1 
ATOM   8062  N  N     . GLN B 1 312 ? 108.875 153.526 133.431 1.00 31.69 ?  312 GLN B N     1 
ATOM   8063  C  CA    . GLN B 1 312 ? 109.639 153.223 134.628 1.00 30.03 ?  312 GLN B CA    1 
ATOM   8064  C  C     . GLN B 1 312 ? 109.888 151.727 134.692 1.00 31.15 ?  312 GLN B C     1 
ATOM   8065  O  O     . GLN B 1 312 ? 109.077 150.927 134.217 1.00 39.00 ?  312 GLN B O     1 
ATOM   8066  C  CB    . GLN B 1 312 ? 108.908 153.678 135.896 1.00 34.29 ?  312 GLN B CB    1 
ATOM   8067  C  CG    . GLN B 1 312 ? 108.518 155.142 135.901 1.00 37.13 ?  312 GLN B CG    1 
ATOM   8068  C  CD    . GLN B 1 312 ? 107.461 155.452 136.940 1.00 39.55 ?  312 GLN B CD    1 
ATOM   8069  O  OE1   . GLN B 1 312 ? 106.281 155.584 136.619 1.00 38.28 ?  312 GLN B OE1   1 
ATOM   8070  N  NE2   . GLN B 1 312 ? 107.881 155.570 138.192 1.00 37.71 ?  312 GLN B NE2   1 
ATOM   8071  N  N     . HIS B 1 313 ? 111.019 151.354 135.281 1.00 28.09 ?  313 HIS B N     1 
ATOM   8072  C  CA    . HIS B 1 313 ? 111.333 149.947 135.464 1.00 28.27 ?  313 HIS B CA    1 
ATOM   8073  C  C     . HIS B 1 313 ? 110.369 149.311 136.459 1.00 32.03 ?  313 HIS B C     1 
ATOM   8074  O  O     . HIS B 1 313 ? 109.849 149.970 137.361 1.00 34.17 ?  313 HIS B O     1 
ATOM   8075  C  CB    . HIS B 1 313 ? 112.773 149.779 135.945 1.00 26.18 ?  313 HIS B CB    1 
ATOM   8076  C  CG    . HIS B 1 313 ? 113.797 150.150 134.921 1.00 27.23 ?  313 HIS B CG    1 
ATOM   8077  N  ND1   . HIS B 1 313 ? 114.052 149.375 133.809 1.00 30.43 ?  313 HIS B ND1   1 
ATOM   8078  C  CD2   . HIS B 1 313 ? 114.634 151.210 134.839 1.00 28.25 ?  313 HIS B CD2   1 
ATOM   8079  C  CE1   . HIS B 1 313 ? 115.001 149.944 133.088 1.00 27.83 ?  313 HIS B CE1   1 
ATOM   8080  N  NE2   . HIS B 1 313 ? 115.371 151.058 133.691 1.00 32.42 ?  313 HIS B NE2   1 
ATOM   8081  N  N     . MET B 1 314 ? 110.131 148.012 136.278 1.00 34.99 ?  314 MET B N     1 
ATOM   8082  C  CA    . MET B 1 314 ? 109.197 147.305 137.148 1.00 29.03 ?  314 MET B CA    1 
ATOM   8083  C  C     . MET B 1 314 ? 109.690 147.295 138.590 1.00 34.23 ?  314 MET B C     1 
ATOM   8084  O  O     . MET B 1 314 ? 108.894 147.435 139.526 1.00 38.94 ?  314 MET B O     1 
ATOM   8085  C  CB    . MET B 1 314 ? 108.980 145.882 136.632 1.00 26.60 ?  314 MET B CB    1 
ATOM   8086  C  CG    . MET B 1 314 ? 108.407 144.916 137.651 1.00 27.15 ?  314 MET B CG    1 
ATOM   8087  S  SD    . MET B 1 314 ? 108.737 143.198 137.223 1.00 43.44 ?  314 MET B SD    1 
ATOM   8088  C  CE    . MET B 1 314 ? 110.387 142.994 137.887 1.00 34.29 ?  314 MET B CE    1 
ATOM   8089  N  N     . ASP B 1 315 ? 110.998 147.140 138.791 1.00 34.31 ?  315 ASP B N     1 
ATOM   8090  C  CA    . ASP B 1 315 ? 111.556 147.163 140.136 1.00 34.44 ?  315 ASP B CA    1 
ATOM   8091  C  C     . ASP B 1 315 ? 111.712 148.571 140.700 1.00 28.83 ?  315 ASP B C     1 
ATOM   8092  O  O     . ASP B 1 315 ? 112.024 148.715 141.886 1.00 38.87 ?  315 ASP B O     1 
ATOM   8093  C  CB    . ASP B 1 315 ? 112.887 146.385 140.163 1.00 29.64 ?  315 ASP B CB    1 
ATOM   8094  C  CG    . ASP B 1 315 ? 114.093 147.195 139.678 1.00 33.54 ?  315 ASP B CG    1 
ATOM   8095  O  OD1   . ASP B 1 315 ? 113.968 148.365 139.262 1.00 40.00 ?  315 ASP B OD1   1 
ATOM   8096  O  OD2   . ASP B 1 315 ? 115.208 146.635 139.724 1.00 35.00 -1 315 ASP B OD2   1 
ATOM   8097  N  N     . GLU B 1 316 ? 111.499 149.604 139.886 1.00 24.99 ?  316 GLU B N     1 
ATOM   8098  C  CA    . GLU B 1 316 ? 111.481 150.979 140.365 1.00 27.13 ?  316 GLU B CA    1 
ATOM   8099  C  C     . GLU B 1 316 ? 110.120 151.401 140.900 1.00 35.65 ?  316 GLU B C     1 
ATOM   8100  O  O     . GLU B 1 316 ? 110.003 152.505 141.440 1.00 35.99 ?  316 GLU B O     1 
ATOM   8101  C  CB    . GLU B 1 316 ? 111.899 151.931 139.244 1.00 31.43 ?  316 GLU B CB    1 
ATOM   8102  C  CG    . GLU B 1 316 ? 112.854 153.023 139.679 1.00 34.63 ?  316 GLU B CG    1 
ATOM   8103  C  CD    . GLU B 1 316 ? 114.231 152.495 140.000 1.00 39.24 ?  316 GLU B CD    1 
ATOM   8104  O  OE1   . GLU B 1 316 ? 114.656 151.518 139.351 1.00 40.91 ?  316 GLU B OE1   1 
ATOM   8105  O  OE2   . GLU B 1 316 ? 114.889 153.057 140.900 1.00 38.33 -1 316 GLU B OE2   1 
ATOM   8106  N  N     . MET B 1 317 ? 109.102 150.559 140.766 1.00 38.87 ?  317 MET B N     1 
ATOM   8107  C  CA    . MET B 1 317 ? 107.741 150.892 141.151 1.00 34.88 ?  317 MET B CA    1 
ATOM   8108  C  C     . MET B 1 317 ? 107.291 150.033 142.326 1.00 38.69 ?  317 MET B C     1 
ATOM   8109  O  O     . MET B 1 317 ? 107.818 148.946 142.573 1.00 39.26 ?  317 MET B O     1 
ATOM   8110  C  CB    . MET B 1 317 ? 106.783 150.710 139.970 1.00 35.43 ?  317 MET B CB    1 
ATOM   8111  C  CG    . MET B 1 317 ? 107.258 151.377 138.691 1.00 37.07 ?  317 MET B CG    1 
ATOM   8112  S  SD    . MET B 1 317 ? 106.604 150.597 137.208 1.00 48.33 ?  317 MET B SD    1 
ATOM   8113  C  CE    . MET B 1 317 ? 105.136 151.584 136.945 1.00 39.01 ?  317 MET B CE    1 
ATOM   8114  N  N     . ASP B 1 318 ? 106.298 150.543 143.050 1.00 40.07 ?  318 ASP B N     1 
ATOM   8115  C  CA    . ASP B 1 318 ? 105.758 149.856 144.217 1.00 37.58 ?  318 ASP B CA    1 
ATOM   8116  C  C     . ASP B 1 318 ? 104.798 148.771 143.747 1.00 42.08 ?  318 ASP B C     1 
ATOM   8117  O  O     . ASP B 1 318 ? 103.718 149.071 143.231 1.00 44.38 ?  318 ASP B O     1 
ATOM   8118  C  CB    . ASP B 1 318 ? 105.059 150.849 145.141 1.00 39.27 ?  318 ASP B CB    1 
ATOM   8119  C  CG    . ASP B 1 318 ? 104.630 150.223 146.452 1.00 49.10 ?  318 ASP B CG    1 
ATOM   8120  O  OD1   . ASP B 1 318 ? 105.336 149.316 146.940 1.00 46.36 ?  318 ASP B OD1   1 
ATOM   8121  O  OD2   . ASP B 1 318 ? 103.586 150.640 146.995 1.00 50.01 -1 318 ASP B OD2   1 
ATOM   8122  N  N     . MET B 1 319 ? 105.188 147.508 143.930 1.00 40.62 ?  319 MET B N     1 
ATOM   8123  C  CA    . MET B 1 319 ? 104.356 146.404 143.465 1.00 35.55 ?  319 MET B CA    1 
ATOM   8124  C  C     . MET B 1 319 ? 103.032 146.331 144.213 1.00 36.85 ?  319 MET B C     1 
ATOM   8125  O  O     . MET B 1 319 ? 102.046 145.829 143.666 1.00 42.15 ?  319 MET B O     1 
ATOM   8126  C  CB    . MET B 1 319 ? 105.108 145.082 143.599 1.00 35.05 ?  319 MET B CB    1 
ATOM   8127  C  CG    . MET B 1 319 ? 104.551 143.971 142.728 1.00 37.88 ?  319 MET B CG    1 
ATOM   8128  S  SD    . MET B 1 319 ? 104.664 144.328 140.966 1.00 47.61 ?  319 MET B SD    1 
ATOM   8129  C  CE    . MET B 1 319 ? 106.438 144.347 140.745 1.00 41.96 ?  319 MET B CE    1 
ATOM   8130  N  N     . ASN B 1 320 ? 102.983 146.839 145.445 1.00 39.09 ?  320 ASN B N     1 
ATOM   8131  C  CA    . ASN B 1 320 ? 101.745 146.783 146.214 1.00 39.65 ?  320 ASN B CA    1 
ATOM   8132  C  C     . ASN B 1 320 ? 100.638 147.587 145.544 1.00 46.07 ?  320 ASN B C     1 
ATOM   8133  O  O     . ASN B 1 320 ? 99.477  147.162 145.523 1.00 46.18 ?  320 ASN B O     1 
ATOM   8134  C  CB    . ASN B 1 320 ? 101.992 147.281 147.638 1.00 40.73 ?  320 ASN B CB    1 
ATOM   8135  C  CG    . ASN B 1 320 ? 103.036 146.458 148.366 1.00 43.14 ?  320 ASN B CG    1 
ATOM   8136  O  OD1   . ASN B 1 320 ? 102.821 145.283 148.661 1.00 42.76 ?  320 ASN B OD1   1 
ATOM   8137  N  ND2   . ASN B 1 320 ? 104.176 147.072 148.656 1.00 43.71 ?  320 ASN B ND2   1 
ATOM   8138  N  N     . GLU B 1 321 ? 100.976 148.750 144.987 1.00 46.25 ?  321 GLU B N     1 
ATOM   8139  C  CA    . GLU B 1 321 ? 99.993  149.556 144.275 1.00 44.91 ?  321 GLU B CA    1 
ATOM   8140  C  C     . GLU B 1 321 ? 99.967  149.273 142.780 1.00 43.62 ?  321 GLU B C     1 
ATOM   8141  O  O     . GLU B 1 321 ? 98.929  149.470 142.138 1.00 45.23 ?  321 GLU B O     1 
ATOM   8142  C  CB    . GLU B 1 321 ? 100.264 151.046 144.501 1.00 43.47 ?  321 GLU B CB    1 
ATOM   8143  C  CG    . GLU B 1 321 ? 101.618 151.515 143.998 1.00 47.11 ?  321 GLU B CG    1 
ATOM   8144  C  CD    . GLU B 1 321 ? 101.568 152.903 143.390 1.00 51.86 ?  321 GLU B CD    1 
ATOM   8145  O  OE1   . GLU B 1 321 ? 100.452 153.421 143.178 1.00 49.66 ?  321 GLU B OE1   1 
ATOM   8146  O  OE2   . GLU B 1 321 ? 102.645 153.476 143.122 1.00 51.96 -1 321 GLU B OE2   1 
ATOM   8147  N  N     . MET B 1 322 ? 101.079 148.813 142.211 1.00 40.70 ?  322 MET B N     1 
ATOM   8148  C  CA    . MET B 1 322 ? 101.188 148.646 140.770 1.00 35.62 ?  322 MET B CA    1 
ATOM   8149  C  C     . MET B 1 322 ? 100.846 147.245 140.284 1.00 37.11 ?  322 MET B C     1 
ATOM   8150  O  O     . MET B 1 322 ? 100.755 147.046 139.071 1.00 47.12 ?  322 MET B O     1 
ATOM   8151  C  CB    . MET B 1 322 ? 102.604 148.999 140.301 1.00 35.35 ?  322 MET B CB    1 
ATOM   8152  C  CG    . MET B 1 322 ? 102.882 150.487 140.196 1.00 39.64 ?  322 MET B CG    1 
ATOM   8153  S  SD    . MET B 1 322 ? 101.428 151.439 139.729 1.00 50.65 ?  322 MET B SD    1 
ATOM   8154  C  CE    . MET B 1 322 ? 101.499 151.306 137.945 1.00 39.32 ?  322 MET B CE    1 
ATOM   8155  N  N     . TYR B 1 323 ? 100.658 146.274 141.179 1.00 37.53 ?  323 TYR B N     1 
ATOM   8156  C  CA    . TYR B 1 323 ? 100.448 144.898 140.736 1.00 33.11 ?  323 TYR B CA    1 
ATOM   8157  C  C     . TYR B 1 323 ? 99.117  144.750 140.009 1.00 40.15 ?  323 TYR B C     1 
ATOM   8158  O  O     . TYR B 1 323 ? 99.044  144.122 138.946 1.00 43.00 ?  323 TYR B O     1 
ATOM   8159  C  CB    . TYR B 1 323 ? 100.521 143.946 141.929 1.00 34.53 ?  323 TYR B CB    1 
ATOM   8160  C  CG    . TYR B 1 323 ? 100.208 142.505 141.586 1.00 37.76 ?  323 TYR B CG    1 
ATOM   8161  C  CD1   . TYR B 1 323 ? 101.183 141.670 141.059 1.00 31.61 ?  323 TYR B CD1   1 
ATOM   8162  C  CD2   . TYR B 1 323 ? 98.939  141.981 141.792 1.00 37.36 ?  323 TYR B CD2   1 
ATOM   8163  C  CE1   . TYR B 1 323 ? 100.902 140.357 140.746 1.00 28.11 ?  323 TYR B CE1   1 
ATOM   8164  C  CE2   . TYR B 1 323 ? 98.650  140.669 141.481 1.00 33.00 ?  323 TYR B CE2   1 
ATOM   8165  C  CZ    . TYR B 1 323 ? 99.635  139.863 140.959 1.00 32.57 ?  323 TYR B CZ    1 
ATOM   8166  O  OH    . TYR B 1 323 ? 99.351  138.556 140.648 1.00 38.21 ?  323 TYR B OH    1 
ATOM   8167  N  N     . ASP B 1 324 ? 98.050  145.320 140.571 1.00 43.32 ?  324 ASP B N     1 
ATOM   8168  C  CA    . ASP B 1 324 ? 96.745  145.238 139.926 1.00 38.89 ?  324 ASP B CA    1 
ATOM   8169  C  C     . ASP B 1 324 ? 96.744  145.976 138.595 1.00 41.91 ?  324 ASP B C     1 
ATOM   8170  O  O     . ASP B 1 324 ? 96.137  145.515 137.622 1.00 47.99 ?  324 ASP B O     1 
ATOM   8171  C  CB    . ASP B 1 324 ? 95.664  145.791 140.853 1.00 42.11 ?  324 ASP B CB    1 
ATOM   8172  C  CG    . ASP B 1 324 ? 95.463  144.935 142.085 1.00 45.33 ?  324 ASP B CG    1 
ATOM   8173  O  OD1   . ASP B 1 324 ? 95.563  143.697 141.971 1.00 45.34 ?  324 ASP B OD1   1 
ATOM   8174  O  OD2   . ASP B 1 324 ? 95.204  145.500 143.168 1.00 46.45 -1 324 ASP B OD2   1 
ATOM   8175  N  N     . LYS B 1 325 ? 97.415  147.127 138.536 1.00 42.05 ?  325 LYS B N     1 
ATOM   8176  C  CA    . LYS B 1 325 ? 97.508  147.867 137.281 1.00 41.84 ?  325 LYS B CA    1 
ATOM   8177  C  C     . LYS B 1 325 ? 98.287  147.083 136.234 1.00 41.15 ?  325 LYS B C     1 
ATOM   8178  O  O     . LYS B 1 325 ? 97.922  147.083 135.053 1.00 46.54 ?  325 LYS B O     1 
ATOM   8179  C  CB    . LYS B 1 325 ? 98.148  149.232 137.526 1.00 39.41 ?  325 LYS B CB    1 
ATOM   8180  C  CG    . LYS B 1 325 ? 97.412  150.072 138.553 1.00 38.15 ?  325 LYS B CG    1 
ATOM   8181  C  CD    . LYS B 1 325 ? 97.355  151.533 138.139 1.00 43.84 ?  325 LYS B CD    1 
ATOM   8182  C  CE    . LYS B 1 325 ? 98.022  152.428 139.168 1.00 44.36 ?  325 LYS B CE    1 
ATOM   8183  N  NZ    . LYS B 1 325 ? 97.275  152.445 140.455 1.00 46.04 1  325 LYS B NZ    1 
ATOM   8184  N  N     . PHE B 1 326 ? 99.368  146.416 136.644 1.00 39.33 ?  326 PHE B N     1 
ATOM   8185  C  CA    . PHE B 1 326 ? 100.123 145.580 135.718 1.00 36.16 ?  326 PHE B CA    1 
ATOM   8186  C  C     . PHE B 1 326 ? 99.270  144.433 135.199 1.00 36.41 ?  326 PHE B C     1 
ATOM   8187  O  O     . PHE B 1 326 ? 99.280  144.136 133.999 1.00 44.28 ?  326 PHE B O     1 
ATOM   8188  C  CB    . PHE B 1 326 ? 101.375 145.029 136.402 1.00 34.73 ?  326 PHE B CB    1 
ATOM   8189  C  CG    . PHE B 1 326 ? 102.402 146.069 136.742 1.00 32.72 ?  326 PHE B CG    1 
ATOM   8190  C  CD1   . PHE B 1 326 ? 102.356 147.330 136.176 1.00 34.49 ?  326 PHE B CD1   1 
ATOM   8191  C  CD2   . PHE B 1 326 ? 103.422 145.779 137.632 1.00 36.10 ?  326 PHE B CD2   1 
ATOM   8192  C  CE1   . PHE B 1 326 ? 103.304 148.280 136.495 1.00 33.27 ?  326 PHE B CE1   1 
ATOM   8193  C  CE2   . PHE B 1 326 ? 104.372 146.724 137.951 1.00 39.21 ?  326 PHE B CE2   1 
ATOM   8194  C  CZ    . PHE B 1 326 ? 104.312 147.975 137.381 1.00 39.45 ?  326 PHE B CZ    1 
ATOM   8195  N  N     . VAL B 1 327 ? 98.527  143.774 136.091 1.00 40.83 ?  327 VAL B N     1 
ATOM   8196  C  CA    . VAL B 1 327 ? 97.719  142.627 135.689 1.00 43.25 ?  327 VAL B CA    1 
ATOM   8197  C  C     . VAL B 1 327 ? 96.594  143.061 134.757 1.00 43.55 ?  327 VAL B C     1 
ATOM   8198  O  O     . VAL B 1 327 ? 96.315  142.400 133.749 1.00 45.72 ?  327 VAL B O     1 
ATOM   8199  C  CB    . VAL B 1 327 ? 97.181  141.893 136.931 1.00 37.68 ?  327 VAL B CB    1 
ATOM   8200  C  CG1   . VAL B 1 327 ? 96.169  140.836 136.530 1.00 40.71 ?  327 VAL B CG1   1 
ATOM   8201  C  CG2   . VAL B 1 327 ? 98.322  141.263 137.708 1.00 31.33 ?  327 VAL B CG2   1 
ATOM   8202  N  N     . ASP B 1 328 ? 95.941  144.180 135.064 1.00 44.04 ?  328 ASP B N     1 
ATOM   8203  C  CA    . ASP B 1 328 ? 94.830  144.659 134.253 1.00 45.35 ?  328 ASP B CA    1 
ATOM   8204  C  C     . ASP B 1 328 ? 95.278  145.356 132.977 1.00 45.87 ?  328 ASP B C     1 
ATOM   8205  O  O     . ASP B 1 328 ? 94.435  145.638 132.120 1.00 49.89 ?  328 ASP B O     1 
ATOM   8206  C  CB    . ASP B 1 328 ? 93.952  145.609 135.069 1.00 45.98 ?  328 ASP B CB    1 
ATOM   8207  C  CG    . ASP B 1 328 ? 93.119  144.883 136.104 1.00 52.99 ?  328 ASP B CG    1 
ATOM   8208  O  OD1   . ASP B 1 328 ? 92.994  143.645 136.006 1.00 52.45 ?  328 ASP B OD1   1 
ATOM   8209  O  OD2   . ASP B 1 328 ? 92.589  145.551 137.017 1.00 51.64 -1 328 ASP B OD2   1 
ATOM   8210  N  N     . ASN B 1 329 ? 96.565  145.645 132.829 1.00 40.44 ?  329 ASN B N     1 
ATOM   8211  C  CA    . ASN B 1 329 ? 97.051  146.299 131.622 1.00 39.47 ?  329 ASN B CA    1 
ATOM   8212  C  C     . ASN B 1 329 ? 97.248  145.266 130.520 1.00 47.37 ?  329 ASN B C     1 
ATOM   8213  O  O     . ASN B 1 329 ? 98.076  144.362 130.676 1.00 44.71 ?  329 ASN B O     1 
ATOM   8214  C  CB    . ASN B 1 329 ? 98.359  147.027 131.897 1.00 36.96 ?  329 ASN B CB    1 
ATOM   8215  C  CG    . ASN B 1 329 ? 98.620  148.147 130.911 1.00 42.80 ?  329 ASN B CG    1 
ATOM   8216  O  OD1   . ASN B 1 329 ? 98.981  147.903 129.762 1.00 47.29 ?  329 ASN B OD1   1 
ATOM   8217  N  ND2   . ASN B 1 329 ? 98.440  149.383 131.359 1.00 40.27 ?  329 ASN B ND2   1 
ATOM   8218  N  N     . PRO B 1 330 ? 96.515  145.354 129.407 1.00 49.24 ?  330 PRO B N     1 
ATOM   8219  C  CA    . PRO B 1 330 ? 96.729  144.394 128.313 1.00 43.76 ?  330 PRO B CA    1 
ATOM   8220  C  C     . PRO B 1 330 ? 98.080  144.532 127.639 1.00 41.32 ?  330 PRO B C     1 
ATOM   8221  O  O     . PRO B 1 330 ? 98.565  143.553 127.058 1.00 44.94 ?  330 PRO B O     1 
ATOM   8222  C  CB    . PRO B 1 330 ? 95.586  144.709 127.341 1.00 46.22 ?  330 PRO B CB    1 
ATOM   8223  C  CG    . PRO B 1 330 ? 95.242  146.129 127.622 1.00 43.83 ?  330 PRO B CG    1 
ATOM   8224  C  CD    . PRO B 1 330 ? 95.453  146.323 129.093 1.00 42.32 ?  330 PRO B CD    1 
ATOM   8225  N  N     . ARG B 1 331 ? 98.702  145.708 127.694 1.00 39.59 ?  331 ARG B N     1 
ATOM   8226  C  CA    . ARG B 1 331 ? 99.995  145.927 127.062 1.00 42.99 ?  331 ARG B CA    1 
ATOM   8227  C  C     . ARG B 1 331 ? 101.160 145.454 127.921 1.00 42.42 ?  331 ARG B C     1 
ATOM   8228  O  O     . ARG B 1 331 ? 102.305 145.496 127.460 1.00 41.85 ?  331 ARG B O     1 
ATOM   8229  C  CB    . ARG B 1 331 ? 100.163 147.410 126.722 1.00 40.58 ?  331 ARG B CB    1 
ATOM   8230  C  CG    . ARG B 1 331 ? 99.035  147.967 125.870 1.00 41.00 ?  331 ARG B CG    1 
ATOM   8231  C  CD    . ARG B 1 331 ? 99.097  149.487 125.783 1.00 41.46 ?  331 ARG B CD    1 
ATOM   8232  N  NE    . ARG B 1 331 ? 98.383  150.185 126.851 1.00 41.04 ?  331 ARG B NE    1 
ATOM   8233  C  CZ    . ARG B 1 331 ? 97.134  149.952 127.239 1.00 45.31 ?  331 ARG B CZ    1 
ATOM   8234  N  NH1   . ARG B 1 331 ? 96.351  149.095 126.604 1.00 45.36 1  331 ARG B NH1   1 
ATOM   8235  N  NH2   . ARG B 1 331 ? 96.645  150.622 128.279 1.00 42.03 ?  331 ARG B NH2   1 
ATOM   8236  N  N     . VAL B 1 332 ? 100.899 145.015 129.147 1.00 37.76 ?  332 VAL B N     1 
ATOM   8237  C  CA    . VAL B 1 332 ? 101.913 144.427 130.013 1.00 34.85 ?  332 VAL B CA    1 
ATOM   8238  C  C     . VAL B 1 332 ? 101.807 142.914 129.888 1.00 38.85 ?  332 VAL B C     1 
ATOM   8239  O  O     . VAL B 1 332 ? 100.736 142.338 130.115 1.00 40.26 ?  332 VAL B O     1 
ATOM   8240  C  CB    . VAL B 1 332 ? 101.739 144.879 131.472 1.00 35.51 ?  332 VAL B CB    1 
ATOM   8241  C  CG1   . VAL B 1 332 ? 102.551 143.996 132.401 1.00 37.32 ?  332 VAL B CG1   1 
ATOM   8242  C  CG2   . VAL B 1 332 ? 102.147 146.335 131.628 1.00 34.26 ?  332 VAL B CG2   1 
ATOM   8243  N  N     . LYS B 1 333 ? 102.908 142.269 129.517 1.00 34.79 ?  333 LYS B N     1 
ATOM   8244  C  CA    . LYS B 1 333 ? 102.926 140.827 129.320 1.00 31.33 ?  333 LYS B CA    1 
ATOM   8245  C  C     . LYS B 1 333 ? 103.253 140.117 130.628 1.00 34.52 ?  333 LYS B C     1 
ATOM   8246  O  O     . LYS B 1 333 ? 104.113 140.560 131.394 1.00 35.76 ?  333 LYS B O     1 
ATOM   8247  C  CB    . LYS B 1 333 ? 103.939 140.445 128.240 1.00 30.40 ?  333 LYS B CB    1 
ATOM   8248  C  CG    . LYS B 1 333 ? 103.754 139.046 127.685 1.00 37.96 ?  333 LYS B CG    1 
ATOM   8249  C  CD    . LYS B 1 333 ? 104.883 138.670 126.742 1.00 38.66 ?  333 LYS B CD    1 
ATOM   8250  C  CE    . LYS B 1 333 ? 104.762 137.228 126.285 1.00 38.80 ?  333 LYS B CE    1 
ATOM   8251  N  NZ    . LYS B 1 333 ? 105.851 136.850 125.344 1.00 40.45 1  333 LYS B NZ    1 
ATOM   8252  N  N     . LYS B 1 334 ? 102.556 139.010 130.878 1.00 37.10 ?  334 LYS B N     1 
ATOM   8253  C  CA    . LYS B 1 334 ? 102.710 138.269 132.120 1.00 32.47 ?  334 LYS B CA    1 
ATOM   8254  C  C     . LYS B 1 334 ? 102.347 136.811 131.882 1.00 35.58 ?  334 LYS B C     1 
ATOM   8255  O  O     . LYS B 1 334 ? 101.689 136.470 130.897 1.00 43.50 ?  334 LYS B O     1 
ATOM   8256  C  CB    . LYS B 1 334 ? 101.829 138.855 133.227 1.00 33.98 ?  334 LYS B CB    1 
ATOM   8257  C  CG    . LYS B 1 334 ? 100.360 138.924 132.849 1.00 35.77 ?  334 LYS B CG    1 
ATOM   8258  C  CD    . LYS B 1 334 ? 99.621  139.994 133.625 1.00 33.80 ?  334 LYS B CD    1 
ATOM   8259  C  CE    . LYS B 1 334 ? 99.504  141.268 132.815 1.00 37.85 ?  334 LYS B CE    1 
ATOM   8260  N  NZ    . LYS B 1 334 ? 98.512  141.153 131.712 1.00 37.62 1  334 LYS B NZ    1 
ATOM   8261  N  N     . GLU B 1 335 ? 102.790 135.948 132.796 1.00 38.13 ?  335 GLU B N     1 
ATOM   8262  C  CA    . GLU B 1 335 ? 102.319 134.571 132.853 1.00 43.58 ?  335 GLU B CA    1 
ATOM   8263  C  C     . GLU B 1 335 ? 101.890 134.235 134.272 1.00 41.91 ?  335 GLU B C     1 
ATOM   8264  O  O     . GLU B 1 335 ? 102.488 134.711 135.241 1.00 44.95 ?  335 GLU B O     1 
ATOM   8265  C  CB    . GLU B 1 335 ? 103.371 133.550 132.408 1.00 39.57 ?  335 GLU B CB    1 
ATOM   8266  C  CG    . GLU B 1 335 ? 104.806 133.942 132.622 1.00 40.04 ?  335 GLU B CG    1 
ATOM   8267  C  CD    . GLU B 1 335 ? 105.749 133.029 131.867 1.00 47.14 ?  335 GLU B CD    1 
ATOM   8268  O  OE1   . GLU B 1 335 ? 106.679 132.484 132.498 1.00 44.33 ?  335 GLU B OE1   1 
ATOM   8269  O  OE2   . GLU B 1 335 ? 105.558 132.851 130.645 1.00 46.65 -1 335 GLU B OE2   1 
ATOM   8270  N  N     . LYS B 1 336 ? 100.857 133.407 134.382 1.00 38.84 ?  336 LYS B N     1 
ATOM   8271  C  CA    . LYS B 1 336 ? 100.373 132.971 135.682 1.00 30.35 ?  336 LYS B CA    1 
ATOM   8272  C  C     . LYS B 1 336 ? 101.405 132.085 136.369 1.00 37.36 ?  336 LYS B C     1 
ATOM   8273  O  O     . LYS B 1 336 ? 102.063 131.260 135.731 1.00 40.56 ?  336 LYS B O     1 
ATOM   8274  C  CB    . LYS B 1 336 ? 99.059  132.208 135.526 1.00 40.33 ?  336 LYS B CB    1 
ATOM   8275  C  CG    . LYS B 1 336 ? 98.257  132.074 136.805 1.00 43.04 ?  336 LYS B CG    1 
ATOM   8276  C  CD    . LYS B 1 336 ? 97.355  133.276 136.996 1.00 44.70 ?  336 LYS B CD    1 
ATOM   8277  C  CE    . LYS B 1 336 ? 95.986  133.035 136.385 1.00 41.52 ?  336 LYS B CE    1 
ATOM   8278  N  NZ    . LYS B 1 336 ? 95.097  132.273 137.302 1.00 41.81 1  336 LYS B NZ    1 
ATOM   8279  N  N     . ILE B 1 337 ? 101.549 132.267 137.680 1.00 38.68 ?  337 ILE B N     1 
ATOM   8280  C  CA    . ILE B 1 337 ? 102.350 131.388 138.520 1.00 36.88 ?  337 ILE B CA    1 
ATOM   8281  C  C     . ILE B 1 337 ? 101.546 131.069 139.772 1.00 39.62 ?  337 ILE B C     1 
ATOM   8282  O  O     . ILE B 1 337 ? 100.552 131.724 140.086 1.00 45.76 ?  337 ILE B O     1 
ATOM   8283  C  CB    . ILE B 1 337 ? 103.714 131.999 138.901 1.00 35.97 ?  337 ILE B CB    1 
ATOM   8284  C  CG1   . ILE B 1 337 ? 103.518 133.343 139.605 1.00 37.24 ?  337 ILE B CG1   1 
ATOM   8285  C  CG2   . ILE B 1 337 ? 104.606 132.140 137.679 1.00 37.46 ?  337 ILE B CG2   1 
ATOM   8286  C  CD1   . ILE B 1 337 ? 104.537 133.624 140.681 1.00 33.60 ?  337 ILE B CD1   1 
ATOM   8287  N  N     . ASN B 1 338 ? 101.991 130.042 140.489 1.00 38.80 ?  338 ASN B N     1 
ATOM   8288  C  CA    . ASN B 1 338 ? 101.437 129.743 141.799 1.00 34.32 ?  338 ASN B CA    1 
ATOM   8289  C  C     . ASN B 1 338 ? 102.400 130.264 142.851 1.00 35.85 ?  338 ASN B C     1 
ATOM   8290  O  O     . ASN B 1 338 ? 103.494 129.702 143.004 1.00 42.95 ?  338 ASN B O     1 
ATOM   8291  C  CB    . ASN B 1 338 ? 101.215 128.243 141.969 1.00 35.42 ?  338 ASN B CB    1 
ATOM   8292  C  CG    . ASN B 1 338 ? 100.220 127.923 143.065 1.00 39.78 ?  338 ASN B CG    1 
ATOM   8293  O  OD1   . ASN B 1 338 ? 99.775  128.808 143.793 1.00 41.66 ?  338 ASN B OD1   1 
ATOM   8294  N  ND2   . ASN B 1 338 ? 99.863  126.650 143.186 1.00 39.95 ?  338 ASN B ND2   1 
ATOM   8295  N  N     . PRO B 1 339 ? 102.060 131.330 143.579 1.00 36.61 ?  339 PRO B N     1 
ATOM   8296  C  CA    . PRO B 1 339 ? 103.004 131.866 144.572 1.00 34.86 ?  339 PRO B CA    1 
ATOM   8297  C  C     . PRO B 1 339 ? 103.352 130.882 145.673 1.00 32.01 ?  339 PRO B C     1 
ATOM   8298  O  O     . PRO B 1 339 ? 104.489 130.893 146.160 1.00 36.23 ?  339 PRO B O     1 
ATOM   8299  C  CB    . PRO B 1 339 ? 102.272 133.097 145.121 1.00 33.12 ?  339 PRO B CB    1 
ATOM   8300  C  CG    . PRO B 1 339 ? 100.839 132.833 144.854 1.00 36.79 ?  339 PRO B CG    1 
ATOM   8301  C  CD    . PRO B 1 339 ? 100.792 132.077 143.565 1.00 36.01 ?  339 PRO B CD    1 
ATOM   8302  N  N     . ARG B 1 340 ? 102.411 130.031 146.084 1.00 33.55 ?  340 ARG B N     1 
ATOM   8303  C  CA    . ARG B 1 340 ? 102.727 129.020 147.086 1.00 32.24 ?  340 ARG B CA    1 
ATOM   8304  C  C     . ARG B 1 340 ? 103.686 127.979 146.530 1.00 33.47 ?  340 ARG B C     1 
ATOM   8305  O  O     . ARG B 1 340 ? 104.596 127.526 147.234 1.00 39.77 ?  340 ARG B O     1 
ATOM   8306  C  CB    . ARG B 1 340 ? 101.448 128.361 147.595 1.00 31.38 ?  340 ARG B CB    1 
ATOM   8307  C  CG    . ARG B 1 340 ? 100.639 129.244 148.518 1.00 29.58 ?  340 ARG B CG    1 
ATOM   8308  C  CD    . ARG B 1 340 ? 99.727  128.432 149.415 1.00 31.39 ?  340 ARG B CD    1 
ATOM   8309  N  NE    . ARG B 1 340 ? 98.818  129.291 150.164 1.00 33.49 ?  340 ARG B NE    1 
ATOM   8310  C  CZ    . ARG B 1 340 ? 97.917  128.854 151.031 1.00 35.94 ?  340 ARG B CZ    1 
ATOM   8311  N  NH1   . ARG B 1 340 ? 97.776  127.565 151.290 1.00 35.30 1  340 ARG B NH1   1 
ATOM   8312  N  NH2   . ARG B 1 340 ? 97.136  129.732 151.653 1.00 36.79 ?  340 ARG B NH2   1 
ATOM   8313  N  N     . LYS B 1 341 ? 103.500 127.586 145.269 1.00 34.62 ?  341 LYS B N     1 
ATOM   8314  C  CA    . LYS B 1 341 ? 104.444 126.669 144.642 1.00 33.59 ?  341 LYS B CA    1 
ATOM   8315  C  C     . LYS B 1 341 ? 105.818 127.308 144.503 1.00 30.60 ?  341 LYS B C     1 
ATOM   8316  O  O     . LYS B 1 341 ? 106.839 126.635 144.670 1.00 32.98 ?  341 LYS B O     1 
ATOM   8317  C  CB    . LYS B 1 341 ? 103.917 126.216 143.281 1.00 37.60 ?  341 LYS B CB    1 
ATOM   8318  C  CG    . LYS B 1 341 ? 102.832 125.151 143.351 1.00 38.96 ?  341 LYS B CG    1 
ATOM   8319  C  CD    . LYS B 1 341 ? 102.956 124.299 144.606 1.00 40.97 ?  341 LYS B CD    1 
ATOM   8320  C  CE    . LYS B 1 341 ? 101.956 123.157 144.603 1.00 41.70 ?  341 LYS B CE    1 
ATOM   8321  N  NZ    . LYS B 1 341 ? 102.614 121.851 144.881 1.00 40.34 1  341 LYS B NZ    1 
ATOM   8322  N  N     . LEU B 1 342 ? 105.866 128.607 144.202 1.00 32.33 ?  342 LEU B N     1 
ATOM   8323  C  CA    . LEU B 1 342 ? 107.148 129.302 144.142 1.00 29.16 ?  342 LEU B CA    1 
ATOM   8324  C  C     . LEU B 1 342 ? 107.813 129.353 145.513 1.00 29.99 ?  342 LEU B C     1 
ATOM   8325  O  O     . LEU B 1 342 ? 109.033 129.193 145.622 1.00 38.62 ?  342 LEU B O     1 
ATOM   8326  C  CB    . LEU B 1 342 ? 106.958 130.709 143.578 1.00 28.81 ?  342 LEU B CB    1 
ATOM   8327  C  CG    . LEU B 1 342 ? 108.216 131.391 143.037 1.00 29.11 ?  342 LEU B CG    1 
ATOM   8328  C  CD1   . LEU B 1 342 ? 109.037 130.419 142.207 1.00 28.49 ?  342 LEU B CD1   1 
ATOM   8329  C  CD2   . LEU B 1 342 ? 107.856 132.617 142.220 1.00 28.15 ?  342 LEU B CD2   1 
ATOM   8330  N  N     . LEU B 1 343 ? 107.029 129.575 146.571 1.00 27.61 ?  343 LEU B N     1 
ATOM   8331  C  CA    . LEU B 1 343 ? 107.580 129.554 147.924 1.00 29.13 ?  343 LEU B CA    1 
ATOM   8332  C  C     . LEU B 1 343 ? 108.119 128.176 148.281 1.00 28.50 ?  343 LEU B C     1 
ATOM   8333  O  O     . LEU B 1 343 ? 109.188 128.054 148.892 1.00 32.52 ?  343 LEU B O     1 
ATOM   8334  C  CB    . LEU B 1 343 ? 106.513 129.983 148.928 1.00 31.73 ?  343 LEU B CB    1 
ATOM   8335  C  CG    . LEU B 1 343 ? 106.477 131.456 149.328 1.00 32.63 ?  343 LEU B CG    1 
ATOM   8336  C  CD1   . LEU B 1 343 ? 105.337 131.708 150.295 1.00 27.04 ?  343 LEU B CD1   1 
ATOM   8337  C  CD2   . LEU B 1 343 ? 107.802 131.878 149.936 1.00 33.94 ?  343 LEU B CD2   1 
ATOM   8338  N  N     . GLU B 1 344 ? 107.383 127.123 147.922 1.00 34.65 ?  344 GLU B N     1 
ATOM   8339  C  CA    . GLU B 1 344 ? 107.853 125.768 148.187 1.00 32.82 ?  344 GLU B CA    1 
ATOM   8340  C  C     . GLU B 1 344 ? 109.113 125.459 147.391 1.00 29.44 ?  344 GLU B C     1 
ATOM   8341  O  O     . GLU B 1 344 ? 110.011 124.769 147.883 1.00 34.99 ?  344 GLU B O     1 
ATOM   8342  C  CB    . GLU B 1 344 ? 106.750 124.759 147.875 1.00 35.28 ?  344 GLU B CB    1 
ATOM   8343  C  CG    . GLU B 1 344 ? 105.512 124.914 148.741 1.00 36.66 ?  344 GLU B CG    1 
ATOM   8344  C  CD    . GLU B 1 344 ? 104.374 124.021 148.292 1.00 45.78 ?  344 GLU B CD    1 
ATOM   8345  O  OE1   . GLU B 1 344 ? 104.650 122.944 147.725 1.00 44.97 ?  344 GLU B OE1   1 
ATOM   8346  O  OE2   . GLU B 1 344 ? 103.203 124.398 148.505 1.00 43.83 -1 344 GLU B OE2   1 
ATOM   8347  N  N     . LYS B 1 345 ? 109.196 125.961 146.158 1.00 29.73 ?  345 LYS B N     1 
ATOM   8348  C  CA    . LYS B 1 345 ? 110.411 125.800 145.367 1.00 28.05 ?  345 LYS B CA    1 
ATOM   8349  C  C     . LYS B 1 345 ? 111.583 126.529 146.008 1.00 33.02 ?  345 LYS B C     1 
ATOM   8350  O  O     . LYS B 1 345 ? 112.708 126.018 146.021 1.00 36.04 ?  345 LYS B O     1 
ATOM   8351  C  CB    . LYS B 1 345 ? 110.174 126.303 143.944 1.00 29.85 ?  345 LYS B CB    1 
ATOM   8352  C  CG    . LYS B 1 345 ? 111.360 126.132 143.017 1.00 30.65 ?  345 LYS B CG    1 
ATOM   8353  C  CD    . LYS B 1 345 ? 111.042 126.636 141.623 1.00 29.51 ?  345 LYS B CD    1 
ATOM   8354  C  CE    . LYS B 1 345 ? 112.260 126.556 140.724 1.00 34.19 ?  345 LYS B CE    1 
ATOM   8355  N  NZ    . LYS B 1 345 ? 111.992 127.124 139.378 1.00 34.65 1  345 LYS B NZ    1 
ATOM   8356  N  N     . LEU B 1 346 ? 111.337 127.726 146.547 1.00 33.81 ?  346 LEU B N     1 
ATOM   8357  C  CA    . LEU B 1 346 ? 112.380 128.452 147.265 1.00 27.40 ?  346 LEU B CA    1 
ATOM   8358  C  C     . LEU B 1 346 ? 112.871 127.652 148.463 1.00 25.79 ?  346 LEU B C     1 
ATOM   8359  O  O     . LEU B 1 346 ? 114.079 127.525 148.685 1.00 28.42 ?  346 LEU B O     1 
ATOM   8360  C  CB    . LEU B 1 346 ? 111.857 129.814 147.720 1.00 27.66 ?  346 LEU B CB    1 
ATOM   8361  C  CG    . LEU B 1 346 ? 111.585 130.893 146.674 1.00 26.18 ?  346 LEU B CG    1 
ATOM   8362  C  CD1   . LEU B 1 346 ? 110.976 132.115 147.333 1.00 30.49 ?  346 LEU B CD1   1 
ATOM   8363  C  CD2   . LEU B 1 346 ? 112.858 131.258 145.949 1.00 27.88 ?  346 LEU B CD2   1 
ATOM   8364  N  N     . ALA B 1 347 ? 111.941 127.101 149.244 1.00 26.69 ?  347 ALA B N     1 
ATOM   8365  C  CA    . ALA B 1 347 ? 112.328 126.327 150.420 1.00 20.04 ?  347 ALA B CA    1 
ATOM   8366  C  C     . ALA B 1 347 ? 113.088 125.066 150.029 1.00 27.48 ?  347 ALA B C     1 
ATOM   8367  O  O     . ALA B 1 347 ? 114.066 124.694 150.687 1.00 35.93 ?  347 ALA B O     1 
ATOM   8368  C  CB    . ALA B 1 347 ? 111.095 125.977 151.248 1.00 19.98 ?  347 ALA B CB    1 
ATOM   8369  N  N     . MET B 1 348 ? 112.649 124.391 148.965 1.00 33.95 ?  348 MET B N     1 
ATOM   8370  C  CA    . MET B 1 348 ? 113.352 123.204 148.491 1.00 31.21 ?  348 MET B CA    1 
ATOM   8371  C  C     . MET B 1 348 ? 114.764 123.547 148.038 1.00 31.70 ?  348 MET B C     1 
ATOM   8372  O  O     . MET B 1 348 ? 115.718 122.819 148.342 1.00 40.09 ?  348 MET B O     1 
ATOM   8373  C  CB    . MET B 1 348 ? 112.558 122.552 147.358 1.00 33.42 ?  348 MET B CB    1 
ATOM   8374  C  CG    . MET B 1 348 ? 113.288 121.439 146.625 1.00 40.99 ?  348 MET B CG    1 
ATOM   8375  S  SD    . MET B 1 348 ? 114.036 121.980 145.074 1.00 60.89 ?  348 MET B SD    1 
ATOM   8376  C  CE    . MET B 1 348 ? 112.701 122.932 144.356 1.00 38.33 ?  348 MET B CE    1 
ATOM   8377  N  N     . LEU B 1 349 ? 114.918 124.658 147.316 1.00 26.74 ?  349 LEU B N     1 
ATOM   8378  C  CA    . LEU B 1 349 ? 116.239 125.070 146.863 1.00 27.33 ?  349 LEU B CA    1 
ATOM   8379  C  C     . LEU B 1 349 ? 117.139 125.431 148.036 1.00 28.95 ?  349 LEU B C     1 
ATOM   8380  O  O     . LEU B 1 349 ? 118.336 125.127 148.023 1.00 32.49 ?  349 LEU B O     1 
ATOM   8381  C  CB    . LEU B 1 349 ? 116.110 126.247 145.902 1.00 27.93 ?  349 LEU B CB    1 
ATOM   8382  C  CG    . LEU B 1 349 ? 116.050 125.874 144.423 1.00 33.81 ?  349 LEU B CG    1 
ATOM   8383  C  CD1   . LEU B 1 349 ? 115.251 126.909 143.671 1.00 34.75 ?  349 LEU B CD1   1 
ATOM   8384  C  CD2   . LEU B 1 349 ? 117.448 125.748 143.848 1.00 33.96 ?  349 LEU B CD2   1 
ATOM   8385  N  N     . ARG B 1 350 ? 116.588 126.099 149.053 1.00 26.35 ?  350 ARG B N     1 
ATOM   8386  C  CA    . ARG B 1 350 ? 117.390 126.437 150.225 1.00 22.58 ?  350 ARG B CA    1 
ATOM   8387  C  C     . ARG B 1 350 ? 117.781 125.196 151.014 1.00 30.68 ?  350 ARG B C     1 
ATOM   8388  O  O     . ARG B 1 350 ? 118.890 125.134 151.557 1.00 41.06 ?  350 ARG B O     1 
ATOM   8389  C  CB    . ARG B 1 350 ? 116.639 127.423 151.118 1.00 25.27 ?  350 ARG B CB    1 
ATOM   8390  C  CG    . ARG B 1 350 ? 116.249 128.715 150.423 1.00 24.47 ?  350 ARG B CG    1 
ATOM   8391  C  CD    . ARG B 1 350 ? 115.886 129.790 151.421 1.00 26.29 ?  350 ARG B CD    1 
ATOM   8392  N  NE    . ARG B 1 350 ? 116.994 130.710 151.640 1.00 33.09 ?  350 ARG B NE    1 
ATOM   8393  C  CZ    . ARG B 1 350 ? 117.397 131.123 152.832 1.00 28.82 ?  350 ARG B CZ    1 
ATOM   8394  N  NH1   . ARG B 1 350 ? 116.822 130.694 153.941 1.00 26.87 1  350 ARG B NH1   1 
ATOM   8395  N  NH2   . ARG B 1 350 ? 118.408 131.982 152.912 1.00 32.13 ?  350 ARG B NH2   1 
ATOM   8396  N  N     . SER B 1 351 ? 116.891 124.207 151.101 1.00 33.84 ?  351 SER B N     1 
ATOM   8397  C  CA    . SER B 1 351 ? 117.255 122.947 151.737 1.00 33.14 ?  351 SER B CA    1 
ATOM   8398  C  C     . SER B 1 351 ? 118.364 122.243 150.968 1.00 34.19 ?  351 SER B C     1 
ATOM   8399  O  O     . SER B 1 351 ? 119.306 121.712 151.566 1.00 42.75 ?  351 SER B O     1 
ATOM   8400  C  CB    . SER B 1 351 ? 116.030 122.040 151.851 1.00 34.41 ?  351 SER B CB    1 
ATOM   8401  O  OG    . SER B 1 351 ? 115.069 122.585 152.736 1.00 44.10 ?  351 SER B OG    1 
ATOM   8402  N  N     . GLU B 1 352 ? 118.271 122.231 149.637 1.00 34.56 ?  352 GLU B N     1 
ATOM   8403  C  CA    . GLU B 1 352 ? 119.236 121.484 148.838 1.00 35.03 ?  352 GLU B CA    1 
ATOM   8404  C  C     . GLU B 1 352 ? 120.598 122.168 148.801 1.00 35.91 ?  352 GLU B C     1 
ATOM   8405  O  O     . GLU B 1 352 ? 121.632 121.508 148.954 1.00 44.61 ?  352 GLU B O     1 
ATOM   8406  C  CB    . GLU B 1 352 ? 118.697 121.284 147.424 1.00 36.46 ?  352 GLU B CB    1 
ATOM   8407  C  CG    . GLU B 1 352 ? 117.592 120.247 147.332 1.00 39.07 ?  352 GLU B CG    1 
ATOM   8408  C  CD    . GLU B 1 352 ? 116.855 120.298 146.011 1.00 47.81 ?  352 GLU B CD    1 
ATOM   8409  O  OE1   . GLU B 1 352 ? 117.139 121.212 145.208 1.00 44.81 ?  352 GLU B OE1   1 
ATOM   8410  O  OE2   . GLU B 1 352 ? 115.997 119.424 145.773 1.00 45.72 -1 352 GLU B OE2   1 
ATOM   8411  N  N     . SER B 1 353 ? 120.627 123.487 148.598 1.00 36.06 ?  353 SER B N     1 
ATOM   8412  C  CA    . SER B 1 353 ? 121.875 124.195 148.351 1.00 36.19 ?  353 SER B CA    1 
ATOM   8413  C  C     . SER B 1 353 ? 122.090 125.436 149.203 1.00 30.27 ?  353 SER B C     1 
ATOM   8414  O  O     . SER B 1 353 ? 123.156 126.051 149.093 1.00 32.66 ?  353 SER B O     1 
ATOM   8415  C  CB    . SER B 1 353 ? 121.971 124.604 146.873 1.00 37.72 ?  353 SER B CB    1 
ATOM   8416  O  OG    . SER B 1 353 ? 121.033 125.620 146.565 1.00 35.84 ?  353 SER B OG    1 
ATOM   8417  N  N     . GLY B 1 354 ? 121.130 125.832 150.036 1.00 25.89 ?  354 GLY B N     1 
ATOM   8418  C  CA    . GLY B 1 354 ? 121.255 127.042 150.820 1.00 27.51 ?  354 GLY B CA    1 
ATOM   8419  C  C     . GLY B 1 354 ? 120.873 128.312 150.098 1.00 23.43 ?  354 GLY B C     1 
ATOM   8420  O  O     . GLY B 1 354 ? 120.887 129.384 150.716 1.00 27.53 ?  354 GLY B O     1 
ATOM   8421  N  N     . TYR B 1 355 ? 120.528 128.233 148.821 1.00 26.70 ?  355 TYR B N     1 
ATOM   8422  C  CA    . TYR B 1 355 ? 120.159 129.366 147.993 1.00 16.72 ?  355 TYR B CA    1 
ATOM   8423  C  C     . TYR B 1 355 ? 118.676 129.311 147.654 1.00 24.56 ?  355 TYR B C     1 
ATOM   8424  O  O     . TYR B 1 355 ? 118.069 128.237 147.661 1.00 29.05 ?  355 TYR B O     1 
ATOM   8425  C  CB    . TYR B 1 355 ? 120.984 129.374 146.699 1.00 19.98 ?  355 TYR B CB    1 
ATOM   8426  C  CG    . TYR B 1 355 ? 122.438 129.711 146.906 1.00 28.27 ?  355 TYR B CG    1 
ATOM   8427  C  CD1   . TYR B 1 355 ? 122.813 130.876 147.559 1.00 25.74 ?  355 TYR B CD1   1 
ATOM   8428  C  CD2   . TYR B 1 355 ? 123.437 128.864 146.453 1.00 30.44 ?  355 TYR B CD2   1 
ATOM   8429  C  CE1   . TYR B 1 355 ? 124.141 131.186 147.750 1.00 27.80 ?  355 TYR B CE1   1 
ATOM   8430  C  CE2   . TYR B 1 355 ? 124.769 129.166 146.641 1.00 29.65 ?  355 TYR B CE2   1 
ATOM   8431  C  CZ    . TYR B 1 355 ? 125.114 130.330 147.291 1.00 30.27 ?  355 TYR B CZ    1 
ATOM   8432  O  OH    . TYR B 1 355 ? 126.439 130.641 147.482 1.00 34.28 ?  355 TYR B OH    1 
ATOM   8433  N  N     . PRO B 1 356 ? 118.054 130.453 147.344 1.00 27.49 ?  356 PRO B N     1 
ATOM   8434  C  CA    . PRO B 1 356 ? 118.598 131.815 147.281 1.00 15.66 ?  356 PRO B CA    1 
ATOM   8435  C  C     . PRO B 1 356 ? 118.577 132.552 148.611 1.00 16.09 ?  356 PRO B C     1 
ATOM   8436  O  O     . PRO B 1 356 ? 117.959 132.111 149.573 1.00 24.60 ?  356 PRO B O     1 
ATOM   8437  C  CB    . PRO B 1 356 ? 117.666 132.490 146.275 1.00 18.31 ?  356 PRO B CB    1 
ATOM   8438  C  CG    . PRO B 1 356 ? 116.345 131.858 146.567 1.00 22.80 ?  356 PRO B CG    1 
ATOM   8439  C  CD    . PRO B 1 356 ? 116.659 130.414 146.869 1.00 13.71 ?  356 PRO B CD    1 
ATOM   8440  N  N     . TYR B 1 357 ? 119.263 133.688 148.689 1.00 21.55 ?  357 TYR B N     1 
ATOM   8441  C  CA    . TYR B 1 357 ? 119.003 134.628 149.766 1.00 13.99 ?  357 TYR B CA    1 
ATOM   8442  C  C     . TYR B 1 357 ? 117.603 135.200 149.593 1.00 17.78 ?  357 TYR B C     1 
ATOM   8443  O  O     . TYR B 1 357 ? 117.143 135.422 148.471 1.00 26.50 ?  357 TYR B O     1 
ATOM   8444  C  CB    . TYR B 1 357 ? 120.029 135.763 149.771 1.00 12.95 ?  357 TYR B CB    1 
ATOM   8445  C  CG    . TYR B 1 357 ? 121.471 135.355 149.557 1.00 16.72 ?  357 TYR B CG    1 
ATOM   8446  C  CD1   . TYR B 1 357 ? 121.953 134.142 150.022 1.00 17.56 ?  357 TYR B CD1   1 
ATOM   8447  C  CD2   . TYR B 1 357 ? 122.355 136.196 148.897 1.00 19.44 ?  357 TYR B CD2   1 
ATOM   8448  C  CE1   . TYR B 1 357 ? 123.265 133.775 149.835 1.00 19.94 ?  357 TYR B CE1   1 
ATOM   8449  C  CE2   . TYR B 1 357 ? 123.671 135.836 148.703 1.00 15.34 ?  357 TYR B CE2   1 
ATOM   8450  C  CZ    . TYR B 1 357 ? 124.120 134.624 149.174 1.00 24.11 ?  357 TYR B CZ    1 
ATOM   8451  O  OH    . TYR B 1 357 ? 125.432 134.257 148.987 1.00 31.95 ?  357 TYR B OH    1 
ATOM   8452  N  N     . ILE B 1 358 ? 116.918 135.430 150.705 1.00 25.86 ?  358 ILE B N     1 
ATOM   8453  C  CA    . ILE B 1 358 ? 115.582 136.011 150.691 1.00 18.22 ?  358 ILE B CA    1 
ATOM   8454  C  C     . ILE B 1 358 ? 115.684 137.427 151.232 1.00 19.32 ?  358 ILE B C     1 
ATOM   8455  O  O     . ILE B 1 358 ? 116.114 137.631 152.373 1.00 24.72 ?  358 ILE B O     1 
ATOM   8456  C  CB    . ILE B 1 358 ? 114.584 135.179 151.511 1.00 18.88 ?  358 ILE B CB    1 
ATOM   8457  C  CG1   . ILE B 1 358 ? 114.559 133.729 151.025 1.00 15.46 ?  358 ILE B CG1   1 
ATOM   8458  C  CG2   . ILE B 1 358 ? 113.202 135.800 151.440 1.00 17.41 ?  358 ILE B CG2   1 
ATOM   8459  C  CD1   . ILE B 1 358 ? 114.099 133.567 149.597 1.00 21.51 ?  358 ILE B CD1   1 
ATOM   8460  N  N     . MET B 1 359 ? 115.293 138.402 150.419 1.00 13.23 ?  359 MET B N     1 
ATOM   8461  C  CA    . MET B 1 359 ? 115.214 139.793 150.836 1.00 2.07  ?  359 MET B CA    1 
ATOM   8462  C  C     . MET B 1 359 ? 113.755 140.221 150.797 1.00 7.01  ?  359 MET B C     1 
ATOM   8463  O  O     . MET B 1 359 ? 113.141 140.244 149.726 1.00 20.50 ?  359 MET B O     1 
ATOM   8464  C  CB    . MET B 1 359 ? 116.071 140.688 149.942 1.00 10.80 ?  359 MET B CB    1 
ATOM   8465  C  CG    . MET B 1 359 ? 116.061 142.154 150.340 1.00 9.94  ?  359 MET B CG    1 
ATOM   8466  S  SD    . MET B 1 359 ? 116.112 143.272 148.933 1.00 38.89 ?  359 MET B SD    1 
ATOM   8467  C  CE    . MET B 1 359 ? 115.234 144.684 149.585 1.00 16.35 ?  359 MET B CE    1 
ATOM   8468  N  N     . PHE B 1 360 ? 113.201 140.539 151.962 1.00 13.11 ?  360 PHE B N     1 
ATOM   8469  C  CA    . PHE B 1 360 ? 111.813 140.983 152.057 1.00 5.13  ?  360 PHE B CA    1 
ATOM   8470  C  C     . PHE B 1 360 ? 111.784 142.474 151.752 1.00 13.75 ?  360 PHE B C     1 
ATOM   8471  O  O     . PHE B 1 360 ? 112.134 143.300 152.596 1.00 21.20 ?  360 PHE B O     1 
ATOM   8472  C  CB    . PHE B 1 360 ? 111.244 140.665 153.432 1.00 11.94 ?  360 PHE B CB    1 
ATOM   8473  C  CG    . PHE B 1 360 ? 111.174 139.193 153.726 1.00 16.25 ?  360 PHE B CG    1 
ATOM   8474  C  CD1   . PHE B 1 360 ? 110.358 138.361 152.978 1.00 19.55 ?  360 PHE B CD1   1 
ATOM   8475  C  CD2   . PHE B 1 360 ? 111.943 138.638 154.733 1.00 13.35 ?  360 PHE B CD2   1 
ATOM   8476  C  CE1   . PHE B 1 360 ? 110.301 137.007 153.239 1.00 18.52 ?  360 PHE B CE1   1 
ATOM   8477  C  CE2   . PHE B 1 360 ? 111.890 137.286 154.998 1.00 18.20 ?  360 PHE B CE2   1 
ATOM   8478  C  CZ    . PHE B 1 360 ? 111.067 136.470 154.251 1.00 15.01 ?  360 PHE B CZ    1 
ATOM   8479  N  N     . GLN B 1 361 ? 111.351 142.812 150.534 1.00 18.99 ?  361 GLN B N     1 
ATOM   8480  C  CA    . GLN B 1 361 ? 111.502 144.171 150.021 1.00 9.60  ?  361 GLN B CA    1 
ATOM   8481  C  C     . GLN B 1 361 ? 110.783 145.193 150.893 1.00 9.13  ?  361 GLN B C     1 
ATOM   8482  O  O     . GLN B 1 361 ? 111.328 146.262 151.185 1.00 14.03 ?  361 GLN B O     1 
ATOM   8483  C  CB    . GLN B 1 361 ? 110.983 144.237 148.584 1.00 19.01 ?  361 GLN B CB    1 
ATOM   8484  C  CG    . GLN B 1 361 ? 110.873 145.637 148.016 1.00 20.19 ?  361 GLN B CG    1 
ATOM   8485  C  CD    . GLN B 1 361 ? 111.852 145.890 146.892 1.00 20.87 ?  361 GLN B CD    1 
ATOM   8486  O  OE1   . GLN B 1 361 ? 111.969 145.091 145.965 1.00 30.14 ?  361 GLN B OE1   1 
ATOM   8487  N  NE2   . GLN B 1 361 ? 112.567 147.004 146.969 1.00 20.20 ?  361 GLN B NE2   1 
ATOM   8488  N  N     . ASP B 1 362 ? 109.557 144.887 151.315 1.00 23.19 ?  362 ASP B N     1 
ATOM   8489  C  CA    . ASP B 1 362 ? 108.781 145.852 152.081 1.00 13.79 ?  362 ASP B CA    1 
ATOM   8490  C  C     . ASP B 1 362 ? 109.197 145.921 153.544 1.00 13.78 ?  362 ASP B C     1 
ATOM   8491  O  O     . ASP B 1 362 ? 108.955 146.943 154.191 1.00 23.01 ?  362 ASP B O     1 
ATOM   8492  C  CB    . ASP B 1 362 ? 107.290 145.536 151.969 1.00 16.01 ?  362 ASP B CB    1 
ATOM   8493  C  CG    . ASP B 1 362 ? 106.787 145.616 150.540 1.00 27.61 ?  362 ASP B CG    1 
ATOM   8494  O  OD1   . ASP B 1 362 ? 107.612 145.502 149.609 1.00 24.96 ?  362 ASP B OD1   1 
ATOM   8495  O  OD2   . ASP B 1 362 ? 105.572 145.812 150.342 1.00 37.15 -1 362 ASP B OD2   1 
ATOM   8496  N  N     . ASN B 1 363 ? 109.809 144.864 154.080 1.00 28.56 ?  363 ASN B N     1 
ATOM   8497  C  CA    . ASN B 1 363 ? 110.402 144.961 155.409 1.00 13.54 ?  363 ASN B CA    1 
ATOM   8498  C  C     . ASN B 1 363 ? 111.578 145.928 155.410 1.00 19.84 ?  363 ASN B C     1 
ATOM   8499  O  O     . ASN B 1 363 ? 111.766 146.687 156.366 1.00 25.82 ?  363 ASN B O     1 
ATOM   8500  C  CB    . ASN B 1 363 ? 110.844 143.581 155.896 1.00 10.51 ?  363 ASN B CB    1 
ATOM   8501  C  CG    . ASN B 1 363 ? 109.695 142.758 156.434 1.00 17.88 ?  363 ASN B CG    1 
ATOM   8502  O  OD1   . ASN B 1 363 ? 108.587 143.259 156.611 1.00 22.12 ?  363 ASN B OD1   1 
ATOM   8503  N  ND2   . ASN B 1 363 ? 109.955 141.485 156.702 1.00 20.62 ?  363 ASN B ND2   1 
ATOM   8504  N  N     . VAL B 1 364 ? 112.381 145.908 154.346 1.00 17.04 ?  364 VAL B N     1 
ATOM   8505  C  CA    . VAL B 1 364 ? 113.510 146.824 154.243 1.00 10.09 ?  364 VAL B CA    1 
ATOM   8506  C  C     . VAL B 1 364 ? 113.024 148.258 154.085 1.00 19.58 ?  364 VAL B C     1 
ATOM   8507  O  O     . VAL B 1 364 ? 113.499 149.172 154.768 1.00 25.50 ?  364 VAL B O     1 
ATOM   8508  C  CB    . VAL B 1 364 ? 114.425 146.414 153.075 1.00 0.06  ?  364 VAL B CB    1 
ATOM   8509  C  CG1   . VAL B 1 364 ? 115.658 147.287 153.044 1.00 7.05  ?  364 VAL B CG1   1 
ATOM   8510  C  CG2   . VAL B 1 364 ? 114.803 144.953 153.181 1.00 3.59  ?  364 VAL B CG2   1 
ATOM   8511  N  N     . ASN B 1 365 ? 112.067 148.475 153.185 1.00 14.89 ?  365 ASN B N     1 
ATOM   8512  C  CA    . ASN B 1 365 ? 111.707 149.823 152.769 1.00 4.58  ?  365 ASN B CA    1 
ATOM   8513  C  C     . ASN B 1 365 ? 110.691 150.494 153.680 1.00 12.69 ?  365 ASN B C     1 
ATOM   8514  O  O     . ASN B 1 365 ? 110.506 151.711 153.574 1.00 24.10 ?  365 ASN B O     1 
ATOM   8515  C  CB    . ASN B 1 365 ? 111.176 149.797 151.337 1.00 18.94 ?  365 ASN B CB    1 
ATOM   8516  C  CG    . ASN B 1 365 ? 112.241 149.416 150.334 1.00 16.80 ?  365 ASN B CG    1 
ATOM   8517  O  OD1   . ASN B 1 365 ? 113.298 150.039 150.271 1.00 14.28 ?  365 ASN B OD1   1 
ATOM   8518  N  ND2   . ASN B 1 365 ? 111.971 148.386 149.547 1.00 18.87 ?  365 ASN B ND2   1 
ATOM   8519  N  N     . LYS B 1 366 ? 110.029 149.749 154.567 1.00 16.21 ?  366 LYS B N     1 
ATOM   8520  C  CA    . LYS B 1 366 ? 109.114 150.381 155.507 1.00 19.85 ?  366 LYS B CA    1 
ATOM   8521  C  C     . LYS B 1 366 ? 109.853 151.122 156.610 1.00 20.14 ?  366 LYS B C     1 
ATOM   8522  O  O     . LYS B 1 366 ? 109.276 152.016 157.238 1.00 30.80 ?  366 LYS B O     1 
ATOM   8523  C  CB    . LYS B 1 366 ? 108.167 149.342 156.107 1.00 16.52 ?  366 LYS B CB    1 
ATOM   8524  C  CG    . LYS B 1 366 ? 108.767 148.503 157.218 1.00 25.80 ?  366 LYS B CG    1 
ATOM   8525  C  CD    . LYS B 1 366 ? 107.683 147.795 158.007 1.00 28.53 ?  366 LYS B CD    1 
ATOM   8526  C  CE    . LYS B 1 366 ? 106.770 146.995 157.093 1.00 23.89 ?  366 LYS B CE    1 
ATOM   8527  N  NZ    . LYS B 1 366 ? 105.835 146.134 157.866 1.00 28.97 1  366 LYS B NZ    1 
ATOM   8528  N  N     . VAL B 1 367 ? 111.116 150.776 156.852 1.00 26.19 ?  367 VAL B N     1 
ATOM   8529  C  CA    . VAL B 1 367 ? 111.961 151.449 157.824 1.00 18.01 ?  367 VAL B CA    1 
ATOM   8530  C  C     . VAL B 1 367 ? 113.170 152.100 157.168 1.00 17.99 ?  367 VAL B C     1 
ATOM   8531  O  O     . VAL B 1 367 ? 114.050 152.606 157.860 1.00 23.59 ?  367 VAL B O     1 
ATOM   8532  C  CB    . VAL B 1 367 ? 112.402 150.482 158.941 1.00 14.88 ?  367 VAL B CB    1 
ATOM   8533  C  CG1   . VAL B 1 367 ? 111.211 150.076 159.786 1.00 17.71 ?  367 VAL B CG1   1 
ATOM   8534  C  CG2   . VAL B 1 367 ? 113.067 149.265 158.339 1.00 8.15  ?  367 VAL B CG2   1 
ATOM   8535  N  N     . HIS B 1 368 ? 113.230 152.087 155.839 1.00 17.51 ?  368 HIS B N     1 
ATOM   8536  C  CA    . HIS B 1 368 ? 114.340 152.699 155.125 1.00 3.61  ?  368 HIS B CA    1 
ATOM   8537  C  C     . HIS B 1 368 ? 114.287 154.213 155.279 1.00 17.40 ?  368 HIS B C     1 
ATOM   8538  O  O     . HIS B 1 368 ? 113.231 154.830 155.111 1.00 30.35 ?  368 HIS B O     1 
ATOM   8539  C  CB    . HIS B 1 368 ? 114.293 152.310 153.650 1.00 10.78 ?  368 HIS B CB    1 
ATOM   8540  C  CG    . HIS B 1 368 ? 115.479 152.768 152.862 1.00 6.15  ?  368 HIS B CG    1 
ATOM   8541  N  ND1   . HIS B 1 368 ? 115.390 153.152 151.544 1.00 18.67 ?  368 HIS B ND1   1 
ATOM   8542  C  CD2   . HIS B 1 368 ? 116.781 152.902 153.206 1.00 7.27  ?  368 HIS B CD2   1 
ATOM   8543  C  CE1   . HIS B 1 368 ? 116.586 153.503 151.107 1.00 17.56 ?  368 HIS B CE1   1 
ATOM   8544  N  NE2   . HIS B 1 368 ? 117.447 153.361 152.097 1.00 16.59 ?  368 HIS B NE2   1 
ATOM   8545  N  N     . ALA B 1 369 ? 115.429 154.811 155.602 1.00 20.81 ?  369 ALA B N     1 
ATOM   8546  C  CA    . ALA B 1 369 ? 115.502 156.239 155.866 1.00 13.95 ?  369 ALA B CA    1 
ATOM   8547  C  C     . ALA B 1 369 ? 115.773 157.070 154.621 1.00 25.08 ?  369 ALA B C     1 
ATOM   8548  O  O     . ALA B 1 369 ? 115.732 158.301 154.700 1.00 32.91 ?  369 ALA B O     1 
ATOM   8549  C  CB    . ALA B 1 369 ? 116.584 156.525 156.911 1.00 11.15 ?  369 ALA B CB    1 
ATOM   8550  N  N     . ASN B 1 370 ? 116.035 156.439 153.481 1.00 18.57 ?  370 ASN B N     1 
ATOM   8551  C  CA    . ASN B 1 370 ? 116.415 157.144 152.265 1.00 12.01 ?  370 ASN B CA    1 
ATOM   8552  C  C     . ASN B 1 370 ? 115.566 156.691 151.089 1.00 13.34 ?  370 ASN B C     1 
ATOM   8553  O  O     . ASN B 1 370 ? 116.065 156.501 149.978 1.00 24.87 ?  370 ASN B O     1 
ATOM   8554  C  CB    . ASN B 1 370 ? 117.899 156.948 151.965 1.00 12.83 ?  370 ASN B CB    1 
ATOM   8555  C  CG    . ASN B 1 370 ? 118.793 157.527 153.042 1.00 12.83 ?  370 ASN B CG    1 
ATOM   8556  O  OD1   . ASN B 1 370 ? 118.781 158.731 153.291 1.00 29.53 ?  370 ASN B OD1   1 
ATOM   8557  N  ND2   . ASN B 1 370 ? 119.572 156.671 153.686 1.00 12.13 ?  370 ASN B ND2   1 
ATOM   8558  N  N     . ASN B 1 371 ? 114.263 156.513 151.315 1.00 19.78 ?  371 ASN B N     1 
ATOM   8559  C  CA    . ASN B 1 371 ? 113.364 156.135 150.230 1.00 11.60 ?  371 ASN B CA    1 
ATOM   8560  C  C     . ASN B 1 371 ? 113.222 157.236 149.190 1.00 16.37 ?  371 ASN B C     1 
ATOM   8561  O  O     . ASN B 1 371 ? 112.864 156.944 148.044 1.00 26.99 ?  371 ASN B O     1 
ATOM   8562  C  CB    . ASN B 1 371 ? 111.988 155.766 150.783 1.00 9.05  ?  371 ASN B CB    1 
ATOM   8563  C  CG    . ASN B 1 371 ? 111.924 154.341 151.284 1.00 17.59 ?  371 ASN B CG    1 
ATOM   8564  O  OD1   . ASN B 1 371 ? 112.745 153.504 150.913 1.00 23.47 ?  371 ASN B OD1   1 
ATOM   8565  N  ND2   . ASN B 1 371 ? 110.948 154.057 152.134 1.00 24.49 ?  371 ASN B ND2   1 
ATOM   8566  N  N     . HIS B 1 372 ? 113.482 158.490 149.565 1.00 19.85 ?  372 HIS B N     1 
ATOM   8567  C  CA    . HIS B 1 372 ? 113.454 159.579 148.596 1.00 19.82 ?  372 HIS B CA    1 
ATOM   8568  C  C     . HIS B 1 372 ? 114.544 159.406 147.546 1.00 22.75 ?  372 HIS B C     1 
ATOM   8569  O  O     . HIS B 1 372 ? 114.321 159.667 146.359 1.00 28.09 ?  372 HIS B O     1 
ATOM   8570  C  CB    . HIS B 1 372 ? 113.603 160.921 149.311 1.00 23.38 ?  372 HIS B CB    1 
ATOM   8571  C  CG    . HIS B 1 372 ? 114.939 161.112 149.958 1.00 22.20 ?  372 HIS B CG    1 
ATOM   8572  N  ND1   . HIS B 1 372 ? 115.381 160.325 150.999 1.00 21.74 ?  372 HIS B ND1   1 
ATOM   8573  C  CD2   . HIS B 1 372 ? 115.933 161.996 149.707 1.00 24.73 ?  372 HIS B CD2   1 
ATOM   8574  C  CE1   . HIS B 1 372 ? 116.590 160.714 151.360 1.00 20.00 ?  372 HIS B CE1   1 
ATOM   8575  N  NE2   . HIS B 1 372 ? 116.946 161.729 150.595 1.00 23.90 ?  372 HIS B NE2   1 
ATOM   8576  N  N     . ILE B 1 373 ? 115.736 158.983 147.969 1.00 16.66 ?  373 ILE B N     1 
ATOM   8577  C  CA    . ILE B 1 373 ? 116.811 158.715 147.018 1.00 19.92 ?  373 ILE B CA    1 
ATOM   8578  C  C     . ILE B 1 373 ? 116.429 157.555 146.113 1.00 21.25 ?  373 ILE B C     1 
ATOM   8579  O  O     . ILE B 1 373 ? 116.505 157.648 144.883 1.00 37.31 ?  373 ILE B O     1 
ATOM   8580  C  CB    . ILE B 1 373 ? 118.128 158.433 147.765 1.00 24.82 ?  373 ILE B CB    1 
ATOM   8581  C  CG1   . ILE B 1 373 ? 118.570 159.665 148.552 1.00 21.51 ?  373 ILE B CG1   1 
ATOM   8582  C  CG2   . ILE B 1 373 ? 119.212 157.995 146.795 1.00 21.97 ?  373 ILE B CG2   1 
ATOM   8583  C  CD1   . ILE B 1 373 ? 119.600 159.369 149.610 1.00 18.19 ?  373 ILE B CD1   1 
ATOM   8584  N  N     . SER B 1 374 ? 115.994 156.451 146.714 1.00 15.22 ?  374 SER B N     1 
ATOM   8585  C  CA    . SER B 1 374 ? 115.556 155.251 146.019 1.00 10.77 ?  374 SER B CA    1 
ATOM   8586  C  C     . SER B 1 374 ? 115.086 154.259 147.069 1.00 20.36 ?  374 SER B C     1 
ATOM   8587  O  O     . SER B 1 374 ? 115.451 154.356 148.244 1.00 23.07 ?  374 SER B O     1 
ATOM   8588  C  CB    . SER B 1 374 ? 116.672 154.634 145.173 1.00 21.86 ?  374 SER B CB    1 
ATOM   8589  O  OG    . SER B 1 374 ? 116.171 153.611 144.337 1.00 35.99 ?  374 SER B OG    1 
ATOM   8590  N  N     . LYS B 1 375 ? 114.270 153.307 146.636 1.00 26.47 ?  375 LYS B N     1 
ATOM   8591  C  CA    . LYS B 1 375 ? 113.976 152.161 147.476 1.00 12.12 ?  375 LYS B CA    1 
ATOM   8592  C  C     . LYS B 1 375 ? 115.149 151.187 147.442 1.00 15.13 ?  375 LYS B C     1 
ATOM   8593  O  O     . LYS B 1 375 ? 115.943 151.164 146.499 1.00 28.03 ?  375 LYS B O     1 
ATOM   8594  C  CB    . LYS B 1 375 ? 112.698 151.464 147.010 1.00 14.41 ?  375 LYS B CB    1 
ATOM   8595  C  CG    . LYS B 1 375 ? 111.460 152.339 147.034 1.00 18.59 ?  375 LYS B CG    1 
ATOM   8596  C  CD    . LYS B 1 375 ? 110.893 152.450 148.432 1.00 21.94 ?  375 LYS B CD    1 
ATOM   8597  C  CE    . LYS B 1 375 ? 109.379 152.518 148.409 1.00 23.73 ?  375 LYS B CE    1 
ATOM   8598  N  NZ    . LYS B 1 375 ? 108.898 153.923 148.340 1.00 26.61 1  375 LYS B NZ    1 
ATOM   8599  N  N     . VAL B 1 376 ? 115.263 150.384 148.493 1.00 12.10 ?  376 VAL B N     1 
ATOM   8600  C  CA    . VAL B 1 376 ? 116.248 149.308 148.510 1.00 13.01 ?  376 VAL B CA    1 
ATOM   8601  C  C     . VAL B 1 376 ? 115.700 148.162 147.672 1.00 15.90 ?  376 VAL B C     1 
ATOM   8602  O  O     . VAL B 1 376 ? 114.657 147.585 147.996 1.00 25.73 ?  376 VAL B O     1 
ATOM   8603  C  CB    . VAL B 1 376 ? 116.558 148.854 149.943 1.00 9.66  ?  376 VAL B CB    1 
ATOM   8604  C  CG1   . VAL B 1 376 ? 117.601 147.747 149.935 1.00 5.98  ?  376 VAL B CG1   1 
ATOM   8605  C  CG2   . VAL B 1 376 ? 117.021 150.027 150.784 1.00 6.35  ?  376 VAL B CG2   1 
ATOM   8606  N  N     . LYS B 1 377 ? 116.398 147.833 146.587 1.00 14.65 ?  377 LYS B N     1 
ATOM   8607  C  CA    . LYS B 1 377 ? 115.919 146.829 145.650 1.00 13.59 ?  377 LYS B CA    1 
ATOM   8608  C  C     . LYS B 1 377 ? 116.612 145.485 145.793 1.00 8.55  ?  377 LYS B C     1 
ATOM   8609  O  O     . LYS B 1 377 ? 116.052 144.474 145.360 1.00 25.31 ?  377 LYS B O     1 
ATOM   8610  C  CB    . LYS B 1 377 ? 116.092 147.320 144.210 1.00 16.40 ?  377 LYS B CB    1 
ATOM   8611  C  CG    . LYS B 1 377 ? 115.324 148.583 143.889 1.00 9.68  ?  377 LYS B CG    1 
ATOM   8612  C  CD    . LYS B 1 377 ? 115.975 149.312 142.736 1.00 20.92 ?  377 LYS B CD    1 
ATOM   8613  C  CE    . LYS B 1 377 ? 115.906 150.810 142.927 1.00 25.14 ?  377 LYS B CE    1 
ATOM   8614  N  NZ    . LYS B 1 377 ? 116.860 151.527 142.039 1.00 23.03 1  377 LYS B NZ    1 
ATOM   8615  N  N     . PHE B 1 378 ? 117.803 145.448 146.380 1.00 6.05  ?  378 PHE B N     1 
ATOM   8616  C  CA    . PHE B 1 378 ? 118.556 144.208 146.504 1.00 5.14  ?  378 PHE B CA    1 
ATOM   8617  C  C     . PHE B 1 378 ? 119.620 144.394 147.573 1.00 10.46 ?  378 PHE B C     1 
ATOM   8618  O  O     . PHE B 1 378 ? 119.821 145.490 148.098 1.00 14.98 ?  378 PHE B O     1 
ATOM   8619  C  CB    . PHE B 1 378 ? 119.170 143.784 145.164 1.00 2.96  ?  378 PHE B CB    1 
ATOM   8620  C  CG    . PHE B 1 378 ? 120.302 144.658 144.695 1.00 7.80  ?  378 PHE B CG    1 
ATOM   8621  C  CD1   . PHE B 1 378 ? 120.124 146.020 144.513 1.00 14.95 ?  378 PHE B CD1   1 
ATOM   8622  C  CD2   . PHE B 1 378 ? 121.539 144.109 144.407 1.00 4.48  ?  378 PHE B CD2   1 
ATOM   8623  C  CE1   . PHE B 1 378 ? 121.158 146.814 144.074 1.00 6.75  ?  378 PHE B CE1   1 
ATOM   8624  C  CE2   . PHE B 1 378 ? 122.576 144.901 143.964 1.00 7.80  ?  378 PHE B CE2   1 
ATOM   8625  C  CZ    . PHE B 1 378 ? 122.384 146.254 143.797 1.00 9.48  ?  378 PHE B CZ    1 
ATOM   8626  N  N     . SER B 1 379 ? 120.299 143.299 147.891 1.00 2.51  ?  379 SER B N     1 
ATOM   8627  C  CA    . SER B 1 379 ? 121.301 143.258 148.944 1.00 7.97  ?  379 SER B CA    1 
ATOM   8628  C  C     . SER B 1 379 ? 122.640 142.825 148.359 1.00 8.40  ?  379 SER B C     1 
ATOM   8629  O  O     . SER B 1 379 ? 122.787 142.641 147.150 1.00 19.01 ?  379 SER B O     1 
ATOM   8630  C  CB    . SER B 1 379 ? 120.864 142.320 150.071 1.00 6.80  ?  379 SER B CB    1 
ATOM   8631  O  OG    . SER B 1 379 ? 121.370 142.756 151.316 1.00 10.43 ?  379 SER B OG    1 
ATOM   8632  N  N     . ASN B 1 380 ? 123.623 142.663 149.237 1.00 10.17 ?  380 ASN B N     1 
ATOM   8633  C  CA    . ASN B 1 380 ? 124.975 142.321 148.829 1.00 7.85  ?  380 ASN B CA    1 
ATOM   8634  C  C     . ASN B 1 380 ? 125.146 140.803 148.813 1.00 13.89 ?  380 ASN B C     1 
ATOM   8635  O  O     . ASN B 1 380 ? 124.181 140.040 148.905 1.00 20.08 ?  380 ASN B O     1 
ATOM   8636  C  CB    . ASN B 1 380 ? 125.994 142.998 149.743 1.00 8.11  ?  380 ASN B CB    1 
ATOM   8637  C  CG    . ASN B 1 380 ? 125.917 142.507 151.169 1.00 8.77  ?  380 ASN B CG    1 
ATOM   8638  O  OD1   . ASN B 1 380 ? 124.832 142.320 151.714 1.00 22.19 ?  380 ASN B OD1   1 
ATOM   8639  N  ND2   . ASN B 1 380 ? 127.072 142.313 151.789 1.00 17.17 ?  380 ASN B ND2   1 
ATOM   8640  N  N     . LEU B 1 381 ? 126.393 140.353 148.679 1.00 19.78 ?  381 LEU B N     1 
ATOM   8641  C  CA    . LEU B 1 381 ? 126.688 138.927 148.668 1.00 8.77  ?  381 LEU B CA    1 
ATOM   8642  C  C     . LEU B 1 381 ? 126.465 138.281 150.029 1.00 6.62  ?  381 LEU B C     1 
ATOM   8643  O  O     . LEU B 1 381 ? 126.260 137.064 150.097 1.00 22.70 ?  381 LEU B O     1 
ATOM   8644  C  CB    . LEU B 1 381 ? 128.129 138.715 148.196 1.00 17.60 ?  381 LEU B CB    1 
ATOM   8645  C  CG    . LEU B 1 381 ? 128.756 137.320 148.188 1.00 20.47 ?  381 LEU B CG    1 
ATOM   8646  C  CD1   . LEU B 1 381 ? 128.007 136.382 147.262 1.00 22.72 ?  381 LEU B CD1   1 
ATOM   8647  C  CD2   . LEU B 1 381 ? 130.212 137.415 147.789 1.00 15.48 ?  381 LEU B CD2   1 
ATOM   8648  N  N     . CYS B 1 382 ? 126.485 139.062 151.105 1.00 21.44 ?  382 CYS B N     1 
ATOM   8649  C  CA    . CYS B 1 382 ? 126.285 138.544 152.451 1.00 3.70  ?  382 CYS B CA    1 
ATOM   8650  C  C     . CYS B 1 382 ? 124.926 138.906 153.032 1.00 12.64 ?  382 CYS B C     1 
ATOM   8651  O  O     . CYS B 1 382 ? 124.654 138.563 154.187 1.00 23.34 ?  382 CYS B O     1 
ATOM   8652  C  CB    . CYS B 1 382 ? 127.401 139.042 153.377 1.00 20.70 ?  382 CYS B CB    1 
ATOM   8653  S  SG    . CYS B 1 382 ? 129.075 138.696 152.787 1.00 37.09 ?  382 CYS B SG    1 
ATOM   8654  N  N     . SER B 1 383 ? 124.078 139.605 152.273 1.00 15.80 ?  383 SER B N     1 
ATOM   8655  C  CA    . SER B 1 383 ? 122.669 139.819 152.605 1.00 11.02 ?  383 SER B CA    1 
ATOM   8656  C  C     . SER B 1 383 ? 122.470 140.722 153.820 1.00 18.31 ?  383 SER B C     1 
ATOM   8657  O  O     . SER B 1 383 ? 121.484 140.579 154.545 1.00 27.77 ?  383 SER B O     1 
ATOM   8658  C  CB    . SER B 1 383 ? 121.939 138.489 152.818 1.00 8.16  ?  383 SER B CB    1 
ATOM   8659  O  OG    . SER B 1 383 ? 121.967 137.703 151.643 1.00 36.35 ?  383 SER B OG    1 
ATOM   8660  N  N     . GLU B 1 384 ? 123.381 141.659 154.066 1.00 11.76 ?  384 GLU B N     1 
ATOM   8661  C  CA    . GLU B 1 384 ? 123.196 142.612 155.150 1.00 9.89  ?  384 GLU B CA    1 
ATOM   8662  C  C     . GLU B 1 384 ? 123.240 144.066 154.706 1.00 16.66 ?  384 GLU B C     1 
ATOM   8663  O  O     . GLU B 1 384 ? 122.798 144.937 155.463 1.00 26.21 ?  384 GLU B O     1 
ATOM   8664  C  CB    . GLU B 1 384 ? 124.243 142.389 156.255 1.00 9.21  ?  384 GLU B CB    1 
ATOM   8665  C  CG    . GLU B 1 384 ? 125.454 143.298 156.184 1.00 11.23 ?  384 GLU B CG    1 
ATOM   8666  C  CD    . GLU B 1 384 ? 126.496 142.802 155.213 1.00 22.17 ?  384 GLU B CD    1 
ATOM   8667  O  OE1   . GLU B 1 384 ? 126.378 141.648 154.763 1.00 23.44 ?  384 GLU B OE1   1 
ATOM   8668  O  OE2   . GLU B 1 384 ? 127.436 143.562 154.908 1.00 29.48 -1 384 GLU B OE2   1 
ATOM   8669  N  N     . VAL B 1 385 ? 123.743 144.356 153.513 1.00 11.10 ?  385 VAL B N     1 
ATOM   8670  C  CA    . VAL B 1 385 ? 123.813 145.723 153.014 1.00 2.81  ?  385 VAL B CA    1 
ATOM   8671  C  C     . VAL B 1 385 ? 122.503 146.045 152.313 1.00 17.93 ?  385 VAL B C     1 
ATOM   8672  O  O     . VAL B 1 385 ? 122.148 145.409 151.316 1.00 25.12 ?  385 VAL B O     1 
ATOM   8673  C  CB    . VAL B 1 385 ? 125.005 145.908 152.066 1.00 5.27  ?  385 VAL B CB    1 
ATOM   8674  C  CG1   . VAL B 1 385 ? 124.970 147.286 151.460 1.00 8.53  ?  385 VAL B CG1   1 
ATOM   8675  C  CG2   . VAL B 1 385 ? 126.301 145.697 152.812 1.00 8.98  ?  385 VAL B CG2   1 
ATOM   8676  N  N     . LEU B 1 386 ? 121.778 147.033 152.839 1.00 19.30 ?  386 LEU B N     1 
ATOM   8677  C  CA    . LEU B 1 386 ? 120.464 147.422 152.329 1.00 2.15  ?  386 LEU B CA    1 
ATOM   8678  C  C     . LEU B 1 386 ? 120.448 148.939 152.188 1.00 5.61  ?  386 LEU B C     1 
ATOM   8679  O  O     . LEU B 1 386 ? 120.107 149.656 153.131 1.00 12.33 ?  386 LEU B O     1 
ATOM   8680  C  CB    . LEU B 1 386 ? 119.360 146.923 153.250 1.00 5.81  ?  386 LEU B CB    1 
ATOM   8681  C  CG    . LEU B 1 386 ? 119.258 145.401 153.331 1.00 0.77  ?  386 LEU B CG    1 
ATOM   8682  C  CD1   . LEU B 1 386 ? 118.235 144.998 154.357 1.00 7.88  ?  386 LEU B CD1   1 
ATOM   8683  C  CD2   . LEU B 1 386 ? 118.912 144.824 151.971 1.00 6.73  ?  386 LEU B CD2   1 
ATOM   8684  N  N     . GLN B 1 387 ? 120.817 149.425 151.006 1.00 13.17 ?  387 GLN B N     1 
ATOM   8685  C  CA    . GLN B 1 387 ? 120.945 150.849 150.751 1.00 3.15  ?  387 GLN B CA    1 
ATOM   8686  C  C     . GLN B 1 387 ? 120.261 151.208 149.440 1.00 8.38  ?  387 GLN B C     1 
ATOM   8687  O  O     . GLN B 1 387 ? 120.038 150.359 148.576 1.00 22.69 ?  387 GLN B O     1 
ATOM   8688  C  CB    . GLN B 1 387 ? 122.418 151.275 150.710 1.00 0.56  ?  387 GLN B CB    1 
ATOM   8689  C  CG    . GLN B 1 387 ? 123.202 150.863 151.935 1.00 4.37  ?  387 GLN B CG    1 
ATOM   8690  C  CD    . GLN B 1 387 ? 124.621 151.364 151.911 1.00 10.53 ?  387 GLN B CD    1 
ATOM   8691  O  OE1   . GLN B 1 387 ? 124.970 152.238 151.120 1.00 20.68 ?  387 GLN B OE1   1 
ATOM   8692  N  NE2   . GLN B 1 387 ? 125.454 150.813 152.778 1.00 9.52  ?  387 GLN B NE2   1 
ATOM   8693  N  N     . ALA B 1 388 ? 119.920 152.486 149.312 1.00 9.62  ?  388 ALA B N     1 
ATOM   8694  C  CA    . ALA B 1 388 ? 119.328 152.988 148.080 1.00 7.64  ?  388 ALA B CA    1 
ATOM   8695  C  C     . ALA B 1 388 ? 120.353 152.984 146.955 1.00 14.26 ?  388 ALA B C     1 
ATOM   8696  O  O     . ALA B 1 388 ? 121.519 153.337 147.151 1.00 25.40 ?  388 ALA B O     1 
ATOM   8697  C  CB    . ALA B 1 388 ? 118.784 154.399 148.289 1.00 11.59 ?  388 ALA B CB    1 
ATOM   8698  N  N     . SER B 1 389 ? 119.911 152.588 145.767 1.00 19.81 ?  389 SER B N     1 
ATOM   8699  C  CA    . SER B 1 389 ? 120.762 152.551 144.590 1.00 8.84  ?  389 SER B CA    1 
ATOM   8700  C  C     . SER B 1 389 ? 120.043 153.198 143.418 1.00 12.83 ?  389 SER B C     1 
ATOM   8701  O  O     . SER B 1 389 ? 118.813 153.185 143.337 1.00 23.31 ?  389 SER B O     1 
ATOM   8702  C  CB    . SER B 1 389 ? 121.158 151.116 144.224 1.00 17.11 ?  389 SER B CB    1 
ATOM   8703  O  OG    . SER B 1 389 ? 120.027 150.265 144.197 1.00 23.86 ?  389 SER B OG    1 
ATOM   8704  N  N     . GLN B 1 390 ? 120.827 153.765 142.508 1.00 22.95 ?  390 GLN B N     1 
ATOM   8705  C  CA    . GLN B 1 390 ? 120.312 154.330 141.270 1.00 12.92 ?  390 GLN B CA    1 
ATOM   8706  C  C     . GLN B 1 390 ? 121.064 153.698 140.113 1.00 14.09 ?  390 GLN B C     1 
ATOM   8707  O  O     . GLN B 1 390 ? 122.298 153.643 140.127 1.00 25.00 ?  390 GLN B O     1 
ATOM   8708  C  CB    . GLN B 1 390 ? 120.464 155.853 141.247 1.00 10.67 ?  390 GLN B CB    1 
ATOM   8709  C  CG    . GLN B 1 390 ? 119.523 156.568 142.194 1.00 11.92 ?  390 GLN B CG    1 
ATOM   8710  C  CD    . GLN B 1 390 ? 119.741 158.063 142.215 1.00 26.59 ?  390 GLN B CD    1 
ATOM   8711  O  OE1   . GLN B 1 390 ? 120.686 158.573 141.615 1.00 33.24 ?  390 GLN B OE1   1 
ATOM   8712  N  NE2   . GLN B 1 390 ? 118.867 158.776 142.914 1.00 18.02 ?  390 GLN B NE2   1 
ATOM   8713  N  N     . VAL B 1 391 ? 120.323 153.212 139.119 1.00 26.31 ?  391 VAL B N     1 
ATOM   8714  C  CA    . VAL B 1 391 ? 120.949 152.523 137.999 1.00 20.02 ?  391 VAL B CA    1 
ATOM   8715  C  C     . VAL B 1 391 ? 121.663 153.532 137.110 1.00 25.64 ?  391 VAL B C     1 
ATOM   8716  O  O     . VAL B 1 391 ? 121.202 154.665 136.920 1.00 22.59 ?  391 VAL B O     1 
ATOM   8717  C  CB    . VAL B 1 391 ? 119.904 151.706 137.217 1.00 15.69 ?  391 VAL B CB    1 
ATOM   8718  C  CG1   . VAL B 1 391 ? 118.957 152.616 136.449 1.00 16.52 ?  391 VAL B CG1   1 
ATOM   8719  C  CG2   . VAL B 1 391 ? 120.589 150.716 136.289 1.00 17.13 ?  391 VAL B CG2   1 
ATOM   8720  N  N     . SER B 1 392 ? 122.815 153.131 136.588 1.00 32.86 ?  392 SER B N     1 
ATOM   8721  C  CA    . SER B 1 392 ? 123.582 153.968 135.683 1.00 21.49 ?  392 SER B CA    1 
ATOM   8722  C  C     . SER B 1 392 ? 123.188 153.686 134.241 1.00 28.88 ?  392 SER B C     1 
ATOM   8723  O  O     . SER B 1 392 ? 122.852 152.557 133.877 1.00 31.81 ?  392 SER B O     1 
ATOM   8724  C  CB    . SER B 1 392 ? 125.082 153.736 135.866 1.00 25.83 ?  392 SER B CB    1 
ATOM   8725  O  OG    . SER B 1 392 ? 125.468 153.921 137.215 1.00 36.93 ?  392 SER B OG    1 
ATOM   8726  N  N     . SER B 1 393 ? 123.230 154.728 133.424 1.00 35.47 ?  393 SER B N     1 
ATOM   8727  C  CA    . SER B 1 393 ? 122.934 154.632 131.998 1.00 28.19 ?  393 SER B CA    1 
ATOM   8728  C  C     . SER B 1 393 ? 124.260 154.735 131.252 1.00 32.27 ?  393 SER B C     1 
ATOM   8729  O  O     . SER B 1 393 ? 124.699 155.826 130.882 1.00 35.82 ?  393 SER B O     1 
ATOM   8730  C  CB    . SER B 1 393 ? 121.956 155.715 131.565 1.00 31.94 ?  393 SER B CB    1 
ATOM   8731  O  OG    . SER B 1 393 ? 120.877 155.817 132.478 1.00 43.25 ?  393 SER B OG    1 
ATOM   8732  N  N     . TYR B 1 394 ? 124.899 153.589 131.038 1.00 32.45 ?  394 TYR B N     1 
ATOM   8733  C  CA    . TYR B 1 394 ? 126.146 153.539 130.283 1.00 29.04 ?  394 TYR B CA    1 
ATOM   8734  C  C     . TYR B 1 394 ? 125.808 153.544 128.799 1.00 30.77 ?  394 TYR B C     1 
ATOM   8735  O  O     . TYR B 1 394 ? 125.240 152.580 128.279 1.00 34.55 ?  394 TYR B O     1 
ATOM   8736  C  CB    . TYR B 1 394 ? 126.956 152.306 130.668 1.00 28.80 ?  394 TYR B CB    1 
ATOM   8737  C  CG    . TYR B 1 394 ? 127.386 152.292 132.116 1.00 28.49 ?  394 TYR B CG    1 
ATOM   8738  C  CD1   . TYR B 1 394 ? 128.384 153.142 132.573 1.00 29.28 ?  394 TYR B CD1   1 
ATOM   8739  C  CD2   . TYR B 1 394 ? 126.789 151.433 133.027 1.00 25.63 ?  394 TYR B CD2   1 
ATOM   8740  C  CE1   . TYR B 1 394 ? 128.778 153.134 133.895 1.00 29.53 ?  394 TYR B CE1   1 
ATOM   8741  C  CE2   . TYR B 1 394 ? 127.176 151.417 134.350 1.00 26.56 ?  394 TYR B CE2   1 
ATOM   8742  C  CZ    . TYR B 1 394 ? 128.169 152.268 134.779 1.00 36.49 ?  394 TYR B CZ    1 
ATOM   8743  O  OH    . TYR B 1 394 ? 128.554 152.252 136.100 1.00 40.21 ?  394 TYR B OH    1 
ATOM   8744  N  N     . THR B 1 395 ? 126.151 154.632 128.123 1.00 38.04 ?  395 THR B N     1 
ATOM   8745  C  CA    . THR B 1 395 ? 125.789 154.842 126.732 1.00 33.83 ?  395 THR B CA    1 
ATOM   8746  C  C     . THR B 1 395 ? 126.892 154.303 125.823 1.00 37.74 ?  395 THR B C     1 
ATOM   8747  O  O     . THR B 1 395 ? 127.790 153.578 126.258 1.00 34.98 ?  395 THR B O     1 
ATOM   8748  C  CB    . THR B 1 395 ? 125.518 156.322 126.487 1.00 36.13 ?  395 THR B CB    1 
ATOM   8749  O  OG1   . THR B 1 395 ? 126.710 157.072 126.749 1.00 37.24 ?  395 THR B OG1   1 
ATOM   8750  C  CG2   . THR B 1 395 ? 124.412 156.816 127.404 1.00 35.65 ?  395 THR B CG2   1 
ATOM   8751  N  N     . ASP B 1 396 ? 126.828 154.654 124.541 1.00 40.82 ?  396 ASP B N     1 
ATOM   8752  C  CA    . ASP B 1 396 ? 127.856 154.242 123.599 1.00 34.89 ?  396 ASP B CA    1 
ATOM   8753  C  C     . ASP B 1 396 ? 129.196 154.881 123.961 1.00 39.22 ?  396 ASP B C     1 
ATOM   8754  O  O     . ASP B 1 396 ? 129.288 155.763 124.818 1.00 46.61 ?  396 ASP B O     1 
ATOM   8755  C  CB    . ASP B 1 396 ? 127.454 154.612 122.172 1.00 39.86 ?  396 ASP B CB    1 
ATOM   8756  C  CG    . ASP B 1 396 ? 126.221 153.866 121.702 1.00 45.72 ?  396 ASP B CG    1 
ATOM   8757  O  OD1   . ASP B 1 396 ? 126.154 152.637 121.907 1.00 42.96 ?  396 ASP B OD1   1 
ATOM   8758  O  OD2   . ASP B 1 396 ? 125.321 154.508 121.122 1.00 46.25 -1 396 ASP B OD2   1 
ATOM   8759  N  N     . TYR B 1 397 ? 130.248 154.414 123.288 1.00 32.24 ?  397 TYR B N     1 
ATOM   8760  C  CA    . TYR B 1 397 ? 131.600 154.844 123.630 1.00 34.09 ?  397 TYR B CA    1 
ATOM   8761  C  C     . TYR B 1 397 ? 131.775 156.346 123.433 1.00 34.30 ?  397 TYR B C     1 
ATOM   8762  O  O     . TYR B 1 397 ? 132.414 157.015 124.253 1.00 41.35 ?  397 TYR B O     1 
ATOM   8763  C  CB    . TYR B 1 397 ? 132.621 154.065 122.800 1.00 32.22 ?  397 TYR B CB    1 
ATOM   8764  C  CG    . TYR B 1 397 ? 134.054 154.496 123.013 1.00 31.70 ?  397 TYR B CG    1 
ATOM   8765  C  CD1   . TYR B 1 397 ? 134.611 155.523 122.261 1.00 32.38 ?  397 TYR B CD1   1 
ATOM   8766  C  CD2   . TYR B 1 397 ? 134.851 153.874 123.962 1.00 28.43 ?  397 TYR B CD2   1 
ATOM   8767  C  CE1   . TYR B 1 397 ? 135.916 155.918 122.452 1.00 33.34 ?  397 TYR B CE1   1 
ATOM   8768  C  CE2   . TYR B 1 397 ? 136.159 154.263 124.159 1.00 30.86 ?  397 TYR B CE2   1 
ATOM   8769  C  CZ    . TYR B 1 397 ? 136.685 155.285 123.401 1.00 36.04 ?  397 TYR B CZ    1 
ATOM   8770  O  OH    . TYR B 1 397 ? 137.988 155.679 123.592 1.00 39.42 ?  397 TYR B OH    1 
ATOM   8771  N  N     . ASP B 1 398 ? 131.221 156.892 122.351 1.00 43.33 ?  398 ASP B N     1 
ATOM   8772  C  CA    . ASP B 1 398 ? 131.403 158.310 122.064 1.00 43.51 ?  398 ASP B CA    1 
ATOM   8773  C  C     . ASP B 1 398 ? 130.567 159.193 122.983 1.00 47.22 ?  398 ASP B C     1 
ATOM   8774  O  O     . ASP B 1 398 ? 130.935 160.344 123.236 1.00 49.56 ?  398 ASP B O     1 
ATOM   8775  C  CB    . ASP B 1 398 ? 131.064 158.598 120.603 1.00 45.31 ?  398 ASP B CB    1 
ATOM   8776  C  CG    . ASP B 1 398 ? 129.814 157.872 120.142 1.00 49.08 ?  398 ASP B CG    1 
ATOM   8777  O  OD1   . ASP B 1 398 ? 129.752 156.635 120.302 1.00 47.02 ?  398 ASP B OD1   1 
ATOM   8778  O  OD2   . ASP B 1 398 ? 128.896 158.536 119.618 1.00 51.13 -1 398 ASP B OD2   1 
ATOM   8779  N  N     . GLU B 1 399 ? 129.451 158.679 123.487 1.00 46.85 ?  399 GLU B N     1 
ATOM   8780  C  CA    . GLU B 1 399 ? 128.526 159.466 124.285 1.00 42.12 ?  399 GLU B CA    1 
ATOM   8781  C  C     . GLU B 1 399 ? 128.967 159.520 125.746 1.00 48.56 ?  399 GLU B C     1 
ATOM   8782  O  O     . GLU B 1 399 ? 129.878 158.811 126.179 1.00 48.89 ?  399 GLU B O     1 
ATOM   8783  C  CB    . GLU B 1 399 ? 127.113 158.895 124.177 1.00 44.22 ?  399 GLU B CB    1 
ATOM   8784  C  CG    . GLU B 1 399 ? 126.447 159.144 122.839 1.00 48.53 ?  399 GLU B CG    1 
ATOM   8785  C  CD    . GLU B 1 399 ? 125.403 158.101 122.509 1.00 52.02 ?  399 GLU B CD    1 
ATOM   8786  O  OE1   . GLU B 1 399 ? 124.809 157.537 123.451 1.00 50.37 ?  399 GLU B OE1   1 
ATOM   8787  O  OE2   . GLU B 1 399 ? 125.174 157.847 121.308 1.00 53.71 -1 399 GLU B OE2   1 
ATOM   8788  N  N     . GLU B 1 400 ? 128.301 160.384 126.507 1.00 47.89 ?  400 GLU B N     1 
ATOM   8789  C  CA    . GLU B 1 400 ? 128.575 160.550 127.928 1.00 41.02 ?  400 GLU B CA    1 
ATOM   8790  C  C     . GLU B 1 400 ? 127.639 159.668 128.742 1.00 44.36 ?  400 GLU B C     1 
ATOM   8791  O  O     . GLU B 1 400 ? 126.423 159.676 128.526 1.00 43.18 ?  400 GLU B O     1 
ATOM   8792  C  CB    . GLU B 1 400 ? 128.411 162.013 128.342 1.00 41.65 ?  400 GLU B CB    1 
ATOM   8793  C  CG    . GLU B 1 400 ? 129.631 162.880 128.086 1.00 47.55 ?  400 GLU B CG    1 
ATOM   8794  C  CD    . GLU B 1 400 ? 130.858 162.403 128.840 1.00 52.56 ?  400 GLU B CD    1 
ATOM   8795  O  OE1   . GLU B 1 400 ? 130.712 161.958 129.997 1.00 52.78 ?  400 GLU B OE1   1 
ATOM   8796  O  OE2   . GLU B 1 400 ? 131.969 162.478 128.275 1.00 49.93 -1 400 GLU B OE2   1 
ATOM   8797  N  N     . ASP B 1 401 ? 128.208 158.912 129.675 1.00 42.88 ?  401 ASP B N     1 
ATOM   8798  C  CA    . ASP B 1 401 ? 127.418 158.025 130.515 1.00 37.73 ?  401 ASP B CA    1 
ATOM   8799  C  C     . ASP B 1 401 ? 126.693 158.807 131.602 1.00 39.48 ?  401 ASP B C     1 
ATOM   8800  O  O     . ASP B 1 401 ? 127.155 159.855 132.061 1.00 43.20 ?  401 ASP B O     1 
ATOM   8801  C  CB    . ASP B 1 401 ? 128.306 156.960 131.159 1.00 37.41 ?  401 ASP B CB    1 
ATOM   8802  C  CG    . ASP B 1 401 ? 128.969 156.060 130.142 1.00 40.11 ?  401 ASP B CG    1 
ATOM   8803  O  OD1   . ASP B 1 401 ? 128.336 155.756 129.110 1.00 44.10 ?  401 ASP B OD1   1 
ATOM   8804  O  OD2   . ASP B 1 401 ? 130.126 155.656 130.374 1.00 40.53 -1 401 ASP B OD2   1 
ATOM   8805  N  N     . GLU B 1 402 ? 125.543 158.282 132.013 1.00 38.02 ?  402 GLU B N     1 
ATOM   8806  C  CA    . GLU B 1 402 ? 124.768 158.836 133.120 1.00 32.62 ?  402 GLU B CA    1 
ATOM   8807  C  C     . GLU B 1 402 ? 125.051 157.978 134.347 1.00 34.97 ?  402 GLU B C     1 
ATOM   8808  O  O     . GLU B 1 402 ? 124.473 156.903 134.516 1.00 39.72 ?  402 GLU B O     1 
ATOM   8809  C  CB    . GLU B 1 402 ? 123.280 158.867 132.787 1.00 37.87 ?  402 GLU B CB    1 
ATOM   8810  C  CG    . GLU B 1 402 ? 122.636 160.261 132.674 1.00 41.50 ?  402 GLU B CG    1 
ATOM   8811  C  CD    . GLU B 1 402 ? 122.748 161.148 133.919 1.00 48.02 ?  402 GLU B CD    1 
ATOM   8812  O  OE1   . GLU B 1 402 ? 121.985 162.134 133.989 1.00 46.69 ?  402 GLU B OE1   1 
ATOM   8813  O  OE2   . GLU B 1 402 ? 123.556 160.877 134.832 1.00 49.75 -1 402 GLU B OE2   1 
ATOM   8814  N  N     . ILE B 1 403 ? 125.940 158.462 135.206 1.00 32.50 ?  403 ILE B N     1 
ATOM   8815  C  CA    . ILE B 1 403 ? 126.404 157.685 136.349 1.00 28.63 ?  403 ILE B CA    1 
ATOM   8816  C  C     . ILE B 1 403 ? 125.382 157.777 137.474 1.00 31.15 ?  403 ILE B C     1 
ATOM   8817  O  O     . ILE B 1 403 ? 124.960 158.872 137.861 1.00 32.16 ?  403 ILE B O     1 
ATOM   8818  C  CB    . ILE B 1 403 ? 127.784 158.177 136.809 1.00 23.85 ?  403 ILE B CB    1 
ATOM   8819  C  CG1   . ILE B 1 403 ? 128.829 157.922 135.720 1.00 26.86 ?  403 ILE B CG1   1 
ATOM   8820  C  CG2   . ILE B 1 403 ? 128.177 157.509 138.106 1.00 23.30 ?  403 ILE B CG2   1 
ATOM   8821  C  CD1   . ILE B 1 403 ? 128.852 156.501 135.217 1.00 31.86 ?  403 ILE B CD1   1 
ATOM   8822  N  N     . GLY B 1 404 ? 124.984 156.626 137.998 1.00 26.12 ?  404 GLY B N     1 
ATOM   8823  C  CA    . GLY B 1 404 ? 124.076 156.524 139.120 1.00 14.51 ?  404 GLY B CA    1 
ATOM   8824  C  C     . GLY B 1 404 ? 124.801 156.287 140.427 1.00 21.90 ?  404 GLY B C     1 
ATOM   8825  O  O     . GLY B 1 404 ? 125.939 156.726 140.624 1.00 34.25 ?  404 GLY B O     1 
ATOM   8826  N  N     . LEU B 1 405 ? 124.134 155.582 141.338 1.00 25.58 ?  405 LEU B N     1 
ATOM   8827  C  CA    . LEU B 1 405 ? 124.688 155.261 142.648 1.00 9.14  ?  405 LEU B CA    1 
ATOM   8828  C  C     . LEU B 1 405 ? 124.723 153.751 142.815 1.00 12.56 ?  405 LEU B C     1 
ATOM   8829  O  O     . LEU B 1 405 ? 123.676 153.097 142.793 1.00 20.84 ?  405 LEU B O     1 
ATOM   8830  C  CB    . LEU B 1 405 ? 123.864 155.902 143.766 1.00 19.52 ?  405 LEU B CB    1 
ATOM   8831  C  CG    . LEU B 1 405 ? 123.730 157.424 143.745 1.00 17.62 ?  405 LEU B CG    1 
ATOM   8832  C  CD1   . LEU B 1 405 ? 122.775 157.885 144.828 1.00 25.45 ?  405 LEU B CD1   1 
ATOM   8833  C  CD2   . LEU B 1 405 ? 125.085 158.086 143.907 1.00 19.08 ?  405 LEU B CD2   1 
ATOM   8834  N  N     . ASP B 1 406 ? 125.922 153.202 142.993 1.00 24.10 ?  406 ASP B N     1 
ATOM   8835  C  CA    . ASP B 1 406 ? 126.110 151.789 143.281 1.00 12.26 ?  406 ASP B CA    1 
ATOM   8836  C  C     . ASP B 1 406 ? 126.650 151.633 144.696 1.00 23.28 ?  406 ASP B C     1 
ATOM   8837  O  O     . ASP B 1 406 ? 127.580 152.336 145.097 1.00 34.31 ?  406 ASP B O     1 
ATOM   8838  C  CB    . ASP B 1 406 ? 127.062 151.137 142.278 1.00 18.39 ?  406 ASP B CB    1 
ATOM   8839  C  CG    . ASP B 1 406 ? 126.398 150.843 140.948 1.00 35.02 ?  406 ASP B CG    1 
ATOM   8840  O  OD1   . ASP B 1 406 ? 125.170 151.035 140.833 1.00 37.66 ?  406 ASP B OD1   1 
ATOM   8841  O  OD2   . ASP B 1 406 ? 127.109 150.418 140.014 1.00 32.49 -1 406 ASP B OD2   1 
ATOM   8842  N  N     . ILE B 1 407 ? 126.078 150.697 145.436 1.00 30.17 ?  407 ILE B N     1 
ATOM   8843  C  CA    . ILE B 1 407 ? 126.297 150.615 146.875 1.00 17.45 ?  407 ILE B CA    1 
ATOM   8844  C  C     . ILE B 1 407 ? 127.649 149.983 147.173 1.00 16.83 ?  407 ILE B C     1 
ATOM   8845  O  O     . ILE B 1 407 ? 128.058 149.006 146.534 1.00 24.89 ?  407 ILE B O     1 
ATOM   8846  C  CB    . ILE B 1 407 ? 125.156 149.829 147.541 1.00 10.96 ?  407 ILE B CB    1 
ATOM   8847  C  CG1   . ILE B 1 407 ? 123.807 150.465 147.219 1.00 4.34  ?  407 ILE B CG1   1 
ATOM   8848  C  CG2   . ILE B 1 407 ? 125.358 149.766 149.027 1.00 16.64 ?  407 ILE B CG2   1 
ATOM   8849  C  CD1   . ILE B 1 407 ? 122.725 149.458 146.962 1.00 18.14 ?  407 ILE B CD1   1 
ATOM   8850  N  N     . SER B 1 408 ? 128.347 150.551 148.154 1.00 28.19 ?  408 SER B N     1 
ATOM   8851  C  CA    . SER B 1 408 ? 129.574 149.967 148.691 1.00 25.83 ?  408 SER B CA    1 
ATOM   8852  C  C     . SER B 1 408 ? 129.813 150.582 150.058 1.00 27.97 ?  408 SER B C     1 
ATOM   8853  O  O     . SER B 1 408 ? 130.077 151.785 150.152 1.00 38.52 ?  408 SER B O     1 
ATOM   8854  C  CB    . SER B 1 408 ? 130.759 150.226 147.764 1.00 30.99 ?  408 SER B CB    1 
ATOM   8855  O  OG    . SER B 1 408 ? 131.454 151.402 148.141 1.00 34.38 ?  408 SER B OG    1 
ATOM   8856  N  N     . CYS B 1 409 ? 129.722 149.777 151.111 1.00 21.98 ?  409 CYS B N     1 
ATOM   8857  C  CA    . CYS B 1 409 ? 129.873 150.277 152.468 1.00 31.49 ?  409 CYS B CA    1 
ATOM   8858  C  C     . CYS B 1 409 ? 131.045 149.593 153.159 1.00 26.72 ?  409 CYS B C     1 
ATOM   8859  O  O     . CYS B 1 409 ? 131.443 148.479 152.811 1.00 25.56 ?  409 CYS B O     1 
ATOM   8860  C  CB    . CYS B 1 409 ? 128.583 150.088 153.283 1.00 27.84 ?  409 CYS B CB    1 
ATOM   8861  S  SG    . CYS B 1 409 ? 128.462 148.558 154.225 1.00 38.82 ?  409 CYS B SG    1 
ATOM   8862  N  N     . ASN B 1 410 ? 131.599 150.289 154.146 1.00 22.62 ?  410 ASN B N     1 
ATOM   8863  C  CA    . ASN B 1 410 ? 132.786 149.849 154.864 1.00 22.90 ?  410 ASN B CA    1 
ATOM   8864  C  C     . ASN B 1 410 ? 132.363 149.156 156.150 1.00 24.05 ?  410 ASN B C     1 
ATOM   8865  O  O     . ASN B 1 410 ? 131.491 149.653 156.869 1.00 31.21 ?  410 ASN B O     1 
ATOM   8866  C  CB    . ASN B 1 410 ? 133.694 151.040 155.164 1.00 28.30 ?  410 ASN B CB    1 
ATOM   8867  C  CG    . ASN B 1 410 ? 133.633 152.097 154.081 1.00 37.57 ?  410 ASN B CG    1 
ATOM   8868  O  OD1   . ASN B 1 410 ? 134.587 152.279 153.327 1.00 42.49 ?  410 ASN B OD1   1 
ATOM   8869  N  ND2   . ASN B 1 410 ? 132.521 152.816 154.015 1.00 31.73 ?  410 ASN B ND2   1 
ATOM   8870  N  N     . LEU B 1 411 ? 132.985 148.019 156.439 1.00 16.74 ?  411 LEU B N     1 
ATOM   8871  C  CA    . LEU B 1 411 ? 132.537 147.134 157.504 1.00 9.81  ?  411 LEU B CA    1 
ATOM   8872  C  C     . LEU B 1 411 ? 133.424 147.250 158.735 1.00 13.17 ?  411 LEU B C     1 
ATOM   8873  O  O     . LEU B 1 411 ? 134.646 147.389 158.630 1.00 24.64 ?  411 LEU B O     1 
ATOM   8874  C  CB    . LEU B 1 411 ? 132.520 145.683 157.023 1.00 20.83 ?  411 LEU B CB    1 
ATOM   8875  C  CG    . LEU B 1 411 ? 131.669 145.347 155.803 1.00 19.90 ?  411 LEU B CG    1 
ATOM   8876  C  CD1   . LEU B 1 411 ? 131.386 143.866 155.767 1.00 25.47 ?  411 LEU B CD1   1 
ATOM   8877  C  CD2   . LEU B 1 411 ? 130.371 146.117 155.854 1.00 18.66 ?  411 LEU B CD2   1 
ATOM   8878  N  N     . GLY B 1 412 ? 132.789 147.204 159.902 1.00 18.40 ?  412 GLY B N     1 
ATOM   8879  C  CA    . GLY B 1 412 ? 133.491 147.095 161.164 1.00 4.64  ?  412 GLY B CA    1 
ATOM   8880  C  C     . GLY B 1 412 ? 132.577 146.431 162.168 1.00 11.43 ?  412 GLY B C     1 
ATOM   8881  O  O     . GLY B 1 412 ? 131.349 146.500 162.054 1.00 29.68 ?  412 GLY B O     1 
ATOM   8882  N  N     . SER B 1 413 ? 133.182 145.778 163.155 1.00 13.53 ?  413 SER B N     1 
ATOM   8883  C  CA    . SER B 1 413 ? 132.423 145.002 164.126 1.00 14.25 ?  413 SER B CA    1 
ATOM   8884  C  C     . SER B 1 413 ? 132.825 145.370 165.543 1.00 15.86 ?  413 SER B C     1 
ATOM   8885  O  O     . SER B 1 413 ? 134.010 145.337 165.886 1.00 23.31 ?  413 SER B O     1 
ATOM   8886  C  CB    . SER B 1 413 ? 132.620 143.501 163.908 1.00 10.59 ?  413 SER B CB    1 
ATOM   8887  O  OG    . SER B 1 413 ? 131.903 143.065 162.772 1.00 30.53 ?  413 SER B OG    1 
ATOM   8888  N  N     . LEU B 1 414 ? 131.836 145.718 166.358 1.00 17.46 ?  414 LEU B N     1 
ATOM   8889  C  CA    . LEU B 1 414 ? 132.049 145.810 167.793 1.00 9.58  ?  414 LEU B CA    1 
ATOM   8890  C  C     . LEU B 1 414 ? 132.077 144.415 168.398 1.00 20.99 ?  414 LEU B C     1 
ATOM   8891  O  O     . LEU B 1 414 ? 131.286 143.545 168.027 1.00 27.41 ?  414 LEU B O     1 
ATOM   8892  C  CB    . LEU B 1 414 ? 130.941 146.628 168.453 1.00 19.06 ?  414 LEU B CB    1 
ATOM   8893  C  CG    . LEU B 1 414 ? 130.537 147.957 167.821 1.00 20.59 ?  414 LEU B CG    1 
ATOM   8894  C  CD1   . LEU B 1 414 ? 129.291 148.482 168.501 1.00 23.38 ?  414 LEU B CD1   1 
ATOM   8895  C  CD2   . LEU B 1 414 ? 131.664 148.961 167.924 1.00 25.08 ?  414 LEU B CD2   1 
ATOM   8896  N  N     . ASN B 1 415 ? 132.998 144.201 169.327 1.00 30.18 ?  415 ASN B N     1 
ATOM   8897  C  CA    . ASN B 1 415 ? 132.999 142.992 170.140 1.00 26.52 ?  415 ASN B CA    1 
ATOM   8898  C  C     . ASN B 1 415 ? 132.085 143.247 171.332 1.00 24.97 ?  415 ASN B C     1 
ATOM   8899  O  O     . ASN B 1 415 ? 132.436 144.010 172.237 1.00 29.48 ?  415 ASN B O     1 
ATOM   8900  C  CB    . ASN B 1 415 ? 134.414 142.636 170.580 1.00 21.57 ?  415 ASN B CB    1 
ATOM   8901  C  CG    . ASN B 1 415 ? 134.534 141.210 171.070 1.00 21.47 ?  415 ASN B CG    1 
ATOM   8902  O  OD1   . ASN B 1 415 ? 133.769 140.767 171.925 1.00 37.85 ?  415 ASN B OD1   1 
ATOM   8903  N  ND2   . ASN B 1 415 ? 135.501 140.482 170.531 1.00 29.64 ?  415 ASN B ND2   1 
ATOM   8904  N  N     . ILE B 1 416 ? 130.909 142.617 171.324 1.00 17.78 ?  416 ILE B N     1 
ATOM   8905  C  CA    . ILE B 1 416 ? 129.899 142.902 172.340 1.00 21.17 ?  416 ILE B CA    1 
ATOM   8906  C  C     . ILE B 1 416 ? 130.417 142.545 173.727 1.00 28.90 ?  416 ILE B C     1 
ATOM   8907  O  O     . ILE B 1 416 ? 130.173 143.268 174.699 1.00 27.87 ?  416 ILE B O     1 
ATOM   8908  C  CB    . ILE B 1 416 ? 128.587 142.167 172.007 1.00 27.96 ?  416 ILE B CB    1 
ATOM   8909  C  CG1   . ILE B 1 416 ? 127.945 142.775 170.761 1.00 20.31 ?  416 ILE B CG1   1 
ATOM   8910  C  CG2   . ILE B 1 416 ? 127.619 142.225 173.172 1.00 9.74  ?  416 ILE B CG2   1 
ATOM   8911  C  CD1   . ILE B 1 416 ? 126.735 142.025 170.263 1.00 15.27 ?  416 ILE B CD1   1 
ATOM   8912  N  N     . LEU B 1 417 ? 131.152 141.438 173.841 1.00 21.36 ?  417 LEU B N     1 
ATOM   8913  C  CA    . LEU B 1 417 ? 131.690 141.038 175.138 1.00 26.32 ?  417 LEU B CA    1 
ATOM   8914  C  C     . LEU B 1 417 ? 132.693 142.061 175.663 1.00 30.42 ?  417 LEU B C     1 
ATOM   8915  O  O     . LEU B 1 417 ? 132.616 142.483 176.823 1.00 38.35 ?  417 LEU B O     1 
ATOM   8916  C  CB    . LEU B 1 417 ? 132.337 139.658 175.032 1.00 29.69 ?  417 LEU B CB    1 
ATOM   8917  C  CG    . LEU B 1 417 ? 133.145 139.178 176.238 1.00 30.91 ?  417 LEU B CG    1 
ATOM   8918  C  CD1   . LEU B 1 417 ? 132.239 138.554 177.282 1.00 28.98 ?  417 LEU B CD1   1 
ATOM   8919  C  CD2   . LEU B 1 417 ? 134.217 138.196 175.804 1.00 35.30 ?  417 LEU B CD2   1 
ATOM   8920  N  N     . ASN B 1 418 ? 133.637 142.480 174.818 1.00 30.35 ?  418 ASN B N     1 
ATOM   8921  C  CA    . ASN B 1 418 ? 134.669 143.412 175.255 1.00 27.79 ?  418 ASN B CA    1 
ATOM   8922  C  C     . ASN B 1 418 ? 134.133 144.827 175.425 1.00 29.87 ?  418 ASN B C     1 
ATOM   8923  O  O     . ASN B 1 418 ? 134.577 145.547 176.325 1.00 34.48 ?  418 ASN B O     1 
ATOM   8924  C  CB    . ASN B 1 418 ? 135.832 143.405 174.265 1.00 25.73 ?  418 ASN B CB    1 
ATOM   8925  C  CG    . ASN B 1 418 ? 136.631 142.122 174.323 1.00 26.42 ?  418 ASN B CG    1 
ATOM   8926  O  OD1   . ASN B 1 418 ? 136.796 141.531 175.388 1.00 34.90 ?  418 ASN B OD1   1 
ATOM   8927  N  ND2   . ASN B 1 418 ? 137.127 141.680 173.177 1.00 30.58 ?  418 ASN B ND2   1 
ATOM   8928  N  N     . VAL B 1 419 ? 133.195 145.242 174.573 1.00 32.67 ?  419 VAL B N     1 
ATOM   8929  C  CA    . VAL B 1 419 ? 132.566 146.546 174.740 1.00 31.64 ?  419 VAL B CA    1 
ATOM   8930  C  C     . VAL B 1 419 ? 131.735 146.574 176.015 1.00 30.72 ?  419 VAL B C     1 
ATOM   8931  O  O     . VAL B 1 419 ? 131.700 147.582 176.732 1.00 33.42 ?  419 VAL B O     1 
ATOM   8932  C  CB    . VAL B 1 419 ? 131.720 146.882 173.497 1.00 28.04 ?  419 VAL B CB    1 
ATOM   8933  C  CG1   . VAL B 1 419 ? 130.735 147.990 173.795 1.00 33.19 ?  419 VAL B CG1   1 
ATOM   8934  C  CG2   . VAL B 1 419 ? 132.618 147.267 172.339 1.00 24.47 ?  419 VAL B CG2   1 
ATOM   8935  N  N     . MET B 1 420 ? 131.073 145.462 176.331 1.00 36.25 ?  420 MET B N     1 
ATOM   8936  C  CA    . MET B 1 420 ? 130.219 145.406 177.509 1.00 33.76 ?  420 MET B CA    1 
ATOM   8937  C  C     . MET B 1 420 ? 131.045 145.343 178.788 1.00 31.81 ?  420 MET B C     1 
ATOM   8938  O  O     . MET B 1 420 ? 130.690 145.963 179.795 1.00 34.69 ?  420 MET B O     1 
ATOM   8939  C  CB    . MET B 1 420 ? 129.286 144.200 177.406 1.00 33.22 ?  420 MET B CB    1 
ATOM   8940  C  CG    . MET B 1 420 ? 127.905 144.517 176.857 1.00 24.56 ?  420 MET B CG    1 
ATOM   8941  S  SD    . MET B 1 420 ? 127.347 146.186 177.227 1.00 41.26 ?  420 MET B SD    1 
ATOM   8942  C  CE    . MET B 1 420 ? 126.594 145.923 178.824 1.00 33.19 ?  420 MET B CE    1 
ATOM   8943  N  N     . GLU B 1 421 ? 132.155 144.597 178.766 1.00 39.01 ?  421 GLU B N     1 
ATOM   8944  C  CA    . GLU B 1 421 ? 133.003 144.500 179.949 1.00 38.31 ?  421 GLU B CA    1 
ATOM   8945  C  C     . GLU B 1 421 ? 133.755 145.799 180.215 1.00 36.84 ?  421 GLU B C     1 
ATOM   8946  O  O     . GLU B 1 421 ? 134.065 146.106 181.371 1.00 39.33 ?  421 GLU B O     1 
ATOM   8947  C  CB    . GLU B 1 421 ? 133.976 143.327 179.805 1.00 33.75 ?  421 GLU B CB    1 
ATOM   8948  C  CG    . GLU B 1 421 ? 135.255 143.650 179.048 1.00 38.99 ?  421 GLU B CG    1 
ATOM   8949  C  CD    . GLU B 1 421 ? 136.293 142.550 179.148 1.00 46.20 ?  421 GLU B CD    1 
ATOM   8950  O  OE1   . GLU B 1 421 ? 137.074 142.551 180.122 1.00 43.21 ?  421 GLU B OE1   1 
ATOM   8951  O  OE2   . GLU B 1 421 ? 136.330 141.685 178.248 1.00 43.32 -1 421 GLU B OE2   1 
ATOM   8952  N  N     . HIS B 1 422 ? 134.058 146.569 179.171 1.00 36.68 ?  422 HIS B N     1 
ATOM   8953  C  CA    . HIS B 1 422 ? 134.723 147.855 179.329 1.00 37.50 ?  422 HIS B CA    1 
ATOM   8954  C  C     . HIS B 1 422 ? 133.751 148.999 179.581 1.00 41.79 ?  422 HIS B C     1 
ATOM   8955  O  O     . HIS B 1 422 ? 134.200 150.115 179.864 1.00 45.27 ?  422 HIS B O     1 
ATOM   8956  C  CB    . HIS B 1 422 ? 135.567 148.177 178.092 1.00 35.17 ?  422 HIS B CB    1 
ATOM   8957  C  CG    . HIS B 1 422 ? 136.913 147.523 178.087 1.00 38.00 ?  422 HIS B CG    1 
ATOM   8958  N  ND1   . HIS B 1 422 ? 137.077 146.159 177.985 1.00 39.87 ?  422 HIS B ND1   1 
ATOM   8959  C  CD2   . HIS B 1 422 ? 138.159 148.046 178.165 1.00 40.59 ?  422 HIS B CD2   1 
ATOM   8960  C  CE1   . HIS B 1 422 ? 138.366 145.868 178.005 1.00 41.07 ?  422 HIS B CE1   1 
ATOM   8961  N  NE2   . HIS B 1 422 ? 139.043 146.996 178.113 1.00 42.75 ?  422 HIS B NE2   1 
ATOM   8962  N  N     . LYS B 1 423 ? 132.444 148.747 179.486 1.00 43.51 ?  423 LYS B N     1 
ATOM   8963  C  CA    . LYS B 1 423 ? 131.420 149.775 179.670 1.00 44.04 ?  423 LYS B CA    1 
ATOM   8964  C  C     . LYS B 1 423 ? 131.657 150.957 178.734 1.00 47.14 ?  423 LYS B C     1 
ATOM   8965  O  O     . LYS B 1 423 ? 131.517 152.119 179.116 1.00 48.45 ?  423 LYS B O     1 
ATOM   8966  C  CB    . LYS B 1 423 ? 131.358 150.235 181.128 1.00 43.16 ?  423 LYS B CB    1 
ATOM   8967  C  CG    . LYS B 1 423 ? 130.733 149.226 182.073 1.00 44.78 ?  423 LYS B CG    1 
ATOM   8968  C  CD    . LYS B 1 423 ? 131.728 148.780 183.131 1.00 48.99 ?  423 LYS B CD    1 
ATOM   8969  C  CE    . LYS B 1 423 ? 131.211 147.579 183.907 1.00 47.55 ?  423 LYS B CE    1 
ATOM   8970  N  NZ    . LYS B 1 423 ? 131.656 146.291 183.305 1.00 42.92 1  423 LYS B NZ    1 
ATOM   8971  N  N     . SER B 1 424 ? 132.013 150.651 177.491 1.00 32.45 ?  424 SER B N     1 
ATOM   8972  C  CA    . SER B 1 424 ? 132.438 151.651 176.519 1.00 32.35 ?  424 SER B CA    1 
ATOM   8973  C  C     . SER B 1 424 ? 131.654 151.515 175.223 1.00 36.47 ?  424 SER B C     1 
ATOM   8974  O  O     . SER B 1 424 ? 132.221 151.463 174.132 1.00 38.35 ?  424 SER B O     1 
ATOM   8975  C  CB    . SER B 1 424 ? 133.935 151.538 176.250 1.00 36.99 ?  424 SER B CB    1 
ATOM   8976  O  OG    . SER B 1 424 ? 134.238 150.345 175.550 1.00 34.67 ?  424 SER B OG    1 
ATOM   8977  N  N     . ILE B 1 425 ? 130.325 151.445 175.322 1.00 35.88 ?  425 ILE B N     1 
ATOM   8978  C  CA    . ILE B 1 425 ? 129.506 151.417 174.112 1.00 28.36 ?  425 ILE B CA    1 
ATOM   8979  C  C     . ILE B 1 425 ? 129.662 152.720 173.340 1.00 34.18 ?  425 ILE B C     1 
ATOM   8980  O  O     . ILE B 1 425 ? 129.909 152.721 172.131 1.00 39.14 ?  425 ILE B O     1 
ATOM   8981  C  CB    . ILE B 1 425 ? 128.032 151.143 174.458 1.00 33.41 ?  425 ILE B CB    1 
ATOM   8982  C  CG1   . ILE B 1 425 ? 127.853 149.714 174.965 1.00 33.95 ?  425 ILE B CG1   1 
ATOM   8983  C  CG2   . ILE B 1 425 ? 127.150 151.385 173.244 1.00 29.70 ?  425 ILE B CG2   1 
ATOM   8984  C  CD1   . ILE B 1 425 ? 126.420 149.356 175.270 1.00 34.91 ?  425 ILE B CD1   1 
ATOM   8985  N  N     . GLU B 1 426 ? 129.548 153.851 174.040 1.00 32.69 ?  426 GLU B N     1 
ATOM   8986  C  CA    . GLU B 1 426 ? 129.605 155.149 173.374 1.00 31.07 ?  426 GLU B CA    1 
ATOM   8987  C  C     . GLU B 1 426 ? 130.962 155.384 172.724 1.00 31.81 ?  426 GLU B C     1 
ATOM   8988  O  O     . GLU B 1 426 ? 131.045 155.721 171.537 1.00 42.23 ?  426 GLU B O     1 
ATOM   8989  C  CB    . GLU B 1 426 ? 129.290 156.256 174.378 1.00 32.52 ?  426 GLU B CB    1 
ATOM   8990  C  CG    . GLU B 1 426 ? 129.696 157.644 173.924 1.00 33.06 ?  426 GLU B CG    1 
ATOM   8991  C  CD    . GLU B 1 426 ? 129.531 158.678 175.016 1.00 42.02 ?  426 GLU B CD    1 
ATOM   8992  O  OE1   . GLU B 1 426 ? 129.206 158.290 176.157 1.00 42.80 ?  426 GLU B OE1   1 
ATOM   8993  O  OE2   . GLU B 1 426 ? 129.731 159.878 174.738 1.00 46.74 -1 426 GLU B OE2   1 
ATOM   8994  N  N     . LYS B 1 427 ? 132.041 155.207 173.490 1.00 33.13 ?  427 LYS B N     1 
ATOM   8995  C  CA    . LYS B 1 427 ? 133.374 155.501 172.977 1.00 31.12 ?  427 LYS B CA    1 
ATOM   8996  C  C     . LYS B 1 427 ? 133.750 154.560 171.841 1.00 32.71 ?  427 LYS B C     1 
ATOM   8997  O  O     . LYS B 1 427 ? 134.279 155.001 170.814 1.00 37.83 ?  427 LYS B O     1 
ATOM   8998  C  CB    . LYS B 1 427 ? 134.427 155.431 174.093 1.00 34.87 ?  427 LYS B CB    1 
ATOM   8999  C  CG    . LYS B 1 427 ? 134.425 156.571 175.139 1.00 41.24 ?  427 LYS B CG    1 
ATOM   9000  C  CD    . LYS B 1 427 ? 133.173 156.716 176.020 1.00 40.26 ?  427 LYS B CD    1 
ATOM   9001  C  CE    . LYS B 1 427 ? 132.564 155.377 176.430 1.00 36.14 ?  427 LYS B CE    1 
ATOM   9002  N  NZ    . LYS B 1 427 ? 131.460 155.534 177.414 1.00 40.00 1  427 LYS B NZ    1 
ATOM   9003  N  N     . THR B 1 428 ? 133.488 153.262 172.005 1.00 28.98 ?  428 THR B N     1 
ATOM   9004  C  CA    . THR B 1 428 ? 133.803 152.313 170.943 1.00 24.30 ?  428 THR B CA    1 
ATOM   9005  C  C     . THR B 1 428 ? 132.984 152.592 169.692 1.00 26.69 ?  428 THR B C     1 
ATOM   9006  O  O     . THR B 1 428 ? 133.515 152.547 168.578 1.00 34.84 ?  428 THR B O     1 
ATOM   9007  C  CB    . THR B 1 428 ? 133.575 150.877 171.415 1.00 21.44 ?  428 THR B CB    1 
ATOM   9008  O  OG1   . THR B 1 428 ? 134.229 150.675 172.673 1.00 25.87 ?  428 THR B OG1   1 
ATOM   9009  C  CG2   . THR B 1 428 ? 134.128 149.898 170.399 1.00 27.34 ?  428 THR B CG2   1 
ATOM   9010  N  N     . VAL B 1 429 ? 131.692 152.888 169.853 1.00 26.34 ?  429 VAL B N     1 
ATOM   9011  C  CA    . VAL B 1 429 ? 130.849 153.160 168.693 1.00 23.04 ?  429 VAL B CA    1 
ATOM   9012  C  C     . VAL B 1 429 ? 131.339 154.398 167.957 1.00 24.84 ?  429 VAL B C     1 
ATOM   9013  O  O     . VAL B 1 429 ? 131.438 154.405 166.724 1.00 30.08 ?  429 VAL B O     1 
ATOM   9014  C  CB    . VAL B 1 429 ? 129.374 153.299 169.118 1.00 24.85 ?  429 VAL B CB    1 
ATOM   9015  C  CG1   . VAL B 1 429 ? 128.593 154.066 168.074 1.00 23.31 ?  429 VAL B CG1   1 
ATOM   9016  C  CG2   . VAL B 1 429 ? 128.751 151.936 169.323 1.00 26.10 ?  429 VAL B CG2   1 
ATOM   9017  N  N     . LYS B 1 430 ? 131.675 155.458 168.694 1.00 29.56 ?  430 LYS B N     1 
ATOM   9018  C  CA    . LYS B 1 430 ? 132.096 156.693 168.044 1.00 24.43 ?  430 LYS B CA    1 
ATOM   9019  C  C     . LYS B 1 430 ? 133.456 156.541 167.370 1.00 23.08 ?  430 LYS B C     1 
ATOM   9020  O  O     . LYS B 1 430 ? 133.657 157.033 166.253 1.00 31.25 ?  430 LYS B O     1 
ATOM   9021  C  CB    . LYS B 1 430 ? 132.105 157.836 169.057 1.00 26.41 ?  430 LYS B CB    1 
ATOM   9022  C  CG    . LYS B 1 430 ? 130.710 158.213 169.528 1.00 23.26 ?  430 LYS B CG    1 
ATOM   9023  C  CD    . LYS B 1 430 ? 130.697 159.529 170.276 1.00 31.44 ?  430 LYS B CD    1 
ATOM   9024  C  CE    . LYS B 1 430 ? 129.277 159.940 170.615 1.00 34.84 ?  430 LYS B CE    1 
ATOM   9025  N  NZ    . LYS B 1 430 ? 129.237 161.187 171.423 1.00 36.10 1  430 LYS B NZ    1 
ATOM   9026  N  N     . LEU B 1 431 ? 134.400 155.854 168.019 1.00 30.77 ?  431 LEU B N     1 
ATOM   9027  C  CA    . LEU B 1 431 ? 135.702 155.636 167.394 1.00 22.41 ?  431 LEU B CA    1 
ATOM   9028  C  C     . LEU B 1 431 ? 135.588 154.730 166.174 1.00 23.25 ?  431 LEU B C     1 
ATOM   9029  O  O     . LEU B 1 431 ? 136.269 154.949 165.166 1.00 32.08 ?  431 LEU B O     1 
ATOM   9030  C  CB    . LEU B 1 431 ? 136.680 155.054 168.412 1.00 30.91 ?  431 LEU B CB    1 
ATOM   9031  C  CG    . LEU B 1 431 ? 137.559 156.055 169.160 1.00 32.90 ?  431 LEU B CG    1 
ATOM   9032  C  CD1   . LEU B 1 431 ? 138.338 155.356 170.260 1.00 28.93 ?  431 LEU B CD1   1 
ATOM   9033  C  CD2   . LEU B 1 431 ? 138.499 156.763 168.203 1.00 34.52 ?  431 LEU B CD2   1 
ATOM   9034  N  N     . ALA B 1 432 ? 134.738 153.701 166.247 1.00 25.20 ?  432 ALA B N     1 
ATOM   9035  C  CA    . ALA B 1 432 ? 134.508 152.844 165.092 1.00 20.02 ?  432 ALA B CA    1 
ATOM   9036  C  C     . ALA B 1 432 ? 133.869 153.623 163.952 1.00 25.84 ?  432 ALA B C     1 
ATOM   9037  O  O     . ALA B 1 432 ? 134.208 153.412 162.783 1.00 29.63 ?  432 ALA B O     1 
ATOM   9038  C  CB    . ALA B 1 432 ? 133.634 151.657 165.490 1.00 24.13 ?  432 ALA B CB    1 
ATOM   9039  N  N     . THR B 1 433 ? 132.939 154.524 164.274 1.00 27.18 ?  433 THR B N     1 
ATOM   9040  C  CA    . THR B 1 433 ? 132.346 155.380 163.254 1.00 17.25 ?  433 THR B CA    1 
ATOM   9041  C  C     . THR B 1 433 ? 133.401 156.265 162.604 1.00 25.04 ?  433 THR B C     1 
ATOM   9042  O  O     . THR B 1 433 ? 133.407 156.438 161.381 1.00 33.17 ?  433 THR B O     1 
ATOM   9043  C  CB    . THR B 1 433 ? 131.233 156.230 163.869 1.00 24.03 ?  433 THR B CB    1 
ATOM   9044  O  OG1   . THR B 1 433 ? 130.254 155.374 164.468 1.00 32.99 ?  433 THR B OG1   1 
ATOM   9045  C  CG2   . THR B 1 433 ? 130.563 157.091 162.811 1.00 24.11 ?  433 THR B CG2   1 
ATOM   9046  N  N     . ASP B 1 434 ? 134.305 156.830 163.407 1.00 24.94 ?  434 ASP B N     1 
ATOM   9047  C  CA    . ASP B 1 434 ? 135.377 157.653 162.853 1.00 18.95 ?  434 ASP B CA    1 
ATOM   9048  C  C     . ASP B 1 434 ? 136.283 156.841 161.934 1.00 19.23 ?  434 ASP B C     1 
ATOM   9049  O  O     . ASP B 1 434 ? 136.660 157.305 160.850 1.00 26.71 ?  434 ASP B O     1 
ATOM   9050  C  CB    . ASP B 1 434 ? 136.189 158.285 163.981 1.00 25.35 ?  434 ASP B CB    1 
ATOM   9051  C  CG    . ASP B 1 434 ? 135.423 159.355 164.722 1.00 31.05 ?  434 ASP B CG    1 
ATOM   9052  O  OD1   . ASP B 1 434 ? 134.530 159.977 164.111 1.00 36.85 ?  434 ASP B OD1   1 
ATOM   9053  O  OD2   . ASP B 1 434 ? 135.713 159.576 165.915 1.00 33.18 -1 434 ASP B OD2   1 
ATOM   9054  N  N     . SER B 1 435 ? 136.645 155.626 162.349 1.00 22.83 ?  435 SER B N     1 
ATOM   9055  C  CA    . SER B 1 435 ? 137.515 154.788 161.527 1.00 15.90 ?  435 SER B CA    1 
ATOM   9056  C  C     . SER B 1 435 ? 136.829 154.379 160.229 1.00 23.26 ?  435 SER B C     1 
ATOM   9057  O  O     . SER B 1 435 ? 137.453 154.385 159.160 1.00 31.44 ?  435 SER B O     1 
ATOM   9058  C  CB    . SER B 1 435 ? 137.954 153.556 162.317 1.00 21.15 ?  435 SER B CB    1 
ATOM   9059  O  OG    . SER B 1 435 ? 136.870 152.672 162.534 1.00 22.23 ?  435 SER B OG    1 
ATOM   9060  N  N     . LEU B 1 436 ? 135.548 154.016 160.300 1.00 18.81 ?  436 LEU B N     1 
ATOM   9061  C  CA    . LEU B 1 436 ? 134.807 153.657 159.096 1.00 11.47 ?  436 LEU B CA    1 
ATOM   9062  C  C     . LEU B 1 436 ? 134.654 154.853 158.169 1.00 19.15 ?  436 LEU B C     1 
ATOM   9063  O  O     . LEU B 1 436 ? 134.731 154.710 156.943 1.00 31.33 ?  436 LEU B O     1 
ATOM   9064  C  CB    . LEU B 1 436 ? 133.443 153.087 159.476 1.00 22.51 ?  436 LEU B CB    1 
ATOM   9065  C  CG    . LEU B 1 436 ? 133.464 151.713 160.140 1.00 18.95 ?  436 LEU B CG    1 
ATOM   9066  C  CD1   . LEU B 1 436 ? 132.166 151.457 160.877 1.00 16.54 ?  436 LEU B CD1   1 
ATOM   9067  C  CD2   . LEU B 1 436 ? 133.721 150.636 159.110 1.00 20.71 ?  436 LEU B CD2   1 
ATOM   9068  N  N     . THR B 1 437 ? 134.442 156.043 158.733 1.00 22.48 ?  437 THR B N     1 
ATOM   9069  C  CA    . THR B 1 437 ? 134.401 157.254 157.924 1.00 19.89 ?  437 THR B CA    1 
ATOM   9070  C  C     . THR B 1 437 ? 135.730 157.485 157.220 1.00 24.99 ?  437 THR B C     1 
ATOM   9071  O  O     . THR B 1 437 ? 135.758 157.823 156.032 1.00 35.50 ?  437 THR B O     1 
ATOM   9072  C  CB    . THR B 1 437 ? 134.042 158.455 158.797 1.00 15.98 ?  437 THR B CB    1 
ATOM   9073  O  OG1   . THR B 1 437 ? 132.801 158.203 159.465 1.00 16.78 ?  437 THR B OG1   1 
ATOM   9074  C  CG2   . THR B 1 437 ? 133.911 159.707 157.954 1.00 21.42 ?  437 THR B CG2   1 
ATOM   9075  N  N     . HIS B 1 438 ? 136.843 157.308 157.936 1.00 18.58 ?  438 HIS B N     1 
ATOM   9076  C  CA    . HIS B 1 438 ? 138.153 157.468 157.312 1.00 18.73 ?  438 HIS B CA    1 
ATOM   9077  C  C     . HIS B 1 438 ? 138.350 156.469 156.179 1.00 20.69 ?  438 HIS B C     1 
ATOM   9078  O  O     . HIS B 1 438 ? 138.856 156.825 155.107 1.00 32.55 ?  438 HIS B O     1 
ATOM   9079  C  CB    . HIS B 1 438 ? 139.261 157.316 158.353 1.00 25.97 ?  438 HIS B CB    1 
ATOM   9080  C  CG    . HIS B 1 438 ? 140.638 157.336 157.770 1.00 28.78 ?  438 HIS B CG    1 
ATOM   9081  N  ND1   . HIS B 1 438 ? 141.324 158.505 157.521 1.00 26.69 ?  438 HIS B ND1   1 
ATOM   9082  C  CD2   . HIS B 1 438 ? 141.453 156.331 157.371 1.00 30.25 ?  438 HIS B CD2   1 
ATOM   9083  C  CE1   . HIS B 1 438 ? 142.504 158.220 157.001 1.00 27.89 ?  438 HIS B CE1   1 
ATOM   9084  N  NE2   . HIS B 1 438 ? 142.607 156.908 156.898 1.00 30.94 ?  438 HIS B NE2   1 
ATOM   9085  N  N     . VAL B 1 439 ? 137.956 155.213 156.397 1.00 23.92 ?  439 VAL B N     1 
ATOM   9086  C  CA    . VAL B 1 439 ? 138.078 154.205 155.348 1.00 17.52 ?  439 VAL B CA    1 
ATOM   9087  C  C     . VAL B 1 439 ? 137.227 154.589 154.144 1.00 27.55 ?  439 VAL B C     1 
ATOM   9088  O  O     . VAL B 1 439 ? 137.633 154.399 152.991 1.00 34.37 ?  439 VAL B O     1 
ATOM   9089  C  CB    . VAL B 1 439 ? 137.700 152.815 155.893 1.00 22.88 ?  439 VAL B CB    1 
ATOM   9090  C  CG1   . VAL B 1 439 ? 137.645 151.794 154.769 1.00 25.20 ?  439 VAL B CG1   1 
ATOM   9091  C  CG2   . VAL B 1 439 ? 138.686 152.379 156.954 1.00 21.17 ?  439 VAL B CG2   1 
ATOM   9092  N  N     . SER B 1 440 ? 136.035 155.133 154.392 1.00 27.83 ?  440 SER B N     1 
ATOM   9093  C  CA    . SER B 1 440 ? 135.172 155.565 153.297 1.00 17.71 ?  440 SER B CA    1 
ATOM   9094  C  C     . SER B 1 440 ? 135.805 156.699 152.501 1.00 23.44 ?  440 SER B C     1 
ATOM   9095  O  O     . SER B 1 440 ? 135.784 156.684 151.265 1.00 33.92 ?  440 SER B O     1 
ATOM   9096  C  CB    . SER B 1 440 ? 133.810 155.987 153.848 1.00 26.57 ?  440 SER B CB    1 
ATOM   9097  O  OG    . SER B 1 440 ? 132.861 156.147 152.809 1.00 33.83 ?  440 SER B OG    1 
ATOM   9098  N  N     . GLU B 1 441 ? 136.370 157.695 153.189 1.00 24.94 ?  441 GLU B N     1 
ATOM   9099  C  CA    . GLU B 1 441 ? 136.984 158.820 152.482 1.00 20.17 ?  441 GLU B CA    1 
ATOM   9100  C  C     . GLU B 1 441 ? 138.222 158.391 151.706 1.00 29.91 ?  441 GLU B C     1 
ATOM   9101  O  O     . GLU B 1 441 ? 138.456 158.872 150.592 1.00 41.35 ?  441 GLU B O     1 
ATOM   9102  C  CB    . GLU B 1 441 ? 137.335 159.955 153.446 1.00 22.01 ?  441 GLU B CB    1 
ATOM   9103  C  CG    . GLU B 1 441 ? 136.289 160.276 154.491 1.00 30.91 ?  441 GLU B CG    1 
ATOM   9104  C  CD    . GLU B 1 441 ? 134.998 160.799 153.894 1.00 42.82 ?  441 GLU B CD    1 
ATOM   9105  O  OE1   . GLU B 1 441 ? 134.928 162.008 153.593 1.00 39.73 ?  441 GLU B OE1   1 
ATOM   9106  O  OE2   . GLU B 1 441 ? 134.050 160.003 153.728 1.00 47.27 -1 441 GLU B OE2   1 
ATOM   9107  N  N     . THR B 1 442 ? 139.028 157.495 152.269 1.00 32.89 ?  442 THR B N     1 
ATOM   9108  C  CA    . THR B 1 442 ? 140.274 157.113 151.616 1.00 29.78 ?  442 THR B CA    1 
ATOM   9109  C  C     . THR B 1 442 ? 140.081 156.073 150.522 1.00 29.77 ?  442 THR B C     1 
ATOM   9110  O  O     . THR B 1 442 ? 141.061 155.694 149.872 1.00 38.02 ?  442 THR B O     1 
ATOM   9111  C  CB    . THR B 1 442 ? 141.279 156.591 152.648 1.00 31.77 ?  442 THR B CB    1 
ATOM   9112  O  OG1   . THR B 1 442 ? 140.746 155.431 153.297 1.00 38.47 ?  442 THR B OG1   1 
ATOM   9113  C  CG2   . THR B 1 442 ? 141.577 157.660 153.683 1.00 28.66 ?  442 THR B CG2   1 
ATOM   9114  N  N     . THR B 1 443 ? 138.858 155.606 150.297 1.00 33.92 ?  443 THR B N     1 
ATOM   9115  C  CA    . THR B 1 443 ? 138.580 154.633 149.250 1.00 37.93 ?  443 THR B CA    1 
ATOM   9116  C  C     . THR B 1 443 ? 138.255 155.365 147.954 1.00 38.05 ?  443 THR B C     1 
ATOM   9117  O  O     . THR B 1 443 ? 137.326 156.178 147.910 1.00 39.87 ?  443 THR B O     1 
ATOM   9118  C  CB    . THR B 1 443 ? 137.424 153.719 149.650 1.00 36.18 ?  443 THR B CB    1 
ATOM   9119  O  OG1   . THR B 1 443 ? 137.752 153.033 150.863 1.00 40.97 ?  443 THR B OG1   1 
ATOM   9120  C  CG2   . THR B 1 443 ? 137.158 152.698 148.557 1.00 29.03 ?  443 THR B CG2   1 
ATOM   9121  N  N     . ASP B 1 444 ? 139.020 155.076 146.904 1.00 46.08 ?  444 ASP B N     1 
ATOM   9122  C  CA    . ASP B 1 444 ? 138.773 155.630 145.575 1.00 44.30 ?  444 ASP B CA    1 
ATOM   9123  C  C     . ASP B 1 444 ? 138.939 154.504 144.566 1.00 47.74 ?  444 ASP B C     1 
ATOM   9124  O  O     . ASP B 1 444 ? 140.039 153.966 144.410 1.00 49.21 ?  444 ASP B O     1 
ATOM   9125  C  CB    . ASP B 1 444 ? 139.719 156.790 145.267 1.00 47.29 ?  444 ASP B CB    1 
ATOM   9126  C  CG    . ASP B 1 444 ? 139.116 157.791 144.302 1.00 51.21 ?  444 ASP B CG    1 
ATOM   9127  O  OD1   . ASP B 1 444 ? 138.009 158.295 144.582 1.00 48.14 ?  444 ASP B OD1   1 
ATOM   9128  O  OD2   . ASP B 1 444 ? 139.749 158.075 143.264 1.00 52.79 -1 444 ASP B OD2   1 
ATOM   9129  N  N     . ILE B 1 445 ? 137.854 154.149 143.885 1.00 38.65 ?  445 ILE B N     1 
ATOM   9130  C  CA    . ILE B 1 445 ? 137.848 153.053 142.925 1.00 40.61 ?  445 ILE B CA    1 
ATOM   9131  C  C     . ILE B 1 445 ? 137.734 153.655 141.531 1.00 45.93 ?  445 ILE B C     1 
ATOM   9132  O  O     . ILE B 1 445 ? 136.771 154.371 141.231 1.00 48.01 ?  445 ILE B O     1 
ATOM   9133  C  CB    . ILE B 1 445 ? 136.710 152.063 143.214 1.00 38.89 ?  445 ILE B CB    1 
ATOM   9134  C  CG1   . ILE B 1 445 ? 137.160 151.049 144.264 1.00 38.21 ?  445 ILE B CG1   1 
ATOM   9135  C  CG2   . ILE B 1 445 ? 136.304 151.328 141.952 1.00 41.28 ?  445 ILE B CG2   1 
ATOM   9136  C  CD1   . ILE B 1 445 ? 136.064 150.615 145.195 1.00 37.47 ?  445 ILE B CD1   1 
ATOM   9137  N  N     . ARG B 1 446 ? 138.720 153.372 140.683 1.00 46.10 ?  446 ARG B N     1 
ATOM   9138  C  CA    . ARG B 1 446 ? 138.880 154.081 139.422 1.00 46.88 ?  446 ARG B CA    1 
ATOM   9139  C  C     . ARG B 1 446 ? 138.145 153.436 138.256 1.00 48.00 ?  446 ARG B C     1 
ATOM   9140  O  O     . ARG B 1 446 ? 138.114 154.021 137.168 1.00 43.19 ?  446 ARG B O     1 
ATOM   9141  C  CB    . ARG B 1 446 ? 140.370 154.202 139.076 1.00 43.09 ?  446 ARG B CB    1 
ATOM   9142  C  CG    . ARG B 1 446 ? 141.285 154.358 140.284 1.00 41.76 ?  446 ARG B CG    1 
ATOM   9143  C  CD    . ARG B 1 446 ? 141.067 155.634 141.111 1.00 46.98 ?  446 ARG B CD    1 
ATOM   9144  N  NE    . ARG B 1 446 ? 141.301 156.874 140.377 1.00 48.53 ?  446 ARG B NE    1 
ATOM   9145  C  CZ    . ARG B 1 446 ? 140.383 157.557 139.704 1.00 49.20 ?  446 ARG B CZ    1 
ATOM   9146  N  NH1   . ARG B 1 446 ? 139.112 157.192 139.699 1.00 45.47 1  446 ARG B NH1   1 
ATOM   9147  N  NH2   . ARG B 1 446 ? 140.747 158.651 139.041 1.00 41.80 ?  446 ARG B NH2   1 
ATOM   9148  N  N     . ASN B 1 447 ? 137.553 152.258 138.443 1.00 37.86 ?  447 ASN B N     1 
ATOM   9149  C  CA    . ASN B 1 447 ? 136.892 151.560 137.351 1.00 30.21 ?  447 ASN B CA    1 
ATOM   9150  C  C     . ASN B 1 447 ? 135.422 151.276 137.614 1.00 33.78 ?  447 ASN B C     1 
ATOM   9151  O  O     . ASN B 1 447 ? 134.782 150.602 136.800 1.00 41.74 ?  447 ASN B O     1 
ATOM   9152  C  CB    . ASN B 1 447 ? 137.622 150.249 137.040 1.00 35.06 ?  447 ASN B CB    1 
ATOM   9153  C  CG    . ASN B 1 447 ? 138.706 150.425 136.000 1.00 33.26 ?  447 ASN B CG    1 
ATOM   9154  O  OD1   . ASN B 1 447 ? 138.422 150.612 134.819 1.00 39.91 ?  447 ASN B OD1   1 
ATOM   9155  N  ND2   . ASN B 1 447 ? 139.957 150.371 136.436 1.00 29.19 ?  447 ASN B ND2   1 
ATOM   9156  N  N     . ALA B 1 448 ? 134.869 151.762 138.723 1.00 35.20 ?  448 ALA B N     1 
ATOM   9157  C  CA    . ALA B 1 448 ? 133.443 151.665 139.026 1.00 30.98 ?  448 ALA B CA    1 
ATOM   9158  C  C     . ALA B 1 448 ? 132.947 153.077 139.298 1.00 34.36 ?  448 ALA B C     1 
ATOM   9159  O  O     . ALA B 1 448 ? 132.950 153.533 140.451 1.00 35.04 ?  448 ALA B O     1 
ATOM   9160  C  CB    . ALA B 1 448 ? 133.187 150.743 140.214 1.00 26.58 ?  448 ALA B CB    1 
ATOM   9161  N  N     . PRO B 1 449 ? 132.528 153.812 138.264 1.00 32.91 ?  449 PRO B N     1 
ATOM   9162  C  CA    . PRO B 1 449 ? 132.163 155.222 138.482 1.00 25.26 ?  449 PRO B CA    1 
ATOM   9163  C  C     . PRO B 1 449 ? 130.972 155.397 139.403 1.00 30.13 ?  449 PRO B C     1 
ATOM   9164  O  O     . PRO B 1 449 ? 130.945 156.345 140.196 1.00 29.44 ?  449 PRO B O     1 
ATOM   9165  C  CB    . PRO B 1 449 ? 131.873 155.743 137.067 1.00 27.13 ?  449 PRO B CB    1 
ATOM   9166  C  CG    . PRO B 1 449 ? 132.030 154.580 136.139 1.00 30.35 ?  449 PRO B CG    1 
ATOM   9167  C  CD    . PRO B 1 449 ? 132.139 153.330 136.930 1.00 24.54 ?  449 PRO B CD    1 
ATOM   9168  N  N     . ALA B 1 450 ? 129.983 154.504 139.323 1.00 32.95 ?  450 ALA B N     1 
ATOM   9169  C  CA    . ALA B 1 450 ? 128.819 154.617 140.194 1.00 19.72 ?  450 ALA B CA    1 
ATOM   9170  C  C     . ALA B 1 450 ? 129.175 154.284 141.635 1.00 27.50 ?  450 ALA B C     1 
ATOM   9171  O  O     . ALA B 1 450 ? 128.687 154.932 142.566 1.00 33.23 ?  450 ALA B O     1 
ATOM   9172  C  CB    . ALA B 1 450 ? 127.697 153.713 139.688 1.00 23.31 ?  450 ALA B CB    1 
ATOM   9173  N  N     . VAL B 1 451 ? 130.037 153.285 141.839 1.00 29.00 ?  451 VAL B N     1 
ATOM   9174  C  CA    . VAL B 1 451 ? 130.485 152.948 143.188 1.00 19.78 ?  451 VAL B CA    1 
ATOM   9175  C  C     . VAL B 1 451 ? 131.240 154.120 143.798 1.00 24.03 ?  451 VAL B C     1 
ATOM   9176  O  O     . VAL B 1 451 ? 131.019 154.489 144.957 1.00 36.06 ?  451 VAL B O     1 
ATOM   9177  C  CB    . VAL B 1 451 ? 131.349 151.674 143.165 1.00 28.00 ?  451 VAL B CB    1 
ATOM   9178  C  CG1   . VAL B 1 451 ? 132.174 151.562 144.434 1.00 28.64 ?  451 VAL B CG1   1 
ATOM   9179  C  CG2   . VAL B 1 451 ? 130.482 150.445 142.984 1.00 23.50 ?  451 VAL B CG2   1 
ATOM   9180  N  N     . ARG B 1 452 ? 132.141 154.726 143.024 1.00 25.98 ?  452 ARG B N     1 
ATOM   9181  C  CA    . ARG B 1 452 ? 132.905 155.868 143.519 1.00 23.15 ?  452 ARG B CA    1 
ATOM   9182  C  C     . ARG B 1 452 ? 132.000 157.059 143.811 1.00 22.13 ?  452 ARG B C     1 
ATOM   9183  O  O     . ARG B 1 452 ? 132.149 157.727 144.843 1.00 36.39 ?  452 ARG B O     1 
ATOM   9184  C  CB    . ARG B 1 452 ? 133.988 156.239 142.506 1.00 23.46 ?  452 ARG B CB    1 
ATOM   9185  C  CG    . ARG B 1 452 ? 134.844 157.427 142.898 1.00 31.33 ?  452 ARG B CG    1 
ATOM   9186  C  CD    . ARG B 1 452 ? 135.171 158.286 141.688 1.00 29.52 ?  452 ARG B CD    1 
ATOM   9187  N  NE    . ARG B 1 452 ? 134.139 158.192 140.662 1.00 41.86 ?  452 ARG B NE    1 
ATOM   9188  C  CZ    . ARG B 1 452 ? 133.116 159.028 140.544 1.00 41.89 ?  452 ARG B CZ    1 
ATOM   9189  N  NH1   . ARG B 1 452 ? 132.960 160.052 141.367 1.00 34.62 1  452 ARG B NH1   1 
ATOM   9190  N  NH2   . ARG B 1 452 ? 132.225 158.830 139.576 1.00 28.38 ?  452 ARG B NH2   1 
ATOM   9191  N  N     . ARG B 1 453 ? 131.045 157.336 142.919 1.00 23.37 ?  453 ARG B N     1 
ATOM   9192  C  CA    . ARG B 1 453 ? 130.129 158.450 143.135 1.00 22.37 ?  453 ARG B CA    1 
ATOM   9193  C  C     . ARG B 1 453 ? 129.280 158.233 144.380 1.00 29.71 ?  453 ARG B C     1 
ATOM   9194  O  O     . ARG B 1 453 ? 129.079 159.161 145.172 1.00 32.37 ?  453 ARG B O     1 
ATOM   9195  C  CB    . ARG B 1 453 ? 129.243 158.647 141.905 1.00 25.06 ?  453 ARG B CB    1 
ATOM   9196  C  CG    . ARG B 1 453 ? 128.078 159.595 142.125 1.00 25.17 ?  453 ARG B CG    1 
ATOM   9197  C  CD    . ARG B 1 453 ? 127.469 160.042 140.812 1.00 24.76 ?  453 ARG B CD    1 
ATOM   9198  N  NE    . ARG B 1 453 ? 126.059 159.682 140.716 1.00 27.52 ?  453 ARG B NE    1 
ATOM   9199  C  CZ    . ARG B 1 453 ? 125.065 160.401 141.219 1.00 29.14 ?  453 ARG B CZ    1 
ATOM   9200  N  NH1   . ARG B 1 453 ? 125.289 161.531 141.868 1.00 30.68 1  453 ARG B NH1   1 
ATOM   9201  N  NH2   . ARG B 1 453 ? 123.816 159.975 141.067 1.00 25.55 ?  453 ARG B NH2   1 
ATOM   9202  N  N     . ALA B 1 454 ? 128.778 157.012 144.576 1.00 31.94 ?  454 ALA B N     1 
ATOM   9203  C  CA    . ALA B 1 454 ? 127.963 156.734 145.751 1.00 20.44 ?  454 ALA B CA    1 
ATOM   9204  C  C     . ALA B 1 454 ? 128.792 156.741 147.026 1.00 20.06 ?  454 ALA B C     1 
ATOM   9205  O  O     . ALA B 1 454 ? 128.289 157.129 148.082 1.00 29.70 ?  454 ALA B O     1 
ATOM   9206  C  CB    . ALA B 1 454 ? 127.242 155.399 145.590 1.00 22.79 ?  454 ALA B CB    1 
ATOM   9207  N  N     . ASN B 1 455 ? 130.053 156.314 146.957 1.00 26.92 ?  455 ASN B N     1 
ATOM   9208  C  CA    . ASN B 1 455 ? 130.920 156.409 148.124 1.00 20.39 ?  455 ASN B CA    1 
ATOM   9209  C  C     . ASN B 1 455 ? 131.172 157.863 148.498 1.00 26.77 ?  455 ASN B C     1 
ATOM   9210  O  O     . ASN B 1 455 ? 131.188 158.213 149.683 1.00 39.86 ?  455 ASN B O     1 
ATOM   9211  C  CB    . ASN B 1 455 ? 132.237 155.681 147.859 1.00 20.18 ?  455 ASN B CB    1 
ATOM   9212  C  CG    . ASN B 1 455 ? 133.140 155.647 149.076 1.00 29.85 ?  455 ASN B CG    1 
ATOM   9213  O  OD1   . ASN B 1 455 ? 132.853 154.962 150.054 1.00 38.69 ?  455 ASN B OD1   1 
ATOM   9214  N  ND2   . ASN B 1 455 ? 134.238 156.389 149.019 1.00 29.79 ?  455 ASN B ND2   1 
ATOM   9215  N  N     . LYS B 1 456 ? 131.373 158.724 147.499 1.00 27.60 ?  456 LYS B N     1 
ATOM   9216  C  CA    . LYS B 1 456 ? 131.607 160.135 147.782 1.00 26.83 ?  456 LYS B CA    1 
ATOM   9217  C  C     . LYS B 1 456 ? 130.347 160.836 148.275 1.00 26.99 ?  456 LYS B C     1 
ATOM   9218  O  O     . LYS B 1 456 ? 130.430 161.731 149.121 1.00 31.45 ?  456 LYS B O     1 
ATOM   9219  C  CB    . LYS B 1 456 ? 132.150 160.834 146.536 1.00 24.22 ?  456 LYS B CB    1 
ATOM   9220  C  CG    . LYS B 1 456 ? 133.158 161.928 146.835 1.00 29.52 ?  456 LYS B CG    1 
ATOM   9221  C  CD    . LYS B 1 456 ? 132.499 163.297 146.843 1.00 35.87 ?  456 LYS B CD    1 
ATOM   9222  C  CE    . LYS B 1 456 ? 133.442 164.366 147.372 1.00 37.12 ?  456 LYS B CE    1 
ATOM   9223  N  NZ    . LYS B 1 456 ? 133.368 164.489 148.855 1.00 31.89 1  456 LYS B NZ    1 
ATOM   9224  N  N     . ALA B 1 457 ? 129.179 160.452 147.763 1.00 25.36 ?  457 ALA B N     1 
ATOM   9225  C  CA    . ALA B 1 457 ? 127.937 161.151 148.069 1.00 17.19 ?  457 ALA B CA    1 
ATOM   9226  C  C     . ALA B 1 457 ? 127.263 160.629 149.333 1.00 23.78 ?  457 ALA B C     1 
ATOM   9227  O  O     . ALA B 1 457 ? 126.955 161.406 150.242 1.00 27.47 ?  457 ALA B O     1 
ATOM   9228  C  CB    . ALA B 1 457 ? 126.977 161.040 146.882 1.00 20.86 ?  457 ALA B CB    1 
ATOM   9229  N  N     . MET B 1 458 ? 127.024 159.320 149.398 1.00 34.34 ?  458 MET B N     1 
ATOM   9230  C  CA    . MET B 1 458 ? 126.275 158.733 150.502 1.00 17.01 ?  458 MET B CA    1 
ATOM   9231  C  C     . MET B 1 458 ? 127.102 158.670 151.779 1.00 25.08 ?  458 MET B C     1 
ATOM   9232  O  O     . MET B 1 458 ? 126.561 158.856 152.875 1.00 33.26 ?  458 MET B O     1 
ATOM   9233  C  CB    . MET B 1 458 ? 125.793 157.337 150.113 1.00 18.15 ?  458 MET B CB    1 
ATOM   9234  C  CG    . MET B 1 458 ? 125.049 157.274 148.785 1.00 21.57 ?  458 MET B CG    1 
ATOM   9235  S  SD    . MET B 1 458 ? 123.266 157.502 148.937 1.00 35.77 ?  458 MET B SD    1 
ATOM   9236  C  CE    . MET B 1 458 ? 123.139 159.287 148.917 1.00 27.87 ?  458 MET B CE    1 
ATOM   9237  N  N     . LYS B 1 459 ? 128.403 158.406 151.658 1.00 15.58 ?  459 LYS B N     1 
ATOM   9238  C  CA    . LYS B 1 459 ? 129.290 158.255 152.812 1.00 18.95 ?  459 LYS B CA    1 
ATOM   9239  C  C     . LYS B 1 459 ? 128.761 157.197 153.776 1.00 20.49 ?  459 LYS B C     1 
ATOM   9240  O  O     . LYS B 1 459 ? 128.838 157.341 154.997 1.00 32.27 ?  459 LYS B O     1 
ATOM   9241  C  CB    . LYS B 1 459 ? 129.498 159.591 153.530 1.00 26.05 ?  459 LYS B CB    1 
ATOM   9242  C  CG    . LYS B 1 459 ? 129.988 160.713 152.637 1.00 31.44 ?  459 LYS B CG    1 
ATOM   9243  C  CD    . LYS B 1 459 ? 129.288 162.016 152.973 1.00 23.51 ?  459 LYS B CD    1 
ATOM   9244  C  CE    . LYS B 1 459 ? 129.669 163.114 152.002 1.00 27.85 ?  459 LYS B CE    1 
ATOM   9245  N  NZ    . LYS B 1 459 ? 128.977 164.392 152.315 1.00 33.22 1  459 LYS B NZ    1 
ATOM   9246  N  N     . SER B 1 460 ? 128.216 156.120 153.220 1.00 16.22 ?  460 SER B N     1 
ATOM   9247  C  CA    . SER B 1 460 ? 127.616 155.074 154.030 1.00 9.49  ?  460 SER B CA    1 
ATOM   9248  C  C     . SER B 1 460 ? 128.685 154.156 154.606 1.00 19.62 ?  460 SER B C     1 
ATOM   9249  O  O     . SER B 1 460 ? 129.663 153.816 153.935 1.00 32.72 ?  460 SER B O     1 
ATOM   9250  C  CB    . SER B 1 460 ? 126.624 154.258 153.204 1.00 17.17 ?  460 SER B CB    1 
ATOM   9251  O  OG    . SER B 1 460 ? 127.297 153.469 152.242 1.00 26.49 ?  460 SER B OG    1 
ATOM   9252  N  N     . ILE B 1 461 ? 128.490 153.756 155.861 1.00 19.65 ?  461 ILE B N     1 
ATOM   9253  C  CA    . ILE B 1 461 ? 129.384 152.837 156.546 1.00 15.15 ?  461 ILE B CA    1 
ATOM   9254  C  C     . ILE B 1 461 ? 128.548 151.711 157.131 1.00 20.77 ?  461 ILE B C     1 
ATOM   9255  O  O     . ILE B 1 461 ? 127.332 151.826 157.291 1.00 23.59 ?  461 ILE B O     1 
ATOM   9256  C  CB    . ILE B 1 461 ? 130.205 153.529 157.655 1.00 12.55 ?  461 ILE B CB    1 
ATOM   9257  C  CG1   . ILE B 1 461 ? 129.273 154.191 158.670 1.00 7.21  ?  461 ILE B CG1   1 
ATOM   9258  C  CG2   . ILE B 1 461 ? 131.157 154.549 157.056 1.00 18.35 ?  461 ILE B CG2   1 
ATOM   9259  C  CD1   . ILE B 1 461 ? 129.953 154.598 159.949 1.00 12.29 ?  461 ILE B CD1   1 
ATOM   9260  N  N     . GLY B 1 462 ? 129.211 150.600 157.425 1.00 20.59 ?  462 GLY B N     1 
ATOM   9261  C  CA    . GLY B 1 462 ? 128.546 149.532 158.138 1.00 9.98  ?  462 GLY B CA    1 
ATOM   9262  C  C     . GLY B 1 462 ? 129.266 149.170 159.416 1.00 11.74 ?  462 GLY B C     1 
ATOM   9263  O  O     . GLY B 1 462 ? 130.363 148.610 159.378 1.00 27.20 ?  462 GLY B O     1 
ATOM   9264  N  N     . LEU B 1 463 ? 128.654 149.469 160.555 1.00 12.75 ?  463 LEU B N     1 
ATOM   9265  C  CA    . LEU B 1 463 ? 129.203 149.115 161.858 1.00 8.74  ?  463 LEU B CA    1 
ATOM   9266  C  C     . LEU B 1 463 ? 128.398 147.947 162.407 1.00 20.47 ?  463 LEU B C     1 
ATOM   9267  O  O     . LEU B 1 463 ? 127.249 148.117 162.826 1.00 28.83 ?  463 LEU B O     1 
ATOM   9268  C  CB    . LEU B 1 463 ? 129.171 150.306 162.812 1.00 18.78 ?  463 LEU B CB    1 
ATOM   9269  C  CG    . LEU B 1 463 ? 129.615 150.002 164.244 1.00 16.77 ?  463 LEU B CG    1 
ATOM   9270  C  CD1   . LEU B 1 463 ? 131.025 149.444 164.250 1.00 3.19  ?  463 LEU B CD1   1 
ATOM   9271  C  CD2   . LEU B 1 463 ? 129.519 151.242 165.116 1.00 16.93 ?  463 LEU B CD2   1 
ATOM   9272  N  N     . GLY B 1 464 ? 129.001 146.760 162.404 1.00 22.67 ?  464 GLY B N     1 
ATOM   9273  C  CA    . GLY B 1 464 ? 128.358 145.564 162.894 1.00 13.17 ?  464 GLY B CA    1 
ATOM   9274  C  C     . GLY B 1 464 ? 128.719 145.256 164.334 1.00 9.46  ?  464 GLY B C     1 
ATOM   9275  O  O     . GLY B 1 464 ? 129.383 146.029 165.029 1.00 18.19 ?  464 GLY B O     1 
ATOM   9276  N  N     . ALA B 1 465 ? 128.260 144.093 164.783 1.00 15.21 ?  465 ALA B N     1 
ATOM   9277  C  CA    . ALA B 1 465 ? 128.561 143.597 166.114 1.00 8.92  ?  465 ALA B CA    1 
ATOM   9278  C  C     . ALA B 1 465 ? 128.794 142.098 166.029 1.00 16.15 ?  465 ALA B C     1 
ATOM   9279  O  O     . ALA B 1 465 ? 128.331 141.428 165.105 1.00 33.48 ?  465 ALA B O     1 
ATOM   9280  C  CB    . ALA B 1 465 ? 127.436 143.910 167.108 1.00 18.90 ?  465 ALA B CB    1 
ATOM   9281  N  N     . MET B 1 466 ? 129.528 141.580 167.006 1.00 22.79 ?  466 MET B N     1 
ATOM   9282  C  CA    . MET B 1 466 ? 129.822 140.158 167.075 1.00 19.06 ?  466 MET B CA    1 
ATOM   9283  C  C     . MET B 1 466 ? 129.938 139.766 168.540 1.00 18.39 ?  466 MET B C     1 
ATOM   9284  O  O     . MET B 1 466 ? 129.868 140.612 169.435 1.00 23.63 ?  466 MET B O     1 
ATOM   9285  C  CB    . MET B 1 466 ? 131.096 139.820 166.297 1.00 24.49 ?  466 MET B CB    1 
ATOM   9286  C  CG    . MET B 1 466 ? 132.365 140.230 167.008 1.00 27.81 ?  466 MET B CG    1 
ATOM   9287  S  SD    . MET B 1 466 ? 133.807 140.248 165.934 1.00 41.52 ?  466 MET B SD    1 
ATOM   9288  C  CE    . MET B 1 466 ? 134.770 141.509 166.751 1.00 25.51 ?  466 MET B CE    1 
ATOM   9289  N  N     . ASN B 1 467 ? 130.110 138.465 168.778 1.00 16.44 ?  467 ASN B N     1 
ATOM   9290  C  CA    . ASN B 1 467 ? 130.238 137.908 170.125 1.00 22.64 ?  467 ASN B CA    1 
ATOM   9291  C  C     . ASN B 1 467 ? 128.982 138.139 170.958 1.00 26.97 ?  467 ASN B C     1 
ATOM   9292  O  O     . ASN B 1 467 ? 129.058 138.318 172.174 1.00 26.62 ?  467 ASN B O     1 
ATOM   9293  C  CB    . ASN B 1 467 ? 131.466 138.467 170.851 1.00 21.75 ?  467 ASN B CB    1 
ATOM   9294  C  CG    . ASN B 1 467 ? 132.151 137.432 171.712 1.00 27.21 ?  467 ASN B CG    1 
ATOM   9295  O  OD1   . ASN B 1 467 ? 131.779 136.260 171.708 1.00 27.28 ?  467 ASN B OD1   1 
ATOM   9296  N  ND2   . ASN B 1 467 ? 133.164 137.858 172.453 1.00 30.72 ?  467 ASN B ND2   1 
ATOM   9297  N  N     . LEU B 1 468 ? 127.817 138.153 170.311 1.00 17.65 ?  468 LEU B N     1 
ATOM   9298  C  CA    . LEU B 1 468 ? 126.568 138.245 171.059 1.00 14.70 ?  468 LEU B CA    1 
ATOM   9299  C  C     . LEU B 1 468 ? 126.312 136.965 171.844 1.00 29.01 ?  468 LEU B C     1 
ATOM   9300  O  O     . LEU B 1 468 ? 126.040 137.006 173.049 1.00 33.40 ?  468 LEU B O     1 
ATOM   9301  C  CB    . LEU B 1 468 ? 125.407 138.534 170.109 1.00 24.99 ?  468 LEU B CB    1 
ATOM   9302  C  CG    . LEU B 1 468 ? 124.028 138.627 170.766 1.00 19.41 ?  468 LEU B CG    1 
ATOM   9303  C  CD1   . LEU B 1 468 ? 124.006 139.729 171.809 1.00 16.93 ?  468 LEU B CD1   1 
ATOM   9304  C  CD2   . LEU B 1 468 ? 122.945 138.845 169.728 1.00 16.14 ?  468 LEU B CD2   1 
ATOM   9305  N  N     . HIS B 1 469 ? 126.417 135.815 171.176 1.00 31.57 ?  469 HIS B N     1 
ATOM   9306  C  CA    . HIS B 1 469 ? 126.194 134.548 171.861 1.00 16.43 ?  469 HIS B CA    1 
ATOM   9307  C  C     . HIS B 1 469 ? 127.288 134.273 172.879 1.00 27.60 ?  469 HIS B C     1 
ATOM   9308  O  O     . HIS B 1 469 ? 127.016 133.732 173.953 1.00 38.08 ?  469 HIS B O     1 
ATOM   9309  C  CB    . HIS B 1 469 ? 126.101 133.404 170.853 1.00 15.93 ?  469 HIS B CB    1 
ATOM   9310  C  CG    . HIS B 1 469 ? 125.504 132.155 171.422 1.00 20.95 ?  469 HIS B CG    1 
ATOM   9311  N  ND1   . HIS B 1 469 ? 125.512 130.953 170.751 1.00 33.35 ?  469 HIS B ND1   1 
ATOM   9312  C  CD2   . HIS B 1 469 ? 124.882 131.923 172.601 1.00 27.48 ?  469 HIS B CD2   1 
ATOM   9313  C  CE1   . HIS B 1 469 ? 124.919 130.034 171.492 1.00 26.03 ?  469 HIS B CE1   1 
ATOM   9314  N  NE2   . HIS B 1 469 ? 124.529 130.598 172.621 1.00 25.19 ?  469 HIS B NE2   1 
ATOM   9315  N  N     . GLY B 1 470 ? 128.531 134.633 172.562 1.00 20.38 ?  470 GLY B N     1 
ATOM   9316  C  CA    . GLY B 1 470 ? 129.600 134.471 173.532 1.00 23.00 ?  470 GLY B CA    1 
ATOM   9317  C  C     . GLY B 1 470 ? 129.378 135.306 174.776 1.00 16.85 ?  470 GLY B C     1 
ATOM   9318  O  O     . GLY B 1 470 ? 129.541 134.821 175.899 1.00 35.43 ?  470 GLY B O     1 
ATOM   9319  N  N     . TYR B 1 471 ? 128.983 136.567 174.595 1.00 17.13 ?  471 TYR B N     1 
ATOM   9320  C  CA    . TYR B 1 471 ? 128.718 137.430 175.739 1.00 20.16 ?  471 TYR B CA    1 
ATOM   9321  C  C     . TYR B 1 471 ? 127.543 136.914 176.561 1.00 25.71 ?  471 TYR B C     1 
ATOM   9322  O  O     . TYR B 1 471 ? 127.578 136.950 177.796 1.00 30.05 ?  471 TYR B O     1 
ATOM   9323  C  CB    . TYR B 1 471 ? 128.448 138.860 175.276 1.00 25.45 ?  471 TYR B CB    1 
ATOM   9324  C  CG    . TYR B 1 471 ? 127.893 139.741 176.369 1.00 24.40 ?  471 TYR B CG    1 
ATOM   9325  C  CD1   . TYR B 1 471 ? 128.723 140.265 177.349 1.00 25.10 ?  471 TYR B CD1   1 
ATOM   9326  C  CD2   . TYR B 1 471 ? 126.538 140.026 176.437 1.00 15.35 ?  471 TYR B CD2   1 
ATOM   9327  C  CE1   . TYR B 1 471 ? 128.221 141.059 178.355 1.00 22.93 ?  471 TYR B CE1   1 
ATOM   9328  C  CE2   . TYR B 1 471 ? 126.029 140.812 177.444 1.00 19.90 ?  471 TYR B CE2   1 
ATOM   9329  C  CZ    . TYR B 1 471 ? 126.872 141.330 178.396 1.00 26.35 ?  471 TYR B CZ    1 
ATOM   9330  O  OH    . TYR B 1 471 ? 126.362 142.122 179.396 1.00 36.38 ?  471 TYR B OH    1 
ATOM   9331  N  N     . LEU B 1 472 ? 126.488 136.440 175.893 1.00 28.49 ?  472 LEU B N     1 
ATOM   9332  C  CA    . LEU B 1 472 ? 125.314 135.965 176.618 1.00 21.62 ?  472 LEU B CA    1 
ATOM   9333  C  C     . LEU B 1 472 ? 125.613 134.673 177.372 1.00 28.12 ?  472 LEU B C     1 
ATOM   9334  O  O     . LEU B 1 472 ? 125.243 134.528 178.542 1.00 35.09 ?  472 LEU B O     1 
ATOM   9335  C  CB    . LEU B 1 472 ? 124.144 135.769 175.653 1.00 23.44 ?  472 LEU B CB    1 
ATOM   9336  C  CG    . LEU B 1 472 ? 123.552 137.036 175.033 1.00 25.83 ?  472 LEU B CG    1 
ATOM   9337  C  CD1   . LEU B 1 472 ? 122.586 136.680 173.916 1.00 24.57 ?  472 LEU B CD1   1 
ATOM   9338  C  CD2   . LEU B 1 472 ? 122.870 137.890 176.089 1.00 22.97 ?  472 LEU B CD2   1 
ATOM   9339  N  N     . ALA B 1 473 ? 126.282 133.723 176.716 1.00 24.54 ?  473 ALA B N     1 
ATOM   9340  C  CA    . ALA B 1 473 ? 126.591 132.451 177.356 1.00 24.14 ?  473 ALA B CA    1 
ATOM   9341  C  C     . ALA B 1 473 ? 127.602 132.616 178.480 1.00 32.15 ?  473 ALA B C     1 
ATOM   9342  O  O     . ALA B 1 473 ? 127.530 131.897 179.484 1.00 39.89 ?  473 ALA B O     1 
ATOM   9343  C  CB    . ALA B 1 473 ? 127.104 131.457 176.317 1.00 25.75 ?  473 ALA B CB    1 
ATOM   9344  N  N     . GLN B 1 474 ? 128.547 133.546 178.340 1.00 31.34 ?  474 GLN B N     1 
ATOM   9345  C  CA    . GLN B 1 474 ? 129.484 133.818 179.420 1.00 29.33 ?  474 GLN B CA    1 
ATOM   9346  C  C     . GLN B 1 474 ? 128.860 134.624 180.550 1.00 29.76 ?  474 GLN B C     1 
ATOM   9347  O  O     . GLN B 1 474 ? 129.503 134.800 181.590 1.00 40.96 ?  474 GLN B O     1 
ATOM   9348  C  CB    . GLN B 1 474 ? 130.714 134.547 178.877 1.00 31.56 ?  474 GLN B CB    1 
ATOM   9349  C  CG    . GLN B 1 474 ? 131.641 133.652 178.077 1.00 29.28 ?  474 GLN B CG    1 
ATOM   9350  C  CD    . GLN B 1 474 ? 132.780 134.415 177.438 1.00 36.08 ?  474 GLN B CD    1 
ATOM   9351  O  OE1   . GLN B 1 474 ? 133.664 134.919 178.127 1.00 42.48 ?  474 GLN B OE1   1 
ATOM   9352  N  NE2   . GLN B 1 474 ? 132.764 134.500 176.114 1.00 36.55 ?  474 GLN B NE2   1 
ATOM   9353  N  N     . ASN B 1 475 ? 127.635 135.115 180.373 1.00 32.74 ?  475 ASN B N     1 
ATOM   9354  C  CA    . ASN B 1 475 ? 126.906 135.818 181.419 1.00 35.35 ?  475 ASN B CA    1 
ATOM   9355  C  C     . ASN B 1 475 ? 125.693 135.036 181.905 1.00 36.04 ?  475 ASN B C     1 
ATOM   9356  O  O     . ASN B 1 475 ? 124.841 135.601 182.599 1.00 38.28 ?  475 ASN B O     1 
ATOM   9357  C  CB    . ASN B 1 475 ? 126.479 137.202 180.930 1.00 34.60 ?  475 ASN B CB    1 
ATOM   9358  C  CG    . ASN B 1 475 ? 127.644 138.159 180.806 1.00 32.50 ?  475 ASN B CG    1 
ATOM   9359  O  OD1   . ASN B 1 475 ? 127.924 138.932 181.721 1.00 39.35 ?  475 ASN B OD1   1 
ATOM   9360  N  ND2   . ASN B 1 475 ? 128.335 138.105 179.677 1.00 28.42 ?  475 ASN B ND2   1 
ATOM   9361  N  N     . GLY B 1 476 ? 125.594 133.757 181.559 1.00 35.89 ?  476 GLY B N     1 
ATOM   9362  C  CA    . GLY B 1 476 ? 124.491 132.925 182.005 1.00 32.40 ?  476 GLY B CA    1 
ATOM   9363  C  C     . GLY B 1 476 ? 123.138 133.309 181.448 1.00 35.20 ?  476 GLY B C     1 
ATOM   9364  O  O     . GLY B 1 476 ? 122.142 133.285 182.183 1.00 42.73 ?  476 GLY B O     1 
ATOM   9365  N  N     . ILE B 1 477 ? 123.073 133.665 180.168 1.00 32.50 ?  477 ILE B N     1 
ATOM   9366  C  CA    . ILE B 1 477 ? 121.824 134.026 179.512 1.00 32.21 ?  477 ILE B CA    1 
ATOM   9367  C  C     . ILE B 1 477 ? 121.665 133.160 178.271 1.00 32.56 ?  477 ILE B C     1 
ATOM   9368  O  O     . ILE B 1 477 ? 122.559 133.119 177.419 1.00 36.67 ?  477 ILE B O     1 
ATOM   9369  C  CB    . ILE B 1 477 ? 121.782 135.521 179.140 1.00 27.66 ?  477 ILE B CB    1 
ATOM   9370  C  CG1   . ILE B 1 477 ? 121.788 136.386 180.401 1.00 30.97 ?  477 ILE B CG1   1 
ATOM   9371  C  CG2   . ILE B 1 477 ? 120.559 135.825 178.301 1.00 26.18 ?  477 ILE B CG2   1 
ATOM   9372  C  CD1   . ILE B 1 477 ? 122.440 137.733 180.211 1.00 33.59 ?  477 ILE B CD1   1 
ATOM   9373  N  N     . ALA B 1 478 ? 120.536 132.465 178.176 1.00 33.33 ?  478 ALA B N     1 
ATOM   9374  C  CA    . ALA B 1 478 ? 120.253 131.661 176.996 1.00 28.73 ?  478 ALA B CA    1 
ATOM   9375  C  C     . ALA B 1 478 ? 119.957 132.562 175.806 1.00 34.04 ?  478 ALA B C     1 
ATOM   9376  O  O     . ALA B 1 478 ? 119.331 133.614 175.945 1.00 38.65 ?  478 ALA B O     1 
ATOM   9377  C  CB    . ALA B 1 478 ? 119.074 130.726 177.257 1.00 29.59 ?  478 ALA B CB    1 
ATOM   9378  N  N     . TYR B 1 479 ? 120.413 132.139 174.624 1.00 29.89 ?  479 TYR B N     1 
ATOM   9379  C  CA    . TYR B 1 479 ? 120.247 132.955 173.425 1.00 21.31 ?  479 TYR B CA    1 
ATOM   9380  C  C     . TYR B 1 479 ? 118.774 133.159 173.090 1.00 33.73 ?  479 TYR B C     1 
ATOM   9381  O  O     . TYR B 1 479 ? 118.374 134.247 172.659 1.00 36.22 ?  479 TYR B O     1 
ATOM   9382  C  CB    . TYR B 1 479 ? 120.986 132.308 172.256 1.00 19.78 ?  479 TYR B CB    1 
ATOM   9383  C  CG    . TYR B 1 479 ? 121.094 133.173 171.021 1.00 26.75 ?  479 TYR B CG    1 
ATOM   9384  C  CD1   . TYR B 1 479 ? 120.120 133.134 170.032 1.00 30.18 ?  479 TYR B CD1   1 
ATOM   9385  C  CD2   . TYR B 1 479 ? 122.179 134.020 170.837 1.00 23.61 ?  479 TYR B CD2   1 
ATOM   9386  C  CE1   . TYR B 1 479 ? 120.219 133.919 168.902 1.00 23.94 ?  479 TYR B CE1   1 
ATOM   9387  C  CE2   . TYR B 1 479 ? 122.287 134.807 169.711 1.00 22.72 ?  479 TYR B CE2   1 
ATOM   9388  C  CZ    . TYR B 1 479 ? 121.305 134.753 168.747 1.00 30.34 ?  479 TYR B CZ    1 
ATOM   9389  O  OH    . TYR B 1 479 ? 121.407 135.536 167.622 1.00 35.04 ?  479 TYR B OH    1 
ATOM   9390  N  N     . GLU B 1 480 ? 117.952 132.125 173.276 1.00 36.31 ?  480 GLU B N     1 
ATOM   9391  C  CA    . GLU B 1 480 ? 116.528 132.228 172.987 1.00 31.16 ?  480 GLU B CA    1 
ATOM   9392  C  C     . GLU B 1 480 ? 115.732 132.853 174.121 1.00 33.32 ?  480 GLU B C     1 
ATOM   9393  O  O     . GLU B 1 480 ? 114.526 133.069 173.961 1.00 38.14 ?  480 GLU B O     1 
ATOM   9394  C  CB    . GLU B 1 480 ? 115.944 130.847 172.684 1.00 34.29 ?  480 GLU B CB    1 
ATOM   9395  C  CG    . GLU B 1 480 ? 116.652 130.078 171.595 1.00 35.17 ?  480 GLU B CG    1 
ATOM   9396  C  CD    . GLU B 1 480 ? 116.568 128.583 171.818 1.00 43.07 ?  480 GLU B CD    1 
ATOM   9397  O  OE1   . GLU B 1 480 ? 117.331 128.066 172.659 1.00 44.45 ?  480 GLU B OE1   1 
ATOM   9398  O  OE2   . GLU B 1 480 ? 115.740 127.925 171.156 1.00 39.62 -1 480 GLU B OE2   1 
ATOM   9399  N  N     . SER B 1 481 ? 116.363 133.137 175.254 1.00 31.50 ?  481 SER B N     1 
ATOM   9400  C  CA    . SER B 1 481 ? 115.636 133.659 176.396 1.00 32.57 ?  481 SER B CA    1 
ATOM   9401  C  C     . SER B 1 481 ? 115.147 135.081 176.119 1.00 36.64 ?  481 SER B C     1 
ATOM   9402  O  O     . SER B 1 481 ? 115.753 135.814 175.333 1.00 38.79 ?  481 SER B O     1 
ATOM   9403  C  CB    . SER B 1 481 ? 116.520 133.646 177.638 1.00 30.75 ?  481 SER B CB    1 
ATOM   9404  O  OG    . SER B 1 481 ? 117.365 134.781 177.674 1.00 35.20 ?  481 SER B OG    1 
ATOM   9405  N  N     . PRO B 1 482 ? 114.035 135.484 176.737 1.00 42.31 ?  482 PRO B N     1 
ATOM   9406  C  CA    . PRO B 1 482 ? 113.602 136.885 176.611 1.00 37.58 ?  482 PRO B CA    1 
ATOM   9407  C  C     . PRO B 1 482 ? 114.615 137.873 177.157 1.00 32.77 ?  482 PRO B C     1 
ATOM   9408  O  O     . PRO B 1 482 ? 114.652 139.022 176.702 1.00 36.90 ?  482 PRO B O     1 
ATOM   9409  C  CB    . PRO B 1 482 ? 112.291 136.917 177.408 1.00 35.59 ?  482 PRO B CB    1 
ATOM   9410  C  CG    . PRO B 1 482 ? 111.819 135.505 177.417 1.00 37.34 ?  482 PRO B CG    1 
ATOM   9411  C  CD    . PRO B 1 482 ? 113.057 134.667 177.472 1.00 37.93 ?  482 PRO B CD    1 
ATOM   9412  N  N     . GLU B 1 483 ? 115.437 137.461 178.124 1.00 35.62 ?  483 GLU B N     1 
ATOM   9413  C  CA    . GLU B 1 483 ? 116.472 138.348 178.647 1.00 32.90 ?  483 GLU B CA    1 
ATOM   9414  C  C     . GLU B 1 483 ? 117.543 138.624 177.601 1.00 30.00 ?  483 GLU B C     1 
ATOM   9415  O  O     . GLU B 1 483 ? 118.096 139.728 177.546 1.00 36.41 ?  483 GLU B O     1 
ATOM   9416  C  CB    . GLU B 1 483 ? 117.090 137.743 179.907 1.00 37.13 ?  483 GLU B CB    1 
ATOM   9417  C  CG    . GLU B 1 483 ? 116.123 137.622 181.072 1.00 39.21 ?  483 GLU B CG    1 
ATOM   9418  C  CD    . GLU B 1 483 ? 115.458 136.260 181.138 1.00 45.79 ?  483 GLU B CD    1 
ATOM   9419  O  OE1   . GLU B 1 483 ? 115.561 135.501 180.155 1.00 42.62 ?  483 GLU B OE1   1 
ATOM   9420  O  OE2   . GLU B 1 483 ? 114.830 135.952 182.172 1.00 44.24 -1 483 GLU B OE2   1 
ATOM   9421  N  N     . ALA B 1 484 ? 117.857 137.631 176.766 1.00 28.45 ?  484 ALA B N     1 
ATOM   9422  C  CA    . ALA B 1 484 ? 118.807 137.854 175.682 1.00 29.24 ?  484 ALA B CA    1 
ATOM   9423  C  C     . ALA B 1 484 ? 118.281 138.884 174.692 1.00 29.55 ?  484 ALA B C     1 
ATOM   9424  O  O     . ALA B 1 484 ? 119.024 139.769 174.252 1.00 31.34 ?  484 ALA B O     1 
ATOM   9425  C  CB    . ALA B 1 484 ? 119.110 136.538 174.972 1.00 21.96 ?  484 ALA B CB    1 
ATOM   9426  N  N     . ARG B 1 485 ? 117.000 138.786 174.335 1.00 26.43 ?  485 ARG B N     1 
ATOM   9427  C  CA    . ARG B 1 485 ? 116.406 139.785 173.455 1.00 26.24 ?  485 ARG B CA    1 
ATOM   9428  C  C     . ARG B 1 485 ? 116.336 141.146 174.127 1.00 24.75 ?  485 ARG B C     1 
ATOM   9429  O  O     . ARG B 1 485 ? 116.483 142.170 173.456 1.00 35.19 ?  485 ARG B O     1 
ATOM   9430  C  CB    . ARG B 1 485 ? 115.018 139.334 173.007 1.00 28.25 ?  485 ARG B CB    1 
ATOM   9431  C  CG    . ARG B 1 485 ? 115.041 138.248 171.952 1.00 26.08 ?  485 ARG B CG    1 
ATOM   9432  C  CD    . ARG B 1 485 ? 113.663 138.027 171.358 1.00 25.72 ?  485 ARG B CD    1 
ATOM   9433  N  NE    . ARG B 1 485 ? 112.707 137.549 172.348 1.00 29.58 ?  485 ARG B NE    1 
ATOM   9434  C  CZ    . ARG B 1 485 ? 112.625 136.293 172.765 1.00 33.69 ?  485 ARG B CZ    1 
ATOM   9435  N  NH1   . ARG B 1 485 ? 113.428 135.354 172.294 1.00 35.12 1  485 ARG B NH1   1 
ATOM   9436  N  NH2   . ARG B 1 485 ? 111.712 135.972 173.677 1.00 29.72 ?  485 ARG B NH2   1 
ATOM   9437  N  N     . ASP B 1 486 ? 116.116 141.179 175.440 1.00 30.77 ?  486 ASP B N     1 
ATOM   9438  C  CA    . ASP B 1 486 ? 116.130 142.445 176.168 1.00 30.72 ?  486 ASP B CA    1 
ATOM   9439  C  C     . ASP B 1 486 ? 117.505 143.100 176.099 1.00 30.06 ?  486 ASP B C     1 
ATOM   9440  O  O     . ASP B 1 486 ? 117.626 144.309 175.844 1.00 32.61 ?  486 ASP B O     1 
ATOM   9441  C  CB    . ASP B 1 486 ? 115.708 142.200 177.617 1.00 34.22 ?  486 ASP B CB    1 
ATOM   9442  C  CG    . ASP B 1 486 ? 115.447 143.479 178.372 1.00 43.15 ?  486 ASP B CG    1 
ATOM   9443  O  OD1   . ASP B 1 486 ? 114.740 144.357 177.837 1.00 45.20 ?  486 ASP B OD1   1 
ATOM   9444  O  OD2   . ASP B 1 486 ? 115.944 143.598 179.510 1.00 34.53 -1 486 ASP B OD2   1 
ATOM   9445  N  N     . PHE B 1 487 ? 118.560 142.309 176.314 1.00 26.92 ?  487 PHE B N     1 
ATOM   9446  C  CA    . PHE B 1 487 ? 119.909 142.847 176.198 1.00 23.40 ?  487 PHE B CA    1 
ATOM   9447  C  C     . PHE B 1 487 ? 120.195 143.317 174.782 1.00 28.27 ?  487 PHE B C     1 
ATOM   9448  O  O     . PHE B 1 487 ? 120.813 144.366 174.587 1.00 30.97 ?  487 PHE B O     1 
ATOM   9449  C  CB    . PHE B 1 487 ? 120.962 141.824 176.611 1.00 24.72 ?  487 PHE B CB    1 
ATOM   9450  C  CG    . PHE B 1 487 ? 122.338 142.184 176.131 1.00 28.11 ?  487 PHE B CG    1 
ATOM   9451  C  CD1   . PHE B 1 487 ? 123.057 143.183 176.762 1.00 21.12 ?  487 PHE B CD1   1 
ATOM   9452  C  CD2   . PHE B 1 487 ? 122.892 141.567 175.023 1.00 27.86 ?  487 PHE B CD2   1 
ATOM   9453  C  CE1   . PHE B 1 487 ? 124.308 143.543 176.314 1.00 23.42 ?  487 PHE B CE1   1 
ATOM   9454  C  CE2   . PHE B 1 487 ? 124.144 141.927 174.573 1.00 26.23 ?  487 PHE B CE2   1 
ATOM   9455  C  CZ    . PHE B 1 487 ? 124.850 142.917 175.219 1.00 25.18 ?  487 PHE B CZ    1 
ATOM   9456  N  N     . ALA B 1 488 ? 119.798 142.532 173.779 1.00 26.01 ?  488 ALA B N     1 
ATOM   9457  C  CA    . ALA B 1 488 ? 120.036 142.939 172.398 1.00 20.12 ?  488 ALA B CA    1 
ATOM   9458  C  C     . ALA B 1 488 ? 119.320 144.245 172.090 1.00 29.34 ?  488 ALA B C     1 
ATOM   9459  O  O     . ALA B 1 488 ? 119.897 145.152 171.480 1.00 38.20 ?  488 ALA B O     1 
ATOM   9460  C  CB    . ALA B 1 488 ? 119.588 141.839 171.440 1.00 21.50 ?  488 ALA B CB    1 
ATOM   9461  N  N     . ASN B 1 489 ? 118.067 144.364 172.533 1.00 28.70 ?  489 ASN B N     1 
ATOM   9462  C  CA    . ASN B 1 489 ? 117.308 145.594 172.354 1.00 26.11 ?  489 ASN B CA    1 
ATOM   9463  C  C     . ASN B 1 489 ? 118.049 146.786 172.939 1.00 20.40 ?  489 ASN B C     1 
ATOM   9464  O  O     . ASN B 1 489 ? 118.304 147.775 172.244 1.00 29.68 ?  489 ASN B O     1 
ATOM   9465  C  CB    . ASN B 1 489 ? 115.935 145.437 173.007 1.00 21.16 ?  489 ASN B CB    1 
ATOM   9466  C  CG    . ASN B 1 489 ? 114.908 146.397 172.459 1.00 32.36 ?  489 ASN B CG    1 
ATOM   9467  O  OD1   . ASN B 1 489 ? 114.644 146.427 171.259 1.00 39.21 ?  489 ASN B OD1   1 
ATOM   9468  N  ND2   . ASN B 1 489 ? 114.309 147.182 173.343 1.00 31.79 ?  489 ASN B ND2   1 
ATOM   9469  N  N     . THR B 1 490 ? 118.443 146.692 174.212 1.00 22.72 ?  490 THR B N     1 
ATOM   9470  C  CA    . THR B 1 490 ? 119.090 147.829 174.862 1.00 22.67 ?  490 THR B CA    1 
ATOM   9471  C  C     . THR B 1 490 ? 120.445 148.136 174.232 1.00 24.87 ?  490 THR B C     1 
ATOM   9472  O  O     . THR B 1 490 ? 120.755 149.297 173.934 1.00 21.06 ?  490 THR B O     1 
ATOM   9473  C  CB    . THR B 1 490 ? 119.243 147.563 176.358 1.00 33.48 ?  490 THR B CB    1 
ATOM   9474  O  OG1   . THR B 1 490 ? 117.980 147.161 176.901 1.00 39.12 ?  490 THR B OG1   1 
ATOM   9475  C  CG2   . THR B 1 490 ? 119.723 148.816 177.073 1.00 27.80 ?  490 THR B CG2   1 
ATOM   9476  N  N     . PHE B 1 491 ? 121.259 147.103 174.009 1.00 25.08 ?  491 PHE B N     1 
ATOM   9477  C  CA    . PHE B 1 491 ? 122.608 147.296 173.491 1.00 19.01 ?  491 PHE B CA    1 
ATOM   9478  C  C     . PHE B 1 491 ? 122.582 147.923 172.108 1.00 25.49 ?  491 PHE B C     1 
ATOM   9479  O  O     . PHE B 1 491 ? 123.325 148.871 171.830 1.00 33.73 ?  491 PHE B O     1 
ATOM   9480  C  CB    . PHE B 1 491 ? 123.347 145.956 173.461 1.00 23.13 ?  491 PHE B CB    1 
ATOM   9481  C  CG    . PHE B 1 491 ? 124.737 146.037 172.893 1.00 25.07 ?  491 PHE B CG    1 
ATOM   9482  C  CD1   . PHE B 1 491 ? 125.818 146.300 173.713 1.00 23.22 ?  491 PHE B CD1   1 
ATOM   9483  C  CD2   . PHE B 1 491 ? 124.964 145.837 171.541 1.00 20.50 ?  491 PHE B CD2   1 
ATOM   9484  C  CE1   . PHE B 1 491 ? 127.095 146.374 173.198 1.00 14.85 ?  491 PHE B CE1   1 
ATOM   9485  C  CE2   . PHE B 1 491 ? 126.237 145.912 171.020 1.00 15.76 ?  491 PHE B CE2   1 
ATOM   9486  C  CZ    . PHE B 1 491 ? 127.305 146.182 171.851 1.00 19.74 ?  491 PHE B CZ    1 
ATOM   9487  N  N     . PHE B 1 492 ? 121.736 147.407 171.218 1.00 20.89 ?  492 PHE B N     1 
ATOM   9488  C  CA    . PHE B 1 492 ? 121.712 147.947 169.871 1.00 12.88 ?  492 PHE B CA    1 
ATOM   9489  C  C     . PHE B 1 492 ? 120.969 149.271 169.785 1.00 10.87 ?  492 PHE B C     1 
ATOM   9490  O  O     . PHE B 1 492 ? 121.280 150.071 168.900 1.00 24.78 ?  492 PHE B O     1 
ATOM   9491  C  CB    . PHE B 1 492 ? 121.134 146.910 168.911 1.00 14.12 ?  492 PHE B CB    1 
ATOM   9492  C  CG    . PHE B 1 492 ? 122.090 145.794 168.611 1.00 16.24 ?  492 PHE B CG    1 
ATOM   9493  C  CD1   . PHE B 1 492 ? 123.119 145.975 167.705 1.00 10.13 ?  492 PHE B CD1   1 
ATOM   9494  C  CD2   . PHE B 1 492 ? 121.990 144.581 169.267 1.00 18.24 ?  492 PHE B CD2   1 
ATOM   9495  C  CE1   . PHE B 1 492 ? 124.010 144.960 167.439 1.00 8.63  ?  492 PHE B CE1   1 
ATOM   9496  C  CE2   . PHE B 1 492 ? 122.879 143.561 169.005 1.00 12.97 ?  492 PHE B CE2   1 
ATOM   9497  C  CZ    . PHE B 1 492 ? 123.889 143.750 168.089 1.00 15.74 ?  492 PHE B CZ    1 
ATOM   9498  N  N     . MET B 1 493 ? 120.044 149.554 170.709 1.00 14.89 ?  493 MET B N     1 
ATOM   9499  C  CA    . MET B 1 493 ? 119.527 150.914 170.805 1.00 17.34 ?  493 MET B CA    1 
ATOM   9500  C  C     . MET B 1 493 ? 120.639 151.886 171.167 1.00 22.68 ?  493 MET B C     1 
ATOM   9501  O  O     . MET B 1 493 ? 120.734 152.973 170.589 1.00 29.67 ?  493 MET B O     1 
ATOM   9502  C  CB    . MET B 1 493 ? 118.412 150.995 171.843 1.00 19.23 ?  493 MET B CB    1 
ATOM   9503  C  CG    . MET B 1 493 ? 117.841 152.397 171.998 1.00 18.99 ?  493 MET B CG    1 
ATOM   9504  S  SD    . MET B 1 493 ? 118.453 153.284 173.444 1.00 37.89 ?  493 MET B SD    1 
ATOM   9505  C  CE    . MET B 1 493 ? 118.416 152.000 174.686 1.00 27.76 ?  493 MET B CE    1 
ATOM   9506  N  N     . MET B 1 494 ? 121.492 151.512 172.125 1.00 22.12 ?  494 MET B N     1 
ATOM   9507  C  CA    . MET B 1 494 ? 122.613 152.374 172.493 1.00 17.02 ?  494 MET B CA    1 
ATOM   9508  C  C     . MET B 1 494 ? 123.589 152.537 171.335 1.00 18.65 ?  494 MET B C     1 
ATOM   9509  O  O     . MET B 1 494 ? 124.103 153.637 171.095 1.00 31.25 ?  494 MET B O     1 
ATOM   9510  C  CB    . MET B 1 494 ? 123.331 151.814 173.720 1.00 23.61 ?  494 MET B CB    1 
ATOM   9511  C  CG    . MET B 1 494 ? 122.458 151.674 174.951 1.00 22.05 ?  494 MET B CG    1 
ATOM   9512  S  SD    . MET B 1 494 ? 123.405 151.286 176.432 1.00 42.56 ?  494 MET B SD    1 
ATOM   9513  C  CE    . MET B 1 494 ? 124.677 152.541 176.353 1.00 31.53 ?  494 MET B CE    1 
ATOM   9514  N  N     . VAL B 1 495 ? 123.867 151.447 170.618 1.00 19.82 ?  495 VAL B N     1 
ATOM   9515  C  CA    . VAL B 1 495 ? 124.768 151.515 169.472 1.00 13.54 ?  495 VAL B CA    1 
ATOM   9516  C  C     . VAL B 1 495 ? 124.207 152.448 168.409 1.00 18.91 ?  495 VAL B C     1 
ATOM   9517  O  O     . VAL B 1 495 ? 124.928 153.285 167.856 1.00 31.74 ?  495 VAL B O     1 
ATOM   9518  C  CB    . VAL B 1 495 ? 125.026 150.104 168.911 1.00 15.39 ?  495 VAL B CB    1 
ATOM   9519  C  CG1   . VAL B 1 495 ? 125.671 150.184 167.537 1.00 13.43 ?  495 VAL B CG1   1 
ATOM   9520  C  CG2   . VAL B 1 495 ? 125.895 149.308 169.865 1.00 14.04 ?  495 VAL B CG2   1 
ATOM   9521  N  N     . ASN B 1 496 ? 122.910 152.326 168.113 1.00 25.04 ?  496 ASN B N     1 
ATOM   9522  C  CA    . ASN B 1 496 ? 122.279 153.217 167.146 1.00 14.39 ?  496 ASN B CA    1 
ATOM   9523  C  C     . ASN B 1 496 ? 122.316 154.661 167.621 1.00 17.48 ?  496 ASN B C     1 
ATOM   9524  O  O     . ASN B 1 496 ? 122.594 155.573 166.835 1.00 27.82 ?  496 ASN B O     1 
ATOM   9525  C  CB    . ASN B 1 496 ? 120.838 152.772 166.894 1.00 13.17 ?  496 ASN B CB    1 
ATOM   9526  C  CG    . ASN B 1 496 ? 120.273 153.330 165.608 1.00 14.73 ?  496 ASN B CG    1 
ATOM   9527  O  OD1   . ASN B 1 496 ? 120.964 153.403 164.595 1.00 25.58 ?  496 ASN B OD1   1 
ATOM   9528  N  ND2   . ASN B 1 496 ? 119.009 153.724 165.642 1.00 17.11 ?  496 ASN B ND2   1 
ATOM   9529  N  N     . PHE B 1 497 ? 122.042 154.887 168.907 1.00 18.74 ?  497 PHE B N     1 
ATOM   9530  C  CA    . PHE B 1 497 ? 122.057 156.237 169.454 1.00 12.68 ?  497 PHE B CA    1 
ATOM   9531  C  C     . PHE B 1 497 ? 123.421 156.881 169.274 1.00 24.73 ?  497 PHE B C     1 
ATOM   9532  O  O     . PHE B 1 497 ? 123.530 158.010 168.781 1.00 30.72 ?  497 PHE B O     1 
ATOM   9533  C  CB    . PHE B 1 497 ? 121.675 156.197 170.936 1.00 15.59 ?  497 PHE B CB    1 
ATOM   9534  C  CG    . PHE B 1 497 ? 121.617 157.547 171.588 1.00 19.96 ?  497 PHE B CG    1 
ATOM   9535  C  CD1   . PHE B 1 497 ? 120.455 158.295 171.559 1.00 29.44 ?  497 PHE B CD1   1 
ATOM   9536  C  CD2   . PHE B 1 497 ? 122.723 158.063 172.243 1.00 22.87 ?  497 PHE B CD2   1 
ATOM   9537  C  CE1   . PHE B 1 497 ? 120.399 159.534 172.161 1.00 27.07 ?  497 PHE B CE1   1 
ATOM   9538  C  CE2   . PHE B 1 497 ? 122.671 159.302 172.846 1.00 25.28 ?  497 PHE B CE2   1 
ATOM   9539  C  CZ    . PHE B 1 497 ? 121.508 160.037 172.804 1.00 28.44 ?  497 PHE B CZ    1 
ATOM   9540  N  N     . TYR B 1 498 ? 124.479 156.167 169.650 1.00 28.15 ?  498 TYR B N     1 
ATOM   9541  C  CA    . TYR B 1 498 ? 125.805 156.762 169.596 1.00 19.30 ?  498 TYR B CA    1 
ATOM   9542  C  C     . TYR B 1 498 ? 126.343 156.834 168.174 1.00 24.34 ?  498 TYR B C     1 
ATOM   9543  O  O     . TYR B 1 498 ? 127.113 157.745 167.864 1.00 35.03 ?  498 TYR B O     1 
ATOM   9544  C  CB    . TYR B 1 498 ? 126.751 156.005 170.524 1.00 20.21 ?  498 TYR B CB    1 
ATOM   9545  C  CG    . TYR B 1 498 ? 126.433 156.283 171.973 1.00 26.02 ?  498 TYR B CG    1 
ATOM   9546  C  CD1   . TYR B 1 498 ? 126.439 157.582 172.460 1.00 29.24 ?  498 TYR B CD1   1 
ATOM   9547  C  CD2   . TYR B 1 498 ? 126.090 155.258 172.841 1.00 25.53 ?  498 TYR B CD2   1 
ATOM   9548  C  CE1   . TYR B 1 498 ? 126.132 157.851 173.776 1.00 29.00 ?  498 TYR B CE1   1 
ATOM   9549  C  CE2   . TYR B 1 498 ? 125.782 155.519 174.161 1.00 26.42 ?  498 TYR B CE2   1 
ATOM   9550  C  CZ    . TYR B 1 498 ? 125.805 156.818 174.623 1.00 33.24 ?  498 TYR B CZ    1 
ATOM   9551  O  OH    . TYR B 1 498 ? 125.501 157.086 175.937 1.00 37.24 ?  498 TYR B OH    1 
ATOM   9552  N  N     . SER B 1 499 ? 125.916 155.937 167.283 1.00 18.28 ?  499 SER B N     1 
ATOM   9553  C  CA    . SER B 1 499 ? 126.310 156.068 165.884 1.00 10.43 ?  499 SER B CA    1 
ATOM   9554  C  C     . SER B 1 499 ? 125.630 157.266 165.233 1.00 18.82 ?  499 SER B C     1 
ATOM   9555  O  O     . SER B 1 499 ? 126.264 158.007 164.474 1.00 27.20 ?  499 SER B O     1 
ATOM   9556  C  CB    . SER B 1 499 ? 125.994 154.781 165.122 1.00 8.27  ?  499 SER B CB    1 
ATOM   9557  O  OG    . SER B 1 499 ? 124.611 154.671 164.849 1.00 24.13 ?  499 SER B OG    1 
ATOM   9558  N  N     . ILE B 1 500 ? 124.346 157.488 165.532 1.00 16.69 ?  500 ILE B N     1 
ATOM   9559  C  CA    . ILE B 1 500 ? 123.660 158.678 165.033 1.00 20.33 ?  500 ILE B CA    1 
ATOM   9560  C  C     . ILE B 1 500 ? 124.301 159.934 165.601 1.00 21.42 ?  500 ILE B C     1 
ATOM   9561  O  O     . ILE B 1 500 ? 124.491 160.929 164.889 1.00 26.70 ?  500 ILE B O     1 
ATOM   9562  C  CB    . ILE B 1 500 ? 122.159 158.617 165.368 1.00 24.31 ?  500 ILE B CB    1 
ATOM   9563  C  CG1   . ILE B 1 500 ? 121.475 157.489 164.606 1.00 21.83 ?  500 ILE B CG1   1 
ATOM   9564  C  CG2   . ILE B 1 500 ? 121.485 159.934 165.034 1.00 19.07 ?  500 ILE B CG2   1 
ATOM   9565  C  CD1   . ILE B 1 500 ? 120.119 157.145 165.152 1.00 18.71 ?  500 ILE B CD1   1 
ATOM   9566  N  N     . GLN B 1 501 ? 124.632 159.916 166.894 1.00 29.10 ?  501 GLN B N     1 
ATOM   9567  C  CA    . GLN B 1 501 ? 125.260 161.076 167.513 1.00 25.39 ?  501 GLN B CA    1 
ATOM   9568  C  C     . GLN B 1 501 ? 126.617 161.373 166.890 1.00 26.73 ?  501 GLN B C     1 
ATOM   9569  O  O     . GLN B 1 501 ? 126.933 162.530 166.603 1.00 39.62 ?  501 GLN B O     1 
ATOM   9570  C  CB    . GLN B 1 501 ? 125.399 160.856 169.018 1.00 30.32 ?  501 GLN B CB    1 
ATOM   9571  C  CG    . GLN B 1 501 ? 125.303 162.129 169.831 1.00 29.00 ?  501 GLN B CG    1 
ATOM   9572  C  CD    . GLN B 1 501 ? 125.448 161.880 171.313 1.00 33.80 ?  501 GLN B CD    1 
ATOM   9573  O  OE1   . GLN B 1 501 ? 126.445 161.318 171.763 1.00 39.72 ?  501 GLN B OE1   1 
ATOM   9574  N  NE2   . GLN B 1 501 ? 124.452 162.298 172.084 1.00 34.98 ?  501 GLN B NE2   1 
ATOM   9575  N  N     . ARG B 1 502 ? 127.429 160.339 166.659 1.00 31.15 ?  502 ARG B N     1 
ATOM   9576  C  CA    . ARG B 1 502 ? 128.731 160.552 166.037 1.00 23.02 ?  502 ARG B CA    1 
ATOM   9577  C  C     . ARG B 1 502 ? 128.588 161.031 164.600 1.00 22.55 ?  502 ARG B C     1 
ATOM   9578  O  O     . ARG B 1 502 ? 129.366 161.873 164.145 1.00 30.10 ?  502 ARG B O     1 
ATOM   9579  C  CB    . ARG B 1 502 ? 129.562 159.272 166.094 1.00 20.77 ?  502 ARG B CB    1 
ATOM   9580  C  CG    . ARG B 1 502 ? 131.023 159.486 165.749 1.00 25.50 ?  502 ARG B CG    1 
ATOM   9581  C  CD    . ARG B 1 502 ? 131.623 160.602 166.583 1.00 28.07 ?  502 ARG B CD    1 
ATOM   9582  N  NE    . ARG B 1 502 ? 132.925 161.020 166.081 1.00 28.04 ?  502 ARG B NE    1 
ATOM   9583  C  CZ    . ARG B 1 502 ? 133.363 162.271 166.087 1.00 27.28 ?  502 ARG B CZ    1 
ATOM   9584  N  NH1   . ARG B 1 502 ? 132.624 163.259 166.562 1.00 32.98 1  502 ARG B NH1   1 
ATOM   9585  N  NH2   . ARG B 1 502 ? 134.571 162.537 165.602 1.00 29.36 ?  502 ARG B NH2   1 
ATOM   9586  N  N     . SER B 1 503 ? 127.609 160.503 163.866 1.00 23.22 ?  503 SER B N     1 
ATOM   9587  C  CA    . SER B 1 503 ? 127.393 160.952 162.495 1.00 22.24 ?  503 SER B CA    1 
ATOM   9588  C  C     . SER B 1 503 ? 126.975 162.416 162.453 1.00 26.36 ?  503 SER B C     1 
ATOM   9589  O  O     . SER B 1 503 ? 127.464 163.187 161.620 1.00 33.93 ?  503 SER B O     1 
ATOM   9590  C  CB    . SER B 1 503 ? 126.345 160.067 161.825 1.00 16.91 ?  503 SER B CB    1 
ATOM   9591  O  OG    . SER B 1 503 ? 126.482 160.078 160.418 1.00 25.82 ?  503 SER B OG    1 
ATOM   9592  N  N     . ALA B 1 504 ? 126.081 162.823 163.355 1.00 25.08 ?  504 ALA B N     1 
ATOM   9593  C  CA    . ALA B 1 504 ? 125.684 164.225 163.418 1.00 22.29 ?  504 ALA B CA    1 
ATOM   9594  C  C     . ALA B 1 504 ? 126.843 165.109 163.863 1.00 31.28 ?  504 ALA B C     1 
ATOM   9595  O  O     . ALA B 1 504 ? 126.982 166.242 163.389 1.00 38.19 ?  504 ALA B O     1 
ATOM   9596  C  CB    . ALA B 1 504 ? 124.488 164.389 164.353 1.00 22.33 ?  504 ALA B CB    1 
ATOM   9597  N  N     . GLU B 1 505 ? 127.688 164.611 164.768 1.00 29.93 ?  505 GLU B N     1 
ATOM   9598  C  CA    . GLU B 1 505 ? 128.868 165.365 165.182 1.00 26.45 ?  505 GLU B CA    1 
ATOM   9599  C  C     . GLU B 1 505 ? 129.842 165.549 164.025 1.00 34.37 ?  505 GLU B C     1 
ATOM   9600  O  O     . GLU B 1 505 ? 130.422 166.627 163.862 1.00 39.07 ?  505 GLU B O     1 
ATOM   9601  C  CB    . GLU B 1 505 ? 129.552 164.660 166.352 1.00 26.96 ?  505 GLU B CB    1 
ATOM   9602  C  CG    . GLU B 1 505 ? 128.864 164.860 167.688 1.00 31.27 ?  505 GLU B CG    1 
ATOM   9603  C  CD    . GLU B 1 505 ? 129.245 163.802 168.703 1.00 37.60 ?  505 GLU B CD    1 
ATOM   9604  O  OE1   . GLU B 1 505 ? 130.123 162.969 168.396 1.00 39.01 ?  505 GLU B OE1   1 
ATOM   9605  O  OE2   . GLU B 1 505 ? 128.669 163.804 169.810 1.00 41.19 -1 505 GLU B OE2   1 
ATOM   9606  N  N     . ILE B 1 506 ? 130.041 164.505 163.219 1.00 32.03 ?  506 ILE B N     1 
ATOM   9607  C  CA    . ILE B 1 506 ? 130.904 164.618 162.047 1.00 26.15 ?  506 ILE B CA    1 
ATOM   9608  C  C     . ILE B 1 506 ? 130.308 165.593 161.041 1.00 26.57 ?  506 ILE B C     1 
ATOM   9609  O  O     . ILE B 1 506 ? 131.028 166.382 160.419 1.00 37.47 ?  506 ILE B O     1 
ATOM   9610  C  CB    . ILE B 1 506 ? 131.144 163.230 161.424 1.00 27.51 ?  506 ILE B CB    1 
ATOM   9611  C  CG1   . ILE B 1 506 ? 131.933 162.342 162.387 1.00 32.53 ?  506 ILE B CG1   1 
ATOM   9612  C  CG2   . ILE B 1 506 ? 131.881 163.351 160.101 1.00 24.74 ?  506 ILE B CG2   1 
ATOM   9613  C  CD1   . ILE B 1 506 ? 131.944 160.881 162.000 1.00 24.63 ?  506 ILE B CD1   1 
ATOM   9614  N  N     . ALA B 1 507 ? 128.985 165.555 160.862 1.00 29.52 ?  507 ALA B N     1 
ATOM   9615  C  CA    . ALA B 1 507 ? 128.334 166.506 159.966 1.00 29.58 ?  507 ALA B CA    1 
ATOM   9616  C  C     . ALA B 1 507 ? 128.517 167.938 160.452 1.00 31.40 ?  507 ALA B C     1 
ATOM   9617  O  O     . ALA B 1 507 ? 128.758 168.847 159.652 1.00 37.98 ?  507 ALA B O     1 
ATOM   9618  C  CB    . ALA B 1 507 ? 126.850 166.168 159.834 1.00 26.16 ?  507 ALA B CB    1 
ATOM   9619  N  N     . LYS B 1 508 ? 128.399 168.157 161.763 1.00 35.98 ?  508 LYS B N     1 
ATOM   9620  C  CA    . LYS B 1 508 ? 128.623 169.484 162.324 1.00 36.46 ?  508 LYS B CA    1 
ATOM   9621  C  C     . LYS B 1 508 ? 130.073 169.926 162.151 1.00 39.38 ?  508 LYS B C     1 
ATOM   9622  O  O     . LYS B 1 508 ? 130.339 171.090 161.832 1.00 43.84 ?  508 LYS B O     1 
ATOM   9623  C  CB    . LYS B 1 508 ? 128.230 169.495 163.801 1.00 41.04 ?  508 LYS B CB    1 
ATOM   9624  C  CG    . LYS B 1 508 ? 128.484 170.811 164.510 1.00 38.72 ?  508 LYS B CG    1 
ATOM   9625  C  CD    . LYS B 1 508 ? 128.301 170.667 166.009 1.00 39.11 ?  508 LYS B CD    1 
ATOM   9626  C  CE    . LYS B 1 508 ? 128.393 172.012 166.708 1.00 41.74 ?  508 LYS B CE    1 
ATOM   9627  N  NZ    . LYS B 1 508 ? 127.560 172.056 167.941 1.00 46.13 1  508 LYS B NZ    1 
ATOM   9628  N  N     . GLU B 1 509 ? 131.022 169.012 162.364 1.00 42.09 ?  509 GLU B N     1 
ATOM   9629  C  CA    . GLU B 1 509 ? 132.434 169.358 162.245 1.00 40.27 ?  509 GLU B CA    1 
ATOM   9630  C  C     . GLU B 1 509 ? 132.803 169.702 160.808 1.00 42.88 ?  509 GLU B C     1 
ATOM   9631  O  O     . GLU B 1 509 ? 133.502 170.692 160.561 1.00 49.18 ?  509 GLU B O     1 
ATOM   9632  C  CB    . GLU B 1 509 ? 133.298 168.207 162.757 1.00 37.70 ?  509 GLU B CB    1 
ATOM   9633  C  CG    . GLU B 1 509 ? 133.598 168.263 164.245 1.00 46.70 ?  509 GLU B CG    1 
ATOM   9634  C  CD    . GLU B 1 509 ? 133.819 166.888 164.848 1.00 50.17 ?  509 GLU B CD    1 
ATOM   9635  O  OE1   . GLU B 1 509 ? 134.378 166.014 164.152 1.00 48.52 ?  509 GLU B OE1   1 
ATOM   9636  O  OE2   . GLU B 1 509 ? 133.433 166.681 166.018 1.00 45.41 -1 509 GLU B OE2   1 
ATOM   9637  N  N     . LYS B 1 510 ? 132.347 168.900 159.850 1.00 38.56 ?  510 LYS B N     1 
ATOM   9638  C  CA    . LYS B 1 510 ? 132.648 169.127 158.446 1.00 32.84 ?  510 LYS B CA    1 
ATOM   9639  C  C     . LYS B 1 510 ? 131.663 170.069 157.768 1.00 38.42 ?  510 LYS B C     1 
ATOM   9640  O  O     . LYS B 1 510 ? 131.902 170.468 156.625 1.00 46.93 ?  510 LYS B O     1 
ATOM   9641  C  CB    . LYS B 1 510 ? 132.675 167.793 157.692 1.00 29.42 ?  510 LYS B CB    1 
ATOM   9642  C  CG    . LYS B 1 510 ? 133.592 166.754 158.307 1.00 32.23 ?  510 LYS B CG    1 
ATOM   9643  C  CD    . LYS B 1 510 ? 133.754 165.554 157.393 1.00 35.69 ?  510 LYS B CD    1 
ATOM   9644  C  CE    . LYS B 1 510 ? 134.702 164.529 157.992 1.00 39.38 ?  510 LYS B CE    1 
ATOM   9645  N  NZ    . LYS B 1 510 ? 135.393 163.732 156.943 1.00 41.14 1  510 LYS B NZ    1 
ATOM   9646  N  N     . GLY B 1 511 ? 130.573 170.431 158.440 1.00 36.32 ?  511 GLY B N     1 
ATOM   9647  C  CA    . GLY B 1 511 ? 129.579 171.300 157.844 1.00 37.95 ?  511 GLY B CA    1 
ATOM   9648  C  C     . GLY B 1 511 ? 128.828 170.706 156.678 1.00 40.49 ?  511 GLY B C     1 
ATOM   9649  O  O     . GLY B 1 511 ? 128.148 171.442 155.958 1.00 43.77 ?  511 GLY B O     1 
ATOM   9650  N  N     . GLU B 1 512 ? 128.924 169.395 156.468 1.00 34.43 ?  512 GLU B N     1 
ATOM   9651  C  CA    . GLU B 1 512 ? 128.291 168.742 155.333 1.00 30.22 ?  512 GLU B CA    1 
ATOM   9652  C  C     . GLU B 1 512 ? 127.603 167.466 155.787 1.00 31.48 ?  512 GLU B C     1 
ATOM   9653  O  O     . GLU B 1 512 ? 128.098 166.762 156.671 1.00 36.31 ?  512 GLU B O     1 
ATOM   9654  C  CB    . GLU B 1 512 ? 129.311 168.418 154.237 1.00 33.01 ?  512 GLU B CB    1 
ATOM   9655  C  CG    . GLU B 1 512 ? 130.545 167.696 154.743 1.00 32.71 ?  512 GLU B CG    1 
ATOM   9656  C  CD    . GLU B 1 512 ? 131.330 167.033 153.632 1.00 38.28 ?  512 GLU B CD    1 
ATOM   9657  O  OE1   . GLU B 1 512 ? 130.734 166.746 152.572 1.00 37.92 ?  512 GLU B OE1   1 
ATOM   9658  O  OE2   . GLU B 1 512 ? 132.541 166.795 153.819 1.00 39.66 -1 512 GLU B OE2   1 
ATOM   9659  N  N     . THR B 1 513 ? 126.462 167.177 155.177 1.00 34.26 ?  513 THR B N     1 
ATOM   9660  C  CA    . THR B 1 513 ? 125.732 165.934 155.364 1.00 32.81 ?  513 THR B CA    1 
ATOM   9661  C  C     . THR B 1 513 ? 125.920 165.061 154.129 1.00 28.84 ?  513 THR B C     1 
ATOM   9662  O  O     . THR B 1 513 ? 126.659 165.408 153.204 1.00 38.58 ?  513 THR B O     1 
ATOM   9663  C  CB    . THR B 1 513 ? 124.252 166.217 155.626 1.00 31.71 ?  513 THR B CB    1 
ATOM   9664  O  OG1   . THR B 1 513 ? 123.644 166.727 154.434 1.00 33.73 ?  513 THR B OG1   1 
ATOM   9665  C  CG2   . THR B 1 513 ? 124.105 167.243 156.727 1.00 29.90 ?  513 THR B CG2   1 
ATOM   9666  N  N     . PHE B 1 514 ? 125.250 163.913 154.111 1.00 22.87 ?  514 PHE B N     1 
ATOM   9667  C  CA    . PHE B 1 514 ? 125.313 163.110 152.903 1.00 25.65 ?  514 PHE B CA    1 
ATOM   9668  C  C     . PHE B 1 514 ? 124.361 163.676 151.855 1.00 25.87 ?  514 PHE B C     1 
ATOM   9669  O  O     . PHE B 1 514 ? 123.444 164.442 152.157 1.00 32.72 ?  514 PHE B O     1 
ATOM   9670  C  CB    . PHE B 1 514 ? 125.000 161.639 153.188 1.00 20.36 ?  514 PHE B CB    1 
ATOM   9671  C  CG    . PHE B 1 514 ? 123.606 161.381 153.689 1.00 20.87 ?  514 PHE B CG    1 
ATOM   9672  C  CD1   . PHE B 1 514 ? 123.305 161.490 155.033 1.00 18.94 ?  514 PHE B CD1   1 
ATOM   9673  C  CD2   . PHE B 1 514 ? 122.605 160.990 152.816 1.00 20.33 ?  514 PHE B CD2   1 
ATOM   9674  C  CE1   . PHE B 1 514 ? 122.032 161.233 155.495 1.00 13.71 ?  514 PHE B CE1   1 
ATOM   9675  C  CE2   . PHE B 1 514 ? 121.330 160.733 153.273 1.00 17.18 ?  514 PHE B CE2   1 
ATOM   9676  C  CZ    . PHE B 1 514 ? 121.044 160.856 154.614 1.00 16.99 ?  514 PHE B CZ    1 
ATOM   9677  N  N     . ASP B 1 515 ? 124.609 163.307 150.601 1.00 27.24 ?  515 ASP B N     1 
ATOM   9678  C  CA    . ASP B 1 515 ? 123.822 163.850 149.504 1.00 29.97 ?  515 ASP B CA    1 
ATOM   9679  C  C     . ASP B 1 515 ? 122.364 163.432 149.633 1.00 33.38 ?  515 ASP B C     1 
ATOM   9680  O  O     . ASP B 1 515 ? 122.055 162.277 149.939 1.00 43.02 ?  515 ASP B O     1 
ATOM   9681  C  CB    . ASP B 1 515 ? 124.393 163.393 148.163 1.00 31.84 ?  515 ASP B CB    1 
ATOM   9682  C  CG    . ASP B 1 515 ? 125.655 164.144 147.786 1.00 34.96 ?  515 ASP B CG    1 
ATOM   9683  O  OD1   . ASP B 1 515 ? 126.273 164.758 148.679 1.00 34.91 ?  515 ASP B OD1   1 
ATOM   9684  O  OD2   . ASP B 1 515 ? 126.027 164.121 146.595 1.00 37.22 -1 515 ASP B OD2   1 
ATOM   9685  N  N     . GLN B 1 516 ? 121.467 164.392 149.400 1.00 33.32 ?  516 GLN B N     1 
ATOM   9686  C  CA    . GLN B 1 516 ? 120.024 164.188 149.527 1.00 29.64 ?  516 GLN B CA    1 
ATOM   9687  C  C     . GLN B 1 516 ? 119.643 163.773 150.947 1.00 32.54 ?  516 GLN B C     1 
ATOM   9688  O  O     . GLN B 1 516 ? 118.734 162.967 151.154 1.00 39.69 ?  516 GLN B O     1 
ATOM   9689  C  CB    . GLN B 1 516 ? 119.514 163.169 148.505 1.00 27.02 ?  516 GLN B CB    1 
ATOM   9690  C  CG    . GLN B 1 516 ? 119.857 163.509 147.068 1.00 30.65 ?  516 GLN B CG    1 
ATOM   9691  C  CD    . GLN B 1 516 ? 119.703 162.323 146.140 1.00 38.64 ?  516 GLN B CD    1 
ATOM   9692  O  OE1   . GLN B 1 516 ? 118.598 162.000 145.707 1.00 37.40 ?  516 GLN B OE1   1 
ATOM   9693  N  NE2   . GLN B 1 516 ? 120.814 161.664 145.834 1.00 38.99 ?  516 GLN B NE2   1 
ATOM   9694  N  N     . TYR B 1 517 ? 120.350 164.323 151.936 1.00 27.08 ?  517 TYR B N     1 
ATOM   9695  C  CA    . TYR B 1 517 ? 119.976 164.085 153.326 1.00 23.87 ?  517 TYR B CA    1 
ATOM   9696  C  C     . TYR B 1 517 ? 118.654 164.762 153.662 1.00 33.52 ?  517 TYR B C     1 
ATOM   9697  O  O     . TYR B 1 517 ? 117.864 164.234 154.454 1.00 42.64 ?  517 TYR B O     1 
ATOM   9698  C  CB    . TYR B 1 517 ? 121.076 164.574 154.269 1.00 21.30 ?  517 TYR B CB    1 
ATOM   9699  C  CG    . TYR B 1 517 ? 120.567 164.977 155.637 1.00 30.35 ?  517 TYR B CG    1 
ATOM   9700  C  CD1   . TYR B 1 517 ? 120.380 164.031 156.635 1.00 21.55 ?  517 TYR B CD1   1 
ATOM   9701  C  CD2   . TYR B 1 517 ? 120.272 166.304 155.930 1.00 31.64 ?  517 TYR B CD2   1 
ATOM   9702  C  CE1   . TYR B 1 517 ? 119.911 164.392 157.881 1.00 28.97 ?  517 TYR B CE1   1 
ATOM   9703  C  CE2   . TYR B 1 517 ? 119.800 166.671 157.171 1.00 27.98 ?  517 TYR B CE2   1 
ATOM   9704  C  CZ    . TYR B 1 517 ? 119.622 165.713 158.143 1.00 32.53 ?  517 TYR B CZ    1 
ATOM   9705  O  OH    . TYR B 1 517 ? 119.155 166.079 159.382 1.00 37.96 ?  517 TYR B OH    1 
ATOM   9706  N  N     . GLU B 1 518 ? 118.402 165.933 153.075 1.00 31.78 ?  518 GLU B N     1 
ATOM   9707  C  CA    . GLU B 1 518 ? 117.246 166.744 153.444 1.00 35.03 ?  518 GLU B CA    1 
ATOM   9708  C  C     . GLU B 1 518 ? 115.925 166.028 153.206 1.00 37.14 ?  518 GLU B C     1 
ATOM   9709  O  O     . GLU B 1 518 ? 114.935 166.339 153.876 1.00 41.81 ?  518 GLU B O     1 
ATOM   9710  C  CB    . GLU B 1 518 ? 117.268 168.067 152.675 1.00 33.49 ?  518 GLU B CB    1 
ATOM   9711  C  CG    . GLU B 1 518 ? 118.636 168.738 152.615 1.00 37.43 ?  518 GLU B CG    1 
ATOM   9712  C  CD    . GLU B 1 518 ? 119.509 168.207 151.492 1.00 46.20 ?  518 GLU B CD    1 
ATOM   9713  O  OE1   . GLU B 1 518 ? 119.026 168.142 150.341 1.00 44.98 ?  518 GLU B OE1   1 
ATOM   9714  O  OE2   . GLU B 1 518 ? 120.676 167.850 151.760 1.00 40.78 -1 518 GLU B OE2   1 
ATOM   9715  N  N     . GLY B 1 519 ? 115.880 165.084 152.269 1.00 28.86 ?  519 GLY B N     1 
ATOM   9716  C  CA    . GLY B 1 519 ? 114.687 164.291 152.064 1.00 23.81 ?  519 GLY B CA    1 
ATOM   9717  C  C     . GLY B 1 519 ? 114.560 163.071 152.943 1.00 25.57 ?  519 GLY B C     1 
ATOM   9718  O  O     . GLY B 1 519 ? 113.521 162.408 152.919 1.00 33.54 ?  519 GLY B O     1 
ATOM   9719  N  N     . SER B 1 520 ? 115.588 162.761 153.727 1.00 25.82 ?  520 SER B N     1 
ATOM   9720  C  CA    . SER B 1 520 ? 115.594 161.547 154.527 1.00 23.88 ?  520 SER B CA    1 
ATOM   9721  C  C     . SER B 1 520 ? 114.679 161.683 155.740 1.00 26.94 ?  520 SER B C     1 
ATOM   9722  O  O     . SER B 1 520 ? 114.261 162.779 156.123 1.00 27.18 ?  520 SER B O     1 
ATOM   9723  C  CB    . SER B 1 520 ? 117.014 161.210 154.979 1.00 21.54 ?  520 SER B CB    1 
ATOM   9724  O  OG    . SER B 1 520 ? 117.584 162.278 155.712 1.00 26.70 ?  520 SER B OG    1 
ATOM   9725  N  N     . THR B 1 521 ? 114.362 160.535 156.344 1.00 24.19 ?  521 THR B N     1 
ATOM   9726  C  CA    . THR B 1 521 ? 113.568 160.528 157.565 1.00 24.61 ?  521 THR B CA    1 
ATOM   9727  C  C     . THR B 1 521 ? 114.333 161.101 158.747 1.00 28.11 ?  521 THR B C     1 
ATOM   9728  O  O     . THR B 1 521 ? 113.709 161.513 159.732 1.00 32.01 ?  521 THR B O     1 
ATOM   9729  C  CB    . THR B 1 521 ? 113.101 159.109 157.883 1.00 28.66 ?  521 THR B CB    1 
ATOM   9730  O  OG1   . THR B 1 521 ? 114.230 158.302 158.236 1.00 30.86 ?  521 THR B OG1   1 
ATOM   9731  C  CG2   . THR B 1 521 ? 112.412 158.501 156.679 1.00 19.23 ?  521 THR B CG2   1 
ATOM   9732  N  N     . TYR B 1 522 ? 115.664 161.126 158.678 1.00 27.68 ?  522 TYR B N     1 
ATOM   9733  C  CA    . TYR B 1 522 ? 116.444 161.827 159.691 1.00 19.35 ?  522 TYR B CA    1 
ATOM   9734  C  C     . TYR B 1 522 ? 116.144 163.319 159.676 1.00 26.13 ?  522 TYR B C     1 
ATOM   9735  O  O     . TYR B 1 522 ? 116.009 163.946 160.733 1.00 31.32 ?  522 TYR B O     1 
ATOM   9736  C  CB    . TYR B 1 522 ? 117.934 161.590 159.467 1.00 21.34 ?  522 TYR B CB    1 
ATOM   9737  C  CG    . TYR B 1 522 ? 118.356 160.144 159.512 1.00 21.56 ?  522 TYR B CG    1 
ATOM   9738  C  CD1   . TYR B 1 522 ? 118.272 159.415 160.688 1.00 20.11 ?  522 TYR B CD1   1 
ATOM   9739  C  CD2   . TYR B 1 522 ? 118.865 159.515 158.385 1.00 22.80 ?  522 TYR B CD2   1 
ATOM   9740  C  CE1   . TYR B 1 522 ? 118.672 158.099 160.738 1.00 24.06 ?  522 TYR B CE1   1 
ATOM   9741  C  CE2   . TYR B 1 522 ? 119.263 158.198 158.426 1.00 19.98 ?  522 TYR B CE2   1 
ATOM   9742  C  CZ    . TYR B 1 522 ? 119.162 157.494 159.605 1.00 25.74 ?  522 TYR B CZ    1 
ATOM   9743  O  OH    . TYR B 1 522 ? 119.558 156.181 159.651 1.00 29.11 ?  522 TYR B OH    1 
ATOM   9744  N  N     . ALA B 1 523 ? 116.050 163.906 158.482 1.00 33.00 ?  523 ALA B N     1 
ATOM   9745  C  CA    . ALA B 1 523 ? 115.792 165.336 158.369 1.00 26.34 ?  523 ALA B CA    1 
ATOM   9746  C  C     . ALA B 1 523 ? 114.391 165.687 158.849 1.00 30.52 ?  523 ALA B C     1 
ATOM   9747  O  O     . ALA B 1 523 ? 114.196 166.705 159.522 1.00 34.10 ?  523 ALA B O     1 
ATOM   9748  C  CB    . ALA B 1 523 ? 115.995 165.790 156.925 1.00 24.96 ?  523 ALA B CB    1 
ATOM   9749  N  N     . THR B 1 524 ? 113.401 164.860 158.511 1.00 30.85 ?  524 THR B N     1 
ATOM   9750  C  CA    . THR B 1 524 ? 112.024 165.127 158.901 1.00 26.94 ?  524 THR B CA    1 
ATOM   9751  C  C     . THR B 1 524 ? 111.707 164.677 160.319 1.00 34.75 ?  524 THR B C     1 
ATOM   9752  O  O     . THR B 1 524 ? 110.634 165.014 160.831 1.00 41.72 ?  524 THR B O     1 
ATOM   9753  C  CB    . THR B 1 524 ? 111.059 164.449 157.927 1.00 33.13 ?  524 THR B CB    1 
ATOM   9754  O  OG1   . THR B 1 524 ? 110.957 163.055 158.243 1.00 35.03 ?  524 THR B OG1   1 
ATOM   9755  C  CG2   . THR B 1 524 ? 111.554 164.600 156.499 1.00 32.61 ?  524 THR B CG2   1 
ATOM   9756  N  N     . GLY B 1 525 ? 112.602 163.931 160.964 1.00 29.82 ?  525 GLY B N     1 
ATOM   9757  C  CA    . GLY B 1 525 ? 112.368 163.447 162.305 1.00 27.05 ?  525 GLY B CA    1 
ATOM   9758  C  C     . GLY B 1 525 ? 111.514 162.203 162.397 1.00 33.85 ?  525 GLY B C     1 
ATOM   9759  O  O     . GLY B 1 525 ? 111.301 161.700 163.507 1.00 32.98 ?  525 GLY B O     1 
ATOM   9760  N  N     . GLU B 1 526 ? 111.016 161.691 161.270 1.00 37.62 ?  526 GLU B N     1 
ATOM   9761  C  CA    . GLU B 1 526 ? 110.209 160.478 161.288 1.00 35.57 ?  526 GLU B CA    1 
ATOM   9762  C  C     . GLU B 1 526 ? 111.016 159.266 161.735 1.00 35.56 ?  526 GLU B C     1 
ATOM   9763  O  O     . GLU B 1 526 ? 110.442 158.307 162.260 1.00 41.96 ?  526 GLU B O     1 
ATOM   9764  C  CB    . GLU B 1 526 ? 109.600 160.254 159.899 1.00 36.25 ?  526 GLU B CB    1 
ATOM   9765  C  CG    . GLU B 1 526 ? 108.940 158.904 159.683 1.00 36.93 ?  526 GLU B CG    1 
ATOM   9766  C  CD    . GLU B 1 526 ? 108.918 158.495 158.224 1.00 44.72 ?  526 GLU B CD    1 
ATOM   9767  O  OE1   . GLU B 1 526 ? 108.899 159.394 157.357 1.00 43.21 ?  526 GLU B OE1   1 
ATOM   9768  O  OE2   . GLU B 1 526 ? 108.924 157.279 157.944 1.00 42.49 -1 526 GLU B OE2   1 
ATOM   9769  N  N     . TYR B 1 527 ? 112.339 159.305 161.563 1.00 35.15 ?  527 TYR B N     1 
ATOM   9770  C  CA    . TYR B 1 527 ? 113.183 158.202 162.008 1.00 25.96 ?  527 TYR B CA    1 
ATOM   9771  C  C     . TYR B 1 527 ? 113.120 158.029 163.521 1.00 28.26 ?  527 TYR B C     1 
ATOM   9772  O  O     . TYR B 1 527 ? 113.102 156.900 164.025 1.00 35.04 ?  527 TYR B O     1 
ATOM   9773  C  CB    . TYR B 1 527 ? 114.624 158.438 161.557 1.00 23.59 ?  527 TYR B CB    1 
ATOM   9774  C  CG    . TYR B 1 527 ? 115.578 157.334 161.943 1.00 28.20 ?  527 TYR B CG    1 
ATOM   9775  C  CD1   . TYR B 1 527 ? 115.787 156.249 161.107 1.00 23.69 ?  527 TYR B CD1   1 
ATOM   9776  C  CD2   . TYR B 1 527 ? 116.271 157.377 163.146 1.00 28.68 ?  527 TYR B CD2   1 
ATOM   9777  C  CE1   . TYR B 1 527 ? 116.656 155.240 161.455 1.00 23.79 ?  527 TYR B CE1   1 
ATOM   9778  C  CE2   . TYR B 1 527 ? 117.139 156.371 163.503 1.00 24.28 ?  527 TYR B CE2   1 
ATOM   9779  C  CZ    . TYR B 1 527 ? 117.328 155.305 162.654 1.00 23.27 ?  527 TYR B CZ    1 
ATOM   9780  O  OH    . TYR B 1 527 ? 118.195 154.299 163.005 1.00 32.61 ?  527 TYR B OH    1 
ATOM   9781  N  N     . PHE B 1 528 ? 113.088 159.134 164.259 1.00 32.99 ?  528 PHE B N     1 
ATOM   9782  C  CA    . PHE B 1 528 ? 113.212 159.118 165.709 1.00 27.64 ?  528 PHE B CA    1 
ATOM   9783  C  C     . PHE B 1 528 ? 111.885 158.901 166.426 1.00 36.60 ?  528 PHE B C     1 
ATOM   9784  O  O     . PHE B 1 528 ? 111.844 158.999 167.655 1.00 46.33 ?  528 PHE B O     1 
ATOM   9785  C  CB    . PHE B 1 528 ? 113.842 160.426 166.194 1.00 30.83 ?  528 PHE B CB    1 
ATOM   9786  C  CG    . PHE B 1 528 ? 115.203 160.694 165.623 1.00 33.47 ?  528 PHE B CG    1 
ATOM   9787  C  CD1   . PHE B 1 528 ? 116.338 160.216 166.252 1.00 24.97 ?  528 PHE B CD1   1 
ATOM   9788  C  CD2   . PHE B 1 528 ? 115.348 161.432 164.461 1.00 34.19 ?  528 PHE B CD2   1 
ATOM   9789  C  CE1   . PHE B 1 528 ? 117.590 160.463 165.730 1.00 28.35 ?  528 PHE B CE1   1 
ATOM   9790  C  CE2   . PHE B 1 528 ? 116.599 161.680 163.935 1.00 33.73 ?  528 PHE B CE2   1 
ATOM   9791  C  CZ    . PHE B 1 528 ? 117.721 161.196 164.573 1.00 31.75 ?  528 PHE B CZ    1 
ATOM   9792  N  N     . ASP B 1 529 ? 110.806 158.612 165.695 1.00 37.70 ?  529 ASP B N     1 
ATOM   9793  C  CA    . ASP B 1 529 ? 109.487 158.525 166.316 1.00 35.02 ?  529 ASP B CA    1 
ATOM   9794  C  C     . ASP B 1 529 ? 109.436 157.427 167.371 1.00 38.65 ?  529 ASP B C     1 
ATOM   9795  O  O     . ASP B 1 529 ? 109.034 157.665 168.518 1.00 42.72 ?  529 ASP B O     1 
ATOM   9796  C  CB    . ASP B 1 529 ? 108.424 158.288 165.245 1.00 32.50 ?  529 ASP B CB    1 
ATOM   9797  C  CG    . ASP B 1 529 ? 108.267 159.468 164.310 1.00 43.06 ?  529 ASP B CG    1 
ATOM   9798  O  OD1   . ASP B 1 529 ? 108.766 160.564 164.642 1.00 42.20 ?  529 ASP B OD1   1 
ATOM   9799  O  OD2   . ASP B 1 529 ? 107.644 159.298 163.241 1.00 48.54 -1 529 ASP B OD2   1 
ATOM   9800  N  N     . LYS B 1 530 ? 109.850 156.213 167.004 1.00 39.76 ?  530 LYS B N     1 
ATOM   9801  C  CA    . LYS B 1 530 ? 109.825 155.104 167.949 1.00 35.45 ?  530 LYS B CA    1 
ATOM   9802  C  C     . LYS B 1 530 ? 110.829 155.283 169.077 1.00 38.94 ?  530 LYS B C     1 
ATOM   9803  O  O     . LYS B 1 530 ? 110.691 154.639 170.120 1.00 43.21 ?  530 LYS B O     1 
ATOM   9804  C  CB    . LYS B 1 530 ? 110.089 153.787 167.222 1.00 37.18 ?  530 LYS B CB    1 
ATOM   9805  C  CG    . LYS B 1 530 ? 111.541 153.354 167.228 1.00 32.74 ?  530 LYS B CG    1 
ATOM   9806  C  CD    . LYS B 1 530 ? 111.729 152.093 166.418 1.00 38.19 ?  530 LYS B CD    1 
ATOM   9807  C  CE    . LYS B 1 530 ? 113.142 151.571 166.537 1.00 34.66 ?  530 LYS B CE    1 
ATOM   9808  N  NZ    . LYS B 1 530 ? 113.658 151.178 165.203 1.00 43.09 1  530 LYS B NZ    1 
ATOM   9809  N  N     . TYR B 1 531 ? 111.832 156.135 168.894 1.00 39.67 ?  531 TYR B N     1 
ATOM   9810  C  CA    . TYR B 1 531 ? 112.818 156.372 169.935 1.00 32.48 ?  531 TYR B CA    1 
ATOM   9811  C  C     . TYR B 1 531 ? 112.401 157.478 170.890 1.00 31.41 ?  531 TYR B C     1 
ATOM   9812  O  O     . TYR B 1 531 ? 112.734 157.418 172.079 1.00 40.60 ?  531 TYR B O     1 
ATOM   9813  C  CB    . TYR B 1 531 ? 114.170 156.710 169.308 1.00 27.04 ?  531 TYR B CB    1 
ATOM   9814  C  CG    . TYR B 1 531 ? 114.879 155.515 168.719 1.00 32.01 ?  531 TYR B CG    1 
ATOM   9815  C  CD1   . TYR B 1 531 ? 115.229 154.432 169.514 1.00 26.09 ?  531 TYR B CD1   1 
ATOM   9816  C  CD2   . TYR B 1 531 ? 115.201 155.468 167.371 1.00 28.89 ?  531 TYR B CD2   1 
ATOM   9817  C  CE1   . TYR B 1 531 ? 115.879 153.340 168.984 1.00 31.55 ?  531 TYR B CE1   1 
ATOM   9818  C  CE2   . TYR B 1 531 ? 115.851 154.380 166.832 1.00 25.44 ?  531 TYR B CE2   1 
ATOM   9819  C  CZ    . TYR B 1 531 ? 116.188 153.319 167.643 1.00 31.42 ?  531 TYR B CZ    1 
ATOM   9820  O  OH    . TYR B 1 531 ? 116.837 152.230 167.114 1.00 30.43 ?  531 TYR B OH    1 
ATOM   9821  N  N     . VAL B 1 532 ? 111.682 158.488 170.395 1.00 38.40 ?  532 VAL B N     1 
ATOM   9822  C  CA    . VAL B 1 532 ? 111.129 159.520 171.269 1.00 34.75 ?  532 VAL B CA    1 
ATOM   9823  C  C     . VAL B 1 532 ? 109.788 159.124 171.857 1.00 39.86 ?  532 VAL B C     1 
ATOM   9824  O  O     . VAL B 1 532 ? 109.257 159.850 172.708 1.00 47.83 ?  532 VAL B O     1 
ATOM   9825  C  CB    . VAL B 1 532 ? 110.966 160.860 170.526 1.00 40.64 ?  532 VAL B CB    1 
ATOM   9826  C  CG1   . VAL B 1 532 ? 112.284 161.293 169.907 1.00 37.44 ?  532 VAL B CG1   1 
ATOM   9827  C  CG2   . VAL B 1 532 ? 109.878 160.754 169.471 1.00 37.46 ?  532 VAL B CG2   1 
ATOM   9828  N  N     . SER B 1 533 ? 109.217 157.998 171.427 1.00 40.67 ?  533 SER B N     1 
ATOM   9829  C  CA    . SER B 1 533 ? 107.954 157.521 171.972 1.00 40.28 ?  533 SER B CA    1 
ATOM   9830  C  C     . SER B 1 533 ? 108.087 156.291 172.856 1.00 41.24 ?  533 SER B C     1 
ATOM   9831  O  O     . SER B 1 533 ? 107.321 156.148 173.809 1.00 46.20 ?  533 SER B O     1 
ATOM   9832  C  CB    . SER B 1 533 ? 106.971 157.204 170.838 1.00 45.12 ?  533 SER B CB    1 
ATOM   9833  O  OG    . SER B 1 533 ? 107.215 155.917 170.299 1.00 46.69 ?  533 SER B OG    1 
ATOM   9834  N  N     . THR B 1 534 ? 109.037 155.404 172.568 1.00 46.10 ?  534 THR B N     1 
ATOM   9835  C  CA    . THR B 1 534 ? 109.200 154.156 173.298 1.00 41.87 ?  534 THR B CA    1 
ATOM   9836  C  C     . THR B 1 534 ? 110.515 154.172 174.065 1.00 41.15 ?  534 THR B C     1 
ATOM   9837  O  O     . THR B 1 534 ? 111.523 154.692 173.576 1.00 49.01 ?  534 THR B O     1 
ATOM   9838  C  CB    . THR B 1 534 ? 109.167 152.951 172.348 1.00 42.71 ?  534 THR B CB    1 
ATOM   9839  O  OG1   . THR B 1 534 ? 108.035 153.056 171.478 1.00 42.40 ?  534 THR B OG1   1 
ATOM   9840  C  CG2   . THR B 1 534 ? 109.076 151.648 173.128 1.00 43.68 ?  534 THR B CG2   1 
ATOM   9841  N  N     . ASP B 1 535 ? 110.497 153.604 175.265 1.00 43.04 ?  535 ASP B N     1 
ATOM   9842  C  CA    . ASP B 1 535 ? 111.687 153.465 176.091 1.00 42.66 ?  535 ASP B CA    1 
ATOM   9843  C  C     . ASP B 1 535 ? 112.314 152.101 175.837 1.00 45.35 ?  535 ASP B C     1 
ATOM   9844  O  O     . ASP B 1 535 ? 111.622 151.078 175.873 1.00 47.18 ?  535 ASP B O     1 
ATOM   9845  C  CB    . ASP B 1 535 ? 111.344 153.625 177.573 1.00 41.53 ?  535 ASP B CB    1 
ATOM   9846  C  CG    . ASP B 1 535 ? 112.576 153.718 178.449 1.00 47.31 ?  535 ASP B CG    1 
ATOM   9847  O  OD1   . ASP B 1 535 ? 113.338 154.696 178.304 1.00 48.84 ?  535 ASP B OD1   1 
ATOM   9848  O  OD2   . ASP B 1 535 ? 112.781 152.813 179.283 1.00 47.75 -1 535 ASP B OD2   1 
ATOM   9849  N  N     . PHE B 1 536 ? 113.622 152.090 175.583 1.00 40.14 ?  536 PHE B N     1 
ATOM   9850  C  CA    . PHE B 1 536 ? 114.340 150.865 175.252 1.00 34.91 ?  536 PHE B CA    1 
ATOM   9851  C  C     . PHE B 1 536 ? 115.308 150.446 176.355 1.00 35.66 ?  536 PHE B C     1 
ATOM   9852  O  O     . PHE B 1 536 ? 116.278 149.731 176.084 1.00 43.03 ?  536 PHE B O     1 
ATOM   9853  C  CB    . PHE B 1 536 ? 115.078 151.029 173.925 1.00 34.94 ?  536 PHE B CB    1 
ATOM   9854  C  CG    . PHE B 1 536 ? 114.169 151.125 172.734 1.00 31.98 ?  536 PHE B CG    1 
ATOM   9855  C  CD1   . PHE B 1 536 ? 113.759 149.986 172.066 1.00 32.97 ?  536 PHE B CD1   1 
ATOM   9856  C  CD2   . PHE B 1 536 ? 113.723 152.354 172.285 1.00 32.10 ?  536 PHE B CD2   1 
ATOM   9857  C  CE1   . PHE B 1 536 ? 112.922 150.069 170.972 1.00 31.04 ?  536 PHE B CE1   1 
ATOM   9858  C  CE2   . PHE B 1 536 ? 112.885 152.442 171.191 1.00 39.85 ?  536 PHE B CE2   1 
ATOM   9859  C  CZ    . PHE B 1 536 ? 112.485 151.298 170.534 1.00 30.69 ?  536 PHE B CZ    1 
ATOM   9860  N  N     . SER B 1 537 ? 115.067 150.882 177.588 1.00 36.35 ?  537 SER B N     1 
ATOM   9861  C  CA    . SER B 1 537 ? 115.833 150.400 178.721 1.00 34.06 ?  537 SER B CA    1 
ATOM   9862  C  C     . SER B 1 537 ? 115.484 148.939 178.998 1.00 38.38 ?  537 SER B C     1 
ATOM   9863  O  O     . SER B 1 537 ? 114.401 148.472 178.635 1.00 41.45 ?  537 SER B O     1 
ATOM   9864  C  CB    . SER B 1 537 ? 115.553 151.258 179.952 1.00 34.61 ?  537 SER B CB    1 
ATOM   9865  O  OG    . SER B 1 537 ? 114.191 151.178 180.330 1.00 39.68 ?  537 SER B OG    1 
ATOM   9866  N  N     . PRO B 1 538 ? 116.393 148.189 179.621 1.00 37.30 ?  538 PRO B N     1 
ATOM   9867  C  CA    . PRO B 1 538 ? 116.114 146.772 179.883 1.00 35.39 ?  538 PRO B CA    1 
ATOM   9868  C  C     . PRO B 1 538 ? 114.909 146.596 180.793 1.00 40.61 ?  538 PRO B C     1 
ATOM   9869  O  O     . PRO B 1 538 ? 114.687 147.374 181.723 1.00 39.18 ?  538 PRO B O     1 
ATOM   9870  C  CB    . PRO B 1 538 ? 117.402 146.273 180.550 1.00 35.57 ?  538 PRO B CB    1 
ATOM   9871  C  CG    . PRO B 1 538 ? 118.443 147.272 180.189 1.00 34.04 ?  538 PRO B CG    1 
ATOM   9872  C  CD    . PRO B 1 538 ? 117.728 148.579 180.101 1.00 36.00 ?  538 PRO B CD    1 
ATOM   9873  N  N     . LYS B 1 539 ? 114.124 145.558 180.511 1.00 45.36 ?  539 LYS B N     1 
ATOM   9874  C  CA    . LYS B 1 539 ? 112.954 145.220 181.309 1.00 45.52 ?  539 LYS B CA    1 
ATOM   9875  C  C     . LYS B 1 539 ? 113.247 144.169 182.369 1.00 47.99 ?  539 LYS B C     1 
ATOM   9876  O  O     . LYS B 1 539 ? 112.344 143.802 183.125 1.00 48.24 ?  539 LYS B O     1 
ATOM   9877  C  CB    . LYS B 1 539 ? 111.819 144.732 180.403 1.00 45.74 ?  539 LYS B CB    1 
ATOM   9878  C  CG    . LYS B 1 539 ? 111.822 145.344 179.014 1.00 43.95 ?  539 LYS B CG    1 
ATOM   9879  C  CD    . LYS B 1 539 ? 111.311 146.775 179.034 1.00 48.13 ?  539 LYS B CD    1 
ATOM   9880  C  CE    . LYS B 1 539 ? 110.526 147.098 177.773 1.00 49.03 ?  539 LYS B CE    1 
ATOM   9881  N  NZ    . LYS B 1 539 ? 111.396 147.126 176.565 1.00 49.69 1  539 LYS B NZ    1 
ATOM   9882  N  N     . TYR B 1 540 ? 114.481 143.680 182.441 1.00 45.89 ?  540 TYR B N     1 
ATOM   9883  C  CA    . TYR B 1 540 ? 114.873 142.655 183.395 1.00 43.91 ?  540 TYR B CA    1 
ATOM   9884  C  C     . TYR B 1 540 ? 115.981 143.190 184.289 1.00 46.08 ?  540 TYR B C     1 
ATOM   9885  O  O     . TYR B 1 540 ? 116.885 143.890 183.822 1.00 47.79 ?  540 TYR B O     1 
ATOM   9886  C  CB    . TYR B 1 540 ? 115.339 141.385 182.679 1.00 44.43 ?  540 TYR B CB    1 
ATOM   9887  C  CG    . TYR B 1 540 ? 114.239 140.682 181.917 1.00 47.68 ?  540 TYR B CG    1 
ATOM   9888  C  CD1   . TYR B 1 540 ? 113.940 141.032 180.607 1.00 44.57 ?  540 TYR B CD1   1 
ATOM   9889  C  CD2   . TYR B 1 540 ? 113.496 139.671 182.510 1.00 48.48 ?  540 TYR B CD2   1 
ATOM   9890  C  CE1   . TYR B 1 540 ? 112.935 140.394 179.910 1.00 43.43 ?  540 TYR B CE1   1 
ATOM   9891  C  CE2   . TYR B 1 540 ? 112.488 139.027 181.819 1.00 45.36 ?  540 TYR B CE2   1 
ATOM   9892  C  CZ    . TYR B 1 540 ? 112.212 139.392 180.520 1.00 44.75 ?  540 TYR B CZ    1 
ATOM   9893  O  OH    . TYR B 1 540 ? 111.210 138.754 179.831 1.00 49.48 ?  540 TYR B OH    1 
ATOM   9894  N  N     . GLU B 1 541 ? 115.899 142.862 185.581 1.00 49.92 ?  541 GLU B N     1 
ATOM   9895  C  CA    . GLU B 1 541 ? 116.891 143.344 186.535 1.00 45.77 ?  541 GLU B CA    1 
ATOM   9896  C  C     . GLU B 1 541 ? 118.279 142.804 186.212 1.00 46.72 ?  541 GLU B C     1 
ATOM   9897  O  O     . GLU B 1 541 ? 119.280 143.512 186.369 1.00 46.88 ?  541 GLU B O     1 
ATOM   9898  C  CB    . GLU B 1 541 ? 116.481 142.962 187.956 1.00 46.79 ?  541 GLU B CB    1 
ATOM   9899  C  CG    . GLU B 1 541 ? 117.337 143.593 189.042 1.00 48.67 ?  541 GLU B CG    1 
ATOM   9900  C  CD    . GLU B 1 541 ? 118.161 142.572 189.801 1.00 53.09 ?  541 GLU B CD    1 
ATOM   9901  O  OE1   . GLU B 1 541 ? 117.941 141.359 189.596 1.00 50.43 ?  541 GLU B OE1   1 
ATOM   9902  O  OE2   . GLU B 1 541 ? 119.027 142.981 190.602 1.00 53.20 -1 541 GLU B OE2   1 
ATOM   9903  N  N     . LYS B 1 542 ? 118.359 141.546 185.771 1.00 43.44 ?  542 LYS B N     1 
ATOM   9904  C  CA    . LYS B 1 542 ? 119.650 140.974 185.400 1.00 39.82 ?  542 LYS B CA    1 
ATOM   9905  C  C     . LYS B 1 542 ? 120.267 141.717 184.223 1.00 44.78 ?  542 LYS B C     1 
ATOM   9906  O  O     . LYS B 1 542 ? 121.470 142.003 184.222 1.00 42.69 ?  542 LYS B O     1 
ATOM   9907  C  CB    . LYS B 1 542 ? 119.490 139.490 185.072 1.00 41.29 ?  542 LYS B CB    1 
ATOM   9908  C  CG    . LYS B 1 542 ? 120.759 138.831 184.558 1.00 43.38 ?  542 LYS B CG    1 
ATOM   9909  C  CD    . LYS B 1 542 ? 120.588 137.329 184.415 1.00 41.03 ?  542 LYS B CD    1 
ATOM   9910  C  CE    . LYS B 1 542 ? 121.910 136.657 184.085 1.00 44.05 ?  542 LYS B CE    1 
ATOM   9911  N  NZ    . LYS B 1 542 ? 121.815 135.175 184.166 1.00 44.68 1  542 LYS B NZ    1 
ATOM   9912  N  N     . ILE B 1 543 ? 119.460 142.038 183.211 1.00 43.71 ?  543 ILE B N     1 
ATOM   9913  C  CA    . ILE B 1 543 ? 119.971 142.768 182.056 1.00 37.51 ?  543 ILE B CA    1 
ATOM   9914  C  C     . ILE B 1 543 ? 120.322 144.200 182.440 1.00 37.39 ?  543 ILE B C     1 
ATOM   9915  O  O     . ILE B 1 543 ? 121.340 144.743 181.997 1.00 37.90 ?  543 ILE B O     1 
ATOM   9916  C  CB    . ILE B 1 543 ? 118.954 142.723 180.903 1.00 36.35 ?  543 ILE B CB    1 
ATOM   9917  C  CG1   . ILE B 1 543 ? 118.583 141.277 180.571 1.00 39.05 ?  543 ILE B CG1   1 
ATOM   9918  C  CG2   . ILE B 1 543 ? 119.514 143.421 179.681 1.00 36.17 ?  543 ILE B CG2   1 
ATOM   9919  C  CD1   . ILE B 1 543 ? 119.772 140.367 180.375 1.00 33.21 ?  543 ILE B CD1   1 
ATOM   9920  N  N     . ALA B 1 544 ? 119.487 144.836 183.266 1.00 35.49 ?  544 ALA B N     1 
ATOM   9921  C  CA    . ALA B 1 544 ? 119.781 146.194 183.710 1.00 39.29 ?  544 ALA B CA    1 
ATOM   9922  C  C     . ALA B 1 544 ? 121.062 146.250 184.530 1.00 44.33 ?  544 ALA B C     1 
ATOM   9923  O  O     . ALA B 1 544 ? 121.733 147.287 184.562 1.00 48.55 ?  544 ALA B O     1 
ATOM   9924  C  CB    . ALA B 1 544 ? 118.609 146.750 184.516 1.00 40.47 ?  544 ALA B CB    1 
ATOM   9925  N  N     . ASN B 1 545 ? 121.415 145.150 185.200 1.00 45.04 ?  545 ASN B N     1 
ATOM   9926  C  CA    . ASN B 1 545 ? 122.676 145.105 185.931 1.00 45.81 ?  545 ASN B CA    1 
ATOM   9927  C  C     . ASN B 1 545 ? 123.865 144.978 184.989 1.00 44.60 ?  545 ASN B C     1 
ATOM   9928  O  O     . ASN B 1 545 ? 124.977 145.388 185.340 1.00 46.40 ?  545 ASN B O     1 
ATOM   9929  C  CB    . ASN B 1 545 ? 122.666 143.948 186.929 1.00 47.28 ?  545 ASN B CB    1 
ATOM   9930  C  CG    . ASN B 1 545 ? 121.833 144.249 188.158 1.00 49.62 ?  545 ASN B CG    1 
ATOM   9931  O  OD1   . ASN B 1 545 ? 121.669 145.406 188.543 1.00 48.80 ?  545 ASN B OD1   1 
ATOM   9932  N  ND2   . ASN B 1 545 ? 121.304 143.205 188.784 1.00 44.89 ?  545 ASN B ND2   1 
ATOM   9933  N  N     . LEU B 1 546 ? 123.655 144.410 183.799 1.00 44.21 ?  546 LEU B N     1 
ATOM   9934  C  CA    . LEU B 1 546 ? 124.740 144.299 182.829 1.00 37.40 ?  546 LEU B CA    1 
ATOM   9935  C  C     . LEU B 1 546 ? 125.204 145.666 182.350 1.00 37.79 ?  546 LEU B C     1 
ATOM   9936  O  O     . LEU B 1 546 ? 126.376 145.836 181.998 1.00 39.54 ?  546 LEU B O     1 
ATOM   9937  C  CB    . LEU B 1 546 ? 124.299 143.446 181.641 1.00 36.36 ?  546 LEU B CB    1 
ATOM   9938  C  CG    . LEU B 1 546 ? 123.904 141.998 181.929 1.00 38.55 ?  546 LEU B CG    1 
ATOM   9939  C  CD1   . LEU B 1 546 ? 123.401 141.326 180.664 1.00 37.37 ?  546 LEU B CD1   1 
ATOM   9940  C  CD2   . LEU B 1 546 ? 125.071 141.227 182.518 1.00 37.55 ?  546 LEU B CD2   1 
ATOM   9941  N  N     . PHE B 1 547 ? 124.308 146.652 182.341 1.00 39.72 ?  547 PHE B N     1 
ATOM   9942  C  CA    . PHE B 1 547 ? 124.616 147.997 181.878 1.00 38.97 ?  547 PHE B CA    1 
ATOM   9943  C  C     . PHE B 1 547 ? 124.968 148.939 183.022 1.00 40.70 ?  547 PHE B C     1 
ATOM   9944  O  O     . PHE B 1 547 ? 124.913 150.161 182.848 1.00 44.69 ?  547 PHE B O     1 
ATOM   9945  C  CB    . PHE B 1 547 ? 123.443 148.560 181.074 1.00 37.62 ?  547 PHE B CB    1 
ATOM   9946  C  CG    . PHE B 1 547 ? 123.212 147.863 179.764 1.00 39.12 ?  547 PHE B CG    1 
ATOM   9947  C  CD1   . PHE B 1 547 ? 122.387 146.754 179.691 1.00 37.61 ?  547 PHE B CD1   1 
ATOM   9948  C  CD2   . PHE B 1 547 ? 123.815 148.318 178.606 1.00 38.44 ?  547 PHE B CD2   1 
ATOM   9949  C  CE1   . PHE B 1 547 ? 122.172 146.113 178.487 1.00 38.08 ?  547 PHE B CE1   1 
ATOM   9950  C  CE2   . PHE B 1 547 ? 123.603 147.681 177.400 1.00 33.49 ?  547 PHE B CE2   1 
ATOM   9951  C  CZ    . PHE B 1 547 ? 122.781 146.578 177.341 1.00 35.40 ?  547 PHE B CZ    1 
ATOM   9952  N  N     . GLU B 1 548 ? 125.314 148.397 184.187 1.00 47.33 ?  548 GLU B N     1 
ATOM   9953  C  CA    . GLU B 1 548 ? 125.679 149.231 185.323 1.00 48.82 ?  548 GLU B CA    1 
ATOM   9954  C  C     . GLU B 1 548 ? 126.932 150.039 185.008 1.00 52.47 ?  548 GLU B C     1 
ATOM   9955  O  O     . GLU B 1 548 ? 127.867 149.546 184.373 1.00 52.34 ?  548 GLU B O     1 
ATOM   9956  C  CB    . GLU B 1 548 ? 125.907 148.367 186.563 1.00 47.67 ?  548 GLU B CB    1 
ATOM   9957  C  CG    . GLU B 1 548 ? 124.672 148.178 187.427 1.00 50.67 ?  548 GLU B CG    1 
ATOM   9958  C  CD    . GLU B 1 548 ? 124.848 147.081 188.459 1.00 56.24 ?  548 GLU B CD    1 
ATOM   9959  O  OE1   . GLU B 1 548 ? 125.720 146.211 188.259 1.00 55.02 ?  548 GLU B OE1   1 
ATOM   9960  O  OE2   . GLU B 1 548 ? 124.116 147.090 189.472 1.00 55.23 -1 548 GLU B OE2   1 
ATOM   9961  N  N     . GLY B 1 549 ? 126.946 151.291 185.457 1.00 50.26 ?  549 GLY B N     1 
ATOM   9962  C  CA    . GLY B 1 549 ? 128.037 152.186 185.137 1.00 49.92 ?  549 GLY B CA    1 
ATOM   9963  C  C     . GLY B 1 549 ? 128.012 152.727 183.729 1.00 51.73 ?  549 GLY B C     1 
ATOM   9964  O  O     . GLY B 1 549 ? 129.021 153.276 183.273 1.00 54.70 ?  549 GLY B O     1 
ATOM   9965  N  N     . MET B 1 550 ? 126.892 152.589 183.024 1.00 48.89 ?  550 MET B N     1 
ATOM   9966  C  CA    . MET B 1 550 ? 126.771 153.017 181.638 1.00 44.47 ?  550 MET B CA    1 
ATOM   9967  C  C     . MET B 1 550 ? 125.415 153.674 181.448 1.00 46.73 ?  550 MET B C     1 
ATOM   9968  O  O     . MET B 1 550 ? 124.385 153.075 181.766 1.00 52.25 ?  550 MET B O     1 
ATOM   9969  C  CB    . MET B 1 550 ? 126.928 151.828 180.688 1.00 44.64 ?  550 MET B CB    1 
ATOM   9970  C  CG    . MET B 1 550 ? 127.642 152.151 179.396 1.00 51.54 ?  550 MET B CG    1 
ATOM   9971  S  SD    . MET B 1 550 ? 127.727 150.725 178.302 1.00 60.33 ?  550 MET B SD    1 
ATOM   9972  C  CE    . MET B 1 550 ? 127.685 149.377 179.477 1.00 48.02 ?  550 MET B CE    1 
ATOM   9973  N  N     . HIS B 1 551 ? 125.416 154.900 180.931 1.00 42.96 ?  551 HIS B N     1 
ATOM   9974  C  CA    . HIS B 1 551 ? 124.176 155.641 180.752 1.00 43.58 ?  551 HIS B CA    1 
ATOM   9975  C  C     . HIS B 1 551 ? 123.424 155.106 179.540 1.00 46.12 ?  551 HIS B C     1 
ATOM   9976  O  O     . HIS B 1 551 ? 123.904 155.211 178.406 1.00 44.91 ?  551 HIS B O     1 
ATOM   9977  C  CB    . HIS B 1 551 ? 124.455 157.132 180.591 1.00 41.99 ?  551 HIS B CB    1 
ATOM   9978  C  CG    . HIS B 1 551 ? 123.251 157.926 180.190 1.00 46.24 ?  551 HIS B CG    1 
ATOM   9979  N  ND1   . HIS B 1 551 ? 122.295 158.335 181.095 1.00 49.73 ?  551 HIS B ND1   1 
ATOM   9980  C  CD2   . HIS B 1 551 ? 122.845 158.382 178.982 1.00 46.93 ?  551 HIS B CD2   1 
ATOM   9981  C  CE1   . HIS B 1 551 ? 121.352 159.009 180.461 1.00 47.40 ?  551 HIS B CE1   1 
ATOM   9982  N  NE2   . HIS B 1 551 ? 121.663 159.053 179.179 1.00 46.40 ?  551 HIS B NE2   1 
ATOM   9983  N  N     . ILE B 1 552 ? 122.251 154.534 179.780 1.00 40.04 ?  552 ILE B N     1 
ATOM   9984  C  CA    . ILE B 1 552 ? 121.381 154.046 178.717 1.00 37.77 ?  552 ILE B CA    1 
ATOM   9985  C  C     . ILE B 1 552 ? 120.558 155.227 178.207 1.00 38.12 ?  552 ILE B C     1 
ATOM   9986  O  O     . ILE B 1 552 ? 119.876 155.879 179.014 1.00 37.71 ?  552 ILE B O     1 
ATOM   9987  C  CB    . ILE B 1 552 ? 120.473 152.915 179.212 1.00 36.38 ?  552 ILE B CB    1 
ATOM   9988  C  CG1   . ILE B 1 552 ? 121.320 151.746 179.715 1.00 35.67 ?  552 ILE B CG1   1 
ATOM   9989  C  CG2   . ILE B 1 552 ? 119.532 152.461 178.110 1.00 36.34 ?  552 ILE B CG2   1 
ATOM   9990  C  CD1   . ILE B 1 552 ? 120.545 150.738 180.519 1.00 38.89 ?  552 ILE B CD1   1 
ATOM   9991  N  N     . PRO B 1 553 ? 120.608 155.544 176.914 1.00 40.67 ?  553 PRO B N     1 
ATOM   9992  C  CA    . PRO B 1 553 ? 119.849 156.694 176.408 1.00 37.77 ?  553 PRO B CA    1 
ATOM   9993  C  C     . PRO B 1 553 ? 118.360 156.545 176.676 1.00 40.06 ?  553 PRO B C     1 
ATOM   9994  O  O     . PRO B 1 553 ? 117.779 155.473 176.503 1.00 41.00 ?  553 PRO B O     1 
ATOM   9995  C  CB    . PRO B 1 553 ? 120.153 156.684 174.907 1.00 34.16 ?  553 PRO B CB    1 
ATOM   9996  C  CG    . PRO B 1 553 ? 121.452 155.972 174.794 1.00 32.33 ?  553 PRO B CG    1 
ATOM   9997  C  CD    . PRO B 1 553 ? 121.451 154.937 175.873 1.00 33.34 ?  553 PRO B CD    1 
ATOM   9998  N  N     . THR B 1 554 ? 117.746 157.645 177.097 1.00 43.12 ?  554 THR B N     1 
ATOM   9999  C  CA    . THR B 1 554 ? 116.335 157.675 177.428 1.00 41.44 ?  554 THR B CA    1 
ATOM   10000 C  C     . THR B 1 554 ? 115.550 158.339 176.302 1.00 38.99 ?  554 THR B C     1 
ATOM   10001 O  O     . THR B 1 554 ? 116.084 158.669 175.241 1.00 37.79 ?  554 THR B O     1 
ATOM   10002 C  CB    . THR B 1 554 ? 116.110 158.405 178.754 1.00 37.55 ?  554 THR B CB    1 
ATOM   10003 O  OG1   . THR B 1 554 ? 116.287 159.813 178.560 1.00 43.39 ?  554 THR B OG1   1 
ATOM   10004 C  CG2   . THR B 1 554 ? 117.097 157.918 179.800 1.00 36.57 ?  554 THR B CG2   1 
ATOM   10005 N  N     . THR B 1 555 ? 114.252 158.527 176.541 1.00 42.76 ?  555 THR B N     1 
ATOM   10006 C  CA    . THR B 1 555 ? 113.417 159.236 175.580 1.00 39.77 ?  555 THR B CA    1 
ATOM   10007 C  C     . THR B 1 555 ? 113.852 160.691 175.442 1.00 40.86 ?  555 THR B C     1 
ATOM   10008 O  O     . THR B 1 555 ? 113.875 161.235 174.332 1.00 44.26 ?  555 THR B O     1 
ATOM   10009 C  CB    . THR B 1 555 ? 111.949 159.135 175.998 1.00 43.88 ?  555 THR B CB    1 
ATOM   10010 O  OG1   . THR B 1 555 ? 111.444 157.839 175.650 1.00 42.11 ?  555 THR B OG1   1 
ATOM   10011 C  CG2   . THR B 1 555 ? 111.112 160.196 175.311 1.00 42.31 ?  555 THR B CG2   1 
ATOM   10012 N  N     . GLU B 1 556 ? 114.212 161.335 176.554 1.00 37.54 ?  556 GLU B N     1 
ATOM   10013 C  CA    . GLU B 1 556 ? 114.699 162.710 176.489 1.00 41.22 ?  556 GLU B CA    1 
ATOM   10014 C  C     . GLU B 1 556 ? 116.030 162.795 175.752 1.00 41.20 ?  556 GLU B C     1 
ATOM   10015 O  O     . GLU B 1 556 ? 116.264 163.739 174.988 1.00 45.19 ?  556 GLU B O     1 
ATOM   10016 C  CB    . GLU B 1 556 ? 114.823 163.289 177.898 1.00 42.16 ?  556 GLU B CB    1 
ATOM   10017 C  CG    . GLU B 1 556 ? 113.489 163.547 178.585 1.00 43.79 ?  556 GLU B CG    1 
ATOM   10018 C  CD    . GLU B 1 556 ? 112.445 164.125 177.646 1.00 46.68 ?  556 GLU B CD    1 
ATOM   10019 O  OE1   . GLU B 1 556 ? 112.459 165.353 177.423 1.00 44.65 ?  556 GLU B OE1   1 
ATOM   10020 O  OE2   . GLU B 1 556 ? 111.604 163.354 177.137 1.00 46.96 -1 556 GLU B OE2   1 
ATOM   10021 N  N     . ASP B 1 557 ? 116.918 161.822 175.973 1.00 39.92 ?  557 ASP B N     1 
ATOM   10022 C  CA    . ASP B 1 557 ? 118.172 161.784 175.228 1.00 35.53 ?  557 ASP B CA    1 
ATOM   10023 C  C     . ASP B 1 557 ? 117.916 161.621 173.738 1.00 36.19 ?  557 ASP B C     1 
ATOM   10024 O  O     . ASP B 1 557 ? 118.591 162.245 172.911 1.00 39.67 ?  557 ASP B O     1 
ATOM   10025 C  CB    . ASP B 1 557 ? 119.058 160.651 175.745 1.00 35.05 ?  557 ASP B CB    1 
ATOM   10026 C  CG    . ASP B 1 557 ? 119.546 160.890 177.157 1.00 42.94 ?  557 ASP B CG    1 
ATOM   10027 O  OD1   . ASP B 1 557 ? 120.144 161.957 177.408 1.00 44.87 ?  557 ASP B OD1   1 
ATOM   10028 O  OD2   . ASP B 1 557 ? 119.335 160.009 178.015 1.00 43.75 -1 557 ASP B OD2   1 
ATOM   10029 N  N     . TRP B 1 558 ? 116.939 160.790 173.374 1.00 30.30 ?  558 TRP B N     1 
ATOM   10030 C  CA    . TRP B 1 558 ? 116.605 160.621 171.965 1.00 26.01 ?  558 TRP B CA    1 
ATOM   10031 C  C     . TRP B 1 558 ? 115.978 161.878 171.376 1.00 31.95 ?  558 TRP B C     1 
ATOM   10032 O  O     . TRP B 1 558 ? 116.213 162.189 170.206 1.00 37.89 ?  558 TRP B O     1 
ATOM   10033 C  CB    . TRP B 1 558 ? 115.678 159.422 171.792 1.00 32.42 ?  558 TRP B CB    1 
ATOM   10034 C  CG    . TRP B 1 558 ? 116.416 158.136 171.620 1.00 28.63 ?  558 TRP B CG    1 
ATOM   10035 C  CD1   . TRP B 1 558 ? 116.535 157.130 172.532 1.00 25.06 ?  558 TRP B CD1   1 
ATOM   10036 C  CD2   . TRP B 1 558 ? 117.141 157.714 170.460 1.00 29.59 ?  558 TRP B CD2   1 
ATOM   10037 N  NE1   . TRP B 1 558 ? 117.287 156.108 172.012 1.00 31.93 ?  558 TRP B NE1   1 
ATOM   10038 C  CE2   . TRP B 1 558 ? 117.669 156.440 170.740 1.00 29.94 ?  558 TRP B CE2   1 
ATOM   10039 C  CE3   . TRP B 1 558 ? 117.386 158.286 169.209 1.00 30.69 ?  558 TRP B CE3   1 
ATOM   10040 C  CZ2   . TRP B 1 558 ? 118.431 155.731 169.816 1.00 25.80 ?  558 TRP B CZ2   1 
ATOM   10041 C  CZ3   . TRP B 1 558 ? 118.143 157.582 168.296 1.00 28.24 ?  558 TRP B CZ3   1 
ATOM   10042 C  CH2   . TRP B 1 558 ? 118.655 156.318 168.603 1.00 23.67 ?  558 TRP B CH2   1 
ATOM   10043 N  N     . LYS B 1 559 ? 115.183 162.612 172.159 1.00 36.67 ?  559 LYS B N     1 
ATOM   10044 C  CA    . LYS B 1 559 ? 114.663 163.890 171.682 1.00 34.56 ?  559 LYS B CA    1 
ATOM   10045 C  C     . LYS B 1 559 ? 115.787 164.895 171.462 1.00 37.87 ?  559 LYS B C     1 
ATOM   10046 O  O     . LYS B 1 559 ? 115.780 165.644 170.476 1.00 38.90 ?  559 LYS B O     1 
ATOM   10047 C  CB    . LYS B 1 559 ? 113.639 164.444 172.670 1.00 37.71 ?  559 LYS B CB    1 
ATOM   10048 C  CG    . LYS B 1 559 ? 112.286 163.762 172.609 1.00 42.19 ?  559 LYS B CG    1 
ATOM   10049 C  CD    . LYS B 1 559 ? 111.381 164.239 173.729 1.00 38.05 ?  559 LYS B CD    1 
ATOM   10050 C  CE    . LYS B 1 559 ? 110.146 163.366 173.847 1.00 41.69 ?  559 LYS B CE    1 
ATOM   10051 N  NZ    . LYS B 1 559 ? 109.618 163.347 175.238 1.00 39.05 1  559 LYS B NZ    1 
ATOM   10052 N  N     . LYS B 1 560 ? 116.760 164.927 172.374 1.00 34.00 ?  560 LYS B N     1 
ATOM   10053 C  CA    . LYS B 1 560 ? 117.915 165.801 172.194 1.00 33.62 ?  560 LYS B CA    1 
ATOM   10054 C  C     . LYS B 1 560 ? 118.706 165.413 170.951 1.00 38.20 ?  560 LYS B C     1 
ATOM   10055 O  O     . LYS B 1 560 ? 119.164 166.282 170.201 1.00 42.72 ?  560 LYS B O     1 
ATOM   10056 C  CB    . LYS B 1 560 ? 118.803 165.756 173.436 1.00 37.36 ?  560 LYS B CB    1 
ATOM   10057 C  CG    . LYS B 1 560 ? 118.393 166.730 174.525 1.00 37.70 ?  560 LYS B CG    1 
ATOM   10058 C  CD    . LYS B 1 560 ? 119.153 166.468 175.814 1.00 42.97 ?  560 LYS B CD    1 
ATOM   10059 C  CE    . LYS B 1 560 ? 118.242 166.586 177.025 1.00 39.49 ?  560 LYS B CE    1 
ATOM   10060 N  NZ    . LYS B 1 560 ? 118.330 165.387 177.904 1.00 44.10 1  560 LYS B NZ    1 
ATOM   10061 N  N     . LEU B 1 561 ? 118.875 164.111 170.715 1.00 36.05 ?  561 LEU B N     1 
ATOM   10062 C  CA    . LEU B 1 561 ? 119.557 163.656 169.508 1.00 30.62 ?  561 LEU B CA    1 
ATOM   10063 C  C     . LEU B 1 561 ? 118.775 164.027 168.254 1.00 34.86 ?  561 LEU B C     1 
ATOM   10064 O  O     . LEU B 1 561 ? 119.366 164.388 167.233 1.00 39.07 ?  561 LEU B O     1 
ATOM   10065 C  CB    . LEU B 1 561 ? 119.787 162.147 169.567 1.00 30.75 ?  561 LEU B CB    1 
ATOM   10066 C  CG    . LEU B 1 561 ? 120.575 161.570 168.391 1.00 32.12 ?  561 LEU B CG    1 
ATOM   10067 C  CD1   . LEU B 1 561 ? 121.904 162.285 168.250 1.00 28.52 ?  561 LEU B CD1   1 
ATOM   10068 C  CD2   . LEU B 1 561 ? 120.781 160.078 168.558 1.00 29.41 ?  561 LEU B CD2   1 
ATOM   10069 N  N     . LYS B 1 562 ? 117.446 163.928 168.309 1.00 30.80 ?  562 LYS B N     1 
ATOM   10070 C  CA    . LYS B 1 562 ? 116.618 164.324 167.175 1.00 32.43 ?  562 LYS B CA    1 
ATOM   10071 C  C     . LYS B 1 562 ? 116.778 165.807 166.870 1.00 37.34 ?  562 LYS B C     1 
ATOM   10072 O  O     . LYS B 1 562 ? 116.913 166.200 165.705 1.00 41.07 ?  562 LYS B O     1 
ATOM   10073 C  CB    . LYS B 1 562 ? 115.156 163.987 167.466 1.00 30.73 ?  562 LYS B CB    1 
ATOM   10074 C  CG    . LYS B 1 562 ? 114.170 164.484 166.430 1.00 31.43 ?  562 LYS B CG    1 
ATOM   10075 C  CD    . LYS B 1 562 ? 112.747 164.210 166.882 1.00 29.50 ?  562 LYS B CD    1 
ATOM   10076 C  CE    . LYS B 1 562 ? 111.742 164.517 165.790 1.00 35.36 ?  562 LYS B CE    1 
ATOM   10077 N  NZ    . LYS B 1 562 ? 110.438 163.851 166.055 1.00 39.56 1  562 LYS B NZ    1 
ATOM   10078 N  N     . ALA B 1 563 ? 116.779 166.644 167.910 1.00 33.87 ?  563 ALA B N     1 
ATOM   10079 C  CA    . ALA B 1 563 ? 117.001 168.072 167.708 1.00 30.54 ?  563 ALA B CA    1 
ATOM   10080 C  C     . ALA B 1 563 ? 118.393 168.340 167.147 1.00 33.60 ?  563 ALA B C     1 
ATOM   10081 O  O     . ALA B 1 563 ? 118.562 169.182 166.258 1.00 40.23 ?  563 ALA B O     1 
ATOM   10082 C  CB    . ALA B 1 563 ? 116.796 168.825 169.021 1.00 34.80 ?  563 ALA B CB    1 
ATOM   10083 N  N     . PHE B 1 564 ? 119.401 167.626 167.654 1.00 36.35 ?  564 PHE B N     1 
ATOM   10084 C  CA    . PHE B 1 564 ? 120.765 167.803 167.167 1.00 31.55 ?  564 PHE B CA    1 
ATOM   10085 C  C     . PHE B 1 564 ? 120.884 167.413 165.698 1.00 36.66 ?  564 PHE B C     1 
ATOM   10086 O  O     . PHE B 1 564 ? 121.566 168.092 164.922 1.00 41.78 ?  564 PHE B O     1 
ATOM   10087 C  CB    . PHE B 1 564 ? 121.726 166.979 168.025 1.00 32.48 ?  564 PHE B CB    1 
ATOM   10088 C  CG    . PHE B 1 564 ? 123.171 167.334 167.834 1.00 35.64 ?  564 PHE B CG    1 
ATOM   10089 C  CD1   . PHE B 1 564 ? 123.703 168.468 168.421 1.00 35.29 ?  564 PHE B CD1   1 
ATOM   10090 C  CD2   . PHE B 1 564 ? 123.999 166.527 167.076 1.00 39.70 ?  564 PHE B CD2   1 
ATOM   10091 C  CE1   . PHE B 1 564 ? 125.034 168.792 168.250 1.00 41.01 ?  564 PHE B CE1   1 
ATOM   10092 C  CE2   . PHE B 1 564 ? 125.329 166.847 166.900 1.00 38.51 ?  564 PHE B CE2   1 
ATOM   10093 C  CZ    . PHE B 1 564 ? 125.848 167.981 167.487 1.00 38.19 ?  564 PHE B CZ    1 
ATOM   10094 N  N     . VAL B 1 565 ? 120.230 166.322 165.302 1.00 32.89 ?  565 VAL B N     1 
ATOM   10095 C  CA    . VAL B 1 565 ? 120.283 165.878 163.913 1.00 29.38 ?  565 VAL B CA    1 
ATOM   10096 C  C     . VAL B 1 565 ? 119.530 166.848 163.013 1.00 35.25 ?  565 VAL B C     1 
ATOM   10097 O  O     . VAL B 1 565 ? 119.961 167.138 161.891 1.00 39.02 ?  565 VAL B O     1 
ATOM   10098 C  CB    . VAL B 1 565 ? 119.739 164.443 163.797 1.00 29.93 ?  565 VAL B CB    1 
ATOM   10099 C  CG1   . VAL B 1 565 ? 119.380 164.112 162.357 1.00 32.07 ?  565 VAL B CG1   1 
ATOM   10100 C  CG2   . VAL B 1 565 ? 120.757 163.455 164.329 1.00 32.11 ?  565 VAL B CG2   1 
ATOM   10101 N  N     . ALA B 1 566 ? 118.398 167.372 163.489 1.00 36.92 ?  566 ALA B N     1 
ATOM   10102 C  CA    . ALA B 1 566 ? 117.671 168.370 162.712 1.00 34.67 ?  566 ALA B CA    1 
ATOM   10103 C  C     . ALA B 1 566 ? 118.503 169.631 162.523 1.00 37.50 ?  566 ALA B C     1 
ATOM   10104 O  O     . ALA B 1 566 ? 118.484 170.243 161.450 1.00 43.33 ?  566 ALA B O     1 
ATOM   10105 C  CB    . ALA B 1 566 ? 116.343 168.699 163.391 1.00 34.64 ?  566 ALA B CB    1 
ATOM   10106 N  N     . GLU B 1 567 ? 119.238 170.038 163.558 1.00 38.02 ?  567 GLU B N     1 
ATOM   10107 C  CA    . GLU B 1 567 ? 120.033 171.257 163.471 1.00 37.40 ?  567 GLU B CA    1 
ATOM   10108 C  C     . GLU B 1 567 ? 121.256 171.069 162.580 1.00 42.54 ?  567 GLU B C     1 
ATOM   10109 O  O     . GLU B 1 567 ? 121.550 171.916 161.728 1.00 50.47 ?  567 GLU B O     1 
ATOM   10110 C  CB    . GLU B 1 567 ? 120.456 171.701 164.870 1.00 39.50 ?  567 GLU B CB    1 
ATOM   10111 C  CG    . GLU B 1 567 ? 121.209 173.016 164.902 1.00 42.29 ?  567 GLU B CG    1 
ATOM   10112 C  CD    . GLU B 1 567 ? 121.774 173.323 166.275 1.00 49.53 ?  567 GLU B CD    1 
ATOM   10113 O  OE1   . GLU B 1 567 ? 121.322 172.698 167.256 1.00 50.64 ?  567 GLU B OE1   1 
ATOM   10114 O  OE2   . GLU B 1 567 ? 122.665 174.191 166.372 1.00 46.30 -1 567 GLU B OE2   1 
ATOM   10115 N  N     . HIS B 1 568 ? 121.980 169.964 162.754 1.00 44.69 ?  568 HIS B N     1 
ATOM   10116 C  CA    . HIS B 1 568 ? 123.292 169.803 162.144 1.00 40.43 ?  568 HIS B CA    1 
ATOM   10117 C  C     . HIS B 1 568 ? 123.332 168.779 161.021 1.00 35.70 ?  568 HIS B C     1 
ATOM   10118 O  O     . HIS B 1 568 ? 124.337 168.714 160.305 1.00 44.65 ?  568 HIS B O     1 
ATOM   10119 C  CB    . HIS B 1 568 ? 124.324 169.414 163.211 1.00 39.32 ?  568 HIS B CB    1 
ATOM   10120 C  CG    . HIS B 1 568 ? 124.599 170.496 164.206 1.00 39.80 ?  568 HIS B CG    1 
ATOM   10121 N  ND1   . HIS B 1 568 ? 124.215 170.407 165.526 1.00 41.70 ?  568 HIS B ND1   1 
ATOM   10122 C  CD2   . HIS B 1 568 ? 125.204 171.699 164.071 1.00 40.68 ?  568 HIS B CD2   1 
ATOM   10123 C  CE1   . HIS B 1 568 ? 124.582 171.503 166.165 1.00 41.70 ?  568 HIS B CE1   1 
ATOM   10124 N  NE2   . HIS B 1 568 ? 125.185 172.303 165.305 1.00 46.63 ?  568 HIS B NE2   1 
ATOM   10125 N  N     . GLY B 1 569 ? 122.290 167.987 160.846 1.00 30.82 ?  569 GLY B N     1 
ATOM   10126 C  CA    . GLY B 1 569 ? 122.292 166.996 159.795 1.00 29.68 ?  569 GLY B CA    1 
ATOM   10127 C  C     . GLY B 1 569 ? 122.959 165.704 160.212 1.00 30.05 ?  569 GLY B C     1 
ATOM   10128 O  O     . GLY B 1 569 ? 123.320 165.479 161.370 1.00 38.28 ?  569 GLY B O     1 
ATOM   10129 N  N     . MET B 1 570 ? 123.116 164.830 159.225 1.00 26.75 ?  570 MET B N     1 
ATOM   10130 C  CA    . MET B 1 570 ? 123.637 163.488 159.439 1.00 22.89 ?  570 MET B CA    1 
ATOM   10131 C  C     . MET B 1 570 ? 124.664 163.200 158.356 1.00 24.69 ?  570 MET B C     1 
ATOM   10132 O  O     . MET B 1 570 ? 124.382 163.391 157.170 1.00 30.73 ?  570 MET B O     1 
ATOM   10133 C  CB    . MET B 1 570 ? 122.492 162.472 159.412 1.00 31.01 ?  570 MET B CB    1 
ATOM   10134 C  CG    . MET B 1 570 ? 121.980 162.083 160.790 1.00 24.56 ?  570 MET B CG    1 
ATOM   10135 S  SD    . MET B 1 570 ? 121.481 160.362 160.920 1.00 46.73 ?  570 MET B SD    1 
ATOM   10136 C  CE    . MET B 1 570 ? 123.054 159.546 160.991 1.00 26.89 ?  570 MET B CE    1 
ATOM   10137 N  N     . TYR B 1 571 ? 125.857 162.758 158.761 1.00 21.99 ?  571 TYR B N     1 
ATOM   10138 C  CA    . TYR B 1 571 ? 126.947 162.606 157.803 1.00 13.75 ?  571 TYR B CA    1 
ATOM   10139 C  C     . TYR B 1 571 ? 126.843 161.324 156.989 1.00 22.97 ?  571 TYR B C     1 
ATOM   10140 O  O     . TYR B 1 571 ? 127.228 161.311 155.816 1.00 21.03 ?  571 TYR B O     1 
ATOM   10141 C  CB    . TYR B 1 571 ? 128.295 162.651 158.519 1.00 18.76 ?  571 TYR B CB    1 
ATOM   10142 C  CG    . TYR B 1 571 ? 129.476 162.724 157.577 1.00 21.18 ?  571 TYR B CG    1 
ATOM   10143 C  CD1   . TYR B 1 571 ? 129.811 163.913 156.943 1.00 23.79 ?  571 TYR B CD1   1 
ATOM   10144 C  CD2   . TYR B 1 571 ? 130.252 161.603 157.318 1.00 21.32 ?  571 TYR B CD2   1 
ATOM   10145 C  CE1   . TYR B 1 571 ? 130.885 163.982 156.081 1.00 22.28 ?  571 TYR B CE1   1 
ATOM   10146 C  CE2   . TYR B 1 571 ? 131.326 161.663 156.458 1.00 23.34 ?  571 TYR B CE2   1 
ATOM   10147 C  CZ    . TYR B 1 571 ? 131.639 162.855 155.844 1.00 28.65 ?  571 TYR B CZ    1 
ATOM   10148 O  OH    . TYR B 1 571 ? 132.712 162.917 154.986 1.00 30.16 ?  571 TYR B OH    1 
ATOM   10149 N  N     . HIS B 1 572 ? 126.337 160.247 157.581 1.00 25.77 ?  572 HIS B N     1 
ATOM   10150 C  CA    . HIS B 1 572 ? 126.261 158.950 156.923 1.00 11.39 ?  572 HIS B CA    1 
ATOM   10151 C  C     . HIS B 1 572 ? 124.813 158.616 156.606 1.00 16.85 ?  572 HIS B C     1 
ATOM   10152 O  O     . HIS B 1 572 ? 123.952 158.663 157.491 1.00 31.90 ?  572 HIS B O     1 
ATOM   10153 C  CB    . HIS B 1 572 ? 126.871 157.849 157.794 1.00 12.19 ?  572 HIS B CB    1 
ATOM   10154 C  CG    . HIS B 1 572 ? 128.205 158.199 158.372 1.00 9.40  ?  572 HIS B CG    1 
ATOM   10155 N  ND1   . HIS B 1 572 ? 128.350 158.804 159.601 1.00 15.89 ?  572 HIS B ND1   1 
ATOM   10156 C  CD2   . HIS B 1 572 ? 129.458 158.022 157.891 1.00 13.40 ?  572 HIS B CD2   1 
ATOM   10157 C  CE1   . HIS B 1 572 ? 129.633 158.989 159.851 1.00 14.22 ?  572 HIS B CE1   1 
ATOM   10158 N  NE2   . HIS B 1 572 ? 130.326 158.524 158.829 1.00 24.57 ?  572 HIS B NE2   1 
ATOM   10159 N  N     . SER B 1 573 ? 124.548 158.282 155.341 1.00 10.81 ?  573 SER B N     1 
ATOM   10160 C  CA    . SER B 1 573 ? 123.224 157.795 154.973 1.00 8.56  ?  573 SER B CA    1 
ATOM   10161 C  C     . SER B 1 573 ? 122.919 156.482 155.675 1.00 17.12 ?  573 SER B C     1 
ATOM   10162 O  O     . SER B 1 573 ? 121.784 156.241 156.099 1.00 29.36 ?  573 SER B O     1 
ATOM   10163 C  CB    . SER B 1 573 ? 123.128 157.624 153.459 1.00 13.78 ?  573 SER B CB    1 
ATOM   10164 O  OG    . SER B 1 573 ? 124.308 157.041 152.944 1.00 25.31 ?  573 SER B OG    1 
ATOM   10165 N  N     . TYR B 1 574 ? 123.922 155.621 155.800 1.00 14.91 ?  574 TYR B N     1 
ATOM   10166 C  CA    . TYR B 1 574 ? 123.792 154.331 156.451 1.00 0.00  ?  574 TYR B CA    1 
ATOM   10167 C  C     . TYR B 1 574 ? 124.979 154.135 157.377 1.00 10.00 ?  574 TYR B C     1 
ATOM   10168 O  O     . TYR B 1 574 ? 126.105 154.510 157.040 1.00 19.34 ?  574 TYR B O     1 
ATOM   10169 C  CB    . TYR B 1 574 ? 123.716 153.207 155.419 1.00 10.33 ?  574 TYR B CB    1 
ATOM   10170 C  CG    . TYR B 1 574 ? 122.656 153.440 154.369 1.00 0.00  ?  574 TYR B CG    1 
ATOM   10171 C  CD1   . TYR B 1 574 ? 121.357 152.995 154.560 1.00 3.61  ?  574 TYR B CD1   1 
ATOM   10172 C  CD2   . TYR B 1 574 ? 122.950 154.118 153.194 1.00 3.57  ?  574 TYR B CD2   1 
ATOM   10173 C  CE1   . TYR B 1 574 ? 120.385 153.211 153.610 1.00 5.96  ?  574 TYR B CE1   1 
ATOM   10174 C  CE2   . TYR B 1 574 ? 121.982 154.341 152.240 1.00 10.55 ?  574 TYR B CE2   1 
ATOM   10175 C  CZ    . TYR B 1 574 ? 120.702 153.883 152.452 1.00 2.73  ?  574 TYR B CZ    1 
ATOM   10176 O  OH    . TYR B 1 574 ? 119.733 154.096 151.504 1.00 15.62 ?  574 TYR B OH    1 
ATOM   10177 N  N     . ARG B 1 575 ? 124.724 153.557 158.543 1.00 12.14 ?  575 ARG B N     1 
ATOM   10178 C  CA    . ARG B 1 575 ? 125.745 153.437 159.576 1.00 0.00  ?  575 ARG B CA    1 
ATOM   10179 C  C     . ARG B 1 575 ? 125.978 152.016 160.049 1.00 11.16 ?  575 ARG B C     1 
ATOM   10180 O  O     . ARG B 1 575 ? 127.126 151.626 160.265 1.00 23.55 ?  575 ARG B O     1 
ATOM   10181 C  CB    . ARG B 1 575 ? 125.366 154.296 160.783 1.00 13.58 ?  575 ARG B CB    1 
ATOM   10182 C  CG    . ARG B 1 575 ? 125.311 155.773 160.504 1.00 8.83  ?  575 ARG B CG    1 
ATOM   10183 C  CD    . ARG B 1 575 ? 124.492 156.464 161.563 1.00 11.19 ?  575 ARG B CD    1 
ATOM   10184 N  NE    . ARG B 1 575 ? 123.070 156.185 161.407 1.00 16.96 ?  575 ARG B NE    1 
ATOM   10185 C  CZ    . ARG B 1 575 ? 122.379 155.355 162.174 1.00 11.69 ?  575 ARG B CZ    1 
ATOM   10186 N  NH1   . ARG B 1 575 ? 122.951 154.694 163.165 1.00 11.22 1  575 ARG B NH1   1 
ATOM   10187 N  NH2   . ARG B 1 575 ? 121.082 155.187 161.944 1.00 11.31 ?  575 ARG B NH2   1 
ATOM   10188 N  N     . LEU B 1 576 ? 124.922 151.228 160.218 1.00 21.07 ?  576 LEU B N     1 
ATOM   10189 C  CA    . LEU B 1 576 ? 125.003 149.949 160.907 1.00 12.04 ?  576 LEU B CA    1 
ATOM   10190 C  C     . LEU B 1 576 ? 124.562 148.829 159.980 1.00 4.46  ?  576 LEU B C     1 
ATOM   10191 O  O     . LEU B 1 576 ? 123.478 148.894 159.394 1.00 20.33 ?  576 LEU B O     1 
ATOM   10192 C  CB    . LEU B 1 576 ? 124.136 149.959 162.168 1.00 7.86  ?  576 LEU B CB    1 
ATOM   10193 C  CG    . LEU B 1 576 ? 124.317 151.150 163.110 1.00 7.05  ?  576 LEU B CG    1 
ATOM   10194 C  CD1   . LEU B 1 576 ? 123.291 151.108 164.225 1.00 12.34 ?  576 LEU B CD1   1 
ATOM   10195 C  CD2   . LEU B 1 576 ? 125.721 151.170 163.679 1.00 11.05 ?  576 LEU B CD2   1 
ATOM   10196 N  N     . CYS B 1 577 ? 125.408 147.813 159.845 1.00 10.65 ?  577 CYS B N     1 
ATOM   10197 C  CA    . CYS B 1 577 ? 125.045 146.575 159.172 1.00 7.20  ?  577 CYS B CA    1 
ATOM   10198 C  C     . CYS B 1 577 ? 125.852 145.456 159.808 1.00 21.29 ?  577 CYS B C     1 
ATOM   10199 O  O     . CYS B 1 577 ? 127.060 145.599 160.010 1.00 26.91 ?  577 CYS B O     1 
ATOM   10200 C  CB    . CYS B 1 577 ? 125.297 146.651 157.658 1.00 4.23  ?  577 CYS B CB    1 
ATOM   10201 S  SG    . CYS B 1 577 ? 127.008 146.450 157.107 1.00 34.79 ?  577 CYS B SG    1 
ATOM   10202 N  N     . ILE B 1 578 ? 125.184 144.358 160.140 1.00 15.00 ?  578 ILE B N     1 
ATOM   10203 C  CA    . ILE B 1 578 ? 125.805 143.255 160.860 1.00 12.69 ?  578 ILE B CA    1 
ATOM   10204 C  C     . ILE B 1 578 ? 126.215 142.208 159.830 1.00 5.09  ?  578 ILE B C     1 
ATOM   10205 O  O     . ILE B 1 578 ? 125.405 141.382 159.404 1.00 20.00 ?  578 ILE B O     1 
ATOM   10206 C  CB    . ILE B 1 578 ? 124.875 142.682 161.932 1.00 10.95 ?  578 ILE B CB    1 
ATOM   10207 C  CG1   . ILE B 1 578 ? 124.389 143.802 162.853 1.00 2.62  ?  578 ILE B CG1   1 
ATOM   10208 C  CG2   . ILE B 1 578 ? 125.591 141.628 162.747 1.00 8.83  ?  578 ILE B CG2   1 
ATOM   10209 C  CD1   . ILE B 1 578 ? 123.640 143.312 164.062 1.00 9.60  ?  578 ILE B CD1   1 
ATOM   10210 N  N     . ALA B 1 579 ? 127.481 142.255 159.427 1.00 14.77 ?  579 ALA B N     1 
ATOM   10211 C  CA    . ALA B 1 579 ? 128.068 141.307 158.497 1.00 4.76  ?  579 ALA B CA    1 
ATOM   10212 C  C     . ALA B 1 579 ? 128.368 139.982 159.195 1.00 18.65 ?  579 ALA B C     1 
ATOM   10213 O  O     . ALA B 1 579 ? 128.396 139.912 160.424 1.00 31.68 ?  579 ALA B O     1 
ATOM   10214 C  CB    . ALA B 1 579 ? 129.341 141.895 157.899 1.00 9.76  ?  579 ALA B CB    1 
ATOM   10215 N  N     . PRO B 1 580 ? 128.571 138.903 158.430 1.00 25.93 ?  580 PRO B N     1 
ATOM   10216 C  CA    . PRO B 1 580 ? 128.862 137.604 159.066 1.00 23.57 ?  580 PRO B CA    1 
ATOM   10217 C  C     . PRO B 1 580 ? 130.122 137.587 159.922 1.00 31.60 ?  580 PRO B C     1 
ATOM   10218 O  O     . PRO B 1 580 ? 130.159 136.844 160.911 1.00 37.76 ?  580 PRO B O     1 
ATOM   10219 C  CB    . PRO B 1 580 ? 128.978 136.643 157.872 1.00 23.45 ?  580 PRO B CB    1 
ATOM   10220 C  CG    . PRO B 1 580 ? 129.073 137.503 156.661 1.00 23.60 ?  580 PRO B CG    1 
ATOM   10221 C  CD    . PRO B 1 580 ? 128.351 138.761 156.982 1.00 20.84 ?  580 PRO B CD    1 
ATOM   10222 N  N     . THR B 1 581 ? 131.145 138.372 159.581 1.00 24.16 ?  581 THR B N     1 
ATOM   10223 C  CA    . THR B 1 581 ? 132.411 138.418 160.325 1.00 33.88 ?  581 THR B CA    1 
ATOM   10224 C  C     . THR B 1 581 ? 133.020 137.020 160.459 1.00 32.21 ?  581 THR B C     1 
ATOM   10225 O  O     . THR B 1 581 ? 133.159 136.465 161.548 1.00 34.51 ?  581 THR B O     1 
ATOM   10226 C  CB    . THR B 1 581 ? 132.242 139.060 161.707 1.00 28.70 ?  581 THR B CB    1 
ATOM   10227 O  OG1   . THR B 1 581 ? 131.776 138.079 162.640 1.00 24.16 ?  581 THR B OG1   1 
ATOM   10228 C  CG2   . THR B 1 581 ? 131.271 140.222 161.655 1.00 31.20 ?  581 THR B CG2   1 
ATOM   10229 N  N     . GLY B 1 582 ? 133.378 136.465 159.304 1.00 31.94 ?  582 GLY B N     1 
ATOM   10230 C  CA    . GLY B 1 582 ? 133.809 135.085 159.231 1.00 34.72 ?  582 GLY B CA    1 
ATOM   10231 C  C     . GLY B 1 582 ? 135.109 134.757 159.937 1.00 37.48 ?  582 GLY B C     1 
ATOM   10232 O  O     . GLY B 1 582 ? 135.107 134.015 160.924 1.00 41.71 ?  582 GLY B O     1 
ATOM   10233 N  N     . SER B 1 583 ? 136.227 135.299 159.453 1.00 37.76 ?  583 SER B N     1 
ATOM   10234 C  CA    . SER B 1 583 ? 137.536 134.891 159.948 1.00 42.54 ?  583 SER B CA    1 
ATOM   10235 C  C     . SER B 1 583 ? 138.071 135.788 161.055 1.00 39.80 ?  583 SER B C     1 
ATOM   10236 O  O     . SER B 1 583 ? 138.895 135.335 161.858 1.00 39.77 ?  583 SER B O     1 
ATOM   10237 C  CB    . SER B 1 583 ? 138.545 134.850 158.798 1.00 47.40 ?  583 SER B CB    1 
ATOM   10238 O  OG    . SER B 1 583 ? 138.394 133.667 158.031 1.00 49.21 ?  583 SER B OG    1 
ATOM   10239 N  N     . ILE B 1 584 ? 137.634 137.047 161.120 1.00 33.05 ?  584 ILE B N     1 
ATOM   10240 C  CA    . ILE B 1 584 ? 138.073 137.937 162.188 1.00 28.91 ?  584 ILE B CA    1 
ATOM   10241 C  C     . ILE B 1 584 ? 137.508 137.552 163.545 1.00 31.88 ?  584 ILE B C     1 
ATOM   10242 O  O     . ILE B 1 584 ? 137.980 138.057 164.567 1.00 36.84 ?  584 ILE B O     1 
ATOM   10243 C  CB    . ILE B 1 584 ? 137.697 139.401 161.879 1.00 36.81 ?  584 ILE B CB    1 
ATOM   10244 C  CG1   . ILE B 1 584 ? 136.206 139.514 161.550 1.00 34.43 ?  584 ILE B CG1   1 
ATOM   10245 C  CG2   . ILE B 1 584 ? 138.559 139.952 160.757 1.00 32.57 ?  584 ILE B CG2   1 
ATOM   10246 C  CD1   . ILE B 1 584 ? 135.705 140.938 161.461 1.00 33.31 ?  584 ILE B CD1   1 
ATOM   10247 N  N     . SER B 1 585 ? 136.501 136.675 163.581 1.00 31.76 ?  585 SER B N     1 
ATOM   10248 C  CA    . SER B 1 585 ? 135.942 136.247 164.857 1.00 29.12 ?  585 SER B CA    1 
ATOM   10249 C  C     . SER B 1 585 ? 136.921 135.380 165.636 1.00 28.92 ?  585 SER B C     1 
ATOM   10250 O  O     . SER B 1 585 ? 136.963 135.453 166.868 1.00 29.13 ?  585 SER B O     1 
ATOM   10251 C  CB    . SER B 1 585 ? 134.629 135.500 164.631 1.00 32.20 ?  585 SER B CB    1 
ATOM   10252 O  OG    . SER B 1 585 ? 134.811 134.398 163.761 1.00 36.22 ?  585 SER B OG    1 
ATOM   10253 N  N     . TYR B 1 586 ? 137.706 134.551 164.943 1.00 35.47 ?  586 TYR B N     1 
ATOM   10254 C  CA    . TYR B 1 586 ? 138.714 133.748 165.626 1.00 36.44 ?  586 TYR B CA    1 
ATOM   10255 C  C     . TYR B 1 586 ? 139.774 134.630 166.268 1.00 34.72 ?  586 TYR B C     1 
ATOM   10256 O  O     . TYR B 1 586 ? 140.157 134.413 167.423 1.00 41.06 ?  586 TYR B O     1 
ATOM   10257 C  CB    . TYR B 1 586 ? 139.368 132.772 164.650 1.00 32.67 ?  586 TYR B CB    1 
ATOM   10258 C  CG    . TYR B 1 586 ? 138.419 131.790 164.009 1.00 33.53 ?  586 TYR B CG    1 
ATOM   10259 C  CD1   . TYR B 1 586 ? 137.840 132.058 162.778 1.00 36.90 ?  586 TYR B CD1   1 
ATOM   10260 C  CD2   . TYR B 1 586 ? 138.107 130.591 164.631 1.00 35.45 ?  586 TYR B CD2   1 
ATOM   10261 C  CE1   . TYR B 1 586 ? 136.976 131.162 162.185 1.00 39.70 ?  586 TYR B CE1   1 
ATOM   10262 C  CE2   . TYR B 1 586 ? 137.244 129.688 164.047 1.00 37.85 ?  586 TYR B CE2   1 
ATOM   10263 C  CZ    . TYR B 1 586 ? 136.679 129.979 162.824 1.00 39.59 ?  586 TYR B CZ    1 
ATOM   10264 O  OH    . TYR B 1 586 ? 135.818 129.082 162.238 1.00 44.24 ?  586 TYR B OH    1 
ATOM   10265 N  N     . VAL B 1 587 ? 140.254 135.635 165.533 1.00 29.79 ?  587 VAL B N     1 
ATOM   10266 C  CA    . VAL B 1 587 ? 141.297 136.519 166.047 1.00 24.81 ?  587 VAL B CA    1 
ATOM   10267 C  C     . VAL B 1 587 ? 140.805 137.263 167.280 1.00 30.49 ?  587 VAL B C     1 
ATOM   10268 O  O     . VAL B 1 587 ? 141.556 137.473 168.240 1.00 39.87 ?  587 VAL B O     1 
ATOM   10269 C  CB    . VAL B 1 587 ? 141.754 137.491 164.944 1.00 31.15 ?  587 VAL B CB    1 
ATOM   10270 C  CG1   . VAL B 1 587 ? 142.785 138.465 165.483 1.00 34.30 ?  587 VAL B CG1   1 
ATOM   10271 C  CG2   . VAL B 1 587 ? 142.309 136.721 163.759 1.00 31.54 ?  587 VAL B CG2   1 
ATOM   10272 N  N     . GLN B 1 588 ? 139.538 137.663 167.280 1.00 34.77 ?  588 GLN B N     1 
ATOM   10273 C  CA    . GLN B 1 588 ? 138.958 138.396 168.395 1.00 29.40 ?  588 GLN B CA    1 
ATOM   10274 C  C     . GLN B 1 588 ? 138.473 137.489 169.514 1.00 34.28 ?  588 GLN B C     1 
ATOM   10275 O  O     . GLN B 1 588 ? 137.990 138.001 170.530 1.00 36.74 ?  588 GLN B O     1 
ATOM   10276 C  CB    . GLN B 1 588 ? 137.799 139.264 167.902 1.00 22.63 ?  588 GLN B CB    1 
ATOM   10277 C  CG    . GLN B 1 588 ? 138.236 140.494 167.136 1.00 24.46 ?  588 GLN B CG    1 
ATOM   10278 C  CD    . GLN B 1 588 ? 138.348 141.714 168.022 1.00 29.18 ?  588 GLN B CD    1 
ATOM   10279 O  OE1   . GLN B 1 588 ? 137.514 141.935 168.899 1.00 29.62 ?  588 GLN B OE1   1 
ATOM   10280 N  NE2   . GLN B 1 588 ? 139.380 142.515 167.800 1.00 33.47 ?  588 GLN B NE2   1 
ATOM   10281 N  N     . SER B 1 589 ? 138.597 136.172 169.357 1.00 34.31 ?  589 SER B N     1 
ATOM   10282 C  CA    . SER B 1 589 ? 138.061 135.200 170.308 1.00 28.15 ?  589 SER B CA    1 
ATOM   10283 C  C     . SER B 1 589 ? 136.587 135.489 170.577 1.00 31.62 ?  589 SER B C     1 
ATOM   10284 O  O     . SER B 1 589 ? 136.158 135.732 171.705 1.00 35.30 ?  589 SER B O     1 
ATOM   10285 C  CB    . SER B 1 589 ? 138.875 135.190 171.603 1.00 36.32 ?  589 SER B CB    1 
ATOM   10286 O  OG    . SER B 1 589 ? 138.717 133.966 172.297 1.00 45.26 ?  589 SER B OG    1 
ATOM   10287 N  N     . SER B 1 590 ? 135.812 135.474 169.497 1.00 30.54 ?  590 SER B N     1 
ATOM   10288 C  CA    . SER B 1 590 ? 134.421 135.888 169.536 1.00 23.07 ?  590 SER B CA    1 
ATOM   10289 C  C     . SER B 1 590 ? 133.580 134.945 168.693 1.00 28.21 ?  590 SER B C     1 
ATOM   10290 O  O     . SER B 1 590 ? 134.076 134.318 167.753 1.00 36.37 ?  590 SER B O     1 
ATOM   10291 C  CB    . SER B 1 590 ? 134.258 137.326 169.028 1.00 26.65 ?  590 SER B CB    1 
ATOM   10292 O  OG    . SER B 1 590 ? 134.081 137.352 167.626 1.00 36.42 ?  590 SER B OG    1 
ATOM   10293 N  N     . THR B 1 591 ? 132.303 134.841 169.045 1.00 30.26 ?  591 THR B N     1 
ATOM   10294 C  CA    . THR B 1 591 ? 131.352 134.119 168.213 1.00 27.61 ?  591 THR B CA    1 
ATOM   10295 C  C     . THR B 1 591 ? 130.975 134.976 167.012 1.00 30.48 ?  591 THR B C     1 
ATOM   10296 O  O     . THR B 1 591 ? 130.904 136.205 167.105 1.00 25.23 ?  591 THR B O     1 
ATOM   10297 C  CB    . THR B 1 591 ? 130.107 133.740 169.013 1.00 28.23 ?  591 THR B CB    1 
ATOM   10298 O  OG1   . THR B 1 591 ? 129.351 134.916 169.321 1.00 36.89 ?  591 THR B OG1   1 
ATOM   10299 C  CG2   . THR B 1 591 ? 130.505 133.049 170.306 1.00 26.83 ?  591 THR B CG2   1 
ATOM   10300 N  N     . ALA B 1 592 ? 130.744 134.321 165.878 1.00 26.62 ?  592 ALA B N     1 
ATOM   10301 C  CA    . ALA B 1 592 ? 130.567 135.038 164.623 1.00 25.14 ?  592 ALA B CA    1 
ATOM   10302 C  C     . ALA B 1 592 ? 129.270 135.834 164.626 1.00 24.71 ?  592 ALA B C     1 
ATOM   10303 O  O     . ALA B 1 592 ? 128.182 135.269 164.778 1.00 32.62 ?  592 ALA B O     1 
ATOM   10304 C  CB    . ALA B 1 592 ? 130.581 134.059 163.451 1.00 31.49 ?  592 ALA B CB    1 
ATOM   10305 N  N     . SER B 1 593 ? 129.394 137.146 164.457 1.00 27.77 ?  593 SER B N     1 
ATOM   10306 C  CA    . SER B 1 593 ? 128.261 138.058 164.253 1.00 16.57 ?  593 SER B CA    1 
ATOM   10307 C  C     . SER B 1 593 ? 127.309 137.952 165.445 1.00 14.42 ?  593 SER B C     1 
ATOM   10308 O  O     . SER B 1 593 ? 127.727 137.647 166.569 1.00 29.93 ?  593 SER B O     1 
ATOM   10309 C  CB    . SER B 1 593 ? 127.626 137.763 162.908 1.00 28.74 ?  593 SER B CB    1 
ATOM   10310 O  OG    . SER B 1 593 ? 126.537 138.626 162.655 1.00 24.93 ?  593 SER B OG    1 
ATOM   10311 N  N     . VAL B 1 594 ? 126.021 138.204 165.211 1.00 20.91 ?  594 VAL B N     1 
ATOM   10312 C  CA    . VAL B 1 594 ? 124.996 138.029 166.229 1.00 17.98 ?  594 VAL B CA    1 
ATOM   10313 C  C     . VAL B 1 594 ? 124.354 136.650 166.146 1.00 15.70 ?  594 VAL B C     1 
ATOM   10314 O  O     . VAL B 1 594 ? 123.409 136.363 166.884 1.00 25.92 ?  594 VAL B O     1 
ATOM   10315 C  CB    . VAL B 1 594 ? 123.932 139.134 166.140 1.00 23.80 ?  594 VAL B CB    1 
ATOM   10316 C  CG1   . VAL B 1 594 ? 124.511 140.462 166.597 1.00 14.10 ?  594 VAL B CG1   1 
ATOM   10317 C  CG2   . VAL B 1 594 ? 123.393 139.240 164.726 1.00 22.03 ?  594 VAL B CG2   1 
ATOM   10318 N  N     . MET B 1 595 ? 124.849 135.790 165.261 1.00 25.63 ?  595 MET B N     1 
ATOM   10319 C  CA    . MET B 1 595 ? 124.307 134.451 165.124 1.00 19.42 ?  595 MET B CA    1 
ATOM   10320 C  C     . MET B 1 595 ? 124.699 133.589 166.322 1.00 24.87 ?  595 MET B C     1 
ATOM   10321 O  O     . MET B 1 595 ? 125.738 133.814 166.948 1.00 32.63 ?  595 MET B O     1 
ATOM   10322 C  CB    . MET B 1 595 ? 124.817 133.799 163.841 1.00 22.58 ?  595 MET B CB    1 
ATOM   10323 C  CG    . MET B 1 595 ? 124.396 134.464 162.533 1.00 24.99 ?  595 MET B CG    1 
ATOM   10324 S  SD    . MET B 1 595 ? 122.710 134.137 161.968 1.00 37.28 ?  595 MET B SD    1 
ATOM   10325 C  CE    . MET B 1 595 ? 121.736 135.218 163.008 1.00 16.63 ?  595 MET B CE    1 
ATOM   10326 N  N     . PRO B 1 596 ? 123.883 132.595 166.661 1.00 32.04 ?  596 PRO B N     1 
ATOM   10327 C  CA    . PRO B 1 596 ? 124.303 131.612 167.663 1.00 20.66 ?  596 PRO B CA    1 
ATOM   10328 C  C     . PRO B 1 596 ? 125.333 130.654 167.085 1.00 31.12 ?  596 PRO B C     1 
ATOM   10329 O  O     . PRO B 1 596 ? 125.479 130.507 165.869 1.00 37.74 ?  596 PRO B O     1 
ATOM   10330 C  CB    . PRO B 1 596 ? 123.002 130.892 168.020 1.00 22.35 ?  596 PRO B CB    1 
ATOM   10331 C  CG    . PRO B 1 596 ? 122.167 131.013 166.798 1.00 27.79 ?  596 PRO B CG    1 
ATOM   10332 C  CD    . PRO B 1 596 ? 122.522 132.331 166.162 1.00 32.26 ?  596 PRO B CD    1 
ATOM   10333 N  N     . ILE B 1 597 ? 126.062 129.997 167.988 1.00 28.45 ?  597 ILE B N     1 
ATOM   10334 C  CA    . ILE B 1 597 ? 127.166 129.141 167.574 1.00 28.60 ?  597 ILE B CA    1 
ATOM   10335 C  C     . ILE B 1 597 ? 126.630 127.886 166.898 1.00 37.55 ?  597 ILE B C     1 
ATOM   10336 O  O     . ILE B 1 597 ? 125.620 127.309 167.319 1.00 40.72 ?  597 ILE B O     1 
ATOM   10337 C  CB    . ILE B 1 597 ? 128.057 128.791 168.778 1.00 33.65 ?  597 ILE B CB    1 
ATOM   10338 C  CG1   . ILE B 1 597 ? 127.251 128.063 169.854 1.00 34.53 ?  597 ILE B CG1   1 
ATOM   10339 C  CG2   . ILE B 1 597 ? 128.684 130.046 169.348 1.00 31.62 ?  597 ILE B CG2   1 
ATOM   10340 C  CD1   . ILE B 1 597 ? 128.073 127.130 170.700 1.00 33.96 ?  597 ILE B CD1   1 
ATOM   10341 N  N     . MET B 1 598 ? 127.303 127.469 165.825 1.00 44.87 ?  598 MET B N     1 
ATOM   10342 C  CA    . MET B 1 598 ? 126.925 126.236 165.146 1.00 41.70 ?  598 MET B CA    1 
ATOM   10343 C  C     . MET B 1 598 ? 127.332 125.016 165.963 1.00 38.38 ?  598 MET B C     1 
ATOM   10344 O  O     . MET B 1 598 ? 126.548 124.074 166.126 1.00 46.97 ?  598 MET B O     1 
ATOM   10345 C  CB    . MET B 1 598 ? 127.561 126.189 163.758 1.00 40.80 ?  598 MET B CB    1 
ATOM   10346 C  CG    . MET B 1 598 ? 127.196 127.360 162.870 1.00 39.04 ?  598 MET B CG    1 
ATOM   10347 S  SD    . MET B 1 598 ? 127.511 127.027 161.129 1.00 59.89 ?  598 MET B SD    1 
ATOM   10348 C  CE    . MET B 1 598 ? 128.932 128.077 160.843 1.00 42.97 ?  598 MET B CE    1 
ATOM   10349 N  N     . GLU B 1 599 ? 128.557 125.017 166.484 1.00 42.37 ?  599 GLU B N     1 
ATOM   10350 C  CA    . GLU B 1 599 ? 129.084 123.918 167.277 1.00 42.26 ?  599 GLU B CA    1 
ATOM   10351 C  C     . GLU B 1 599 ? 129.699 124.467 168.553 1.00 40.25 ?  599 GLU B C     1 
ATOM   10352 O  O     . GLU B 1 599 ? 130.210 125.589 168.580 1.00 46.11 ?  599 GLU B O     1 
ATOM   10353 C  CB    . GLU B 1 599 ? 130.142 123.116 166.505 1.00 44.07 ?  599 GLU B CB    1 
ATOM   10354 C  CG    . GLU B 1 599 ? 130.023 123.206 164.994 1.00 43.73 ?  599 GLU B CG    1 
ATOM   10355 C  CD    . GLU B 1 599 ? 131.184 122.547 164.279 1.00 50.12 ?  599 GLU B CD    1 
ATOM   10356 O  OE1   . GLU B 1 599 ? 131.614 121.460 164.715 1.00 49.97 ?  599 GLU B OE1   1 
ATOM   10357 O  OE2   . GLU B 1 599 ? 131.667 123.118 163.279 1.00 48.55 -1 599 GLU B OE2   1 
ATOM   10358 N  N     . ARG B 1 600 ? 129.642 123.669 169.619 1.00 43.29 ?  600 ARG B N     1 
ATOM   10359 C  CA    . ARG B 1 600 ? 130.277 124.073 170.870 1.00 35.78 ?  600 ARG B CA    1 
ATOM   10360 C  C     . ARG B 1 600 ? 131.793 124.044 170.746 1.00 37.20 ?  600 ARG B C     1 
ATOM   10361 O  O     . ARG B 1 600 ? 132.481 124.975 171.180 1.00 41.36 ?  600 ARG B O     1 
ATOM   10362 C  CB    . ARG B 1 600 ? 129.810 123.176 172.013 1.00 38.87 ?  600 ARG B CB    1 
ATOM   10363 C  CG    . ARG B 1 600 ? 128.496 123.610 172.618 1.00 39.64 ?  600 ARG B CG    1 
ATOM   10364 C  CD    . ARG B 1 600 ? 128.232 122.893 173.920 1.00 36.65 ?  600 ARG B CD    1 
ATOM   10365 N  NE    . ARG B 1 600 ? 126.923 123.217 174.471 1.00 36.86 ?  600 ARG B NE    1 
ATOM   10366 C  CZ    . ARG B 1 600 ? 125.791 122.634 174.102 1.00 40.58 ?  600 ARG B CZ    1 
ATOM   10367 N  NH1   . ARG B 1 600 ? 125.770 121.697 173.169 1.00 39.73 1  600 ARG B NH1   1 
ATOM   10368 N  NH2   . ARG B 1 600 ? 124.653 123.000 174.683 1.00 41.50 ?  600 ARG B NH2   1 
ATOM   10369 N  N     . ILE B 1 601 ? 132.333 122.982 170.158 1.00 49.15 ?  601 ILE B N     1 
ATOM   10370 C  CA    . ILE B 1 601 ? 133.759 122.860 169.892 1.00 43.12 ?  601 ILE B CA    1 
ATOM   10371 C  C     . ILE B 1 601 ? 133.939 122.630 168.401 1.00 43.56 ?  601 ILE B C     1 
ATOM   10372 O  O     . ILE B 1 601 ? 133.330 121.719 167.830 1.00 46.37 ?  601 ILE B O     1 
ATOM   10373 C  CB    . ILE B 1 601 ? 134.399 121.725 170.711 1.00 40.56 ?  601 ILE B CB    1 
ATOM   10374 C  CG1   . ILE B 1 601 ? 134.126 121.938 172.200 1.00 42.38 ?  601 ILE B CG1   1 
ATOM   10375 C  CG2   . ILE B 1 601 ? 135.889 121.668 170.444 1.00 41.67 ?  601 ILE B CG2   1 
ATOM   10376 C  CD1   . ILE B 1 601 ? 134.302 120.705 173.042 1.00 44.89 ?  601 ILE B CD1   1 
ATOM   10377 N  N     . GLU B 1 602 ? 134.770 123.454 167.777 1.00 53.69 ?  602 GLU B N     1 
ATOM   10378 C  CA    . GLU B 1 602 ? 134.917 123.482 166.330 1.00 50.17 ?  602 GLU B CA    1 
ATOM   10379 C  C     . GLU B 1 602 ? 136.061 122.562 165.920 1.00 53.61 ?  602 GLU B C     1 
ATOM   10380 O  O     . GLU B 1 602 ? 137.210 122.782 166.314 1.00 57.39 ?  602 GLU B O     1 
ATOM   10381 C  CB    . GLU B 1 602 ? 135.170 124.912 165.856 1.00 50.44 ?  602 GLU B CB    1 
ATOM   10382 C  CG    . GLU B 1 602 ? 134.816 125.174 164.415 1.00 50.20 ?  602 GLU B CG    1 
ATOM   10383 C  CD    . GLU B 1 602 ? 134.834 126.650 164.080 1.00 56.99 ?  602 GLU B CD    1 
ATOM   10384 O  OE1   . GLU B 1 602 ? 134.034 127.404 164.671 1.00 55.91 ?  602 GLU B OE1   1 
ATOM   10385 O  OE2   . GLU B 1 602 ? 135.651 127.055 163.228 1.00 58.72 -1 602 GLU B OE2   1 
ATOM   10386 N  N     . GLU B 1 603 ? 135.744 121.538 165.133 1.00 56.22 ?  603 GLU B N     1 
ATOM   10387 C  CA    . GLU B 1 603 ? 136.733 120.590 164.634 1.00 55.13 ?  603 GLU B CA    1 
ATOM   10388 C  C     . GLU B 1 603 ? 137.074 120.944 163.191 1.00 57.66 ?  603 GLU B C     1 
ATOM   10389 O  O     . GLU B 1 603 ? 136.211 120.867 162.309 1.00 59.08 ?  603 GLU B O     1 
ATOM   10390 C  CB    . GLU B 1 603 ? 136.212 119.154 164.720 1.00 58.25 ?  603 GLU B CB    1 
ATOM   10391 C  CG    . GLU B 1 603 ? 135.686 118.753 166.088 1.00 60.56 ?  603 GLU B CG    1 
ATOM   10392 C  CD    . GLU B 1 603 ? 134.184 118.919 166.211 1.00 60.85 ?  603 GLU B CD    1 
ATOM   10393 O  OE1   . GLU B 1 603 ? 133.511 119.063 165.168 1.00 54.69 ?  603 GLU B OE1   1 
ATOM   10394 O  OE2   . GLU B 1 603 ? 133.675 118.902 167.351 1.00 59.56 -1 603 GLU B OE2   1 
ATOM   10395 N  N     . ARG B 1 604 ? 138.326 121.327 162.956 1.00 60.93 ?  604 ARG B N     1 
ATOM   10396 C  CA    . ARG B 1 604 ? 138.799 121.705 161.634 1.00 61.64 ?  604 ARG B CA    1 
ATOM   10397 C  C     . ARG B 1 604 ? 140.161 121.085 161.366 1.00 62.36 ?  604 ARG B C     1 
ATOM   10398 O  O     . ARG B 1 604 ? 140.924 120.796 162.291 1.00 61.58 ?  604 ARG B O     1 
ATOM   10399 C  CB    . ARG B 1 604 ? 138.878 123.230 161.479 1.00 61.50 ?  604 ARG B CB    1 
ATOM   10400 C  CG    . ARG B 1 604 ? 137.541 123.933 161.609 1.00 61.72 ?  604 ARG B CG    1 
ATOM   10401 C  CD    . ARG B 1 604 ? 136.843 123.982 160.255 1.00 61.06 ?  604 ARG B CD    1 
ATOM   10402 N  NE    . ARG B 1 604 ? 135.805 125.004 160.194 1.00 64.58 ?  604 ARG B NE    1 
ATOM   10403 C  CZ    . ARG B 1 604 ? 134.655 124.950 160.851 1.00 62.16 ?  604 ARG B CZ    1 
ATOM   10404 N  NH1   . ARG B 1 604 ? 134.311 123.887 161.558 1.00 59.27 1  604 ARG B NH1   1 
ATOM   10405 N  NH2   . ARG B 1 604 ? 133.818 125.981 160.778 1.00 60.26 ?  604 ARG B NH2   1 
ATOM   10406 N  N     . THR B 1 605 ? 140.454 120.884 160.085 1.00 68.88 ?  605 THR B N     1 
ATOM   10407 C  CA    . THR B 1 605 ? 141.714 120.307 159.638 1.00 69.05 ?  605 THR B CA    1 
ATOM   10408 C  C     . THR B 1 605 ? 142.481 121.355 158.844 1.00 68.94 ?  605 THR B C     1 
ATOM   10409 O  O     . THR B 1 605 ? 141.967 121.887 157.853 1.00 68.34 ?  605 THR B O     1 
ATOM   10410 C  CB    . THR B 1 605 ? 141.476 119.061 158.786 1.00 68.77 ?  605 THR B CB    1 
ATOM   10411 O  OG1   . THR B 1 605 ? 140.831 118.054 159.575 1.00 68.65 ?  605 THR B OG1   1 
ATOM   10412 C  CG2   . THR B 1 605 ? 142.794 118.519 158.259 1.00 69.06 ?  605 THR B CG2   1 
ATOM   10413 N  N     . TYR B 1 606 ? 143.703 121.647 159.278 1.00 70.93 ?  606 TYR B N     1 
ATOM   10414 C  CA    . TYR B 1 606 ? 144.591 122.568 158.579 1.00 72.42 ?  606 TYR B CA    1 
ATOM   10415 C  C     . TYR B 1 606 ? 145.841 121.802 158.176 1.00 73.83 ?  606 TYR B C     1 
ATOM   10416 O  O     . TYR B 1 606 ? 146.521 121.225 159.032 1.00 71.71 ?  606 TYR B O     1 
ATOM   10417 C  CB    . TYR B 1 606 ? 144.937 123.771 159.458 1.00 70.45 ?  606 TYR B CB    1 
ATOM   10418 C  CG    . TYR B 1 606 ? 143.739 124.631 159.783 1.00 71.00 ?  606 TYR B CG    1 
ATOM   10419 C  CD1   . TYR B 1 606 ? 143.257 125.557 158.869 1.00 68.19 ?  606 TYR B CD1   1 
ATOM   10420 C  CD2   . TYR B 1 606 ? 143.082 124.506 160.999 1.00 71.01 ?  606 TYR B CD2   1 
ATOM   10421 C  CE1   . TYR B 1 606 ? 142.158 126.341 159.160 1.00 69.99 ?  606 TYR B CE1   1 
ATOM   10422 C  CE2   . TYR B 1 606 ? 141.984 125.284 161.299 1.00 68.85 ?  606 TYR B CE2   1 
ATOM   10423 C  CZ    . TYR B 1 606 ? 141.526 126.200 160.376 1.00 72.54 ?  606 TYR B CZ    1 
ATOM   10424 O  OH    . TYR B 1 606 ? 140.430 126.977 160.672 1.00 74.18 ?  606 TYR B OH    1 
ATOM   10425 N  N     . GLY B 1 607 ? 146.145 121.806 156.883 1.00 79.93 ?  607 GLY B N     1 
ATOM   10426 C  CA    . GLY B 1 607 ? 147.200 120.939 156.389 1.00 79.31 ?  607 GLY B CA    1 
ATOM   10427 C  C     . GLY B 1 607 ? 146.812 119.488 156.593 1.00 79.82 ?  607 GLY B C     1 
ATOM   10428 O  O     . GLY B 1 607 ? 145.703 119.063 156.252 1.00 79.29 ?  607 GLY B O     1 
ATOM   10429 N  N     . ASN B 1 608 ? 147.733 118.710 157.158 1.00 81.39 ?  608 ASN B N     1 
ATOM   10430 C  CA    . ASN B 1 608 ? 147.482 117.309 157.468 1.00 82.54 ?  608 ASN B CA    1 
ATOM   10431 C  C     . ASN B 1 608 ? 147.136 117.092 158.936 1.00 83.77 ?  608 ASN B C     1 
ATOM   10432 O  O     . ASN B 1 608 ? 146.936 115.947 159.353 1.00 83.08 ?  608 ASN B O     1 
ATOM   10433 C  CB    . ASN B 1 608 ? 148.692 116.458 157.079 1.00 83.72 ?  608 ASN B CB    1 
ATOM   10434 C  CG    . ASN B 1 608 ? 148.980 116.501 155.590 1.00 84.36 ?  608 ASN B CG    1 
ATOM   10435 O  OD1   . ASN B 1 608 ? 148.169 116.990 154.803 1.00 82.31 ?  608 ASN B OD1   1 
ATOM   10436 N  ND2   . ASN B 1 608 ? 150.138 115.985 155.195 1.00 83.01 ?  608 ASN B ND2   1 
ATOM   10437 N  N     . SER B 1 609 ? 147.054 118.160 159.724 1.00 76.85 ?  609 SER B N     1 
ATOM   10438 C  CA    . SER B 1 609 ? 146.778 118.070 161.150 1.00 76.36 ?  609 SER B CA    1 
ATOM   10439 C  C     . SER B 1 609 ? 145.411 118.666 161.458 1.00 74.44 ?  609 SER B C     1 
ATOM   10440 O  O     . SER B 1 609 ? 145.058 119.735 160.950 1.00 74.33 ?  609 SER B O     1 
ATOM   10441 C  CB    . SER B 1 609 ? 147.858 118.790 161.963 1.00 73.85 ?  609 SER B CB    1 
ATOM   10442 O  OG    . SER B 1 609 ? 147.875 120.177 161.672 1.00 73.50 ?  609 SER B OG    1 
ATOM   10443 N  N     . LYS B 1 610 ? 144.647 117.967 162.291 1.00 64.40 ?  610 LYS B N     1 
ATOM   10444 C  CA    . LYS B 1 610 ? 143.320 118.411 162.690 1.00 63.80 ?  610 LYS B CA    1 
ATOM   10445 C  C     . LYS B 1 610 ? 143.398 119.258 163.955 1.00 63.31 ?  610 LYS B C     1 
ATOM   10446 O  O     . LYS B 1 610 ? 144.199 118.988 164.855 1.00 64.06 ?  610 LYS B O     1 
ATOM   10447 C  CB    . LYS B 1 610 ? 142.396 117.204 162.884 1.00 64.70 ?  610 LYS B CB    1 
ATOM   10448 C  CG    . LYS B 1 610 ? 142.333 116.635 164.291 1.00 63.25 ?  610 LYS B CG    1 
ATOM   10449 C  CD    . LYS B 1 610 ? 141.774 115.220 164.266 1.00 64.78 ?  610 LYS B CD    1 
ATOM   10450 C  CE    . LYS B 1 610 ? 142.426 114.336 165.318 1.00 64.56 ?  610 LYS B CE    1 
ATOM   10451 N  NZ    . LYS B 1 610 ? 141.982 114.658 166.699 1.00 64.14 1  610 LYS B NZ    1 
ATOM   10452 N  N     . THR B 1 611 ? 142.581 120.307 164.000 1.00 63.68 ?  611 THR B N     1 
ATOM   10453 C  CA    . THR B 1 611 ? 142.593 121.275 165.085 1.00 61.02 ?  611 THR B CA    1 
ATOM   10454 C  C     . THR B 1 611 ? 141.222 121.340 165.742 1.00 56.76 ?  611 THR B C     1 
ATOM   10455 O  O     . THR B 1 611 ? 140.199 121.059 165.112 1.00 60.25 ?  611 THR B O     1 
ATOM   10456 C  CB    . THR B 1 611 ? 142.993 122.669 164.586 1.00 61.00 ?  611 THR B CB    1 
ATOM   10457 O  OG1   . THR B 1 611 ? 143.955 122.545 163.531 1.00 61.18 ?  611 THR B OG1   1 
ATOM   10458 C  CG2   . THR B 1 611 ? 143.604 123.472 165.712 1.00 60.84 ?  611 THR B CG2   1 
ATOM   10459 N  N     . TYR B 1 612 ? 141.211 121.715 167.019 1.00 51.00 ?  612 TYR B N     1 
ATOM   10460 C  CA    . TYR B 1 612 ? 139.991 121.818 167.806 1.00 52.40 ?  612 TYR B CA    1 
ATOM   10461 C  C     . TYR B 1 612 ? 139.868 123.230 168.355 1.00 54.60 ?  612 TYR B C     1 
ATOM   10462 O  O     . TYR B 1 612 ? 140.818 123.757 168.942 1.00 53.52 ?  612 TYR B O     1 
ATOM   10463 C  CB    . TYR B 1 612 ? 139.997 120.799 168.944 1.00 54.04 ?  612 TYR B CB    1 
ATOM   10464 C  CG    . TYR B 1 612 ? 139.947 119.376 168.452 1.00 57.49 ?  612 TYR B CG    1 
ATOM   10465 C  CD1   . TYR B 1 612 ? 138.859 118.910 167.730 1.00 55.55 ?  612 TYR B CD1   1 
ATOM   10466 C  CD2   . TYR B 1 612 ? 141.004 118.507 168.680 1.00 56.40 ?  612 TYR B CD2   1 
ATOM   10467 C  CE1   . TYR B 1 612 ? 138.813 117.611 167.268 1.00 54.86 ?  612 TYR B CE1   1 
ATOM   10468 C  CE2   . TYR B 1 612 ? 140.969 117.210 168.219 1.00 59.31 ?  612 TYR B CE2   1 
ATOM   10469 C  CZ    . TYR B 1 612 ? 139.871 116.765 167.516 1.00 59.22 ?  612 TYR B CZ    1 
ATOM   10470 O  OH    . TYR B 1 612 ? 139.831 115.470 167.056 1.00 60.84 ?  612 TYR B OH    1 
ATOM   10471 N  N     . TYR B 1 613 ? 138.700 123.838 168.164 1.00 51.35 ?  613 TYR B N     1 
ATOM   10472 C  CA    . TYR B 1 613 ? 138.446 125.207 168.609 1.00 45.38 ?  613 TYR B CA    1 
ATOM   10473 C  C     . TYR B 1 613 ? 137.182 125.255 169.455 1.00 43.07 ?  613 TYR B C     1 
ATOM   10474 O  O     . TYR B 1 613 ? 136.070 125.335 168.909 1.00 43.80 ?  613 TYR B O     1 
ATOM   10475 C  CB    . TYR B 1 613 ? 138.331 126.158 167.426 1.00 42.88 ?  613 TYR B CB    1 
ATOM   10476 C  CG    . TYR B 1 613 ? 138.031 127.584 167.825 1.00 43.43 ?  613 TYR B CG    1 
ATOM   10477 C  CD1   . TYR B 1 613 ? 138.800 128.232 168.783 1.00 42.09 ?  613 TYR B CD1   1 
ATOM   10478 C  CD2   . TYR B 1 613 ? 136.980 128.280 167.247 1.00 45.50 ?  613 TYR B CD2   1 
ATOM   10479 C  CE1   . TYR B 1 613 ? 138.530 129.533 169.150 1.00 44.64 ?  613 TYR B CE1   1 
ATOM   10480 C  CE2   . TYR B 1 613 ? 136.703 129.581 167.609 1.00 45.24 ?  613 TYR B CE2   1 
ATOM   10481 C  CZ    . TYR B 1 613 ? 137.481 130.203 168.560 1.00 48.46 ?  613 TYR B CZ    1 
ATOM   10482 O  OH    . TYR B 1 613 ? 137.208 131.501 168.922 1.00 47.39 ?  613 TYR B OH    1 
ATOM   10483 N  N     . PRO B 1 614 ? 137.304 125.203 170.777 1.00 39.22 ?  614 PRO B N     1 
ATOM   10484 C  CA    . PRO B 1 614 ? 136.139 125.459 171.626 1.00 42.67 ?  614 PRO B CA    1 
ATOM   10485 C  C     . PRO B 1 614 ? 135.675 126.896 171.469 1.00 41.86 ?  614 PRO B C     1 
ATOM   10486 O  O     . PRO B 1 614 ? 136.466 127.803 171.200 1.00 42.89 ?  614 PRO B O     1 
ATOM   10487 C  CB    . PRO B 1 614 ? 136.658 125.194 173.046 1.00 39.16 ?  614 PRO B CB    1 
ATOM   10488 C  CG    . PRO B 1 614 ? 137.978 124.507 172.873 1.00 42.11 ?  614 PRO B CG    1 
ATOM   10489 C  CD    . PRO B 1 614 ? 138.522 124.969 171.566 1.00 40.31 ?  614 PRO B CD    1 
ATOM   10490 N  N     . MET B 1 615 ? 134.373 127.098 171.630 1.00 40.49 ?  615 MET B N     1 
ATOM   10491 C  CA    . MET B 1 615 ? 133.832 128.442 171.520 1.00 40.16 ?  615 MET B CA    1 
ATOM   10492 C  C     . MET B 1 615 ? 134.396 129.321 172.634 1.00 44.34 ?  615 MET B C     1 
ATOM   10493 O  O     . MET B 1 615 ? 134.645 128.834 173.742 1.00 42.90 ?  615 MET B O     1 
ATOM   10494 C  CB    . MET B 1 615 ? 132.305 128.416 171.568 1.00 38.52 ?  615 MET B CB    1 
ATOM   10495 C  CG    . MET B 1 615 ? 131.681 128.040 170.235 1.00 41.18 ?  615 MET B CG    1 
ATOM   10496 S  SD    . MET B 1 615 ? 132.737 128.547 168.863 1.00 52.06 ?  615 MET B SD    1 
ATOM   10497 C  CE    . MET B 1 615 ? 131.752 128.064 167.451 1.00 41.46 ?  615 MET B CE    1 
ATOM   10498 N  N     . PRO B 1 616 ? 134.632 130.604 172.369 1.00 45.96 ?  616 PRO B N     1 
ATOM   10499 C  CA    . PRO B 1 616 ? 135.323 131.451 173.350 1.00 39.83 ?  616 PRO B CA    1 
ATOM   10500 C  C     . PRO B 1 616 ? 134.553 131.543 174.657 1.00 41.31 ?  616 PRO B C     1 
ATOM   10501 O  O     . PRO B 1 616 ? 133.375 131.906 174.681 1.00 42.63 ?  616 PRO B O     1 
ATOM   10502 C  CB    . PRO B 1 616 ? 135.405 132.810 172.647 1.00 36.23 ?  616 PRO B CB    1 
ATOM   10503 C  CG    . PRO B 1 616 ? 135.212 132.508 171.200 1.00 41.50 ?  616 PRO B CG    1 
ATOM   10504 C  CD    . PRO B 1 616 ? 134.298 131.340 171.139 1.00 40.52 ?  616 PRO B CD    1 
ATOM   10505 N  N     . GLY B 1 617 ? 135.236 131.220 175.750 1.00 40.43 ?  617 GLY B N     1 
ATOM   10506 C  CA    . GLY B 1 617 ? 134.622 131.206 177.057 1.00 36.58 ?  617 GLY B CA    1 
ATOM   10507 C  C     . GLY B 1 617 ? 133.895 129.929 177.412 1.00 41.88 ?  617 GLY B C     1 
ATOM   10508 O  O     . GLY B 1 617 ? 133.267 129.873 178.476 1.00 45.55 ?  617 GLY B O     1 
ATOM   10509 N  N     . LEU B 1 618 ? 133.954 128.909 176.560 1.00 44.70 ?  618 LEU B N     1 
ATOM   10510 C  CA    . LEU B 1 618 ? 133.305 127.642 176.864 1.00 38.50 ?  618 LEU B CA    1 
ATOM   10511 C  C     . LEU B 1 618 ? 133.982 126.969 178.050 1.00 39.94 ?  618 LEU B C     1 
ATOM   10512 O  O     . LEU B 1 618 ? 135.210 126.917 178.140 1.00 44.64 ?  618 LEU B O     1 
ATOM   10513 C  CB    . LEU B 1 618 ? 133.340 126.718 175.648 1.00 38.04 ?  618 LEU B CB    1 
ATOM   10514 C  CG    . LEU B 1 618 ? 132.609 125.381 175.766 1.00 40.00 ?  618 LEU B CG    1 
ATOM   10515 C  CD1   . LEU B 1 618 ? 131.132 125.598 176.029 1.00 41.29 ?  618 LEU B CD1   1 
ATOM   10516 C  CD2   . LEU B 1 618 ? 132.813 124.557 174.510 1.00 40.82 ?  618 LEU B CD2   1 
ATOM   10517 N  N     . ALA B 1 619 ? 133.166 126.454 178.962 1.00 47.78 ?  619 ALA B N     1 
ATOM   10518 C  CA    . ALA B 1 619 ? 133.652 125.769 180.149 1.00 47.23 ?  619 ALA B CA    1 
ATOM   10519 C  C     . ALA B 1 619 ? 132.573 124.798 180.607 1.00 49.90 ?  619 ALA B C     1 
ATOM   10520 O  O     . ALA B 1 619 ? 131.610 124.527 179.884 1.00 54.00 ?  619 ALA B O     1 
ATOM   10521 C  CB    . ALA B 1 619 ? 134.033 126.777 181.240 1.00 46.77 ?  619 ALA B CB    1 
ATOM   10522 N  N     . SER B 1 620 ? 132.738 124.263 181.815 1.00 56.15 ?  620 SER B N     1 
ATOM   10523 C  CA    . SER B 1 620 ? 131.730 123.366 182.367 1.00 55.66 ?  620 SER B CA    1 
ATOM   10524 C  C     . SER B 1 620 ? 130.517 124.133 182.879 1.00 55.44 ?  620 SER B C     1 
ATOM   10525 O  O     . SER B 1 620 ? 129.382 123.658 182.757 1.00 57.57 ?  620 SER B O     1 
ATOM   10526 C  CB    . SER B 1 620 ? 132.340 122.521 183.484 1.00 57.26 ?  620 SER B CB    1 
ATOM   10527 O  OG    . SER B 1 620 ? 133.558 121.935 183.065 1.00 59.15 ?  620 SER B OG    1 
ATOM   10528 N  N     . ASN B 1 621 ? 130.737 125.319 183.452 1.00 50.85 ?  621 ASN B N     1 
ATOM   10529 C  CA    . ASN B 1 621 ? 129.636 126.069 184.048 1.00 52.15 ?  621 ASN B CA    1 
ATOM   10530 C  C     . ASN B 1 621 ? 128.707 126.647 182.985 1.00 54.39 ?  621 ASN B C     1 
ATOM   10531 O  O     . ASN B 1 621 ? 127.489 126.709 183.187 1.00 56.25 ?  621 ASN B O     1 
ATOM   10532 C  CB    . ASN B 1 621 ? 130.182 127.177 184.950 1.00 53.65 ?  621 ASN B CB    1 
ATOM   10533 C  CG    . ASN B 1 621 ? 130.948 128.234 184.178 1.00 57.66 ?  621 ASN B CG    1 
ATOM   10534 O  OD1   . ASN B 1 621 ? 131.974 127.949 183.561 1.00 59.16 ?  621 ASN B OD1   1 
ATOM   10535 N  ND2   . ASN B 1 621 ? 130.454 129.467 184.212 1.00 55.87 ?  621 ASN B ND2   1 
ATOM   10536 N  N     . ASN B 1 622 ? 129.258 127.076 181.849 1.00 46.91 ?  622 ASN B N     1 
ATOM   10537 C  CA    . ASN B 1 622 ? 128.471 127.688 180.785 1.00 45.83 ?  622 ASN B CA    1 
ATOM   10538 C  C     . ASN B 1 622 ? 128.326 126.779 179.570 1.00 47.47 ?  622 ASN B C     1 
ATOM   10539 O  O     . ASN B 1 622 ? 128.084 127.266 178.463 1.00 53.86 ?  622 ASN B O     1 
ATOM   10540 C  CB    . ASN B 1 622 ? 129.079 129.036 180.383 1.00 46.81 ?  622 ASN B CB    1 
ATOM   10541 C  CG    . ASN B 1 622 ? 130.491 128.914 179.826 1.00 46.56 ?  622 ASN B CG    1 
ATOM   10542 O  OD1   . ASN B 1 622 ? 130.955 127.827 179.489 1.00 52.25 ?  622 ASN B OD1   1 
ATOM   10543 N  ND2   . ASN B 1 622 ? 131.180 130.042 179.733 1.00 43.47 ?  622 ASN B ND2   1 
ATOM   10544 N  N     . TRP B 1 623 ? 128.479 125.466 179.757 1.00 41.95 ?  623 TRP B N     1 
ATOM   10545 C  CA    . TRP B 1 623 ? 128.420 124.545 178.626 1.00 40.84 ?  623 TRP B CA    1 
ATOM   10546 C  C     . TRP B 1 623 ? 127.047 124.560 177.965 1.00 42.27 ?  623 TRP B C     1 
ATOM   10547 O  O     . TRP B 1 623 ? 126.946 124.575 176.732 1.00 42.30 ?  623 TRP B O     1 
ATOM   10548 C  CB    . TRP B 1 623 ? 128.776 123.132 179.085 1.00 45.73 ?  623 TRP B CB    1 
ATOM   10549 C  CG    . TRP B 1 623 ? 128.560 122.080 178.041 1.00 43.63 ?  623 TRP B CG    1 
ATOM   10550 C  CD1   . TRP B 1 623 ? 127.418 121.371 177.816 1.00 40.76 ?  623 TRP B CD1   1 
ATOM   10551 C  CD2   . TRP B 1 623 ? 129.515 121.615 177.081 1.00 42.24 ?  623 TRP B CD2   1 
ATOM   10552 N  NE1   . TRP B 1 623 ? 127.601 120.497 176.776 1.00 42.99 ?  623 TRP B NE1   1 
ATOM   10553 C  CE2   . TRP B 1 623 ? 128.881 120.624 176.308 1.00 40.39 ?  623 TRP B CE2   1 
ATOM   10554 C  CE3   . TRP B 1 623 ? 130.846 121.940 176.802 1.00 39.81 ?  623 TRP B CE3   1 
ATOM   10555 C  CZ2   . TRP B 1 623 ? 129.530 119.958 175.272 1.00 38.39 ?  623 TRP B CZ2   1 
ATOM   10556 C  CZ3   . TRP B 1 623 ? 131.487 121.277 175.773 1.00 42.86 ?  623 TRP B CZ3   1 
ATOM   10557 C  CH2   . TRP B 1 623 ? 130.829 120.298 175.021 1.00 42.62 ?  623 TRP B CH2   1 
ATOM   10558 N  N     . PHE B 1 624 ? 125.981 124.557 178.761 1.00 48.20 ?  624 PHE B N     1 
ATOM   10559 C  CA    . PHE B 1 624 ? 124.635 124.475 178.214 1.00 45.50 ?  624 PHE B CA    1 
ATOM   10560 C  C     . PHE B 1 624 ? 124.053 125.830 177.839 1.00 45.25 ?  624 PHE B C     1 
ATOM   10561 O  O     . PHE B 1 624 ? 123.000 125.875 177.195 1.00 52.40 ?  624 PHE B O     1 
ATOM   10562 C  CB    . PHE B 1 624 ? 123.709 123.763 179.204 1.00 49.11 ?  624 PHE B CB    1 
ATOM   10563 C  CG    . PHE B 1 624 ? 123.913 122.276 179.247 1.00 50.34 ?  624 PHE B CG    1 
ATOM   10564 C  CD1   . PHE B 1 624 ? 123.505 121.478 178.192 1.00 44.39 ?  624 PHE B CD1   1 
ATOM   10565 C  CD2   . PHE B 1 624 ? 124.528 121.679 180.334 1.00 48.19 ?  624 PHE B CD2   1 
ATOM   10566 C  CE1   . PHE B 1 624 ? 123.696 120.112 178.223 1.00 44.64 ?  624 PHE B CE1   1 
ATOM   10567 C  CE2   . PHE B 1 624 ? 124.723 120.311 180.372 1.00 49.33 ?  624 PHE B CE2   1 
ATOM   10568 C  CZ    . PHE B 1 624 ? 124.306 119.527 179.315 1.00 48.15 ?  624 PHE B CZ    1 
ATOM   10569 N  N     . PHE B 1 625 ? 124.705 126.928 178.219 1.00 39.83 ?  625 PHE B N     1 
ATOM   10570 C  CA    . PHE B 1 625 ? 124.351 128.224 177.658 1.00 37.08 ?  625 PHE B CA    1 
ATOM   10571 C  C     . PHE B 1 625 ? 124.915 128.411 176.260 1.00 36.39 ?  625 PHE B C     1 
ATOM   10572 O  O     . PHE B 1 625 ? 124.430 129.270 175.518 1.00 41.33 ?  625 PHE B O     1 
ATOM   10573 C  CB    . PHE B 1 625 ? 124.831 129.353 178.569 1.00 32.77 ?  625 PHE B CB    1 
ATOM   10574 C  CG    . PHE B 1 625 ? 124.045 129.481 179.838 1.00 35.96 ?  625 PHE B CG    1 
ATOM   10575 C  CD1   . PHE B 1 625 ? 122.716 129.862 179.805 1.00 37.62 ?  625 PHE B CD1   1 
ATOM   10576 C  CD2   . PHE B 1 625 ? 124.633 129.223 181.064 1.00 37.97 ?  625 PHE B CD2   1 
ATOM   10577 C  CE1   . PHE B 1 625 ? 121.987 129.983 180.970 1.00 40.00 ?  625 PHE B CE1   1 
ATOM   10578 C  CE2   . PHE B 1 625 ? 123.910 129.344 182.232 1.00 37.58 ?  625 PHE B CE2   1 
ATOM   10579 C  CZ    . PHE B 1 625 ? 122.585 129.725 182.185 1.00 40.99 ?  625 PHE B CZ    1 
ATOM   10580 N  N     . TYR B 1 626 ? 125.921 127.626 175.888 1.00 29.50 ?  626 TYR B N     1 
ATOM   10581 C  CA    . TYR B 1 626 ? 126.444 127.618 174.525 1.00 33.44 ?  626 TYR B CA    1 
ATOM   10582 C  C     . TYR B 1 626 ? 125.667 126.637 173.655 1.00 30.15 ?  626 TYR B C     1 
ATOM   10583 O  O     . TYR B 1 626 ? 126.236 125.775 172.991 1.00 36.11 ?  626 TYR B O     1 
ATOM   10584 C  CB    . TYR B 1 626 ? 127.928 127.279 174.540 1.00 32.29 ?  626 TYR B CB    1 
ATOM   10585 C  CG    . TYR B 1 626 ? 128.825 128.483 174.682 1.00 34.18 ?  626 TYR B CG    1 
ATOM   10586 C  CD1   . TYR B 1 626 ? 129.067 129.323 173.606 1.00 35.39 ?  626 TYR B CD1   1 
ATOM   10587 C  CD2   . TYR B 1 626 ? 129.429 128.779 175.896 1.00 34.34 ?  626 TYR B CD2   1 
ATOM   10588 C  CE1   . TYR B 1 626 ? 129.886 130.423 173.733 1.00 35.36 ?  626 TYR B CE1   1 
ATOM   10589 C  CE2   . TYR B 1 626 ? 130.249 129.878 176.032 1.00 31.69 ?  626 TYR B CE2   1 
ATOM   10590 C  CZ    . TYR B 1 626 ? 130.474 130.696 174.948 1.00 30.87 ?  626 TYR B CZ    1 
ATOM   10591 O  OH    . TYR B 1 626 ? 131.287 131.792 175.078 1.00 38.82 ?  626 TYR B OH    1 
ATOM   10592 N  N     . LYS B 1 627 ? 124.346 126.772 173.665 1.00 33.87 ?  627 LYS B N     1 
ATOM   10593 C  CA    . LYS B 1 627 ? 123.491 125.881 172.895 1.00 34.18 ?  627 LYS B CA    1 
ATOM   10594 C  C     . LYS B 1 627 ? 123.780 126.029 171.407 1.00 37.69 ?  627 LYS B C     1 
ATOM   10595 O  O     . LYS B 1 627 ? 123.900 127.144 170.893 1.00 44.50 ?  627 LYS B O     1 
ATOM   10596 C  CB    . LYS B 1 627 ? 122.025 126.188 173.195 1.00 37.36 ?  627 LYS B CB    1 
ATOM   10597 C  CG    . LYS B 1 627 ? 121.027 125.247 172.556 1.00 37.26 ?  627 LYS B CG    1 
ATOM   10598 C  CD    . LYS B 1 627 ? 119.639 125.488 173.123 1.00 32.29 ?  627 LYS B CD    1 
ATOM   10599 C  CE    . LYS B 1 627 ? 118.607 124.594 172.467 1.00 39.91 ?  627 LYS B CE    1 
ATOM   10600 N  NZ    . LYS B 1 627 ? 117.249 124.826 173.027 1.00 41.71 1  627 LYS B NZ    1 
ATOM   10601 N  N     . GLU B 1 628 ? 123.912 124.900 170.719 1.00 39.03 ?  628 GLU B N     1 
ATOM   10602 C  CA    . GLU B 1 628 ? 124.205 124.936 169.294 1.00 35.29 ?  628 GLU B CA    1 
ATOM   10603 C  C     . GLU B 1 628 ? 123.013 125.485 168.520 1.00 40.27 ?  628 GLU B C     1 
ATOM   10604 O  O     . GLU B 1 628 ? 121.856 125.324 168.916 1.00 45.56 ?  628 GLU B O     1 
ATOM   10605 C  CB    . GLU B 1 628 ? 124.575 123.545 168.788 1.00 39.70 ?  628 GLU B CB    1 
ATOM   10606 C  CG    . GLU B 1 628 ? 125.737 122.912 169.534 1.00 41.43 ?  628 GLU B CG    1 
ATOM   10607 C  CD    . GLU B 1 628 ? 126.470 121.879 168.705 1.00 47.84 ?  628 GLU B CD    1 
ATOM   10608 O  OE1   . GLU B 1 628 ? 125.938 121.479 167.648 1.00 43.73 ?  628 GLU B OE1   1 
ATOM   10609 O  OE2   . GLU B 1 628 ? 127.578 121.469 169.107 1.00 45.74 -1 628 GLU B OE2   1 
ATOM   10610 N  N     . ALA B 1 629 ? 123.316 126.152 167.404 1.00 41.50 ?  629 ALA B N     1 
ATOM   10611 C  CA    . ALA B 1 629 ? 122.277 126.824 166.630 1.00 32.10 ?  629 ALA B CA    1 
ATOM   10612 C  C     . ALA B 1 629 ? 121.249 125.837 166.094 1.00 37.00 ?  629 ALA B C     1 
ATOM   10613 O  O     . ALA B 1 629 ? 120.051 126.140 166.052 1.00 44.16 ?  629 ALA B O     1 
ATOM   10614 C  CB    . ALA B 1 629 ? 122.912 127.614 165.487 1.00 30.45 ?  629 ALA B CB    1 
ATOM   10615 N  N     . TYR B 1 630 ? 121.697 124.655 165.669 1.00 40.68 ?  630 TYR B N     1 
ATOM   10616 C  CA    . TYR B 1 630 ? 120.770 123.666 165.127 1.00 39.14 ?  630 TYR B CA    1 
ATOM   10617 C  C     . TYR B 1 630 ? 119.805 123.153 166.188 1.00 42.65 ?  630 TYR B C     1 
ATOM   10618 O  O     . TYR B 1 630 ? 118.649 122.850 165.876 1.00 49.05 ?  630 TYR B O     1 
ATOM   10619 C  CB    . TYR B 1 630 ? 121.548 122.510 164.506 1.00 37.55 ?  630 TYR B CB    1 
ATOM   10620 C  CG    . TYR B 1 630 ? 122.509 122.948 163.428 1.00 37.64 ?  630 TYR B CG    1 
ATOM   10621 C  CD1   . TYR B 1 630 ? 122.070 123.176 162.132 1.00 38.02 ?  630 TYR B CD1   1 
ATOM   10622 C  CD2   . TYR B 1 630 ? 123.853 123.144 163.707 1.00 37.73 ?  630 TYR B CD2   1 
ATOM   10623 C  CE1   . TYR B 1 630 ? 122.943 123.579 161.144 1.00 38.57 ?  630 TYR B CE1   1 
ATOM   10624 C  CE2   . TYR B 1 630 ? 124.734 123.548 162.726 1.00 40.36 ?  630 TYR B CE2   1 
ATOM   10625 C  CZ    . TYR B 1 630 ? 124.272 123.764 161.446 1.00 45.55 ?  630 TYR B CZ    1 
ATOM   10626 O  OH    . TYR B 1 630 ? 125.146 124.165 160.463 1.00 51.53 ?  630 TYR B OH    1 
ATOM   10627 N  N     . ASP B 1 631 ? 120.255 123.050 167.439 1.00 42.26 ?  631 ASP B N     1 
ATOM   10628 C  CA    . ASP B 1 631 ? 119.376 122.638 168.526 1.00 37.01 ?  631 ASP B CA    1 
ATOM   10629 C  C     . ASP B 1 631 ? 118.379 123.718 168.919 1.00 43.14 ?  631 ASP B C     1 
ATOM   10630 O  O     . ASP B 1 631 ? 117.466 123.439 169.703 1.00 47.63 ?  631 ASP B O     1 
ATOM   10631 C  CB    . ASP B 1 631 ? 120.203 122.239 169.748 1.00 41.58 ?  631 ASP B CB    1 
ATOM   10632 C  CG    . ASP B 1 631 ? 121.185 121.125 169.450 1.00 48.57 ?  631 ASP B CG    1 
ATOM   10633 O  OD1   . ASP B 1 631 ? 120.852 120.236 168.640 1.00 49.25 ?  631 ASP B OD1   1 
ATOM   10634 O  OD2   . ASP B 1 631 ? 122.293 121.139 170.028 1.00 50.10 -1 631 ASP B OD2   1 
ATOM   10635 N  N     . MET B 1 632 ? 118.524 124.929 168.396 1.00 37.56 ?  632 MET B N     1 
ATOM   10636 C  CA    . MET B 1 632 ? 117.703 126.058 168.800 1.00 38.15 ?  632 MET B CA    1 
ATOM   10637 C  C     . MET B 1 632 ? 116.397 126.099 168.018 1.00 37.21 ?  632 MET B C     1 
ATOM   10638 O  O     . MET B 1 632 ? 116.256 125.493 166.953 1.00 36.18 ?  632 MET B O     1 
ATOM   10639 C  CB    . MET B 1 632 ? 118.459 127.369 168.597 1.00 36.52 ?  632 MET B CB    1 
ATOM   10640 C  CG    . MET B 1 632 ? 119.126 127.900 169.842 1.00 35.34 ?  632 MET B CG    1 
ATOM   10641 S  SD    . MET B 1 632 ? 120.511 128.975 169.468 1.00 45.68 ?  632 MET B SD    1 
ATOM   10642 C  CE    . MET B 1 632 ? 121.345 128.996 171.047 1.00 33.51 ?  632 MET B CE    1 
ATOM   10643 N  N     . ASP B 1 633 ? 115.434 126.833 168.567 1.00 37.50 ?  633 ASP B N     1 
ATOM   10644 C  CA    . ASP B 1 633 ? 114.191 127.120 167.866 1.00 33.40 ?  633 ASP B CA    1 
ATOM   10645 C  C     . ASP B 1 633 ? 114.416 128.306 166.939 1.00 36.19 ?  633 ASP B C     1 
ATOM   10646 O  O     . ASP B 1 633 ? 114.703 129.415 167.403 1.00 43.42 ?  633 ASP B O     1 
ATOM   10647 C  CB    . ASP B 1 633 ? 113.072 127.414 168.862 1.00 30.86 ?  633 ASP B CB    1 
ATOM   10648 C  CG    . ASP B 1 633 ? 111.722 127.578 168.193 1.00 40.37 ?  633 ASP B CG    1 
ATOM   10649 O  OD1   . ASP B 1 633 ? 111.604 127.261 166.991 1.00 43.37 ?  633 ASP B OD1   1 
ATOM   10650 O  OD2   . ASP B 1 633 ? 110.776 128.027 168.871 1.00 41.05 -1 633 ASP B OD2   1 
ATOM   10651 N  N     . MET B 1 634 ? 114.294 128.075 165.630 1.00 30.22 ?  634 MET B N     1 
ATOM   10652 C  CA    . MET B 1 634 ? 114.536 129.143 164.668 1.00 23.54 ?  634 MET B CA    1 
ATOM   10653 C  C     . MET B 1 634 ? 113.553 130.294 164.817 1.00 26.50 ?  634 MET B C     1 
ATOM   10654 O  O     . MET B 1 634 ? 113.869 131.414 164.407 1.00 31.39 ?  634 MET B O     1 
ATOM   10655 C  CB    . MET B 1 634 ? 114.484 128.594 163.243 1.00 26.08 ?  634 MET B CB    1 
ATOM   10656 C  CG    . MET B 1 634 ? 115.776 127.935 162.796 1.00 31.31 ?  634 MET B CG    1 
ATOM   10657 S  SD    . MET B 1 634 ? 117.207 129.015 163.000 1.00 43.09 ?  634 MET B SD    1 
ATOM   10658 C  CE    . MET B 1 634 ? 118.076 128.188 164.331 1.00 29.75 ?  634 MET B CE    1 
ATOM   10659 N  N     . PHE B 1 635 ? 112.374 130.050 165.391 1.00 26.09 ?  635 PHE B N     1 
ATOM   10660 C  CA    . PHE B 1 635 ? 111.453 131.148 165.664 1.00 23.44 ?  635 PHE B CA    1 
ATOM   10661 C  C     . PHE B 1 635 ? 112.035 132.107 166.694 1.00 21.59 ?  635 PHE B C     1 
ATOM   10662 O  O     . PHE B 1 635 ? 111.916 133.329 166.554 1.00 26.28 ?  635 PHE B O     1 
ATOM   10663 C  CB    . PHE B 1 635 ? 110.107 130.600 166.136 1.00 27.07 ?  635 PHE B CB    1 
ATOM   10664 C  CG    . PHE B 1 635 ? 109.129 130.362 165.022 1.00 30.07 ?  635 PHE B CG    1 
ATOM   10665 C  CD1   . PHE B 1 635 ? 109.534 129.753 163.848 1.00 26.06 ?  635 PHE B CD1   1 
ATOM   10666 C  CD2   . PHE B 1 635 ? 107.807 130.749 165.149 1.00 25.64 ?  635 PHE B CD2   1 
ATOM   10667 C  CE1   . PHE B 1 635 ? 108.639 129.533 162.821 1.00 24.41 ?  635 PHE B CE1   1 
ATOM   10668 C  CE2   . PHE B 1 635 ? 106.907 130.531 164.124 1.00 28.30 ?  635 PHE B CE2   1 
ATOM   10669 C  CZ    . PHE B 1 635 ? 107.324 129.920 162.960 1.00 25.18 ?  635 PHE B CZ    1 
ATOM   10670 N  N     . LYS B 1 636 ? 112.686 131.575 167.729 1.00 27.48 ?  636 LYS B N     1 
ATOM   10671 C  CA    . LYS B 1 636 ? 113.298 132.435 168.734 1.00 30.38 ?  636 LYS B CA    1 
ATOM   10672 C  C     . LYS B 1 636 ? 114.524 133.157 168.187 1.00 26.86 ?  636 LYS B C     1 
ATOM   10673 O  O     . LYS B 1 636 ? 114.795 134.298 168.574 1.00 36.77 ?  636 LYS B O     1 
ATOM   10674 C  CB    . LYS B 1 636 ? 113.658 131.616 169.970 1.00 30.54 ?  636 LYS B CB    1 
ATOM   10675 C  CG    . LYS B 1 636 ? 112.469 130.912 170.599 1.00 29.29 ?  636 LYS B CG    1 
ATOM   10676 C  CD    . LYS B 1 636 ? 111.995 131.639 171.843 1.00 34.76 ?  636 LYS B CD    1 
ATOM   10677 C  CE    . LYS B 1 636 ? 110.530 131.356 172.125 1.00 33.40 ?  636 LYS B CE    1 
ATOM   10678 N  NZ    . LYS B 1 636 ? 109.756 132.609 172.339 1.00 35.79 1  636 LYS B NZ    1 
ATOM   10679 N  N     . VAL B 1 637 ? 115.269 132.517 167.285 1.00 24.28 ?  637 VAL B N     1 
ATOM   10680 C  CA    . VAL B 1 637 ? 116.375 133.204 166.624 1.00 17.58 ?  637 VAL B CA    1 
ATOM   10681 C  C     . VAL B 1 637 ? 115.846 134.331 165.747 1.00 27.32 ?  637 VAL B C     1 
ATOM   10682 O  O     . VAL B 1 637 ? 116.438 135.417 165.679 1.00 31.76 ?  637 VAL B O     1 
ATOM   10683 C  CB    . VAL B 1 637 ? 117.221 132.200 165.821 1.00 21.70 ?  637 VAL B CB    1 
ATOM   10684 C  CG1   . VAL B 1 637 ? 118.395 132.901 165.163 1.00 22.34 ?  637 VAL B CG1   1 
ATOM   10685 C  CG2   . VAL B 1 637 ? 117.700 131.076 166.723 1.00 23.89 ?  637 VAL B CG2   1 
ATOM   10686 N  N     . VAL B 1 638 ? 114.725 134.093 165.062 1.00 25.42 ?  638 VAL B N     1 
ATOM   10687 C  CA    . VAL B 1 638 ? 114.074 135.151 164.296 1.00 22.70 ?  638 VAL B CA    1 
ATOM   10688 C  C     . VAL B 1 638 ? 113.662 136.290 165.217 1.00 19.58 ?  638 VAL B C     1 
ATOM   10689 O  O     . VAL B 1 638 ? 113.815 137.468 164.879 1.00 30.46 ?  638 VAL B O     1 
ATOM   10690 C  CB    . VAL B 1 638 ? 112.863 134.591 163.525 1.00 24.93 ?  638 VAL B CB    1 
ATOM   10691 C  CG1   . VAL B 1 638 ? 111.958 135.720 163.067 1.00 14.67 ?  638 VAL B CG1   1 
ATOM   10692 C  CG2   . VAL B 1 638 ? 113.310 133.758 162.341 1.00 23.91 ?  638 VAL B CG2   1 
ATOM   10693 N  N     . ASP B 1 639 ? 113.124 135.955 166.389 1.00 17.63 ?  639 ASP B N     1 
ATOM   10694 C  CA    . ASP B 1 639 ? 112.733 136.980 167.353 1.00 21.91 ?  639 ASP B CA    1 
ATOM   10695 C  C     . ASP B 1 639 ? 113.932 137.813 167.786 1.00 26.76 ?  639 ASP B C     1 
ATOM   10696 O  O     . ASP B 1 639 ? 113.847 139.043 167.869 1.00 34.74 ?  639 ASP B O     1 
ATOM   10697 C  CB    . ASP B 1 639 ? 112.071 136.327 168.565 1.00 25.22 ?  639 ASP B CB    1 
ATOM   10698 C  CG    . ASP B 1 639 ? 110.609 136.017 168.336 1.00 36.03 ?  639 ASP B CG    1 
ATOM   10699 O  OD1   . ASP B 1 639 ? 109.958 136.746 167.559 1.00 33.39 ?  639 ASP B OD1   1 
ATOM   10700 O  OD2   . ASP B 1 639 ? 110.109 135.042 168.933 1.00 39.17 -1 639 ASP B OD2   1 
ATOM   10701 N  N     . MET B 1 640 ? 115.060 137.157 168.057 1.00 24.69 ?  640 MET B N     1 
ATOM   10702 C  CA    . MET B 1 640 ? 116.272 137.875 168.440 1.00 17.97 ?  640 MET B CA    1 
ATOM   10703 C  C     . MET B 1 640 ? 116.748 138.800 167.325 1.00 23.27 ?  640 MET B C     1 
ATOM   10704 O  O     . MET B 1 640 ? 117.065 139.972 167.564 1.00 32.90 ?  640 MET B O     1 
ATOM   10705 C  CB    . MET B 1 640 ? 117.370 136.879 168.811 1.00 22.73 ?  640 MET B CB    1 
ATOM   10706 C  CG    . MET B 1 640 ? 118.767 137.466 168.789 1.00 28.17 ?  640 MET B CG    1 
ATOM   10707 S  SD    . MET B 1 640 ? 119.088 138.507 170.220 1.00 39.52 ?  640 MET B SD    1 
ATOM   10708 C  CE    . MET B 1 640 ? 119.460 137.267 171.449 1.00 26.08 ?  640 MET B CE    1 
ATOM   10709 N  N     . ILE B 1 641 ? 116.802 138.288 166.094 1.00 28.94 ?  641 ILE B N     1 
ATOM   10710 C  CA    . ILE B 1 641 ? 117.310 139.092 164.988 1.00 21.13 ?  641 ILE B CA    1 
ATOM   10711 C  C     . ILE B 1 641 ? 116.373 140.252 164.686 1.00 19.87 ?  641 ILE B C     1 
ATOM   10712 O  O     . ILE B 1 641 ? 116.826 141.346 164.331 1.00 29.61 ?  641 ILE B O     1 
ATOM   10713 C  CB    . ILE B 1 641 ? 117.552 138.209 163.751 1.00 25.85 ?  641 ILE B CB    1 
ATOM   10714 C  CG1   . ILE B 1 641 ? 118.559 137.109 164.083 1.00 18.83 ?  641 ILE B CG1   1 
ATOM   10715 C  CG2   . ILE B 1 641 ? 118.074 139.041 162.591 1.00 18.72 ?  641 ILE B CG2   1 
ATOM   10716 C  CD1   . ILE B 1 641 ? 119.786 137.610 164.813 1.00 20.70 ?  641 ILE B CD1   1 
ATOM   10717 N  N     . ALA B 1 642 ? 115.062 140.048 164.829 1.00 17.45 ?  642 ALA B N     1 
ATOM   10718 C  CA    . ALA B 1 642 ? 114.115 141.140 164.643 1.00 20.38 ?  642 ALA B CA    1 
ATOM   10719 C  C     . ALA B 1 642 ? 114.223 142.164 165.763 1.00 21.19 ?  642 ALA B C     1 
ATOM   10720 O  O     . ALA B 1 642 ? 113.997 143.357 165.532 1.00 25.52 ?  642 ALA B O     1 
ATOM   10721 C  CB    . ALA B 1 642 ? 112.692 140.594 164.556 1.00 15.88 ?  642 ALA B CB    1 
ATOM   10722 N  N     . THR B 1 643 ? 114.546 141.720 166.977 1.00 21.94 ?  643 THR B N     1 
ATOM   10723 C  CA    . THR B 1 643 ? 114.833 142.661 168.052 1.00 18.28 ?  643 THR B CA    1 
ATOM   10724 C  C     . THR B 1 643 ? 116.053 143.510 167.721 1.00 24.19 ?  643 THR B C     1 
ATOM   10725 O  O     . THR B 1 643 ? 116.058 144.724 167.953 1.00 26.56 ?  643 THR B O     1 
ATOM   10726 C  CB    . THR B 1 643 ? 115.044 141.909 169.364 1.00 17.26 ?  643 THR B CB    1 
ATOM   10727 O  OG1   . THR B 1 643 ? 113.887 141.115 169.650 1.00 22.86 ?  643 THR B OG1   1 
ATOM   10728 C  CG2   . THR B 1 643 ? 115.279 142.879 170.501 1.00 17.83 ?  643 THR B CG2   1 
ATOM   10729 N  N     . ILE B 1 644 ? 117.100 142.885 167.182 1.00 22.78 ?  644 ILE B N     1 
ATOM   10730 C  CA    . ILE B 1 644 ? 118.280 143.640 166.775 1.00 10.33 ?  644 ILE B CA    1 
ATOM   10731 C  C     . ILE B 1 644 ? 117.982 144.483 165.540 1.00 16.72 ?  644 ILE B C     1 
ATOM   10732 O  O     . ILE B 1 644 ? 118.430 145.630 165.433 1.00 22.18 ?  644 ILE B O     1 
ATOM   10733 C  CB    . ILE B 1 644 ? 119.467 142.692 166.536 1.00 12.86 ?  644 ILE B CB    1 
ATOM   10734 C  CG1   . ILE B 1 644 ? 119.743 141.853 167.783 1.00 16.38 ?  644 ILE B CG1   1 
ATOM   10735 C  CG2   . ILE B 1 644 ? 120.701 143.478 166.148 1.00 8.54  ?  644 ILE B CG2   1 
ATOM   10736 C  CD1   . ILE B 1 644 ? 120.563 140.620 167.505 1.00 22.52 ?  644 ILE B CD1   1 
ATOM   10737 N  N     . GLN B 1 645 ? 117.218 143.930 164.591 1.00 12.43 ?  645 GLN B N     1 
ATOM   10738 C  CA    . GLN B 1 645 ? 117.005 144.597 163.308 1.00 13.88 ?  645 GLN B CA    1 
ATOM   10739 C  C     . GLN B 1 645 ? 116.307 145.940 163.465 1.00 17.48 ?  645 GLN B C     1 
ATOM   10740 O  O     . GLN B 1 645 ? 116.488 146.833 162.630 1.00 29.59 ?  645 GLN B O     1 
ATOM   10741 C  CB    . GLN B 1 645 ? 116.199 143.690 162.379 1.00 12.98 ?  645 GLN B CB    1 
ATOM   10742 C  CG    . GLN B 1 645 ? 116.020 144.230 160.973 1.00 3.84  ?  645 GLN B CG    1 
ATOM   10743 C  CD    . GLN B 1 645 ? 117.283 144.128 160.149 1.00 19.17 ?  645 GLN B CD    1 
ATOM   10744 O  OE1   . GLN B 1 645 ? 118.080 145.061 160.097 1.00 13.42 ?  645 GLN B OE1   1 
ATOM   10745 N  NE2   . GLN B 1 645 ? 117.471 142.989 159.495 1.00 16.27 ?  645 GLN B NE2   1 
ATOM   10746 N  N     . GLN B 1 646 ? 115.519 146.114 164.524 1.00 19.98 ?  646 GLN B N     1 
ATOM   10747 C  CA    . GLN B 1 646 ? 114.809 147.371 164.712 1.00 11.37 ?  646 GLN B CA    1 
ATOM   10748 C  C     . GLN B 1 646 ? 115.734 148.525 165.078 1.00 11.49 ?  646 GLN B C     1 
ATOM   10749 O  O     . GLN B 1 646 ? 115.287 149.674 165.077 1.00 15.53 ?  646 GLN B O     1 
ATOM   10750 C  CB    . GLN B 1 646 ? 113.725 147.209 165.776 1.00 19.79 ?  646 GLN B CB    1 
ATOM   10751 C  CG    . GLN B 1 646 ? 114.235 147.224 167.197 1.00 22.80 ?  646 GLN B CG    1 
ATOM   10752 C  CD    . GLN B 1 646 ? 113.146 146.922 168.201 1.00 27.77 ?  646 GLN B CD    1 
ATOM   10753 O  OE1   . GLN B 1 646 ? 113.212 145.930 168.924 1.00 26.85 ?  646 GLN B OE1   1 
ATOM   10754 N  NE2   . GLN B 1 646 ? 112.134 147.778 168.249 1.00 23.34 ?  646 GLN B NE2   1 
ATOM   10755 N  N     . HIS B 1 647 ? 117.001 148.255 165.382 1.00 29.18 ?  647 HIS B N     1 
ATOM   10756 C  CA    . HIS B 1 647 ? 117.972 149.301 165.662 1.00 12.41 ?  647 HIS B CA    1 
ATOM   10757 C  C     . HIS B 1 647 ? 119.086 149.369 164.627 1.00 13.61 ?  647 HIS B C     1 
ATOM   10758 O  O     . HIS B 1 647 ? 119.990 150.199 164.767 1.00 27.00 ?  647 HIS B O     1 
ATOM   10759 C  CB    . HIS B 1 647 ? 118.580 149.106 167.057 1.00 5.67  ?  647 HIS B CB    1 
ATOM   10760 C  CG    . HIS B 1 647 ? 117.563 148.927 168.139 1.00 14.52 ?  647 HIS B CG    1 
ATOM   10761 N  ND1   . HIS B 1 647 ? 116.659 149.909 168.480 1.00 18.16 ?  647 HIS B ND1   1 
ATOM   10762 C  CD2   . HIS B 1 647 ? 117.307 147.880 168.958 1.00 12.29 ?  647 HIS B CD2   1 
ATOM   10763 C  CE1   . HIS B 1 647 ? 115.889 149.474 169.461 1.00 20.52 ?  647 HIS B CE1   1 
ATOM   10764 N  NE2   . HIS B 1 647 ? 116.264 148.246 169.770 1.00 15.87 ?  647 HIS B NE2   1 
ATOM   10765 N  N     . ILE B 1 648 ? 119.044 148.529 163.599 1.00 14.96 ?  648 ILE B N     1 
ATOM   10766 C  CA    . ILE B 1 648 ? 120.050 148.502 162.544 1.00 16.22 ?  648 ILE B CA    1 
ATOM   10767 C  C     . ILE B 1 648 ? 119.410 149.078 161.289 1.00 14.31 ?  648 ILE B C     1 
ATOM   10768 O  O     . ILE B 1 648 ? 118.366 148.591 160.841 1.00 28.02 ?  648 ILE B O     1 
ATOM   10769 C  CB    . ILE B 1 648 ? 120.568 147.074 162.304 1.00 10.01 ?  648 ILE B CB    1 
ATOM   10770 C  CG1   . ILE B 1 648 ? 121.165 146.496 163.591 1.00 10.50 ?  648 ILE B CG1   1 
ATOM   10771 C  CG2   . ILE B 1 648 ? 121.598 147.052 161.194 1.00 3.67  ?  648 ILE B CG2   1 
ATOM   10772 C  CD1   . ILE B 1 648 ? 122.322 147.290 164.144 1.00 4.55  ?  648 ILE B CD1   1 
ATOM   10773 N  N     . ASP B 1 649 ? 120.026 150.120 160.723 1.00 7.88  ?  649 ASP B N     1 
ATOM   10774 C  CA    . ASP B 1 649 ? 119.423 150.778 159.568 1.00 9.36  ?  649 ASP B CA    1 
ATOM   10775 C  C     . ASP B 1 649 ? 119.553 149.936 158.306 1.00 7.99  ?  649 ASP B C     1 
ATOM   10776 O  O     . ASP B 1 649 ? 118.653 149.950 157.460 1.00 32.55 ?  649 ASP B O     1 
ATOM   10777 C  CB    . ASP B 1 649 ? 120.039 152.164 159.357 1.00 21.54 ?  649 ASP B CB    1 
ATOM   10778 C  CG    . ASP B 1 649 ? 121.553 152.141 159.329 1.00 16.61 ?  649 ASP B CG    1 
ATOM   10779 O  OD1   . ASP B 1 649 ? 122.168 152.393 160.382 1.00 20.43 ?  649 ASP B OD1   1 
ATOM   10780 O  OD2   . ASP B 1 649 ? 122.127 151.882 158.254 1.00 28.60 -1 649 ASP B OD2   1 
ATOM   10781 N  N     . GLN B 1 650 ? 120.653 149.211 158.158 1.00 10.05 ?  650 GLN B N     1 
ATOM   10782 C  CA    . GLN B 1 650 ? 120.806 148.232 157.093 1.00 2.07  ?  650 GLN B CA    1 
ATOM   10783 C  C     . GLN B 1 650 ? 120.342 146.872 157.613 1.00 5.15  ?  650 GLN B C     1 
ATOM   10784 O  O     . GLN B 1 650 ? 119.674 146.787 158.646 1.00 22.73 ?  650 GLN B O     1 
ATOM   10785 C  CB    . GLN B 1 650 ? 122.249 148.224 156.589 1.00 9.86  ?  650 GLN B CB    1 
ATOM   10786 C  CG    . GLN B 1 650 ? 122.698 149.544 156.009 1.00 8.84  ?  650 GLN B CG    1 
ATOM   10787 C  CD    . GLN B 1 650 ? 124.063 149.458 155.379 1.00 14.00 ?  650 GLN B CD    1 
ATOM   10788 O  OE1   . GLN B 1 650 ? 124.239 148.822 154.343 1.00 17.40 ?  650 GLN B OE1   1 
ATOM   10789 N  NE2   . GLN B 1 650 ? 125.043 150.105 155.997 1.00 8.23  ?  650 GLN B NE2   1 
ATOM   10790 N  N     . GLY B 1 651 ? 120.657 145.796 156.896 1.00 12.16 ?  651 GLY B N     1 
ATOM   10791 C  CA    . GLY B 1 651 ? 120.221 144.475 157.288 1.00 13.22 ?  651 GLY B CA    1 
ATOM   10792 C  C     . GLY B 1 651 ? 121.225 143.743 158.160 1.00 7.23  ?  651 GLY B C     1 
ATOM   10793 O  O     . GLY B 1 651 ? 122.265 144.265 158.553 1.00 12.16 ?  651 GLY B O     1 
ATOM   10794 N  N     . ILE B 1 652 ? 120.876 142.497 158.468 1.00 20.05 ?  652 ILE B N     1 
ATOM   10795 C  CA    . ILE B 1 652 ? 121.693 141.600 159.272 1.00 4.72  ?  652 ILE B CA    1 
ATOM   10796 C  C     . ILE B 1 652 ? 121.828 140.288 158.515 1.00 13.37 ?  652 ILE B C     1 
ATOM   10797 O  O     . ILE B 1 652 ? 120.839 139.772 157.985 1.00 24.03 ?  652 ILE B O     1 
ATOM   10798 C  CB    . ILE B 1 652 ? 121.079 141.354 160.665 1.00 2.58  ?  652 ILE B CB    1 
ATOM   10799 C  CG1   . ILE B 1 652 ? 120.875 142.671 161.411 1.00 3.36  ?  652 ILE B CG1   1 
ATOM   10800 C  CG2   . ILE B 1 652 ? 121.938 140.400 161.475 1.00 7.53  ?  652 ILE B CG2   1 
ATOM   10801 C  CD1   . ILE B 1 652 ? 120.093 142.520 162.688 1.00 8.68  ?  652 ILE B CD1   1 
ATOM   10802 N  N     . SER B 1 653 ? 123.042 139.753 158.458 1.00 14.90 ?  653 SER B N     1 
ATOM   10803 C  CA    . SER B 1 653 ? 123.272 138.456 157.828 1.00 13.87 ?  653 SER B CA    1 
ATOM   10804 C  C     . SER B 1 653 ? 122.639 137.378 158.696 1.00 20.31 ?  653 SER B C     1 
ATOM   10805 O  O     . SER B 1 653 ? 123.198 136.972 159.717 1.00 26.45 ?  653 SER B O     1 
ATOM   10806 C  CB    . SER B 1 653 ? 124.763 138.211 157.637 1.00 16.66 ?  653 SER B CB    1 
ATOM   10807 O  OG    . SER B 1 653 ? 125.163 138.534 156.320 1.00 22.31 ?  653 SER B OG    1 
ATOM   10808 N  N     . PHE B 1 654 ? 121.464 136.909 158.290 1.00 23.30 ?  654 PHE B N     1 
ATOM   10809 C  CA    . PHE B 1 654 ? 120.656 135.985 159.077 1.00 6.98  ?  654 PHE B CA    1 
ATOM   10810 C  C     . PHE B 1 654 ? 120.723 134.605 158.434 1.00 18.15 ?  654 PHE B C     1 
ATOM   10811 O  O     . PHE B 1 654 ? 120.074 134.356 157.414 1.00 27.86 ?  654 PHE B O     1 
ATOM   10812 C  CB    . PHE B 1 654 ? 119.217 136.484 159.172 1.00 13.53 ?  654 PHE B CB    1 
ATOM   10813 C  CG    . PHE B 1 654 ? 118.351 135.686 160.104 1.00 17.85 ?  654 PHE B CG    1 
ATOM   10814 C  CD1   . PHE B 1 654 ? 118.907 134.804 161.013 1.00 21.93 ?  654 PHE B CD1   1 
ATOM   10815 C  CD2   . PHE B 1 654 ? 116.978 135.826 160.073 1.00 20.97 ?  654 PHE B CD2   1 
ATOM   10816 C  CE1   . PHE B 1 654 ? 118.113 134.074 161.865 1.00 18.47 ?  654 PHE B CE1   1 
ATOM   10817 C  CE2   . PHE B 1 654 ? 116.179 135.100 160.926 1.00 24.46 ?  654 PHE B CE2   1 
ATOM   10818 C  CZ    . PHE B 1 654 ? 116.748 134.223 161.823 1.00 16.24 ?  654 PHE B CZ    1 
ATOM   10819 N  N     . THR B 1 655 ? 121.490 133.709 159.046 1.00 22.48 ?  655 THR B N     1 
ATOM   10820 C  CA    . THR B 1 655 ? 121.611 132.337 158.578 1.00 19.91 ?  655 THR B CA    1 
ATOM   10821 C  C     . THR B 1 655 ? 120.587 131.461 159.288 1.00 20.63 ?  655 THR B C     1 
ATOM   10822 O  O     . THR B 1 655 ? 120.460 131.515 160.515 1.00 29.03 ?  655 THR B O     1 
ATOM   10823 C  CB    . THR B 1 655 ? 123.023 131.806 158.826 1.00 29.28 ?  655 THR B CB    1 
ATOM   10824 O  OG1   . THR B 1 655 ? 123.962 132.564 158.054 1.00 35.51 ?  655 THR B OG1   1 
ATOM   10825 C  CG2   . THR B 1 655 ? 123.125 130.341 158.435 1.00 29.23 ?  655 THR B CG2   1 
ATOM   10826 N  N     . LEU B 1 656 ? 119.854 130.666 158.516 1.00 31.41 ?  656 LEU B N     1 
ATOM   10827 C  CA    . LEU B 1 656 ? 118.933 129.686 159.070 1.00 31.82 ?  656 LEU B CA    1 
ATOM   10828 C  C     . LEU B 1 656 ? 119.682 128.390 159.341 1.00 28.18 ?  656 LEU B C     1 
ATOM   10829 O  O     . LEU B 1 656 ? 120.348 127.854 158.452 1.00 33.03 ?  656 LEU B O     1 
ATOM   10830 C  CB    . LEU B 1 656 ? 117.766 129.430 158.117 1.00 34.25 ?  656 LEU B CB    1 
ATOM   10831 C  CG    . LEU B 1 656 ? 116.858 130.617 157.807 1.00 34.34 ?  656 LEU B CG    1 
ATOM   10832 C  CD1   . LEU B 1 656 ? 115.602 130.147 157.091 1.00 29.57 ?  656 LEU B CD1   1 
ATOM   10833 C  CD2   . LEU B 1 656 ? 116.509 131.378 159.075 1.00 25.37 ?  656 LEU B CD2   1 
ATOM   10834 N  N     . PHE B 1 657 ? 119.574 127.896 160.566 1.00 30.01 ?  657 PHE B N     1 
ATOM   10835 C  CA    . PHE B 1 657 ? 120.220 126.657 160.980 1.00 27.17 ?  657 PHE B CA    1 
ATOM   10836 C  C     . PHE B 1 657 ? 119.136 125.603 161.140 1.00 36.86 ?  657 PHE B C     1 
ATOM   10837 O  O     . PHE B 1 657 ? 118.320 125.677 162.064 1.00 39.95 ?  657 PHE B O     1 
ATOM   10838 C  CB    . PHE B 1 657 ? 121.005 126.861 162.271 1.00 31.39 ?  657 PHE B CB    1 
ATOM   10839 C  CG    . PHE B 1 657 ? 121.995 127.984 162.200 1.00 38.03 ?  657 PHE B CG    1 
ATOM   10840 C  CD1   . PHE B 1 657 ? 123.259 127.776 161.678 1.00 32.64 ?  657 PHE B CD1   1 
ATOM   10841 C  CD2   . PHE B 1 657 ? 121.660 129.250 162.648 1.00 35.57 ?  657 PHE B CD2   1 
ATOM   10842 C  CE1   . PHE B 1 657 ? 124.171 128.806 161.608 1.00 34.17 ?  657 PHE B CE1   1 
ATOM   10843 C  CE2   . PHE B 1 657 ? 122.569 130.284 162.580 1.00 34.07 ?  657 PHE B CE2   1 
ATOM   10844 C  CZ    . PHE B 1 657 ? 123.826 130.062 162.060 1.00 38.39 ?  657 PHE B CZ    1 
ATOM   10845 N  N     . LEU B 1 658 ? 119.130 124.625 160.241 1.00 40.65 ?  658 LEU B N     1 
ATOM   10846 C  CA    . LEU B 1 658 ? 118.055 123.653 160.144 1.00 41.19 ?  658 LEU B CA    1 
ATOM   10847 C  C     . LEU B 1 658 ? 118.575 122.254 160.437 1.00 45.56 ?  658 LEU B C     1 
ATOM   10848 O  O     . LEU B 1 658 ? 119.741 121.939 160.184 1.00 48.21 ?  658 LEU B O     1 
ATOM   10849 C  CB    . LEU B 1 658 ? 117.418 123.679 158.751 1.00 41.13 ?  658 LEU B CB    1 
ATOM   10850 C  CG    . LEU B 1 658 ? 117.297 125.055 158.098 1.00 40.87 ?  658 LEU B CG    1 
ATOM   10851 C  CD1   . LEU B 1 658 ? 117.204 124.917 156.592 1.00 38.06 ?  658 LEU B CD1   1 
ATOM   10852 C  CD2   . LEU B 1 658 ? 116.096 125.805 158.647 1.00 41.11 ?  658 LEU B CD2   1 
ATOM   10853 N  N     . LYS B 1 659 ? 117.700 121.422 160.986 1.00 49.14 ?  659 LYS B N     1 
ATOM   10854 C  CA    . LYS B 1 659 ? 117.989 120.009 161.154 1.00 50.62 ?  659 LYS B CA    1 
ATOM   10855 C  C     . LYS B 1 659 ? 117.659 119.253 159.871 1.00 52.29 ?  659 LYS B C     1 
ATOM   10856 O  O     . LYS B 1 659 ? 116.953 119.751 158.992 1.00 52.44 ?  659 LYS B O     1 
ATOM   10857 C  CB    . LYS B 1 659 ? 117.200 119.431 162.329 1.00 49.58 ?  659 LYS B CB    1 
ATOM   10858 C  CG    . LYS B 1 659 ? 117.564 120.040 163.669 1.00 52.09 ?  659 LYS B CG    1 
ATOM   10859 C  CD    . LYS B 1 659 ? 117.014 119.221 164.822 1.00 52.73 ?  659 LYS B CD    1 
ATOM   10860 C  CE    . LYS B 1 659 ? 117.464 119.786 166.160 1.00 51.17 ?  659 LYS B CE    1 
ATOM   10861 N  NZ    . LYS B 1 659 ? 117.310 118.800 167.265 1.00 53.28 1  659 LYS B NZ    1 
ATOM   10862 N  N     . ASP B 1 660 ? 118.194 118.035 159.769 1.00 57.27 ?  660 ASP B N     1 
ATOM   10863 C  CA    . ASP B 1 660 ? 117.891 117.201 158.611 1.00 56.83 ?  660 ASP B CA    1 
ATOM   10864 C  C     . ASP B 1 660 ? 116.429 116.773 158.597 1.00 55.41 ?  660 ASP B C     1 
ATOM   10865 O  O     . ASP B 1 660 ? 115.868 116.523 157.525 1.00 55.37 ?  660 ASP B O     1 
ATOM   10866 C  CB    . ASP B 1 660 ? 118.804 115.975 158.589 1.00 57.50 ?  660 ASP B CB    1 
ATOM   10867 C  CG    . ASP B 1 660 ? 118.776 115.200 159.893 1.00 58.83 ?  660 ASP B CG    1 
ATOM   10868 O  OD1   . ASP B 1 660 ? 118.326 115.762 160.914 1.00 57.20 ?  660 ASP B OD1   1 
ATOM   10869 O  OD2   . ASP B 1 660 ? 119.205 114.026 159.897 1.00 59.06 -1 660 ASP B OD2   1 
ATOM   10870 N  N     . THR B 1 661 ? 115.800 116.687 159.770 1.00 52.39 ?  661 THR B N     1 
ATOM   10871 C  CA    . THR B 1 661 ? 114.405 116.279 159.854 1.00 53.63 ?  661 THR B CA    1 
ATOM   10872 C  C     . THR B 1 661 ? 113.439 117.373 159.423 1.00 56.03 ?  661 THR B C     1 
ATOM   10873 O  O     . THR B 1 661 ? 112.268 117.076 159.160 1.00 54.76 ?  661 THR B O     1 
ATOM   10874 C  CB    . THR B 1 661 ? 114.071 115.843 161.282 1.00 54.73 ?  661 THR B CB    1 
ATOM   10875 O  OG1   . THR B 1 661 ? 114.349 116.919 162.186 1.00 52.56 ?  661 THR B OG1   1 
ATOM   10876 C  CG2   . THR B 1 661 ? 114.902 114.633 161.673 1.00 54.63 ?  661 THR B CG2   1 
ATOM   10877 N  N     . MET B 1 662 ? 113.893 118.620 159.348 1.00 55.39 ?  662 MET B N     1 
ATOM   10878 C  CA    . MET B 1 662 ? 113.011 119.714 158.971 1.00 51.19 ?  662 MET B CA    1 
ATOM   10879 C  C     . MET B 1 662 ? 112.594 119.587 157.511 1.00 52.53 ?  662 MET B C     1 
ATOM   10880 O  O     . MET B 1 662 ? 113.410 119.279 156.638 1.00 53.26 ?  662 MET B O     1 
ATOM   10881 C  CB    . MET B 1 662 ? 113.697 121.056 159.214 1.00 51.81 ?  662 MET B CB    1 
ATOM   10882 C  CG    . MET B 1 662 ? 113.314 121.707 160.531 1.00 51.85 ?  662 MET B CG    1 
ATOM   10883 S  SD    . MET B 1 662 ? 114.329 123.139 160.934 1.00 60.76 ?  662 MET B SD    1 
ATOM   10884 C  CE    . MET B 1 662 ? 113.237 124.020 162.046 1.00 51.82 ?  662 MET B CE    1 
ATOM   10885 N  N     . THR B 1 663 ? 111.312 119.827 157.252 1.00 48.30 ?  663 THR B N     1 
ATOM   10886 C  CA    . THR B 1 663 ? 110.751 119.676 155.921 1.00 45.04 ?  663 THR B CA    1 
ATOM   10887 C  C     . THR B 1 663 ? 110.808 121.001 155.164 1.00 46.54 ?  663 THR B C     1 
ATOM   10888 O  O     . THR B 1 663 ? 111.298 122.018 155.660 1.00 49.48 ?  663 THR B O     1 
ATOM   10889 C  CB    . THR B 1 663 ? 109.312 119.170 156.004 1.00 41.89 ?  663 THR B CB    1 
ATOM   10890 O  OG1   . THR B 1 663 ? 108.643 119.806 157.100 1.00 42.37 ?  663 THR B OG1   1 
ATOM   10891 C  CG2   . THR B 1 663 ? 109.288 117.667 156.219 1.00 44.20 ?  663 THR B CG2   1 
ATOM   10892 N  N     . THR B 1 664 ? 110.300 120.981 153.930 1.00 41.28 ?  664 THR B N     1 
ATOM   10893 C  CA    . THR B 1 664 ? 110.131 122.217 153.174 1.00 38.99 ?  664 THR B CA    1 
ATOM   10894 C  C     . THR B 1 664 ? 109.136 123.143 153.864 1.00 38.44 ?  664 THR B C     1 
ATOM   10895 O  O     . THR B 1 664 ? 109.331 124.365 153.901 1.00 41.92 ?  664 THR B O     1 
ATOM   10896 C  CB    . THR B 1 664 ? 109.683 121.888 151.746 1.00 41.98 ?  664 THR B CB    1 
ATOM   10897 O  OG1   . THR B 1 664 ? 110.817 121.477 150.971 1.00 40.54 ?  664 THR B OG1   1 
ATOM   10898 C  CG2   . THR B 1 664 ? 109.018 123.080 151.079 1.00 41.48 ?  664 THR B CG2   1 
ATOM   10899 N  N     . ARG B 1 665 ? 108.073 122.573 154.435 1.00 39.22 ?  665 ARG B N     1 
ATOM   10900 C  CA    . ARG B 1 665 ? 107.077 123.381 155.128 1.00 38.75 ?  665 ARG B CA    1 
ATOM   10901 C  C     . ARG B 1 665 ? 107.680 124.101 156.325 1.00 41.96 ?  665 ARG B C     1 
ATOM   10902 O  O     . ARG B 1 665 ? 107.310 125.240 156.618 1.00 47.88 ?  665 ARG B O     1 
ATOM   10903 C  CB    . ARG B 1 665 ? 105.904 122.507 155.570 1.00 40.49 ?  665 ARG B CB    1 
ATOM   10904 C  CG    . ARG B 1 665 ? 104.624 123.281 155.828 1.00 37.78 ?  665 ARG B CG    1 
ATOM   10905 C  CD    . ARG B 1 665 ? 103.699 122.518 156.756 1.00 41.85 ?  665 ARG B CD    1 
ATOM   10906 N  NE    . ARG B 1 665 ? 103.988 122.791 158.158 1.00 46.72 ?  665 ARG B NE    1 
ATOM   10907 C  CZ    . ARG B 1 665 ? 103.178 122.489 159.163 1.00 48.71 ?  665 ARG B CZ    1 
ATOM   10908 N  NH1   . ARG B 1 665 ? 102.016 121.892 158.959 1.00 43.92 1  665 ARG B NH1   1 
ATOM   10909 N  NH2   . ARG B 1 665 ? 103.545 122.795 160.405 1.00 46.34 ?  665 ARG B NH2   1 
ATOM   10910 N  N     . ASP B 1 666 ? 108.608 123.454 157.034 1.00 39.87 ?  666 ASP B N     1 
ATOM   10911 C  CA    . ASP B 1 666 ? 109.231 124.100 158.186 1.00 35.12 ?  666 ASP B CA    1 
ATOM   10912 C  C     . ASP B 1 666 ? 110.101 125.278 157.763 1.00 40.01 ?  666 ASP B C     1 
ATOM   10913 O  O     . ASP B 1 666 ? 110.078 126.336 158.404 1.00 42.48 ?  666 ASP B O     1 
ATOM   10914 C  CB    . ASP B 1 666 ? 110.049 123.081 158.977 1.00 42.29 ?  666 ASP B CB    1 
ATOM   10915 C  CG    . ASP B 1 666 ? 109.189 122.000 159.593 1.00 49.42 ?  666 ASP B CG    1 
ATOM   10916 O  OD1   . ASP B 1 666 ? 108.074 122.320 160.054 1.00 46.16 ?  666 ASP B OD1   1 
ATOM   10917 O  OD2   . ASP B 1 666 ? 109.626 120.831 159.619 1.00 50.89 -1 666 ASP B OD2   1 
ATOM   10918 N  N     . LEU B 1 667 ? 110.872 125.119 156.685 1.00 35.25 ?  667 LEU B N     1 
ATOM   10919 C  CA    . LEU B 1 667 ? 111.670 126.231 156.179 1.00 28.35 ?  667 LEU B CA    1 
ATOM   10920 C  C     . LEU B 1 667 ? 110.776 127.373 155.714 1.00 30.94 ?  667 LEU B C     1 
ATOM   10921 O  O     . LEU B 1 667 ? 111.068 128.548 155.969 1.00 32.33 ?  667 LEU B O     1 
ATOM   10922 C  CB    . LEU B 1 667 ? 112.571 125.753 155.042 1.00 31.84 ?  667 LEU B CB    1 
ATOM   10923 C  CG    . LEU B 1 667 ? 113.975 126.355 154.927 1.00 33.11 ?  667 LEU B CG    1 
ATOM   10924 C  CD1   . LEU B 1 667 ? 114.777 125.604 153.882 1.00 33.42 ?  667 LEU B CD1   1 
ATOM   10925 C  CD2   . LEU B 1 667 ? 113.932 127.834 154.594 1.00 38.02 ?  667 LEU B CD2   1 
ATOM   10926 N  N     . ASN B 1 668 ? 109.677 127.046 155.031 1.00 36.62 ?  668 ASN B N     1 
ATOM   10927 C  CA    . ASN B 1 668 ? 108.738 128.077 154.605 1.00 23.50 ?  668 ASN B CA    1 
ATOM   10928 C  C     . ASN B 1 668 ? 108.117 128.786 155.800 1.00 22.91 ?  668 ASN B C     1 
ATOM   10929 O  O     . ASN B 1 668 ? 107.914 130.004 155.772 1.00 31.40 ?  668 ASN B O     1 
ATOM   10930 C  CB    . ASN B 1 668 ? 107.654 127.466 153.721 1.00 28.51 ?  668 ASN B CB    1 
ATOM   10931 C  CG    . ASN B 1 668 ? 108.077 127.361 152.274 1.00 33.12 ?  668 ASN B CG    1 
ATOM   10932 O  OD1   . ASN B 1 668 ? 107.771 126.381 151.596 1.00 40.18 ?  668 ASN B OD1   1 
ATOM   10933 N  ND2   . ASN B 1 668 ? 108.788 128.372 151.791 1.00 30.35 ?  668 ASN B ND2   1 
ATOM   10934 N  N     . ARG B 1 669 ? 107.795 128.038 156.856 1.00 31.32 ?  669 ARG B N     1 
ATOM   10935 C  CA    . ARG B 1 669 ? 107.249 128.647 158.062 1.00 32.98 ?  669 ARG B CA    1 
ATOM   10936 C  C     . ARG B 1 669 ? 108.255 129.591 158.703 1.00 29.08 ?  669 ARG B C     1 
ATOM   10937 O  O     . ARG B 1 669 ? 107.889 130.675 159.168 1.00 28.03 ?  669 ARG B O     1 
ATOM   10938 C  CB    . ARG B 1 669 ? 106.827 127.563 159.052 1.00 32.09 ?  669 ARG B CB    1 
ATOM   10939 C  CG    . ARG B 1 669 ? 105.331 127.354 159.133 1.00 28.78 ?  669 ARG B CG    1 
ATOM   10940 C  CD    . ARG B 1 669 ? 104.971 126.376 160.238 1.00 33.13 ?  669 ARG B CD    1 
ATOM   10941 N  NE    . ARG B 1 669 ? 104.953 127.003 161.555 1.00 35.06 ?  669 ARG B NE    1 
ATOM   10942 C  CZ    . ARG B 1 669 ? 104.063 127.902 161.952 1.00 36.71 ?  669 ARG B CZ    1 
ATOM   10943 N  NH1   . ARG B 1 669 ? 103.084 128.305 161.159 1.00 35.18 1  669 ARG B NH1   1 
ATOM   10944 N  NH2   . ARG B 1 669 ? 104.153 128.406 163.179 1.00 38.29 ?  669 ARG B NH2   1 
ATOM   10945 N  N     . ILE B 1 670 ? 109.529 129.193 158.741 1.00 25.86 ?  670 ILE B N     1 
ATOM   10946 C  CA    . ILE B 1 670 ? 110.561 130.074 159.283 1.00 25.29 ?  670 ILE B CA    1 
ATOM   10947 C  C     . ILE B 1 670 ? 110.667 131.345 158.449 1.00 24.13 ?  670 ILE B C     1 
ATOM   10948 O  O     . ILE B 1 670 ? 110.756 132.453 158.992 1.00 27.90 ?  670 ILE B O     1 
ATOM   10949 C  CB    . ILE B 1 670 ? 111.910 129.338 159.369 1.00 32.05 ?  670 ILE B CB    1 
ATOM   10950 C  CG1   . ILE B 1 670 ? 111.827 128.175 160.356 1.00 31.60 ?  670 ILE B CG1   1 
ATOM   10951 C  CG2   . ILE B 1 670 ? 113.013 130.296 159.784 1.00 28.90 ?  670 ILE B CG2   1 
ATOM   10952 C  CD1   . ILE B 1 670 ? 112.839 127.087 160.093 1.00 27.50 ?  670 ILE B CD1   1 
ATOM   10953 N  N     . ASP B 1 671 ? 110.651 131.208 157.121 1.00 25.07 ?  671 ASP B N     1 
ATOM   10954 C  CA    . ASP B 1 671 ? 110.734 132.381 156.253 1.00 20.62 ?  671 ASP B CA    1 
ATOM   10955 C  C     . ASP B 1 671 ? 109.535 133.304 156.443 1.00 21.54 ?  671 ASP B C     1 
ATOM   10956 O  O     . ASP B 1 671 ? 109.686 134.530 156.490 1.00 30.77 ?  671 ASP B O     1 
ATOM   10957 C  CB    . ASP B 1 671 ? 110.848 131.950 154.791 1.00 21.88 ?  671 ASP B CB    1 
ATOM   10958 C  CG    . ASP B 1 671 ? 112.040 131.050 154.538 1.00 40.20 ?  671 ASP B CG    1 
ATOM   10959 O  OD1   . ASP B 1 671 ? 112.979 131.058 155.361 1.00 39.79 ?  671 ASP B OD1   1 
ATOM   10960 O  OD2   . ASP B 1 671 ? 112.039 130.332 153.516 1.00 39.34 -1 671 ASP B OD2   1 
ATOM   10961 N  N     . LEU B 1 672 ? 108.336 132.734 156.560 1.00 21.76 ?  672 LEU B N     1 
ATOM   10962 C  CA    . LEU B 1 672 ? 107.137 133.549 156.715 1.00 16.89 ?  672 LEU B CA    1 
ATOM   10963 C  C     . LEU B 1 672 ? 107.074 134.207 158.085 1.00 18.59 ?  672 LEU B C     1 
ATOM   10964 O  O     . LEU B 1 672 ? 106.556 135.321 158.210 1.00 24.78 ?  672 LEU B O     1 
ATOM   10965 C  CB    . LEU B 1 672 ? 105.890 132.703 156.473 1.00 24.55 ?  672 LEU B CB    1 
ATOM   10966 C  CG    . LEU B 1 672 ? 105.713 132.190 155.044 1.00 24.78 ?  672 LEU B CG    1 
ATOM   10967 C  CD1   . LEU B 1 672 ? 104.720 131.041 155.007 1.00 20.61 ?  672 LEU B CD1   1 
ATOM   10968 C  CD2   . LEU B 1 672 ? 105.283 133.315 154.118 1.00 23.39 ?  672 LEU B CD2   1 
ATOM   10969 N  N     . TYR B 1 673 ? 107.583 133.543 159.123 1.00 22.69 ?  673 TYR B N     1 
ATOM   10970 C  CA    . TYR B 1 673 ? 107.643 134.174 160.436 1.00 14.92 ?  673 TYR B CA    1 
ATOM   10971 C  C     . TYR B 1 673 ? 108.694 135.275 160.466 1.00 18.79 ?  673 TYR B C     1 
ATOM   10972 O  O     . TYR B 1 673 ? 108.514 136.295 161.140 1.00 25.74 ?  673 TYR B O     1 
ATOM   10973 C  CB    . TYR B 1 673 ? 107.929 133.131 161.513 1.00 19.00 ?  673 TYR B CB    1 
ATOM   10974 C  CG    . TYR B 1 673 ? 107.971 133.706 162.908 1.00 20.29 ?  673 TYR B CG    1 
ATOM   10975 C  CD1   . TYR B 1 673 ? 106.845 134.280 163.476 1.00 22.11 ?  673 TYR B CD1   1 
ATOM   10976 C  CD2   . TYR B 1 673 ? 109.138 133.673 163.656 1.00 15.22 ?  673 TYR B CD2   1 
ATOM   10977 C  CE1   . TYR B 1 673 ? 106.878 134.805 164.749 1.00 20.83 ?  673 TYR B CE1   1 
ATOM   10978 C  CE2   . TYR B 1 673 ? 109.182 134.196 164.929 1.00 24.30 ?  673 TYR B CE2   1 
ATOM   10979 C  CZ    . TYR B 1 673 ? 108.050 134.759 165.472 1.00 25.45 ?  673 TYR B CZ    1 
ATOM   10980 O  OH    . TYR B 1 673 ? 108.091 135.282 166.742 1.00 29.84 ?  673 TYR B OH    1 
ATOM   10981 N  N     . ALA B 1 674 ? 109.804 135.080 159.752 1.00 21.72 ?  674 ALA B N     1 
ATOM   10982 C  CA    . ALA B 1 674 ? 110.785 136.148 159.609 1.00 12.28 ?  674 ALA B CA    1 
ATOM   10983 C  C     . ALA B 1 674 ? 110.178 137.350 158.899 1.00 17.86 ?  674 ALA B C     1 
ATOM   10984 O  O     . ALA B 1 674 ? 110.369 138.494 159.324 1.00 30.35 ?  674 ALA B O     1 
ATOM   10985 C  CB    . ALA B 1 674 ? 112.009 135.632 158.854 1.00 10.16 ?  674 ALA B CB    1 
ATOM   10986 N  N     . HIS B 1 675 ? 109.427 137.106 157.826 1.00 15.42 ?  675 HIS B N     1 
ATOM   10987 C  CA    . HIS B 1 675 ? 108.732 138.192 157.143 1.00 16.56 ?  675 HIS B CA    1 
ATOM   10988 C  C     . HIS B 1 675 ? 107.733 138.875 158.070 1.00 21.20 ?  675 HIS B C     1 
ATOM   10989 O  O     . HIS B 1 675 ? 107.608 140.104 158.065 1.00 26.90 ?  675 HIS B O     1 
ATOM   10990 C  CB    . HIS B 1 675 ? 108.031 137.658 155.896 1.00 18.38 ?  675 HIS B CB    1 
ATOM   10991 C  CG    . HIS B 1 675 ? 107.159 138.666 155.217 1.00 21.58 ?  675 HIS B CG    1 
ATOM   10992 N  ND1   . HIS B 1 675 ? 105.812 138.784 155.484 1.00 27.58 ?  675 HIS B ND1   1 
ATOM   10993 C  CD2   . HIS B 1 675 ? 107.440 139.606 154.285 1.00 15.77 ?  675 HIS B CD2   1 
ATOM   10994 C  CE1   . HIS B 1 675 ? 105.302 139.753 154.747 1.00 25.50 ?  675 HIS B CE1   1 
ATOM   10995 N  NE2   . HIS B 1 675 ? 106.269 140.267 154.009 1.00 29.27 ?  675 HIS B NE2   1 
ATOM   10996 N  N     . HIS B 1 676 ? 107.012 138.090 158.870 1.00 22.09 ?  676 HIS B N     1 
ATOM   10997 C  CA    . HIS B 1 676 ? 106.022 138.648 159.785 1.00 20.05 ?  676 HIS B CA    1 
ATOM   10998 C  C     . HIS B 1 676 ? 106.677 139.498 160.867 1.00 26.00 ?  676 HIS B C     1 
ATOM   10999 O  O     . HIS B 1 676 ? 106.124 140.522 161.279 1.00 25.33 ?  676 HIS B O     1 
ATOM   11000 C  CB    . HIS B 1 676 ? 105.204 137.519 160.410 1.00 24.17 ?  676 HIS B CB    1 
ATOM   11001 C  CG    . HIS B 1 676 ? 104.287 137.968 161.505 1.00 22.97 ?  676 HIS B CG    1 
ATOM   11002 N  ND1   . HIS B 1 676 ? 103.242 138.842 161.290 1.00 21.33 ?  676 HIS B ND1   1 
ATOM   11003 C  CD2   . HIS B 1 676 ? 104.257 137.664 162.823 1.00 25.21 ?  676 HIS B CD2   1 
ATOM   11004 C  CE1   . HIS B 1 676 ? 102.609 139.055 162.428 1.00 28.69 ?  676 HIS B CE1   1 
ATOM   11005 N  NE2   . HIS B 1 676 ? 103.205 138.353 163.374 1.00 27.27 ?  676 HIS B NE2   1 
ATOM   11006 N  N     . ARG B 1 677 ? 107.852 139.090 161.336 1.00 24.54 ?  677 ARG B N     1 
ATOM   11007 C  CA    . ARG B 1 677 ? 108.525 139.757 162.441 1.00 19.48 ?  677 ARG B CA    1 
ATOM   11008 C  C     . ARG B 1 677 ? 109.373 140.941 161.999 1.00 23.24 ?  677 ARG B C     1 
ATOM   11009 O  O     . ARG B 1 677 ? 110.021 141.567 162.843 1.00 30.96 ?  677 ARG B O     1 
ATOM   11010 C  CB    . ARG B 1 677 ? 109.396 138.757 163.203 1.00 19.00 ?  677 ARG B CB    1 
ATOM   11011 C  CG    . ARG B 1 677 ? 108.628 137.900 164.185 1.00 19.85 ?  677 ARG B CG    1 
ATOM   11012 C  CD    . ARG B 1 677 ? 108.101 138.727 165.341 1.00 23.48 ?  677 ARG B CD    1 
ATOM   11013 N  NE    . ARG B 1 677 ? 109.109 138.905 166.378 1.00 30.10 ?  677 ARG B NE    1 
ATOM   11014 C  CZ    . ARG B 1 677 ? 109.543 140.082 166.804 1.00 34.53 ?  677 ARG B CZ    1 
ATOM   11015 N  NH1   . ARG B 1 677 ? 109.076 141.213 166.302 1.00 29.29 1  677 ARG B NH1   1 
ATOM   11016 N  NH2   . ARG B 1 677 ? 110.472 140.127 167.754 1.00 29.06 ?  677 ARG B NH2   1 
ATOM   11017 N  N     . GLY B 1 678 ? 109.388 141.262 160.710 1.00 22.05 ?  678 GLY B N     1 
ATOM   11018 C  CA    . GLY B 1 678 ? 110.148 142.390 160.223 1.00 12.98 ?  678 GLY B CA    1 
ATOM   11019 C  C     . GLY B 1 678 ? 111.562 142.083 159.793 1.00 16.33 ?  678 GLY B C     1 
ATOM   11020 O  O     . GLY B 1 678 ? 112.357 143.016 159.634 1.00 24.40 ?  678 GLY B O     1 
ATOM   11021 N  N     . ILE B 1 679 ? 111.907 140.808 159.607 1.00 18.05 ?  679 ILE B N     1 
ATOM   11022 C  CA    . ILE B 1 679 ? 113.236 140.459 159.125 1.00 15.19 ?  679 ILE B CA    1 
ATOM   11023 C  C     . ILE B 1 679 ? 113.400 140.982 157.707 1.00 21.06 ?  679 ILE B C     1 
ATOM   11024 O  O     . ILE B 1 679 ? 112.515 140.817 156.859 1.00 28.13 ?  679 ILE B O     1 
ATOM   11025 C  CB    . ILE B 1 679 ? 113.452 138.941 159.202 1.00 13.44 ?  679 ILE B CB    1 
ATOM   11026 C  CG1   . ILE B 1 679 ? 113.517 138.481 160.661 1.00 13.99 ?  679 ILE B CG1   1 
ATOM   11027 C  CG2   . ILE B 1 679 ? 114.703 138.527 158.447 1.00 15.28 ?  679 ILE B CG2   1 
ATOM   11028 C  CD1   . ILE B 1 679 ? 114.647 139.083 161.435 1.00 18.66 ?  679 ILE B CD1   1 
ATOM   11029 N  N     . LYS B 1 680 ? 114.531 141.632 157.446 1.00 10.64 ?  680 LYS B N     1 
ATOM   11030 C  CA    . LYS B 1 680 ? 114.770 142.243 156.147 1.00 5.62  ?  680 LYS B CA    1 
ATOM   11031 C  C     . LYS B 1 680 ? 115.353 141.253 155.143 1.00 0.15  ?  680 LYS B C     1 
ATOM   11032 O  O     . LYS B 1 680 ? 114.906 141.195 153.996 1.00 19.15 ?  680 LYS B O     1 
ATOM   11033 C  CB    . LYS B 1 680 ? 115.701 143.446 156.300 1.00 11.81 ?  680 LYS B CB    1 
ATOM   11034 C  CG    . LYS B 1 680 ? 115.123 144.584 157.112 1.00 0.00  ?  680 LYS B CG    1 
ATOM   11035 C  CD    . LYS B 1 680 ? 116.051 145.781 157.089 1.00 2.10  ?  680 LYS B CD    1 
ATOM   11036 C  CE    . LYS B 1 680 ? 115.645 146.809 158.120 1.00 12.27 ?  680 LYS B CE    1 
ATOM   11037 N  NZ    . LYS B 1 680 ? 116.497 148.024 158.065 1.00 15.62 1  680 LYS B NZ    1 
ATOM   11038 N  N     . THR B 1 681 ? 116.352 140.481 155.555 1.00 6.84  ?  681 THR B N     1 
ATOM   11039 C  CA    . THR B 1 681 ? 117.008 139.534 154.667 1.00 7.07  ?  681 THR B CA    1 
ATOM   11040 C  C     . THR B 1 681 ? 117.237 138.222 155.400 1.00 12.62 ?  681 THR B C     1 
ATOM   11041 O  O     . THR B 1 681 ? 117.372 138.190 156.624 1.00 25.64 ?  681 THR B O     1 
ATOM   11042 C  CB    . THR B 1 681 ? 118.351 140.071 154.141 1.00 13.07 ?  681 THR B CB    1 
ATOM   11043 O  OG1   . THR B 1 681 ? 119.122 140.598 155.229 1.00 29.37 ?  681 THR B OG1   1 
ATOM   11044 C  CG2   . THR B 1 681 ? 118.136 141.162 153.109 1.00 7.92  ?  681 THR B CG2   1 
ATOM   11045 N  N     . ILE B 1 682 ? 117.278 137.136 154.634 1.00 13.30 ?  682 ILE B N     1 
ATOM   11046 C  CA    . ILE B 1 682 ? 117.658 135.822 155.135 1.00 8.69  ?  682 ILE B CA    1 
ATOM   11047 C  C     . ILE B 1 682 ? 118.863 135.349 154.335 1.00 17.51 ?  682 ILE B C     1 
ATOM   11048 O  O     . ILE B 1 682 ? 118.810 135.288 153.102 1.00 13.41 ?  682 ILE B O     1 
ATOM   11049 C  CB    . ILE B 1 682 ? 116.501 134.813 155.035 1.00 11.16 ?  682 ILE B CB    1 
ATOM   11050 C  CG1   . ILE B 1 682 ? 115.267 135.346 155.763 1.00 19.69 ?  682 ILE B CG1   1 
ATOM   11051 C  CG2   . ILE B 1 682 ? 116.918 133.489 155.625 1.00 18.50 ?  682 ILE B CG2   1 
ATOM   11052 C  CD1   . ILE B 1 682 ? 114.143 134.344 155.875 1.00 21.11 ?  682 ILE B CD1   1 
ATOM   11053 N  N     . TYR B 1 683 ? 119.948 135.021 155.036 1.00 23.45 ?  683 TYR B N     1 
ATOM   11054 C  CA    . TYR B 1 683 ? 121.215 134.744 154.360 1.00 18.72 ?  683 TYR B CA    1 
ATOM   11055 C  C     . TYR B 1 683 ? 121.292 133.310 153.846 1.00 21.31 ?  683 TYR B C     1 
ATOM   11056 O  O     . TYR B 1 683 ? 121.324 133.072 152.637 1.00 36.30 ?  683 TYR B O     1 
ATOM   11057 C  CB    . TYR B 1 683 ? 122.377 135.042 155.312 1.00 18.95 ?  683 TYR B CB    1 
ATOM   11058 C  CG    . TYR B 1 683 ? 123.741 135.014 154.667 1.00 13.76 ?  683 TYR B CG    1 
ATOM   11059 C  CD1   . TYR B 1 683 ? 123.890 135.218 153.303 1.00 10.60 ?  683 TYR B CD1   1 
ATOM   11060 C  CD2   . TYR B 1 683 ? 124.882 134.793 155.425 1.00 10.01 ?  683 TYR B CD2   1 
ATOM   11061 C  CE1   . TYR B 1 683 ? 125.132 135.196 152.714 1.00 19.38 ?  683 TYR B CE1   1 
ATOM   11062 C  CE2   . TYR B 1 683 ? 126.130 134.770 154.841 1.00 19.11 ?  683 TYR B CE2   1 
ATOM   11063 C  CZ    . TYR B 1 683 ? 126.249 134.974 153.485 1.00 21.30 ?  683 TYR B CZ    1 
ATOM   11064 O  OH    . TYR B 1 683 ? 127.490 134.953 152.894 1.00 23.65 ?  683 TYR B OH    1 
ATOM   11065 N  N     . TYR B 1 684 ? 121.297 132.339 154.750 1.00 29.13 ?  684 TYR B N     1 
ATOM   11066 C  CA    . TYR B 1 684 ? 121.638 130.978 154.374 1.00 22.22 ?  684 TYR B CA    1 
ATOM   11067 C  C     . TYR B 1 684 ? 120.729 129.999 155.093 1.00 37.02 ?  684 TYR B C     1 
ATOM   11068 O  O     . TYR B 1 684 ? 120.264 130.259 156.205 1.00 37.92 ?  684 TYR B O     1 
ATOM   11069 C  CB    . TYR B 1 684 ? 123.098 130.651 154.708 1.00 24.34 ?  684 TYR B CB    1 
ATOM   11070 C  CG    . TYR B 1 684 ? 124.048 130.782 153.545 1.00 25.68 ?  684 TYR B CG    1 
ATOM   11071 C  CD1   . TYR B 1 684 ? 123.681 130.366 152.274 1.00 26.99 ?  684 TYR B CD1   1 
ATOM   11072 C  CD2   . TYR B 1 684 ? 125.314 131.318 153.720 1.00 30.41 ?  684 TYR B CD2   1 
ATOM   11073 C  CE1   . TYR B 1 684 ? 124.550 130.484 151.208 1.00 33.90 ?  684 TYR B CE1   1 
ATOM   11074 C  CE2   . TYR B 1 684 ? 126.190 131.441 152.662 1.00 25.07 ?  684 TYR B CE2   1 
ATOM   11075 C  CZ    . TYR B 1 684 ? 125.803 131.023 151.409 1.00 30.64 ?  684 TYR B CZ    1 
ATOM   11076 O  OH    . TYR B 1 684 ? 126.673 131.143 150.351 1.00 35.44 ?  684 TYR B OH    1 
ATOM   11077 N  N     . ALA B 1 685 ? 120.487 128.869 154.443 1.00 37.12 ?  685 ALA B N     1 
ATOM   11078 C  CA    . ALA B 1 685 ? 119.797 127.736 155.045 1.00 33.67 ?  685 ALA B CA    1 
ATOM   11079 C  C     . ALA B 1 685 ? 120.851 126.653 155.257 1.00 34.24 ?  685 ALA B C     1 
ATOM   11080 O  O     . ALA B 1 685 ? 121.179 125.896 154.342 1.00 42.25 ?  685 ALA B O     1 
ATOM   11081 C  CB    . ALA B 1 685 ? 118.652 127.257 154.166 1.00 31.43 ?  685 ALA B CB    1 
ATOM   11082 N  N     . ARG B 1 686 ? 121.388 126.591 156.472 1.00 32.67 ?  686 ARG B N     1 
ATOM   11083 C  CA    . ARG B 1 686 ? 122.401 125.605 156.821 1.00 38.58 ?  686 ARG B CA    1 
ATOM   11084 C  C     . ARG B 1 686 ? 121.729 124.420 157.500 1.00 41.88 ?  686 ARG B C     1 
ATOM   11085 O  O     . ARG B 1 686 ? 121.075 124.581 158.536 1.00 42.46 ?  686 ARG B O     1 
ATOM   11086 C  CB    . ARG B 1 686 ? 123.463 126.218 157.731 1.00 40.04 ?  686 ARG B CB    1 
ATOM   11087 C  CG    . ARG B 1 686 ? 124.545 126.974 156.987 1.00 40.60 ?  686 ARG B CG    1 
ATOM   11088 C  CD    . ARG B 1 686 ? 125.799 127.113 157.831 1.00 44.30 ?  686 ARG B CD    1 
ATOM   11089 N  NE    . ARG B 1 686 ? 126.637 125.922 157.768 1.00 46.43 ?  686 ARG B NE    1 
ATOM   11090 C  CZ    . ARG B 1 686 ? 127.962 125.941 157.711 1.00 48.20 ?  686 ARG B CZ    1 
ATOM   11091 N  NH1   . ARG B 1 686 ? 128.635 127.079 157.688 1.00 43.79 1  686 ARG B NH1   1 
ATOM   11092 N  NH2   . ARG B 1 686 ? 128.626 124.790 157.672 1.00 47.81 ?  686 ARG B NH2   1 
ATOM   11093 N  N     . THR B 1 687 ? 121.890 123.236 156.920 1.00 46.89 ?  687 THR B N     1 
ATOM   11094 C  CA    . THR B 1 687 ? 121.267 122.021 157.420 1.00 50.40 ?  687 THR B CA    1 
ATOM   11095 C  C     . THR B 1 687 ? 122.315 121.126 158.066 1.00 49.85 ?  687 THR B C     1 
ATOM   11096 O  O     . THR B 1 687 ? 123.431 120.990 157.557 1.00 51.44 ?  687 THR B O     1 
ATOM   11097 C  CB    . THR B 1 687 ? 120.556 121.263 156.295 1.00 47.33 ?  687 THR B CB    1 
ATOM   11098 O  OG1   . THR B 1 687 ? 119.922 122.198 155.413 1.00 44.31 ?  687 THR B OG1   1 
ATOM   11099 C  CG2   . THR B 1 687 ? 119.507 120.326 156.865 1.00 45.39 ?  687 THR B CG2   1 
ATOM   11100 N  N     . LYS B 1 688 ? 121.950 120.523 159.193 1.00 47.38 ?  688 LYS B N     1 
ATOM   11101 C  CA    . LYS B 1 688 ? 122.847 119.620 159.903 1.00 49.75 ?  688 LYS B CA    1 
ATOM   11102 C  C     . LYS B 1 688 ? 122.652 118.182 159.437 1.00 54.70 ?  688 LYS B C     1 
ATOM   11103 O  O     . LYS B 1 688 ? 121.522 117.725 159.261 1.00 55.57 ?  688 LYS B O     1 
ATOM   11104 C  CB    . LYS B 1 688 ? 122.623 119.717 161.412 1.00 47.73 ?  688 LYS B CB    1 
ATOM   11105 C  CG    . LYS B 1 688 ? 123.695 119.031 162.239 1.00 49.97 ?  688 LYS B CG    1 
ATOM   11106 C  CD    . LYS B 1 688 ? 123.687 119.527 163.672 1.00 50.55 ?  688 LYS B CD    1 
ATOM   11107 C  CE    . LYS B 1 688 ? 124.893 119.015 164.440 1.00 52.82 ?  688 LYS B CE    1 
ATOM   11108 N  NZ    . LYS B 1 688 ? 124.951 119.580 165.816 1.00 54.26 ?  688 LYS B NZ    1 
ATOM   11109 N  N     . ASP C 2 37  ? 137.733 79.738  117.911 1.00 45.99 ?  16  ASP C N     1 
ATOM   11110 C  CA    . ASP C 2 37  ? 137.816 80.154  116.508 1.00 45.47 ?  16  ASP C CA    1 
ATOM   11111 C  C     . ASP C 2 37  ? 137.051 81.437  116.180 1.00 44.13 ?  16  ASP C C     1 
ATOM   11112 O  O     . ASP C 2 37  ? 137.130 81.932  115.054 1.00 44.46 ?  16  ASP C O     1 
ATOM   11113 C  CB    . ASP C 2 37  ? 137.316 79.026  115.603 1.00 45.90 ?  16  ASP C CB    1 
ATOM   11114 C  CG    . ASP C 2 37  ? 137.952 77.697  115.933 1.00 47.25 ?  16  ASP C CG    1 
ATOM   11115 O  OD1   . ASP C 2 37  ? 139.163 77.673  116.239 1.00 47.99 ?  16  ASP C OD1   1 
ATOM   11116 O  OD2   . ASP C 2 37  ? 137.235 76.676  115.889 1.00 49.50 -1 16  ASP C OD2   1 
ATOM   11117 N  N     . PHE C 2 38  ? 136.318 81.975  117.152 1.00 42.17 ?  17  PHE C N     1 
ATOM   11118 C  CA    . PHE C 2 38  ? 135.377 83.063  116.864 1.00 40.67 ?  17  PHE C CA    1 
ATOM   11119 C  C     . PHE C 2 38  ? 135.391 84.276  117.801 1.00 39.46 ?  17  PHE C C     1 
ATOM   11120 O  O     . PHE C 2 38  ? 134.978 85.365  117.396 1.00 39.17 ?  17  PHE C O     1 
ATOM   11121 C  CB    . PHE C 2 38  ? 133.946 82.507  116.743 1.00 40.24 ?  17  PHE C CB    1 
ATOM   11122 C  CG    . PHE C 2 38  ? 133.490 81.709  117.942 1.00 39.58 ?  17  PHE C CG    1 
ATOM   11123 C  CD1   . PHE C 2 38  ? 132.906 82.345  119.039 1.00 38.78 ?  17  PHE C CD1   1 
ATOM   11124 C  CD2   . PHE C 2 38  ? 133.631 80.321  117.970 1.00 39.43 ?  17  PHE C CD2   1 
ATOM   11125 C  CE1   . PHE C 2 38  ? 132.473 81.614  120.145 1.00 38.07 ?  17  PHE C CE1   1 
ATOM   11126 C  CE2   . PHE C 2 38  ? 133.201 79.579  119.075 1.00 39.10 ?  17  PHE C CE2   1 
ATOM   11127 C  CZ    . PHE C 2 38  ? 132.622 80.230  120.165 1.00 38.63 ?  17  PHE C CZ    1 
ATOM   11128 N  N     . THR C 2 39  ? 135.851 84.096  119.041 1.00 38.22 ?  18  THR C N     1 
ATOM   11129 C  CA    . THR C 2 39  ? 135.763 85.168  120.047 1.00 37.09 ?  18  THR C CA    1 
ATOM   11130 C  C     . THR C 2 39  ? 136.446 86.472  119.600 1.00 36.84 ?  18  THR C C     1 
ATOM   11131 O  O     . THR C 2 39  ? 135.865 87.560  119.741 1.00 36.13 ?  18  THR C O     1 
ATOM   11132 C  CB    . THR C 2 39  ? 136.223 84.711  121.462 1.00 36.59 ?  18  THR C CB    1 
ATOM   11133 O  OG1   . THR C 2 39  ? 135.217 83.869  122.031 1.00 36.50 ?  18  THR C OG1   1 
ATOM   11134 C  CG2   . THR C 2 39  ? 136.405 85.897  122.389 1.00 36.06 ?  18  THR C CG2   1 
ATOM   11135 N  N     . GLN C 2 40  ? 137.656 86.355  119.045 1.00 37.01 ?  19  GLN C N     1 
ATOM   11136 C  CA    . GLN C 2 40  ? 138.412 87.534  118.595 1.00 37.33 ?  19  GLN C CA    1 
ATOM   11137 C  C     . GLN C 2 40  ? 137.668 88.362  117.560 1.00 36.63 ?  19  GLN C C     1 
ATOM   11138 O  O     . GLN C 2 40  ? 137.656 89.589  117.640 1.00 36.10 ?  19  GLN C O     1 
ATOM   11139 C  CB    . GLN C 2 40  ? 139.798 87.162  118.069 1.00 38.24 ?  19  GLN C CB    1 
ATOM   11140 C  CG    . GLN C 2 40  ? 140.819 86.998  119.172 1.00 41.33 ?  19  GLN C CG    1 
ATOM   11141 C  CD    . GLN C 2 40  ? 142.205 87.471  118.778 1.00 45.15 ?  19  GLN C CD    1 
ATOM   11142 O  OE1   . GLN C 2 40  ? 142.615 87.353  117.617 1.00 47.33 ?  19  GLN C OE1   1 
ATOM   11143 N  NE2   . GLN C 2 40  ? 142.940 88.010  119.749 1.00 46.51 ?  19  GLN C NE2   1 
ATOM   11144 N  N     . MET C 2 41  ? 137.038 87.688  116.602 1.00 36.23 ?  20  MET C N     1 
ATOM   11145 C  CA    . MET C 2 41  ? 136.265 88.392  115.588 1.00 36.40 ?  20  MET C CA    1 
ATOM   11146 C  C     . MET C 2 41  ? 134.981 89.013  116.169 1.00 34.93 ?  20  MET C C     1 
ATOM   11147 O  O     . MET C 2 41  ? 134.578 90.095  115.749 1.00 34.20 ?  20  MET C O     1 
ATOM   11148 C  CB    . MET C 2 41  ? 136.040 87.527  114.328 1.00 37.35 ?  20  MET C CB    1 
ATOM   11149 C  CG    . MET C 2 41  ? 134.838 86.602  114.312 1.00 40.49 ?  20  MET C CG    1 
ATOM   11150 S  SD    . MET C 2 41  ? 134.631 85.850  112.667 1.00 48.68 ?  20  MET C SD    1 
ATOM   11151 C  CE    . MET C 2 41  ? 135.703 84.412  112.794 1.00 47.17 ?  20  MET C CE    1 
ATOM   11152 N  N     . PHE C 2 42  ? 134.376 88.357  117.163 1.00 33.75 ?  21  PHE C N     1 
ATOM   11153 C  CA    . PHE C 2 42  ? 133.246 88.961  117.884 1.00 32.62 ?  21  PHE C CA    1 
ATOM   11154 C  C     . PHE C 2 42  ? 133.678 90.142  118.745 1.00 32.59 ?  21  PHE C C     1 
ATOM   11155 O  O     . PHE C 2 42  ? 132.974 91.154  118.819 1.00 32.23 ?  21  PHE C O     1 
ATOM   11156 C  CB    . PHE C 2 42  ? 132.481 87.926  118.708 1.00 32.12 ?  21  PHE C CB    1 
ATOM   11157 C  CG    . PHE C 2 42  ? 131.495 87.131  117.903 1.00 31.04 ?  21  PHE C CG    1 
ATOM   11158 C  CD1   . PHE C 2 42  ? 130.159 87.525  117.828 1.00 30.75 ?  21  PHE C CD1   1 
ATOM   11159 C  CD2   . PHE C 2 42  ? 131.898 85.994  117.213 1.00 30.99 ?  21  PHE C CD2   1 
ATOM   11160 C  CE1   . PHE C 2 42  ? 129.236 86.790  117.075 1.00 30.30 ?  21  PHE C CE1   1 
ATOM   11161 C  CE2   . PHE C 2 42  ? 130.983 85.248  116.452 1.00 30.74 ?  21  PHE C CE2   1 
ATOM   11162 C  CZ    . PHE C 2 42  ? 129.652 85.648  116.384 1.00 30.48 ?  21  PHE C CZ    1 
ATOM   11163 N  N     . TYR C 2 43  ? 134.841 90.015  119.383 1.00 32.33 ?  22  TYR C N     1 
ATOM   11164 C  CA    . TYR C 2 43  ? 135.417 91.124  120.139 1.00 32.50 ?  22  TYR C CA    1 
ATOM   11165 C  C     . TYR C 2 43  ? 135.574 92.352  119.245 1.00 33.01 ?  22  TYR C C     1 
ATOM   11166 O  O     . TYR C 2 43  ? 135.121 93.444  119.598 1.00 32.50 ?  22  TYR C O     1 
ATOM   11167 C  CB    . TYR C 2 43  ? 136.760 90.742  120.790 1.00 32.53 ?  22  TYR C CB    1 
ATOM   11168 C  CG    . TYR C 2 43  ? 137.483 91.947  121.367 1.00 33.27 ?  22  TYR C CG    1 
ATOM   11169 C  CD1   . TYR C 2 43  ? 137.138 92.461  122.620 1.00 32.34 ?  22  TYR C CD1   1 
ATOM   11170 C  CD2   . TYR C 2 43  ? 138.482 92.596  120.638 1.00 33.71 ?  22  TYR C CD2   1 
ATOM   11171 C  CE1   . TYR C 2 43  ? 137.784 93.581  123.142 1.00 33.58 ?  22  TYR C CE1   1 
ATOM   11172 C  CE2   . TYR C 2 43  ? 139.133 93.722  121.146 1.00 35.12 ?  22  TYR C CE2   1 
ATOM   11173 C  CZ    . TYR C 2 43  ? 138.782 94.206  122.400 1.00 35.30 ?  22  TYR C CZ    1 
ATOM   11174 O  OH    . TYR C 2 43  ? 139.427 95.316  122.901 1.00 36.54 ?  22  TYR C OH    1 
ATOM   11175 N  N     . ASN C 2 44  ? 136.204 92.159  118.083 1.00 33.80 ?  23  ASN C N     1 
ATOM   11176 C  CA    . ASN C 2 44  ? 136.443 93.245  117.143 1.00 34.80 ?  23  ASN C CA    1 
ATOM   11177 C  C     . ASN C 2 44  ? 135.141 93.843  116.613 1.00 34.40 ?  23  ASN C C     1 
ATOM   11178 O  O     . ASN C 2 44  ? 135.013 95.059  116.518 1.00 33.99 ?  23  ASN C O     1 
ATOM   11179 C  CB    . ASN C 2 44  ? 137.345 92.788  115.985 1.00 35.46 ?  23  ASN C CB    1 
ATOM   11180 C  CG    . ASN C 2 44  ? 138.749 92.370  116.447 1.00 38.28 ?  23  ASN C CG    1 
ATOM   11181 O  OD1   . ASN C 2 44  ? 139.237 92.789  117.507 1.00 41.01 ?  23  ASN C OD1   1 
ATOM   11182 N  ND2   . ASN C 2 44  ? 139.407 91.541  115.638 1.00 39.13 ?  23  ASN C ND2   1 
ATOM   11183 N  N     . GLN C 2 45  ? 134.174 92.983  116.288 1.00 34.49 ?  24  GLN C N     1 
ATOM   11184 C  CA    . GLN C 2 45  ? 132.877 93.437  115.797 1.00 34.81 ?  24  GLN C CA    1 
ATOM   11185 C  C     . GLN C 2 45  ? 132.113 94.229  116.865 1.00 34.68 ?  24  GLN C C     1 
ATOM   11186 O  O     . GLN C 2 45  ? 131.561 95.294  116.577 1.00 34.59 ?  24  GLN C O     1 
ATOM   11187 C  CB    . GLN C 2 45  ? 132.048 92.258  115.279 1.00 34.83 ?  24  GLN C CB    1 
ATOM   11188 C  CG    . GLN C 2 45  ? 130.853 92.653  114.407 1.00 36.14 ?  24  GLN C CG    1 
ATOM   11189 C  CD    . GLN C 2 45  ? 131.246 93.404  113.133 1.00 38.04 ?  24  GLN C CD    1 
ATOM   11190 O  OE1   . GLN C 2 45  ? 132.336 93.213  112.585 1.00 38.57 ?  24  GLN C OE1   1 
ATOM   11191 N  NE2   . GLN C 2 45  ? 130.350 94.271  112.660 1.00 38.67 ?  24  GLN C NE2   1 
ATOM   11192 N  N     . ASN C 2 46  ? 132.097 93.725  118.096 1.00 34.71 ?  25  ASN C N     1 
ATOM   11193 C  CA    . ASN C 2 46  ? 131.407 94.420  119.183 1.00 34.99 ?  25  ASN C CA    1 
ATOM   11194 C  C     . ASN C 2 46  ? 131.986 95.807  119.460 1.00 35.69 ?  25  ASN C C     1 
ATOM   11195 O  O     . ASN C 2 46  ? 131.245 96.792  119.546 1.00 35.41 ?  25  ASN C O     1 
ATOM   11196 C  CB    . ASN C 2 46  ? 131.365 93.569  120.458 1.00 34.64 ?  25  ASN C CB    1 
ATOM   11197 C  CG    . ASN C 2 46  ? 130.250 92.545  120.431 1.00 34.71 ?  25  ASN C CG    1 
ATOM   11198 O  OD1   . ASN C 2 46  ? 129.153 92.811  120.914 1.00 35.68 ?  25  ASN C OD1   1 
ATOM   11199 N  ND2   . ASN C 2 46  ? 130.511 91.380  119.831 1.00 34.71 ?  25  ASN C ND2   1 
ATOM   11200 N  N     . VAL C 2 47  ? 133.308 95.894  119.573 1.00 36.69 ?  26  VAL C N     1 
ATOM   11201 C  CA    . VAL C 2 47  ? 133.937 97.181  119.879 1.00 38.00 ?  26  VAL C CA    1 
ATOM   11202 C  C     . VAL C 2 47  ? 133.846 98.181  118.718 1.00 38.90 ?  26  VAL C C     1 
ATOM   11203 O  O     . VAL C 2 47  ? 133.772 99.384  118.951 1.00 39.46 ?  26  VAL C O     1 
ATOM   11204 C  CB    . VAL C 2 47  ? 135.390 97.046  120.406 1.00 38.16 ?  26  VAL C CB    1 
ATOM   11205 C  CG1   . VAL C 2 47  ? 135.416 96.185  121.654 1.00 37.75 ?  26  VAL C CG1   1 
ATOM   11206 C  CG2   . VAL C 2 47  ? 136.329 96.496  119.333 1.00 38.81 ?  26  VAL C CG2   1 
ATOM   11207 N  N     . LYS C 2 48  ? 133.816 97.685  117.481 1.00 39.67 ?  27  LYS C N     1 
ATOM   11208 C  CA    . LYS C 2 48  ? 133.680 98.567  116.319 1.00 40.50 ?  27  LYS C CA    1 
ATOM   11209 C  C     . LYS C 2 48  ? 132.233 99.042  116.130 1.00 40.02 ?  27  LYS C C     1 
ATOM   11210 O  O     . LYS C 2 48  ? 131.972 99.991  115.387 1.00 40.55 ?  27  LYS C O     1 
ATOM   11211 C  CB    . LYS C 2 48  ? 134.221 97.901  115.039 1.00 41.23 ?  27  LYS C CB    1 
ATOM   11212 C  CG    . LYS C 2 48  ? 133.235 96.976  114.326 1.00 42.50 ?  27  LYS C CG    1 
ATOM   11213 C  CD    . LYS C 2 48  ? 133.807 96.395  113.024 1.00 44.92 ?  27  LYS C CD    1 
ATOM   11214 C  CE    . LYS C 2 48  ? 133.719 97.384  111.863 1.00 46.66 ?  27  LYS C CE    1 
ATOM   11215 N  NZ    . LYS C 2 48  ? 132.311 97.776  111.562 1.00 47.26 1  27  LYS C NZ    1 
ATOM   11216 N  N     . GLN C 2 49  ? 131.296 98.375  116.794 1.00 39.10 ?  28  GLN C N     1 
ATOM   11217 C  CA    . GLN C 2 49  ? 129.906 98.772  116.727 1.00 38.22 ?  28  GLN C CA    1 
ATOM   11218 C  C     . GLN C 2 49  ? 129.540 99.750  117.844 1.00 37.23 ?  28  GLN C C     1 
ATOM   11219 O  O     . GLN C 2 49  ? 128.395 100.191 117.909 1.00 37.40 ?  28  GLN C O     1 
ATOM   11220 C  CB    . GLN C 2 49  ? 128.976 97.546  116.735 1.00 38.69 ?  28  GLN C CB    1 
ATOM   11221 C  CG    . GLN C 2 49  ? 128.962 96.764  115.413 1.00 39.57 ?  28  GLN C CG    1 
ATOM   11222 C  CD    . GLN C 2 49  ? 127.901 95.668  115.355 1.00 41.20 ?  28  GLN C CD    1 
ATOM   11223 O  OE1   . GLN C 2 49  ? 127.835 94.917  114.381 1.00 42.94 ?  28  GLN C OE1   1 
ATOM   11224 N  NE2   . GLN C 2 49  ? 127.065 95.573  116.394 1.00 41.23 ?  28  GLN C NE2   1 
ATOM   11225 N  N     . PHE C 2 50  ? 130.507 100.103 118.698 1.00 35.83 ?  29  PHE C N     1 
ATOM   11226 C  CA    . PHE C 2 50  ? 130.226 100.973 119.849 1.00 34.51 ?  29  PHE C CA    1 
ATOM   11227 C  C     . PHE C 2 50  ? 129.555 102.293 119.458 1.00 33.81 ?  29  PHE C C     1 
ATOM   11228 O  O     . PHE C 2 50  ? 129.982 102.954 118.512 1.00 33.66 ?  29  PHE C O     1 
ATOM   11229 C  CB    . PHE C 2 50  ? 131.475 101.247 120.692 1.00 34.59 ?  29  PHE C CB    1 
ATOM   11230 C  CG    . PHE C 2 50  ? 131.206 102.115 121.909 1.00 34.59 ?  29  PHE C CG    1 
ATOM   11231 C  CD1   . PHE C 2 50  ? 130.513 101.606 123.013 1.00 34.34 ?  29  PHE C CD1   1 
ATOM   11232 C  CD2   . PHE C 2 50  ? 131.626 103.445 121.940 1.00 35.49 ?  29  PHE C CD2   1 
ATOM   11233 C  CE1   . PHE C 2 50  ? 130.254 102.406 124.136 1.00 33.88 ?  29  PHE C CE1   1 
ATOM   11234 C  CE2   . PHE C 2 50  ? 131.371 104.260 123.059 1.00 34.12 ?  29  PHE C CE2   1 
ATOM   11235 C  CZ    . PHE C 2 50  ? 130.686 103.740 124.156 1.00 33.87 ?  29  PHE C CZ    1 
ATOM   11236 N  N     . TRP C 2 51  ? 128.511 102.659 120.204 1.00 32.24 ?  30  TRP C N     1 
ATOM   11237 C  CA    . TRP C 2 51  ? 127.746 103.878 119.949 1.00 31.28 ?  30  TRP C CA    1 
ATOM   11238 C  C     . TRP C 2 51  ? 127.089 104.412 121.224 1.00 31.12 ?  30  TRP C C     1 
ATOM   11239 O  O     . TRP C 2 51  ? 126.999 103.694 122.227 1.00 30.71 ?  30  TRP C O     1 
ATOM   11240 C  CB    . TRP C 2 51  ? 126.691 103.634 118.861 1.00 30.85 ?  30  TRP C CB    1 
ATOM   11241 C  CG    . TRP C 2 51  ? 125.653 102.601 119.227 1.00 29.31 ?  30  TRP C CG    1 
ATOM   11242 C  CD1   . TRP C 2 51  ? 125.773 101.241 119.126 1.00 29.07 ?  30  TRP C CD1   1 
ATOM   11243 C  CD2   . TRP C 2 51  ? 124.354 102.847 119.771 1.00 28.33 ?  30  TRP C CD2   1 
ATOM   11244 N  NE1   . TRP C 2 51  ? 124.625 100.629 119.564 1.00 28.01 ?  30  TRP C NE1   1 
ATOM   11245 C  CE2   . TRP C 2 51  ? 123.736 101.590 119.966 1.00 27.67 ?  30  TRP C CE2   1 
ATOM   11246 C  CE3   . TRP C 2 51  ? 123.649 104.008 120.119 1.00 27.27 ?  30  TRP C CE3   1 
ATOM   11247 C  CZ2   . TRP C 2 51  ? 122.450 101.461 120.490 1.00 26.54 ?  30  TRP C CZ2   1 
ATOM   11248 C  CZ3   . TRP C 2 51  ? 122.365 103.881 120.631 1.00 27.07 ?  30  TRP C CZ3   1 
ATOM   11249 C  CH2   . TRP C 2 51  ? 121.782 102.614 120.819 1.00 26.52 ?  30  TRP C CH2   1 
ATOM   11250 N  N     . LEU C 2 52  ? 126.642 105.670 121.174 1.00 30.65 ?  31  LEU C N     1 
ATOM   11251 C  CA    . LEU C 2 52  ? 125.866 106.297 122.247 1.00 30.38 ?  31  LEU C CA    1 
ATOM   11252 C  C     . LEU C 2 52  ? 124.636 106.982 121.657 1.00 30.51 ?  31  LEU C C     1 
ATOM   11253 O  O     . LEU C 2 52  ? 124.728 107.564 120.575 1.00 30.77 ?  31  LEU C O     1 
ATOM   11254 C  CB    . LEU C 2 52  ? 126.718 107.326 123.009 1.00 30.45 ?  31  LEU C CB    1 
ATOM   11255 C  CG    . LEU C 2 52  ? 127.915 106.760 123.780 1.00 30.29 ?  31  LEU C CG    1 
ATOM   11256 C  CD1   . LEU C 2 52  ? 128.958 107.838 124.108 1.00 30.69 ?  31  LEU C CD1   1 
ATOM   11257 C  CD2   . LEU C 2 52  ? 127.456 106.015 125.043 1.00 29.91 ?  31  LEU C CD2   1 
ATOM   11258 N  N     . PRO C 2 53  ? 123.483 106.926 122.362 1.00 30.73 ?  32  PRO C N     1 
ATOM   11259 C  CA    . PRO C 2 53  ? 122.249 107.531 121.833 1.00 31.17 ?  32  PRO C CA    1 
ATOM   11260 C  C     . PRO C 2 53  ? 122.384 109.020 121.520 1.00 32.18 ?  32  PRO C C     1 
ATOM   11261 O  O     . PRO C 2 53  ? 121.726 109.513 120.590 1.00 32.66 ?  32  PRO C O     1 
ATOM   11262 C  CB    . PRO C 2 53  ? 121.231 107.318 122.959 1.00 30.99 ?  32  PRO C CB    1 
ATOM   11263 C  CG    . PRO C 2 53  ? 122.049 106.980 124.183 1.00 30.50 ?  32  PRO C CG    1 
ATOM   11264 C  CD    . PRO C 2 53  ? 123.250 106.267 123.663 1.00 30.46 ?  32  PRO C CD    1 
ATOM   11265 N  N     . GLU C 2 54  ? 123.239 109.717 122.274 1.00 32.62 ?  33  GLU C N     1 
ATOM   11266 C  CA    . GLU C 2 54  ? 123.477 111.156 122.075 1.00 33.44 ?  33  GLU C CA    1 
ATOM   11267 C  C     . GLU C 2 54  ? 124.060 111.500 120.699 1.00 33.59 ?  33  GLU C C     1 
ATOM   11268 O  O     . GLU C 2 54  ? 124.031 112.659 120.292 1.00 34.05 ?  33  GLU C O     1 
ATOM   11269 C  CB    . GLU C 2 54  ? 124.376 111.736 123.182 1.00 33.72 ?  33  GLU C CB    1 
ATOM   11270 C  CG    . GLU C 2 54  ? 123.705 111.868 124.563 1.00 34.53 ?  33  GLU C CG    1 
ATOM   11271 C  CD    . GLU C 2 54  ? 123.548 110.529 125.285 1.00 35.09 ?  33  GLU C CD    1 
ATOM   11272 O  OE1   . GLU C 2 54  ? 124.300 109.573 124.968 1.00 34.38 ?  33  GLU C OE1   1 
ATOM   11273 O  OE2   . GLU C 2 54  ? 122.667 110.436 126.171 1.00 35.53 -1 33  GLU C OE2   1 
ATOM   11274 N  N     . GLU C 2 55  ? 124.587 110.498 119.992 1.00 33.82 ?  34  GLU C N     1 
ATOM   11275 C  CA    . GLU C 2 55  ? 125.082 110.680 118.625 1.00 34.19 ?  34  GLU C CA    1 
ATOM   11276 C  C     . GLU C 2 55  ? 123.939 110.989 117.646 1.00 33.83 ?  34  GLU C C     1 
ATOM   11277 O  O     . GLU C 2 55  ? 124.171 111.539 116.571 1.00 33.93 ?  34  GLU C O     1 
ATOM   11278 C  CB    . GLU C 2 55  ? 125.841 109.435 118.132 1.00 34.52 ?  34  GLU C CB    1 
ATOM   11279 C  CG    . GLU C 2 55  ? 127.104 109.070 118.908 1.00 36.50 ?  34  GLU C CG    1 
ATOM   11280 C  CD    . GLU C 2 55  ? 127.935 108.007 118.196 1.00 40.03 ?  34  GLU C CD    1 
ATOM   11281 O  OE1   . GLU C 2 55  ? 128.746 108.363 117.312 1.00 42.43 ?  34  GLU C OE1   1 
ATOM   11282 O  OE2   . GLU C 2 55  ? 127.787 106.813 118.521 1.00 39.35 -1 34  GLU C OE2   1 
ATOM   11283 N  N     . ILE C 2 56  ? 122.721 110.600 118.024 1.00 33.31 ?  35  ILE C N     1 
ATOM   11284 C  CA    . ILE C 2 56  ? 121.519 110.763 117.203 1.00 33.14 ?  35  ILE C CA    1 
ATOM   11285 C  C     . ILE C 2 56  ? 120.646 111.867 117.807 1.00 32.58 ?  35  ILE C C     1 
ATOM   11286 O  O     . ILE C 2 56  ? 120.179 111.735 118.934 1.00 32.12 ?  35  ILE C O     1 
ATOM   11287 C  CB    . ILE C 2 56  ? 120.690 109.434 117.147 1.00 33.03 ?  35  ILE C CB    1 
ATOM   11288 C  CG1   . ILE C 2 56  ? 121.561 108.224 116.745 1.00 34.76 ?  35  ILE C CG1   1 
ATOM   11289 C  CG2   . ILE C 2 56  ? 119.456 109.574 116.246 1.00 33.61 ?  35  ILE C CG2   1 
ATOM   11290 C  CD1   . ILE C 2 56  ? 122.089 108.231 115.309 1.00 36.75 ?  35  ILE C CD1   1 
ATOM   11291 N  N     . ALA C 2 57  ? 120.437 112.955 117.068 1.00 32.36 ?  36  ALA C N     1 
ATOM   11292 C  CA    . ALA C 2 57  ? 119.543 114.025 117.520 1.00 32.17 ?  36  ALA C CA    1 
ATOM   11293 C  C     . ALA C 2 57  ? 118.083 113.613 117.301 1.00 31.76 ?  36  ALA C C     1 
ATOM   11294 O  O     . ALA C 2 57  ? 117.720 113.145 116.220 1.00 31.95 ?  36  ALA C O     1 
ATOM   11295 C  CB    . ALA C 2 57  ? 119.851 115.320 116.785 1.00 33.01 ?  36  ALA C CB    1 
ATOM   11296 N  N     . LEU C 2 58  ? 117.249 113.787 118.321 1.00 30.68 ?  37  LEU C N     1 
ATOM   11297 C  CA    . LEU C 2 58  ? 115.908 113.205 118.304 1.00 30.14 ?  37  LEU C CA    1 
ATOM   11298 C  C     . LEU C 2 58  ? 114.778 114.194 118.041 1.00 30.21 ?  37  LEU C C     1 
ATOM   11299 O  O     . LEU C 2 58  ? 113.639 113.782 117.784 1.00 29.91 ?  37  LEU C O     1 
ATOM   11300 C  CB    . LEU C 2 58  ? 115.650 112.426 119.599 1.00 29.46 ?  37  LEU C CB    1 
ATOM   11301 C  CG    . LEU C 2 58  ? 116.491 111.156 119.789 1.00 29.08 ?  37  LEU C CG    1 
ATOM   11302 C  CD1   . LEU C 2 58  ? 116.283 110.572 121.174 1.00 29.23 ?  37  LEU C CD1   1 
ATOM   11303 C  CD2   . LEU C 2 58  ? 116.177 110.112 118.718 1.00 28.84 ?  37  LEU C CD2   1 
ATOM   11304 N  N     . ASN C 2 59  ? 115.095 115.485 118.081 1.00 30.50 ?  38  ASN C N     1 
ATOM   11305 C  CA    . ASN C 2 59  ? 114.085 116.531 117.896 1.00 31.23 ?  38  ASN C CA    1 
ATOM   11306 C  C     . ASN C 2 59  ? 113.393 116.498 116.523 1.00 31.03 ?  38  ASN C C     1 
ATOM   11307 O  O     . ASN C 2 59  ? 112.297 117.028 116.368 1.00 30.82 ?  38  ASN C O     1 
ATOM   11308 C  CB    . ASN C 2 59  ? 114.656 117.924 118.223 1.00 31.98 ?  38  ASN C CB    1 
ATOM   11309 C  CG    . ASN C 2 59  ? 115.865 118.287 117.376 1.00 33.59 ?  38  ASN C CG    1 
ATOM   11310 O  OD1   . ASN C 2 59  ? 116.860 117.552 117.337 1.00 36.48 ?  38  ASN C OD1   1 
ATOM   11311 N  ND2   . ASN C 2 59  ? 115.794 119.433 116.704 1.00 34.77 ?  38  ASN C ND2   1 
ATOM   11312 N  N     . GLY C 2 60  ? 114.025 115.843 115.552 1.00 30.88 ?  39  GLY C N     1 
ATOM   11313 C  CA    . GLY C 2 60  ? 113.428 115.613 114.231 1.00 31.37 ?  39  GLY C CA    1 
ATOM   11314 C  C     . GLY C 2 60  ? 112.195 114.717 114.212 1.00 31.05 ?  39  GLY C C     1 
ATOM   11315 O  O     . GLY C 2 60  ? 111.366 114.849 113.322 1.00 31.21 ?  39  GLY C O     1 
ATOM   11316 N  N     . ASP C 2 61  ? 112.067 113.818 115.190 1.00 30.63 ?  40  ASP C N     1 
ATOM   11317 C  CA    . ASP C 2 61  ? 110.857 112.986 115.341 1.00 30.65 ?  40  ASP C CA    1 
ATOM   11318 C  C     . ASP C 2 61  ? 109.656 113.700 115.969 1.00 31.00 ?  40  ASP C C     1 
ATOM   11319 O  O     . ASP C 2 61  ? 108.562 113.134 116.000 1.00 30.91 ?  40  ASP C O     1 
ATOM   11320 C  CB    . ASP C 2 61  ? 111.146 111.740 116.188 1.00 30.00 ?  40  ASP C CB    1 
ATOM   11321 C  CG    . ASP C 2 61  ? 112.086 110.769 115.515 1.00 30.88 ?  40  ASP C CG    1 
ATOM   11322 O  OD1   . ASP C 2 61  ? 112.555 111.043 114.385 1.00 30.42 ?  40  ASP C OD1   1 
ATOM   11323 O  OD2   . ASP C 2 61  ? 112.362 109.721 116.137 1.00 31.17 -1 40  ASP C OD2   1 
ATOM   11324 N  N     . LEU C 2 62  ? 109.857 114.913 116.482 1.00 31.54 ?  41  LEU C N     1 
ATOM   11325 C  CA    . LEU C 2 62  ? 108.817 115.612 117.256 1.00 32.47 ?  41  LEU C CA    1 
ATOM   11326 C  C     . LEU C 2 62  ? 107.481 115.742 116.533 1.00 33.21 ?  41  LEU C C     1 
ATOM   11327 O  O     . LEU C 2 62  ? 106.421 115.553 117.140 1.00 32.84 ?  41  LEU C O     1 
ATOM   11328 C  CB    . LEU C 2 62  ? 109.295 116.992 117.712 1.00 33.14 ?  41  LEU C CB    1 
ATOM   11329 C  CG    . LEU C 2 62  ? 110.111 117.067 119.002 1.00 34.44 ?  41  LEU C CG    1 
ATOM   11330 C  CD1   . LEU C 2 62  ? 110.751 118.442 119.132 1.00 35.04 ?  41  LEU C CD1   1 
ATOM   11331 C  CD2   . LEU C 2 62  ? 109.234 116.750 120.220 1.00 35.52 ?  41  LEU C CD2   1 
ATOM   11332 N  N     . LEU C 2 63  ? 107.537 116.059 115.241 1.00 33.75 ?  42  LEU C N     1 
ATOM   11333 C  CA    . LEU C 2 63  ? 106.320 116.239 114.460 1.00 34.79 ?  42  LEU C CA    1 
ATOM   11334 C  C     . LEU C 2 63  ? 105.613 114.946 114.060 1.00 34.66 ?  42  LEU C C     1 
ATOM   11335 O  O     . LEU C 2 63  ? 104.397 114.859 114.215 1.00 34.67 ?  42  LEU C O     1 
ATOM   11336 C  CB    . LEU C 2 63  ? 106.558 117.141 113.247 1.00 35.27 ?  42  LEU C CB    1 
ATOM   11337 C  CG    . LEU C 2 63  ? 106.510 118.638 113.575 1.00 36.82 ?  42  LEU C CG    1 
ATOM   11338 C  CD1   . LEU C 2 63  ? 106.799 119.449 112.318 1.00 37.93 ?  42  LEU C CD1   1 
ATOM   11339 C  CD2   . LEU C 2 63  ? 105.165 119.053 114.169 1.00 37.85 ?  42  LEU C CD2   1 
ATOM   11340 N  N     . THR C 2 64  ? 106.345 113.950 113.552 1.00 34.70 ?  43  THR C N     1 
ATOM   11341 C  CA    . THR C 2 64  ? 105.702 112.667 113.221 1.00 35.10 ?  43  THR C CA    1 
ATOM   11342 C  C     . THR C 2 64  ? 105.124 111.976 114.466 1.00 34.78 ?  43  THR C C     1 
ATOM   11343 O  O     . THR C 2 64  ? 104.168 111.217 114.360 1.00 35.04 ?  43  THR C O     1 
ATOM   11344 C  CB    . THR C 2 64  ? 106.593 111.694 112.386 1.00 35.30 ?  43  THR C CB    1 
ATOM   11345 O  OG1   . THR C 2 64  ? 107.837 111.443 113.056 1.00 36.01 ?  43  THR C OG1   1 
ATOM   11346 C  CG2   . THR C 2 64  ? 106.858 112.255 110.990 1.00 35.96 ?  43  THR C CG2   1 
ATOM   11347 N  N     . TRP C 2 65  ? 105.685 112.270 115.642 1.00 34.63 ?  44  TRP C N     1 
ATOM   11348 C  CA    . TRP C 2 65  ? 105.153 111.757 116.911 1.00 34.37 ?  44  TRP C CA    1 
ATOM   11349 C  C     . TRP C 2 65  ? 103.842 112.450 117.283 1.00 35.13 ?  44  TRP C C     1 
ATOM   11350 O  O     . TRP C 2 65  ? 102.842 111.794 117.604 1.00 34.98 ?  44  TRP C O     1 
ATOM   11351 C  CB    . TRP C 2 65  ? 106.173 111.940 118.033 1.00 33.95 ?  44  TRP C CB    1 
ATOM   11352 C  CG    . TRP C 2 65  ? 105.637 111.641 119.397 1.00 33.26 ?  44  TRP C CG    1 
ATOM   11353 C  CD1   . TRP C 2 65  ? 105.267 112.546 120.353 1.00 32.51 ?  44  TRP C CD1   1 
ATOM   11354 C  CD2   . TRP C 2 65  ? 105.414 110.343 119.963 1.00 30.93 ?  44  TRP C CD2   1 
ATOM   11355 N  NE1   . TRP C 2 65  ? 104.832 111.890 121.484 1.00 31.66 ?  44  TRP C NE1   1 
ATOM   11356 C  CE2   . TRP C 2 65  ? 104.911 110.538 121.271 1.00 30.39 ?  44  TRP C CE2   1 
ATOM   11357 C  CE3   . TRP C 2 65  ? 105.596 109.034 119.495 1.00 30.36 ?  44  TRP C CE3   1 
ATOM   11358 C  CZ2   . TRP C 2 65  ? 104.577 109.474 122.112 1.00 29.16 ?  44  TRP C CZ2   1 
ATOM   11359 C  CZ3   . TRP C 2 65  ? 105.266 107.969 120.336 1.00 28.84 ?  44  TRP C CZ3   1 
ATOM   11360 C  CH2   . TRP C 2 65  ? 104.769 108.198 121.631 1.00 29.34 ?  44  TRP C CH2   1 
ATOM   11361 N  N     . LYS C 2 66  ? 103.871 113.780 117.253 1.00 35.69 ?  45  LYS C N     1 
ATOM   11362 C  CA    . LYS C 2 66  ? 102.697 114.606 117.496 1.00 36.38 ?  45  LYS C CA    1 
ATOM   11363 C  C     . LYS C 2 66  ? 101.493 114.165 116.656 1.00 36.24 ?  45  LYS C C     1 
ATOM   11364 O  O     . LYS C 2 66  ? 100.363 114.249 117.121 1.00 36.78 ?  45  LYS C O     1 
ATOM   11365 C  CB    . LYS C 2 66  ? 103.045 116.065 117.191 1.00 37.14 ?  45  LYS C CB    1 
ATOM   11366 C  CG    . LYS C 2 66  ? 101.933 117.069 117.442 1.00 38.91 ?  45  LYS C CG    1 
ATOM   11367 C  CD    . LYS C 2 66  ? 102.310 118.435 116.866 1.00 41.12 ?  45  LYS C CD    1 
ATOM   11368 C  CE    . LYS C 2 66  ? 101.395 119.527 117.396 1.00 43.00 ?  45  LYS C CE    1 
ATOM   11369 N  NZ    . LYS C 2 66  ? 101.272 119.463 118.884 1.00 44.38 1  45  LYS C NZ    1 
ATOM   11370 N  N     . TYR C 2 67  ? 101.762 113.662 115.447 1.00 36.03 ?  46  TYR C N     1 
ATOM   11371 C  CA    . TYR C 2 67  ? 100.739 113.318 114.445 1.00 36.03 ?  46  TYR C CA    1 
ATOM   11372 C  C     . TYR C 2 67  ? 100.110 111.927 114.602 1.00 35.25 ?  46  TYR C C     1 
ATOM   11373 O  O     . TYR C 2 67  ? 99.109  111.616 113.948 1.00 35.32 ?  46  TYR C O     1 
ATOM   11374 C  CB    . TYR C 2 67  ? 101.322 113.424 113.024 1.00 36.60 ?  46  TYR C CB    1 
ATOM   11375 C  CG    . TYR C 2 67  ? 101.796 114.811 112.608 1.00 37.85 ?  46  TYR C CG    1 
ATOM   11376 C  CD1   . TYR C 2 67  ? 101.434 115.945 113.333 1.00 38.97 ?  46  TYR C CD1   1 
ATOM   11377 C  CD2   . TYR C 2 67  ? 102.599 114.983 111.471 1.00 40.06 ?  46  TYR C CD2   1 
ATOM   11378 C  CE1   . TYR C 2 67  ? 101.871 117.216 112.962 1.00 40.36 ?  46  TYR C CE1   1 
ATOM   11379 C  CE2   . TYR C 2 67  ? 103.042 116.258 111.084 1.00 40.53 ?  46  TYR C CE2   1 
ATOM   11380 C  CZ    . TYR C 2 67  ? 102.667 117.369 111.838 1.00 41.43 ?  46  TYR C CZ    1 
ATOM   11381 O  OH    . TYR C 2 67  ? 103.077 118.641 111.480 1.00 41.48 ?  46  TYR C OH    1 
ATOM   11382 N  N     . LEU C 2 68  ? 100.707 111.087 115.443 1.00 33.80 ?  47  LEU C N     1 
ATOM   11383 C  CA    . LEU C 2 68  ? 100.172 109.751 115.682 1.00 32.77 ?  47  LEU C CA    1 
ATOM   11384 C  C     . LEU C 2 68  ? 98.931  109.829 116.561 1.00 31.84 ?  47  LEU C C     1 
ATOM   11385 O  O     . LEU C 2 68  ? 98.814  110.719 117.399 1.00 31.90 ?  47  LEU C O     1 
ATOM   11386 C  CB    . LEU C 2 68  ? 101.217 108.861 116.359 1.00 32.39 ?  47  LEU C CB    1 
ATOM   11387 C  CG    . LEU C 2 68  ? 102.520 108.480 115.653 1.00 32.68 ?  47  LEU C CG    1 
ATOM   11388 C  CD1   . LEU C 2 68  ? 103.357 107.603 116.579 1.00 33.03 ?  47  LEU C CD1   1 
ATOM   11389 C  CD2   . LEU C 2 68  ? 102.278 107.773 114.315 1.00 32.78 ?  47  LEU C CD2   1 
ATOM   11390 N  N     . GLY C 2 69  ? 98.016  108.883 116.380 1.00 30.99 ?  48  GLY C N     1 
ATOM   11391 C  CA    . GLY C 2 69  ? 96.858  108.766 117.263 1.00 30.58 ?  48  GLY C CA    1 
ATOM   11392 C  C     . GLY C 2 69  ? 97.249  108.409 118.692 1.00 29.87 ?  48  GLY C C     1 
ATOM   11393 O  O     . GLY C 2 69  ? 98.353  107.927 118.939 1.00 28.79 ?  48  GLY C O     1 
ATOM   11394 N  N     . LYS C 2 70  ? 96.347  108.658 119.635 1.00 29.89 ?  49  LYS C N     1 
ATOM   11395 C  CA    . LYS C 2 70  ? 96.602  108.334 121.038 1.00 29.49 ?  49  LYS C CA    1 
ATOM   11396 C  C     . LYS C 2 70  ? 96.885  106.834 121.243 1.00 28.74 ?  49  LYS C C     1 
ATOM   11397 O  O     . LYS C 2 70  ? 97.771  106.471 122.029 1.00 27.27 ?  49  LYS C O     1 
ATOM   11398 C  CB    . LYS C 2 70  ? 95.460  108.829 121.931 1.00 30.67 ?  49  LYS C CB    1 
ATOM   11399 C  CG    . LYS C 2 70  ? 95.542  110.347 122.228 1.00 33.73 ?  49  LYS C CG    1 
ATOM   11400 C  CD    . LYS C 2 70  ? 94.220  110.931 122.757 1.00 38.93 ?  49  LYS C CD    1 
ATOM   11401 C  CE    . LYS C 2 70  ? 93.976  110.635 124.242 1.00 41.04 ?  49  LYS C CE    1 
ATOM   11402 N  NZ    . LYS C 2 70  ? 94.860  111.415 125.159 1.00 42.21 1  49  LYS C NZ    1 
ATOM   11403 N  N     . ASN C 2 71  ? 96.146  105.985 120.521 1.00 27.54 ?  50  ASN C N     1 
ATOM   11404 C  CA    . ASN C 2 71  ? 96.370  104.537 120.537 1.00 27.00 ?  50  ASN C CA    1 
ATOM   11405 C  C     . ASN C 2 71  ? 97.779  104.156 120.083 1.00 26.19 ?  50  ASN C C     1 
ATOM   11406 O  O     . ASN C 2 71  ? 98.430  103.279 120.689 1.00 25.38 ?  50  ASN C O     1 
ATOM   11407 C  CB    . ASN C 2 71  ? 95.317  103.801 119.677 1.00 27.08 ?  50  ASN C CB    1 
ATOM   11408 C  CG    . ASN C 2 71  ? 95.325  104.230 118.190 1.00 28.69 ?  50  ASN C CG    1 
ATOM   11409 O  OD1   . ASN C 2 71  ? 95.406  105.427 117.852 1.00 30.45 ?  50  ASN C OD1   1 
ATOM   11410 N  ND2   . ASN C 2 71  ? 95.210  103.238 117.294 1.00 29.42 ?  50  ASN C ND2   1 
ATOM   11411 N  N     . GLU C 2 72  ? 98.241  104.815 119.022 1.00 24.91 ?  51  GLU C N     1 
ATOM   11412 C  CA    . GLU C 2 72  ? 99.555  104.540 118.454 1.00 24.97 ?  51  GLU C CA    1 
ATOM   11413 C  C     . GLU C 2 72  ? 100.677 104.955 119.412 1.00 24.45 ?  51  GLU C C     1 
ATOM   11414 O  O     . GLU C 2 72  ? 101.641 104.201 119.618 1.00 23.90 ?  51  GLU C O     1 
ATOM   11415 C  CB    . GLU C 2 72  ? 99.708  105.240 117.103 1.00 25.27 ?  51  GLU C CB    1 
ATOM   11416 C  CG    . GLU C 2 72  ? 98.775  104.708 116.018 1.00 26.16 ?  51  GLU C CG    1 
ATOM   11417 C  CD    . GLU C 2 72  ? 98.930  105.472 114.709 1.00 28.70 ?  51  GLU C CD    1 
ATOM   11418 O  OE1   . GLU C 2 72  ? 98.414  106.604 114.617 1.00 28.70 ?  51  GLU C OE1   1 
ATOM   11419 O  OE2   . GLU C 2 72  ? 99.567  104.940 113.773 1.00 28.92 -1 51  GLU C OE2   1 
ATOM   11420 N  N     . GLN C 2 73  ? 100.532 106.138 120.007 1.00 23.75 ?  52  GLN C N     1 
ATOM   11421 C  CA    . GLN C 2 73  ? 101.511 106.639 120.967 1.00 23.94 ?  52  GLN C CA    1 
ATOM   11422 C  C     . GLN C 2 73  ? 101.571 105.747 122.208 1.00 23.36 ?  52  GLN C C     1 
ATOM   11423 O  O     . GLN C 2 73  ? 102.648 105.501 122.740 1.00 22.95 ?  52  GLN C O     1 
ATOM   11424 C  CB    . GLN C 2 73  ? 101.184 108.080 121.389 1.00 24.28 ?  52  GLN C CB    1 
ATOM   11425 C  CG    . GLN C 2 73  ? 101.460 109.158 120.322 1.00 25.22 ?  52  GLN C CG    1 
ATOM   11426 C  CD    . GLN C 2 73  ? 101.207 110.583 120.828 1.00 29.02 ?  52  GLN C CD    1 
ATOM   11427 O  OE1   . GLN C 2 73  ? 100.812 110.787 121.974 1.00 32.08 ?  52  GLN C OE1   1 
ATOM   11428 N  NE2   . GLN C 2 73  ? 101.438 111.568 119.969 1.00 29.13 ?  52  GLN C NE2   1 
ATOM   11429 N  N     . ASP C 2 74  ? 100.405 105.296 122.673 1.00 23.02 ?  53  ASP C N     1 
ATOM   11430 C  CA    . ASP C 2 74  ? 100.311 104.427 123.839 1.00 23.44 ?  53  ASP C CA    1 
ATOM   11431 C  C     . ASP C 2 74  ? 101.057 103.109 123.592 1.00 23.00 ?  53  ASP C C     1 
ATOM   11432 O  O     . ASP C 2 74  ? 101.865 102.692 124.416 1.00 22.96 ?  53  ASP C O     1 
ATOM   11433 C  CB    . ASP C 2 74  ? 98.844  104.143 124.187 1.00 23.31 ?  53  ASP C CB    1 
ATOM   11434 C  CG    . ASP C 2 74  ? 98.689  103.387 125.491 1.00 25.80 ?  53  ASP C CG    1 
ATOM   11435 O  OD1   . ASP C 2 74  ? 99.111  103.910 126.554 1.00 27.95 ?  53  ASP C OD1   1 
ATOM   11436 O  OD2   . ASP C 2 74  ? 98.133  102.271 125.454 1.00 26.30 -1 53  ASP C OD2   1 
ATOM   11437 N  N     . THR C 2 75  ? 100.765 102.464 122.465 1.00 22.20 ?  54  THR C N     1 
ATOM   11438 C  CA    . THR C 2 75  ? 101.416 101.212 122.101 1.00 21.84 ?  54  THR C CA    1 
ATOM   11439 C  C     . THR C 2 75  ? 102.921 101.416 121.963 1.00 22.09 ?  54  THR C C     1 
ATOM   11440 O  O     . THR C 2 75  ? 103.702 100.618 122.469 1.00 21.88 ?  54  THR C O     1 
ATOM   11441 C  CB    . THR C 2 75  ? 100.811 100.595 120.810 1.00 21.74 ?  54  THR C CB    1 
ATOM   11442 O  OG1   . THR C 2 75  ? 99.458  100.219 121.073 1.00 22.09 ?  54  THR C OG1   1 
ATOM   11443 C  CG2   . THR C 2 75  ? 101.578 99.336  120.385 1.00 19.76 ?  54  THR C CG2   1 
ATOM   11444 N  N     . TYR C 2 76  ? 103.319 102.492 121.291 1.00 22.38 ?  55  TYR C N     1 
ATOM   11445 C  CA    . TYR C 2 76  ? 104.737 102.798 121.116 1.00 22.85 ?  55  TYR C CA    1 
ATOM   11446 C  C     . TYR C 2 76  ? 105.487 102.951 122.450 1.00 22.56 ?  55  TYR C C     1 
ATOM   11447 O  O     . TYR C 2 76  ? 106.556 102.370 122.616 1.00 21.97 ?  55  TYR C O     1 
ATOM   11448 C  CB    . TYR C 2 76  ? 104.905 104.049 120.264 1.00 23.57 ?  55  TYR C CB    1 
ATOM   11449 C  CG    . TYR C 2 76  ? 106.291 104.246 119.686 1.00 25.59 ?  55  TYR C CG    1 
ATOM   11450 C  CD1   . TYR C 2 76  ? 106.621 103.746 118.422 1.00 27.49 ?  55  TYR C CD1   1 
ATOM   11451 C  CD2   . TYR C 2 76  ? 107.262 104.963 120.387 1.00 27.70 ?  55  TYR C CD2   1 
ATOM   11452 C  CE1   . TYR C 2 76  ? 107.893 103.950 117.875 1.00 30.28 ?  55  TYR C CE1   1 
ATOM   11453 C  CE2   . TYR C 2 76  ? 108.541 105.168 119.852 1.00 30.38 ?  55  TYR C CE2   1 
ATOM   11454 C  CZ    . TYR C 2 76  ? 108.848 104.657 118.597 1.00 31.39 ?  55  TYR C CZ    1 
ATOM   11455 O  OH    . TYR C 2 76  ? 110.105 104.870 118.063 1.00 32.67 ?  55  TYR C OH    1 
ATOM   11456 N  N     . MET C 2 77  ? 104.932 103.731 123.381 1.00 23.14 ?  56  MET C N     1 
ATOM   11457 C  CA    . MET C 2 77  ? 105.552 103.943 124.703 1.00 23.90 ?  56  MET C CA    1 
ATOM   11458 C  C     . MET C 2 77  ? 105.710 102.623 125.446 1.00 23.24 ?  56  MET C C     1 
ATOM   11459 O  O     . MET C 2 77  ? 106.743 102.356 126.072 1.00 22.47 ?  56  MET C O     1 
ATOM   11460 C  CB    . MET C 2 77  ? 104.699 104.875 125.573 1.00 24.38 ?  56  MET C CB    1 
ATOM   11461 C  CG    . MET C 2 77  ? 104.556 106.307 125.081 1.00 28.52 ?  56  MET C CG    1 
ATOM   11462 S  SD    . MET C 2 77  ? 106.027 107.286 125.356 1.00 34.32 ?  56  MET C SD    1 
ATOM   11463 C  CE    . MET C 2 77  ? 106.092 107.355 127.150 1.00 33.84 ?  56  MET C CE    1 
ATOM   11464 N  N     . LYS C 2 78  ? 104.663 101.805 125.378 1.00 23.25 ?  57  LYS C N     1 
ATOM   11465 C  CA    . LYS C 2 78  ? 104.605 100.577 126.160 1.00 22.98 ?  57  LYS C CA    1 
ATOM   11466 C  C     . LYS C 2 78  ? 105.586 99.557  125.602 1.00 22.77 ?  57  LYS C C     1 
ATOM   11467 O  O     . LYS C 2 78  ? 106.302 98.902  126.354 1.00 22.56 ?  57  LYS C O     1 
ATOM   11468 C  CB    . LYS C 2 78  ? 103.168 100.047 126.218 1.00 22.99 ?  57  LYS C CB    1 
ATOM   11469 C  CG    . LYS C 2 78  ? 102.286 100.842 127.185 1.00 24.86 ?  57  LYS C CG    1 
ATOM   11470 C  CD    . LYS C 2 78  ? 100.813 100.442 127.100 1.00 27.37 ?  57  LYS C CD    1 
ATOM   11471 C  CE    . LYS C 2 78  ? 100.007 101.073 128.242 1.00 28.99 ?  57  LYS C CE    1 
ATOM   11472 N  NZ    . LYS C 2 78  ? 98.549  100.834 128.026 1.00 29.82 1  57  LYS C NZ    1 
ATOM   11473 N  N     . VAL C 2 79  ? 105.618 99.459  124.274 1.00 22.70 ?  58  VAL C N     1 
ATOM   11474 C  CA    . VAL C 2 79  ? 106.559 98.621  123.535 1.00 23.48 ?  58  VAL C CA    1 
ATOM   11475 C  C     . VAL C 2 79  ? 108.023 98.917  123.943 1.00 23.04 ?  58  VAL C C     1 
ATOM   11476 O  O     . VAL C 2 79  ? 108.780 97.996  124.309 1.00 22.83 ?  58  VAL C O     1 
ATOM   11477 C  CB    . VAL C 2 79  ? 106.278 98.792  122.009 1.00 24.24 ?  58  VAL C CB    1 
ATOM   11478 C  CG1   . VAL C 2 79  ? 107.536 98.759  121.160 1.00 25.71 ?  58  VAL C CG1   1 
ATOM   11479 C  CG2   . VAL C 2 79  ? 105.213 97.773  121.546 1.00 25.04 ?  58  VAL C CG2   1 
ATOM   11480 N  N     . LEU C 2 80  ? 108.399 100.193 123.931 1.00 22.84 ?  59  LEU C N     1 
ATOM   11481 C  CA    . LEU C 2 80  ? 109.760 100.586 124.300 1.00 23.35 ?  59  LEU C CA    1 
ATOM   11482 C  C     . LEU C 2 80  ? 110.031 100.352 125.791 1.00 22.75 ?  59  LEU C C     1 
ATOM   11483 O  O     . LEU C 2 80  ? 111.150 100.012 126.166 1.00 22.75 ?  59  LEU C O     1 
ATOM   11484 C  CB    . LEU C 2 80  ? 110.057 102.045 123.926 1.00 23.91 ?  59  LEU C CB    1 
ATOM   11485 C  CG    . LEU C 2 80  ? 110.144 102.526 122.464 1.00 26.63 ?  59  LEU C CG    1 
ATOM   11486 C  CD1   . LEU C 2 80  ? 110.872 103.859 122.397 1.00 26.99 ?  59  LEU C CD1   1 
ATOM   11487 C  CD2   . LEU C 2 80  ? 110.825 101.527 121.543 1.00 27.23 ?  59  LEU C CD2   1 
ATOM   11488 N  N     . ALA C 2 81  ? 109.001 100.509 126.626 1.00 22.28 ?  60  ALA C N     1 
ATOM   11489 C  CA    . ALA C 2 81  ? 109.118 100.245 128.063 1.00 22.21 ?  60  ALA C CA    1 
ATOM   11490 C  C     . ALA C 2 81  ? 109.390 98.762  128.339 1.00 22.07 ?  60  ALA C C     1 
ATOM   11491 O  O     . ALA C 2 81  ? 110.221 98.442  129.182 1.00 21.97 ?  60  ALA C O     1 
ATOM   11492 C  CB    . ALA C 2 81  ? 107.869 100.744 128.821 1.00 22.38 ?  60  ALA C CB    1 
ATOM   11493 N  N     . GLY C 2 82  ? 108.717 97.878  127.592 1.00 21.67 ?  61  GLY C N     1 
ATOM   11494 C  CA    . GLY C 2 82  ? 108.945 96.436  127.653 1.00 21.74 ?  61  GLY C CA    1 
ATOM   11495 C  C     . GLY C 2 82  ? 110.360 96.069  127.240 1.00 21.79 ?  61  GLY C C     1 
ATOM   11496 O  O     . GLY C 2 82  ? 110.994 95.188  127.840 1.00 21.93 ?  61  GLY C O     1 
ATOM   11497 N  N     . LEU C 2 83  ? 110.862 96.766  126.222 1.00 21.54 ?  62  LEU C N     1 
ATOM   11498 C  CA    . LEU C 2 83  ? 112.246 96.609  125.776 1.00 21.12 ?  62  LEU C CA    1 
ATOM   11499 C  C     . LEU C 2 83  ? 113.221 97.081  126.845 1.00 20.89 ?  62  LEU C C     1 
ATOM   11500 O  O     . LEU C 2 83  ? 114.229 96.417  127.093 1.00 20.84 ?  62  LEU C O     1 
ATOM   11501 C  CB    . LEU C 2 83  ? 112.505 97.372  124.472 1.00 21.23 ?  62  LEU C CB    1 
ATOM   11502 C  CG    . LEU C 2 83  ? 111.788 96.930  123.189 1.00 21.98 ?  62  LEU C CG    1 
ATOM   11503 C  CD1   . LEU C 2 83  ? 112.049 97.911  122.043 1.00 24.12 ?  62  LEU C CD1   1 
ATOM   11504 C  CD2   . LEU C 2 83  ? 112.185 95.528  122.769 1.00 22.03 ?  62  LEU C CD2   1 
ATOM   11505 N  N     . THR C 2 84  ? 112.918 98.224  127.464 1.00 19.93 ?  63  THR C N     1 
ATOM   11506 C  CA    . THR C 2 84  ? 113.763 98.780  128.518 1.00 19.71 ?  63  THR C CA    1 
ATOM   11507 C  C     . THR C 2 84  ? 113.922 97.791  129.661 1.00 19.63 ?  63  THR C C     1 
ATOM   11508 O  O     . THR C 2 84  ? 115.025 97.627  130.191 1.00 19.62 ?  63  THR C O     1 
ATOM   11509 C  CB    . THR C 2 84  ? 113.196 100.113 129.065 1.00 20.22 ?  63  THR C CB    1 
ATOM   11510 O  OG1   . THR C 2 84  ? 112.916 101.007 127.973 1.00 19.37 ?  63  THR C OG1   1 
ATOM   11511 C  CG2   . THR C 2 84  ? 114.172 100.751 130.023 1.00 19.45 ?  63  THR C CG2   1 
ATOM   11512 N  N     . LEU C 2 85  ? 112.824 97.143  130.041 1.00 19.66 ?  64  LEU C N     1 
ATOM   11513 C  CA    . LEU C 2 85  ? 112.843 96.164  131.125 1.00 20.51 ?  64  LEU C CA    1 
ATOM   11514 C  C     . LEU C 2 85  ? 113.767 94.990  130.788 1.00 20.84 ?  64  LEU C C     1 
ATOM   11515 O  O     . LEU C 2 85  ? 114.633 94.627  131.586 1.00 21.30 ?  64  LEU C O     1 
ATOM   11516 C  CB    . LEU C 2 85  ? 111.426 95.678  131.475 1.00 20.03 ?  64  LEU C CB    1 
ATOM   11517 C  CG    . LEU C 2 85  ? 111.382 94.613  132.595 1.00 21.43 ?  64  LEU C CG    1 
ATOM   11518 C  CD1   . LEU C 2 85  ? 111.848 95.175  133.958 1.00 21.61 ?  64  LEU C CD1   1 
ATOM   11519 C  CD2   . LEU C 2 85  ? 110.004 93.969  132.736 1.00 20.99 ?  64  LEU C CD2   1 
ATOM   11520 N  N     . LEU C 2 86  ? 113.586 94.420  129.602 1.00 21.37 ?  65  LEU C N     1 
ATOM   11521 C  CA    . LEU C 2 86  ? 114.431 93.325  129.121 1.00 21.92 ?  65  LEU C CA    1 
ATOM   11522 C  C     . LEU C 2 86  ? 115.928 93.675  129.134 1.00 21.76 ?  65  LEU C C     1 
ATOM   11523 O  O     . LEU C 2 86  ? 116.738 92.893  129.633 1.00 21.72 ?  65  LEU C O     1 
ATOM   11524 C  CB    . LEU C 2 86  ? 114.003 92.883  127.712 1.00 22.42 ?  65  LEU C CB    1 
ATOM   11525 C  CG    . LEU C 2 86  ? 112.653 92.173  127.479 1.00 24.26 ?  65  LEU C CG    1 
ATOM   11526 C  CD1   . LEU C 2 86  ? 112.428 91.974  125.981 1.00 24.67 ?  65  LEU C CD1   1 
ATOM   11527 C  CD2   . LEU C 2 86  ? 112.589 90.838  128.200 1.00 25.60 ?  65  LEU C CD2   1 
ATOM   11528 N  N     . ASP C 2 87  ? 116.288 94.838  128.589 1.00 21.75 ?  66  ASP C N     1 
ATOM   11529 C  CA    . ASP C 2 87  ? 117.689 95.303  128.594 1.00 21.99 ?  66  ASP C CA    1 
ATOM   11530 C  C     . ASP C 2 87  ? 118.240 95.612  129.990 1.00 21.76 ?  66  ASP C C     1 
ATOM   11531 O  O     . ASP C 2 87  ? 119.435 95.413  130.254 1.00 21.65 ?  66  ASP C O     1 
ATOM   11532 C  CB    . ASP C 2 87  ? 117.857 96.549  127.719 1.00 22.23 ?  66  ASP C CB    1 
ATOM   11533 C  CG    . ASP C 2 87  ? 118.284 96.219  126.316 1.00 24.59 ?  66  ASP C CG    1 
ATOM   11534 O  OD1   . ASP C 2 87  ? 119.168 95.350  126.139 1.00 27.46 ?  66  ASP C OD1   1 
ATOM   11535 O  OD2   . ASP C 2 87  ? 117.737 96.845  125.385 1.00 27.98 -1 66  ASP C OD2   1 
ATOM   11536 N  N     . THR C 2 88  ? 117.380 96.132  130.862 1.00 21.50 ?  67  THR C N     1 
ATOM   11537 C  CA    . THR C 2 88  ? 117.743 96.354  132.257 1.00 21.80 ?  67  THR C CA    1 
ATOM   11538 C  C     . THR C 2 88  ? 118.229 95.043  132.905 1.00 22.04 ?  67  THR C C     1 
ATOM   11539 O  O     . THR C 2 88  ? 119.293 95.011  133.539 1.00 22.21 ?  67  THR C O     1 
ATOM   11540 C  CB    . THR C 2 88  ? 116.571 96.966  133.044 1.00 22.15 ?  67  THR C CB    1 
ATOM   11541 O  OG1   . THR C 2 88  ? 116.216 98.218  132.453 1.00 22.23 ?  67  THR C OG1   1 
ATOM   11542 C  CG2   . THR C 2 88  ? 116.938 97.202  134.513 1.00 21.19 ?  67  THR C CG2   1 
ATOM   11543 N  N     . GLU C 2 89  ? 117.468 93.969  132.713 1.00 21.55 ?  68  GLU C N     1 
ATOM   11544 C  CA    . GLU C 2 89  ? 117.805 92.693  133.328 1.00 21.81 ?  68  GLU C CA    1 
ATOM   11545 C  C     . GLU C 2 89  ? 118.940 91.970  132.586 1.00 21.35 ?  68  GLU C C     1 
ATOM   11546 O  O     . GLU C 2 89  ? 119.770 91.311  133.209 1.00 21.34 ?  68  GLU C O     1 
ATOM   11547 C  CB    . GLU C 2 89  ? 116.554 91.823  133.496 1.00 22.25 ?  68  GLU C CB    1 
ATOM   11548 C  CG    . GLU C 2 89  ? 115.693 92.236  134.724 1.00 24.02 ?  68  GLU C CG    1 
ATOM   11549 C  CD    . GLU C 2 89  ? 116.504 92.303  136.020 1.00 25.78 ?  68  GLU C CD    1 
ATOM   11550 O  OE1   . GLU C 2 89  ? 117.291 91.372  136.294 1.00 26.69 ?  68  GLU C OE1   1 
ATOM   11551 O  OE2   . GLU C 2 89  ? 116.356 93.292  136.776 1.00 28.98 -1 68  GLU C OE2   1 
ATOM   11552 N  N     . GLN C 2 90  ? 119.004 92.141  131.267 1.00 20.82 ?  69  GLN C N     1 
ATOM   11553 C  CA    . GLN C 2 90  ? 120.094 91.575  130.480 1.00 21.28 ?  69  GLN C CA    1 
ATOM   11554 C  C     . GLN C 2 90  ? 121.433 92.213  130.862 1.00 21.24 ?  69  GLN C C     1 
ATOM   11555 O  O     . GLN C 2 90  ? 122.458 91.527  130.915 1.00 20.99 ?  69  GLN C O     1 
ATOM   11556 C  CB    . GLN C 2 90  ? 119.818 91.715  128.972 1.00 21.86 ?  69  GLN C CB    1 
ATOM   11557 C  CG    . GLN C 2 90  ? 120.730 90.840  128.082 1.00 24.29 ?  69  GLN C CG    1 
ATOM   11558 C  CD    . GLN C 2 90  ? 120.435 89.342  128.209 1.00 27.14 ?  69  GLN C CD    1 
ATOM   11559 O  OE1   . GLN C 2 90  ? 119.852 88.893  129.200 1.00 27.13 ?  69  GLN C OE1   1 
ATOM   11560 N  NE2   . GLN C 2 90  ? 120.856 88.564  127.209 1.00 27.69 ?  69  GLN C NE2   1 
ATOM   11561 N  N     . GLY C 2 91  ? 121.407 93.515  131.160 1.00 20.62 ?  70  GLY C N     1 
ATOM   11562 C  CA    . GLY C 2 91  ? 122.609 94.254  131.557 1.00 22.00 ?  70  GLY C CA    1 
ATOM   11563 C  C     . GLY C 2 91  ? 122.982 94.069  133.015 1.00 22.45 ?  70  GLY C C     1 
ATOM   11564 O  O     . GLY C 2 91  ? 124.155 93.869  133.320 1.00 23.53 ?  70  GLY C O     1 
ATOM   11565 N  N     . ASN C 2 92  ? 121.990 94.134  133.906 1.00 22.79 ?  71  ASN C N     1 
ATOM   11566 C  CA    . ASN C 2 92  ? 122.218 94.001  135.354 1.00 23.85 ?  71  ASN C CA    1 
ATOM   11567 C  C     . ASN C 2 92  ? 122.578 92.578  135.764 1.00 24.33 ?  71  ASN C C     1 
ATOM   11568 O  O     . ASN C 2 92  ? 123.375 92.377  136.688 1.00 24.17 ?  71  ASN C O     1 
ATOM   11569 C  CB    . ASN C 2 92  ? 120.971 94.404  136.152 1.00 23.74 ?  71  ASN C CB    1 
ATOM   11570 C  CG    . ASN C 2 92  ? 120.668 95.892  136.093 1.00 24.38 ?  71  ASN C CG    1 
ATOM   11571 O  OD1   . ASN C 2 92  ? 121.358 96.674  135.427 1.00 25.16 ?  71  ASN C OD1   1 
ATOM   11572 N  ND2   . ASN C 2 92  ? 119.617 96.287  136.791 1.00 24.07 ?  71  ASN C ND2   1 
ATOM   11573 N  N     . THR C 2 93  ? 121.991 91.598  135.075 1.00 23.97 ?  72  THR C N     1 
ATOM   11574 C  CA    . THR C 2 93  ? 121.966 90.220  135.586 1.00 24.97 ?  72  THR C CA    1 
ATOM   11575 C  C     . THR C 2 93  ? 122.475 89.206  134.572 1.00 24.52 ?  72  THR C C     1 
ATOM   11576 O  O     . THR C 2 93  ? 123.442 88.504  134.839 1.00 25.39 ?  72  THR C O     1 
ATOM   11577 C  CB    . THR C 2 93  ? 120.540 89.812  136.048 1.00 24.54 ?  72  THR C CB    1 
ATOM   11578 O  OG1   . THR C 2 93  ? 120.045 90.771  136.991 1.00 26.43 ?  72  THR C OG1   1 
ATOM   11579 C  CG2   . THR C 2 93  ? 120.546 88.439  136.701 1.00 26.83 ?  72  THR C CG2   1 
ATOM   11580 N  N     . GLY C 2 94  ? 121.822 89.148  133.421 1.00 24.37 ?  73  GLY C N     1 
ATOM   11581 C  CA    . GLY C 2 94  ? 122.052 88.096  132.418 1.00 24.24 ?  73  GLY C CA    1 
ATOM   11582 C  C     . GLY C 2 94  ? 123.470 88.030  131.892 1.00 24.94 ?  73  GLY C C     1 
ATOM   11583 O  O     . GLY C 2 94  ? 124.151 87.011  132.046 1.00 25.86 ?  73  GLY C O     1 
ATOM   11584 N  N     . MET C 2 95  ? 123.920 89.113  131.268 1.00 24.07 ?  74  MET C N     1 
ATOM   11585 C  CA    . MET C 2 95  ? 125.268 89.133  130.716 1.00 24.35 ?  74  MET C CA    1 
ATOM   11586 C  C     . MET C 2 95  ? 126.397 89.025  131.759 1.00 23.52 ?  74  MET C C     1 
ATOM   11587 O  O     . MET C 2 95  ? 127.325 88.257  131.529 1.00 23.40 ?  74  MET C O     1 
ATOM   11588 C  CB    . MET C 2 95  ? 125.468 90.314  129.766 1.00 24.38 ?  74  MET C CB    1 
ATOM   11589 C  CG    . MET C 2 95  ? 124.705 90.185  128.447 1.00 27.47 ?  74  MET C CG    1 
ATOM   11590 S  SD    . MET C 2 95  ? 125.280 88.745  127.505 1.00 32.54 ?  74  MET C SD    1 
ATOM   11591 C  CE    . MET C 2 95  ? 126.865 89.305  126.989 1.00 34.32 ?  74  MET C CE    1 
ATOM   11592 N  N     . PRO C 2 96  ? 126.323 89.774  132.896 1.00 23.36 ?  75  PRO C N     1 
ATOM   11593 C  CA    . PRO C 2 96  ? 127.348 89.621  133.951 1.00 23.27 ?  75  PRO C CA    1 
ATOM   11594 C  C     . PRO C 2 96  ? 127.437 88.217  134.540 1.00 23.77 ?  75  PRO C C     1 
ATOM   11595 O  O     . PRO C 2 96  ? 128.541 87.727  134.776 1.00 23.46 ?  75  PRO C O     1 
ATOM   11596 C  CB    . PRO C 2 96  ? 126.887 90.595  135.048 1.00 23.55 ?  75  PRO C CB    1 
ATOM   11597 C  CG    . PRO C 2 96  ? 126.107 91.636  134.322 1.00 23.85 ?  75  PRO C CG    1 
ATOM   11598 C  CD    . PRO C 2 96  ? 125.393 90.877  133.214 1.00 22.76 ?  75  PRO C CD    1 
ATOM   11599 N  N     . ILE C 2 97  ? 126.291 87.582  134.799 1.00 23.81 ?  76  ILE C N     1 
ATOM   11600 C  CA    . ILE C 2 97  ? 126.287 86.229  135.360 1.00 24.52 ?  76  ILE C CA    1 
ATOM   11601 C  C     . ILE C 2 97  ? 126.854 85.169  134.391 1.00 23.92 ?  76  ILE C C     1 
ATOM   11602 O  O     . ILE C 2 97  ? 127.631 84.293  134.797 1.00 23.99 ?  76  ILE C O     1 
ATOM   11603 C  CB    . ILE C 2 97  ? 124.893 85.833  135.924 1.00 24.49 ?  76  ILE C CB    1 
ATOM   11604 C  CG1   . ILE C 2 97  ? 125.030 84.724  136.965 1.00 27.08 ?  76  ILE C CG1   1 
ATOM   11605 C  CG2   . ILE C 2 97  ? 123.911 85.411  134.811 1.00 26.06 ?  76  ILE C CG2   1 
ATOM   11606 C  CD1   . ILE C 2 97  ? 123.880 84.701  137.960 1.00 31.37 ?  76  ILE C CD1   1 
ATOM   11607 N  N     . VAL C 2 98  ? 126.495 85.266  133.115 1.00 23.97 ?  77  VAL C N     1 
ATOM   11608 C  CA    . VAL C 2 98  ? 127.088 84.391  132.093 1.00 24.01 ?  77  VAL C CA    1 
ATOM   11609 C  C     . VAL C 2 98  ? 128.605 84.658  131.990 1.00 25.23 ?  77  VAL C C     1 
ATOM   11610 O  O     . VAL C 2 98  ? 129.403 83.716  131.943 1.00 25.77 ?  77  VAL C O     1 
ATOM   11611 C  CB    . VAL C 2 98  ? 126.375 84.545  130.725 1.00 23.98 ?  77  VAL C CB    1 
ATOM   11612 C  CG1   . VAL C 2 98  ? 127.161 83.857  129.611 1.00 23.17 ?  77  VAL C CG1   1 
ATOM   11613 C  CG2   . VAL C 2 98  ? 124.954 83.974  130.811 1.00 22.55 ?  77  VAL C CG2   1 
ATOM   11614 N  N     . ALA C 2 99  ? 129.000 85.932  132.013 1.00 25.42 ?  78  ALA C N     1 
ATOM   11615 C  CA    . ALA C 2 99  ? 130.431 86.284  132.007 1.00 26.72 ?  78  ALA C CA    1 
ATOM   11616 C  C     . ALA C 2 99  ? 131.177 85.610  133.163 1.00 27.46 ?  78  ALA C C     1 
ATOM   11617 O  O     . ALA C 2 99  ? 132.277 85.090  132.975 1.00 28.07 ?  78  ALA C O     1 
ATOM   11618 C  CB    . ALA C 2 99  ? 130.623 87.788  132.058 1.00 26.52 ?  78  ALA C CB    1 
ATOM   11619 N  N     . GLU C 2 100 ? 130.555 85.588  134.340 1.00 28.33 ?  79  GLU C N     1 
ATOM   11620 C  CA    . GLU C 2 100 ? 131.168 85.000  135.534 1.00 29.60 ?  79  GLU C CA    1 
ATOM   11621 C  C     . GLU C 2 100 ? 131.482 83.512  135.358 1.00 29.64 ?  79  GLU C C     1 
ATOM   11622 O  O     . GLU C 2 100 ? 132.513 83.023  135.836 1.00 29.72 ?  79  GLU C O     1 
ATOM   11623 C  CB    . GLU C 2 100 ? 130.278 85.220  136.758 1.00 29.70 ?  79  GLU C CB    1 
ATOM   11624 C  CG    . GLU C 2 100 ? 130.879 84.706  138.066 1.00 33.58 ?  79  GLU C CG    1 
ATOM   11625 C  CD    . GLU C 2 100 ? 129.939 84.811  139.251 1.00 37.83 ?  79  GLU C CD    1 
ATOM   11626 O  OE1   . GLU C 2 100 ? 128.854 85.432  139.135 1.00 40.64 ?  79  GLU C OE1   1 
ATOM   11627 O  OE2   . GLU C 2 100 ? 130.289 84.257  140.315 1.00 41.40 -1 79  GLU C OE2   1 
ATOM   11628 N  N     . HIS C 2 101 ? 130.606 82.799  134.654 1.00 29.43 ?  80  HIS C N     1 
ATOM   11629 C  CA    . HIS C 2 101 ? 130.709 81.349  134.569 1.00 29.74 ?  80  HIS C CA    1 
ATOM   11630 C  C     . HIS C 2 101 ? 131.441 80.822  133.333 1.00 30.18 ?  80  HIS C C     1 
ATOM   11631 O  O     . HIS C 2 101 ? 131.849 79.667  133.304 1.00 30.30 ?  80  HIS C O     1 
ATOM   11632 C  CB    . HIS C 2 101 ? 129.325 80.705  134.752 1.00 29.21 ?  80  HIS C CB    1 
ATOM   11633 C  CG    . HIS C 2 101 ? 128.798 80.834  136.148 1.00 29.60 ?  80  HIS C CG    1 
ATOM   11634 N  ND1   . HIS C 2 101 ? 128.010 81.890  136.555 1.00 30.06 ?  80  HIS C ND1   1 
ATOM   11635 C  CD2   . HIS C 2 101 ? 128.986 80.062  137.244 1.00 29.49 ?  80  HIS C CD2   1 
ATOM   11636 C  CE1   . HIS C 2 101 ? 127.722 81.756  137.839 1.00 29.56 ?  80  HIS C CE1   1 
ATOM   11637 N  NE2   . HIS C 2 101 ? 128.301 80.654  138.280 1.00 30.20 ?  80  HIS C NE2   1 
ATOM   11638 N  N     . VAL C 2 102 ? 131.618 81.674  132.327 1.00 30.70 ?  81  VAL C N     1 
ATOM   11639 C  CA    . VAL C 2 102 ? 132.327 81.305  131.105 1.00 31.47 ?  81  VAL C CA    1 
ATOM   11640 C  C     . VAL C 2 102 ? 133.828 81.502  131.305 1.00 32.45 ?  81  VAL C C     1 
ATOM   11641 O  O     . VAL C 2 102 ? 134.256 82.561  131.779 1.00 32.50 ?  81  VAL C O     1 
ATOM   11642 C  CB    . VAL C 2 102 ? 131.839 82.125  129.881 1.00 31.18 ?  81  VAL C CB    1 
ATOM   11643 C  CG1   . VAL C 2 102 ? 132.727 81.879  128.660 1.00 31.20 ?  81  VAL C CG1   1 
ATOM   11644 C  CG2   . VAL C 2 102 ? 130.397 81.771  129.546 1.00 31.28 ?  81  VAL C CG2   1 
ATOM   11645 N  N     . ASP C 2 103 ? 134.610 80.487  130.933 1.00 33.38 ?  82  ASP C N     1 
ATOM   11646 C  CA    . ASP C 2 103 ? 136.068 80.513  131.094 1.00 34.82 ?  82  ASP C CA    1 
ATOM   11647 C  C     . ASP C 2 103 ? 136.790 81.176  129.927 1.00 34.74 ?  82  ASP C C     1 
ATOM   11648 O  O     . ASP C 2 103 ? 136.406 81.002  128.764 1.00 35.00 ?  82  ASP C O     1 
ATOM   11649 C  CB    . ASP C 2 103 ? 136.617 79.093  131.301 1.00 35.82 ?  82  ASP C CB    1 
ATOM   11650 C  CG    . ASP C 2 103 ? 136.302 78.534  132.686 1.00 38.29 ?  82  ASP C CG    1 
ATOM   11651 O  OD1   . ASP C 2 103 ? 136.234 79.317  133.664 1.00 41.49 ?  82  ASP C OD1   1 
ATOM   11652 O  OD2   . ASP C 2 103 ? 136.124 77.306  132.798 1.00 41.10 -1 82  ASP C OD2   1 
ATOM   11653 N  N     . GLY C 2 104 ? 137.840 81.930  130.251 1.00 34.89 ?  83  GLY C N     1 
ATOM   11654 C  CA    . GLY C 2 104 ? 138.695 82.571  129.247 1.00 35.11 ?  83  GLY C CA    1 
ATOM   11655 C  C     . GLY C 2 104 ? 138.553 84.080  129.228 1.00 34.96 ?  83  GLY C C     1 
ATOM   11656 O  O     . GLY C 2 104 ? 137.450 84.598  129.036 1.00 34.57 ?  83  GLY C O     1 
ATOM   11657 N  N     . HIS C 2 105 ? 139.673 84.783  129.411 1.00 35.02 ?  84  HIS C N     1 
ATOM   11658 C  CA    . HIS C 2 105 ? 139.676 86.248  129.530 1.00 34.83 ?  84  HIS C CA    1 
ATOM   11659 C  C     . HIS C 2 105 ? 139.092 86.975  128.326 1.00 33.77 ?  84  HIS C C     1 
ATOM   11660 O  O     . HIS C 2 105 ? 138.439 88.009  128.482 1.00 33.25 ?  84  HIS C O     1 
ATOM   11661 C  CB    . HIS C 2 105 ? 141.077 86.783  129.850 1.00 36.09 ?  84  HIS C CB    1 
ATOM   11662 C  CG    . HIS C 2 105 ? 141.492 86.558  131.272 1.00 39.17 ?  84  HIS C CG    1 
ATOM   11663 N  ND1   . HIS C 2 105 ? 142.801 86.316  131.638 1.00 43.00 ?  84  HIS C ND1   1 
ATOM   11664 C  CD2   . HIS C 2 105 ? 140.768 86.516  132.418 1.00 41.84 ?  84  HIS C CD2   1 
ATOM   11665 C  CE1   . HIS C 2 105 ? 142.865 86.145  132.948 1.00 43.47 ?  84  HIS C CE1   1 
ATOM   11666 N  NE2   . HIS C 2 105 ? 141.645 86.262  133.445 1.00 43.10 ?  84  HIS C NE2   1 
ATOM   11667 N  N     . GLN C 2 106 ? 139.306 86.432  127.134 1.00 32.84 ?  85  GLN C N     1 
ATOM   11668 C  CA    . GLN C 2 106 ? 138.754 87.047  125.930 1.00 32.29 ?  85  GLN C CA    1 
ATOM   11669 C  C     . GLN C 2 106 ? 137.239 86.842  125.817 1.00 30.88 ?  85  GLN C C     1 
ATOM   11670 O  O     . GLN C 2 106 ? 136.514 87.767  125.432 1.00 30.44 ?  85  GLN C O     1 
ATOM   11671 C  CB    . GLN C 2 106 ? 139.461 86.538  124.683 1.00 32.85 ?  85  GLN C CB    1 
ATOM   11672 C  CG    . GLN C 2 106 ? 140.927 86.944  124.607 1.00 35.55 ?  85  GLN C CG    1 
ATOM   11673 C  CD    . GLN C 2 106 ? 141.622 86.334  123.417 1.00 38.12 ?  85  GLN C CD    1 
ATOM   11674 O  OE1   . GLN C 2 106 ? 141.038 86.211  122.341 1.00 39.96 ?  85  GLN C OE1   1 
ATOM   11675 N  NE2   . GLN C 2 106 ? 142.882 85.946  123.602 1.00 40.39 ?  85  GLN C NE2   1 
ATOM   11676 N  N     . ARG C 2 107 ? 136.769 85.639  126.144 1.00 29.75 ?  86  ARG C N     1 
ATOM   11677 C  CA    . ARG C 2 107 ? 135.327 85.368  126.169 1.00 28.87 ?  86  ARG C CA    1 
ATOM   11678 C  C     . ARG C 2 107 ? 134.657 86.268  127.198 1.00 28.16 ?  86  ARG C C     1 
ATOM   11679 O  O     . ARG C 2 107 ? 133.595 86.829  126.933 1.00 27.55 ?  86  ARG C O     1 
ATOM   11680 C  CB    . ARG C 2 107 ? 135.037 83.901  126.484 1.00 28.48 ?  86  ARG C CB    1 
ATOM   11681 C  CG    . ARG C 2 107 ? 135.378 82.962  125.340 1.00 29.86 ?  86  ARG C CG    1 
ATOM   11682 C  CD    . ARG C 2 107 ? 135.117 81.507  125.692 1.00 30.23 ?  86  ARG C CD    1 
ATOM   11683 N  NE    . ARG C 2 107 ? 135.021 80.733  124.461 1.00 33.04 ?  86  ARG C NE    1 
ATOM   11684 C  CZ    . ARG C 2 107 ? 134.461 79.539  124.358 1.00 31.54 ?  86  ARG C CZ    1 
ATOM   11685 N  NH1   . ARG C 2 107 ? 133.949 78.941  125.424 1.00 31.85 1  86  ARG C NH1   1 
ATOM   11686 N  NH2   . ARG C 2 107 ? 134.426 78.944  123.177 1.00 34.74 ?  86  ARG C NH2   1 
ATOM   11687 N  N     . LYS C 2 108 ? 135.290 86.414  128.361 1.00 27.65 ?  87  LYS C N     1 
ATOM   11688 C  CA    . LYS C 2 108 ? 134.770 87.302  129.406 1.00 27.96 ?  87  LYS C CA    1 
ATOM   11689 C  C     . LYS C 2 108 ? 134.746 88.763  128.981 1.00 27.75 ?  87  LYS C C     1 
ATOM   11690 O  O     . LYS C 2 108 ? 133.817 89.489  129.333 1.00 28.29 ?  87  LYS C O     1 
ATOM   11691 C  CB    . LYS C 2 108 ? 135.550 87.157  130.712 1.00 27.80 ?  87  LYS C CB    1 
ATOM   11692 C  CG    . LYS C 2 108 ? 135.334 85.829  131.408 1.00 29.04 ?  87  LYS C CG    1 
ATOM   11693 C  CD    . LYS C 2 108 ? 136.123 85.789  132.708 1.00 31.15 ?  87  LYS C CD    1 
ATOM   11694 C  CE    . LYS C 2 108 ? 136.108 84.403  133.324 1.00 32.05 ?  87  LYS C CE    1 
ATOM   11695 N  NZ    . LYS C 2 108 ? 134.813 84.139  134.000 1.00 30.88 1  87  LYS C NZ    1 
ATOM   11696 N  N     . ALA C 2 109 ? 135.758 89.193  128.227 1.00 27.69 ?  88  ALA C N     1 
ATOM   11697 C  CA    . ALA C 2 109 ? 135.808 90.572  127.724 1.00 27.46 ?  88  ALA C CA    1 
ATOM   11698 C  C     . ALA C 2 109 ? 134.663 90.889  126.758 1.00 26.87 ?  88  ALA C C     1 
ATOM   11699 O  O     . ALA C 2 109 ? 134.103 91.984  126.794 1.00 26.47 ?  88  ALA C O     1 
ATOM   11700 C  CB    . ALA C 2 109 ? 137.143 90.854  127.065 1.00 27.98 ?  88  ALA C CB    1 
ATOM   11701 N  N     . VAL C 2 110 ? 134.334 89.936  125.889 1.00 25.98 ?  89  VAL C N     1 
ATOM   11702 C  CA    . VAL C 2 110 ? 133.211 90.083  124.959 1.00 25.46 ?  89  VAL C CA    1 
ATOM   11703 C  C     . VAL C 2 110 ? 131.896 90.165  125.741 1.00 24.57 ?  89  VAL C C     1 
ATOM   11704 O  O     . VAL C 2 110 ? 131.096 91.082  125.533 1.00 23.62 ?  89  VAL C O     1 
ATOM   11705 C  CB    . VAL C 2 110 ? 133.170 88.927  123.929 1.00 25.80 ?  89  VAL C CB    1 
ATOM   11706 C  CG1   . VAL C 2 110 ? 131.868 88.943  123.117 1.00 25.44 ?  89  VAL C CG1   1 
ATOM   11707 C  CG2   . VAL C 2 110 ? 134.384 88.999  123.003 1.00 26.23 ?  89  VAL C CG2   1 
ATOM   11708 N  N     . LEU C 2 111 ? 131.697 89.227  126.664 1.00 24.33 ?  90  LEU C N     1 
ATOM   11709 C  CA    . LEU C 2 111 ? 130.471 89.203  127.462 1.00 23.93 ?  90  LEU C CA    1 
ATOM   11710 C  C     . LEU C 2 111 ? 130.311 90.437  128.350 1.00 23.77 ?  90  LEU C C     1 
ATOM   11711 O  O     . LEU C 2 111 ? 129.199 90.943  128.503 1.00 23.04 ?  90  LEU C O     1 
ATOM   11712 C  CB    . LEU C 2 111 ? 130.358 87.913  128.279 1.00 23.73 ?  90  LEU C CB    1 
ATOM   11713 C  CG    . LEU C 2 111 ? 130.244 86.634  127.445 1.00 24.50 ?  90  LEU C CG    1 
ATOM   11714 C  CD1   . LEU C 2 111 ? 130.608 85.411  128.271 1.00 24.02 ?  90  LEU C CD1   1 
ATOM   11715 C  CD2   . LEU C 2 111 ? 128.852 86.484  126.828 1.00 25.38 ?  90  LEU C CD2   1 
ATOM   11716 N  N     . ASN C 2 112 ? 131.415 90.910  128.939 1.00 24.24 ?  91  ASN C N     1 
ATOM   11717 C  CA    . ASN C 2 112 ? 131.405 92.172  129.696 1.00 24.95 ?  91  ASN C CA    1 
ATOM   11718 C  C     . ASN C 2 112 ? 131.043 93.384  128.842 1.00 24.25 ?  91  ASN C C     1 
ATOM   11719 O  O     . ASN C 2 112 ? 130.312 94.265  129.294 1.00 23.99 ?  91  ASN C O     1 
ATOM   11720 C  CB    . ASN C 2 112 ? 132.755 92.428  130.373 1.00 25.81 ?  91  ASN C CB    1 
ATOM   11721 C  CG    . ASN C 2 112 ? 132.860 91.760  131.716 1.00 29.96 ?  91  ASN C CG    1 
ATOM   11722 O  OD1   . ASN C 2 112 ? 132.526 92.359  132.740 1.00 35.44 ?  91  ASN C OD1   1 
ATOM   11723 N  ND2   . ASN C 2 112 ? 133.321 90.509  131.731 1.00 32.37 ?  91  ASN C ND2   1 
ATOM   11724 N  N     . PHE C 2 113 ? 131.587 93.440  127.627 1.00 23.60 ?  92  PHE C N     1 
ATOM   11725 C  CA    . PHE C 2 113 ? 131.253 94.509  126.693 1.00 23.32 ?  92  PHE C CA    1 
ATOM   11726 C  C     . PHE C 2 113 ? 129.762 94.485  126.327 1.00 22.63 ?  92  PHE C C     1 
ATOM   11727 O  O     . PHE C 2 113 ? 129.109 95.529  126.318 1.00 21.94 ?  92  PHE C O     1 
ATOM   11728 C  CB    . PHE C 2 113 ? 132.084 94.410  125.406 1.00 23.27 ?  92  PHE C CB    1 
ATOM   11729 C  CG    . PHE C 2 113 ? 131.960 95.620  124.522 1.00 24.66 ?  92  PHE C CG    1 
ATOM   11730 C  CD1   . PHE C 2 113 ? 132.826 96.711  124.686 1.00 25.72 ?  92  PHE C CD1   1 
ATOM   11731 C  CD2   . PHE C 2 113 ? 130.969 95.689  123.546 1.00 25.36 ?  92  PHE C CD2   1 
ATOM   11732 C  CE1   . PHE C 2 113 ? 132.704 97.845  123.883 1.00 25.92 ?  92  PHE C CE1   1 
ATOM   11733 C  CE2   . PHE C 2 113 ? 130.836 96.823  122.735 1.00 25.82 ?  92  PHE C CE2   1 
ATOM   11734 C  CZ    . PHE C 2 113 ? 131.703 97.904  122.907 1.00 25.80 ?  92  PHE C CZ    1 
ATOM   11735 N  N     . MET C 2 114 ? 129.250 93.295  126.004 1.00 22.03 ?  93  MET C N     1 
ATOM   11736 C  CA    . MET C 2 114 ? 127.821 93.116  125.705 1.00 22.14 ?  93  MET C CA    1 
ATOM   11737 C  C     . MET C 2 114 ? 126.926 93.550  126.879 1.00 21.64 ?  93  MET C C     1 
ATOM   11738 O  O     . MET C 2 114 ? 125.914 94.227  126.669 1.00 21.59 ?  93  MET C O     1 
ATOM   11739 C  CB    . MET C 2 114 ? 127.531 91.672  125.313 1.00 22.46 ?  93  MET C CB    1 
ATOM   11740 C  CG    . MET C 2 114 ? 128.134 91.268  123.977 1.00 23.80 ?  93  MET C CG    1 
ATOM   11741 S  SD    . MET C 2 114 ? 127.931 89.505  123.640 1.00 28.07 ?  93  MET C SD    1 
ATOM   11742 C  CE    . MET C 2 114 ? 128.420 89.477  121.895 1.00 26.42 ?  93  MET C CE    1 
ATOM   11743 N  N     . ALA C 2 115 ? 127.320 93.189  128.106 1.00 20.98 ?  94  ALA C N     1 
ATOM   11744 C  CA    . ALA C 2 115 ? 126.619 93.631  129.326 1.00 20.58 ?  94  ALA C CA    1 
ATOM   11745 C  C     . ALA C 2 115 ? 126.548 95.151  129.456 1.00 21.01 ?  94  ALA C C     1 
ATOM   11746 O  O     . ALA C 2 115 ? 125.500 95.717  129.820 1.00 21.06 ?  94  ALA C O     1 
ATOM   11747 C  CB    . ALA C 2 115 ? 127.288 93.017  130.579 1.00 20.83 ?  94  ALA C CB    1 
ATOM   11748 N  N     . MET C 2 116 ? 127.673 95.813  129.194 1.00 20.36 ?  95  MET C N     1 
ATOM   11749 C  CA    . MET C 2 116 ? 127.729 97.263  129.235 1.00 20.83 ?  95  MET C CA    1 
ATOM   11750 C  C     . MET C 2 116 ? 126.752 97.867  128.213 1.00 20.55 ?  95  MET C C     1 
ATOM   11751 O  O     . MET C 2 116 ? 126.003 98.789  128.530 1.00 20.70 ?  95  MET C O     1 
ATOM   11752 C  CB    . MET C 2 116 ? 129.168 97.737  128.994 1.00 20.64 ?  95  MET C CB    1 
ATOM   11753 C  CG    . MET C 2 116 ? 129.348 99.252  128.887 1.00 21.42 ?  95  MET C CG    1 
ATOM   11754 S  SD    . MET C 2 116 ? 128.904 99.881  127.255 1.00 22.51 ?  95  MET C SD    1 
ATOM   11755 C  CE    . MET C 2 116 ? 130.060 99.002  126.202 1.00 20.66 ?  95  MET C CE    1 
ATOM   11756 N  N     . MET C 2 117 ? 126.752 97.325  126.999 1.00 20.50 ?  96  MET C N     1 
ATOM   11757 C  CA    . MET C 2 117 ? 125.851 97.802  125.958 1.00 21.22 ?  96  MET C CA    1 
ATOM   11758 C  C     . MET C 2 117 ? 124.392 97.715  126.402 1.00 21.11 ?  96  MET C C     1 
ATOM   11759 O  O     . MET C 2 117 ? 123.630 98.664  126.198 1.00 20.71 ?  96  MET C O     1 
ATOM   11760 C  CB    . MET C 2 117 ? 126.074 97.050  124.640 1.00 21.35 ?  96  MET C CB    1 
ATOM   11761 C  CG    . MET C 2 117 ? 127.394 97.409  123.888 1.00 22.54 ?  96  MET C CG    1 
ATOM   11762 S  SD    . MET C 2 117 ? 127.650 99.164  123.536 1.00 24.89 ?  96  MET C SD    1 
ATOM   11763 C  CE    . MET C 2 117 ? 126.506 99.420  122.180 1.00 24.95 ?  96  MET C CE    1 
ATOM   11764 N  N     . GLU C 2 118 ? 124.021 96.596  127.025 1.00 21.18 ?  97  GLU C N     1 
ATOM   11765 C  CA    . GLU C 2 118 ? 122.648 96.374  127.490 1.00 21.99 ?  97  GLU C CA    1 
ATOM   11766 C  C     . GLU C 2 118 ? 122.142 97.496  128.398 1.00 22.10 ?  97  GLU C C     1 
ATOM   11767 O  O     . GLU C 2 118 ? 121.103 98.100  128.121 1.00 22.22 ?  97  GLU C O     1 
ATOM   11768 C  CB    . GLU C 2 118 ? 122.493 95.023  128.208 1.00 22.01 ?  97  GLU C CB    1 
ATOM   11769 C  CG    . GLU C 2 118 ? 122.967 93.771  127.459 1.00 24.38 ?  97  GLU C CG    1 
ATOM   11770 C  CD    . GLU C 2 118 ? 122.259 93.500  126.126 1.00 26.32 ?  97  GLU C CD    1 
ATOM   11771 O  OE1   . GLU C 2 118 ? 121.850 94.442  125.432 1.00 29.86 ?  97  GLU C OE1   1 
ATOM   11772 O  OE2   . GLU C 2 118 ? 122.157 92.323  125.740 1.00 29.19 -1 97  GLU C OE2   1 
ATOM   11773 N  N     . ASN C 2 119 ? 122.866 97.779  129.479 1.00 22.26 ?  98  ASN C N     1 
ATOM   11774 C  CA    . ASN C 2 119 ? 122.358 98.745  130.454 1.00 21.91 ?  98  ASN C CA    1 
ATOM   11775 C  C     . ASN C 2 119 ? 122.899 100.179 130.360 1.00 22.41 ?  98  ASN C C     1 
ATOM   11776 O  O     . ASN C 2 119 ? 122.202 101.124 130.725 1.00 23.07 ?  98  ASN C O     1 
ATOM   11777 C  CB    . ASN C 2 119 ? 122.341 98.182  131.892 1.00 21.93 ?  98  ASN C CB    1 
ATOM   11778 C  CG    . ASN C 2 119 ? 123.718 97.851  132.427 1.00 21.31 ?  98  ASN C CG    1 
ATOM   11779 O  OD1   . ASN C 2 119 ? 124.729 97.995  131.737 1.00 21.88 ?  98  ASN C OD1   1 
ATOM   11780 N  ND2   . ASN C 2 119 ? 123.764 97.411  133.683 1.00 21.73 ?  98  ASN C ND2   1 
ATOM   11781 N  N     . ALA C 2 120 ? 124.132 100.336 129.886 1.00 22.75 ?  99  ALA C N     1 
ATOM   11782 C  CA    . ALA C 2 120 ? 124.731 101.662 129.734 1.00 23.12 ?  99  ALA C CA    1 
ATOM   11783 C  C     . ALA C 2 120 ? 124.390 102.316 128.410 1.00 23.60 ?  99  ALA C C     1 
ATOM   11784 O  O     . ALA C 2 120 ? 124.432 103.546 128.311 1.00 24.14 ?  99  ALA C O     1 
ATOM   11785 C  CB    . ALA C 2 120 ? 126.260 101.618 129.940 1.00 23.28 ?  99  ALA C CB    1 
ATOM   11786 N  N     . VAL C 2 121 ? 124.047 101.512 127.398 1.00 23.23 ?  100 VAL C N     1 
ATOM   11787 C  CA    . VAL C 2 121 ? 123.708 102.076 126.077 1.00 23.74 ?  100 VAL C CA    1 
ATOM   11788 C  C     . VAL C 2 121 ? 122.254 101.843 125.664 1.00 23.62 ?  100 VAL C C     1 
ATOM   11789 O  O     . VAL C 2 121 ? 121.530 102.804 125.421 1.00 24.51 ?  100 VAL C O     1 
ATOM   11790 C  CB    . VAL C 2 121 ? 124.668 101.599 124.967 1.00 23.19 ?  100 VAL C CB    1 
ATOM   11791 C  CG1   . VAL C 2 121 ? 124.249 102.168 123.599 1.00 24.10 ?  100 VAL C CG1   1 
ATOM   11792 C  CG2   . VAL C 2 121 ? 126.111 102.009 125.301 1.00 23.48 ?  100 VAL C CG2   1 
ATOM   11793 N  N     . HIS C 2 122 ? 121.836 100.580 125.597 1.00 23.45 ?  101 HIS C N     1 
ATOM   11794 C  CA    . HIS C 2 122 ? 120.499 100.237 125.108 1.00 23.81 ?  101 HIS C CA    1 
ATOM   11795 C  C     . HIS C 2 122 ? 119.385 100.718 126.014 1.00 24.33 ?  101 HIS C C     1 
ATOM   11796 O  O     . HIS C 2 122 ? 118.501 101.452 125.560 1.00 24.80 ?  101 HIS C O     1 
ATOM   11797 C  CB    . HIS C 2 122 ? 120.341 98.735  124.889 1.00 23.30 ?  101 HIS C CB    1 
ATOM   11798 C  CG    . HIS C 2 122 ? 121.261 98.171  123.853 1.00 22.96 ?  101 HIS C CG    1 
ATOM   11799 N  ND1   . HIS C 2 122 ? 121.357 96.817  123.607 1.00 22.78 ?  101 HIS C ND1   1 
ATOM   11800 C  CD2   . HIS C 2 122 ? 122.149 98.772  123.027 1.00 23.25 ?  101 HIS C CD2   1 
ATOM   11801 C  CE1   . HIS C 2 122 ? 122.254 96.612  122.661 1.00 22.57 ?  101 HIS C CE1   1 
ATOM   11802 N  NE2   . HIS C 2 122 ? 122.749 97.780  122.291 1.00 21.75 ?  101 HIS C NE2   1 
ATOM   11803 N  N     . ALA C 2 123 ? 119.407 100.281 127.276 1.00 24.40 ?  102 ALA C N     1 
ATOM   11804 C  CA    . ALA C 2 123 ? 118.352 100.648 128.224 1.00 24.00 ?  102 ALA C CA    1 
ATOM   11805 C  C     . ALA C 2 123 ? 118.247 102.170 128.345 1.00 24.05 ?  102 ALA C C     1 
ATOM   11806 O  O     . ALA C 2 123 ? 117.144 102.710 128.405 1.00 23.89 ?  102 ALA C O     1 
ATOM   11807 C  CB    . ALA C 2 123 ? 118.587 99.999  129.587 1.00 23.73 ?  102 ALA C CB    1 
ATOM   11808 N  N     . LYS C 2 124 ? 119.391 102.851 128.359 1.00 24.36 ?  103 LYS C N     1 
ATOM   11809 C  CA    . LYS C 2 124 ? 119.425 104.315 128.469 1.00 24.31 ?  103 LYS C CA    1 
ATOM   11810 C  C     . LYS C 2 124 ? 118.862 105.049 127.247 1.00 23.84 ?  103 LYS C C     1 
ATOM   11811 O  O     . LYS C 2 124 ? 118.175 106.068 127.400 1.00 24.21 ?  103 LYS C O     1 
ATOM   11812 C  CB    . LYS C 2 124 ? 120.827 104.825 128.818 1.00 24.93 ?  103 LYS C CB    1 
ATOM   11813 C  CG    . LYS C 2 124 ? 120.852 106.323 129.159 1.00 26.37 ?  103 LYS C CG    1 
ATOM   11814 C  CD    . LYS C 2 124 ? 122.208 106.772 129.677 1.00 29.42 ?  103 LYS C CD    1 
ATOM   11815 C  CE    . LYS C 2 124 ? 122.250 108.294 129.842 1.00 31.51 ?  103 LYS C CE    1 
ATOM   11816 N  NZ    . LYS C 2 124 ? 122.126 109.009 128.537 1.00 32.37 1  103 LYS C NZ    1 
ATOM   11817 N  N     . SER C 2 125 ? 119.136 104.532 126.047 1.00 23.52 ?  104 SER C N     1 
ATOM   11818 C  CA    . SER C 2 125 ? 118.618 105.110 124.802 0.50 23.23 ?  104 SER C CA    1 
ATOM   11819 C  C     . SER C 2 125 ? 117.097 105.262 124.825 1.00 22.91 ?  104 SER C C     1 
ATOM   11820 O  O     . SER C 2 125 ? 116.554 106.213 124.280 1.00 22.33 ?  104 SER C O     1 
ATOM   11821 C  CB    . SER C 2 125 ? 119.022 104.255 123.595 0.50 23.25 ?  104 SER C CB    1 
ATOM   11822 O  OG    . SER C 2 125 ? 120.428 104.157 123.475 0.50 24.57 ?  104 SER C OG    1 
ATOM   11823 N  N     . TYR C 2 126 ? 116.405 104.308 125.443 1.00 22.72 ?  105 TYR C N     1 
ATOM   11824 C  CA    . TYR C 2 126 ? 114.945 104.389 125.506 1.00 23.34 ?  105 TYR C CA    1 
ATOM   11825 C  C     . TYR C 2 126 ? 114.490 105.589 126.302 1.00 23.32 ?  105 TYR C C     1 
ATOM   11826 O  O     . TYR C 2 126 ? 113.487 106.196 125.954 1.00 23.17 ?  105 TYR C O     1 
ATOM   11827 C  CB    . TYR C 2 126 ? 114.303 103.122 126.075 1.00 23.45 ?  105 TYR C CB    1 
ATOM   11828 C  CG    . TYR C 2 126 ? 114.660 101.859 125.327 1.00 25.16 ?  105 TYR C CG    1 
ATOM   11829 C  CD1   . TYR C 2 126 ? 114.323 101.694 123.986 1.00 26.75 ?  105 TYR C CD1   1 
ATOM   11830 C  CD2   . TYR C 2 126 ? 115.337 100.825 125.973 1.00 26.36 ?  105 TYR C CD2   1 
ATOM   11831 C  CE1   . TYR C 2 126 ? 114.671 100.525 123.298 1.00 28.22 ?  105 TYR C CE1   1 
ATOM   11832 C  CE2   . TYR C 2 126 ? 115.688 99.665  125.300 1.00 27.17 ?  105 TYR C CE2   1 
ATOM   11833 C  CZ    . TYR C 2 126 ? 115.340 99.514  123.971 1.00 29.26 ?  105 TYR C CZ    1 
ATOM   11834 O  OH    . TYR C 2 126 ? 115.678 98.351  123.307 1.00 30.76 ?  105 TYR C OH    1 
ATOM   11835 N  N     . SER C 2 127 ? 115.230 105.922 127.363 1.00 23.61 ?  106 SER C N     1 
ATOM   11836 C  CA    . SER C 2 127 ? 114.942 107.113 128.152 1.00 24.40 ?  106 SER C CA    1 
ATOM   11837 C  C     . SER C 2 127 ? 115.196 108.384 127.353 1.00 24.55 ?  106 SER C C     1 
ATOM   11838 O  O     . SER C 2 127 ? 114.496 109.366 127.542 1.00 24.74 ?  106 SER C O     1 
ATOM   11839 C  CB    . SER C 2 127 ? 115.731 107.139 129.460 1.00 24.54 ?  106 SER C CB    1 
ATOM   11840 O  OG    . SER C 2 127 ? 115.153 106.262 130.420 1.00 24.69 ?  106 SER C OG    1 
ATOM   11841 N  N     . ASN C 2 128 ? 116.198 108.363 126.474 1.00 25.28 ?  107 ASN C N     1 
ATOM   11842 C  CA    . ASN C 2 128 ? 116.448 109.498 125.579 1.00 25.88 ?  107 ASN C CA    1 
ATOM   11843 C  C     . ASN C 2 128 ? 115.247 109.708 124.667 1.00 25.48 ?  107 ASN C C     1 
ATOM   11844 O  O     . ASN C 2 128 ? 114.792 110.834 124.471 1.00 25.23 ?  107 ASN C O     1 
ATOM   11845 C  CB    . ASN C 2 128 ? 117.716 109.295 124.741 1.00 26.40 ?  107 ASN C CB    1 
ATOM   11846 C  CG    . ASN C 2 128 ? 118.998 109.536 125.527 1.00 27.90 ?  107 ASN C CG    1 
ATOM   11847 O  OD1   . ASN C 2 128 ? 119.062 109.303 126.735 1.00 30.62 ?  107 ASN C OD1   1 
ATOM   11848 N  ND2   . ASN C 2 128 ? 120.035 109.992 124.831 1.00 27.91 ?  107 ASN C ND2   1 
ATOM   11849 N  N     . ILE C 2 129 ? 114.732 108.612 124.120 1.00 25.44 ?  108 ILE C N     1 
ATOM   11850 C  CA    . ILE C 2 129 ? 113.530 108.680 123.289 1.00 25.48 ?  108 ILE C CA    1 
ATOM   11851 C  C     . ILE C 2 129 ? 112.335 109.195 124.107 1.00 25.93 ?  108 ILE C C     1 
ATOM   11852 O  O     . ILE C 2 129 ? 111.675 110.153 123.691 1.00 25.54 ?  108 ILE C O     1 
ATOM   11853 C  CB    . ILE C 2 129 ? 113.232 107.341 122.565 1.00 25.21 ?  108 ILE C CB    1 
ATOM   11854 C  CG1   . ILE C 2 129 ? 114.395 106.992 121.620 1.00 25.96 ?  108 ILE C CG1   1 
ATOM   11855 C  CG2   . ILE C 2 129 ? 111.896 107.421 121.796 1.00 24.43 ?  108 ILE C CG2   1 
ATOM   11856 C  CD1   . ILE C 2 129 ? 114.373 105.574 121.052 1.00 26.11 ?  108 ILE C CD1   1 
ATOM   11857 N  N     . PHE C 2 130 ? 112.074 108.584 125.267 1.00 26.04 ?  109 PHE C N     1 
ATOM   11858 C  CA    . PHE C 2 130 ? 110.966 109.013 126.141 1.00 26.66 ?  109 PHE C CA    1 
ATOM   11859 C  C     . PHE C 2 130 ? 111.050 110.498 126.507 1.00 27.38 ?  109 PHE C C     1 
ATOM   11860 O  O     . PHE C 2 130 ? 110.042 111.220 126.456 1.00 27.22 ?  109 PHE C O     1 
ATOM   11861 C  CB    . PHE C 2 130 ? 110.925 108.192 127.449 1.00 26.98 ?  109 PHE C CB    1 
ATOM   11862 C  CG    . PHE C 2 130 ? 110.484 106.759 127.281 1.00 27.46 ?  109 PHE C CG    1 
ATOM   11863 C  CD1   . PHE C 2 130 ? 109.619 106.381 126.261 1.00 28.57 ?  109 PHE C CD1   1 
ATOM   11864 C  CD2   . PHE C 2 130 ? 110.929 105.783 128.174 1.00 28.51 ?  109 PHE C CD2   1 
ATOM   11865 C  CE1   . PHE C 2 130 ? 109.218 105.054 126.118 1.00 29.17 ?  109 PHE C CE1   1 
ATOM   11866 C  CE2   . PHE C 2 130 ? 110.527 104.447 128.045 1.00 29.27 ?  109 PHE C CE2   1 
ATOM   11867 C  CZ    . PHE C 2 130 ? 109.668 104.080 127.021 1.00 28.83 ?  109 PHE C CZ    1 
ATOM   11868 N  N     . MET C 2 131 ? 112.248 110.956 126.874 1.00 27.52 ?  110 MET C N     1 
ATOM   11869 C  CA    . MET C 2 131 ? 112.426 112.334 127.344 1.00 29.07 ?  110 MET C CA    1 
ATOM   11870 C  C     . MET C 2 131 ? 112.213 113.372 126.255 1.00 29.58 ?  110 MET C C     1 
ATOM   11871 O  O     . MET C 2 131 ? 111.846 114.511 126.544 1.00 30.07 ?  110 MET C O     1 
ATOM   11872 C  CB    . MET C 2 131 ? 113.790 112.533 127.999 1.00 28.96 ?  110 MET C CB    1 
ATOM   11873 C  CG    . MET C 2 131 ? 113.844 112.028 129.426 1.00 31.09 ?  110 MET C CG    1 
ATOM   11874 S  SD    . MET C 2 131 ? 115.466 112.207 130.206 1.00 35.43 ?  110 MET C SD    1 
ATOM   11875 C  CE    . MET C 2 131 ? 116.475 111.081 129.247 1.00 33.13 ?  110 MET C CE    1 
ATOM   11876 N  N     . THR C 2 132 ? 112.439 112.966 125.012 1.00 30.25 ?  111 THR C N     1 
ATOM   11877 C  CA    . THR C 2 132 ? 112.191 113.815 123.851 1.00 30.97 ?  111 THR C CA    1 
ATOM   11878 C  C     . THR C 2 132 ? 110.696 113.909 123.527 1.00 31.36 ?  111 THR C C     1 
ATOM   11879 O  O     . THR C 2 132 ? 110.140 115.009 123.405 1.00 31.60 ?  111 THR C O     1 
ATOM   11880 C  CB    . THR C 2 132 ? 112.982 113.288 122.619 1.00 30.88 ?  111 THR C CB    1 
ATOM   11881 O  OG1   . THR C 2 132 ? 114.384 113.347 122.903 1.00 29.86 ?  111 THR C OG1   1 
ATOM   11882 C  CG2   . THR C 2 132 ? 112.695 114.118 121.357 1.00 31.44 ?  111 THR C CG2   1 
ATOM   11883 N  N     . LEU C 2 133 ? 110.052 112.752 123.404 1.00 31.34 ?  112 LEU C N     1 
ATOM   11884 C  CA    . LEU C 2 133 ? 108.682 112.678 122.892 1.00 31.68 ?  112 LEU C CA    1 
ATOM   11885 C  C     . LEU C 2 133 ? 107.563 112.896 123.915 1.00 31.96 ?  112 LEU C C     1 
ATOM   11886 O  O     . LEU C 2 133 ? 106.497 113.404 123.570 1.00 31.69 ?  112 LEU C O     1 
ATOM   11887 C  CB    . LEU C 2 133 ? 108.463 111.342 122.188 1.00 31.35 ?  112 LEU C CB    1 
ATOM   11888 C  CG    . LEU C 2 133 ? 109.463 110.950 121.095 1.00 32.14 ?  112 LEU C CG    1 
ATOM   11889 C  CD1   . LEU C 2 133 ? 109.117 109.574 120.576 1.00 32.15 ?  112 LEU C CD1   1 
ATOM   11890 C  CD2   . LEU C 2 133 ? 109.482 111.976 119.964 1.00 32.39 ?  112 LEU C CD2   1 
ATOM   11891 N  N     . ALA C 2 134 ? 107.804 112.513 125.165 1.00 32.12 ?  113 ALA C N     1 
ATOM   11892 C  CA    . ALA C 2 134 ? 106.731 112.434 126.146 1.00 32.53 ?  113 ALA C CA    1 
ATOM   11893 C  C     . ALA C 2 134 ? 106.936 113.341 127.352 1.00 33.15 ?  113 ALA C C     1 
ATOM   11894 O  O     . ALA C 2 134 ? 108.069 113.565 127.772 1.00 32.47 ?  113 ALA C O     1 
ATOM   11895 C  CB    . ALA C 2 134 ? 106.536 110.981 126.599 1.00 32.20 ?  113 ALA C CB    1 
ATOM   11896 N  N     . PRO C 2 135 ? 105.827 113.853 127.923 1.00 34.27 ?  114 PRO C N     1 
ATOM   11897 C  CA    . PRO C 2 135 ? 105.906 114.597 129.174 1.00 35.35 ?  114 PRO C CA    1 
ATOM   11898 C  C     . PRO C 2 135 ? 106.175 113.654 130.341 1.00 36.17 ?  114 PRO C C     1 
ATOM   11899 O  O     . PRO C 2 135 ? 105.865 112.462 130.258 1.00 35.92 ?  114 PRO C O     1 
ATOM   11900 C  CB    . PRO C 2 135 ? 104.524 115.252 129.291 1.00 35.48 ?  114 PRO C CB    1 
ATOM   11901 C  CG    . PRO C 2 135 ? 103.618 114.416 128.474 1.00 34.94 ?  114 PRO C CG    1 
ATOM   11902 C  CD    . PRO C 2 135 ? 104.444 113.741 127.420 1.00 34.50 ?  114 PRO C CD    1 
ATOM   11903 N  N     . THR C 2 136 ? 106.757 114.189 131.409 1.00 37.30 ?  115 THR C N     1 
ATOM   11904 C  CA    . THR C 2 136 ? 107.183 113.399 132.569 1.00 38.49 ?  115 THR C CA    1 
ATOM   11905 C  C     . THR C 2 136 ? 106.114 112.455 133.139 1.00 38.48 ?  115 THR C C     1 
ATOM   11906 O  O     . THR C 2 136 ? 106.438 111.334 133.545 1.00 38.74 ?  115 THR C O     1 
ATOM   11907 C  CB    . THR C 2 136 ? 107.711 114.318 133.690 1.00 38.95 ?  115 THR C CB    1 
ATOM   11908 O  OG1   . THR C 2 136 ? 108.702 115.193 133.144 1.00 40.08 ?  115 THR C OG1   1 
ATOM   11909 C  CG2   . THR C 2 136 ? 108.329 113.510 134.831 1.00 39.82 ?  115 THR C CG2   1 
ATOM   11910 N  N     . GLU C 2 137 ? 104.858 112.906 133.163 1.00 38.89 ?  116 GLU C N     1 
ATOM   11911 C  CA    . GLU C 2 137 ? 103.757 112.123 133.740 1.00 38.65 ?  116 GLU C CA    1 
ATOM   11912 C  C     . GLU C 2 137 ? 103.472 110.862 132.932 1.00 37.38 ?  116 GLU C C     1 
ATOM   11913 O  O     . GLU C 2 137 ? 103.180 109.809 133.497 1.00 37.22 ?  116 GLU C O     1 
ATOM   11914 C  CB    . GLU C 2 137 ? 102.473 112.962 133.923 1.00 39.52 ?  116 GLU C CB    1 
ATOM   11915 C  CG    . GLU C 2 137 ? 101.729 113.376 132.632 1.00 41.90 ?  116 GLU C CG    1 
ATOM   11916 C  CD    . GLU C 2 137 ? 101.605 114.897 132.440 1.00 46.43 ?  116 GLU C CD    1 
ATOM   11917 O  OE1   . GLU C 2 137 ? 102.274 115.670 133.166 1.00 47.84 ?  116 GLU C OE1   1 
ATOM   11918 O  OE2   . GLU C 2 137 ? 100.826 115.320 131.550 1.00 47.52 -1 116 GLU C OE2   1 
ATOM   11919 N  N     . THR C 2 138 ? 103.573 110.979 131.611 1.00 36.05 ?  117 THR C N     1 
ATOM   11920 C  CA    . THR C 2 138 ? 103.387 109.849 130.714 1.00 34.88 ?  117 THR C CA    1 
ATOM   11921 C  C     . THR C 2 138 ? 104.550 108.874 130.865 1.00 33.58 ?  117 THR C C     1 
ATOM   11922 O  O     . THR C 2 138 ? 104.348 107.657 130.823 1.00 33.61 ?  117 THR C O     1 
ATOM   11923 C  CB    . THR C 2 138 ? 103.255 110.310 129.256 1.00 34.85 ?  117 THR C CB    1 
ATOM   11924 O  OG1   . THR C 2 138 ? 102.248 111.325 129.178 1.00 35.98 ?  117 THR C OG1   1 
ATOM   11925 C  CG2   . THR C 2 138 ? 102.866 109.149 128.351 1.00 34.92 ?  117 THR C CG2   1 
ATOM   11926 N  N     . ILE C 2 139 ? 105.754 109.413 131.045 1.00 32.29 ?  118 ILE C N     1 
ATOM   11927 C  CA    . ILE C 2 139 ? 106.935 108.594 131.313 1.00 31.19 ?  118 ILE C CA    1 
ATOM   11928 C  C     . ILE C 2 139 ? 106.781 107.841 132.648 1.00 30.85 ?  118 ILE C C     1 
ATOM   11929 O  O     . ILE C 2 139 ? 106.984 106.628 132.698 1.00 29.77 ?  118 ILE C O     1 
ATOM   11930 C  CB    . ILE C 2 139 ? 108.260 109.414 131.275 1.00 31.25 ?  118 ILE C CB    1 
ATOM   11931 C  CG1   . ILE C 2 139 ? 108.450 110.101 129.912 1.00 30.12 ?  118 ILE C CG1   1 
ATOM   11932 C  CG2   . ILE C 2 139 ? 109.470 108.521 131.588 1.00 30.21 ?  118 ILE C CG2   1 
ATOM   11933 C  CD1   . ILE C 2 139 ? 109.662 111.050 129.855 1.00 29.41 ?  118 ILE C CD1   1 
ATOM   11934 N  N     . ASN C 2 140 ? 106.404 108.560 133.711 1.00 31.17 ?  119 ASN C N     1 
ATOM   11935 C  CA    . ASN C 2 140 ? 106.160 107.945 135.026 1.00 31.76 ?  119 ASN C CA    1 
ATOM   11936 C  C     . ASN C 2 140 ? 105.116 106.825 134.955 1.00 31.25 ?  119 ASN C C     1 
ATOM   11937 O  O     . ASN C 2 140 ? 105.322 105.745 135.510 1.00 31.47 ?  119 ASN C O     1 
ATOM   11938 C  CB    . ASN C 2 140 ? 105.712 108.984 136.066 1.00 32.65 ?  119 ASN C CB    1 
ATOM   11939 C  CG    . ASN C 2 140 ? 106.829 109.928 136.498 1.00 35.14 ?  119 ASN C CG    1 
ATOM   11940 O  OD1   . ASN C 2 140 ? 108.017 109.592 136.455 1.00 36.75 ?  119 ASN C OD1   1 
ATOM   11941 N  ND2   . ASN C 2 140 ? 106.436 111.122 136.951 1.00 38.05 ?  119 ASN C ND2   1 
ATOM   11942 N  N     . GLU C 2 141 ? 104.013 107.096 134.260 1.00 30.96 ?  120 GLU C N     1 
ATOM   11943 C  CA    . GLU C 2 141 ? 102.921 106.140 134.089 1.00 30.36 ?  120 GLU C CA    1 
ATOM   11944 C  C     . GLU C 2 141 ? 103.361 104.866 133.361 1.00 28.60 ?  120 GLU C C     1 
ATOM   11945 O  O     . GLU C 2 141 ? 102.978 103.769 133.760 1.00 27.94 ?  120 GLU C O     1 
ATOM   11946 C  CB    . GLU C 2 141 ? 101.749 106.783 133.341 1.00 30.86 ?  120 GLU C CB    1 
ATOM   11947 C  CG    . GLU C 2 141 ? 100.891 107.717 134.188 1.00 34.89 ?  120 GLU C CG    1 
ATOM   11948 C  CD    . GLU C 2 141 ? 99.867  108.481 133.360 1.00 39.82 ?  120 GLU C CD    1 
ATOM   11949 O  OE1   . GLU C 2 141 ? 99.626  108.103 132.186 1.00 41.95 ?  120 GLU C OE1   1 
ATOM   11950 O  OE2   . GLU C 2 141 ? 99.295  109.460 133.883 1.00 41.94 -1 120 GLU C OE2   1 
ATOM   11951 N  N     . VAL C 2 142 ? 104.155 105.002 132.303 1.00 27.29 ?  121 VAL C N     1 
ATOM   11952 C  CA    . VAL C 2 142 ? 104.582 103.799 131.557 1.00 25.89 ?  121 VAL C CA    1 
ATOM   11953 C  C     . VAL C 2 142 ? 105.537 102.914 132.366 1.00 25.11 ?  121 VAL C C     1 
ATOM   11954 O  O     . VAL C 2 142 ? 105.500 101.689 132.252 1.00 24.23 ?  121 VAL C O     1 
ATOM   11955 C  CB    . VAL C 2 142 ? 105.109 104.107 130.113 1.00 25.99 ?  121 VAL C CB    1 
ATOM   11956 C  CG1   . VAL C 2 142 ? 106.595 104.477 130.097 1.00 25.21 ?  121 VAL C CG1   1 
ATOM   11957 C  CG2   . VAL C 2 142 ? 104.870 102.915 129.199 1.00 25.78 ?  121 VAL C CG2   1 
ATOM   11958 N  N     . PHE C 2 143 ? 106.381 103.520 133.195 1.00 24.69 ?  122 PHE C N     1 
ATOM   11959 C  CA    . PHE C 2 143 ? 107.257 102.724 134.068 1.00 24.77 ?  122 PHE C CA    1 
ATOM   11960 C  C     . PHE C 2 143 ? 106.464 102.044 135.198 1.00 24.99 ?  122 PHE C C     1 
ATOM   11961 O  O     . PHE C 2 143 ? 106.783 100.929 135.611 1.00 24.73 ?  122 PHE C O     1 
ATOM   11962 C  CB    . PHE C 2 143 ? 108.445 103.545 134.582 1.00 24.83 ?  122 PHE C CB    1 
ATOM   11963 C  CG    . PHE C 2 143 ? 109.543 103.711 133.553 1.00 25.12 ?  122 PHE C CG    1 
ATOM   11964 C  CD1   . PHE C 2 143 ? 110.372 102.642 133.221 1.00 26.58 ?  122 PHE C CD1   1 
ATOM   11965 C  CD2   . PHE C 2 143 ? 109.732 104.922 132.906 1.00 24.49 ?  122 PHE C CD2   1 
ATOM   11966 C  CE1   . PHE C 2 143 ? 111.378 102.787 132.257 1.00 26.96 ?  122 PHE C CE1   1 
ATOM   11967 C  CE2   . PHE C 2 143 ? 110.727 105.078 131.952 1.00 25.79 ?  122 PHE C CE2   1 
ATOM   11968 C  CZ    . PHE C 2 143 ? 111.554 104.009 131.621 1.00 26.45 ?  122 PHE C CZ    1 
ATOM   11969 N  N     . GLU C 2 144 ? 105.416 102.710 135.678 1.00 25.22 ?  123 GLU C N     1 
ATOM   11970 C  CA    . GLU C 2 144 ? 104.478 102.073 136.607 1.00 25.72 ?  123 GLU C CA    1 
ATOM   11971 C  C     . GLU C 2 144 ? 103.750 100.914 135.929 1.00 25.08 ?  123 GLU C C     1 
ATOM   11972 O  O     . GLU C 2 144 ? 103.553 99.857  136.531 1.00 24.67 ?  123 GLU C O     1 
ATOM   11973 C  CB    . GLU C 2 144 ? 103.492 103.089 137.176 1.00 26.23 ?  123 GLU C CB    1 
ATOM   11974 C  CG    . GLU C 2 144 ? 104.140 104.041 138.168 1.00 29.96 ?  123 GLU C CG    1 
ATOM   11975 C  CD    . GLU C 2 144 ? 104.877 103.304 139.273 1.00 33.82 ?  123 GLU C CD    1 
ATOM   11976 O  OE1   . GLU C 2 144 ? 104.208 102.612 140.070 1.00 36.54 ?  123 GLU C OE1   1 
ATOM   11977 O  OE2   . GLU C 2 144 ? 106.121 103.399 139.336 1.00 35.84 -1 123 GLU C OE2   1 
ATOM   11978 N  N     . TRP C 2 145 ? 103.381 101.113 134.666 1.00 24.21 ?  124 TRP C N     1 
ATOM   11979 C  CA    . TRP C 2 145 ? 102.726 100.076 133.870 1.00 23.99 ?  124 TRP C CA    1 
ATOM   11980 C  C     . TRP C 2 145 ? 103.584 98.818  133.675 1.00 23.95 ?  124 TRP C C     1 
ATOM   11981 O  O     . TRP C 2 145 ? 103.046 97.695  133.705 1.00 23.31 ?  124 TRP C O     1 
ATOM   11982 C  CB    . TRP C 2 145 ? 102.268 100.638 132.515 1.00 24.13 ?  124 TRP C CB    1 
ATOM   11983 C  CG    . TRP C 2 145 ? 101.852 99.571  131.529 1.00 24.37 ?  124 TRP C CG    1 
ATOM   11984 C  CD1   . TRP C 2 145 ? 100.601 99.022  131.374 1.00 24.76 ?  124 TRP C CD1   1 
ATOM   11985 C  CD2   . TRP C 2 145 ? 102.695 98.931  130.560 1.00 23.31 ?  124 TRP C CD2   1 
ATOM   11986 N  NE1   . TRP C 2 145 ? 100.625 98.073  130.369 1.00 24.97 ?  124 TRP C NE1   1 
ATOM   11987 C  CE2   . TRP C 2 145 ? 101.893 98.000  129.854 1.00 24.20 ?  124 TRP C CE2   1 
ATOM   11988 C  CE3   . TRP C 2 145 ? 104.051 99.046  130.227 1.00 23.76 ?  124 TRP C CE3   1 
ATOM   11989 C  CZ2   . TRP C 2 145 ? 102.407 97.193  128.830 1.00 23.41 ?  124 TRP C CZ2   1 
ATOM   11990 C  CZ3   . TRP C 2 145 ? 104.564 98.240  129.212 1.00 23.29 ?  124 TRP C CZ3   1 
ATOM   11991 C  CH2   . TRP C 2 145 ? 103.737 97.330  128.522 1.00 22.93 ?  124 TRP C CH2   1 
ATOM   11992 N  N     . VAL C 2 146 ? 104.896 98.971  133.469 1.00 23.35 ?  125 VAL C N     1 
ATOM   11993 C  CA    . VAL C 2 146 ? 105.740 97.751  133.379 1.00 23.53 ?  125 VAL C CA    1 
ATOM   11994 C  C     . VAL C 2 146 ? 105.703 96.920  134.668 1.00 23.73 ?  125 VAL C C     1 
ATOM   11995 O  O     . VAL C 2 146 ? 105.617 95.703  134.601 1.00 23.03 ?  125 VAL C O     1 
ATOM   11996 C  CB    . VAL C 2 146 ? 107.207 97.936  132.765 1.00 23.63 ?  125 VAL C CB    1 
ATOM   11997 C  CG1   . VAL C 2 146 ? 107.485 99.324  132.253 1.00 24.40 ?  125 VAL C CG1   1 
ATOM   11998 C  CG2   . VAL C 2 146 ? 108.336 97.404  133.668 1.00 22.97 ?  125 VAL C CG2   1 
ATOM   11999 N  N     . LYS C 2 147 ? 105.709 97.589  135.825 1.00 24.06 ?  126 LYS C N     1 
ATOM   12000 C  CA    . LYS C 2 147 ? 105.706 96.892  137.123 1.00 25.41 ?  126 LYS C CA    1 
ATOM   12001 C  C     . LYS C 2 147 ? 104.467 96.021  137.345 1.00 25.82 ?  126 LYS C C     1 
ATOM   12002 O  O     . LYS C 2 147 ? 104.554 94.982  138.005 1.00 26.08 ?  126 LYS C O     1 
ATOM   12003 C  CB    . LYS C 2 147 ? 105.821 97.888  138.279 1.00 25.49 ?  126 LYS C CB    1 
ATOM   12004 C  CG    . LYS C 2 147 ? 107.152 98.603  138.386 1.00 27.52 ?  126 LYS C CG    1 
ATOM   12005 C  CD    . LYS C 2 147 ? 107.086 99.618  139.521 1.00 30.43 ?  126 LYS C CD    1 
ATOM   12006 C  CE    . LYS C 2 147 ? 108.239 100.598 139.464 1.00 33.10 ?  126 LYS C CE    1 
ATOM   12007 N  NZ    . LYS C 2 147 ? 108.074 101.644 140.512 1.00 34.86 1  126 LYS C NZ    1 
ATOM   12008 N  N     . GLN C 2 148 ? 103.328 96.445  136.800 1.00 26.45 ?  127 GLN C N     1 
ATOM   12009 C  CA    . GLN C 2 148 ? 102.050 95.772  137.046 1.00 26.85 ?  127 GLN C CA    1 
ATOM   12010 C  C     . GLN C 2 148 ? 101.547 94.914  135.883 1.00 26.01 ?  127 GLN C C     1 
ATOM   12011 O  O     . GLN C 2 148 ? 100.539 94.219  136.025 1.00 26.12 ?  127 GLN C O     1 
ATOM   12012 C  CB    . GLN C 2 148 ? 100.968 96.780  137.479 1.00 28.08 ?  127 GLN C CB    1 
ATOM   12013 C  CG    . GLN C 2 148 ? 100.612 97.847  136.440 1.00 30.69 ?  127 GLN C CG    1 
ATOM   12014 C  CD    . GLN C 2 148 ? 99.750  97.316  135.297 1.00 34.64 ?  127 GLN C CD    1 
ATOM   12015 O  OE1   . GLN C 2 148 ? 100.187 97.277  134.133 1.00 33.80 ?  127 GLN C OE1   1 
ATOM   12016 N  NE2   . GLN C 2 148 ? 98.523  96.891  135.623 1.00 36.24 ?  127 GLN C NE2   1 
ATOM   12017 N  N     . ASN C 2 149 ? 102.235 94.967  134.739 1.00 24.97 ?  128 ASN C N     1 
ATOM   12018 C  CA    . ASN C 2 149 ? 101.841 94.181  133.574 1.00 24.03 ?  128 ASN C CA    1 
ATOM   12019 C  C     . ASN C 2 149 ? 102.218 92.719  133.758 1.00 24.13 ?  128 ASN C C     1 
ATOM   12020 O  O     . ASN C 2 149 ? 103.403 92.412  133.911 1.00 22.93 ?  128 ASN C O     1 
ATOM   12021 C  CB    . ASN C 2 149 ? 102.520 94.709  132.320 1.00 23.97 ?  128 ASN C CB    1 
ATOM   12022 C  CG    . ASN C 2 149 ? 102.035 94.014  131.070 1.00 23.94 ?  128 ASN C CG    1 
ATOM   12023 O  OD1   . ASN C 2 149 ? 102.583 92.992  130.662 1.00 24.85 ?  128 ASN C OD1   1 
ATOM   12024 N  ND2   . ASN C 2 149 ? 100.968 94.537  130.481 1.00 24.76 ?  128 ASN C ND2   1 
ATOM   12025 N  N     . LYS C 2 150 ? 101.226 91.826  133.715 1.00 24.32 ?  129 LYS C N     1 
ATOM   12026 C  CA    . LYS C 2 150 ? 101.453 90.414  134.083 1.00 24.77 ?  129 LYS C CA    1 
ATOM   12027 C  C     . LYS C 2 150 ? 102.321 89.612  133.110 1.00 24.54 ?  129 LYS C C     1 
ATOM   12028 O  O     . LYS C 2 150 ? 103.046 88.710  133.531 1.00 24.17 ?  129 LYS C O     1 
ATOM   12029 C  CB    . LYS C 2 150 ? 100.136 89.687  134.383 1.00 25.27 ?  129 LYS C CB    1 
ATOM   12030 C  CG    . LYS C 2 150 ? 99.161  89.586  133.228 1.00 28.72 ?  129 LYS C CG    1 
ATOM   12031 C  CD    . LYS C 2 150 ? 98.077  88.558  133.555 1.00 33.40 ?  129 LYS C CD    1 
ATOM   12032 C  CE    . LYS C 2 150 ? 96.831  88.784  132.721 1.00 36.77 ?  129 LYS C CE    1 
ATOM   12033 N  NZ    . LYS C 2 150 ? 95.716  87.914  133.208 1.00 39.66 1  129 LYS C NZ    1 
ATOM   12034 N  N     . TYR C 2 151 ? 102.240 89.938  131.816 1.00 23.92 ?  130 TYR C N     1 
ATOM   12035 C  CA    . TYR C 2 151 ? 103.043 89.251  130.795 1.00 24.12 ?  130 TYR C CA    1 
ATOM   12036 C  C     . TYR C 2 151 ? 104.511 89.642  130.857 1.00 23.54 ?  130 TYR C C     1 
ATOM   12037 O  O     . TYR C 2 151 ? 105.402 88.797  130.683 1.00 23.32 ?  130 TYR C O     1 
ATOM   12038 C  CB    . TYR C 2 151 ? 102.460 89.505  129.392 1.00 24.53 ?  130 TYR C CB    1 
ATOM   12039 C  CG    . TYR C 2 151 ? 100.953 89.367  129.364 1.00 25.83 ?  130 TYR C CG    1 
ATOM   12040 C  CD1   . TYR C 2 151 ? 100.345 88.140  129.628 1.00 26.57 ?  130 TYR C CD1   1 
ATOM   12041 C  CD2   . TYR C 2 151 ? 100.135 90.476  129.118 1.00 27.87 ?  130 TYR C CD2   1 
ATOM   12042 C  CE1   . TYR C 2 151 ? 98.961  88.005  129.627 1.00 29.65 ?  130 TYR C CE1   1 
ATOM   12043 C  CE2   . TYR C 2 151 ? 98.740  90.352  129.118 1.00 29.91 ?  130 TYR C CE2   1 
ATOM   12044 C  CZ    . TYR C 2 151 ? 98.166  89.115  129.375 1.00 31.19 ?  130 TYR C CZ    1 
ATOM   12045 O  OH    . TYR C 2 151 ? 96.793  88.974  129.378 1.00 34.44 ?  130 TYR C OH    1 
ATOM   12046 N  N     . LEU C 2 152 ? 104.758 90.924  131.104 1.00 23.38 ?  131 LEU C N     1 
ATOM   12047 C  CA    . LEU C 2 152 ? 106.109 91.438  131.232 1.00 23.43 ?  131 LEU C CA    1 
ATOM   12048 C  C     . LEU C 2 152 ? 106.748 90.912  132.522 1.00 23.37 ?  131 LEU C C     1 
ATOM   12049 O  O     . LEU C 2 152 ? 107.916 90.511  132.518 1.00 23.05 ?  131 LEU C O     1 
ATOM   12050 C  CB    . LEU C 2 152 ? 106.067 92.965  131.212 1.00 23.73 ?  131 LEU C CB    1 
ATOM   12051 C  CG    . LEU C 2 152 ? 107.007 93.853  130.404 1.00 24.71 ?  131 LEU C CG    1 
ATOM   12052 C  CD1   . LEU C 2 152 ? 107.733 93.156  129.241 1.00 21.63 ?  131 LEU C CD1   1 
ATOM   12053 C  CD2   . LEU C 2 152 ? 106.229 95.048  129.905 1.00 26.87 ?  131 LEU C CD2   1 
ATOM   12054 N  N     . GLN C 2 153 ? 105.992 90.911  133.624 1.00 22.80 ?  132 GLN C N     1 
ATOM   12055 C  CA    . GLN C 2 153 ? 106.486 90.286  134.861 1.00 22.70 ?  132 GLN C CA    1 
ATOM   12056 C  C     . GLN C 2 153 ? 106.755 88.785  134.713 1.00 22.54 ?  132 GLN C C     1 
ATOM   12057 O  O     . GLN C 2 153 ? 107.795 88.295  135.177 1.00 21.73 ?  132 GLN C O     1 
ATOM   12058 C  CB    . GLN C 2 153 ? 105.580 90.579  136.059 1.00 23.07 ?  132 GLN C CB    1 
ATOM   12059 C  CG    . GLN C 2 153 ? 105.530 92.065  136.415 1.00 21.83 ?  132 GLN C CG    1 
ATOM   12060 C  CD    . GLN C 2 153 ? 106.904 92.659  136.736 1.00 22.34 ?  132 GLN C CD    1 
ATOM   12061 O  OE1   . GLN C 2 153 ? 107.679 92.091  137.510 1.00 24.07 ?  132 GLN C OE1   1 
ATOM   12062 N  NE2   . GLN C 2 153 ? 107.199 93.813  136.153 1.00 22.26 ?  132 GLN C NE2   1 
ATOM   12063 N  N     . LYS C 2 154 ? 105.838 88.063  134.063 1.00 22.53 ?  133 LYS C N     1 
ATOM   12064 C  CA    . LYS C 2 154 ? 106.054 86.635  133.829 1.00 22.84 ?  133 LYS C CA    1 
ATOM   12065 C  C     . LYS C 2 154 ? 107.325 86.368  133.021 1.00 22.42 ?  133 LYS C C     1 
ATOM   12066 O  O     . LYS C 2 154 ? 108.100 85.491  133.386 1.00 21.90 ?  133 LYS C O     1 
ATOM   12067 C  CB    . LYS C 2 154 ? 104.829 85.939  133.191 1.00 22.96 ?  133 LYS C CB    1 
ATOM   12068 C  CG    . LYS C 2 154 ? 105.008 84.405  132.969 1.00 23.45 ?  133 LYS C CG    1 
ATOM   12069 C  CD    . LYS C 2 154 ? 105.158 83.607  134.282 1.00 26.74 ?  133 LYS C CD    1 
ATOM   12070 C  CE    . LYS C 2 154 ? 105.288 82.101  134.015 1.00 27.93 ?  133 LYS C CE    1 
ATOM   12071 N  NZ    . LYS C 2 154 ? 105.638 81.312  135.227 1.00 27.86 1  133 LYS C NZ    1 
ATOM   12072 N  N     . LYS C 2 155 ? 107.559 87.126  131.945 1.00 22.77 ?  134 LYS C N     1 
ATOM   12073 C  CA    . LYS C 2 155 ? 108.721 86.838  131.099 1.00 22.87 ?  134 LYS C CA    1 
ATOM   12074 C  C     . LYS C 2 155 ? 110.031 87.158  131.812 1.00 22.30 ?  134 LYS C C     1 
ATOM   12075 O  O     . LYS C 2 155 ? 110.990 86.372  131.723 1.00 21.89 ?  134 LYS C O     1 
ATOM   12076 C  CB    . LYS C 2 155 ? 108.620 87.462  129.687 1.00 23.33 ?  134 LYS C CB    1 
ATOM   12077 C  CG    . LYS C 2 155 ? 108.876 88.943  129.564 1.00 24.25 ?  134 LYS C CG    1 
ATOM   12078 C  CD    . LYS C 2 155 ? 108.754 89.409  128.103 1.00 26.87 ?  134 LYS C CD    1 
ATOM   12079 C  CE    . LYS C 2 155 ? 107.305 89.717  127.739 1.00 28.26 ?  134 LYS C CE    1 
ATOM   12080 N  NZ    . LYS C 2 155 ? 107.242 90.460  126.444 1.00 28.97 1  134 LYS C NZ    1 
ATOM   12081 N  N     . ALA C 2 156 ? 110.051 88.269  132.548 1.00 21.96 ?  135 ALA C N     1 
ATOM   12082 C  CA    . ALA C 2 156 ? 111.181 88.599  133.439 1.00 22.43 ?  135 ALA C CA    1 
ATOM   12083 C  C     . ALA C 2 156 ? 111.413 87.542  134.519 1.00 22.02 ?  135 ALA C C     1 
ATOM   12084 O  O     . ALA C 2 156 ? 112.553 87.168  134.778 1.00 22.60 ?  135 ALA C O     1 
ATOM   12085 C  CB    . ALA C 2 156 ? 110.991 89.983  134.097 1.00 22.05 ?  135 ALA C CB    1 
ATOM   12086 N  N     . GLN C 2 157 ? 110.339 87.078  135.159 1.00 21.97 ?  136 GLN C N     1 
ATOM   12087 C  CA    . GLN C 2 157 ? 110.449 86.034  136.187 1.00 22.10 ?  136 GLN C CA    1 
ATOM   12088 C  C     . GLN C 2 157 ? 111.120 84.793  135.635 1.00 21.87 ?  136 GLN C C     1 
ATOM   12089 O  O     . GLN C 2 157 ? 111.988 84.215  136.288 1.00 21.75 ?  136 GLN C O     1 
ATOM   12090 C  CB    . GLN C 2 157 ? 109.076 85.622  136.719 1.00 22.50 ?  136 GLN C CB    1 
ATOM   12091 C  CG    . GLN C 2 157 ? 108.479 86.561  137.757 1.00 23.55 ?  136 GLN C CG    1 
ATOM   12092 C  CD    . GLN C 2 157 ? 106.984 86.334  137.892 1.00 26.93 ?  136 GLN C CD    1 
ATOM   12093 O  OE1   . GLN C 2 157 ? 106.488 85.254  137.576 1.00 26.36 ?  136 GLN C OE1   1 
ATOM   12094 N  NE2   . GLN C 2 157 ? 106.257 87.355  138.333 1.00 28.09 ?  136 GLN C NE2   1 
ATOM   12095 N  N     . MET C 2 158 ? 110.694 84.386  134.440 1.00 21.38 ?  137 MET C N     1 
ATOM   12096 C  CA    . MET C 2 158 ? 111.178 83.161  133.820 1.00 22.08 ?  137 MET C CA    1 
ATOM   12097 C  C     . MET C 2 158 ? 112.634 83.269  133.384 1.00 21.70 ?  137 MET C C     1 
ATOM   12098 O  O     . MET C 2 158 ? 113.428 82.348  133.584 1.00 21.83 ?  137 MET C O     1 
ATOM   12099 C  CB    . MET C 2 158 ? 110.327 82.812  132.604 1.00 22.05 ?  137 MET C CB    1 
ATOM   12100 C  CG    . MET C 2 158 ? 108.944 82.240  132.939 1.00 23.93 ?  137 MET C CG    1 
ATOM   12101 S  SD    . MET C 2 158 ? 107.961 82.081  131.434 1.00 27.75 ?  137 MET C SD    1 
ATOM   12102 C  CE    . MET C 2 158 ? 108.853 80.742  130.629 1.00 26.00 ?  137 MET C CE    1 
ATOM   12103 N  N     . ILE C 2 159 ? 112.971 84.383  132.750 1.00 20.90 ?  138 ILE C N     1 
ATOM   12104 C  CA    . ILE C 2 159 ? 114.312 84.552  132.216 1.00 20.60 ?  138 ILE C CA    1 
ATOM   12105 C  C     . ILE C 2 159 ? 115.317 84.748  133.355 1.00 20.36 ?  138 ILE C C     1 
ATOM   12106 O  O     . ILE C 2 159 ? 116.337 84.058  133.403 1.00 19.65 ?  138 ILE C O     1 
ATOM   12107 C  CB    . ILE C 2 159 ? 114.375 85.703  131.169 1.00 20.17 ?  138 ILE C CB    1 
ATOM   12108 C  CG1   . ILE C 2 159 ? 113.556 85.344  129.915 1.00 20.66 ?  138 ILE C CG1   1 
ATOM   12109 C  CG2   . ILE C 2 159 ? 115.831 86.092  130.861 1.00 20.62 ?  138 ILE C CG2   1 
ATOM   12110 C  CD1   . ILE C 2 159 ? 114.042 84.153  129.085 1.00 22.17 ?  138 ILE C CD1   1 
ATOM   12111 N  N     . VAL C 2 160 ? 115.012 85.663  134.275 1.00 19.58 ?  139 VAL C N     1 
ATOM   12112 C  CA    . VAL C 2 160 ? 115.910 85.976  135.391 1.00 19.88 ?  139 VAL C CA    1 
ATOM   12113 C  C     . VAL C 2 160 ? 116.027 84.780  136.340 1.00 19.44 ?  139 VAL C C     1 
ATOM   12114 O  O     . VAL C 2 160 ? 117.069 84.566  136.951 1.00 19.88 ?  139 VAL C O     1 
ATOM   12115 C  CB    . VAL C 2 160 ? 115.466 87.257  136.186 1.00 19.52 ?  139 VAL C CB    1 
ATOM   12116 C  CG1   . VAL C 2 160 ? 116.379 87.497  137.401 1.00 20.75 ?  139 VAL C CG1   1 
ATOM   12117 C  CG2   . VAL C 2 160 ? 115.501 88.489  135.288 1.00 20.03 ?  139 VAL C CG2   1 
ATOM   12118 N  N     . GLY C 2 161 ? 114.959 83.997  136.456 1.00 19.13 ?  140 GLY C N     1 
ATOM   12119 C  CA    . GLY C 2 161 ? 114.998 82.815  137.301 1.00 18.05 ?  140 GLY C CA    1 
ATOM   12120 C  C     . GLY C 2 161 ? 116.055 81.855  136.819 1.00 17.86 ?  140 GLY C C     1 
ATOM   12121 O  O     . GLY C 2 161 ? 116.832 81.311  137.611 1.00 17.47 ?  140 GLY C O     1 
ATOM   12122 N  N     . LEU C 2 162 ? 116.078 81.634  135.509 1.00 17.92 ?  141 LEU C N     1 
ATOM   12123 C  CA    . LEU C 2 162 ? 117.089 80.772  134.906 1.00 18.32 ?  141 LEU C CA    1 
ATOM   12124 C  C     . LEU C 2 162 ? 118.523 81.324  135.071 1.00 18.55 ?  141 LEU C C     1 
ATOM   12125 O  O     . LEU C 2 162 ? 119.443 80.564  135.371 1.00 18.49 ?  141 LEU C O     1 
ATOM   12126 C  CB    . LEU C 2 162 ? 116.751 80.521  133.431 1.00 18.50 ?  141 LEU C CB    1 
ATOM   12127 C  CG    . LEU C 2 162 ? 115.527 79.624  133.220 1.00 19.32 ?  141 LEU C CG    1 
ATOM   12128 C  CD1   . LEU C 2 162 ? 115.026 79.734  131.784 1.00 20.38 ?  141 LEU C CD1   1 
ATOM   12129 C  CD2   . LEU C 2 162 ? 115.838 78.171  133.589 1.00 19.94 ?  141 LEU C CD2   1 
ATOM   12130 N  N     . TYR C 2 163 ? 118.707 82.633  134.913 1.00 19.16 ?  142 TYR C N     1 
ATOM   12131 C  CA    . TYR C 2 163 ? 120.017 83.257  135.184 1.00 20.16 ?  142 TYR C CA    1 
ATOM   12132 C  C     . TYR C 2 163 ? 120.488 83.003  136.605 1.00 20.78 ?  142 TYR C C     1 
ATOM   12133 O  O     . TYR C 2 163 ? 121.660 82.698  136.843 1.00 20.36 ?  142 TYR C O     1 
ATOM   12134 C  CB    . TYR C 2 163 ? 119.984 84.779  134.958 1.00 20.34 ?  142 TYR C CB    1 
ATOM   12135 C  CG    . TYR C 2 163 ? 119.741 85.214  133.520 1.00 22.46 ?  142 TYR C CG    1 
ATOM   12136 C  CD1   . TYR C 2 163 ? 120.043 84.379  132.449 1.00 23.88 ?  142 TYR C CD1   1 
ATOM   12137 C  CD2   . TYR C 2 163 ? 119.219 86.471  133.239 1.00 22.41 ?  142 TYR C CD2   1 
ATOM   12138 C  CE1   . TYR C 2 163 ? 119.814 84.789  131.123 1.00 25.93 ?  142 TYR C CE1   1 
ATOM   12139 C  CE2   . TYR C 2 163 ? 118.993 86.886  131.929 1.00 22.07 ?  142 TYR C CE2   1 
ATOM   12140 C  CZ    . TYR C 2 163 ? 119.299 86.050  130.882 1.00 25.19 ?  142 TYR C CZ    1 
ATOM   12141 O  OH    . TYR C 2 163 ? 119.063 86.487  129.595 1.00 27.43 ?  142 TYR C OH    1 
ATOM   12142 N  N     . LYS C 2 164 ? 119.569 83.129  137.554 1.00 21.39 ?  143 LYS C N     1 
ATOM   12143 C  CA    . LYS C 2 164 ? 119.948 83.020  138.953 1.00 22.49 ?  143 LYS C CA    1 
ATOM   12144 C  C     . LYS C 2 164 ? 120.055 81.572  139.425 1.00 22.49 ?  143 LYS C C     1 
ATOM   12145 O  O     . LYS C 2 164 ? 120.584 81.312  140.500 1.00 22.45 ?  143 LYS C O     1 
ATOM   12146 C  CB    . LYS C 2 164 ? 119.044 83.877  139.835 1.00 23.16 ?  143 LYS C CB    1 
ATOM   12147 C  CG    . LYS C 2 164 ? 119.263 85.366  139.578 1.00 26.08 ?  143 LYS C CG    1 
ATOM   12148 C  CD    . LYS C 2 164 ? 118.829 86.218  140.734 1.00 30.38 ?  143 LYS C CD    1 
ATOM   12149 C  CE    . LYS C 2 164 ? 119.234 87.656  140.524 1.00 32.69 ?  143 LYS C CE    1 
ATOM   12150 N  NZ    . LYS C 2 164 ? 118.754 88.498  141.655 1.00 35.60 1  143 LYS C NZ    1 
ATOM   12151 N  N     . ALA C 2 165 ? 119.622 80.634  138.581 1.00 22.02 ?  144 ALA C N     1 
ATOM   12152 C  CA    . ALA C 2 165 ? 119.754 79.223  138.890 1.00 22.69 ?  144 ALA C CA    1 
ATOM   12153 C  C     . ALA C 2 165 ? 121.112 78.636  138.467 1.00 23.20 ?  144 ALA C C     1 
ATOM   12154 O  O     . ALA C 2 165 ? 121.416 77.496  138.793 1.00 23.80 ?  144 ALA C O     1 
ATOM   12155 C  CB    . ALA C 2 165 ? 118.583 78.419  138.274 1.00 21.79 ?  144 ALA C CB    1 
ATOM   12156 N  N     . ILE C 2 166 ? 121.932 79.405  137.746 1.00 23.97 ?  145 ILE C N     1 
ATOM   12157 C  CA    . ILE C 2 166 ? 123.250 78.909  137.332 1.00 24.29 ?  145 ILE C CA    1 
ATOM   12158 C  C     . ILE C 2 166 ? 124.078 78.509  138.556 1.00 25.49 ?  145 ILE C C     1 
ATOM   12159 O  O     . ILE C 2 166 ? 124.153 79.251  139.531 1.00 25.82 ?  145 ILE C O     1 
ATOM   12160 C  CB    . ILE C 2 166 ? 124.046 79.940  136.479 1.00 24.22 ?  145 ILE C CB    1 
ATOM   12161 C  CG1   . ILE C 2 166 ? 123.294 80.293  135.200 1.00 23.45 ?  145 ILE C CG1   1 
ATOM   12162 C  CG2   . ILE C 2 166 ? 125.430 79.391  136.126 1.00 23.42 ?  145 ILE C CG2   1 
ATOM   12163 C  CD1   . ILE C 2 166 ? 123.864 81.535  134.467 1.00 21.99 ?  145 ILE C CD1   1 
ATOM   12164 N  N     . GLN C 2 167 ? 124.647 77.313  138.511 1.00 26.83 ?  146 GLN C N     1 
ATOM   12165 C  CA    . GLN C 2 167 ? 125.498 76.826  139.587 1.00 28.85 ?  146 GLN C CA    1 
ATOM   12166 C  C     . GLN C 2 167 ? 126.924 76.773  139.073 1.00 29.77 ?  146 GLN C C     1 
ATOM   12167 O  O     . GLN C 2 167 ? 127.166 76.343  137.940 1.00 29.74 ?  146 GLN C O     1 
ATOM   12168 C  CB    . GLN C 2 167 ? 125.054 75.436  140.067 1.00 28.99 ?  146 GLN C CB    1 
ATOM   12169 C  CG    . GLN C 2 167 ? 123.747 75.421  140.861 1.00 30.30 ?  146 GLN C CG    1 
ATOM   12170 C  CD    . GLN C 2 167 ? 123.882 76.049  142.242 1.00 33.32 ?  146 GLN C CD    1 
ATOM   12171 O  OE1   . GLN C 2 167 ? 124.990 76.333  142.702 1.00 34.63 ?  146 GLN C OE1   1 
ATOM   12172 N  NE2   . GLN C 2 167 ? 122.753 76.246  142.918 1.00 32.32 ?  146 GLN C NE2   1 
ATOM   12173 N  N     . LYS C 2 168 ? 127.861 77.215  139.903 1.00 31.29 ?  147 LYS C N     1 
ATOM   12174 C  CA    . LYS C 2 168 ? 129.278 77.205  139.541 1.00 33.14 ?  147 LYS C CA    1 
ATOM   12175 C  C     . LYS C 2 168 ? 129.682 75.802  139.110 1.00 33.79 ?  147 LYS C C     1 
ATOM   12176 O  O     . LYS C 2 168 ? 129.223 74.808  139.683 1.00 34.06 ?  147 LYS C O     1 
ATOM   12177 C  CB    . LYS C 2 168 ? 130.130 77.688  140.712 1.00 33.44 ?  147 LYS C CB    1 
ATOM   12178 C  CG    . LYS C 2 168 ? 131.520 78.203  140.344 1.00 35.61 ?  147 LYS C CG    1 
ATOM   12179 C  CD    . LYS C 2 168 ? 132.235 78.694  141.598 1.00 38.40 ?  147 LYS C CD    1 
ATOM   12180 C  CE    . LYS C 2 168 ? 133.500 79.476  141.285 1.00 40.48 ?  147 LYS C CE    1 
ATOM   12181 N  NZ    . LYS C 2 168 ? 134.700 78.604  141.385 1.00 41.56 1  147 LYS C NZ    1 
ATOM   12182 N  N     . ASP C 2 169 ? 130.500 75.733  138.065 1.00 35.10 ?  148 ASP C N     1 
ATOM   12183 C  CA    . ASP C 2 169 ? 130.995 74.459  137.516 1.00 36.27 ?  148 ASP C CA    1 
ATOM   12184 C  C     . ASP C 2 169 ? 129.911 73.481  137.060 1.00 36.29 ?  148 ASP C C     1 
ATOM   12185 O  O     . ASP C 2 169 ? 130.181 72.295  136.863 1.00 36.95 ?  148 ASP C O     1 
ATOM   12186 C  CB    . ASP C 2 169 ? 131.922 73.767  138.521 1.00 37.15 ?  148 ASP C CB    1 
ATOM   12187 C  CG    . ASP C 2 169 ? 133.233 74.486  138.694 1.00 38.94 ?  148 ASP C CG    1 
ATOM   12188 O  OD1   . ASP C 2 169 ? 133.624 75.256  137.786 1.00 41.71 ?  148 ASP C OD1   1 
ATOM   12189 O  OD2   . ASP C 2 169 ? 133.874 74.279  139.744 1.00 41.64 -1 148 ASP C OD2   1 
ATOM   12190 N  N     . ASP C 2 170 ? 128.687 73.969  136.897 1.00 35.87 ?  149 ASP C N     1 
ATOM   12191 C  CA    . ASP C 2 170 ? 127.601 73.122  136.420 1.00 35.24 ?  149 ASP C CA    1 
ATOM   12192 C  C     . ASP C 2 170 ? 127.176 73.642  135.053 1.00 34.12 ?  149 ASP C C     1 
ATOM   12193 O  O     . ASP C 2 170 ? 126.450 74.649  134.936 1.00 33.52 ?  149 ASP C O     1 
ATOM   12194 C  CB    . ASP C 2 170 ? 126.449 73.086  137.429 1.00 36.09 ?  149 ASP C CB    1 
ATOM   12195 C  CG    . ASP C 2 170 ? 125.206 72.370  136.899 1.00 38.39 ?  149 ASP C CG    1 
ATOM   12196 O  OD1   . ASP C 2 170 ? 125.277 71.648  135.877 1.00 42.06 ?  149 ASP C OD1   1 
ATOM   12197 O  OD2   . ASP C 2 170 ? 124.141 72.525  137.527 1.00 42.21 -1 149 ASP C OD2   1 
ATOM   12198 N  N     . GLU C 2 171 ? 127.659 72.946  134.028 1.00 32.48 ?  150 GLU C N     1 
ATOM   12199 C  CA    . GLU C 2 171 ? 127.503 73.373  132.649 1.00 30.93 ?  150 GLU C CA    1 
ATOM   12200 C  C     . GLU C 2 171 ? 126.052 73.295  132.165 1.00 29.37 ?  150 GLU C C     1 
ATOM   12201 O  O     . GLU C 2 171 ? 125.654 74.055  131.282 1.00 28.99 ?  150 GLU C O     1 
ATOM   12202 C  CB    . GLU C 2 171 ? 128.456 72.592  131.723 1.00 31.30 ?  150 GLU C CB    1 
ATOM   12203 C  CG    . GLU C 2 171 ? 128.114 71.103  131.476 1.00 33.64 ?  150 GLU C CG    1 
ATOM   12204 C  CD    . GLU C 2 171 ? 129.253 70.300  130.801 1.00 36.40 ?  150 GLU C CD    1 
ATOM   12205 O  OE1   . GLU C 2 171 ? 130.311 70.882  130.477 1.00 38.62 ?  150 GLU C OE1   1 
ATOM   12206 O  OE2   . GLU C 2 171 ? 129.089 69.076  130.595 1.00 37.42 -1 150 GLU C OE2   1 
ATOM   12207 N  N     . ILE C 2 172 ? 125.269 72.381  132.740 1.00 27.68 ?  151 ILE C N     1 
ATOM   12208 C  CA    . ILE C 2 172 ? 123.867 72.228  132.342 1.00 26.26 ?  151 ILE C CA    1 
ATOM   12209 C  C     . ILE C 2 172 ? 123.033 73.436  132.776 1.00 24.85 ?  151 ILE C C     1 
ATOM   12210 O  O     . ILE C 2 172 ? 122.238 73.940  131.985 1.00 23.53 ?  151 ILE C O     1 
ATOM   12211 C  CB    . ILE C 2 172 ? 123.247 70.896  132.844 1.00 26.53 ?  151 ILE C CB    1 
ATOM   12212 C  CG1   . ILE C 2 172 ? 123.997 69.690  132.253 1.00 27.59 ?  151 ILE C CG1   1 
ATOM   12213 C  CG2   . ILE C 2 172 ? 121.736 70.829  132.551 1.00 26.51 ?  151 ILE C CG2   1 
ATOM   12214 C  CD1   . ILE C 2 172 ? 123.861 69.507  130.735 1.00 26.91 ?  151 ILE C CD1   1 
ATOM   12215 N  N     . SER C 2 173 ? 123.218 73.909  134.011 1.00 23.58 ?  152 SER C N     1 
ATOM   12216 C  CA    . SER C 2 173 ? 122.489 75.097  134.449 1.00 22.36 ?  152 SER C CA    1 
ATOM   12217 C  C     . SER C 2 173 ? 122.904 76.315  133.622 1.00 21.79 ?  152 SER C C     1 
ATOM   12218 O  O     . SER C 2 173 ? 122.082 77.196  133.341 1.00 20.91 ?  152 SER C O     1 
ATOM   12219 C  CB    . SER C 2 173 ? 122.643 75.350  135.954 1.00 22.43 ?  152 SER C CB    1 
ATOM   12220 O  OG    . SER C 2 173 ? 123.998 75.567  136.314 1.00 24.02 ?  152 SER C OG    1 
ATOM   12221 N  N     . LEU C 2 174 ? 124.180 76.355  133.237 1.00 21.65 ?  153 LEU C N     1 
ATOM   12222 C  CA    . LEU C 2 174 ? 124.701 77.433  132.399 1.00 21.86 ?  153 LEU C CA    1 
ATOM   12223 C  C     . LEU C 2 174 ? 124.070 77.398  131.005 1.00 21.98 ?  153 LEU C C     1 
ATOM   12224 O  O     . LEU C 2 174 ? 123.636 78.439  130.506 1.00 21.64 ?  153 LEU C O     1 
ATOM   12225 C  CB    . LEU C 2 174 ? 126.242 77.410  132.326 1.00 21.71 ?  153 LEU C CB    1 
ATOM   12226 C  CG    . LEU C 2 174 ? 126.959 78.473  131.471 1.00 22.04 ?  153 LEU C CG    1 
ATOM   12227 C  CD1   . LEU C 2 174 ? 126.523 79.897  131.811 1.00 21.99 ?  153 LEU C CD1   1 
ATOM   12228 C  CD2   . LEU C 2 174 ? 128.477 78.326  131.622 1.00 23.37 ?  153 LEU C CD2   1 
ATOM   12229 N  N     . PHE C 2 175 ? 124.014 76.210  130.394 1.00 22.17 ?  154 PHE C N     1 
ATOM   12230 C  CA    . PHE C 2 175 ? 123.344 76.016  129.088 1.00 22.02 ?  154 PHE C CA    1 
ATOM   12231 C  C     . PHE C 2 175 ? 121.909 76.528  129.102 1.00 21.86 ?  154 PHE C C     1 
ATOM   12232 O  O     . PHE C 2 175 ? 121.460 77.188  128.156 1.00 21.62 ?  154 PHE C O     1 
ATOM   12233 C  CB    . PHE C 2 175 ? 123.329 74.531  128.694 1.00 22.08 ?  154 PHE C CB    1 
ATOM   12234 C  CG    . PHE C 2 175 ? 122.513 74.233  127.451 1.00 21.99 ?  154 PHE C CG    1 
ATOM   12235 C  CD1   . PHE C 2 175 ? 123.063 74.406  126.178 1.00 20.87 ?  154 PHE C CD1   1 
ATOM   12236 C  CD2   . PHE C 2 175 ? 121.185 73.793  127.558 1.00 20.82 ?  154 PHE C CD2   1 
ATOM   12237 C  CE1   . PHE C 2 175 ? 122.310 74.161  125.029 1.00 20.27 ?  154 PHE C CE1   1 
ATOM   12238 C  CE2   . PHE C 2 175 ? 120.419 73.533  126.418 1.00 20.19 ?  154 PHE C CE2   1 
ATOM   12239 C  CZ    . PHE C 2 175 ? 120.985 73.711  125.143 1.00 20.93 ?  154 PHE C CZ    1 
ATOM   12240 N  N     . LYS C 2 176 ? 121.180 76.180  130.163 1.00 21.98 ?  155 LYS C N     1 
ATOM   12241 C  CA    . LYS C 2 176 ? 119.777 76.581  130.295 1.00 21.79 ?  155 LYS C CA    1 
ATOM   12242 C  C     . LYS C 2 176 ? 119.632 78.106  130.325 1.00 21.70 ?  155 LYS C C     1 
ATOM   12243 O  O     . LYS C 2 176 ? 118.746 78.666  129.664 1.00 21.10 ?  155 LYS C O     1 
ATOM   12244 C  CB    . LYS C 2 176 ? 119.146 75.928  131.532 1.00 22.00 ?  155 LYS C CB    1 
ATOM   12245 C  CG    . LYS C 2 176 ? 119.019 74.413  131.435 1.00 21.93 ?  155 LYS C CG    1 
ATOM   12246 C  CD    . LYS C 2 176 ? 118.453 73.812  132.710 1.00 23.06 ?  155 LYS C CD    1 
ATOM   12247 C  CE    . LYS C 2 176 ? 118.269 72.314  132.584 1.00 24.91 ?  155 LYS C CE    1 
ATOM   12248 N  NZ    . LYS C 2 176 ? 118.030 71.677  133.922 1.00 25.16 1  155 LYS C NZ    1 
ATOM   12249 N  N     . ALA C 2 177 ? 120.505 78.771  131.088 1.00 21.49 ?  156 ALA C N     1 
ATOM   12250 C  CA    . ALA C 2 177 ? 120.532 80.231  131.111 1.00 20.60 ?  156 ALA C CA    1 
ATOM   12251 C  C     . ALA C 2 177 ? 120.935 80.853  129.755 1.00 20.37 ?  156 ALA C C     1 
ATOM   12252 O  O     . ALA C 2 177 ? 120.404 81.888  129.375 1.00 19.61 ?  156 ALA C O     1 
ATOM   12253 C  CB    . ALA C 2 177 ? 121.433 80.746  132.229 1.00 20.88 ?  156 ALA C CB    1 
ATOM   12254 N  N     . MET C 2 178 ? 121.855 80.215  129.033 1.00 20.70 ?  157 MET C N     1 
ATOM   12255 C  CA    . MET C 2 178 ? 122.253 80.693  127.698 1.00 21.06 ?  157 MET C CA    1 
ATOM   12256 C  C     . MET C 2 178 ? 121.130 80.548  126.689 1.00 20.83 ?  157 MET C C     1 
ATOM   12257 O  O     . MET C 2 178 ? 121.015 81.364  125.769 1.00 21.28 ?  157 MET C O     1 
ATOM   12258 C  CB    . MET C 2 178 ? 123.497 79.954  127.170 1.00 20.68 ?  157 MET C CB    1 
ATOM   12259 C  CG    . MET C 2 178 ? 124.806 80.246  127.901 1.00 21.61 ?  157 MET C CG    1 
ATOM   12260 S  SD    . MET C 2 178 ? 126.111 79.129  127.339 1.00 24.32 ?  157 MET C SD    1 
ATOM   12261 C  CE    . MET C 2 178 ? 127.564 79.924  128.056 1.00 23.64 ?  157 MET C CE    1 
ATOM   12262 N  N     . VAL C 2 179 ? 120.326 79.494  126.826 1.00 20.76 ?  158 VAL C N     1 
ATOM   12263 C  CA    . VAL C 2 179 ? 119.144 79.326  125.971 1.00 20.14 ?  158 VAL C CA    1 
ATOM   12264 C  C     . VAL C 2 179 ? 118.164 80.470  126.254 1.00 20.35 ?  158 VAL C C     1 
ATOM   12265 O  O     . VAL C 2 179 ? 117.624 81.089  125.333 1.00 19.82 ?  158 VAL C O     1 
ATOM   12266 C  CB    . VAL C 2 179 ? 118.435 77.967  126.211 1.00 20.07 ?  158 VAL C CB    1 
ATOM   12267 C  CG1   . VAL C 2 179 ? 117.079 77.933  125.501 1.00 20.07 ?  158 VAL C CG1   1 
ATOM   12268 C  CG2   . VAL C 2 179 ? 119.311 76.813  125.731 1.00 20.57 ?  158 VAL C CG2   1 
ATOM   12269 N  N     . ALA C 2 180 ? 117.950 80.737  127.539 1.00 19.89 ?  159 ALA C N     1 
ATOM   12270 C  CA    . ALA C 2 180 ? 117.087 81.834  127.977 1.00 20.50 ?  159 ALA C CA    1 
ATOM   12271 C  C     . ALA C 2 180 ? 117.578 83.174  127.402 1.00 20.67 ?  159 ALA C C     1 
ATOM   12272 O  O     . ALA C 2 180 ? 116.782 83.959  126.885 1.00 21.27 ?  159 ALA C O     1 
ATOM   12273 C  CB    . ALA C 2 180 ? 117.056 81.889  129.489 1.00 20.03 ?  159 ALA C CB    1 
ATOM   12274 N  N     . SER C 2 181 ? 118.886 83.413  127.486 1.00 20.78 ?  160 SER C N     1 
ATOM   12275 C  CA    . SER C 2 181 ? 119.504 84.624  126.932 1.00 21.26 ?  160 SER C CA    1 
ATOM   12276 C  C     . SER C 2 181 ? 119.337 84.723  125.409 1.00 21.19 ?  160 SER C C     1 
ATOM   12277 O  O     . SER C 2 181 ? 118.967 85.775  124.899 1.00 20.89 ?  160 SER C O     1 
ATOM   12278 C  CB    . SER C 2 181 ? 120.987 84.711  127.325 1.00 21.42 ?  160 SER C CB    1 
ATOM   12279 O  OG    . SER C 2 181 ? 121.569 85.924  126.867 1.00 23.69 ?  160 SER C OG    1 
ATOM   12280 N  N     . VAL C 2 182 ? 119.606 83.636  124.679 1.00 20.99 ?  161 VAL C N     1 
ATOM   12281 C  CA    . VAL C 2 182 ? 119.337 83.649  123.237 1.00 21.18 ?  161 VAL C CA    1 
ATOM   12282 C  C     . VAL C 2 182 ? 117.858 83.962  122.954 1.00 21.15 ?  161 VAL C C     1 
ATOM   12283 O  O     . VAL C 2 182 ? 117.548 84.769  122.063 1.00 21.18 ?  161 VAL C O     1 
ATOM   12284 C  CB    . VAL C 2 182 ? 119.780 82.329  122.527 1.00 21.11 ?  161 VAL C CB    1 
ATOM   12285 C  CG1   . VAL C 2 182 ? 119.296 82.307  121.079 1.00 21.75 ?  161 VAL C CG1   1 
ATOM   12286 C  CG2   . VAL C 2 182 ? 121.300 82.179  122.580 1.00 20.98 ?  161 VAL C CG2   1 
ATOM   12287 N  N     . TYR C 2 183 ? 116.939 83.347  123.711 1.00 21.10 ?  162 TYR C N     1 
ATOM   12288 C  CA    . TYR C 2 183 ? 115.508 83.633  123.527 1.00 21.21 ?  162 TYR C CA    1 
ATOM   12289 C  C     . TYR C 2 183 ? 115.149 85.090  123.814 1.00 21.38 ?  162 TYR C C     1 
ATOM   12290 O  O     . TYR C 2 183 ? 114.265 85.647  123.173 1.00 20.97 ?  162 TYR C O     1 
ATOM   12291 C  CB    . TYR C 2 183 ? 114.601 82.697  124.353 1.00 21.50 ?  162 TYR C CB    1 
ATOM   12292 C  CG    . TYR C 2 183 ? 114.557 81.280  123.848 1.00 22.20 ?  162 TYR C CG    1 
ATOM   12293 C  CD1   . TYR C 2 183 ? 114.912 80.975  122.536 1.00 23.80 ?  162 TYR C CD1   1 
ATOM   12294 C  CD2   . TYR C 2 183 ? 114.137 80.236  124.681 1.00 23.71 ?  162 TYR C CD2   1 
ATOM   12295 C  CE1   . TYR C 2 183 ? 114.872 79.658  122.064 1.00 25.52 ?  162 TYR C CE1   1 
ATOM   12296 C  CE2   . TYR C 2 183 ? 114.089 78.929  124.222 1.00 24.01 ?  162 TYR C CE2   1 
ATOM   12297 C  CZ    . TYR C 2 183 ? 114.465 78.643  122.921 1.00 25.47 ?  162 TYR C CZ    1 
ATOM   12298 O  OH    . TYR C 2 183 ? 114.435 77.342  122.464 1.00 25.37 ?  162 TYR C OH    1 
ATOM   12299 N  N     . LEU C 2 184 ? 115.825 85.690  124.782 1.00 22.12 ?  163 LEU C N     1 
ATOM   12300 C  CA    . LEU C 2 184 ? 115.655 87.132  125.052 1.00 23.80 ?  163 LEU C CA    1 
ATOM   12301 C  C     . LEU C 2 184 ? 116.218 87.963  123.891 1.00 24.21 ?  163 LEU C C     1 
ATOM   12302 O  O     . LEU C 2 184 ? 115.554 88.863  123.421 1.00 24.72 ?  163 LEU C O     1 
ATOM   12303 C  CB    . LEU C 2 184 ? 116.317 87.524  126.377 1.00 23.52 ?  163 LEU C CB    1 
ATOM   12304 C  CG    . LEU C 2 184 ? 116.185 88.963  126.916 1.00 24.91 ?  163 LEU C CG    1 
ATOM   12305 C  CD1   . LEU C 2 184 ? 116.148 88.940  128.423 1.00 24.81 ?  163 LEU C CD1   1 
ATOM   12306 C  CD2   . LEU C 2 184 ? 117.299 89.900  126.426 1.00 26.39 ?  163 LEU C CD2   1 
ATOM   12307 N  N     . GLU C 2 185 ? 117.431 87.637  123.425 1.00 25.17 ?  164 GLU C N     1 
ATOM   12308 C  CA    . GLU C 2 185 ? 118.113 88.427  122.387 1.00 25.30 ?  164 GLU C CA    1 
ATOM   12309 C  C     . GLU C 2 185 ? 117.420 88.363  121.016 1.00 25.07 ?  164 GLU C C     1 
ATOM   12310 O  O     . GLU C 2 185 ? 117.276 89.382  120.319 1.00 24.49 ?  164 GLU C O     1 
ATOM   12311 C  CB    . GLU C 2 185 ? 119.577 87.961  122.210 1.00 26.17 ?  164 GLU C CB    1 
ATOM   12312 C  CG    . GLU C 2 185 ? 120.496 88.208  123.427 1.00 27.05 ?  164 GLU C CG    1 
ATOM   12313 C  CD    . GLU C 2 185 ? 120.954 89.666  123.553 1.00 29.23 ?  164 GLU C CD    1 
ATOM   12314 O  OE1   . GLU C 2 185 ? 120.566 90.528  122.713 1.00 28.79 ?  164 GLU C OE1   1 
ATOM   12315 O  OE2   . GLU C 2 185 ? 121.743 89.963  124.480 1.00 28.65 -1 164 GLU C OE2   1 
ATOM   12316 N  N     . SER C 2 186 ? 117.023 87.154  120.639 1.00 24.23 ?  165 SER C N     1 
ATOM   12317 C  CA    . SER C 2 186 ? 116.688 86.827  119.259 1.00 24.71 ?  165 SER C CA    1 
ATOM   12318 C  C     . SER C 2 186 ? 115.204 86.558  119.035 1.00 24.51 ?  165 SER C C     1 
ATOM   12319 O  O     . SER C 2 186 ? 114.772 86.422  117.893 1.00 24.87 ?  165 SER C O     1 
ATOM   12320 C  CB    . SER C 2 186 ? 117.495 85.601  118.810 1.00 25.06 ?  165 SER C CB    1 
ATOM   12321 O  OG    . SER C 2 186 ? 118.888 85.825  118.925 1.00 26.29 ?  165 SER C OG    1 
ATOM   12322 N  N     . PHE C 2 187 ? 114.439 86.466  120.119 1.00 24.71 ?  166 PHE C N     1 
ATOM   12323 C  CA    . PHE C 2 187 ? 113.001 86.207  120.046 1.00 25.69 ?  166 PHE C CA    1 
ATOM   12324 C  C     . PHE C 2 187 ? 112.177 87.265  120.796 1.00 25.87 ?  166 PHE C C     1 
ATOM   12325 O  O     . PHE C 2 187 ? 111.369 87.955  120.171 1.00 26.03 ?  166 PHE C O     1 
ATOM   12326 C  CB    . PHE C 2 187 ? 112.666 84.788  120.548 1.00 25.54 ?  166 PHE C CB    1 
ATOM   12327 C  CG    . PHE C 2 187 ? 111.186 84.537  120.755 1.00 26.64 ?  166 PHE C CG    1 
ATOM   12328 C  CD1   . PHE C 2 187 ? 110.285 84.619  119.686 1.00 25.90 ?  166 PHE C CD1   1 
ATOM   12329 C  CD2   . PHE C 2 187 ? 110.695 84.205  122.021 1.00 27.45 ?  166 PHE C CD2   1 
ATOM   12330 C  CE1   . PHE C 2 187 ? 108.909 84.389  119.878 1.00 25.64 ?  166 PHE C CE1   1 
ATOM   12331 C  CE2   . PHE C 2 187 ? 109.315 83.967  122.228 1.00 26.52 ?  166 PHE C CE2   1 
ATOM   12332 C  CZ    . PHE C 2 187 ? 108.428 84.059  121.152 1.00 27.18 ?  166 PHE C CZ    1 
ATOM   12333 N  N     . LEU C 2 188 ? 112.397 87.391  122.106 1.00 26.13 ?  167 LEU C N     1 
ATOM   12334 C  CA    . LEU C 2 188 ? 111.558 88.242  122.990 1.00 27.13 ?  167 LEU C CA    1 
ATOM   12335 C  C     . LEU C 2 188 ? 111.573 89.752  122.690 1.00 27.22 ?  167 LEU C C     1 
ATOM   12336 O  O     . LEU C 2 188 ? 110.575 90.445  122.933 1.00 28.03 ?  167 LEU C O     1 
ATOM   12337 C  CB    . LEU C 2 188 ? 111.927 88.037  124.468 1.00 26.89 ?  167 LEU C CB    1 
ATOM   12338 C  CG    . LEU C 2 188 ? 111.696 86.704  125.197 1.00 28.64 ?  167 LEU C CG    1 
ATOM   12339 C  CD1   . LEU C 2 188 ? 112.202 86.795  126.635 1.00 28.34 ?  167 LEU C CD1   1 
ATOM   12340 C  CD2   . LEU C 2 188 ? 110.238 86.279  125.184 1.00 27.90 ?  167 LEU C CD2   1 
ATOM   12341 N  N     . PHE C 2 189 ? 112.701 90.265  122.212 1.00 26.79 ?  168 PHE C N     1 
ATOM   12342 C  CA    . PHE C 2 189 ? 112.796 91.684  121.871 1.00 26.90 ?  168 PHE C CA    1 
ATOM   12343 C  C     . PHE C 2 189 ? 111.879 92.037  120.694 1.00 26.52 ?  168 PHE C C     1 
ATOM   12344 O  O     . PHE C 2 189 ? 111.524 93.208  120.503 1.00 26.02 ?  168 PHE C O     1 
ATOM   12345 C  CB    . PHE C 2 189 ? 114.239 92.074  121.492 1.00 27.03 ?  168 PHE C CB    1 
ATOM   12346 C  CG    . PHE C 2 189 ? 115.132 92.453  122.671 1.00 28.09 ?  168 PHE C CG    1 
ATOM   12347 C  CD1   . PHE C 2 189 ? 114.770 93.464  123.563 1.00 28.69 ?  168 PHE C CD1   1 
ATOM   12348 C  CD2   . PHE C 2 189 ? 116.371 91.846  122.837 1.00 29.15 ?  168 PHE C CD2   1 
ATOM   12349 C  CE1   . PHE C 2 189 ? 115.601 93.827  124.634 1.00 28.50 ?  168 PHE C CE1   1 
ATOM   12350 C  CE2   . PHE C 2 189 ? 117.218 92.197  123.904 1.00 30.19 ?  168 PHE C CE2   1 
ATOM   12351 C  CZ    . PHE C 2 189 ? 116.823 93.198  124.810 1.00 29.81 ?  168 PHE C CZ    1 
ATOM   12352 N  N     . TYR C 2 190 ? 111.512 91.036  119.894 1.00 26.18 ?  169 TYR C N     1 
ATOM   12353 C  CA    . TYR C 2 190 ? 110.953 91.333  118.580 1.00 26.24 ?  169 TYR C CA    1 
ATOM   12354 C  C     . TYR C 2 190 ? 109.484 91.784  118.545 1.00 25.94 ?  169 TYR C C     1 
ATOM   12355 O  O     . TYR C 2 190 ? 109.069 92.485  117.621 1.00 25.71 ?  169 TYR C O     1 
ATOM   12356 C  CB    . TYR C 2 190 ? 111.311 90.231  117.581 1.00 27.13 ?  169 TYR C CB    1 
ATOM   12357 C  CG    . TYR C 2 190 ? 112.758 90.380  117.163 1.00 28.07 ?  169 TYR C CG    1 
ATOM   12358 C  CD1   . TYR C 2 190 ? 113.792 89.838  117.935 1.00 29.54 ?  169 TYR C CD1   1 
ATOM   12359 C  CD2   . TYR C 2 190 ? 113.102 91.126  116.034 1.00 29.31 ?  169 TYR C CD2   1 
ATOM   12360 C  CE1   . TYR C 2 190 ? 115.131 90.003  117.568 1.00 30.44 ?  169 TYR C CE1   1 
ATOM   12361 C  CE2   . TYR C 2 190 ? 114.443 91.295  115.656 1.00 30.64 ?  169 TYR C CE2   1 
ATOM   12362 C  CZ    . TYR C 2 190 ? 115.449 90.735  116.432 1.00 30.40 ?  169 TYR C CZ    1 
ATOM   12363 O  OH    . TYR C 2 190 ? 116.766 90.906  116.071 1.00 28.85 ?  169 TYR C OH    1 
ATOM   12364 N  N     . SER C 2 191 ? 108.725 91.433  119.580 1.00 25.17 ?  170 SER C N     1 
ATOM   12365 C  CA    . SER C 2 191 ? 107.365 91.943  119.730 1.00 25.10 ?  170 SER C CA    1 
ATOM   12366 C  C     . SER C 2 191 ? 107.429 93.460  119.947 1.00 25.16 ?  170 SER C C     1 
ATOM   12367 O  O     . SER C 2 191 ? 106.507 94.187  119.562 1.00 25.30 ?  170 SER C O     1 
ATOM   12368 C  CB    . SER C 2 191 ? 106.644 91.248  120.886 1.00 24.56 ?  170 SER C CB    1 
ATOM   12369 O  OG    . SER C 2 191 ? 107.260 91.538  122.125 1.00 24.98 ?  170 SER C OG    1 
ATOM   12370 N  N     . GLY C 2 192 ? 108.533 93.907  120.557 1.00 24.32 ?  171 GLY C N     1 
ATOM   12371 C  CA    . GLY C 2 192 ? 108.838 95.315  120.767 1.00 23.97 ?  171 GLY C CA    1 
ATOM   12372 C  C     . GLY C 2 192 ? 109.429 96.000  119.545 1.00 23.85 ?  171 GLY C C     1 
ATOM   12373 O  O     . GLY C 2 192 ? 108.934 97.054  119.145 1.00 23.99 ?  171 GLY C O     1 
ATOM   12374 N  N     . PHE C 2 193 ? 110.461 95.401  118.947 1.00 23.28 ?  172 PHE C N     1 
ATOM   12375 C  CA    . PHE C 2 193 ? 111.120 95.967  117.755 1.00 23.85 ?  172 PHE C CA    1 
ATOM   12376 C  C     . PHE C 2 193 ? 110.184 96.200  116.569 1.00 23.72 ?  172 PHE C C     1 
ATOM   12377 O  O     . PHE C 2 193 ? 110.441 97.080  115.750 1.00 23.92 ?  172 PHE C O     1 
ATOM   12378 C  CB    . PHE C 2 193 ? 112.273 95.082  117.262 1.00 23.47 ?  172 PHE C CB    1 
ATOM   12379 C  CG    . PHE C 2 193 ? 113.513 95.130  118.126 1.00 24.32 ?  172 PHE C CG    1 
ATOM   12380 C  CD1   . PHE C 2 193 ? 113.784 96.226  118.946 1.00 22.28 ?  172 PHE C CD1   1 
ATOM   12381 C  CD2   . PHE C 2 193 ? 114.427 94.075  118.092 1.00 23.82 ?  172 PHE C CD2   1 
ATOM   12382 C  CE1   . PHE C 2 193 ? 114.934 96.268  119.744 1.00 23.41 ?  172 PHE C CE1   1 
ATOM   12383 C  CE2   . PHE C 2 193 ? 115.588 94.098  118.885 1.00 24.70 ?  172 PHE C CE2   1 
ATOM   12384 C  CZ    . PHE C 2 193 ? 115.844 95.204  119.712 1.00 24.87 ?  172 PHE C CZ    1 
ATOM   12385 N  N     . TYR C 2 194 ? 109.124 95.395  116.462 1.00 23.31 ?  173 TYR C N     1 
ATOM   12386 C  CA    . TYR C 2 194 ? 108.212 95.467  115.318 1.00 23.26 ?  173 TYR C CA    1 
ATOM   12387 C  C     . TYR C 2 194 ? 107.755 96.902  115.042 1.00 23.04 ?  173 TYR C C     1 
ATOM   12388 O  O     . TYR C 2 194 ? 107.777 97.361  113.896 1.00 23.47 ?  173 TYR C O     1 
ATOM   12389 C  CB    . TYR C 2 194 ? 106.978 94.568  115.511 1.00 23.13 ?  173 TYR C CB    1 
ATOM   12390 C  CG    . TYR C 2 194 ? 106.061 94.536  114.295 1.00 24.10 ?  173 TYR C CG    1 
ATOM   12391 C  CD1   . TYR C 2 194 ? 106.189 93.534  113.332 1.00 25.72 ?  173 TYR C CD1   1 
ATOM   12392 C  CD2   . TYR C 2 194 ? 105.088 95.516  114.098 1.00 27.04 ?  173 TYR C CD2   1 
ATOM   12393 C  CE1   . TYR C 2 194 ? 105.353 93.498  112.208 1.00 28.94 ?  173 TYR C CE1   1 
ATOM   12394 C  CE2   . TYR C 2 194 ? 104.250 95.496  112.967 1.00 27.84 ?  173 TYR C CE2   1 
ATOM   12395 C  CZ    . TYR C 2 194 ? 104.395 94.483  112.033 1.00 29.97 ?  173 TYR C CZ    1 
ATOM   12396 O  OH    . TYR C 2 194 ? 103.588 94.448  110.909 1.00 34.34 ?  173 TYR C OH    1 
ATOM   12397 N  N     . TYR C 2 195 ? 107.339 97.595  116.090 1.00 22.51 ?  174 TYR C N     1 
ATOM   12398 C  CA    . TYR C 2 195 ? 106.627 98.857  115.925 1.00 22.60 ?  174 TYR C CA    1 
ATOM   12399 C  C     . TYR C 2 195 ? 107.533 100.021 115.483 1.00 22.64 ?  174 TYR C C     1 
ATOM   12400 O  O     . TYR C 2 195 ? 107.175 100.729 114.535 1.00 22.39 ?  174 TYR C O     1 
ATOM   12401 C  CB    . TYR C 2 195 ? 105.813 99.179  117.179 1.00 22.32 ?  174 TYR C CB    1 
ATOM   12402 C  CG    . TYR C 2 195 ? 104.544 99.969  116.929 1.00 23.39 ?  174 TYR C CG    1 
ATOM   12403 C  CD1   . TYR C 2 195 ? 103.806 99.814  115.744 1.00 22.84 ?  174 TYR C CD1   1 
ATOM   12404 C  CD2   . TYR C 2 195 ? 104.059 100.844 117.898 1.00 22.23 ?  174 TYR C CD2   1 
ATOM   12405 C  CE1   . TYR C 2 195 ? 102.629 100.541 115.529 1.00 24.05 ?  174 TYR C CE1   1 
ATOM   12406 C  CE2   . TYR C 2 195 ? 102.878 101.563 117.700 1.00 24.11 ?  174 TYR C CE2   1 
ATOM   12407 C  CZ    . TYR C 2 195 ? 102.172 101.405 116.520 1.00 23.92 ?  174 TYR C CZ    1 
ATOM   12408 O  OH    . TYR C 2 195 ? 101.029 102.134 116.331 1.00 25.00 ?  174 TYR C OH    1 
ATOM   12409 N  N     . PRO C 2 196 ? 108.713 100.211 116.145 1.00 22.25 ?  175 PRO C N     1 
ATOM   12410 C  CA    . PRO C 2 196 ? 109.662 101.201 115.612 1.00 22.45 ?  175 PRO C CA    1 
ATOM   12411 C  C     . PRO C 2 196 ? 110.078 100.911 114.169 1.00 22.59 ?  175 PRO C C     1 
ATOM   12412 O  O     . PRO C 2 196 ? 110.227 101.852 113.381 1.00 22.19 ?  175 PRO C O     1 
ATOM   12413 C  CB    . PRO C 2 196 ? 110.878 101.092 116.544 1.00 22.25 ?  175 PRO C CB    1 
ATOM   12414 C  CG    . PRO C 2 196 ? 110.368 100.472 117.803 1.00 22.22 ?  175 PRO C CG    1 
ATOM   12415 C  CD    . PRO C 2 196 ? 109.197 99.607  117.408 1.00 22.32 ?  175 PRO C CD    1 
ATOM   12416 N  N     . LEU C 2 197 ? 110.251 99.630  113.827 1.00 21.92 ?  176 LEU C N     1 
ATOM   12417 C  CA    . LEU C 2 197 ? 110.605 99.245  112.459 1.00 22.35 ?  176 LEU C CA    1 
ATOM   12418 C  C     . LEU C 2 197 ? 109.459 99.533  111.484 1.00 22.60 ?  176 LEU C C     1 
ATOM   12419 O  O     . LEU C 2 197 ? 109.682 99.968  110.351 1.00 22.41 ?  176 LEU C O     1 
ATOM   12420 C  CB    . LEU C 2 197 ? 110.983 97.767  112.374 1.00 22.69 ?  176 LEU C CB    1 
ATOM   12421 C  CG    . LEU C 2 197 ? 112.223 97.238  113.108 1.00 23.68 ?  176 LEU C CG    1 
ATOM   12422 C  CD1   . LEU C 2 197 ? 112.346 95.723  112.878 1.00 23.70 ?  176 LEU C CD1   1 
ATOM   12423 C  CD2   . LEU C 2 197 ? 113.485 97.958  112.645 1.00 23.09 ?  176 LEU C CD2   1 
ATOM   12424 N  N     . TYR C 2 198 ? 108.233 99.284  111.941 1.00 22.64 ?  177 TYR C N     1 
ATOM   12425 C  CA    . TYR C 2 198 ? 107.034 99.505  111.145 1.00 22.92 ?  177 TYR C CA    1 
ATOM   12426 C  C     . TYR C 2 198 ? 106.919 100.998 110.784 1.00 23.68 ?  177 TYR C C     1 
ATOM   12427 O  O     . TYR C 2 198 ? 106.625 101.350 109.639 1.00 23.81 ?  177 TYR C O     1 
ATOM   12428 C  CB    . TYR C 2 198 ? 105.830 99.009  111.939 1.00 22.73 ?  177 TYR C CB    1 
ATOM   12429 C  CG    . TYR C 2 198 ? 104.472 99.185  111.316 1.00 22.91 ?  177 TYR C CG    1 
ATOM   12430 C  CD1   . TYR C 2 198 ? 104.054 98.364  110.269 1.00 23.49 ?  177 TYR C CD1   1 
ATOM   12431 C  CD2   . TYR C 2 198 ? 103.577 100.130 111.819 1.00 21.97 ?  177 TYR C CD2   1 
ATOM   12432 C  CE1   . TYR C 2 198 ? 102.785 98.502  109.707 1.00 23.57 ?  177 TYR C CE1   1 
ATOM   12433 C  CE2   . TYR C 2 198 ? 102.294 100.276 111.266 1.00 22.54 ?  177 TYR C CE2   1 
ATOM   12434 C  CZ    . TYR C 2 198 ? 101.912 99.462  110.210 1.00 22.88 ?  177 TYR C CZ    1 
ATOM   12435 O  OH    . TYR C 2 198 ? 100.651 99.580  109.656 1.00 23.17 ?  177 TYR C OH    1 
ATOM   12436 N  N     . PHE C 2 199 ? 107.196 101.871 111.746 1.00 23.50 ?  178 PHE C N     1 
ATOM   12437 C  CA    . PHE C 2 199 ? 107.209 103.308 111.473 1.00 24.60 ?  178 PHE C CA    1 
ATOM   12438 C  C     . PHE C 2 199 ? 108.385 103.774 110.604 1.00 24.72 ?  178 PHE C C     1 
ATOM   12439 O  O     . PHE C 2 199 ? 108.199 104.533 109.654 1.00 24.19 ?  178 PHE C O     1 
ATOM   12440 C  CB    . PHE C 2 199 ? 107.140 104.108 112.776 1.00 24.35 ?  178 PHE C CB    1 
ATOM   12441 C  CG    . PHE C 2 199 ? 105.773 104.127 113.393 1.00 26.36 ?  178 PHE C CG    1 
ATOM   12442 C  CD1   . PHE C 2 199 ? 104.643 104.368 112.611 1.00 28.53 ?  178 PHE C CD1   1 
ATOM   12443 C  CD2   . PHE C 2 199 ? 105.608 103.924 114.755 1.00 28.23 ?  178 PHE C CD2   1 
ATOM   12444 C  CE1   . PHE C 2 199 ? 103.366 104.381 113.182 1.00 29.37 ?  178 PHE C CE1   1 
ATOM   12445 C  CE2   . PHE C 2 199 ? 104.328 103.949 115.335 1.00 28.69 ?  178 PHE C CE2   1 
ATOM   12446 C  CZ    . PHE C 2 199 ? 103.217 104.174 114.550 1.00 28.43 ?  178 PHE C CZ    1 
ATOM   12447 N  N     . TYR C 2 200 ? 109.588 103.309 110.936 1.00 25.36 ?  179 TYR C N     1 
ATOM   12448 C  CA    . TYR C 2 200 ? 110.800 103.619 110.167 1.00 26.02 ?  179 TYR C CA    1 
ATOM   12449 C  C     . TYR C 2 200 ? 110.573 103.324 108.684 1.00 26.57 ?  179 TYR C C     1 
ATOM   12450 O  O     . TYR C 2 200 ? 110.915 104.131 107.814 1.00 26.30 ?  179 TYR C O     1 
ATOM   12451 C  CB    . TYR C 2 200 ? 111.979 102.785 110.687 1.00 26.19 ?  179 TYR C CB    1 
ATOM   12452 C  CG    . TYR C 2 200 ? 113.326 103.173 110.119 1.00 27.82 ?  179 TYR C CG    1 
ATOM   12453 C  CD1   . TYR C 2 200 ? 113.913 102.426 109.093 1.00 30.77 ?  179 TYR C CD1   1 
ATOM   12454 C  CD2   . TYR C 2 200 ? 114.022 104.280 110.612 1.00 29.20 ?  179 TYR C CD2   1 
ATOM   12455 C  CE1   . TYR C 2 200 ? 115.152 102.775 108.568 1.00 31.82 ?  179 TYR C CE1   1 
ATOM   12456 C  CE2   . TYR C 2 200 ? 115.259 104.641 110.096 1.00 30.44 ?  179 TYR C CE2   1 
ATOM   12457 C  CZ    . TYR C 2 200 ? 115.818 103.881 109.073 1.00 32.74 ?  179 TYR C CZ    1 
ATOM   12458 O  OH    . TYR C 2 200 ? 117.037 104.226 108.544 1.00 34.58 ?  179 TYR C OH    1 
ATOM   12459 N  N     . GLY C 2 201 ? 109.968 102.168 108.415 1.00 26.71 ?  180 GLY C N     1 
ATOM   12460 C  CA    . GLY C 2 201 ? 109.686 101.732 107.055 1.00 27.38 ?  180 GLY C CA    1 
ATOM   12461 C  C     . GLY C 2 201 ? 108.693 102.599 106.297 1.00 27.62 ?  180 GLY C C     1 
ATOM   12462 O  O     . GLY C 2 201 ? 108.639 102.529 105.081 1.00 28.25 ?  180 GLY C O     1 
ATOM   12463 N  N     . GLN C 2 202 ? 107.917 103.409 107.016 1.00 27.60 ?  181 GLN C N     1 
ATOM   12464 C  CA    . GLN C 2 202 ? 106.961 104.350 106.407 1.00 28.24 ?  181 GLN C CA    1 
ATOM   12465 C  C     . GLN C 2 202 ? 107.500 105.772 106.397 1.00 28.30 ?  181 GLN C C     1 
ATOM   12466 O  O     . GLN C 2 202 ? 106.774 106.702 106.040 1.00 27.98 ?  181 GLN C O     1 
ATOM   12467 C  CB    . GLN C 2 202 ? 105.647 104.386 107.192 1.00 27.90 ?  181 GLN C CB    1 
ATOM   12468 C  CG    . GLN C 2 202 ? 104.888 103.100 107.263 1.00 29.54 ?  181 GLN C CG    1 
ATOM   12469 C  CD    . GLN C 2 202 ? 103.678 103.219 108.163 1.00 31.54 ?  181 GLN C CD    1 
ATOM   12470 O  OE1   . GLN C 2 202 ? 102.705 103.901 107.830 1.00 32.11 ?  181 GLN C OE1   1 
ATOM   12471 N  NE2   . GLN C 2 202 ? 103.734 102.565 109.316 1.00 31.29 ?  181 GLN C NE2   1 
ATOM   12472 N  N     . GLY C 2 203 ? 108.748 105.938 106.834 1.00 28.14 ?  182 GLY C N     1 
ATOM   12473 C  CA    . GLY C 2 203 ? 109.377 107.247 106.923 1.00 28.38 ?  182 GLY C CA    1 
ATOM   12474 C  C     . GLY C 2 203 ? 108.900 108.054 108.112 1.00 28.71 ?  182 GLY C C     1 
ATOM   12475 O  O     . GLY C 2 203 ? 108.863 109.279 108.051 1.00 28.80 ?  182 GLY C O     1 
ATOM   12476 N  N     . LYS C 2 204 ? 108.521 107.363 109.186 1.00 28.24 ?  183 LYS C N     1 
ATOM   12477 C  CA    . LYS C 2 204 ? 108.026 108.012 110.389 1.00 28.48 ?  183 LYS C CA    1 
ATOM   12478 C  C     . LYS C 2 204 ? 108.894 107.639 111.588 1.00 27.82 ?  183 LYS C C     1 
ATOM   12479 O  O     . LYS C 2 204 ? 109.372 106.501 111.693 1.00 26.73 ?  183 LYS C O     1 
ATOM   12480 C  CB    . LYS C 2 204 ? 106.569 107.628 110.656 1.00 29.13 ?  183 LYS C CB    1 
ATOM   12481 C  CG    . LYS C 2 204 ? 105.586 108.128 109.597 1.00 30.41 ?  183 LYS C CG    1 
ATOM   12482 C  CD    . LYS C 2 204 ? 104.319 107.287 109.593 1.00 33.74 ?  183 LYS C CD    1 
ATOM   12483 C  CE    . LYS C 2 204 ? 103.296 107.835 108.585 1.00 36.26 ?  183 LYS C CE    1 
ATOM   12484 N  NZ    . LYS C 2 204 ? 102.046 107.022 108.613 1.00 39.17 1  183 LYS C NZ    1 
ATOM   12485 N  N     . LEU C 2 205 ? 109.088 108.606 112.483 1.00 27.77 ?  184 LEU C N     1 
ATOM   12486 C  CA    . LEU C 2 205 ? 109.918 108.430 113.681 1.00 27.79 ?  184 LEU C CA    1 
ATOM   12487 C  C     . LEU C 2 205 ? 111.292 107.851 113.330 1.00 27.85 ?  184 LEU C C     1 
ATOM   12488 O  O     . LEU C 2 205 ? 111.757 106.864 113.917 1.00 27.07 ?  184 LEU C O     1 
ATOM   12489 C  CB    . LEU C 2 205 ? 109.190 107.565 114.730 1.00 27.76 ?  184 LEU C CB    1 
ATOM   12490 C  CG    . LEU C 2 205 ? 107.810 108.071 115.169 1.00 28.62 ?  184 LEU C CG    1 
ATOM   12491 C  CD1   . LEU C 2 205 ? 107.138 107.080 116.097 1.00 29.18 ?  184 LEU C CD1   1 
ATOM   12492 C  CD2   . LEU C 2 205 ? 107.909 109.435 115.837 1.00 28.43 ?  184 LEU C CD2   1 
ATOM   12493 N  N     . MET C 2 206 ? 111.953 108.485 112.373 1.00 28.15 ?  185 MET C N     1 
ATOM   12494 C  CA    . MET C 2 206 ? 113.147 107.895 111.811 1.00 28.80 ?  185 MET C CA    1 
ATOM   12495 C  C     . MET C 2 206 ? 114.399 108.039 112.665 1.00 28.77 ?  185 MET C C     1 
ATOM   12496 O  O     . MET C 2 206 ? 115.316 107.230 112.540 1.00 28.79 ?  185 MET C O     1 
ATOM   12497 C  CB    . MET C 2 206 ? 113.351 108.392 110.392 1.00 29.96 ?  185 MET C CB    1 
ATOM   12498 C  CG    . MET C 2 206 ? 112.256 107.868 109.458 1.00 31.23 ?  185 MET C CG    1 
ATOM   12499 S  SD    . MET C 2 206 ? 112.770 108.004 107.767 1.00 40.10 ?  185 MET C SD    1 
ATOM   12500 C  CE    . MET C 2 206 ? 113.997 106.717 107.649 1.00 35.10 ?  185 MET C CE    1 
ATOM   12501 N  N     . GLN C 2 207 ? 114.431 109.035 113.545 1.00 28.62 ?  186 GLN C N     1 
ATOM   12502 C  CA    . GLN C 2 207 ? 115.575 109.207 114.447 1.00 29.10 ?  186 GLN C CA    1 
ATOM   12503 C  C     . GLN C 2 207 ? 115.542 108.168 115.570 1.00 28.52 ?  186 GLN C C     1 
ATOM   12504 O  O     . GLN C 2 207 ? 116.548 107.508 115.824 1.00 28.28 ?  186 GLN C O     1 
ATOM   12505 C  CB    . GLN C 2 207 ? 115.651 110.630 115.008 1.00 29.21 ?  186 GLN C CB    1 
ATOM   12506 C  CG    . GLN C 2 207 ? 115.880 111.710 113.949 1.00 31.41 ?  186 GLN C CG    1 
ATOM   12507 C  CD    . GLN C 2 207 ? 117.225 111.575 113.264 1.00 34.70 ?  186 GLN C CD    1 
ATOM   12508 O  OE1   . GLN C 2 207 ? 117.342 110.919 112.232 1.00 37.69 ?  186 GLN C OE1   1 
ATOM   12509 N  NE2   . GLN C 2 207 ? 118.256 112.170 113.853 1.00 34.75 ?  186 GLN C NE2   1 
ATOM   12510 N  N     . SER C 2 208 ? 114.382 108.029 116.224 1.00 28.38 ?  187 SER C N     1 
ATOM   12511 C  CA    . SER C 2 208 ? 114.128 106.943 117.179 1.00 28.25 ?  187 SER C CA    1 
ATOM   12512 C  C     . SER C 2 208 ? 114.387 105.599 116.508 1.00 28.00 ?  187 SER C C     1 
ATOM   12513 O  O     . SER C 2 208 ? 114.979 104.704 117.112 1.00 27.90 ?  187 SER C O     1 
ATOM   12514 C  CB    . SER C 2 208 ? 112.674 106.964 117.655 1.00 27.88 ?  187 SER C CB    1 
ATOM   12515 O  OG    . SER C 2 208 ? 112.362 108.162 118.334 1.00 30.27 ?  187 SER C OG    1 
ATOM   12516 N  N     . GLY C 2 209 ? 113.922 105.472 115.261 1.00 27.31 ?  188 GLY C N     1 
ATOM   12517 C  CA    . GLY C 2 209 ? 114.106 104.260 114.465 1.00 27.86 ?  188 GLY C CA    1 
ATOM   12518 C  C     . GLY C 2 209 ? 115.563 103.927 114.200 1.00 27.96 ?  188 GLY C C     1 
ATOM   12519 O  O     . GLY C 2 209 ? 115.940 102.750 114.163 1.00 27.84 ?  188 GLY C O     1 
ATOM   12520 N  N     . GLU C 2 210 ? 116.381 104.963 114.010 1.00 28.21 ?  189 GLU C N     1 
ATOM   12521 C  CA    . GLU C 2 210 ? 117.819 104.790 113.828 1.00 29.15 ?  189 GLU C CA    1 
ATOM   12522 C  C     . GLU C 2 210 ? 118.464 104.192 115.094 1.00 28.02 ?  189 GLU C C     1 
ATOM   12523 O  O     . GLU C 2 210 ? 119.299 103.289 115.017 1.00 27.15 ?  189 GLU C O     1 
ATOM   12524 C  CB    . GLU C 2 210 ? 118.467 106.129 113.465 1.00 30.17 ?  189 GLU C CB    1 
ATOM   12525 C  CG    . GLU C 2 210 ? 119.371 106.076 112.243 1.00 35.68 ?  189 GLU C CG    1 
ATOM   12526 C  CD    . GLU C 2 210 ? 118.592 106.083 110.924 1.00 40.25 ?  189 GLU C CD    1 
ATOM   12527 O  OE1   . GLU C 2 210 ? 117.873 107.067 110.629 1.00 42.98 ?  189 GLU C OE1   1 
ATOM   12528 O  OE2   . GLU C 2 210 ? 118.709 105.100 110.167 1.00 43.59 -1 189 GLU C OE2   1 
ATOM   12529 N  N     . ILE C 2 211 ? 118.066 104.702 116.258 1.00 27.57 ?  190 ILE C N     1 
ATOM   12530 C  CA    . ILE C 2 211 ? 118.509 104.142 117.539 1.00 27.47 ?  190 ILE C CA    1 
ATOM   12531 C  C     . ILE C 2 211 ? 118.139 102.659 117.657 1.00 26.69 ?  190 ILE C C     1 
ATOM   12532 O  O     . ILE C 2 211 ? 118.984 101.808 117.962 1.00 26.56 ?  190 ILE C O     1 
ATOM   12533 C  CB    . ILE C 2 211 ? 117.949 104.963 118.738 1.00 27.84 ?  190 ILE C CB    1 
ATOM   12534 C  CG1   . ILE C 2 211 ? 118.649 106.330 118.802 1.00 28.56 ?  190 ILE C CG1   1 
ATOM   12535 C  CG2   . ILE C 2 211 ? 118.100 104.175 120.060 1.00 27.27 ?  190 ILE C CG2   1 
ATOM   12536 C  CD1   . ILE C 2 211 ? 118.219 107.208 119.972 1.00 30.09 ?  190 ILE C CD1   1 
ATOM   12537 N  N     . ILE C 2 212 ? 116.878 102.354 117.374 1.00 26.33 ?  191 ILE C N     1 
ATOM   12538 C  CA    . ILE C 2 212 ? 116.367 100.989 117.453 1.00 25.96 ?  191 ILE C CA    1 
ATOM   12539 C  C     . ILE C 2 212 ? 117.119 100.033 116.517 1.00 25.46 ?  191 ILE C C     1 
ATOM   12540 O  O     . ILE C 2 212 ? 117.416 98.906  116.906 1.00 24.84 ?  191 ILE C O     1 
ATOM   12541 C  CB    . ILE C 2 212 ? 114.827 100.945 117.208 1.00 26.00 ?  191 ILE C CB    1 
ATOM   12542 C  CG1   . ILE C 2 212 ? 114.082 101.683 118.333 1.00 27.16 ?  191 ILE C CG1   1 
ATOM   12543 C  CG2   . ILE C 2 212 ? 114.313 99.518  117.076 1.00 26.87 ?  191 ILE C CG2   1 
ATOM   12544 C  CD1   . ILE C 2 212 ? 114.231 101.070 119.713 1.00 29.84 ?  191 ILE C CD1   1 
ATOM   12545 N  N     . ASN C 2 213 ? 117.425 100.482 115.296 1.00 25.35 ?  192 ASN C N     1 
ATOM   12546 C  CA    . ASN C 2 213 ? 118.206 99.676  114.351 1.00 25.60 ?  192 ASN C CA    1 
ATOM   12547 C  C     . ASN C 2 213 ? 119.612 99.373  114.859 1.00 25.14 ?  192 ASN C C     1 
ATOM   12548 O  O     . ASN C 2 213 ? 120.147 98.276  114.638 1.00 25.61 ?  192 ASN C O     1 
ATOM   12549 C  CB    . ASN C 2 213 ? 118.286 100.345 112.972 1.00 26.55 ?  192 ASN C CB    1 
ATOM   12550 C  CG    . ASN C 2 213 ? 117.111 99.992  112.087 1.00 28.10 ?  192 ASN C CG    1 
ATOM   12551 O  OD1   . ASN C 2 213 ? 116.907 98.826  111.732 1.00 31.67 ?  192 ASN C OD1   1 
ATOM   12552 N  ND2   . ASN C 2 213 ? 116.337 100.995 111.715 1.00 30.36 ?  192 ASN C ND2   1 
ATOM   12553 N  N     . LEU C 2 214 ? 120.210 100.343 115.540 1.00 24.54 ?  193 LEU C N     1 
ATOM   12554 C  CA    . LEU C 2 214 ? 121.520 100.126 116.160 1.00 24.40 ?  193 LEU C CA    1 
ATOM   12555 C  C     . LEU C 2 214 ? 121.431 99.100  117.291 1.00 23.55 ?  193 LEU C C     1 
ATOM   12556 O  O     . LEU C 2 214 ? 122.270 98.200  117.382 1.00 23.09 ?  193 LEU C O     1 
ATOM   12557 C  CB    . LEU C 2 214 ? 122.132 101.445 116.626 1.00 24.00 ?  193 LEU C CB    1 
ATOM   12558 C  CG    . LEU C 2 214 ? 122.630 102.381 115.503 1.00 25.69 ?  193 LEU C CG    1 
ATOM   12559 C  CD1   . LEU C 2 214 ? 122.951 103.778 116.035 1.00 26.28 ?  193 LEU C CD1   1 
ATOM   12560 C  CD2   . LEU C 2 214 ? 123.857 101.811 114.786 1.00 26.05 ?  193 LEU C CD2   1 
ATOM   12561 N  N     . ILE C 2 215 ? 120.407 99.230  118.139 1.00 23.19 ?  194 ILE C N     1 
ATOM   12562 C  CA    . ILE C 2 215 ? 120.129 98.244  119.189 1.00 22.88 ?  194 ILE C CA    1 
ATOM   12563 C  C     . ILE C 2 215 ? 119.932 96.857  118.555 1.00 23.81 ?  194 ILE C C     1 
ATOM   12564 O  O     . ILE C 2 215 ? 120.533 95.878  118.999 1.00 23.83 ?  194 ILE C O     1 
ATOM   12565 C  CB    . ILE C 2 215 ? 118.895 98.637  120.050 1.00 22.92 ?  194 ILE C CB    1 
ATOM   12566 C  CG1   . ILE C 2 215 ? 119.133 99.974  120.755 1.00 21.11 ?  194 ILE C CG1   1 
ATOM   12567 C  CG2   . ILE C 2 215 ? 118.542 97.541  121.068 1.00 21.89 ?  194 ILE C CG2   1 
ATOM   12568 C  CD1   . ILE C 2 215 ? 117.968 100.449 121.599 1.00 22.26 ?  194 ILE C CD1   1 
ATOM   12569 N  N     . LEU C 2 216 ? 119.128 96.780  117.494 1.00 24.23 ?  195 LEU C N     1 
ATOM   12570 C  CA    . LEU C 2 216 ? 118.834 95.495  116.851 1.00 25.41 ?  195 LEU C CA    1 
ATOM   12571 C  C     . LEU C 2 216 ? 120.086 94.858  116.245 1.00 25.63 ?  195 LEU C C     1 
ATOM   12572 O  O     . LEU C 2 216 ? 120.301 93.644  116.376 1.00 25.46 ?  195 LEU C O     1 
ATOM   12573 C  CB    . LEU C 2 216 ? 117.729 95.654  115.788 1.00 26.03 ?  195 LEU C CB    1 
ATOM   12574 C  CG    . LEU C 2 216 ? 117.209 94.436  115.012 1.00 28.00 ?  195 LEU C CG    1 
ATOM   12575 C  CD1   . LEU C 2 216 ? 115.830 94.758  114.459 1.00 31.45 ?  195 LEU C CD1   1 
ATOM   12576 C  CD2   . LEU C 2 216 ? 118.156 94.011  113.884 1.00 29.83 ?  195 LEU C CD2   1 
ATOM   12577 N  N     . ARG C 2 217 ? 120.906 95.679  115.595 1.00 25.98 ?  196 ARG C N     1 
ATOM   12578 C  CA    . ARG C 2 217 ? 122.186 95.236  115.053 1.00 26.73 ?  196 ARG C CA    1 
ATOM   12579 C  C     . ARG C 2 217 ? 123.062 94.595  116.158 1.00 25.95 ?  196 ARG C C     1 
ATOM   12580 O  O     . ARG C 2 217 ? 123.655 93.535  115.929 1.00 25.75 ?  196 ARG C O     1 
ATOM   12581 C  CB    . ARG C 2 217 ? 122.909 96.412  114.391 1.00 27.29 ?  196 ARG C CB    1 
ATOM   12582 C  CG    . ARG C 2 217 ? 124.134 96.044  113.541 1.00 30.12 ?  196 ARG C CG    1 
ATOM   12583 C  CD    . ARG C 2 217 ? 125.138 97.181  113.582 1.00 35.40 ?  196 ARG C CD    1 
ATOM   12584 N  NE    . ARG C 2 217 ? 125.270 97.637  114.966 1.00 39.87 ?  196 ARG C NE    1 
ATOM   12585 C  CZ    . ARG C 2 217 ? 125.874 98.748  115.368 1.00 40.55 ?  196 ARG C CZ    1 
ATOM   12586 N  NH1   . ARG C 2 217 ? 126.449 99.574  114.494 1.00 40.77 1  196 ARG C NH1   1 
ATOM   12587 N  NH2   . ARG C 2 217 ? 125.893 99.026  116.666 1.00 41.10 ?  196 ARG C NH2   1 
ATOM   12588 N  N     . ASP C 2 218 ? 123.122 95.228  117.336 1.00 24.70 ?  197 ASP C N     1 
ATOM   12589 C  CA    . ASP C 2 218 ? 123.826 94.665  118.506 1.00 24.55 ?  197 ASP C CA    1 
ATOM   12590 C  C     . ASP C 2 218 ? 123.209 93.328  118.963 1.00 24.23 ?  197 ASP C C     1 
ATOM   12591 O  O     . ASP C 2 218 ? 123.931 92.340  119.128 1.00 23.69 ?  197 ASP C O     1 
ATOM   12592 C  CB    . ASP C 2 218 ? 123.856 95.637  119.704 1.00 24.50 ?  197 ASP C CB    1 
ATOM   12593 C  CG    . ASP C 2 218 ? 124.699 96.902  119.457 1.00 25.84 ?  197 ASP C CG    1 
ATOM   12594 O  OD1   . ASP C 2 218 ? 125.621 96.900  118.612 1.00 26.91 ?  197 ASP C OD1   1 
ATOM   12595 O  OD2   . ASP C 2 218 ? 124.441 97.911  120.142 1.00 25.72 -1 197 ASP C OD2   1 
ATOM   12596 N  N     . GLU C 2 219 ? 121.884 93.286  119.141 1.00 23.92 ?  198 GLU C N     1 
ATOM   12597 C  CA    . GLU C 2 219 ? 121.256 92.068  119.682 1.00 24.20 ?  198 GLU C CA    1 
ATOM   12598 C  C     . GLU C 2 219 ? 121.451 90.880  118.759 1.00 24.02 ?  198 GLU C C     1 
ATOM   12599 O  O     . GLU C 2 219 ? 121.607 89.762  119.239 1.00 24.24 ?  198 GLU C O     1 
ATOM   12600 C  CB    . GLU C 2 219 ? 119.765 92.233  119.989 1.00 24.05 ?  198 GLU C CB    1 
ATOM   12601 C  CG    . GLU C 2 219 ? 119.329 93.555  120.595 1.00 25.03 ?  198 GLU C CG    1 
ATOM   12602 C  CD    . GLU C 2 219 ? 119.747 93.807  122.056 1.00 26.31 ?  198 GLU C CD    1 
ATOM   12603 O  OE1   . GLU C 2 219 ? 120.751 93.234  122.574 1.00 27.65 ?  198 GLU C OE1   1 
ATOM   12604 O  OE2   . GLU C 2 219 ? 119.047 94.645  122.689 1.00 26.87 -1 198 GLU C OE2   1 
ATOM   12605 N  N     . ALA C 2 220 ? 121.439 91.117  117.446 1.00 24.00 ?  199 ALA C N     1 
ATOM   12606 C  CA    . ALA C 2 220 ? 121.664 90.048  116.480 1.00 24.72 ?  199 ALA C CA    1 
ATOM   12607 C  C     . ALA C 2 220 ? 123.016 89.348  116.700 1.00 24.80 ?  199 ALA C C     1 
ATOM   12608 O  O     . ALA C 2 220 ? 123.083 88.116  116.701 1.00 25.04 ?  199 ALA C O     1 
ATOM   12609 C  CB    . ALA C 2 220 ? 121.537 90.566  115.025 1.00 24.66 ?  199 ALA C CB    1 
ATOM   12610 N  N     . ILE C 2 221 ? 124.078 90.128  116.894 1.00 24.85 ?  200 ILE C N     1 
ATOM   12611 C  CA    . ILE C 2 221 ? 125.406 89.546  117.163 1.00 25.07 ?  200 ILE C CA    1 
ATOM   12612 C  C     . ILE C 2 221 ? 125.513 88.962  118.580 1.00 23.86 ?  200 ILE C C     1 
ATOM   12613 O  O     . ILE C 2 221 ? 126.205 87.960  118.779 1.00 23.72 ?  200 ILE C O     1 
ATOM   12614 C  CB    . ILE C 2 221 ? 126.603 90.512  116.843 1.00 25.71 ?  200 ILE C CB    1 
ATOM   12615 C  CG1   . ILE C 2 221 ? 126.726 91.630  117.884 1.00 27.10 ?  200 ILE C CG1   1 
ATOM   12616 C  CG2   . ILE C 2 221 ? 126.503 91.051  115.403 1.00 27.18 ?  200 ILE C CG2   1 
ATOM   12617 C  CD1   . ILE C 2 221 ? 127.981 92.501  117.756 1.00 29.63 ?  200 ILE C CD1   1 
ATOM   12618 N  N     . HIS C 2 222 ? 124.821 89.570  119.544 1.00 22.79 ?  201 HIS C N     1 
ATOM   12619 C  CA    . HIS C 2 222 ? 124.758 89.019  120.917 1.00 22.48 ?  201 HIS C CA    1 
ATOM   12620 C  C     . HIS C 2 222 ? 124.103 87.640  120.932 1.00 22.04 ?  201 HIS C C     1 
ATOM   12621 O  O     . HIS C 2 222 ? 124.580 86.741  121.616 1.00 22.06 ?  201 HIS C O     1 
ATOM   12622 C  CB    . HIS C 2 222 ? 123.949 89.910  121.861 1.00 21.77 ?  201 HIS C CB    1 
ATOM   12623 C  CG    . HIS C 2 222 ? 124.554 91.248  122.127 1.00 21.76 ?  201 HIS C CG    1 
ATOM   12624 N  ND1   . HIS C 2 222 ? 124.011 92.131  123.032 1.00 20.70 ?  201 HIS C ND1   1 
ATOM   12625 C  CD2   . HIS C 2 222 ? 125.651 91.857  121.619 1.00 22.07 ?  201 HIS C CD2   1 
ATOM   12626 C  CE1   . HIS C 2 222 ? 124.739 93.231  123.064 1.00 22.26 ?  201 HIS C CE1   1 
ATOM   12627 N  NE2   . HIS C 2 222 ? 125.735 93.094  122.211 1.00 22.52 ?  201 HIS C NE2   1 
ATOM   12628 N  N     . GLY C 2 223 ? 122.991 87.496  120.210 1.00 22.35 ?  202 GLY C N     1 
ATOM   12629 C  CA    . GLY C 2 223 ? 122.276 86.215  120.092 1.00 22.01 ?  202 GLY C CA    1 
ATOM   12630 C  C     . GLY C 2 223 ? 123.096 85.124  119.410 1.00 22.73 ?  202 GLY C C     1 
ATOM   12631 O  O     . GLY C 2 223 ? 123.068 83.954  119.830 1.00 21.99 ?  202 GLY C O     1 
ATOM   12632 N  N     . VAL C 2 224 ? 123.834 85.496  118.362 1.00 22.45 ?  203 VAL C N     1 
ATOM   12633 C  CA    . VAL C 2 224 ? 124.720 84.544  117.687 1.00 22.54 ?  203 VAL C CA    1 
ATOM   12634 C  C     . VAL C 2 224 ? 125.833 84.079  118.628 1.00 22.28 ?  203 VAL C C     1 
ATOM   12635 O  O     . VAL C 2 224 ? 126.055 82.881  118.784 1.00 22.44 ?  203 VAL C O     1 
ATOM   12636 C  CB    . VAL C 2 224 ? 125.332 85.119  116.365 1.00 23.00 ?  203 VAL C CB    1 
ATOM   12637 C  CG1   . VAL C 2 224 ? 126.415 84.174  115.814 1.00 23.10 ?  203 VAL C CG1   1 
ATOM   12638 C  CG2   . VAL C 2 224 ? 124.231 85.345  115.293 1.00 23.14 ?  203 VAL C CG2   1 
ATOM   12639 N  N     . TYR C 2 225 ? 126.501 85.031  119.277 1.00 22.41 ?  204 TYR C N     1 
ATOM   12640 C  CA    . TYR C 2 225 ? 127.614 84.717  120.172 1.00 22.03 ?  204 TYR C CA    1 
ATOM   12641 C  C     . TYR C 2 225 ? 127.207 83.797  121.323 1.00 21.66 ?  204 TYR C C     1 
ATOM   12642 O  O     . TYR C 2 225 ? 127.823 82.741  121.527 1.00 21.72 ?  204 TYR C O     1 
ATOM   12643 C  CB    . TYR C 2 225 ? 128.285 85.990  120.711 1.00 22.22 ?  204 TYR C CB    1 
ATOM   12644 C  CG    . TYR C 2 225 ? 129.572 85.699  121.458 1.00 21.92 ?  204 TYR C CG    1 
ATOM   12645 C  CD1   . TYR C 2 225 ? 130.700 85.232  120.782 1.00 22.36 ?  204 TYR C CD1   1 
ATOM   12646 C  CD2   . TYR C 2 225 ? 129.654 85.881  122.839 1.00 21.43 ?  204 TYR C CD2   1 
ATOM   12647 C  CE1   . TYR C 2 225 ? 131.881 84.947  121.466 1.00 23.82 ?  204 TYR C CE1   1 
ATOM   12648 C  CE2   . TYR C 2 225 ? 130.834 85.607  123.538 1.00 21.49 ?  204 TYR C CE2   1 
ATOM   12649 C  CZ    . TYR C 2 225 ? 131.936 85.143  122.845 1.00 23.58 ?  204 TYR C CZ    1 
ATOM   12650 O  OH    . TYR C 2 225 ? 133.092 84.874  123.528 1.00 25.42 ?  204 TYR C OH    1 
ATOM   12651 N  N     . VAL C 2 226 ? 126.170 84.187  122.068 1.00 20.95 ?  205 VAL C N     1 
ATOM   12652 C  CA    . VAL C 2 226 ? 125.669 83.348  123.165 1.00 20.49 ?  205 VAL C CA    1 
ATOM   12653 C  C     . VAL C 2 226 ? 125.193 81.982  122.638 1.00 20.84 ?  205 VAL C C     1 
ATOM   12654 O  O     . VAL C 2 226 ? 125.444 80.942  123.262 1.00 21.10 ?  205 VAL C O     1 
ATOM   12655 C  CB    . VAL C 2 226 ? 124.591 84.069  124.020 1.00 20.57 ?  205 VAL C CB    1 
ATOM   12656 C  CG1   . VAL C 2 226 ? 124.068 83.145  125.119 1.00 20.35 ?  205 VAL C CG1   1 
ATOM   12657 C  CG2   . VAL C 2 226 ? 125.187 85.341  124.643 1.00 19.60 ?  205 VAL C CG2   1 
ATOM   12658 N  N     . GLY C 2 227 ? 124.557 81.982  121.471 1.00 21.08 ?  206 GLY C N     1 
ATOM   12659 C  CA    . GLY C 2 227 ? 124.193 80.727  120.795 1.00 21.43 ?  206 GLY C CA    1 
ATOM   12660 C  C     . GLY C 2 227 ? 125.366 79.783  120.569 1.00 21.95 ?  206 GLY C C     1 
ATOM   12661 O  O     . GLY C 2 227 ? 125.257 78.567  120.802 1.00 21.84 ?  206 GLY C O     1 
ATOM   12662 N  N     . LEU C 2 228 ? 126.496 80.332  120.122 1.00 22.09 ?  207 LEU C N     1 
ATOM   12663 C  CA    . LEU C 2 228 ? 127.696 79.516  119.912 1.00 22.96 ?  207 LEU C CA    1 
ATOM   12664 C  C     . LEU C 2 228 ? 128.239 78.929  121.223 1.00 22.60 ?  207 LEU C C     1 
ATOM   12665 O  O     . LEU C 2 228 ? 128.666 77.770  121.259 1.00 22.04 ?  207 LEU C O     1 
ATOM   12666 C  CB    . LEU C 2 228 ? 128.779 80.293  119.151 1.00 23.39 ?  207 LEU C CB    1 
ATOM   12667 C  CG    . LEU C 2 228 ? 128.486 80.684  117.691 1.00 24.35 ?  207 LEU C CG    1 
ATOM   12668 C  CD1   . LEU C 2 228 ? 129.449 81.791  117.241 1.00 25.01 ?  207 LEU C CD1   1 
ATOM   12669 C  CD2   . LEU C 2 228 ? 128.568 79.493  116.743 1.00 25.11 ?  207 LEU C CD2   1 
ATOM   12670 N  N     . LEU C 2 229 ? 128.196 79.709  122.300 1.00 22.37 ?  208 LEU C N     1 
ATOM   12671 C  CA    . LEU C 2 229 ? 128.602 79.201  123.625 1.00 22.62 ?  208 LEU C CA    1 
ATOM   12672 C  C     . LEU C 2 229 ? 127.682 78.084  124.130 1.00 22.77 ?  208 LEU C C     1 
ATOM   12673 O  O     . LEU C 2 229 ? 128.153 77.079  124.690 1.00 22.57 ?  208 LEU C O     1 
ATOM   12674 C  CB    . LEU C 2 229 ? 128.706 80.336  124.649 1.00 22.44 ?  208 LEU C CB    1 
ATOM   12675 C  CG    . LEU C 2 229 ? 129.669 81.478  124.292 1.00 23.54 ?  208 LEU C CG    1 
ATOM   12676 C  CD1   . LEU C 2 229 ? 129.602 82.585  125.341 1.00 23.37 ?  208 LEU C CD1   1 
ATOM   12677 C  CD2   . LEU C 2 229 ? 131.113 80.971  124.121 1.00 23.91 ?  208 LEU C CD2   1 
ATOM   12678 N  N     . ALA C 2 230 ? 126.376 78.256  123.922 1.00 22.42 ?  209 ALA C N     1 
ATOM   12679 C  CA    . ALA C 2 230 ? 125.396 77.231  124.273 1.00 22.02 ?  209 ALA C CA    1 
ATOM   12680 C  C     . ALA C 2 230 ? 125.649 75.929  123.505 1.00 22.58 ?  209 ALA C C     1 
ATOM   12681 O  O     . ALA C 2 230 ? 125.635 74.853  124.090 1.00 22.14 ?  209 ALA C O     1 
ATOM   12682 C  CB    . ALA C 2 230 ? 123.992 77.728  124.015 1.00 22.04 ?  209 ALA C CB    1 
ATOM   12683 N  N     . GLN C 2 231 ? 125.900 76.043  122.203 1.00 22.96 ?  210 GLN C N     1 
ATOM   12684 C  CA    . GLN C 2 231 ? 126.218 74.868  121.371 1.00 24.30 ?  210 GLN C CA    1 
ATOM   12685 C  C     . GLN C 2 231 ? 127.458 74.126  121.835 1.00 25.11 ?  210 GLN C C     1 
ATOM   12686 O  O     . GLN C 2 231 ? 127.515 72.895  121.744 1.00 24.97 ?  210 GLN C O     1 
ATOM   12687 C  CB    . GLN C 2 231 ? 126.370 75.265  119.907 1.00 24.38 ?  210 GLN C CB    1 
ATOM   12688 C  CG    . GLN C 2 231 ? 125.045 75.708  119.264 1.00 25.12 ?  210 GLN C CG    1 
ATOM   12689 C  CD    . GLN C 2 231 ? 125.213 76.097  117.811 1.00 28.08 ?  210 GLN C CD    1 
ATOM   12690 O  OE1   . GLN C 2 231 ? 125.717 75.313  117.006 1.00 27.83 ?  210 GLN C OE1   1 
ATOM   12691 N  NE2   . GLN C 2 231 ? 124.806 77.320  117.467 1.00 26.38 ?  210 GLN C NE2   1 
ATOM   12692 N  N     . GLU C 2 232 ? 128.452 74.869  122.327 1.00 25.80 ?  211 GLU C N     1 
ATOM   12693 C  CA    . GLU C 2 232 ? 129.654 74.250  122.897 1.00 27.16 ?  211 GLU C CA    1 
ATOM   12694 C  C     . GLU C 2 232 ? 129.295 73.285  124.023 1.00 26.47 ?  211 GLU C C     1 
ATOM   12695 O  O     . GLU C 2 232 ? 129.819 72.166  124.086 1.00 26.10 ?  211 GLU C O     1 
ATOM   12696 C  CB    . GLU C 2 232 ? 130.595 75.305  123.465 1.00 27.59 ?  211 GLU C CB    1 
ATOM   12697 C  CG    . GLU C 2 232 ? 131.614 75.825  122.498 1.00 32.55 ?  211 GLU C CG    1 
ATOM   12698 C  CD    . GLU C 2 232 ? 132.919 76.202  123.189 1.00 36.72 ?  211 GLU C CD    1 
ATOM   12699 O  OE1   . GLU C 2 232 ? 132.991 76.144  124.440 1.00 38.32 ?  211 GLU C OE1   1 
ATOM   12700 O  OE2   . GLU C 2 232 ? 133.877 76.552  122.471 1.00 40.62 -1 211 GLU C OE2   1 
ATOM   12701 N  N     . ILE C 2 233 ? 128.416 73.732  124.918 1.00 25.55 ?  212 ILE C N     1 
ATOM   12702 C  CA    . ILE C 2 233 ? 128.014 72.921  126.067 1.00 25.32 ?  212 ILE C CA    1 
ATOM   12703 C  C     . ILE C 2 233 ? 127.156 71.738  125.637 1.00 25.48 ?  212 ILE C C     1 
ATOM   12704 O  O     . ILE C 2 233 ? 127.408 70.601  126.042 1.00 25.82 ?  212 ILE C O     1 
ATOM   12705 C  CB    . ILE C 2 233 ? 127.291 73.759  127.143 1.00 25.39 ?  212 ILE C CB    1 
ATOM   12706 C  CG1   . ILE C 2 233 ? 128.275 74.752  127.768 1.00 24.37 ?  212 ILE C CG1   1 
ATOM   12707 C  CG2   . ILE C 2 233 ? 126.667 72.848  128.206 1.00 24.86 ?  212 ILE C CG2   1 
ATOM   12708 C  CD1   . ILE C 2 233 ? 127.602 75.885  128.526 1.00 25.10 ?  212 ILE C CD1   1 
ATOM   12709 N  N     . TYR C 2 234 ? 126.161 72.008  124.796 1.00 25.27 ?  213 TYR C N     1 
ATOM   12710 C  CA    . TYR C 2 234 ? 125.310 70.968  124.213 1.00 25.77 ?  213 TYR C CA    1 
ATOM   12711 C  C     . TYR C 2 234 ? 126.130 69.858  123.531 1.00 26.44 ?  213 TYR C C     1 
ATOM   12712 O  O     . TYR C 2 234 ? 125.832 68.671  123.680 1.00 26.29 ?  213 TYR C O     1 
ATOM   12713 C  CB    . TYR C 2 234 ? 124.337 71.615  123.214 1.00 25.67 ?  213 TYR C CB    1 
ATOM   12714 C  CG    . TYR C 2 234 ? 123.411 70.684  122.459 1.00 25.65 ?  213 TYR C CG    1 
ATOM   12715 C  CD1   . TYR C 2 234 ? 122.134 70.396  122.946 1.00 25.02 ?  213 TYR C CD1   1 
ATOM   12716 C  CD2   . TYR C 2 234 ? 123.791 70.136  121.223 1.00 26.59 ?  213 TYR C CD2   1 
ATOM   12717 C  CE1   . TYR C 2 234 ? 121.268 69.564  122.244 1.00 26.52 ?  213 TYR C CE1   1 
ATOM   12718 C  CE2   . TYR C 2 234 ? 122.933 69.295  120.512 1.00 27.00 ?  213 TYR C CE2   1 
ATOM   12719 C  CZ    . TYR C 2 234 ? 121.677 69.014  121.034 1.00 27.79 ?  213 TYR C CZ    1 
ATOM   12720 O  OH    . TYR C 2 234 ? 120.823 68.205  120.338 1.00 29.00 ?  213 TYR C OH    1 
ATOM   12721 N  N     . ASN C 2 235 ? 127.161 70.245  122.783 1.00 26.96 ?  214 ASN C N     1 
ATOM   12722 C  CA    . ASN C 2 235 ? 127.954 69.269  122.038 1.00 28.05 ?  214 ASN C CA    1 
ATOM   12723 C  C     . ASN C 2 235 ? 128.802 68.341  122.902 1.00 28.24 ?  214 ASN C C     1 
ATOM   12724 O  O     . ASN C 2 235 ? 129.275 67.317  122.419 1.00 28.63 ?  214 ASN C O     1 
ATOM   12725 C  CB    . ASN C 2 235 ? 128.795 69.945  120.945 1.00 28.38 ?  214 ASN C CB    1 
ATOM   12726 C  CG    . ASN C 2 235 ? 127.936 70.532  119.830 1.00 31.14 ?  214 ASN C CG    1 
ATOM   12727 O  OD1   . ASN C 2 235 ? 126.866 70.006  119.506 1.00 34.16 ?  214 ASN C OD1   1 
ATOM   12728 N  ND2   . ASN C 2 235 ? 128.399 71.629  119.242 1.00 32.42 ?  214 ASN C ND2   1 
ATOM   12729 N  N     . LYS C 2 236 ? 128.971 68.687  124.178 1.00 27.91 ?  215 LYS C N     1 
ATOM   12730 C  CA    . LYS C 2 236 ? 129.689 67.841  125.135 1.00 28.49 ?  215 LYS C CA    1 
ATOM   12731 C  C     . LYS C 2 236 ? 128.839 66.694  125.693 1.00 28.50 ?  215 LYS C C     1 
ATOM   12732 O  O     . LYS C 2 236 ? 129.366 65.768  126.315 1.00 28.98 ?  215 LYS C O     1 
ATOM   12733 C  CB    . LYS C 2 236 ? 130.228 68.680  126.299 1.00 28.10 ?  215 LYS C CB    1 
ATOM   12734 C  CG    . LYS C 2 236 ? 131.276 69.708  125.899 1.00 29.25 ?  215 LYS C CG    1 
ATOM   12735 C  CD    . LYS C 2 236 ? 131.780 70.486  127.104 1.00 30.19 ?  215 LYS C CD    1 
ATOM   12736 C  CE    . LYS C 2 236 ? 132.571 71.689  126.647 1.00 32.63 ?  215 LYS C CE    1 
ATOM   12737 N  NZ    . LYS C 2 236 ? 133.072 72.478  127.797 1.00 35.39 1  215 LYS C NZ    1 
ATOM   12738 N  N     . GLN C 2 237 ? 127.532 66.740  125.459 1.00 28.25 ?  216 GLN C N     1 
ATOM   12739 C  CA    . GLN C 2 237 ? 126.619 65.809  126.124 1.00 28.34 ?  216 GLN C CA    1 
ATOM   12740 C  C     . GLN C 2 237 ? 126.450 64.467  125.393 1.00 28.92 ?  216 GLN C C     1 
ATOM   12741 O  O     . GLN C 2 237 ? 126.730 64.360  124.199 1.00 28.53 ?  216 GLN C O     1 
ATOM   12742 C  CB    . GLN C 2 237 ? 125.262 66.489  126.361 1.00 27.68 ?  216 GLN C CB    1 
ATOM   12743 C  CG    . GLN C 2 237 ? 125.354 67.875  127.044 1.00 26.67 ?  216 GLN C CG    1 
ATOM   12744 C  CD    . GLN C 2 237 ? 126.198 67.883  128.314 1.00 25.32 ?  216 GLN C CD    1 
ATOM   12745 O  OE1   . GLN C 2 237 ? 126.088 66.991  129.158 1.00 25.49 ?  216 GLN C OE1   1 
ATOM   12746 N  NE2   . GLN C 2 237 ? 127.046 68.898  128.456 1.00 23.63 ?  216 GLN C NE2   1 
ATOM   12747 N  N     . THR C 2 238 ? 125.986 63.451  126.122 1.00 29.53 ?  217 THR C N     1 
ATOM   12748 C  CA    . THR C 2 238 ? 125.538 62.198  125.507 1.00 30.73 ?  217 THR C CA    1 
ATOM   12749 C  C     . THR C 2 238 ? 124.307 62.478  124.636 1.00 31.13 ?  217 THR C C     1 
ATOM   12750 O  O     . THR C 2 238 ? 123.662 63.534  124.774 1.00 30.17 ?  217 THR C O     1 
ATOM   12751 C  CB    . THR C 2 238 ? 125.123 61.152  126.557 1.00 30.79 ?  217 THR C CB    1 
ATOM   12752 O  OG1   . THR C 2 238 ? 123.928 61.593  127.216 1.00 31.16 ?  217 THR C OG1   1 
ATOM   12753 C  CG2   . THR C 2 238 ? 126.231 60.923  127.591 1.00 31.22 ?  217 THR C CG2   1 
ATOM   12754 N  N     . GLU C 2 239 ? 123.965 61.527  123.764 1.00 31.67 ?  218 GLU C N     1 
ATOM   12755 C  CA    . GLU C 2 239 ? 122.771 61.667  122.930 1.00 32.25 ?  218 GLU C CA    1 
ATOM   12756 C  C     . GLU C 2 239 ? 121.492 61.766  123.770 1.00 31.86 ?  218 GLU C C     1 
ATOM   12757 O  O     . GLU C 2 239 ? 120.588 62.543  123.451 1.00 31.09 ?  218 GLU C O     1 
ATOM   12758 C  CB    . GLU C 2 239 ? 122.685 60.534  121.892 1.00 33.29 ?  218 GLU C CB    1 
ATOM   12759 C  CG    . GLU C 2 239 ? 123.776 60.615  120.807 1.00 35.65 ?  218 GLU C CG    1 
ATOM   12760 C  CD    . GLU C 2 239 ? 123.738 61.929  120.017 1.00 39.17 ?  218 GLU C CD    1 
ATOM   12761 O  OE1   . GLU C 2 239 ? 122.632 62.352  119.594 1.00 41.08 ?  218 GLU C OE1   1 
ATOM   12762 O  OE2   . GLU C 2 239 ? 124.815 62.546  119.824 1.00 39.64 -1 218 GLU C OE2   1 
ATOM   12763 N  N     . GLU C 2 240 ? 121.448 61.003  124.863 1.00 31.72 ?  219 GLU C N     1 
ATOM   12764 C  CA    . GLU C 2 240 ? 120.324 61.017  125.788 1.00 31.76 ?  219 GLU C CA    1 
ATOM   12765 C  C     . GLU C 2 240 ? 120.162 62.393  126.450 1.00 30.21 ?  219 GLU C C     1 
ATOM   12766 O  O     . GLU C 2 240 ? 119.047 62.928  126.533 1.00 29.63 ?  219 GLU C O     1 
ATOM   12767 C  CB    . GLU C 2 240 ? 120.507 59.915  126.835 1.00 32.58 ?  219 GLU C CB    1 
ATOM   12768 C  CG    . GLU C 2 240 ? 119.296 59.666  127.721 1.00 36.93 ?  219 GLU C CG    1 
ATOM   12769 C  CD    . GLU C 2 240 ? 119.383 58.337  128.463 1.00 42.06 ?  219 GLU C CD    1 
ATOM   12770 O  OE1   . GLU C 2 240 ? 119.495 58.351  129.709 1.00 44.09 ?  219 GLU C OE1   1 
ATOM   12771 O  OE2   . GLU C 2 240 ? 119.347 57.275  127.798 1.00 44.45 -1 219 GLU C OE2   1 
ATOM   12772 N  N     . LYS C 2 241 ? 121.280 62.960  126.902 1.00 28.91 ?  220 LYS C N     1 
ATOM   12773 C  CA    . LYS C 2 241 ? 121.289 64.280  127.518 1.00 28.14 ?  220 LYS C CA    1 
ATOM   12774 C  C     . LYS C 2 241 ? 120.891 65.379  126.531 1.00 27.03 ?  220 LYS C C     1 
ATOM   12775 O  O     . LYS C 2 241 ? 120.134 66.288  126.885 1.00 26.72 ?  220 LYS C O     1 
ATOM   12776 C  CB    . LYS C 2 241 ? 122.655 64.588  128.138 1.00 27.83 ?  220 LYS C CB    1 
ATOM   12777 C  CG    . LYS C 2 241 ? 122.697 65.917  128.906 1.00 29.68 ?  220 LYS C CG    1 
ATOM   12778 C  CD    . LYS C 2 241 ? 122.517 65.724  130.405 1.00 33.58 ?  220 LYS C CD    1 
ATOM   12779 C  CE    . LYS C 2 241 ? 121.069 65.614  130.792 1.00 33.71 ?  220 LYS C CE    1 
ATOM   12780 N  NZ    . LYS C 2 241 ? 120.890 65.262  132.239 1.00 34.69 1  220 LYS C NZ    1 
ATOM   12781 N  N     . LYS C 2 242 ? 121.411 65.287  125.305 1.00 26.38 ?  221 LYS C N     1 
ATOM   12782 C  CA    . LYS C 2 242 ? 121.052 66.194  124.211 1.00 25.87 ?  221 LYS C CA    1 
ATOM   12783 C  C     . LYS C 2 242 ? 119.558 66.207  123.950 1.00 25.72 ?  221 LYS C C     1 
ATOM   12784 O  O     . LYS C 2 242 ? 118.964 67.281  123.776 1.00 24.52 ?  221 LYS C O     1 
ATOM   12785 C  CB    . LYS C 2 242 ? 121.782 65.823  122.919 1.00 25.83 ?  221 LYS C CB    1 
ATOM   12786 C  CG    . LYS C 2 242 ? 123.241 66.216  122.873 1.00 26.76 ?  221 LYS C CG    1 
ATOM   12787 C  CD    . LYS C 2 242 ? 123.814 65.917  121.492 1.00 28.40 ?  221 LYS C CD    1 
ATOM   12788 C  CE    . LYS C 2 242 ? 125.307 66.074  121.462 1.00 29.84 ?  221 LYS C CE    1 
ATOM   12789 N  NZ    . LYS C 2 242 ? 125.861 65.568  120.184 1.00 30.96 1  221 LYS C NZ    1 
ATOM   12790 N  N     . ALA C 2 243 ? 118.962 65.011  123.912 1.00 25.97 ?  222 ALA C N     1 
ATOM   12791 C  CA    . ALA C 2 243 ? 117.514 64.871  123.736 1.00 25.79 ?  222 ALA C CA    1 
ATOM   12792 C  C     . ALA C 2 243 ? 116.738 65.612  124.826 1.00 25.24 ?  222 ALA C C     1 
ATOM   12793 O  O     . ALA C 2 243 ? 115.732 66.275  124.534 1.00 25.37 ?  222 ALA C O     1 
ATOM   12794 C  CB    . ALA C 2 243 ? 117.114 63.396  123.674 1.00 26.17 ?  222 ALA C CB    1 
ATOM   12795 N  N     . GLU C 2 244 ? 117.211 65.531  126.068 1.00 25.02 ?  223 GLU C N     1 
ATOM   12796 C  CA    . GLU C 2 244 ? 116.594 66.278  127.175 1.00 25.08 ?  223 GLU C CA    1 
ATOM   12797 C  C     . GLU C 2 244 ? 116.775 67.800  127.031 1.00 24.70 ?  223 GLU C C     1 
ATOM   12798 O  O     . GLU C 2 244 ? 115.857 68.578  127.330 1.00 24.20 ?  223 GLU C O     1 
ATOM   12799 C  CB    . GLU C 2 244 ? 117.128 65.804  128.531 1.00 25.35 ?  223 GLU C CB    1 
ATOM   12800 C  CG    . GLU C 2 244 ? 116.468 66.517  129.724 1.00 26.67 ?  223 GLU C CG    1 
ATOM   12801 C  CD    . GLU C 2 244 ? 117.183 66.267  131.040 1.00 28.29 ?  223 GLU C CD    1 
ATOM   12802 O  OE1   . GLU C 2 244 ? 117.884 65.246  131.169 1.00 29.51 ?  223 GLU C OE1   1 
ATOM   12803 O  OE2   . GLU C 2 244 ? 117.043 67.104  131.951 1.00 29.09 -1 223 GLU C OE2   1 
ATOM   12804 N  N     . LEU C 2 245 ? 117.955 68.218  126.585 1.00 24.27 ?  224 LEU C N     1 
ATOM   12805 C  CA    . LEU C 2 245 ? 118.231 69.644  126.394 1.00 24.54 ?  224 LEU C CA    1 
ATOM   12806 C  C     . LEU C 2 245 ? 117.371 70.272  125.288 1.00 24.42 ?  224 LEU C C     1 
ATOM   12807 O  O     . LEU C 2 245 ? 116.923 71.414  125.422 1.00 24.10 ?  224 LEU C O     1 
ATOM   12808 C  CB    . LEU C 2 245 ? 119.734 69.888  126.166 1.00 23.86 ?  224 LEU C CB    1 
ATOM   12809 C  CG    . LEU C 2 245 ? 120.643 69.599  127.368 1.00 24.78 ?  224 LEU C CG    1 
ATOM   12810 C  CD1   . LEU C 2 245 ? 122.104 69.932  127.044 1.00 25.54 ?  224 LEU C CD1   1 
ATOM   12811 C  CD2   . LEU C 2 245 ? 120.195 70.346  128.632 1.00 25.29 ?  224 LEU C CD2   1 
ATOM   12812 N  N     . ARG C 2 246 ? 117.135 69.521  124.214 1.00 25.26 ?  225 ARG C N     1 
ATOM   12813 C  CA    . ARG C 2 246 ? 116.218 69.949  123.147 1.00 25.97 ?  225 ARG C CA    1 
ATOM   12814 C  C     . ARG C 2 246 ? 114.803 70.084  123.694 1.00 25.85 ?  225 ARG C C     1 
ATOM   12815 O  O     . ARG C 2 246 ? 114.108 71.052  123.379 1.00 25.01 ?  225 ARG C O     1 
ATOM   12816 C  CB    . ARG C 2 246 ? 116.245 68.985  121.942 1.00 26.65 ?  225 ARG C CB    1 
ATOM   12817 C  CG    . ARG C 2 246 ? 117.573 68.975  121.188 1.00 28.90 ?  225 ARG C CG    1 
ATOM   12818 C  CD    . ARG C 2 246 ? 117.479 68.327  119.786 1.00 31.26 ?  225 ARG C CD    1 
ATOM   12819 N  NE    . ARG C 2 246 ? 117.030 66.933  119.828 1.00 34.01 ?  225 ARG C NE    1 
ATOM   12820 C  CZ    . ARG C 2 246 ? 117.789 65.895  120.180 1.00 35.64 ?  225 ARG C CZ    1 
ATOM   12821 N  NH1   . ARG C 2 246 ? 119.056 66.069  120.535 1.00 36.11 1  225 ARG C NH1   1 
ATOM   12822 N  NH2   . ARG C 2 246 ? 117.273 64.671  120.179 1.00 37.05 ?  225 ARG C NH2   1 
ATOM   12823 N  N     . GLU C 2 247 ? 114.385 69.121  124.520 1.00 26.01 ?  226 GLU C N     1 
ATOM   12824 C  CA    . GLU C 2 247 ? 113.084 69.194  125.195 1.00 26.48 ?  226 GLU C CA    1 
ATOM   12825 C  C     . GLU C 2 247 ? 112.981 70.457  126.049 1.00 25.72 ?  226 GLU C C     1 
ATOM   12826 O  O     . GLU C 2 247 ? 111.976 71.179  125.981 1.00 25.16 ?  226 GLU C O     1 
ATOM   12827 C  CB    . GLU C 2 247 ? 112.833 67.967  126.076 1.00 27.18 ?  226 GLU C CB    1 
ATOM   12828 C  CG    . GLU C 2 247 ? 111.365 67.793  126.447 1.00 30.38 ?  226 GLU C CG    1 
ATOM   12829 C  CD    . GLU C 2 247 ? 111.133 67.265  127.850 1.00 35.77 ?  226 GLU C CD    1 
ATOM   12830 O  OE1   . GLU C 2 247 ? 111.984 66.526  128.391 1.00 38.02 ?  226 GLU C OE1   1 
ATOM   12831 O  OE2   . GLU C 2 247 ? 110.071 67.593  128.422 1.00 40.39 -1 226 GLU C OE2   1 
ATOM   12832 N  N     . PHE C 2 248 ? 114.021 70.719  126.845 1.00 24.71 ?  227 PHE C N     1 
ATOM   12833 C  CA    . PHE C 2 248 ? 114.064 71.930  127.661 1.00 23.71 ?  227 PHE C CA    1 
ATOM   12834 C  C     . PHE C 2 248 ? 113.899 73.172  126.783 1.00 23.14 ?  227 PHE C C     1 
ATOM   12835 O  O     . PHE C 2 248 ? 113.081 74.042  127.087 1.00 22.40 ?  227 PHE C O     1 
ATOM   12836 C  CB    . PHE C 2 248 ? 115.363 72.037  128.480 1.00 23.85 ?  227 PHE C CB    1 
ATOM   12837 C  CG    . PHE C 2 248 ? 115.591 73.414  129.050 1.00 23.64 ?  227 PHE C CG    1 
ATOM   12838 C  CD1   . PHE C 2 248 ? 114.966 73.798  130.239 1.00 23.07 ?  227 PHE C CD1   1 
ATOM   12839 C  CD2   . PHE C 2 248 ? 116.376 74.353  128.358 1.00 23.04 ?  227 PHE C CD2   1 
ATOM   12840 C  CE1   . PHE C 2 248 ? 115.147 75.078  130.762 1.00 22.73 ?  227 PHE C CE1   1 
ATOM   12841 C  CE2   . PHE C 2 248 ? 116.561 75.641  128.864 1.00 23.31 ?  227 PHE C CE2   1 
ATOM   12842 C  CZ    . PHE C 2 248 ? 115.947 76.008  130.073 1.00 21.51 ?  227 PHE C CZ    1 
ATOM   12843 N  N     . ALA C 2 249 ? 114.674 73.239  125.699 1.00 22.95 ?  228 ALA C N     1 
ATOM   12844 C  CA    . ALA C 2 249 ? 114.707 74.424  124.832 1.00 22.96 ?  228 ALA C CA    1 
ATOM   12845 C  C     . ALA C 2 249 ? 113.361 74.665  124.154 1.00 23.31 ?  228 ALA C C     1 
ATOM   12846 O  O     . ALA C 2 249 ? 112.883 75.799  124.085 1.00 22.63 ?  228 ALA C O     1 
ATOM   12847 C  CB    . ALA C 2 249 ? 115.817 74.300  123.791 1.00 22.40 ?  228 ALA C CB    1 
ATOM   12848 N  N     . ILE C 2 250 ? 112.760 73.588  123.658 1.00 23.66 ?  229 ILE C N     1 
ATOM   12849 C  CA    . ILE C 2 250 ? 111.469 73.665  122.973 1.00 25.00 ?  229 ILE C CA    1 
ATOM   12850 C  C     . ILE C 2 250 ? 110.316 73.949  123.947 1.00 24.64 ?  229 ILE C C     1 
ATOM   12851 O  O     . ILE C 2 250 ? 109.460 74.795  123.661 1.00 24.26 ?  229 ILE C O     1 
ATOM   12852 C  CB    . ILE C 2 250 ? 111.223 72.413  122.074 1.00 25.43 ?  229 ILE C CB    1 
ATOM   12853 C  CG1   . ILE C 2 250 ? 112.159 72.475  120.858 1.00 27.27 ?  229 ILE C CG1   1 
ATOM   12854 C  CG2   . ILE C 2 250 ? 109.756 72.375  121.564 1.00 27.62 ?  229 ILE C CG2   1 
ATOM   12855 C  CD1   . ILE C 2 250 ? 112.694 71.118  120.379 1.00 31.32 ?  229 ILE C CD1   1 
ATOM   12856 N  N     . ASP C 2 251 ? 110.311 73.282  125.100 1.00 24.78 ?  230 ASP C N     1 
ATOM   12857 C  CA    . ASP C 2 251 ? 109.319 73.586  126.149 1.00 25.20 ?  230 ASP C CA    1 
ATOM   12858 C  C     . ASP C 2 251 ? 109.400 75.041  126.609 1.00 24.08 ?  230 ASP C C     1 
ATOM   12859 O  O     . ASP C 2 251 ? 108.370 75.704  126.810 1.00 23.34 ?  230 ASP C O     1 
ATOM   12860 C  CB    . ASP C 2 251 ? 109.505 72.691  127.382 1.00 25.73 ?  230 ASP C CB    1 
ATOM   12861 C  CG    . ASP C 2 251 ? 109.004 71.281  127.172 1.00 28.78 ?  230 ASP C CG    1 
ATOM   12862 O  OD1   . ASP C 2 251 ? 108.407 70.988  126.110 1.00 29.99 ?  230 ASP C OD1   1 
ATOM   12863 O  OD2   . ASP C 2 251 ? 109.218 70.459  128.087 1.00 33.31 -1 230 ASP C OD2   1 
ATOM   12864 N  N     . LEU C 2 252 ? 110.624 75.531  126.790 1.00 22.98 ?  231 LEU C N     1 
ATOM   12865 C  CA    . LEU C 2 252 ? 110.817 76.915  127.224 1.00 21.63 ?  231 LEU C CA    1 
ATOM   12866 C  C     . LEU C 2 252 ? 110.346 77.882  126.144 1.00 21.66 ?  231 LEU C C     1 
ATOM   12867 O  O     . LEU C 2 252 ? 109.692 78.886  126.430 1.00 19.41 ?  231 LEU C O     1 
ATOM   12868 C  CB    . LEU C 2 252 ? 112.283 77.191  127.560 1.00 21.89 ?  231 LEU C CB    1 
ATOM   12869 C  CG    . LEU C 2 252 ? 112.658 78.633  127.948 1.00 21.33 ?  231 LEU C CG    1 
ATOM   12870 C  CD1   . LEU C 2 252 ? 111.859 79.125  129.174 1.00 20.89 ?  231 LEU C CD1   1 
ATOM   12871 C  CD2   . LEU C 2 252 ? 114.167 78.711  128.194 1.00 20.31 ?  231 LEU C CD2   1 
ATOM   12872 N  N     . LEU C 2 253 ? 110.692 77.574  124.897 1.00 22.28 ?  232 LEU C N     1 
ATOM   12873 C  CA    . LEU C 2 253 ? 110.293 78.433  123.788 1.00 23.05 ?  232 LEU C CA    1 
ATOM   12874 C  C     . LEU C 2 253 ? 108.773 78.531  123.698 1.00 23.36 ?  232 LEU C C     1 
ATOM   12875 O  O     . LEU C 2 253 ? 108.226 79.644  123.618 1.00 22.96 ?  232 LEU C O     1 
ATOM   12876 C  CB    . LEU C 2 253 ? 110.893 77.951  122.466 1.00 23.53 ?  232 LEU C CB    1 
ATOM   12877 C  CG    . LEU C 2 253 ? 110.519 78.820  121.259 1.00 25.63 ?  232 LEU C CG    1 
ATOM   12878 C  CD1   . LEU C 2 253 ? 111.082 80.235  121.385 1.00 25.88 ?  232 LEU C CD1   1 
ATOM   12879 C  CD2   . LEU C 2 253 ? 111.005 78.154  119.981 1.00 27.67 ?  232 LEU C CD2   1 
ATOM   12880 N  N     . ASN C 2 254 ? 108.099 77.376  123.729 1.00 23.55 ?  233 ASN C N     1 
ATOM   12881 C  CA    . ASN C 2 254 ? 106.626 77.339  123.711 1.00 24.61 ?  233 ASN C CA    1 
ATOM   12882 C  C     . ASN C 2 254 ? 105.978 78.102  124.869 1.00 23.57 ?  233 ASN C C     1 
ATOM   12883 O  O     . ASN C 2 254 ? 104.998 78.819  124.679 1.00 23.52 ?  233 ASN C O     1 
ATOM   12884 C  CB    . ASN C 2 254 ? 106.108 75.899  123.665 1.00 24.99 ?  233 ASN C CB    1 
ATOM   12885 C  CG    . ASN C 2 254 ? 106.053 75.341  122.248 1.00 28.92 ?  233 ASN C CG    1 
ATOM   12886 O  OD1   . ASN C 2 254 ? 105.398 75.900  121.366 1.00 33.75 ?  233 ASN C OD1   1 
ATOM   12887 N  ND2   . ASN C 2 254 ? 106.737 74.235  122.029 1.00 30.99 ?  233 ASN C ND2   1 
ATOM   12888 N  N     . GLN C 2 255 ? 106.531 77.951  126.068 1.00 23.22 ?  234 GLN C N     1 
ATOM   12889 C  CA    . GLN C 2 255 ? 106.013 78.670  127.224 1.00 22.54 ?  234 GLN C CA    1 
ATOM   12890 C  C     . GLN C 2 255 ? 106.171 80.196  127.061 1.00 22.00 ?  234 GLN C C     1 
ATOM   12891 O  O     . GLN C 2 255 ? 105.236 80.967  127.340 1.00 21.73 ?  234 GLN C O     1 
ATOM   12892 C  CB    . GLN C 2 255 ? 106.691 78.183  128.504 1.00 22.85 ?  234 GLN C CB    1 
ATOM   12893 C  CG    . GLN C 2 255 ? 106.000 78.656  129.766 1.00 23.87 ?  234 GLN C CG    1 
ATOM   12894 C  CD    . GLN C 2 255 ? 106.699 78.194  131.040 1.00 24.95 ?  234 GLN C CD    1 
ATOM   12895 O  OE1   . GLN C 2 255 ? 107.619 77.370  131.001 1.00 24.21 ?  234 GLN C OE1   1 
ATOM   12896 N  NE2   . GLN C 2 255 ? 106.277 78.750  132.177 1.00 25.97 ?  234 GLN C NE2   1 
ATOM   12897 N  N     . LEU C 2 256 ? 107.345 80.623  126.613 1.00 21.27 ?  235 LEU C N     1 
ATOM   12898 C  CA    . LEU C 2 256 ? 107.594 82.037  126.351 1.00 21.37 ?  235 LEU C CA    1 
ATOM   12899 C  C     . LEU C 2 256 ? 106.714 82.544  125.205 1.00 21.21 ?  235 LEU C C     1 
ATOM   12900 O  O     . LEU C 2 256 ? 106.189 83.655  125.255 1.00 20.75 ?  235 LEU C O     1 
ATOM   12901 C  CB    . LEU C 2 256 ? 109.074 82.256  126.009 1.00 20.93 ?  235 LEU C CB    1 
ATOM   12902 C  CG    . LEU C 2 256 ? 110.116 82.136  127.124 1.00 21.74 ?  235 LEU C CG    1 
ATOM   12903 C  CD1   . LEU C 2 256 ? 111.529 82.264  126.535 1.00 20.15 ?  235 LEU C CD1   1 
ATOM   12904 C  CD2   . LEU C 2 256 ? 109.898 83.166  128.231 1.00 20.90 ?  235 LEU C CD2   1 
ATOM   12905 N  N     . TYR C 2 257 ? 106.580 81.719  124.172 1.00 21.68 ?  236 TYR C N     1 
ATOM   12906 C  CA    . TYR C 2 257 ? 105.776 82.047  122.995 1.00 22.40 ?  236 TYR C CA    1 
ATOM   12907 C  C     . TYR C 2 257 ? 104.310 82.317  123.372 1.00 23.31 ?  236 TYR C C     1 
ATOM   12908 O  O     . TYR C 2 257 ? 103.749 83.365  122.994 1.00 22.99 ?  236 TYR C O     1 
ATOM   12909 C  CB    . TYR C 2 257 ? 105.891 80.933  121.951 1.00 22.81 ?  236 TYR C CB    1 
ATOM   12910 C  CG    . TYR C 2 257 ? 104.991 81.091  120.741 1.00 23.76 ?  236 TYR C CG    1 
ATOM   12911 C  CD1   . TYR C 2 257 ? 105.191 82.129  119.827 1.00 24.05 ?  236 TYR C CD1   1 
ATOM   12912 C  CD2   . TYR C 2 257 ? 103.933 80.211  120.521 1.00 24.04 ?  236 TYR C CD2   1 
ATOM   12913 C  CE1   . TYR C 2 257 ? 104.360 82.285  118.723 1.00 24.40 ?  236 TYR C CE1   1 
ATOM   12914 C  CE2   . TYR C 2 257 ? 103.098 80.359  119.415 1.00 26.30 ?  236 TYR C CE2   1 
ATOM   12915 C  CZ    . TYR C 2 257 ? 103.327 81.391  118.524 1.00 25.80 ?  236 TYR C CZ    1 
ATOM   12916 O  OH    . TYR C 2 257 ? 102.512 81.528  117.437 1.00 28.42 ?  236 TYR C OH    1 
ATOM   12917 N  N     . GLU C 2 258 ? 103.712 81.405  124.145 1.00 22.99 ?  237 GLU C N     1 
ATOM   12918 C  CA    . GLU C 2 258 ? 102.311 81.541  124.559 1.00 24.46 ?  237 GLU C CA    1 
ATOM   12919 C  C     . GLU C 2 258 ? 102.078 82.812  125.358 1.00 23.86 ?  237 GLU C C     1 
ATOM   12920 O  O     . GLU C 2 258 ? 101.080 83.502  125.156 1.00 24.01 ?  237 GLU C O     1 
ATOM   12921 C  CB    . GLU C 2 258 ? 101.822 80.301  125.328 1.00 25.21 ?  237 GLU C CB    1 
ATOM   12922 C  CG    . GLU C 2 258 ? 101.695 79.036  124.449 1.00 30.12 ?  237 GLU C CG    1 
ATOM   12923 C  CD    . GLU C 2 258 ? 100.606 79.155  123.378 1.00 35.29 ?  237 GLU C CD    1 
ATOM   12924 O  OE1   . GLU C 2 258 ? 99.611  79.885  123.594 1.00 37.71 ?  237 GLU C OE1   1 
ATOM   12925 O  OE2   . GLU C 2 258 ? 100.745 78.510  122.312 1.00 39.07 -1 237 GLU C OE2   1 
ATOM   12926 N  N     . ASN C 2 259 ? 103.018 83.137  126.245 1.00 23.25 ?  238 ASN C N     1 
ATOM   12927 C  CA    . ASN C 2 259 ? 102.966 84.393  126.989 1.00 23.10 ?  238 ASN C CA    1 
ATOM   12928 C  C     . ASN C 2 259 ? 103.125 85.612  126.060 1.00 22.68 ?  238 ASN C C     1 
ATOM   12929 O  O     . ASN C 2 259 ? 102.425 86.618  126.210 1.00 22.73 ?  238 ASN C O     1 
ATOM   12930 C  CB    . ASN C 2 259 ? 104.028 84.390  128.091 1.00 23.22 ?  238 ASN C CB    1 
ATOM   12931 C  CG    . ASN C 2 259 ? 104.003 85.652  128.929 1.00 24.46 ?  238 ASN C CG    1 
ATOM   12932 O  OD1   . ASN C 2 259 ? 103.072 85.881  129.707 1.00 26.28 ?  238 ASN C OD1   1 
ATOM   12933 N  ND2   . ASN C 2 259 ? 105.029 86.481  128.775 1.00 24.93 ?  238 ASN C ND2   1 
ATOM   12934 N  N     . GLU C 2 260 ? 104.025 85.509  125.085 1.00 22.64 ?  239 GLU C N     1 
ATOM   12935 C  CA    . GLU C 2 260 ? 104.279 86.615  124.161 1.00 23.18 ?  239 GLU C CA    1 
ATOM   12936 C  C     . GLU C 2 260 ? 103.059 86.911  123.272 1.00 23.40 ?  239 GLU C C     1 
ATOM   12937 O  O     . GLU C 2 260 ? 102.793 88.075  122.933 1.00 23.57 ?  239 GLU C O     1 
ATOM   12938 C  CB    . GLU C 2 260 ? 105.529 86.349  123.312 1.00 23.19 ?  239 GLU C CB    1 
ATOM   12939 C  CG    . GLU C 2 260 ? 106.251 87.631  122.831 1.00 24.33 ?  239 GLU C CG    1 
ATOM   12940 C  CD    . GLU C 2 260 ? 106.840 88.471  123.979 1.00 27.99 ?  239 GLU C CD    1 
ATOM   12941 O  OE1   . GLU C 2 260 ? 106.838 88.027  125.148 1.00 27.36 ?  239 GLU C OE1   1 
ATOM   12942 O  OE2   . GLU C 2 260 ? 107.304 89.601  123.710 1.00 28.98 -1 239 GLU C OE2   1 
ATOM   12943 N  N     . LEU C 2 261 ? 102.319 85.862  122.909 1.00 23.35 ?  240 LEU C N     1 
ATOM   12944 C  CA    . LEU C 2 261 ? 101.058 86.027  122.169 1.00 23.74 ?  240 LEU C CA    1 
ATOM   12945 C  C     . LEU C 2 261 ? 100.065 86.924  122.912 1.00 23.80 ?  240 LEU C C     1 
ATOM   12946 O  O     . LEU C 2 261 ? 99.488  87.856  122.329 1.00 23.33 ?  240 LEU C O     1 
ATOM   12947 C  CB    . LEU C 2 261 ? 100.410 84.672  121.874 1.00 24.09 ?  240 LEU C CB    1 
ATOM   12948 C  CG    . LEU C 2 261 ? 101.110 83.769  120.858 1.00 24.07 ?  240 LEU C CG    1 
ATOM   12949 C  CD1   . LEU C 2 261 ? 100.336 82.465  120.709 1.00 24.77 ?  240 LEU C CD1   1 
ATOM   12950 C  CD2   . LEU C 2 261 ? 101.266 84.478  119.498 1.00 24.38 ?  240 LEU C CD2   1 
ATOM   12951 N  N     . GLU C 2 262 ? 99.864  86.632  124.192 1.00 23.41 ?  241 GLU C N     1 
ATOM   12952 C  CA    . GLU C 2 262 ? 98.971  87.426  125.033 1.00 24.02 ?  241 GLU C CA    1 
ATOM   12953 C  C     . GLU C 2 262 ? 99.466  88.871  125.197 1.00 22.91 ?  241 GLU C C     1 
ATOM   12954 O  O     . GLU C 2 262 ? 98.674  89.804  125.143 1.00 22.94 ?  241 GLU C O     1 
ATOM   12955 C  CB    . GLU C 2 262 ? 98.811  86.757  126.399 1.00 24.92 ?  241 GLU C CB    1 
ATOM   12956 C  CG    . GLU C 2 262 ? 98.104  85.412  126.359 1.00 27.82 ?  241 GLU C CG    1 
ATOM   12957 C  CD    . GLU C 2 262 ? 97.943  84.803  127.741 1.00 33.08 ?  241 GLU C CD    1 
ATOM   12958 O  OE1   . GLU C 2 262 ? 98.906  84.190  128.256 1.00 36.94 ?  241 GLU C OE1   1 
ATOM   12959 O  OE2   . GLU C 2 262 ? 96.845  84.931  128.313 1.00 37.48 -1 241 GLU C OE2   1 
ATOM   12960 N  N     . TYR C 2 263 ? 100.774 89.037  125.407 1.00 21.84 ?  242 TYR C N     1 
ATOM   12961 C  CA    . TYR C 2 263 ? 101.419 90.348  125.470 1.00 21.66 ?  242 TYR C CA    1 
ATOM   12962 C  C     . TYR C 2 263 ? 101.212 91.120  124.173 1.00 21.28 ?  242 TYR C C     1 
ATOM   12963 O  O     . TYR C 2 263 ? 100.882 92.314  124.195 1.00 21.14 ?  242 TYR C O     1 
ATOM   12964 C  CB    . TYR C 2 263 ? 102.927 90.173  125.708 1.00 21.44 ?  242 TYR C CB    1 
ATOM   12965 C  CG    . TYR C 2 263 ? 103.742 91.453  125.823 1.00 21.89 ?  242 TYR C CG    1 
ATOM   12966 C  CD1   . TYR C 2 263 ? 103.617 92.288  126.934 1.00 22.52 ?  242 TYR C CD1   1 
ATOM   12967 C  CD2   . TYR C 2 263 ? 104.667 91.806  124.836 1.00 22.58 ?  242 TYR C CD2   1 
ATOM   12968 C  CE1   . TYR C 2 263 ? 104.381 93.450  127.053 1.00 22.67 ?  242 TYR C CE1   1 
ATOM   12969 C  CE2   . TYR C 2 263 ? 105.442 92.967  124.947 1.00 24.03 ?  242 TYR C CE2   1 
ATOM   12970 C  CZ    . TYR C 2 263 ? 105.295 93.776  126.068 1.00 23.75 ?  242 TYR C CZ    1 
ATOM   12971 O  OH    . TYR C 2 263 ? 106.045 94.929  126.195 1.00 26.82 ?  242 TYR C OH    1 
ATOM   12972 N  N     . THR C 2 264 ? 101.410 90.435  123.049 1.00 20.66 ?  243 THR C N     1 
ATOM   12973 C  CA    . THR C 2 264 ? 101.271 91.055  121.724 1.00 20.99 ?  243 THR C CA    1 
ATOM   12974 C  C     . THR C 2 264 ? 99.836  91.541  121.495 1.00 21.22 ?  243 THR C C     1 
ATOM   12975 O  O     . THR C 2 264 ? 99.623  92.683  121.059 1.00 20.95 ?  243 THR C O     1 
ATOM   12976 C  CB    . THR C 2 264 ? 101.712 90.081  120.597 1.00 20.58 ?  243 THR C CB    1 
ATOM   12977 O  OG1   . THR C 2 264 ? 103.113 89.823  120.725 1.00 20.84 ?  243 THR C OG1   1 
ATOM   12978 C  CG2   . THR C 2 264 ? 101.444 90.669  119.210 1.00 20.90 ?  243 THR C CG2   1 
ATOM   12979 N  N     . GLU C 2 265 ? 98.858  90.692  121.815 1.00 21.62 ?  244 GLU C N     1 
ATOM   12980 C  CA    . GLU C 2 265 ? 97.453  91.073  121.666 1.00 23.46 ?  244 GLU C CA    1 
ATOM   12981 C  C     . GLU C 2 265 ? 97.104  92.255  122.549 1.00 23.33 ?  244 GLU C C     1 
ATOM   12982 O  O     . GLU C 2 265 ? 96.423  93.189  122.123 1.00 22.86 ?  244 GLU C O     1 
ATOM   12983 C  CB    . GLU C 2 265 ? 96.516  89.902  121.965 1.00 24.31 ?  244 GLU C CB    1 
ATOM   12984 C  CG    . GLU C 2 265 ? 96.527  88.823  120.888 1.00 27.63 ?  244 GLU C CG    1 
ATOM   12985 C  CD    . GLU C 2 265 ? 95.578  87.671  121.202 1.00 33.27 ?  244 GLU C CD    1 
ATOM   12986 O  OE1   . GLU C 2 265 ? 94.547  87.902  121.874 1.00 35.56 ?  244 GLU C OE1   1 
ATOM   12987 O  OE2   . GLU C 2 265 ? 95.861  86.531  120.768 1.00 35.96 -1 244 GLU C OE2   1 
ATOM   12988 N  N     . ASP C 2 266 ? 97.585  92.211  123.782 1.00 23.36 ?  245 ASP C N     1 
ATOM   12989 C  CA    . ASP C 2 266 ? 97.347  93.285  124.732 1.00 24.18 ?  245 ASP C CA    1 
ATOM   12990 C  C     . ASP C 2 266 ? 97.851  94.646  124.215 1.00 23.96 ?  245 ASP C C     1 
ATOM   12991 O  O     . ASP C 2 266 ? 97.184  95.664  124.380 1.00 24.19 ?  245 ASP C O     1 
ATOM   12992 C  CB    . ASP C 2 266 ? 98.016  92.939  126.060 1.00 25.14 ?  245 ASP C CB    1 
ATOM   12993 C  CG    . ASP C 2 266 ? 97.614  93.870  127.162 1.00 27.35 ?  245 ASP C CG    1 
ATOM   12994 O  OD1   . ASP C 2 266 ? 96.398  94.000  127.415 1.00 28.45 ?  245 ASP C OD1   1 
ATOM   12995 O  OD2   . ASP C 2 266 ? 98.522  94.472  127.774 1.00 31.99 -1 245 ASP C OD2   1 
ATOM   12996 N  N     . LEU C 2 267 ? 99.015  94.654  123.576 1.00 23.34 ?  246 LEU C N     1 
ATOM   12997 C  CA    . LEU C 2 267 ? 99.599  95.902  123.072 1.00 23.53 ?  246 LEU C CA    1 
ATOM   12998 C  C     . LEU C 2 267 ? 99.089  96.337  121.707 1.00 22.94 ?  246 LEU C C     1 
ATOM   12999 O  O     . LEU C 2 267 ? 98.851  97.525  121.482 1.00 23.14 ?  246 LEU C O     1 
ATOM   13000 C  CB    . LEU C 2 267 ? 101.120 95.784  123.012 1.00 23.37 ?  246 LEU C CB    1 
ATOM   13001 C  CG    . LEU C 2 267 ? 101.877 95.780  124.342 1.00 26.17 ?  246 LEU C CG    1 
ATOM   13002 C  CD1   . LEU C 2 267 ? 103.357 95.680  124.050 1.00 27.31 ?  246 LEU C CD1   1 
ATOM   13003 C  CD2   . LEU C 2 267 ? 101.583 97.048  125.138 1.00 28.08 ?  246 LEU C CD2   1 
ATOM   13004 N  N     . TYR C 2 268 ? 98.947  95.380  120.795 1.00 22.46 ?  247 TYR C N     1 
ATOM   13005 C  CA    . TYR C 2 268 ? 98.701  95.704  119.392 1.00 22.00 ?  247 TYR C CA    1 
ATOM   13006 C  C     . TYR C 2 268 ? 97.261  95.699  118.905 1.00 22.26 ?  247 TYR C C     1 
ATOM   13007 O  O     . TYR C 2 268 ? 96.998  96.236  117.829 1.00 22.17 ?  247 TYR C O     1 
ATOM   13008 C  CB    . TYR C 2 268 ? 99.553  94.814  118.478 1.00 21.73 ?  247 TYR C CB    1 
ATOM   13009 C  CG    . TYR C 2 268 ? 101.024 95.147  118.515 1.00 21.49 ?  247 TYR C CG    1 
ATOM   13010 C  CD1   . TYR C 2 268 ? 101.913 94.381  119.277 1.00 19.45 ?  247 TYR C CD1   1 
ATOM   13011 C  CD2   . TYR C 2 268 ? 101.528 96.241  117.802 1.00 22.71 ?  247 TYR C CD2   1 
ATOM   13012 C  CE1   . TYR C 2 268 ? 103.275 94.694  119.321 1.00 20.30 ?  247 TYR C CE1   1 
ATOM   13013 C  CE2   . TYR C 2 268 ? 102.894 96.565  117.833 1.00 21.69 ?  247 TYR C CE2   1 
ATOM   13014 C  CZ    . TYR C 2 268 ? 103.755 95.778  118.582 1.00 21.40 ?  247 TYR C CZ    1 
ATOM   13015 O  OH    . TYR C 2 268 ? 105.090 96.089  118.606 1.00 22.11 ?  247 TYR C OH    1 
ATOM   13016 N  N     . ASP C 2 269 ? 96.335  95.085  119.650 1.00 22.40 ?  248 ASP C N     1 
ATOM   13017 C  CA    . ASP C 2 269 ? 94.924  95.089  119.223 1.00 22.75 ?  248 ASP C CA    1 
ATOM   13018 C  C     . ASP C 2 269 ? 94.398  96.508  119.001 1.00 22.55 ?  248 ASP C C     1 
ATOM   13019 O  O     . ASP C 2 269 ? 93.642  96.748  118.051 1.00 22.22 ?  248 ASP C O     1 
ATOM   13020 C  CB    . ASP C 2 269 ? 94.009  94.320  120.195 1.00 23.03 ?  248 ASP C CB    1 
ATOM   13021 C  CG    . ASP C 2 269 ? 94.049  92.816  119.981 1.00 25.02 ?  248 ASP C CG    1 
ATOM   13022 O  OD1   . ASP C 2 269 ? 94.614  92.347  118.970 1.00 26.85 ?  248 ASP C OD1   1 
ATOM   13023 O  OD2   . ASP C 2 269 ? 93.500  92.089  120.834 1.00 28.74 -1 248 ASP C OD2   1 
ATOM   13024 N  N     . GLN C 2 270 ? 94.807  97.445  119.861 1.00 22.21 ?  249 GLN C N     1 
ATOM   13025 C  CA    . GLN C 2 270 ? 94.339  98.845  119.740 1.00 22.39 ?  249 GLN C CA    1 
ATOM   13026 C  C     . GLN C 2 270 ? 94.883  99.595  118.517 1.00 21.65 ?  249 GLN C C     1 
ATOM   13027 O  O     . GLN C 2 270 ? 94.386  100.672 118.186 1.00 21.70 ?  249 GLN C O     1 
ATOM   13028 C  CB    . GLN C 2 270 ? 94.594  99.648  121.026 1.00 22.53 ?  249 GLN C CB    1 
ATOM   13029 C  CG    . GLN C 2 270 ? 96.079  99.804  121.443 1.00 22.73 ?  249 GLN C CG    1 
ATOM   13030 C  CD    . GLN C 2 270 ? 96.221  100.610 122.718 1.00 25.39 ?  249 GLN C CD    1 
ATOM   13031 O  OE1   . GLN C 2 270 ? 95.251  100.799 123.453 1.00 27.88 ?  249 GLN C OE1   1 
ATOM   13032 N  NE2   . GLN C 2 270 ? 97.428  101.101 122.987 1.00 24.88 ?  249 GLN C NE2   1 
ATOM   13033 N  N     . VAL C 2 271 ? 95.897  99.030  117.858 1.00 20.91 ?  250 VAL C N     1 
ATOM   13034 C  CA    . VAL C 2 271 ? 96.458  99.622  116.621 1.00 20.62 ?  250 VAL C CA    1 
ATOM   13035 C  C     . VAL C 2 271 ? 96.267  98.699  115.402 1.00 20.53 ?  250 VAL C C     1 
ATOM   13036 O  O     . VAL C 2 271 ? 96.702  99.021  114.284 1.00 20.05 ?  250 VAL C O     1 
ATOM   13037 C  CB    . VAL C 2 271 ? 97.955  100.082 116.780 1.00 20.32 ?  250 VAL C CB    1 
ATOM   13038 C  CG1   . VAL C 2 271 ? 98.072  101.212 117.797 1.00 20.35 ?  250 VAL C CG1   1 
ATOM   13039 C  CG2   . VAL C 2 271 ? 98.881  98.922  117.177 1.00 19.32 ?  250 VAL C CG2   1 
ATOM   13040 N  N     . GLY C 2 272 ? 95.605  97.564  115.632 1.00 20.29 ?  251 GLY C N     1 
ATOM   13041 C  CA    . GLY C 2 272 ? 95.176  96.667  114.555 1.00 20.51 ?  251 GLY C CA    1 
ATOM   13042 C  C     . GLY C 2 272 ? 96.248  95.765  113.964 1.00 20.99 ?  251 GLY C C     1 
ATOM   13043 O  O     . GLY C 2 272 ? 96.099  95.279  112.831 1.00 20.22 ?  251 GLY C O     1 
ATOM   13044 N  N     . LEU C 2 273 ? 97.328  95.535  114.717 1.00 20.76 ?  252 LEU C N     1 
ATOM   13045 C  CA    . LEU C 2 273 ? 98.510  94.883  114.145 1.00 21.38 ?  252 LEU C CA    1 
ATOM   13046 C  C     . LEU C 2 273 ? 98.898  93.537  114.751 1.00 21.86 ?  252 LEU C C     1 
ATOM   13047 O  O     . LEU C 2 273 ? 99.932  92.977  114.392 1.00 22.45 ?  252 LEU C O     1 
ATOM   13048 C  CB    . LEU C 2 273 ? 99.715  95.838  114.154 1.00 21.44 ?  252 LEU C CB    1 
ATOM   13049 C  CG    . LEU C 2 273 ? 99.599  97.177  113.422 1.00 22.02 ?  252 LEU C CG    1 
ATOM   13050 C  CD1   . LEU C 2 273 ? 100.876 97.984  113.629 1.00 22.86 ?  252 LEU C CD1   1 
ATOM   13051 C  CD2   . LEU C 2 273 ? 99.310  96.971  111.919 1.00 23.88 ?  252 LEU C CD2   1 
ATOM   13052 N  N     . SER C 2 274 ? 98.071  93.002  115.647 1.00 22.19 ?  253 SER C N     1 
ATOM   13053 C  CA    . SER C 2 274 ? 98.468  91.843  116.444 1.00 22.47 ?  253 SER C CA    1 
ATOM   13054 C  C     . SER C 2 274 ? 98.860  90.631  115.598 1.00 22.94 ?  253 SER C C     1 
ATOM   13055 O  O     . SER C 2 274 ? 99.878  89.997  115.856 1.00 22.07 ?  253 SER C O     1 
ATOM   13056 C  CB    . SER C 2 274 ? 97.362  91.467  117.434 1.00 22.91 ?  253 SER C CB    1 
ATOM   13057 O  OG    . SER C 2 274 ? 97.241  92.474  118.417 1.00 24.25 ?  253 SER C OG    1 
ATOM   13058 N  N     . HIS C 2 275 ? 98.069  90.339  114.569 1.00 24.59 ?  254 HIS C N     1 
ATOM   13059 C  CA    . HIS C 2 275 ? 98.328  89.185  113.700 1.00 25.66 ?  254 HIS C CA    1 
ATOM   13060 C  C     . HIS C 2 275 ? 99.661  89.321  112.947 1.00 26.01 ?  254 HIS C C     1 
ATOM   13061 O  O     . HIS C 2 275 ? 100.415 88.343  112.797 1.00 26.23 ?  254 HIS C O     1 
ATOM   13062 C  CB    . HIS C 2 275 ? 97.167  88.991  112.716 1.00 26.89 ?  254 HIS C CB    1 
ATOM   13063 C  CG    . HIS C 2 275 ? 97.303  87.773  111.856 1.00 29.10 ?  254 HIS C CG    1 
ATOM   13064 N  ND1   . HIS C 2 275 ? 97.497  86.510  112.378 1.00 32.70 ?  254 HIS C ND1   1 
ATOM   13065 C  CD2   . HIS C 2 275 ? 97.270  87.622  110.512 1.00 31.68 ?  254 HIS C CD2   1 
ATOM   13066 C  CE1   . HIS C 2 275 ? 97.581  85.636  111.391 1.00 33.55 ?  254 HIS C CE1   1 
ATOM   13067 N  NE2   . HIS C 2 275 ? 97.431  86.282  110.250 1.00 33.71 ?  254 HIS C NE2   1 
ATOM   13068 N  N     . ASP C 2 276 ? 99.940  90.531  112.478 1.00 25.93 ?  255 ASP C N     1 
ATOM   13069 C  CA    . ASP C 2 276 ? 101.189 90.838  111.787 1.00 26.65 ?  255 ASP C CA    1 
ATOM   13070 C  C     . ASP C 2 276 ? 102.409 90.657  112.692 1.00 25.61 ?  255 ASP C C     1 
ATOM   13071 O  O     . ASP C 2 276 ? 103.403 90.044  112.279 1.00 25.34 ?  255 ASP C O     1 
ATOM   13072 C  CB    . ASP C 2 276 ? 101.155 92.260  111.224 1.00 27.44 ?  255 ASP C CB    1 
ATOM   13073 C  CG    . ASP C 2 276 ? 101.143 92.281  109.711 1.00 32.09 ?  255 ASP C CG    1 
ATOM   13074 O  OD1   . ASP C 2 276 ? 101.929 91.516  109.100 1.00 36.67 ?  255 ASP C OD1   1 
ATOM   13075 O  OD2   . ASP C 2 276 ? 100.342 93.048  109.128 1.00 36.30 -1 255 ASP C OD2   1 
ATOM   13076 N  N     . VAL C 2 277 ? 102.322 91.190  113.915 1.00 24.17 ?  256 VAL C N     1 
ATOM   13077 C  CA    . VAL C 2 277 ? 103.400 91.056  114.904 1.00 23.71 ?  256 VAL C CA    1 
ATOM   13078 C  C     . VAL C 2 277 ? 103.642 89.585  115.252 1.00 23.48 ?  256 VAL C C     1 
ATOM   13079 O  O     . VAL C 2 277 ? 104.790 89.154  115.372 1.00 23.08 ?  256 VAL C O     1 
ATOM   13080 C  CB    . VAL C 2 277 ? 103.115 91.855  116.206 1.00 23.27 ?  256 VAL C CB    1 
ATOM   13081 C  CG1   . VAL C 2 277 ? 104.262 91.694  117.209 1.00 24.02 ?  256 VAL C CG1   1 
ATOM   13082 C  CG2   . VAL C 2 277 ? 102.888 93.331  115.904 1.00 23.35 ?  256 VAL C CG2   1 
ATOM   13083 N  N     . LYS C 2 278 ? 102.564 88.822  115.411 1.00 23.36 ?  257 LYS C N     1 
ATOM   13084 C  CA    . LYS C 2 278 ? 102.666 87.390  115.694 1.00 24.12 ?  257 LYS C CA    1 
ATOM   13085 C  C     . LYS C 2 278 ? 103.473 86.636  114.639 1.00 24.30 ?  257 LYS C C     1 
ATOM   13086 O  O     . LYS C 2 278 ? 104.285 85.762  114.974 1.00 24.37 ?  257 LYS C O     1 
ATOM   13087 C  CB    . LYS C 2 278 ? 101.283 86.760  115.850 1.00 24.22 ?  257 LYS C CB    1 
ATOM   13088 C  CG    . LYS C 2 278 ? 100.590 87.107  117.157 1.00 24.96 ?  257 LYS C CG    1 
ATOM   13089 C  CD    . LYS C 2 278 ? 99.172  86.553  117.145 1.00 26.34 ?  257 LYS C CD    1 
ATOM   13090 C  CE    . LYS C 2 278 ? 98.429  86.907  118.404 1.00 27.16 ?  257 LYS C CE    1 
ATOM   13091 N  NZ    . LYS C 2 278 ? 97.053  86.328  118.332 1.00 29.60 1  257 LYS C NZ    1 
ATOM   13092 N  N     . LYS C 2 279 ? 103.258 86.975  113.369 1.00 24.55 ?  258 LYS C N     1 
ATOM   13093 C  CA    . LYS C 2 279 ? 104.042 86.382  112.290 1.00 24.85 ?  258 LYS C CA    1 
ATOM   13094 C  C     . LYS C 2 279 ? 105.520 86.734  112.449 1.00 24.57 ?  258 LYS C C     1 
ATOM   13095 O  O     . LYS C 2 279 ? 106.386 85.885  112.241 1.00 24.07 ?  258 LYS C O     1 
ATOM   13096 C  CB    . LYS C 2 279 ? 103.534 86.853  110.928 1.00 25.30 ?  258 LYS C CB    1 
ATOM   13097 C  CG    . LYS C 2 279 ? 102.102 86.467  110.637 1.00 26.63 ?  258 LYS C CG    1 
ATOM   13098 C  CD    . LYS C 2 279 ? 101.702 86.991  109.263 1.00 29.30 ?  258 LYS C CD    1 
ATOM   13099 C  CE    . LYS C 2 279 ? 100.343 86.493  108.877 1.00 31.79 ?  258 LYS C CE    1 
ATOM   13100 N  NZ    . LYS C 2 279 ? 99.839  87.280  107.724 1.00 33.80 1  258 LYS C NZ    1 
ATOM   13101 N  N     . PHE C 2 280 ? 105.790 87.978  112.846 1.00 24.29 ?  259 PHE C N     1 
ATOM   13102 C  CA    . PHE C 2 280 ? 107.161 88.474  113.031 1.00 24.90 ?  259 PHE C CA    1 
ATOM   13103 C  C     . PHE C 2 280 ? 107.894 87.749  114.174 1.00 24.86 ?  259 PHE C C     1 
ATOM   13104 O  O     . PHE C 2 280 ? 109.065 87.377  114.035 1.00 24.68 ?  259 PHE C O     1 
ATOM   13105 C  CB    . PHE C 2 280 ? 107.127 89.993  113.252 1.00 24.70 ?  259 PHE C CB    1 
ATOM   13106 C  CG    . PHE C 2 280 ? 108.478 90.669  113.220 1.00 25.70 ?  259 PHE C CG    1 
ATOM   13107 C  CD1   . PHE C 2 280 ? 109.297 90.587  112.094 1.00 26.86 ?  259 PHE C CD1   1 
ATOM   13108 C  CD2   . PHE C 2 280 ? 108.911 91.432  114.312 1.00 26.19 ?  259 PHE C CD2   1 
ATOM   13109 C  CE1   . PHE C 2 280 ? 110.540 91.236  112.057 1.00 26.66 ?  259 PHE C CE1   1 
ATOM   13110 C  CE2   . PHE C 2 280 ? 110.145 92.089  114.281 1.00 26.52 ?  259 PHE C CE2   1 
ATOM   13111 C  CZ    . PHE C 2 280 ? 110.965 91.985  113.150 1.00 26.23 ?  259 PHE C CZ    1 
ATOM   13112 N  N     . ILE C 2 281 ? 107.204 87.541  115.297 1.00 25.53 ?  260 ILE C N     1 
ATOM   13113 C  CA    . ILE C 2 281 ? 107.823 86.863  116.438 1.00 26.21 ?  260 ILE C CA    1 
ATOM   13114 C  C     . ILE C 2 281 ? 108.097 85.380  116.149 1.00 26.47 ?  260 ILE C C     1 
ATOM   13115 O  O     . ILE C 2 281 ? 109.094 84.839  116.615 1.00 26.52 ?  260 ILE C O     1 
ATOM   13116 C  CB    . ILE C 2 281 ? 107.067 87.092  117.792 1.00 26.27 ?  260 ILE C CB    1 
ATOM   13117 C  CG1   . ILE C 2 281 ? 105.818 86.216  117.908 1.00 27.37 ?  260 ILE C CG1   1 
ATOM   13118 C  CG2   . ILE C 2 281 ? 106.760 88.592  117.994 1.00 26.92 ?  260 ILE C CG2   1 
ATOM   13119 C  CD1   . ILE C 2 281 ? 105.079 86.346  119.241 1.00 29.51 ?  260 ILE C CD1   1 
ATOM   13120 N  N     . ARG C 2 282 ? 107.237 84.746  115.349 1.00 26.57 ?  261 ARG C N     1 
ATOM   13121 C  CA    . ARG C 2 282 ? 107.468 83.360  114.930 1.00 26.84 ?  261 ARG C CA    1 
ATOM   13122 C  C     . ARG C 2 282 ? 108.701 83.261  114.031 1.00 27.34 ?  261 ARG C C     1 
ATOM   13123 O  O     . ARG C 2 282 ? 109.527 82.369  114.203 1.00 27.54 ?  261 ARG C O     1 
ATOM   13124 C  CB    . ARG C 2 282 ? 106.238 82.766  114.240 1.00 26.98 ?  261 ARG C CB    1 
ATOM   13125 C  CG    . ARG C 2 282 ? 105.146 82.313  115.190 1.00 26.53 ?  261 ARG C CG    1 
ATOM   13126 C  CD    . ARG C 2 282 ? 104.075 81.469  114.468 1.00 27.77 ?  261 ARG C CD    1 
ATOM   13127 N  NE    . ARG C 2 282 ? 103.255 82.258  113.553 1.00 28.67 ?  261 ARG C NE    1 
ATOM   13128 C  CZ    . ARG C 2 282 ? 102.168 82.945  113.910 1.00 29.68 ?  261 ARG C CZ    1 
ATOM   13129 N  NH1   . ARG C 2 282 ? 101.749 82.951  115.175 1.00 28.31 1  261 ARG C NH1   1 
ATOM   13130 N  NH2   . ARG C 2 282 ? 101.489 83.623  112.998 1.00 29.15 ?  261 ARG C NH2   1 
ATOM   13131 N  N     . TYR C 2 283 ? 108.812 84.193  113.087 1.00 27.78 ?  262 TYR C N     1 
ATOM   13132 C  CA    . TYR C 2 283 ? 109.990 84.335  112.233 1.00 28.18 ?  262 TYR C CA    1 
ATOM   13133 C  C     . TYR C 2 283 ? 111.278 84.416  113.072 1.00 27.08 ?  262 TYR C C     1 
ATOM   13134 O  O     . TYR C 2 283 ? 112.254 83.688  112.832 1.00 26.51 ?  262 TYR C O     1 
ATOM   13135 C  CB    . TYR C 2 283 ? 109.838 85.590  111.365 1.00 29.11 ?  262 TYR C CB    1 
ATOM   13136 C  CG    . TYR C 2 283 ? 110.982 85.848  110.416 1.00 32.56 ?  262 TYR C CG    1 
ATOM   13137 C  CD1   . TYR C 2 283 ? 111.125 85.096  109.249 1.00 36.59 ?  262 TYR C CD1   1 
ATOM   13138 C  CD2   . TYR C 2 283 ? 111.917 86.857  110.673 1.00 36.34 ?  262 TYR C CD2   1 
ATOM   13139 C  CE1   . TYR C 2 283 ? 112.179 85.331  108.360 1.00 39.47 ?  262 TYR C CE1   1 
ATOM   13140 C  CE2   . TYR C 2 283 ? 112.978 87.105  109.782 1.00 39.23 ?  262 TYR C CE2   1 
ATOM   13141 C  CZ    . TYR C 2 283 ? 113.098 86.333  108.631 1.00 40.48 ?  262 TYR C CZ    1 
ATOM   13142 O  OH    . TYR C 2 283 ? 114.130 86.555  107.748 1.00 44.00 ?  262 TYR C OH    1 
ATOM   13143 N  N     . ASN C 2 284 ? 111.264 85.286  114.073 1.00 26.08 ?  263 ASN C N     1 
ATOM   13144 C  CA    . ASN C 2 284 ? 112.424 85.460  114.932 1.00 25.73 ?  263 ASN C CA    1 
ATOM   13145 C  C     . ASN C 2 284 ? 112.675 84.316  115.917 1.00 25.24 ?  263 ASN C C     1 
ATOM   13146 O  O     . ASN C 2 284 ? 113.835 84.020  116.233 1.00 25.56 ?  263 ASN C O     1 
ATOM   13147 C  CB    . ASN C 2 284 ? 112.382 86.830  115.610 1.00 25.69 ?  263 ASN C CB    1 
ATOM   13148 C  CG    . ASN C 2 284 ? 112.729 87.946  114.651 1.00 26.39 ?  263 ASN C CG    1 
ATOM   13149 O  OD1   . ASN C 2 284 ? 113.898 88.143  114.308 1.00 26.91 ?  263 ASN C OD1   1 
ATOM   13150 N  ND2   . ASN C 2 284 ? 111.720 88.678  114.202 1.00 27.56 ?  263 ASN C ND2   1 
ATOM   13151 N  N     . ALA C 2 285 ? 111.610 83.653  116.377 1.00 24.51 ?  264 ALA C N     1 
ATOM   13152 C  CA    . ALA C 2 285 ? 111.765 82.400  117.140 1.00 24.19 ?  264 ALA C CA    1 
ATOM   13153 C  C     . ALA C 2 285 ? 112.610 81.359  116.379 1.00 24.63 ?  264 ALA C C     1 
ATOM   13154 O  O     . ALA C 2 285 ? 113.477 80.710  116.961 1.00 24.01 ?  264 ALA C O     1 
ATOM   13155 C  CB    . ALA C 2 285 ? 110.417 81.809  117.506 1.00 23.63 ?  264 ALA C CB    1 
ATOM   13156 N  N     . ASN C 2 286 ? 112.351 81.211  115.080 1.00 24.66 ?  265 ASN C N     1 
ATOM   13157 C  CA    . ASN C 2 286 ? 113.150 80.328  114.230 1.00 25.24 ?  265 ASN C CA    1 
ATOM   13158 C  C     . ASN C 2 286 ? 114.625 80.708  114.155 1.00 25.09 ?  265 ASN C C     1 
ATOM   13159 O  O     . ASN C 2 286 ? 115.490 79.818  114.097 1.00 24.14 ?  265 ASN C O     1 
ATOM   13160 C  CB    . ASN C 2 286 ? 112.561 80.235  112.811 1.00 25.62 ?  265 ASN C CB    1 
ATOM   13161 C  CG    . ASN C 2 286 ? 111.302 79.384  112.758 1.00 26.46 ?  265 ASN C CG    1 
ATOM   13162 O  OD1   . ASN C 2 286 ? 110.972 78.677  113.714 1.00 27.14 ?  265 ASN C OD1   1 
ATOM   13163 N  ND2   . ASN C 2 286 ? 110.578 79.463  111.640 1.00 27.89 ?  265 ASN C ND2   1 
ATOM   13164 N  N     . LYS C 2 287 ? 114.897 82.016  114.137 1.00 24.99 ?  266 LYS C N     1 
ATOM   13165 C  CA    . LYS C 2 287 ? 116.262 82.546  114.154 1.00 25.91 ?  266 LYS C CA    1 
ATOM   13166 C  C     . LYS C 2 287 ? 116.951 82.246  115.481 1.00 25.23 ?  266 LYS C C     1 
ATOM   13167 O  O     . LYS C 2 287 ? 118.139 81.918  115.505 1.00 25.34 ?  266 LYS C O     1 
ATOM   13168 C  CB    . LYS C 2 287 ? 116.279 84.058  113.927 1.00 25.96 ?  266 LYS C CB    1 
ATOM   13169 C  CG    . LYS C 2 287 ? 116.022 84.517  112.500 1.00 29.60 ?  266 LYS C CG    1 
ATOM   13170 C  CD    . LYS C 2 287 ? 116.337 86.016  112.400 1.00 34.20 ?  266 LYS C CD    1 
ATOM   13171 C  CE    . LYS C 2 287 ? 116.204 86.541  110.993 1.00 37.67 ?  266 LYS C CE    1 
ATOM   13172 N  NZ    . LYS C 2 287 ? 116.658 87.970  110.934 1.00 39.48 1  266 LYS C NZ    1 
ATOM   13173 N  N     . ALA C 2 288 ? 116.211 82.375  116.580 1.00 24.87 ?  267 ALA C N     1 
ATOM   13174 C  CA    . ALA C 2 288 ? 116.732 81.999  117.908 1.00 24.23 ?  267 ALA C CA    1 
ATOM   13175 C  C     . ALA C 2 288 ? 117.091 80.509  117.968 1.00 24.24 ?  267 ALA C C     1 
ATOM   13176 O  O     . ALA C 2 288 ? 118.171 80.143  118.436 1.00 23.96 ?  267 ALA C O     1 
ATOM   13177 C  CB    . ALA C 2 288 ? 115.734 82.351  118.995 1.00 24.23 ?  267 ALA C CB    1 
ATOM   13178 N  N     . LEU C 2 289 ? 116.190 79.651  117.489 1.00 24.63 ?  268 LEU C N     1 
ATOM   13179 C  CA    . LEU C 2 289 ? 116.473 78.215  117.424 1.00 25.14 ?  268 LEU C CA    1 
ATOM   13180 C  C     . LEU C 2 289 ? 117.715 77.950  116.589 1.00 25.58 ?  268 LEU C C     1 
ATOM   13181 O  O     . LEU C 2 289 ? 118.574 77.170  116.985 1.00 25.42 ?  268 LEU C O     1 
ATOM   13182 C  CB    . LEU C 2 289 ? 115.277 77.419  116.877 1.00 25.28 ?  268 LEU C CB    1 
ATOM   13183 C  CG    . LEU C 2 289 ? 114.098 77.262  117.842 1.00 25.93 ?  268 LEU C CG    1 
ATOM   13184 C  CD1   . LEU C 2 289 ? 112.835 76.883  117.094 1.00 26.50 ?  268 LEU C CD1   1 
ATOM   13185 C  CD2   . LEU C 2 289 ? 114.397 76.269  118.980 1.00 25.20 ?  268 LEU C CD2   1 
ATOM   13186 N  N     . MET C 2 290 ? 117.821 78.618  115.440 1.00 26.32 ?  269 MET C N     1 
ATOM   13187 C  CA    . MET C 2 290 ? 118.991 78.436  114.586 1.00 27.41 ?  269 MET C CA    1 
ATOM   13188 C  C     . MET C 2 290 ? 120.290 78.880  115.255 1.00 26.66 ?  269 MET C C     1 
ATOM   13189 O  O     . MET C 2 290 ? 121.319 78.218  115.100 1.00 26.69 ?  269 MET C O     1 
ATOM   13190 C  CB    . MET C 2 290 ? 118.791 79.093  113.225 1.00 28.28 ?  269 MET C CB    1 
ATOM   13191 C  CG    . MET C 2 290 ? 118.176 78.121  112.219 1.00 32.91 ?  269 MET C CG    1 
ATOM   13192 S  SD    . MET C 2 290 ? 117.608 78.926  110.718 1.00 42.49 ?  269 MET C SD    1 
ATOM   13193 C  CE    . MET C 2 290 ? 115.832 78.879  110.952 1.00 38.74 ?  269 MET C CE    1 
ATOM   13194 N  N     . ASN C 2 291 ? 120.231 79.970  116.021 1.00 25.48 ?  270 ASN C N     1 
ATOM   13195 C  CA    . ASN C 2 291 ? 121.382 80.441  116.809 1.00 25.39 ?  270 ASN C CA    1 
ATOM   13196 C  C     . ASN C 2 291 ? 121.854 79.392  117.829 1.00 25.18 ?  270 ASN C C     1 
ATOM   13197 O  O     . ASN C 2 291 ? 123.034 79.358  118.206 1.00 24.73 ?  270 ASN C O     1 
ATOM   13198 C  CB    . ASN C 2 291 ? 121.053 81.764  117.513 1.00 24.83 ?  270 ASN C CB    1 
ATOM   13199 C  CG    . ASN C 2 291 ? 121.048 82.961  116.556 1.00 25.58 ?  270 ASN C CG    1 
ATOM   13200 O  OD1   . ASN C 2 291 ? 121.514 82.873  115.424 1.00 25.58 ?  270 ASN C OD1   1 
ATOM   13201 N  ND2   . ASN C 2 291 ? 120.518 84.082  117.020 1.00 24.32 ?  270 ASN C ND2   1 
ATOM   13202 N  N     . LEU C 2 292 ? 120.918 78.530  118.238 1.00 25.09 ?  271 LEU C N     1 
ATOM   13203 C  CA    . LEU C 2 292 ? 121.176 77.409  119.152 1.00 25.46 ?  271 LEU C CA    1 
ATOM   13204 C  C     . LEU C 2 292 ? 121.524 76.086  118.450 1.00 26.18 ?  271 LEU C C     1 
ATOM   13205 O  O     . LEU C 2 292 ? 121.738 75.051  119.107 1.00 26.06 ?  271 LEU C O     1 
ATOM   13206 C  CB    . LEU C 2 292 ? 119.976 77.224  120.089 1.00 25.19 ?  271 LEU C CB    1 
ATOM   13207 C  CG    . LEU C 2 292 ? 119.717 78.380  121.070 1.00 25.03 ?  271 LEU C CG    1 
ATOM   13208 C  CD1   . LEU C 2 292 ? 118.360 78.230  121.720 1.00 24.50 ?  271 LEU C CD1   1 
ATOM   13209 C  CD2   . LEU C 2 292 ? 120.830 78.446  122.129 1.00 25.64 ?  271 LEU C CD2   1 
ATOM   13210 N  N     . GLY C 2 293 ? 121.585 76.119  117.119 1.00 26.71 ?  272 GLY C N     1 
ATOM   13211 C  CA    . GLY C 2 293 ? 121.890 74.925  116.321 1.00 28.06 ?  272 GLY C CA    1 
ATOM   13212 C  C     . GLY C 2 293 ? 120.729 73.960  116.138 1.00 29.34 ?  272 GLY C C     1 
ATOM   13213 O  O     . GLY C 2 293 ? 120.938 72.771  115.853 1.00 29.73 ?  272 GLY C O     1 
ATOM   13214 N  N     . PHE C 2 294 ? 119.507 74.464  116.299 1.00 29.88 ?  273 PHE C N     1 
ATOM   13215 C  CA    . PHE C 2 294 ? 118.300 73.653  116.161 1.00 31.24 ?  273 PHE C CA    1 
ATOM   13216 C  C     . PHE C 2 294 ? 117.533 74.012  114.881 1.00 32.42 ?  273 PHE C C     1 
ATOM   13217 O  O     . PHE C 2 294 ? 117.687 75.115  114.337 1.00 32.30 ?  273 PHE C O     1 
ATOM   13218 C  CB    . PHE C 2 294 ? 117.393 73.808  117.389 1.00 30.82 ?  273 PHE C CB    1 
ATOM   13219 C  CG    . PHE C 2 294 ? 118.032 73.373  118.691 1.00 30.93 ?  273 PHE C CG    1 
ATOM   13220 C  CD1   . PHE C 2 294 ? 118.690 72.148  118.798 1.00 30.85 ?  273 PHE C CD1   1 
ATOM   13221 C  CD2   . PHE C 2 294 ? 117.962 74.187  119.813 1.00 30.30 ?  273 PHE C CD2   1 
ATOM   13222 C  CE1   . PHE C 2 294 ? 119.281 71.756  119.997 1.00 30.75 ?  273 PHE C CE1   1 
ATOM   13223 C  CE2   . PHE C 2 294 ? 118.537 73.798  121.025 1.00 30.41 ?  273 PHE C CE2   1 
ATOM   13224 C  CZ    . PHE C 2 294 ? 119.194 72.578  121.119 1.00 30.88 ?  273 PHE C CZ    1 
ATOM   13225 N  N     . ASP C 2 295 ? 116.725 73.069  114.402 1.00 33.81 ?  274 ASP C N     1 
ATOM   13226 C  CA    . ASP C 2 295 ? 115.872 73.278  113.228 1.00 35.32 ?  274 ASP C CA    1 
ATOM   13227 C  C     . ASP C 2 295 ? 114.742 74.281  113.519 1.00 35.36 ?  274 ASP C C     1 
ATOM   13228 O  O     . ASP C 2 295 ? 114.262 74.353  114.648 1.00 34.78 ?  274 ASP C O     1 
ATOM   13229 C  CB    . ASP C 2 295 ? 115.253 71.946  112.781 1.00 35.95 ?  274 ASP C CB    1 
ATOM   13230 C  CG    . ASP C 2 295 ? 116.293 70.930  112.315 1.00 37.98 ?  274 ASP C CG    1 
ATOM   13231 O  OD1   . ASP C 2 295 ? 117.379 71.328  111.840 1.00 39.83 ?  274 ASP C OD1   1 
ATOM   13232 O  OD2   . ASP C 2 295 ? 116.011 69.717  112.425 1.00 40.03 -1 274 ASP C OD2   1 
ATOM   13233 N  N     . PRO C 2 296 ? 114.308 75.048  112.500 1.00 36.33 ?  275 PRO C N     1 
ATOM   13234 C  CA    . PRO C 2 296 ? 113.141 75.941  112.668 1.00 36.92 ?  275 PRO C CA    1 
ATOM   13235 C  C     . PRO C 2 296 ? 111.882 75.192  113.134 1.00 37.68 ?  275 PRO C C     1 
ATOM   13236 O  O     . PRO C 2 296 ? 111.661 74.046  112.733 1.00 38.07 ?  275 PRO C O     1 
ATOM   13237 C  CB    . PRO C 2 296 ? 112.932 76.527  111.263 1.00 36.82 ?  275 PRO C CB    1 
ATOM   13238 C  CG    . PRO C 2 296 ? 113.779 75.671  110.332 1.00 37.42 ?  275 PRO C CG    1 
ATOM   13239 C  CD    . PRO C 2 296 ? 114.920 75.188  111.166 1.00 36.41 ?  275 PRO C CD    1 
ATOM   13240 N  N     . TYR C 2 297 ? 111.073 75.839  113.974 1.00 38.10 ?  276 TYR C N     1 
ATOM   13241 C  CA    . TYR C 2 297 ? 109.906 75.205  114.605 1.00 38.96 ?  276 TYR C CA    1 
ATOM   13242 C  C     . TYR C 2 297 ? 108.575 75.688  114.017 1.00 39.71 ?  276 TYR C C     1 
ATOM   13243 O  O     . TYR C 2 297 ? 107.581 74.954  114.026 1.00 40.18 ?  276 TYR C O     1 
ATOM   13244 C  CB    . TYR C 2 297 ? 109.941 75.478  116.113 1.00 38.94 ?  276 TYR C CB    1 
ATOM   13245 C  CG    . TYR C 2 297 ? 108.878 74.819  116.965 1.00 39.64 ?  276 TYR C CG    1 
ATOM   13246 C  CD1   . TYR C 2 297 ? 109.011 73.495  117.392 1.00 40.43 ?  276 TYR C CD1   1 
ATOM   13247 C  CD2   . TYR C 2 297 ? 107.768 75.537  117.400 1.00 41.04 ?  276 TYR C CD2   1 
ATOM   13248 C  CE1   . TYR C 2 297 ? 108.040 72.894  118.195 1.00 41.69 ?  276 TYR C CE1   1 
ATOM   13249 C  CE2   . TYR C 2 297 ? 106.790 74.948  118.201 1.00 41.60 ?  276 TYR C CE2   1 
ATOM   13250 C  CZ    . TYR C 2 297 ? 106.935 73.630  118.599 1.00 41.92 ?  276 TYR C CZ    1 
ATOM   13251 O  OH    . TYR C 2 297 ? 105.971 73.056  119.400 1.00 42.52 ?  276 TYR C OH    1 
ATOM   13252 N  N     . PHE C 2 298 ? 108.551 76.921  113.523 1.00 39.85 ?  277 PHE C N     1 
ATOM   13253 C  CA    . PHE C 2 298 ? 107.333 77.486  112.954 1.00 40.77 ?  277 PHE C CA    1 
ATOM   13254 C  C     . PHE C 2 298 ? 107.422 77.534  111.437 1.00 41.95 ?  277 PHE C C     1 
ATOM   13255 O  O     . PHE C 2 298 ? 108.511 77.686  110.885 1.00 41.91 ?  277 PHE C O     1 
ATOM   13256 C  CB    . PHE C 2 298 ? 107.082 78.891  113.514 1.00 39.94 ?  277 PHE C CB    1 
ATOM   13257 C  CG    . PHE C 2 298 ? 106.841 78.923  114.999 1.00 39.09 ?  277 PHE C CG    1 
ATOM   13258 C  CD1   . PHE C 2 298 ? 107.817 79.407  115.862 1.00 37.84 ?  277 PHE C CD1   1 
ATOM   13259 C  CD2   . PHE C 2 298 ? 105.633 78.484  115.533 1.00 38.97 ?  277 PHE C CD2   1 
ATOM   13260 C  CE1   . PHE C 2 298 ? 107.601 79.447  117.238 1.00 37.46 ?  277 PHE C CE1   1 
ATOM   13261 C  CE2   . PHE C 2 298 ? 105.405 78.518  116.904 1.00 38.20 ?  277 PHE C CE2   1 
ATOM   13262 C  CZ    . PHE C 2 298 ? 106.392 79.002  117.760 1.00 37.91 ?  277 PHE C CZ    1 
ATOM   13263 N  N     . GLU C 2 299 ? 106.283 77.400  110.756 1.00 43.74 ?  278 GLU C N     1 
ATOM   13264 C  CA    . GLU C 2 299 ? 106.273 77.483  109.292 1.00 45.61 ?  278 GLU C CA    1 
ATOM   13265 C  C     . GLU C 2 299 ? 106.486 78.926  108.833 1.00 46.04 ?  278 GLU C C     1 
ATOM   13266 O  O     . GLU C 2 299 ? 106.105 79.870  109.525 1.00 45.88 ?  278 GLU C O     1 
ATOM   13267 C  CB    . GLU C 2 299 ? 104.978 76.919  108.698 1.00 46.43 ?  278 GLU C CB    1 
ATOM   13268 C  CG    . GLU C 2 299 ? 105.168 76.299  107.303 1.00 48.82 ?  278 GLU C CG    1 
ATOM   13269 C  CD    . GLU C 2 299 ? 103.878 76.194  106.503 1.00 51.86 ?  278 GLU C CD    1 
ATOM   13270 O  OE1   . GLU C 2 299 ? 103.939 75.715  105.348 1.00 53.35 ?  278 GLU C OE1   1 
ATOM   13271 O  OE2   . GLU C 2 299 ? 102.805 76.591  107.016 1.00 53.10 -1 278 GLU C OE2   1 
ATOM   13272 N  N     . GLU C 2 300 ? 107.112 79.083  107.668 1.00 47.16 ?  279 GLU C N     1 
ATOM   13273 C  CA    . GLU C 2 300 ? 107.375 80.400  107.079 1.00 47.75 ?  279 GLU C CA    1 
ATOM   13274 C  C     . GLU C 2 300 ? 106.088 81.140  106.687 1.00 47.71 ?  279 GLU C C     1 
ATOM   13275 O  O     . GLU C 2 300 ? 105.133 80.526  106.197 1.00 47.77 ?  279 GLU C O     1 
ATOM   13276 C  CB    . GLU C 2 300 ? 108.325 80.268  105.875 1.00 48.42 ?  279 GLU C CB    1 
ATOM   13277 C  CG    . GLU C 2 300 ? 107.907 79.218  104.839 1.00 50.63 ?  279 GLU C CG    1 
ATOM   13278 C  CD    . GLU C 2 300 ? 109.074 78.713  103.990 1.00 53.06 ?  279 GLU C CD    1 
ATOM   13279 O  OE1   . GLU C 2 300 ? 109.786 79.547  103.381 1.00 54.35 ?  279 GLU C OE1   1 
ATOM   13280 O  OE2   . GLU C 2 300 ? 109.268 77.478  103.923 1.00 53.32 -1 279 GLU C OE2   1 
ATOM   13281 N  N     . GLU C 2 301 ? 106.072 82.451  106.929 1.00 47.40 ?  280 GLU C N     1 
ATOM   13282 C  CA    . GLU C 2 301 ? 104.941 83.324  106.586 1.00 47.46 ?  280 GLU C CA    1 
ATOM   13283 C  C     . GLU C 2 301 ? 105.443 84.649  106.000 1.00 47.31 ?  280 GLU C C     1 
ATOM   13284 O  O     . GLU C 2 301 ? 106.581 85.051  106.254 1.00 47.21 ?  280 GLU C O     1 
ATOM   13285 C  CB    . GLU C 2 301 ? 104.082 83.615  107.824 1.00 47.19 ?  280 GLU C CB    1 
ATOM   13286 C  CG    . GLU C 2 301 ? 103.440 82.398  108.494 1.00 47.14 ?  280 GLU C CG    1 
ATOM   13287 C  CD    . GLU C 2 301 ? 103.053 82.669  109.945 1.00 47.21 ?  280 GLU C CD    1 
ATOM   13288 O  OE1   . GLU C 2 301 ? 101.843 82.808  110.220 1.00 46.97 ?  280 GLU C OE1   1 
ATOM   13289 O  OE2   . GLU C 2 301 ? 103.959 82.755  110.808 1.00 46.13 -1 280 GLU C OE2   1 
ATOM   13290 N  N     . ASP C 2 302 ? 104.594 85.323  105.224 1.00 47.15 ?  281 ASP C N     1 
ATOM   13291 C  CA    . ASP C 2 302 ? 104.940 86.632  104.659 1.00 47.04 ?  281 ASP C CA    1 
ATOM   13292 C  C     . ASP C 2 302 ? 104.875 87.721  105.735 1.00 46.05 ?  281 ASP C C     1 
ATOM   13293 O  O     . ASP C 2 302 ? 103.815 87.963  106.321 1.00 46.10 ?  281 ASP C O     1 
ATOM   13294 C  CB    . ASP C 2 302 ? 104.015 86.999  103.484 1.00 47.66 ?  281 ASP C CB    1 
ATOM   13295 C  CG    . ASP C 2 302 ? 104.306 86.194  102.214 1.00 49.53 ?  281 ASP C CG    1 
ATOM   13296 O  OD1   . ASP C 2 302 ? 105.484 85.864  101.952 1.00 50.58 ?  281 ASP C OD1   1 
ATOM   13297 O  OD2   . ASP C 2 302 ? 103.344 85.913  101.459 1.00 51.14 -1 281 ASP C OD2   1 
ATOM   13298 N  N     . ILE C 2 303 ? 106.015 88.359  105.994 1.00 44.96 ?  282 ILE C N     1 
ATOM   13299 C  CA    . ILE C 2 303 ? 106.104 89.475  106.942 1.00 43.99 ?  282 ILE C CA    1 
ATOM   13300 C  C     . ILE C 2 303 ? 105.738 90.783  106.235 1.00 43.53 ?  282 ILE C C     1 
ATOM   13301 O  O     . ILE C 2 303 ? 106.016 90.940  105.045 1.00 43.52 ?  282 ILE C O     1 
ATOM   13302 C  CB    . ILE C 2 303 ? 107.531 89.584  107.557 1.00 43.84 ?  282 ILE C CB    1 
ATOM   13303 C  CG1   . ILE C 2 303 ? 107.967 88.253  108.199 1.00 43.91 ?  282 ILE C CG1   1 
ATOM   13304 C  CG2   . ILE C 2 303 ? 107.634 90.759  108.544 1.00 43.55 ?  282 ILE C CG2   1 
ATOM   13305 C  CD1   . ILE C 2 303 ? 107.058 87.736  109.318 1.00 42.76 ?  282 ILE C CD1   1 
ATOM   13306 N  N     . ASN C 2 304 ? 105.108 91.707  106.962 1.00 42.51 ?  283 ASN C N     1 
ATOM   13307 C  CA    . ASN C 2 304 ? 104.757 93.019  106.418 1.00 41.93 ?  283 ASN C CA    1 
ATOM   13308 C  C     . ASN C 2 304 ? 105.976 93.658  105.733 1.00 41.78 ?  283 ASN C C     1 
ATOM   13309 O  O     . ASN C 2 304 ? 107.014 93.852  106.380 1.00 41.13 ?  283 ASN C O     1 
ATOM   13310 C  CB    . ASN C 2 304 ? 104.220 93.932  107.531 1.00 41.83 ?  283 ASN C CB    1 
ATOM   13311 C  CG    . ASN C 2 304 ? 103.393 95.102  106.999 1.00 41.27 ?  283 ASN C CG    1 
ATOM   13312 O  OD1   . ASN C 2 304 ? 103.770 95.771  106.040 1.00 41.28 ?  283 ASN C OD1   1 
ATOM   13313 N  ND2   . ASN C 2 304 ? 102.260 95.353  107.638 1.00 40.67 ?  283 ASN C ND2   1 
ATOM   13314 N  N     . PRO C 2 305 ? 105.862 93.970  104.418 1.00 41.74 ?  284 PRO C N     1 
ATOM   13315 C  CA    . PRO C 2 305 ? 107.012 94.514  103.679 1.00 41.82 ?  284 PRO C CA    1 
ATOM   13316 C  C     . PRO C 2 305 ? 107.485 95.870  104.214 1.00 41.56 ?  284 PRO C C     1 
ATOM   13317 O  O     . PRO C 2 305 ? 108.642 96.242  104.008 1.00 41.46 ?  284 PRO C O     1 
ATOM   13318 C  CB    . PRO C 2 305 ? 106.494 94.633  102.232 1.00 42.14 ?  284 PRO C CB    1 
ATOM   13319 C  CG    . PRO C 2 305 ? 105.014 94.644  102.343 1.00 42.59 ?  284 PRO C CG    1 
ATOM   13320 C  CD    . PRO C 2 305 ? 104.682 93.799  103.549 1.00 42.05 ?  284 PRO C CD    1 
ATOM   13321 N  N     . ILE C 2 306 ? 106.599 96.584  104.904 1.00 41.19 ?  285 ILE C N     1 
ATOM   13322 C  CA    . ILE C 2 306 ? 106.947 97.838  105.572 1.00 41.47 ?  285 ILE C CA    1 
ATOM   13323 C  C     . ILE C 2 306 ? 108.042 97.597  106.619 1.00 41.71 ?  285 ILE C C     1 
ATOM   13324 O  O     . ILE C 2 306 ? 109.026 98.333  106.679 1.00 41.38 ?  285 ILE C O     1 
ATOM   13325 C  CB    . ILE C 2 306 ? 105.709 98.483  106.252 1.00 41.22 ?  285 ILE C CB    1 
ATOM   13326 C  CG1   . ILE C 2 306 ? 104.641 98.839  105.210 1.00 41.27 ?  285 ILE C CG1   1 
ATOM   13327 C  CG2   . ILE C 2 306 ? 106.112 99.706  107.073 1.00 40.37 ?  285 ILE C CG2   1 
ATOM   13328 C  CD1   . ILE C 2 306 ? 103.269 99.120  105.809 1.00 41.85 ?  285 ILE C CD1   1 
ATOM   13329 N  N     . VAL C 2 307 ? 107.854 96.559  107.432 1.00 42.33 ?  286 VAL C N     1 
ATOM   13330 C  CA    . VAL C 2 307 ? 108.821 96.171  108.464 1.00 43.36 ?  286 VAL C CA    1 
ATOM   13331 C  C     . VAL C 2 307 ? 110.161 95.730  107.861 1.00 44.51 ?  286 VAL C C     1 
ATOM   13332 O  O     . VAL C 2 307 ? 111.215 95.992  108.438 1.00 44.57 ?  286 VAL C O     1 
ATOM   13333 C  CB    . VAL C 2 307 ? 108.228 95.096  109.407 1.00 42.97 ?  286 VAL C CB    1 
ATOM   13334 C  CG1   . VAL C 2 307 ? 109.316 94.424  110.260 1.00 42.86 ?  286 VAL C CG1   1 
ATOM   13335 C  CG2   . VAL C 2 307 ? 107.169 95.730  110.288 1.00 41.93 ?  286 VAL C CG2   1 
ATOM   13336 N  N     . LEU C 2 308 ? 110.103 95.086  106.696 1.00 46.21 ?  287 LEU C N     1 
ATOM   13337 C  CA    . LEU C 2 308 ? 111.296 94.669  105.944 1.00 47.66 ?  287 LEU C CA    1 
ATOM   13338 C  C     . LEU C 2 308 ? 112.069 95.859  105.379 1.00 48.82 ?  287 LEU C C     1 
ATOM   13339 O  O     . LEU C 2 308 ? 113.306 95.829  105.314 1.00 49.02 ?  287 LEU C O     1 
ATOM   13340 C  CB    . LEU C 2 308 ? 110.914 93.689  104.826 1.00 47.95 ?  287 LEU C CB    1 
ATOM   13341 C  CG    . LEU C 2 308 ? 110.916 92.182  105.135 1.00 48.23 ?  287 LEU C CG    1 
ATOM   13342 C  CD1   . LEU C 2 308 ? 110.683 91.851  106.617 1.00 48.10 ?  287 LEU C CD1   1 
ATOM   13343 C  CD2   . LEU C 2 308 ? 109.926 91.435  104.246 1.00 48.81 ?  287 LEU C CD2   1 
ATOM   13344 N  N     . ASN C 2 309 ? 111.338 96.897  104.971 1.00 49.80 ?  288 ASN C N     1 
ATOM   13345 C  CA    . ASN C 2 309 ? 111.938 98.183  104.625 1.00 51.09 ?  288 ASN C CA    1 
ATOM   13346 C  C     . ASN C 2 309 ? 112.474 98.931  105.849 1.00 51.08 ?  288 ASN C C     1 
ATOM   13347 O  O     . ASN C 2 309 ? 113.379 99.756  105.727 1.00 51.41 ?  288 ASN C O     1 
ATOM   13348 C  CB    . ASN C 2 309 ? 110.957 99.057  103.839 1.00 51.37 ?  288 ASN C CB    1 
ATOM   13349 C  CG    . ASN C 2 309 ? 110.899 98.689  102.370 1.00 53.22 ?  288 ASN C CG    1 
ATOM   13350 O  OD1   . ASN C 2 309 ? 110.807 97.510  102.011 1.00 54.39 ?  288 ASN C OD1   1 
ATOM   13351 N  ND2   . ASN C 2 309 ? 110.956 99.698  101.508 1.00 54.70 ?  288 ASN C ND2   1 
ATOM   13352 N  N     . GLY C 2 310 ? 111.913 98.635  107.021 1.00 51.25 ?  289 GLY C N     1 
ATOM   13353 C  CA    . GLY C 2 310 ? 112.414 99.160  108.293 1.00 51.35 ?  289 GLY C CA    1 
ATOM   13354 C  C     . GLY C 2 310 ? 113.802 98.646  108.652 1.00 51.86 ?  289 GLY C C     1 
ATOM   13355 O  O     . GLY C 2 310 ? 114.513 99.266  109.452 1.00 51.49 ?  289 GLY C O     1 
ATOM   13356 N  N     . LEU C 2 311 ? 114.187 97.512  108.065 1.00 52.45 ?  290 LEU C N     1 
ATOM   13357 C  CA    . LEU C 2 311 ? 115.516 96.931  108.267 1.00 52.99 ?  290 LEU C CA    1 
ATOM   13358 C  C     . LEU C 2 311 ? 116.533 97.503  107.277 1.00 53.65 ?  290 LEU C C     1 
ATOM   13359 O  O     . LEU C 2 311 ? 116.488 97.219  106.073 1.00 54.22 ?  290 LEU C O     1 
ATOM   13360 C  CB    . LEU C 2 311 ? 115.464 95.404  108.152 1.00 53.08 ?  290 LEU C CB    1 
ATOM   13361 C  CG    . LEU C 2 311 ? 114.813 94.591  109.275 1.00 53.33 ?  290 LEU C CG    1 
ATOM   13362 C  CD1   . LEU C 2 311 ? 114.528 93.173  108.804 1.00 53.79 ?  290 LEU C CD1   1 
ATOM   13363 C  CD2   . LEU C 2 311 ? 115.682 94.578  110.535 1.00 53.22 ?  290 LEU C CD2   1 
ATOM   13364 N  N     . LYS C 2 330 ? 138.977 109.476 114.283 1.00 57.38 ?  309 LYS C N     1 
ATOM   13365 C  CA    . LYS C 2 330 ? 140.206 110.234 114.074 1.00 58.57 ?  309 LYS C CA    1 
ATOM   13366 C  C     . LYS C 2 330 ? 140.912 109.798 112.795 1.00 57.73 ?  309 LYS C C     1 
ATOM   13367 O  O     . LYS C 2 330 ? 140.724 108.678 112.322 1.00 59.72 ?  309 LYS C O     1 
ATOM   13368 C  CB    . LYS C 2 330 ? 141.149 110.069 115.268 1.00 55.66 ?  309 LYS C CB    1 
ATOM   13369 C  CG    . LYS C 2 330 ? 140.879 111.021 116.420 1.00 56.05 ?  309 LYS C CG    1 
ATOM   13370 C  CD    . LYS C 2 330 ? 142.029 111.009 117.415 1.00 57.52 ?  309 LYS C CD    1 
ATOM   13371 C  CE    . LYS C 2 330 ? 141.754 111.923 118.597 1.00 58.27 ?  309 LYS C CE    1 
ATOM   13372 N  NZ    . LYS C 2 330 ? 140.952 111.242 119.650 1.00 57.81 1  309 LYS C NZ    1 
ATOM   13373 N  N     . ALA C 2 331 ? 141.726 110.690 112.241 1.00 46.74 ?  310 ALA C N     1 
ATOM   13374 C  CA    . ALA C 2 331 ? 142.556 110.361 111.095 1.00 47.69 ?  310 ALA C CA    1 
ATOM   13375 C  C     . ALA C 2 331 ? 143.879 109.776 111.568 1.00 44.34 ?  310 ALA C C     1 
ATOM   13376 O  O     . ALA C 2 331 ? 144.406 110.152 112.618 1.00 44.88 ?  310 ALA C O     1 
ATOM   13377 C  CB    . ALA C 2 331 ? 142.806 111.595 110.226 1.00 44.94 ?  310 ALA C CB    1 
ATOM   13378 N  N     . THR C 2 332 ? 144.407 108.839 110.784 1.00 40.86 ?  311 THR C N     1 
ATOM   13379 C  CA    . THR C 2 332 ? 145.635 108.146 111.151 1.00 38.81 ?  311 THR C CA    1 
ATOM   13380 C  C     . THR C 2 332 ? 146.786 109.129 111.299 1.00 36.15 ?  311 THR C C     1 
ATOM   13381 O  O     . THR C 2 332 ? 146.998 109.990 110.441 1.00 43.30 ?  311 THR C O     1 
ATOM   13382 C  CB    . THR C 2 332 ? 145.975 107.084 110.102 1.00 39.78 ?  311 THR C CB    1 
ATOM   13383 O  OG1   . THR C 2 332 ? 144.918 106.119 110.038 1.00 41.99 ?  311 THR C OG1   1 
ATOM   13384 C  CG2   . THR C 2 332 ? 147.278 106.382 110.454 1.00 37.37 ?  311 THR C CG2   1 
ATOM   13385 N  N     . VAL C 2 333 ? 147.527 108.997 112.394 1.00 29.00 ?  312 VAL C N     1 
ATOM   13386 C  CA    . VAL C 2 333 ? 148.648 109.887 112.675 1.00 27.73 ?  312 VAL C CA    1 
ATOM   13387 C  C     . VAL C 2 333 ? 149.920 109.263 112.117 1.00 34.73 ?  312 VAL C C     1 
ATOM   13388 O  O     . VAL C 2 333 ? 150.309 108.160 112.514 1.00 34.24 ?  312 VAL C O     1 
ATOM   13389 C  CB    . VAL C 2 333 ? 148.775 110.155 114.180 1.00 29.67 ?  312 VAL C CB    1 
ATOM   13390 C  CG1   . VAL C 2 333 ? 150.070 110.895 114.480 1.00 33.09 ?  312 VAL C CG1   1 
ATOM   13391 C  CG2   . VAL C 2 333 ? 147.576 110.943 114.679 1.00 33.00 ?  312 VAL C CG2   1 
ATOM   13392 N  N     . GLU C 2 334 ? 150.567 109.968 111.194 1.00 31.99 ?  313 GLU C N     1 
ATOM   13393 C  CA    . GLU C 2 334 ? 151.810 109.520 110.598 1.00 30.19 ?  313 GLU C CA    1 
ATOM   13394 C  C     . GLU C 2 334 ? 152.882 110.579 110.815 1.00 35.47 ?  313 GLU C C     1 
ATOM   13395 O  O     . GLU C 2 334 ? 152.660 111.752 110.481 1.00 39.91 ?  313 GLU C O     1 
ATOM   13396 C  CB    . GLU C 2 334 ? 151.632 109.246 109.096 1.00 31.98 ?  313 GLU C CB    1 
ATOM   13397 C  CG    . GLU C 2 334 ? 152.665 108.298 108.513 1.00 30.40 ?  313 GLU C CG    1 
ATOM   13398 C  CD    . GLU C 2 334 ? 152.670 108.300 106.997 1.00 36.69 ?  313 GLU C CD    1 
ATOM   13399 O  OE1   . GLU C 2 334 ? 151.576 108.289 106.397 1.00 35.22 ?  313 GLU C OE1   1 
ATOM   13400 O  OE2   . GLU C 2 334 ? 153.770 108.292 106.405 1.00 37.50 -1 313 GLU C OE2   1 
ATOM   13401 N  N     . PRO C 2 335 ? 154.035 110.222 111.374 1.00 33.23 ?  314 PRO C N     1 
ATOM   13402 C  CA    . PRO C 2 335 ? 155.049 111.236 111.681 1.00 32.48 ?  314 PRO C CA    1 
ATOM   13403 C  C     . PRO C 2 335 ? 155.605 111.887 110.425 1.00 32.75 ?  314 PRO C C     1 
ATOM   13404 O  O     . PRO C 2 335 ? 155.695 111.271 109.360 1.00 33.62 ?  314 PRO C O     1 
ATOM   13405 C  CB    . PRO C 2 335 ? 156.132 110.440 112.418 1.00 27.14 ?  314 PRO C CB    1 
ATOM   13406 C  CG    . PRO C 2 335 ? 155.974 109.048 111.909 1.00 33.25 ?  314 PRO C CG    1 
ATOM   13407 C  CD    . PRO C 2 335 ? 154.496 108.863 111.704 1.00 31.97 ?  314 PRO C CD    1 
ATOM   13408 N  N     . LEU C 2 336 ? 155.977 113.156 110.566 1.00 31.37 ?  315 LEU C N     1 
ATOM   13409 C  CA    . LEU C 2 336 ? 156.572 113.903 109.469 1.00 25.32 ?  315 LEU C CA    1 
ATOM   13410 C  C     . LEU C 2 336 ? 158.012 113.463 109.246 1.00 30.05 ?  315 LEU C C     1 
ATOM   13411 O  O     . LEU C 2 336 ? 158.781 113.295 110.196 1.00 28.04 ?  315 LEU C O     1 
ATOM   13412 C  CB    . LEU C 2 336 ? 156.534 115.402 109.761 1.00 24.68 ?  315 LEU C CB    1 
ATOM   13413 C  CG    . LEU C 2 336 ? 155.319 116.206 109.302 1.00 29.53 ?  315 LEU C CG    1 
ATOM   13414 C  CD1   . LEU C 2 336 ? 155.269 117.527 110.049 1.00 23.58 ?  315 LEU C CD1   1 
ATOM   13415 C  CD2   . LEU C 2 336 ? 155.358 116.437 107.803 1.00 23.76 ?  315 LEU C CD2   1 
ATOM   13416 N  N     . LYS C 2 337 ? 158.375 113.283 107.982 1.00 29.08 ?  316 LYS C N     1 
ATOM   13417 C  CA    . LYS C 2 337 ? 159.747 112.973 107.622 1.00 24.90 ?  316 LYS C CA    1 
ATOM   13418 C  C     . LYS C 2 337 ? 160.518 114.257 107.326 1.00 25.51 ?  316 LYS C C     1 
ATOM   13419 O  O     . LYS C 2 337 ? 159.945 115.337 107.166 1.00 33.13 ?  316 LYS C O     1 
ATOM   13420 C  CB    . LYS C 2 337 ? 159.792 112.036 106.415 1.00 29.23 ?  316 LYS C CB    1 
ATOM   13421 C  CG    . LYS C 2 337 ? 158.879 110.828 106.519 1.00 29.66 ?  316 LYS C CG    1 
ATOM   13422 C  CD    . LYS C 2 337 ? 159.302 109.741 105.545 1.00 30.93 ?  316 LYS C CD    1 
ATOM   13423 C  CE    . LYS C 2 337 ? 158.723 108.390 105.931 1.00 33.14 ?  316 LYS C CE    1 
ATOM   13424 N  NZ    . LYS C 2 337 ? 157.368 108.519 106.538 1.00 33.67 1  316 LYS C NZ    1 
ATOM   13425 N  N     . ASP C 2 338 ? 161.844 114.129 107.263 1.00 26.51 ?  317 ASP C N     1 
ATOM   13426 C  CA    . ASP C 2 338 ? 162.672 115.270 106.894 1.00 29.94 ?  317 ASP C CA    1 
ATOM   13427 C  C     . ASP C 2 338 ? 162.398 115.703 105.460 1.00 29.65 ?  317 ASP C C     1 
ATOM   13428 O  O     . ASP C 2 338 ? 162.346 116.901 105.163 1.00 24.94 ?  317 ASP C O     1 
ATOM   13429 C  CB    . ASP C 2 338 ? 164.151 114.931 107.081 1.00 32.12 ?  317 ASP C CB    1 
ATOM   13430 C  CG    . ASP C 2 338 ? 164.643 115.228 108.482 1.00 35.61 ?  317 ASP C CG    1 
ATOM   13431 O  OD1   . ASP C 2 338 ? 164.460 114.371 109.373 1.00 36.45 ?  317 ASP C OD1   1 
ATOM   13432 O  OD2   . ASP C 2 338 ? 165.214 116.318 108.696 1.00 32.88 -1 317 ASP C OD2   1 
ATOM   13433 N  N     . ASP C 2 339 ? 162.208 114.738 104.558 1.00 31.98 ?  318 ASP C N     1 
ATOM   13434 C  CA    . ASP C 2 339 ? 161.957 115.044 103.155 1.00 23.82 ?  318 ASP C CA    1 
ATOM   13435 C  C     . ASP C 2 339 ? 160.600 115.694 102.921 1.00 21.90 ?  318 ASP C C     1 
ATOM   13436 O  O     . ASP C 2 339 ? 160.365 116.213 101.824 1.00 29.62 ?  318 ASP C O     1 
ATOM   13437 C  CB    . ASP C 2 339 ? 162.070 113.770 102.314 1.00 24.61 ?  318 ASP C CB    1 
ATOM   13438 C  CG    . ASP C 2 339 ? 163.502 113.296 102.167 1.00 36.61 ?  318 ASP C CG    1 
ATOM   13439 O  OD1   . ASP C 2 339 ? 164.415 114.147 102.158 1.00 34.94 ?  318 ASP C OD1   1 
ATOM   13440 O  OD2   . ASP C 2 339 ? 163.714 112.069 102.059 1.00 37.02 -1 318 ASP C OD2   1 
ATOM   13441 N  N     . ASP C 2 340 ? 159.704 115.674 103.908 1.00 21.75 ?  319 ASP C N     1 
ATOM   13442 C  CA    . ASP C 2 340 ? 158.407 116.324 103.767 1.00 12.52 ?  319 ASP C CA    1 
ATOM   13443 C  C     . ASP C 2 340 ? 158.505 117.843 103.776 1.00 11.68 ?  319 ASP C C     1 
ATOM   13444 O  O     . ASP C 2 340 ? 157.553 118.509 103.355 1.00 29.94 ?  319 ASP C O     1 
ATOM   13445 C  CB    . ASP C 2 340 ? 157.468 115.870 104.884 1.00 15.38 ?  319 ASP C CB    1 
ATOM   13446 C  CG    . ASP C 2 340 ? 156.984 114.451 104.695 1.00 27.80 ?  319 ASP C CG    1 
ATOM   13447 O  OD1   . ASP C 2 340 ? 156.291 113.937 105.596 1.00 35.11 ?  319 ASP C OD1   1 
ATOM   13448 O  OD2   . ASP C 2 340 ? 157.292 113.849 103.645 1.00 32.85 -1 319 ASP C OD2   1 
ATOM   13449 N  N     . PHE C 2 341 ? 159.619 118.400 104.240 1.00 19.10 ?  320 PHE C N     1 
ATOM   13450 C  CA    . PHE C 2 341 ? 159.793 119.840 104.355 1.00 9.08  ?  320 PHE C CA    1 
ATOM   13451 C  C     . PHE C 2 341 ? 160.458 120.459 103.135 1.00 17.46 ?  320 PHE C C     1 
ATOM   13452 O  O     . PHE C 2 341 ? 160.653 121.678 103.106 1.00 21.47 ?  320 PHE C O     1 
ATOM   13453 C  CB    . PHE C 2 341 ? 160.605 120.167 105.608 1.00 14.57 ?  320 PHE C CB    1 
ATOM   13454 C  CG    . PHE C 2 341 ? 159.855 119.945 106.888 1.00 10.84 ?  320 PHE C CG    1 
ATOM   13455 C  CD1   . PHE C 2 341 ? 159.142 120.973 107.474 1.00 9.48  ?  320 PHE C CD1   1 
ATOM   13456 C  CD2   . PHE C 2 341 ? 159.857 118.703 107.500 1.00 12.36 ?  320 PHE C CD2   1 
ATOM   13457 C  CE1   . PHE C 2 341 ? 158.449 120.770 108.650 1.00 7.91  ?  320 PHE C CE1   1 
ATOM   13458 C  CE2   . PHE C 2 341 ? 159.165 118.495 108.674 1.00 13.16 ?  320 PHE C CE2   1 
ATOM   13459 C  CZ    . PHE C 2 341 ? 158.460 119.529 109.249 1.00 4.56  ?  320 PHE C CZ    1 
ATOM   13460 N  N     . TYR C 2 342 ? 160.811 119.661 102.132 1.00 9.53  ?  321 TYR C N     1 
ATOM   13461 C  CA    . TYR C 2 342 ? 161.409 120.164 100.907 1.00 17.23 ?  321 TYR C CA    1 
ATOM   13462 C  C     . TYR C 2 342 ? 160.584 119.716 99.712  1.00 16.10 ?  321 TYR C C     1 
ATOM   13463 O  O     . TYR C 2 342 ? 160.014 118.622 99.700  1.00 16.88 ?  321 TYR C O     1 
ATOM   13464 C  CB    . TYR C 2 342 ? 162.876 119.716 100.734 1.00 17.88 ?  321 TYR C CB    1 
ATOM   13465 C  CG    . TYR C 2 342 ? 163.717 119.770 101.992 1.00 13.83 ?  321 TYR C CG    1 
ATOM   13466 C  CD1   . TYR C 2 342 ? 163.573 118.829 103.002 1.00 18.12 ?  321 TYR C CD1   1 
ATOM   13467 C  CD2   . TYR C 2 342 ? 164.655 120.777 102.170 1.00 16.03 ?  321 TYR C CD2   1 
ATOM   13468 C  CE1   . TYR C 2 342 ? 164.344 118.889 104.147 1.00 15.48 ?  321 TYR C CE1   1 
ATOM   13469 C  CE2   . TYR C 2 342 ? 165.428 120.844 103.311 1.00 17.80 ?  321 TYR C CE2   1 
ATOM   13470 C  CZ    . TYR C 2 342 ? 165.268 119.898 104.296 1.00 19.62 ?  321 TYR C CZ    1 
ATOM   13471 O  OH    . TYR C 2 342 ? 166.037 119.960 105.436 1.00 28.71 ?  321 TYR C OH    1 
ATOM   13472 N  N     . PHE C 2 343 ? 160.524 120.583 98.707  1.00 7.71  ?  322 PHE C N     1 
ATOM   13473 C  CA    . PHE C 2 343 ? 159.667 120.371 97.550  1.00 20.35 ?  322 PHE C CA    1 
ATOM   13474 C  C     . PHE C 2 343 ? 160.409 120.683 96.255  1.00 25.47 ?  322 PHE C C     1 
ATOM   13475 O  O     . PHE C 2 343 ? 161.386 121.431 96.251  1.00 26.11 ?  322 PHE C O     1 
ATOM   13476 C  CB    . PHE C 2 343 ? 158.410 121.236 97.666  1.00 15.28 ?  322 PHE C CB    1 
ATOM   13477 C  CG    . PHE C 2 343 ? 157.647 121.021 98.941  1.00 13.74 ?  322 PHE C CG    1 
ATOM   13478 C  CD1   . PHE C 2 343 ? 156.746 119.979 99.057  1.00 17.31 ?  322 PHE C CD1   1 
ATOM   13479 C  CD2   . PHE C 2 343 ? 157.848 121.850 100.029 1.00 4.75  ?  322 PHE C CD2   1 
ATOM   13480 C  CE1   . PHE C 2 343 ? 156.051 119.777 100.231 1.00 16.31 ?  322 PHE C CE1   1 
ATOM   13481 C  CE2   . PHE C 2 343 ? 157.158 121.651 101.204 1.00 5.64  ?  322 PHE C CE2   1 
ATOM   13482 C  CZ    . PHE C 2 343 ? 156.257 120.614 101.305 1.00 10.19 ?  322 PHE C CZ    1 
ATOM   13483 N  N     . ASP D 2 37  ? 122.906 111.833 143.688 1.00 32.44 ?  16  ASP D N     1 
ATOM   13484 C  CA    . ASP D 2 37  ? 123.359 113.175 143.311 1.00 32.83 ?  16  ASP D CA    1 
ATOM   13485 C  C     . ASP D 2 37  ? 124.477 113.185 142.270 1.00 31.65 ?  16  ASP D C     1 
ATOM   13486 O  O     . ASP D 2 37  ? 124.860 114.258 141.795 1.00 32.65 ?  16  ASP D O     1 
ATOM   13487 C  CB    . ASP D 2 37  ? 123.866 113.943 144.542 1.00 33.73 ?  16  ASP D CB    1 
ATOM   13488 C  CG    . ASP D 2 37  ? 122.774 114.230 145.561 1.00 36.81 ?  16  ASP D CG    1 
ATOM   13489 O  OD1   . ASP D 2 37  ? 123.134 114.515 146.729 1.00 39.69 ?  16  ASP D OD1   1 
ATOM   13490 O  OD2   . ASP D 2 37  ? 121.573 114.170 145.213 1.00 39.67 -1 16  ASP D OD2   1 
ATOM   13491 N  N     . PHE D 2 38  ? 125.007 112.016 141.916 1.00 29.55 ?  17  PHE D N     1 
ATOM   13492 C  CA    . PHE D 2 38  ? 126.284 111.985 141.201 1.00 27.75 ?  17  PHE D CA    1 
ATOM   13493 C  C     . PHE D 2 38  ? 126.429 110.974 140.051 1.00 26.21 ?  17  PHE D C     1 
ATOM   13494 O  O     . PHE D 2 38  ? 127.309 111.132 139.211 1.00 25.93 ?  17  PHE D O     1 
ATOM   13495 C  CB    . PHE D 2 38  ? 127.436 111.812 142.217 1.00 27.37 ?  17  PHE D CB    1 
ATOM   13496 C  CG    . PHE D 2 38  ? 127.338 110.550 143.032 1.00 27.32 ?  17  PHE D CG    1 
ATOM   13497 C  CD1   . PHE D 2 38  ? 127.832 109.347 142.537 1.00 27.01 ?  17  PHE D CD1   1 
ATOM   13498 C  CD2   . PHE D 2 38  ? 126.752 110.561 144.292 1.00 28.02 ?  17  PHE D CD2   1 
ATOM   13499 C  CE1   . PHE D 2 38  ? 127.738 108.175 143.284 1.00 27.66 ?  17  PHE D CE1   1 
ATOM   13500 C  CE2   . PHE D 2 38  ? 126.650 109.394 145.039 1.00 27.68 ?  17  PHE D CE2   1 
ATOM   13501 C  CZ    . PHE D 2 38  ? 127.145 108.197 144.533 1.00 27.47 ?  17  PHE D CZ    1 
ATOM   13502 N  N     . THR D 2 39  ? 125.583 109.950 140.011 1.00 24.88 ?  18  THR D N     1 
ATOM   13503 C  CA    . THR D 2 39  ? 125.764 108.845 139.056 1.00 23.81 ?  18  THR D CA    1 
ATOM   13504 C  C     . THR D 2 39  ? 125.644 109.255 137.577 1.00 23.56 ?  18  THR D C     1 
ATOM   13505 O  O     . THR D 2 39  ? 126.433 108.823 136.737 1.00 23.02 ?  18  THR D O     1 
ATOM   13506 C  CB    . THR D 2 39  ? 124.872 107.630 139.410 1.00 23.40 ?  18  THR D CB    1 
ATOM   13507 O  OG1   . THR D 2 39  ? 125.470 106.913 140.498 1.00 23.77 ?  18  THR D OG1   1 
ATOM   13508 C  CG2   . THR D 2 39  ? 124.732 106.674 138.237 1.00 22.31 ?  18  THR D CG2   1 
ATOM   13509 N  N     . GLN D 2 40  ? 124.674 110.101 137.254 1.00 23.78 ?  19  GLN D N     1 
ATOM   13510 C  CA    . GLN D 2 40  ? 124.545 110.550 135.864 1.00 23.88 ?  19  GLN D CA    1 
ATOM   13511 C  C     . GLN D 2 40  ? 125.743 111.392 135.415 1.00 24.09 ?  19  GLN D C     1 
ATOM   13512 O  O     . GLN D 2 40  ? 126.239 111.225 134.309 1.00 23.15 ?  19  GLN D O     1 
ATOM   13513 C  CB    . GLN D 2 40  ? 123.218 111.275 135.630 1.00 24.53 ?  19  GLN D CB    1 
ATOM   13514 C  CG    . GLN D 2 40  ? 122.028 110.334 135.736 1.00 24.06 ?  19  GLN D CG    1 
ATOM   13515 C  CD    . GLN D 2 40  ? 120.776 110.874 135.086 1.00 25.83 ?  19  GLN D CD    1 
ATOM   13516 O  OE1   . GLN D 2 40  ? 120.825 111.852 134.343 1.00 25.90 ?  19  GLN D OE1   1 
ATOM   13517 N  NE2   . GLN D 2 40  ? 119.643 110.221 135.345 1.00 23.56 ?  19  GLN D NE2   1 
ATOM   13518 N  N     . MET D 2 41  ? 126.232 112.260 136.292 1.00 24.07 ?  20  MET D N     1 
ATOM   13519 C  CA    . MET D 2 41  ? 127.457 113.008 136.008 1.00 25.53 ?  20  MET D CA    1 
ATOM   13520 C  C     . MET D 2 41  ? 128.666 112.088 135.745 1.00 24.24 ?  20  MET D C     1 
ATOM   13521 O  O     . MET D 2 41  ? 129.433 112.316 134.805 1.00 23.16 ?  20  MET D O     1 
ATOM   13522 C  CB    . MET D 2 41  ? 127.750 113.986 137.150 1.00 26.79 ?  20  MET D CB    1 
ATOM   13523 C  CG    . MET D 2 41  ? 129.017 114.803 136.983 1.00 32.62 ?  20  MET D CG    1 
ATOM   13524 S  SD    . MET D 2 41  ? 129.415 115.652 138.529 1.00 44.01 ?  20  MET D SD    1 
ATOM   13525 C  CE    . MET D 2 41  ? 131.188 115.874 138.356 1.00 41.93 ?  20  MET D CE    1 
ATOM   13526 N  N     . PHE D 2 42  ? 128.828 111.044 136.560 1.00 23.31 ?  21  PHE D N     1 
ATOM   13527 C  CA    . PHE D 2 42  ? 129.933 110.107 136.356 1.00 23.44 ?  21  PHE D CA    1 
ATOM   13528 C  C     . PHE D 2 42  ? 129.736 109.251 135.121 1.00 23.55 ?  21  PHE D C     1 
ATOM   13529 O  O     . PHE D 2 42  ? 130.701 108.909 134.447 1.00 23.74 ?  21  PHE D O     1 
ATOM   13530 C  CB    . PHE D 2 42  ? 130.176 109.239 137.593 1.00 22.97 ?  21  PHE D CB    1 
ATOM   13531 C  CG    . PHE D 2 42  ? 131.070 109.890 138.589 1.00 23.86 ?  21  PHE D CG    1 
ATOM   13532 C  CD1   . PHE D 2 42  ? 132.436 109.622 138.596 1.00 24.55 ?  21  PHE D CD1   1 
ATOM   13533 C  CD2   . PHE D 2 42  ? 130.562 110.806 139.492 1.00 24.06 ?  21  PHE D CD2   1 
ATOM   13534 C  CE1   . PHE D 2 42  ? 133.280 110.248 139.517 1.00 25.78 ?  21  PHE D CE1   1 
ATOM   13535 C  CE2   . PHE D 2 42  ? 131.400 111.438 140.416 1.00 25.25 ?  21  PHE D CE2   1 
ATOM   13536 C  CZ    . PHE D 2 42  ? 132.751 111.164 140.425 1.00 25.79 ?  21  PHE D CZ    1 
ATOM   13537 N  N     . TYR D 2 43  ? 128.479 108.928 134.823 1.00 24.08 ?  22  TYR D N     1 
ATOM   13538 C  CA    . TYR D 2 43  ? 128.147 108.240 133.585 1.00 24.74 ?  22  TYR D CA    1 
ATOM   13539 C  C     . TYR D 2 43  ? 128.708 109.029 132.399 1.00 25.72 ?  22  TYR D C     1 
ATOM   13540 O  O     . TYR D 2 43  ? 129.400 108.472 131.542 1.00 25.56 ?  22  TYR D O     1 
ATOM   13541 C  CB    . TYR D 2 43  ? 126.631 108.044 133.427 1.00 24.90 ?  22  TYR D CB    1 
ATOM   13542 C  CG    . TYR D 2 43  ? 126.272 107.481 132.059 1.00 24.38 ?  22  TYR D CG    1 
ATOM   13543 C  CD1   . TYR D 2 43  ? 126.218 106.110 131.845 1.00 23.96 ?  22  TYR D CD1   1 
ATOM   13544 C  CD2   . TYR D 2 43  ? 126.048 108.329 130.971 1.00 24.73 ?  22  TYR D CD2   1 
ATOM   13545 C  CE1   . TYR D 2 43  ? 125.925 105.589 130.582 1.00 23.42 ?  22  TYR D CE1   1 
ATOM   13546 C  CE2   . TYR D 2 43  ? 125.741 107.824 129.705 1.00 26.65 ?  22  TYR D CE2   1 
ATOM   13547 C  CZ    . TYR D 2 43  ? 125.686 106.452 129.523 1.00 25.68 ?  22  TYR D CZ    1 
ATOM   13548 O  OH    . TYR D 2 43  ? 125.387 105.949 128.277 1.00 26.57 ?  22  TYR D OH    1 
ATOM   13549 N  N     . ASN D 2 44  ? 128.394 110.322 132.365 1.00 26.77 ?  23  ASN D N     1 
ATOM   13550 C  CA    . ASN D 2 44  ? 128.832 111.205 131.290 1.00 28.57 ?  23  ASN D CA    1 
ATOM   13551 C  C     . ASN D 2 44  ? 130.343 111.245 131.152 1.00 28.70 ?  23  ASN D C     1 
ATOM   13552 O  O     . ASN D 2 44  ? 130.870 111.024 130.059 1.00 28.99 ?  23  ASN D O     1 
ATOM   13553 C  CB    . ASN D 2 44  ? 128.248 112.608 131.477 1.00 29.62 ?  23  ASN D CB    1 
ATOM   13554 C  CG    . ASN D 2 44  ? 126.743 112.642 131.241 1.00 32.44 ?  23  ASN D CG    1 
ATOM   13555 O  OD1   . ASN D 2 44  ? 126.187 111.767 130.565 1.00 34.30 ?  23  ASN D OD1   1 
ATOM   13556 N  ND2   . ASN D 2 44  ? 126.075 113.650 131.797 1.00 35.17 ?  23  ASN D ND2   1 
ATOM   13557 N  N     . GLN D 2 45  ? 131.030 111.481 132.266 1.00 28.97 ?  24  GLN D N     1 
ATOM   13558 C  CA    . GLN D 2 45  ? 132.487 111.558 132.263 1.00 29.99 ?  24  GLN D CA    1 
ATOM   13559 C  C     . GLN D 2 45  ? 133.141 110.233 131.840 1.00 29.69 ?  24  GLN D C     1 
ATOM   13560 O  O     . GLN D 2 45  ? 134.122 110.235 131.098 1.00 30.01 ?  24  GLN D O     1 
ATOM   13561 C  CB    . GLN D 2 45  ? 133.017 112.026 133.623 1.00 30.27 ?  24  GLN D CB    1 
ATOM   13562 C  CG    . GLN D 2 45  ? 134.527 112.355 133.625 1.00 32.29 ?  24  GLN D CG    1 
ATOM   13563 C  CD    . GLN D 2 45  ? 134.892 113.510 132.700 1.00 35.95 ?  24  GLN D CD    1 
ATOM   13564 O  OE1   . GLN D 2 45  ? 134.078 114.401 132.441 1.00 36.72 ?  24  GLN D OE1   1 
ATOM   13565 N  NE2   . GLN D 2 45  ? 136.124 113.499 132.200 1.00 37.05 ?  24  GLN D NE2   1 
ATOM   13566 N  N     . ASN D 2 46  ? 132.580 109.112 132.291 1.00 28.93 ?  25  ASN D N     1 
ATOM   13567 C  CA    . ASN D 2 46  ? 133.082 107.803 131.908 1.00 28.70 ?  25  ASN D CA    1 
ATOM   13568 C  C     . ASN D 2 46  ? 132.972 107.518 130.416 1.00 29.05 ?  25  ASN D C     1 
ATOM   13569 O  O     . ASN D 2 46  ? 133.964 107.142 129.783 1.00 28.51 ?  25  ASN D O     1 
ATOM   13570 C  CB    . ASN D 2 46  ? 132.403 106.688 132.714 1.00 28.36 ?  25  ASN D CB    1 
ATOM   13571 C  CG    . ASN D 2 46  ? 133.111 106.409 134.022 1.00 28.45 ?  25  ASN D CG    1 
ATOM   13572 O  OD1   . ASN D 2 46  ? 133.925 105.492 134.102 1.00 28.03 ?  25  ASN D OD1   1 
ATOM   13573 N  ND2   . ASN D 2 46  ? 132.831 107.215 135.045 1.00 26.53 ?  25  ASN D ND2   1 
ATOM   13574 N  N     . VAL D 2 47  ? 131.782 107.719 129.851 1.00 29.66 ?  26  VAL D N     1 
ATOM   13575 C  CA    . VAL D 2 47  ? 131.550 107.365 128.450 1.00 31.15 ?  26  VAL D CA    1 
ATOM   13576 C  C     . VAL D 2 47  ? 132.274 108.314 127.500 1.00 32.39 ?  26  VAL D C     1 
ATOM   13577 O  O     . VAL D 2 47  ? 132.684 107.912 126.413 1.00 32.80 ?  26  VAL D O     1 
ATOM   13578 C  CB    . VAL D 2 47  ? 130.036 107.218 128.078 1.00 31.08 ?  26  VAL D CB    1 
ATOM   13579 C  CG1   . VAL D 2 47  ? 129.352 106.204 128.986 1.00 31.09 ?  26  VAL D CG1   1 
ATOM   13580 C  CG2   . VAL D 2 47  ? 129.305 108.569 128.100 1.00 30.81 ?  26  VAL D CG2   1 
ATOM   13581 N  N     . LYS D 2 48  ? 132.464 109.562 127.912 1.00 33.28 ?  27  LYS D N     1 
ATOM   13582 C  CA    . LYS D 2 48  ? 133.191 110.484 127.055 1.00 34.87 ?  27  LYS D CA    1 
ATOM   13583 C  C     . LYS D 2 48  ? 134.718 110.262 127.072 1.00 34.91 ?  27  LYS D C     1 
ATOM   13584 O  O     . LYS D 2 48  ? 135.431 110.797 126.228 1.00 34.92 ?  27  LYS D O     1 
ATOM   13585 C  CB    . LYS D 2 48  ? 132.788 111.941 127.325 1.00 35.45 ?  27  LYS D CB    1 
ATOM   13586 C  CG    . LYS D 2 48  ? 133.518 112.646 128.445 1.00 37.41 ?  27  LYS D CG    1 
ATOM   13587 C  CD    . LYS D 2 48  ? 133.299 114.163 128.334 1.00 40.91 ?  27  LYS D CD    1 
ATOM   13588 C  CE    . LYS D 2 48  ? 134.318 114.932 129.179 1.00 42.46 ?  27  LYS D CE    1 
ATOM   13589 N  NZ    . LYS D 2 48  ? 134.242 116.409 128.981 1.00 45.13 1  27  LYS D NZ    1 
ATOM   13590 N  N     . GLN D 2 49  ? 135.194 109.455 128.023 1.00 34.66 ?  28  GLN D N     1 
ATOM   13591 C  CA    . GLN D 2 49  ? 136.602 109.076 128.119 1.00 34.64 ?  28  GLN D CA    1 
ATOM   13592 C  C     . GLN D 2 49  ? 136.884 107.762 127.394 1.00 34.20 ?  28  GLN D C     1 
ATOM   13593 O  O     . GLN D 2 49  ? 137.987 107.224 127.508 1.00 34.53 ?  28  GLN D O     1 
ATOM   13594 C  CB    . GLN D 2 49  ? 137.034 108.942 129.593 1.00 34.89 ?  28  GLN D CB    1 
ATOM   13595 C  CG    . GLN D 2 49  ? 137.509 110.237 130.247 1.00 36.47 ?  28  GLN D CG    1 
ATOM   13596 C  CD    . GLN D 2 49  ? 137.743 110.110 131.755 1.00 38.37 ?  28  GLN D CD    1 
ATOM   13597 O  OE1   . GLN D 2 49  ? 137.558 111.075 132.497 1.00 40.68 ?  28  GLN D OE1   1 
ATOM   13598 N  NE2   . GLN D 2 49  ? 138.146 108.924 132.211 1.00 38.57 ?  28  GLN D NE2   1 
ATOM   13599 N  N     . PHE D 2 50  ? 135.903 107.237 126.660 1.00 33.42 ?  29  PHE D N     1 
ATOM   13600 C  CA    . PHE D 2 50  ? 136.065 105.940 126.005 1.00 32.57 ?  29  PHE D CA    1 
ATOM   13601 C  C     . PHE D 2 50  ? 137.204 105.997 124.986 1.00 32.60 ?  29  PHE D C     1 
ATOM   13602 O  O     . PHE D 2 50  ? 137.354 106.982 124.257 1.00 32.39 ?  29  PHE D O     1 
ATOM   13603 C  CB    . PHE D 2 50  ? 134.760 105.458 125.351 1.00 32.77 ?  29  PHE D CB    1 
ATOM   13604 C  CG    . PHE D 2 50  ? 134.871 104.100 124.688 1.00 32.24 ?  29  PHE D CG    1 
ATOM   13605 C  CD1   . PHE D 2 50  ? 134.903 102.934 125.448 1.00 31.50 ?  29  PHE D CD1   1 
ATOM   13606 C  CD2   . PHE D 2 50  ? 134.945 103.992 123.304 1.00 33.60 ?  29  PHE D CD2   1 
ATOM   13607 C  CE1   . PHE D 2 50  ? 135.007 101.690 124.847 1.00 33.02 ?  29  PHE D CE1   1 
ATOM   13608 C  CE2   . PHE D 2 50  ? 135.054 102.745 122.685 1.00 33.78 ?  29  PHE D CE2   1 
ATOM   13609 C  CZ    . PHE D 2 50  ? 135.077 101.593 123.456 1.00 33.13 ?  29  PHE D CZ    1 
ATOM   13610 N  N     . TRP D 2 51  ? 138.004 104.939 124.955 1.00 31.95 ?  30  TRP D N     1 
ATOM   13611 C  CA    . TRP D 2 51  ? 139.146 104.840 124.046 1.00 32.03 ?  30  TRP D CA    1 
ATOM   13612 C  C     . TRP D 2 51  ? 139.444 103.373 123.770 1.00 33.03 ?  30  TRP D C     1 
ATOM   13613 O  O     . TRP D 2 51  ? 138.918 102.485 124.444 1.00 32.54 ?  30  TRP D O     1 
ATOM   13614 C  CB    . TRP D 2 51  ? 140.377 105.560 124.616 1.00 31.19 ?  30  TRP D CB    1 
ATOM   13615 C  CG    . TRP D 2 51  ? 140.869 104.994 125.934 1.00 28.11 ?  30  TRP D CG    1 
ATOM   13616 C  CD1   . TRP D 2 51  ? 140.342 105.224 127.167 1.00 26.51 ?  30  TRP D CD1   1 
ATOM   13617 C  CD2   . TRP D 2 51  ? 141.977 104.101 126.131 1.00 25.93 ?  30  TRP D CD2   1 
ATOM   13618 N  NE1   . TRP D 2 51  ? 141.056 104.536 128.127 1.00 24.52 ?  30  TRP D NE1   1 
ATOM   13619 C  CE2   . TRP D 2 51  ? 142.061 103.837 127.518 1.00 24.42 ?  30  TRP D CE2   1 
ATOM   13620 C  CE3   . TRP D 2 51  ? 142.911 103.503 125.272 1.00 25.37 ?  30  TRP D CE3   1 
ATOM   13621 C  CZ2   . TRP D 2 51  ? 143.045 103.005 128.068 1.00 24.00 ?  30  TRP D CZ2   1 
ATOM   13622 C  CZ3   . TRP D 2 51  ? 143.885 102.668 125.820 1.00 24.99 ?  30  TRP D CZ3   1 
ATOM   13623 C  CH2   . TRP D 2 51  ? 143.942 102.427 127.204 1.00 23.72 ?  30  TRP D CH2   1 
ATOM   13624 N  N     . LEU D 2 52  ? 140.278 103.130 122.763 1.00 34.81 ?  31  LEU D N     1 
ATOM   13625 C  CA    . LEU D 2 52  ? 140.652 101.786 122.352 1.00 36.58 ?  31  LEU D CA    1 
ATOM   13626 C  C     . LEU D 2 52  ? 142.164 101.698 122.167 1.00 37.80 ?  31  LEU D C     1 
ATOM   13627 O  O     . LEU D 2 52  ? 142.789 102.675 121.765 1.00 37.92 ?  31  LEU D O     1 
ATOM   13628 C  CB    . LEU D 2 52  ? 139.924 101.397 121.055 1.00 36.95 ?  31  LEU D CB    1 
ATOM   13629 C  CG    . LEU D 2 52  ? 138.474 100.906 121.135 1.00 38.15 ?  31  LEU D CG    1 
ATOM   13630 C  CD1   . LEU D 2 52  ? 138.068 100.252 119.819 1.00 39.50 ?  31  LEU D CD1   1 
ATOM   13631 C  CD2   . LEU D 2 52  ? 138.267 99.920  122.280 1.00 37.94 ?  31  LEU D CD2   1 
ATOM   13632 N  N     . PRO D 2 53  ? 142.760 100.523 122.452 1.00 39.26 ?  32  PRO D N     1 
ATOM   13633 C  CA    . PRO D 2 53  ? 144.216 100.322 122.330 1.00 40.41 ?  32  PRO D CA    1 
ATOM   13634 C  C     . PRO D 2 53  ? 144.773 100.681 120.945 1.00 41.91 ?  32  PRO D C     1 
ATOM   13635 O  O     . PRO D 2 53  ? 145.808 101.349 120.848 1.00 42.52 ?  32  PRO D O     1 
ATOM   13636 C  CB    . PRO D 2 53  ? 144.384 98.819  122.578 1.00 40.42 ?  32  PRO D CB    1 
ATOM   13637 C  CG    . PRO D 2 53  ? 143.171 98.407  123.310 1.00 40.01 ?  32  PRO D CG    1 
ATOM   13638 C  CD    . PRO D 2 53  ? 142.064 99.283  122.840 1.00 39.30 ?  32  PRO D CD    1 
ATOM   13639 N  N     . GLU D 2 54  ? 144.076 100.255 119.896 1.00 43.27 ?  33  GLU D N     1 
ATOM   13640 C  CA    . GLU D 2 54  ? 144.483 100.470 118.498 1.00 45.17 ?  33  GLU D CA    1 
ATOM   13641 C  C     . GLU D 2 54  ? 144.779 101.930 118.117 1.00 45.57 ?  33  GLU D C     1 
ATOM   13642 O  O     . GLU D 2 54  ? 145.485 102.187 117.137 1.00 46.08 ?  33  GLU D O     1 
ATOM   13643 C  CB    . GLU D 2 54  ? 143.416 99.900  117.550 1.00 45.55 ?  33  GLU D CB    1 
ATOM   13644 C  CG    . GLU D 2 54  ? 143.501 98.390  117.318 1.00 48.19 ?  33  GLU D CG    1 
ATOM   13645 C  CD    . GLU D 2 54  ? 143.265 97.563  118.575 1.00 50.61 ?  33  GLU D CD    1 
ATOM   13646 O  OE1   . GLU D 2 54  ? 142.279 97.834  119.300 1.00 51.10 ?  33  GLU D OE1   1 
ATOM   13647 O  OE2   . GLU D 2 54  ? 144.074 96.641  118.835 1.00 52.64 -1 33  GLU D OE2   1 
ATOM   13648 N  N     . GLU D 2 55  ? 144.240 102.873 118.889 1.00 45.74 ?  34  GLU D N     1 
ATOM   13649 C  CA    . GLU D 2 55  ? 144.392 104.305 118.605 1.00 46.28 ?  34  GLU D CA    1 
ATOM   13650 C  C     . GLU D 2 55  ? 145.836 104.803 118.744 1.00 46.49 ?  34  GLU D C     1 
ATOM   13651 O  O     . GLU D 2 55  ? 146.244 105.744 118.057 1.00 46.73 ?  34  GLU D O     1 
ATOM   13652 C  CB    . GLU D 2 55  ? 143.460 105.139 119.491 1.00 46.17 ?  34  GLU D CB    1 
ATOM   13653 C  CG    . GLU D 2 55  ? 141.965 104.892 119.267 1.00 47.10 ?  34  GLU D CG    1 
ATOM   13654 C  CD    . GLU D 2 55  ? 141.091 105.793 120.137 1.00 48.43 ?  34  GLU D CD    1 
ATOM   13655 O  OE1   . GLU D 2 55  ? 141.144 107.030 119.962 1.00 49.62 ?  34  GLU D OE1   1 
ATOM   13656 O  OE2   . GLU D 2 55  ? 140.349 105.266 120.992 1.00 47.11 -1 34  GLU D OE2   1 
ATOM   13657 N  N     . ILE D 2 56  ? 146.600 104.173 119.637 1.00 46.23 ?  35  ILE D N     1 
ATOM   13658 C  CA    . ILE D 2 56  ? 148.003 104.526 119.842 1.00 46.25 ?  35  ILE D CA    1 
ATOM   13659 C  C     . ILE D 2 56  ? 148.893 103.491 119.156 1.00 46.30 ?  35  ILE D C     1 
ATOM   13660 O  O     . ILE D 2 56  ? 148.834 102.301 119.478 1.00 46.36 ?  35  ILE D O     1 
ATOM   13661 C  CB    . ILE D 2 56  ? 148.372 104.611 121.364 1.00 45.84 ?  35  ILE D CB    1 
ATOM   13662 C  CG1   . ILE D 2 56  ? 147.278 105.316 122.193 1.00 46.15 ?  35  ILE D CG1   1 
ATOM   13663 C  CG2   . ILE D 2 56  ? 149.766 105.240 121.567 1.00 45.72 ?  35  ILE D CG2   1 
ATOM   13664 C  CD1   . ILE D 2 56  ? 147.014 106.776 121.844 1.00 47.27 ?  35  ILE D CD1   1 
ATOM   13665 N  N     . ALA D 2 57  ? 149.707 103.941 118.205 1.00 46.51 ?  36  ALA D N     1 
ATOM   13666 C  CA    . ALA D 2 57  ? 150.698 103.074 117.564 1.00 46.56 ?  36  ALA D CA    1 
ATOM   13667 C  C     . ALA D 2 57  ? 151.884 102.877 118.513 1.00 46.08 ?  36  ALA D C     1 
ATOM   13668 O  O     . ALA D 2 57  ? 152.468 103.853 118.980 1.00 45.70 ?  36  ALA D O     1 
ATOM   13669 C  CB    . ALA D 2 57  ? 151.161 103.673 116.238 1.00 47.10 ?  36  ALA D CB    1 
ATOM   13670 N  N     . LEU D 2 58  ? 152.240 101.621 118.780 1.00 45.66 ?  37  LEU D N     1 
ATOM   13671 C  CA    . LEU D 2 58  ? 153.258 101.312 119.794 1.00 45.27 ?  37  LEU D CA    1 
ATOM   13672 C  C     . LEU D 2 58  ? 154.686 101.112 119.290 1.00 45.25 ?  37  LEU D C     1 
ATOM   13673 O  O     . LEU D 2 58  ? 155.641 101.239 120.064 1.00 44.82 ?  37  LEU D O     1 
ATOM   13674 C  CB    . LEU D 2 58  ? 152.837 100.098 120.621 1.00 45.05 ?  37  LEU D CB    1 
ATOM   13675 C  CG    . LEU D 2 58  ? 151.797 100.389 121.700 1.00 45.41 ?  37  LEU D CG    1 
ATOM   13676 C  CD1   . LEU D 2 58  ? 151.409 99.103  122.403 1.00 45.40 ?  37  LEU D CD1   1 
ATOM   13677 C  CD2   . LEU D 2 58  ? 152.322 101.418 122.700 1.00 44.70 ?  37  LEU D CD2   1 
ATOM   13678 N  N     . ASN D 2 59  ? 154.836 100.815 118.002 1.00 45.33 ?  38  ASN D N     1 
ATOM   13679 C  CA    . ASN D 2 59  ? 156.128 100.376 117.467 1.00 45.22 ?  38  ASN D CA    1 
ATOM   13680 C  C     . ASN D 2 59  ? 157.292 101.360 117.648 1.00 44.39 ?  38  ASN D C     1 
ATOM   13681 O  O     . ASN D 2 59  ? 158.440 100.935 117.827 1.00 44.33 ?  38  ASN D O     1 
ATOM   13682 C  CB    . ASN D 2 59  ? 155.987 99.967  116.003 1.00 46.22 ?  38  ASN D CB    1 
ATOM   13683 C  CG    . ASN D 2 59  ? 156.882 98.796  115.638 1.00 47.90 ?  38  ASN D CG    1 
ATOM   13684 O  OD1   . ASN D 2 59  ? 157.768 98.917  114.793 1.00 49.28 ?  38  ASN D OD1   1 
ATOM   13685 N  ND2   . ASN D 2 59  ? 156.652 97.648  116.279 1.00 49.18 ?  38  ASN D ND2   1 
ATOM   13686 N  N     . GLY D 2 60  ? 156.991 102.659 117.627 1.00 43.45 ?  39  GLY D N     1 
ATOM   13687 C  CA    . GLY D 2 60  ? 157.998 103.711 117.803 1.00 42.42 ?  39  GLY D CA    1 
ATOM   13688 C  C     . GLY D 2 60  ? 158.663 103.778 119.176 1.00 41.55 ?  39  GLY D C     1 
ATOM   13689 O  O     . GLY D 2 60  ? 159.619 104.535 119.373 1.00 41.29 ?  39  GLY D O     1 
ATOM   13690 N  N     . ASP D 2 61  ? 158.158 102.999 120.130 1.00 40.35 ?  40  ASP D N     1 
ATOM   13691 C  CA    . ASP D 2 61  ? 158.789 102.893 121.451 1.00 39.53 ?  40  ASP D CA    1 
ATOM   13692 C  C     . ASP D 2 61  ? 160.106 102.130 121.425 1.00 39.38 ?  40  ASP D C     1 
ATOM   13693 O  O     . ASP D 2 61  ? 160.952 102.313 122.298 1.00 38.90 ?  40  ASP D O     1 
ATOM   13694 C  CB    . ASP D 2 61  ? 157.846 102.227 122.441 1.00 38.93 ?  40  ASP D CB    1 
ATOM   13695 C  CG    . ASP D 2 61  ? 156.899 103.201 123.081 1.00 38.21 ?  40  ASP D CG    1 
ATOM   13696 O  OD1   . ASP D 2 61  ? 156.973 104.414 122.783 1.00 38.79 ?  40  ASP D OD1   1 
ATOM   13697 O  OD2   . ASP D 2 61  ? 156.079 102.750 123.898 1.00 38.02 -1 40  ASP D OD2   1 
ATOM   13698 N  N     . LEU D 2 62  ? 160.270 101.275 120.421 1.00 39.82 ?  41  LEU D N     1 
ATOM   13699 C  CA    . LEU D 2 62  ? 161.473 100.465 120.277 1.00 40.22 ?  41  LEU D CA    1 
ATOM   13700 C  C     . LEU D 2 62  ? 162.714 101.328 120.055 1.00 40.40 ?  41  LEU D C     1 
ATOM   13701 O  O     . LEU D 2 62  ? 163.836 100.881 120.298 1.00 40.91 ?  41  LEU D O     1 
ATOM   13702 C  CB    . LEU D 2 62  ? 161.293 99.449  119.146 1.00 40.52 ?  41  LEU D CB    1 
ATOM   13703 C  CG    . LEU D 2 62  ? 160.225 98.372  119.371 1.00 41.03 ?  41  LEU D CG    1 
ATOM   13704 C  CD1   . LEU D 2 62  ? 160.081 97.493  118.136 1.00 42.53 ?  41  LEU D CD1   1 
ATOM   13705 C  CD2   . LEU D 2 62  ? 160.529 97.527  120.615 1.00 41.89 ?  41  LEU D CD2   1 
ATOM   13706 N  N     . LEU D 2 63  ? 162.493 102.570 119.615 1.00 40.20 ?  42  LEU D N     1 
ATOM   13707 C  CA    . LEU D 2 63  ? 163.553 103.546 119.366 1.00 39.85 ?  42  LEU D CA    1 
ATOM   13708 C  C     . LEU D 2 63  ? 164.125 104.169 120.653 1.00 38.90 ?  42  LEU D C     1 
ATOM   13709 O  O     . LEU D 2 63  ? 165.198 104.785 120.632 1.00 39.48 ?  42  LEU D O     1 
ATOM   13710 C  CB    . LEU D 2 63  ? 163.030 104.637 118.418 1.00 40.50 ?  42  LEU D CB    1 
ATOM   13711 C  CG    . LEU D 2 63  ? 163.938 105.337 117.394 1.00 41.98 ?  42  LEU D CG    1 
ATOM   13712 C  CD1   . LEU D 2 63  ? 164.636 104.351 116.463 1.00 43.07 ?  42  LEU D CD1   1 
ATOM   13713 C  CD2   . LEU D 2 63  ? 163.114 106.310 116.568 1.00 43.17 ?  42  LEU D CD2   1 
ATOM   13714 N  N     . THR D 2 64  ? 163.417 104.029 121.771 1.00 37.28 ?  43  THR D N     1 
ATOM   13715 C  CA    . THR D 2 64  ? 163.971 104.451 123.067 1.00 35.53 ?  43  THR D CA    1 
ATOM   13716 C  C     . THR D 2 64  ? 164.215 103.268 123.997 1.00 34.57 ?  43  THR D C     1 
ATOM   13717 O  O     . THR D 2 64  ? 165.113 103.311 124.842 1.00 34.23 ?  43  THR D O     1 
ATOM   13718 C  CB    . THR D 2 64  ? 163.124 105.527 123.781 1.00 35.18 ?  43  THR D CB    1 
ATOM   13719 O  OG1   . THR D 2 64  ? 161.745 105.147 123.796 1.00 34.59 ?  43  THR D OG1   1 
ATOM   13720 C  CG2   . THR D 2 64  ? 163.268 106.854 123.088 1.00 35.48 ?  43  THR D CG2   1 
ATOM   13721 N  N     . TRP D 2 65  ? 163.415 102.216 123.823 1.00 33.62 ?  44  TRP D N     1 
ATOM   13722 C  CA    . TRP D 2 65  ? 163.535 100.978 124.611 1.00 32.87 ?  44  TRP D CA    1 
ATOM   13723 C  C     . TRP D 2 65  ? 164.932 100.356 124.490 1.00 33.46 ?  44  TRP D C     1 
ATOM   13724 O  O     . TRP D 2 65  ? 165.519 99.935  125.488 1.00 32.58 ?  44  TRP D O     1 
ATOM   13725 C  CB    . TRP D 2 65  ? 162.459 99.974  124.169 1.00 32.09 ?  44  TRP D CB    1 
ATOM   13726 C  CG    . TRP D 2 65  ? 162.518 98.638  124.857 1.00 30.42 ?  44  TRP D CG    1 
ATOM   13727 C  CD1   . TRP D 2 65  ? 162.951 97.460  124.316 1.00 29.35 ?  44  TRP D CD1   1 
ATOM   13728 C  CD2   . TRP D 2 65  ? 162.124 98.340  126.205 1.00 28.04 ?  44  TRP D CD2   1 
ATOM   13729 N  NE1   . TRP D 2 65  ? 162.852 96.448  125.242 1.00 28.44 ?  44  TRP D NE1   1 
ATOM   13730 C  CE2   . TRP D 2 65  ? 162.352 96.961  126.410 1.00 28.14 ?  44  TRP D CE2   1 
ATOM   13731 C  CE3   . TRP D 2 65  ? 161.610 99.105  127.261 1.00 27.11 ?  44  TRP D CE3   1 
ATOM   13732 C  CZ2   . TRP D 2 65  ? 162.075 96.324  127.628 1.00 27.21 ?  44  TRP D CZ2   1 
ATOM   13733 C  CZ3   . TRP D 2 65  ? 161.327 98.469  128.473 1.00 27.45 ?  44  TRP D CZ3   1 
ATOM   13734 C  CH2   . TRP D 2 65  ? 161.557 97.089  128.640 1.00 27.25 ?  44  TRP D CH2   1 
ATOM   13735 N  N     . LYS D 2 66  ? 165.446 100.316 123.262 1.00 34.52 ?  45  LYS D N     1 
ATOM   13736 C  CA    . LYS D 2 66  ? 166.771 99.777  122.969 1.00 36.41 ?  45  LYS D CA    1 
ATOM   13737 C  C     . LYS D 2 66  ? 167.909 100.509 123.678 1.00 36.26 ?  45  LYS D C     1 
ATOM   13738 O  O     . LYS D 2 66  ? 168.992 99.948  123.840 1.00 36.52 ?  45  LYS D O     1 
ATOM   13739 C  CB    . LYS D 2 66  ? 167.022 99.760  121.455 1.00 36.98 ?  45  LYS D CB    1 
ATOM   13740 C  CG    . LYS D 2 66  ? 166.858 98.385  120.814 1.00 40.03 ?  45  LYS D CG    1 
ATOM   13741 C  CD    . LYS D 2 66  ? 165.396 97.924  120.774 1.00 43.70 ?  45  LYS D CD    1 
ATOM   13742 C  CE    . LYS D 2 66  ? 165.257 96.568  120.075 1.00 45.57 ?  45  LYS D CE    1 
ATOM   13743 N  NZ    . LYS D 2 66  ? 165.696 96.603  118.649 1.00 46.59 1  45  LYS D NZ    1 
ATOM   13744 N  N     . TYR D 2 67  ? 167.656 101.742 124.108 1.00 36.26 ?  46  TYR D N     1 
ATOM   13745 C  CA    . TYR D 2 67  ? 168.690 102.536 124.779 1.00 36.90 ?  46  TYR D CA    1 
ATOM   13746 C  C     . TYR D 2 67  ? 168.660 102.480 126.309 1.00 36.28 ?  46  TYR D C     1 
ATOM   13747 O  O     . TYR D 2 67  ? 169.501 103.093 126.959 1.00 36.44 ?  46  TYR D O     1 
ATOM   13748 C  CB    . TYR D 2 67  ? 168.680 103.990 124.292 1.00 37.15 ?  46  TYR D CB    1 
ATOM   13749 C  CG    . TYR D 2 67  ? 168.860 104.128 122.798 1.00 39.40 ?  46  TYR D CG    1 
ATOM   13750 C  CD1   . TYR D 2 67  ? 169.814 103.367 122.117 1.00 41.26 ?  46  TYR D CD1   1 
ATOM   13751 C  CD2   . TYR D 2 67  ? 168.099 105.036 122.069 1.00 41.06 ?  46  TYR D CD2   1 
ATOM   13752 C  CE1   . TYR D 2 67  ? 169.984 103.489 120.738 1.00 43.03 ?  46  TYR D CE1   1 
ATOM   13753 C  CE2   . TYR D 2 67  ? 168.266 105.172 120.689 1.00 43.05 ?  46  TYR D CE2   1 
ATOM   13754 C  CZ    . TYR D 2 67  ? 169.209 104.399 120.030 1.00 43.80 ?  46  TYR D CZ    1 
ATOM   13755 O  OH    . TYR D 2 67  ? 169.369 104.532 118.663 1.00 45.18 ?  46  TYR D OH    1 
ATOM   13756 N  N     . LEU D 2 68  ? 167.697 101.761 126.882 1.00 35.71 ?  47  LEU D N     1 
ATOM   13757 C  CA    . LEU D 2 68  ? 167.648 101.597 128.336 1.00 34.92 ?  47  LEU D CA    1 
ATOM   13758 C  C     . LEU D 2 68  ? 168.597 100.482 128.788 1.00 34.32 ?  47  LEU D C     1 
ATOM   13759 O  O     . LEU D 2 68  ? 168.809 99.505  128.066 1.00 34.50 ?  47  LEU D O     1 
ATOM   13760 C  CB    . LEU D 2 68  ? 166.220 101.314 128.823 1.00 35.00 ?  47  LEU D CB    1 
ATOM   13761 C  CG    . LEU D 2 68  ? 165.073 102.247 128.398 1.00 35.82 ?  47  LEU D CG    1 
ATOM   13762 C  CD1   . LEU D 2 68  ? 163.761 101.769 129.003 1.00 35.95 ?  47  LEU D CD1   1 
ATOM   13763 C  CD2   . LEU D 2 68  ? 165.328 103.709 128.764 1.00 35.97 ?  47  LEU D CD2   1 
ATOM   13764 N  N     . GLY D 2 69  ? 169.160 100.639 129.984 1.00 33.50 ?  48  GLY D N     1 
ATOM   13765 C  CA    . GLY D 2 69  ? 169.950 99.589  130.622 1.00 32.41 ?  48  GLY D CA    1 
ATOM   13766 C  C     . GLY D 2 69  ? 169.113 98.379  131.010 1.00 32.15 ?  48  GLY D C     1 
ATOM   13767 O  O     . GLY D 2 69  ? 167.876 98.435  131.013 1.00 30.98 ?  48  GLY D O     1 
ATOM   13768 N  N     . LYS D 2 70  ? 169.792 97.286  131.349 1.00 32.14 ?  49  LYS D N     1 
ATOM   13769 C  CA    . LYS D 2 70  ? 169.126 96.052  131.756 1.00 32.25 ?  49  LYS D CA    1 
ATOM   13770 C  C     . LYS D 2 70  ? 168.248 96.239  132.992 1.00 31.24 ?  49  LYS D C     1 
ATOM   13771 O  O     . LYS D 2 70  ? 167.135 95.721  133.026 1.00 31.34 ?  49  LYS D O     1 
ATOM   13772 C  CB    . LYS D 2 70  ? 170.141 94.932  131.994 1.00 33.07 ?  49  LYS D CB    1 
ATOM   13773 C  CG    . LYS D 2 70  ? 170.937 94.548  130.756 1.00 35.74 ?  49  LYS D CG    1 
ATOM   13774 C  CD    . LYS D 2 70  ? 172.109 93.649  131.138 1.00 39.67 ?  49  LYS D CD    1 
ATOM   13775 C  CE    . LYS D 2 70  ? 173.100 93.514  129.993 1.00 40.96 ?  49  LYS D CE    1 
ATOM   13776 N  NZ    . LYS D 2 70  ? 174.358 92.895  130.480 1.00 42.55 1  49  LYS D NZ    1 
ATOM   13777 N  N     . ASN D 2 71  ? 168.741 96.981  133.990 1.00 29.92 ?  50  ASN D N     1 
ATOM   13778 C  CA    . ASN D 2 71  ? 167.972 97.239  135.212 1.00 29.37 ?  50  ASN D CA    1 
ATOM   13779 C  C     . ASN D 2 71  ? 166.706 98.042  134.929 1.00 28.35 ?  50  ASN D C     1 
ATOM   13780 O  O     . ASN D 2 71  ? 165.651 97.760  135.510 1.00 27.64 ?  50  ASN D O     1 
ATOM   13781 C  CB    . ASN D 2 71  ? 168.807 97.944  136.298 1.00 29.38 ?  50  ASN D CB    1 
ATOM   13782 C  CG    . ASN D 2 71  ? 169.784 97.005  137.004 1.00 31.22 ?  50  ASN D CG    1 
ATOM   13783 O  OD1   . ASN D 2 71  ? 169.533 95.807  137.150 1.00 33.03 ?  50  ASN D OD1   1 
ATOM   13784 N  ND2   . ASN D 2 71  ? 170.904 97.557  137.458 1.00 31.97 ?  50  ASN D ND2   1 
ATOM   13785 N  N     . GLU D 2 72  ? 166.814 99.025  134.031 1.00 27.72 ?  51  GLU D N     1 
ATOM   13786 C  CA    . GLU D 2 72  ? 165.653 99.835  133.630 1.00 27.70 ?  51  GLU D CA    1 
ATOM   13787 C  C     . GLU D 2 72  ? 164.602 98.990  132.906 1.00 27.62 ?  51  GLU D C     1 
ATOM   13788 O  O     . GLU D 2 72  ? 163.400 99.124  133.157 1.00 27.56 ?  51  GLU D O     1 
ATOM   13789 C  CB    . GLU D 2 72  ? 166.070 101.009 132.739 1.00 27.55 ?  51  GLU D CB    1 
ATOM   13790 C  CG    . GLU D 2 72  ? 167.062 101.989 133.378 1.00 28.77 ?  51  GLU D CG    1 
ATOM   13791 C  CD    . GLU D 2 72  ? 167.325 103.185 132.480 1.00 31.18 ?  51  GLU D CD    1 
ATOM   13792 O  OE1   . GLU D 2 72  ? 168.009 103.018 131.448 1.00 33.17 ?  51  GLU D OE1   1 
ATOM   13793 O  OE2   . GLU D 2 72  ? 166.838 104.287 132.802 1.00 31.66 -1 51  GLU D OE2   1 
ATOM   13794 N  N     . GLN D 2 73  ? 165.064 98.123  132.009 1.00 27.32 ?  52  GLN D N     1 
ATOM   13795 C  CA    . GLN D 2 73  ? 164.173 97.249  131.252 1.00 27.33 ?  52  GLN D CA    1 
ATOM   13796 C  C     . GLN D 2 73  ? 163.515 96.228  132.183 1.00 26.85 ?  52  GLN D C     1 
ATOM   13797 O  O     . GLN D 2 73  ? 162.314 95.963  132.073 1.00 26.24 ?  52  GLN D O     1 
ATOM   13798 C  CB    . GLN D 2 73  ? 164.927 96.555  130.124 1.00 27.65 ?  52  GLN D CB    1 
ATOM   13799 C  CG    . GLN D 2 73  ? 165.290 97.465  128.934 1.00 29.66 ?  52  GLN D CG    1 
ATOM   13800 C  CD    . GLN D 2 73  ? 165.868 96.695  127.747 1.00 32.60 ?  52  GLN D CD    1 
ATOM   13801 O  OE1   . GLN D 2 73  ? 166.354 95.576  127.894 1.00 34.76 ?  52  GLN D OE1   1 
ATOM   13802 N  NE2   . GLN D 2 73  ? 165.832 97.303  126.571 1.00 33.42 ?  52  GLN D NE2   1 
ATOM   13803 N  N     . ASP D 2 74  ? 164.304 95.698  133.115 1.00 26.26 ?  53  ASP D N     1 
ATOM   13804 C  CA    . ASP D 2 74  ? 163.834 94.738  134.121 1.00 26.50 ?  53  ASP D CA    1 
ATOM   13805 C  C     . ASP D 2 74  ? 162.777 95.356  135.026 1.00 25.81 ?  53  ASP D C     1 
ATOM   13806 O  O     . ASP D 2 74  ? 161.727 94.759  135.249 1.00 26.12 ?  53  ASP D O     1 
ATOM   13807 C  CB    . ASP D 2 74  ? 165.019 94.249  134.966 1.00 26.84 ?  53  ASP D CB    1 
ATOM   13808 C  CG    . ASP D 2 74  ? 164.647 93.133  135.941 1.00 29.50 ?  53  ASP D CG    1 
ATOM   13809 O  OD1   . ASP D 2 74  ? 164.255 92.032  135.497 1.00 32.08 ?  53  ASP D OD1   1 
ATOM   13810 O  OD2   . ASP D 2 74  ? 164.795 93.343  137.162 1.00 33.52 -1 53  ASP D OD2   1 
ATOM   13811 N  N     . THR D 2 75  ? 163.050 96.552  135.546 1.00 25.10 ?  54  THR D N     1 
ATOM   13812 C  CA    . THR D 2 75  ? 162.089 97.230  136.421 1.00 24.11 ?  54  THR D CA    1 
ATOM   13813 C  C     . THR D 2 75  ? 160.785 97.509  135.669 1.00 23.82 ?  54  THR D C     1 
ATOM   13814 O  O     . THR D 2 75  ? 159.700 97.219  136.174 1.00 23.81 ?  54  THR D O     1 
ATOM   13815 C  CB    . THR D 2 75  ? 162.676 98.522  137.024 1.00 23.80 ?  54  THR D CB    1 
ATOM   13816 O  OG1   . THR D 2 75  ? 163.797 98.183  137.851 1.00 24.62 ?  54  THR D OG1   1 
ATOM   13817 C  CG2   . THR D 2 75  ? 161.626 99.257  137.876 1.00 23.25 ?  54  THR D CG2   1 
ATOM   13818 N  N     . TYR D 2 76  ? 160.900 98.081  134.479 1.00 24.06 ?  55  TYR D N     1 
ATOM   13819 C  CA    . TYR D 2 76  ? 159.737 98.356  133.641 1.00 24.76 ?  55  TYR D CA    1 
ATOM   13820 C  C     . TYR D 2 76  ? 158.867 97.113  133.404 1.00 24.85 ?  55  TYR D C     1 
ATOM   13821 O  O     . TYR D 2 76  ? 157.648 97.166  133.586 1.00 24.83 ?  55  TYR D O     1 
ATOM   13822 C  CB    . TYR D 2 76  ? 160.159 98.961  132.302 1.00 24.78 ?  55  TYR D CB    1 
ATOM   13823 C  CG    . TYR D 2 76  ? 159.039 99.712  131.612 1.00 26.19 ?  55  TYR D CG    1 
ATOM   13824 C  CD1   . TYR D 2 76  ? 158.859 101.078 131.840 1.00 27.81 ?  55  TYR D CD1   1 
ATOM   13825 C  CD2   . TYR D 2 76  ? 158.152 99.064  130.746 1.00 28.03 ?  55  TYR D CD2   1 
ATOM   13826 C  CE1   . TYR D 2 76  ? 157.839 101.785 131.218 1.00 29.32 ?  55  TYR D CE1   1 
ATOM   13827 C  CE2   . TYR D 2 76  ? 157.116 99.767  130.115 1.00 29.01 ?  55  TYR D CE2   1 
ATOM   13828 C  CZ    . TYR D 2 76  ? 156.972 101.128 130.361 1.00 30.76 ?  55  TYR D CZ    1 
ATOM   13829 O  OH    . TYR D 2 76  ? 155.973 101.855 129.756 1.00 34.50 ?  55  TYR D OH    1 
ATOM   13830 N  N     . MET D 2 77  ? 159.496 96.011  132.997 1.00 25.76 ?  56  MET D N     1 
ATOM   13831 C  CA    . MET D 2 77  ? 158.783 94.747  132.780 1.00 26.81 ?  56  MET D CA    1 
ATOM   13832 C  C     . MET D 2 77  ? 158.039 94.290  134.039 1.00 26.23 ?  56  MET D C     1 
ATOM   13833 O  O     . MET D 2 77  ? 156.868 93.910  133.975 1.00 25.00 ?  56  MET D O     1 
ATOM   13834 C  CB    . MET D 2 77  ? 159.744 93.652  132.322 1.00 28.11 ?  56  MET D CB    1 
ATOM   13835 C  CG    . MET D 2 77  ? 160.315 93.833  130.911 1.00 32.52 ?  56  MET D CG    1 
ATOM   13836 S  SD    . MET D 2 77  ? 159.127 93.524  129.593 1.00 42.68 ?  56  MET D SD    1 
ATOM   13837 C  CE    . MET D 2 77  ? 158.320 95.114  129.414 1.00 38.97 ?  56  MET D CE    1 
ATOM   13838 N  N     . LYS D 2 78  ? 158.736 94.327  135.175 1.00 26.01 ?  57  LYS D N     1 
ATOM   13839 C  CA    . LYS D 2 78  ? 158.171 93.874  136.449 1.00 26.07 ?  57  LYS D CA    1 
ATOM   13840 C  C     . LYS D 2 78  ? 157.012 94.753  136.915 1.00 25.69 ?  57  LYS D C     1 
ATOM   13841 O  O     . LYS D 2 78  ? 156.005 94.250  137.428 1.00 25.58 ?  57  LYS D O     1 
ATOM   13842 C  CB    . LYS D 2 78  ? 159.253 93.792  137.535 1.00 26.08 ?  57  LYS D CB    1 
ATOM   13843 C  CG    . LYS D 2 78  ? 160.268 92.662  137.311 1.00 27.64 ?  57  LYS D CG    1 
ATOM   13844 C  CD    . LYS D 2 78  ? 161.414 92.733  138.314 1.00 29.47 ?  57  LYS D CD    1 
ATOM   13845 C  CE    . LYS D 2 78  ? 162.290 91.494  138.215 1.00 31.69 ?  57  LYS D CE    1 
ATOM   13846 N  NZ    . LYS D 2 78  ? 163.408 91.516  139.196 1.00 33.36 1  57  LYS D NZ    1 
ATOM   13847 N  N     . VAL D 2 79  ? 157.162 96.063  136.736 1.00 25.32 ?  58  VAL D N     1 
ATOM   13848 C  CA    . VAL D 2 79  ? 156.120 97.031  137.098 1.00 25.47 ?  58  VAL D CA    1 
ATOM   13849 C  C     . VAL D 2 79  ? 154.892 96.794  136.226 1.00 25.09 ?  58  VAL D C     1 
ATOM   13850 O  O     . VAL D 2 79  ? 153.764 96.717  136.719 1.00 24.46 ?  58  VAL D O     1 
ATOM   13851 C  CB    . VAL D 2 79  ? 156.650 98.483  136.929 1.00 25.83 ?  58  VAL D CB    1 
ATOM   13852 C  CG1   . VAL D 2 79  ? 155.528 99.456  136.646 1.00 27.35 ?  58  VAL D CG1   1 
ATOM   13853 C  CG2   . VAL D 2 79  ? 157.464 98.890  138.156 1.00 26.42 ?  58  VAL D CG2   1 
ATOM   13854 N  N     . LEU D 2 80  ? 155.138 96.629  134.928 1.00 25.27 ?  59  LEU D N     1 
ATOM   13855 C  CA    . LEU D 2 80  ? 154.078 96.436  133.963 1.00 25.55 ?  59  LEU D CA    1 
ATOM   13856 C  C     . LEU D 2 80  ? 153.278 95.177  134.295 1.00 24.94 ?  59  LEU D C     1 
ATOM   13857 O  O     . LEU D 2 80  ? 152.050 95.200  134.259 1.00 24.82 ?  59  LEU D O     1 
ATOM   13858 C  CB    . LEU D 2 80  ? 154.663 96.339  132.553 1.00 25.80 ?  59  LEU D CB    1 
ATOM   13859 C  CG    . LEU D 2 80  ? 154.233 97.287  131.428 1.00 28.76 ?  59  LEU D CG    1 
ATOM   13860 C  CD1   . LEU D 2 80  ? 154.330 96.531  130.102 1.00 30.25 ?  59  LEU D CD1   1 
ATOM   13861 C  CD2   . LEU D 2 80  ? 152.844 97.879  131.597 1.00 27.79 ?  59  LEU D CD2   1 
ATOM   13862 N  N     . ALA D 2 81  ? 153.982 94.092  134.622 1.00 24.86 ?  60  ALA D N     1 
ATOM   13863 C  CA    . ALA D 2 81  ? 153.337 92.819  134.972 1.00 24.60 ?  60  ALA D CA    1 
ATOM   13864 C  C     . ALA D 2 81  ? 152.533 92.959  136.261 1.00 23.80 ?  60  ALA D C     1 
ATOM   13865 O  O     . ALA D 2 81  ? 151.450 92.400  136.390 1.00 24.07 ?  60  ALA D O     1 
ATOM   13866 C  CB    . ALA D 2 81  ? 154.376 91.708  135.107 1.00 24.48 ?  60  ALA D CB    1 
ATOM   13867 N  N     . GLY D 2 82  ? 153.071 93.716  137.210 1.00 23.54 ?  61  GLY D N     1 
ATOM   13868 C  CA    . GLY D 2 82  ? 152.367 94.018  138.452 1.00 22.53 ?  61  GLY D CA    1 
ATOM   13869 C  C     . GLY D 2 82  ? 151.041 94.701  138.188 1.00 22.23 ?  61  GLY D C     1 
ATOM   13870 O  O     . GLY D 2 82  ? 150.007 94.287  138.710 1.00 21.27 ?  61  GLY D O     1 
ATOM   13871 N  N     . LEU D 2 83  ? 151.069 95.751  137.369 1.00 22.36 ?  62  LEU D N     1 
ATOM   13872 C  CA    . LEU D 2 83  ? 149.844 96.474  137.008 1.00 22.42 ?  62  LEU D CA    1 
ATOM   13873 C  C     . LEU D 2 83  ? 148.859 95.566  136.286 1.00 22.91 ?  62  LEU D C     1 
ATOM   13874 O  O     . LEU D 2 83  ? 147.655 95.586  136.578 1.00 22.99 ?  62  LEU D O     1 
ATOM   13875 C  CB    . LEU D 2 83  ? 150.155 97.695  136.133 1.00 22.19 ?  62  LEU D CB    1 
ATOM   13876 C  CG    . LEU D 2 83  ? 150.965 98.826  136.787 1.00 22.17 ?  62  LEU D CG    1 
ATOM   13877 C  CD1   . LEU D 2 83  ? 151.484 99.785  135.708 1.00 21.55 ?  62  LEU D CD1   1 
ATOM   13878 C  CD2   . LEU D 2 83  ? 150.102 99.559  137.799 1.00 22.42 ?  62  LEU D CD2   1 
ATOM   13879 N  N     . THR D 2 84  ? 149.374 94.758  135.364 1.00 23.39 ?  63  THR D N     1 
ATOM   13880 C  CA    . THR D 2 84  ? 148.532 93.861  134.575 1.00 24.42 ?  63  THR D CA    1 
ATOM   13881 C  C     . THR D 2 84  ? 147.785 92.875  135.476 1.00 24.55 ?  63  THR D C     1 
ATOM   13882 O  O     . THR D 2 84  ? 146.567 92.718  135.366 1.00 23.68 ?  63  THR D O     1 
ATOM   13883 C  CB    . THR D 2 84  ? 149.355 93.081  133.517 1.00 24.70 ?  63  THR D CB    1 
ATOM   13884 O  OG1   . THR D 2 84  ? 150.001 94.009  132.637 1.00 25.57 ?  63  THR D OG1   1 
ATOM   13885 C  CG2   . THR D 2 84  ? 148.444 92.188  132.693 1.00 25.36 ?  63  THR D CG2   1 
ATOM   13886 N  N     . LEU D 2 85  ? 148.537 92.227  136.361 1.00 25.38 ?  64  LEU D N     1 
ATOM   13887 C  CA    . LEU D 2 85  ? 147.980 91.238  137.274 1.00 26.44 ?  64  LEU D CA    1 
ATOM   13888 C  C     . LEU D 2 85  ? 146.926 91.839  138.209 1.00 25.96 ?  64  LEU D C     1 
ATOM   13889 O  O     . LEU D 2 85  ? 145.835 91.269  138.348 1.00 25.83 ?  64  LEU D O     1 
ATOM   13890 C  CB    . LEU D 2 85  ? 149.094 90.493  138.026 1.00 26.65 ?  64  LEU D CB    1 
ATOM   13891 C  CG    . LEU D 2 85  ? 149.800 89.444  137.146 1.00 29.62 ?  64  LEU D CG    1 
ATOM   13892 C  CD1   . LEU D 2 85  ? 151.196 89.123  137.649 1.00 31.57 ?  64  LEU D CD1   1 
ATOM   13893 C  CD2   . LEU D 2 85  ? 148.977 88.148  137.018 1.00 30.96 ?  64  LEU D CD2   1 
ATOM   13894 N  N     . LEU D 2 86  ? 147.216 93.000  138.802 1.00 25.63 ?  65  LEU D N     1 
ATOM   13895 C  CA    . LEU D 2 86  ? 146.228 93.662  139.657 1.00 25.59 ?  65  LEU D CA    1 
ATOM   13896 C  C     . LEU D 2 86  ? 144.975 94.106  138.904 1.00 25.60 ?  65  LEU D C     1 
ATOM   13897 O  O     . LEU D 2 86  ? 143.861 94.021  139.430 1.00 25.47 ?  65  LEU D O     1 
ATOM   13898 C  CB    . LEU D 2 86  ? 146.834 94.843  140.439 1.00 25.76 ?  65  LEU D CB    1 
ATOM   13899 C  CG    . LEU D 2 86  ? 147.842 94.481  141.537 1.00 26.71 ?  65  LEU D CG    1 
ATOM   13900 C  CD1   . LEU D 2 86  ? 148.614 95.705  142.018 1.00 28.01 ?  65  LEU D CD1   1 
ATOM   13901 C  CD2   . LEU D 2 86  ? 147.165 93.805  142.707 1.00 28.01 ?  65  LEU D CD2   1 
ATOM   13902 N  N     . ASP D 2 87  ? 145.150 94.590  137.680 1.00 25.49 ?  66  ASP D N     1 
ATOM   13903 C  CA    . ASP D 2 87  ? 144.022 95.096  136.915 1.00 25.83 ?  66  ASP D CA    1 
ATOM   13904 C  C     . ASP D 2 87  ? 143.080 93.973  136.459 1.00 26.20 ?  66  ASP D C     1 
ATOM   13905 O  O     . ASP D 2 87  ? 141.878 94.179  136.337 1.00 25.99 ?  66  ASP D O     1 
ATOM   13906 C  CB    . ASP D 2 87  ? 144.504 95.923  135.730 1.00 25.50 ?  66  ASP D CB    1 
ATOM   13907 C  CG    . ASP D 2 87  ? 143.551 97.031  135.388 1.00 25.76 ?  66  ASP D CG    1 
ATOM   13908 O  OD1   . ASP D 2 87  ? 142.839 97.504  136.307 1.00 26.91 ?  66  ASP D OD1   1 
ATOM   13909 O  OD2   . ASP D 2 87  ? 143.505 97.439  134.211 1.00 23.11 -1 66  ASP D OD2   1 
ATOM   13910 N  N     . THR D 2 88  ? 143.640 92.787  136.234 1.00 27.12 ?  67  THR D N     1 
ATOM   13911 C  CA    . THR D 2 88  ? 142.862 91.602  135.900 1.00 28.40 ?  67  THR D CA    1 
ATOM   13912 C  C     . THR D 2 88  ? 141.939 91.205  137.040 1.00 28.28 ?  67  THR D C     1 
ATOM   13913 O  O     . THR D 2 88  ? 140.784 90.854  136.808 1.00 28.10 ?  67  THR D O     1 
ATOM   13914 C  CB    . THR D 2 88  ? 143.772 90.417  135.523 1.00 29.04 ?  67  THR D CB    1 
ATOM   13915 O  OG1   . THR D 2 88  ? 144.575 90.789  134.400 1.00 31.00 ?  67  THR D OG1   1 
ATOM   13916 C  CG2   . THR D 2 88  ? 142.939 89.196  135.141 1.00 30.16 ?  67  THR D CG2   1 
ATOM   13917 N  N     . GLU D 2 89  ? 142.441 91.263  138.272 1.00 28.28 ?  68  GLU D N     1 
ATOM   13918 C  CA    . GLU D 2 89  ? 141.593 91.000  139.430 1.00 29.16 ?  68  GLU D CA    1 
ATOM   13919 C  C     . GLU D 2 89  ? 140.435 91.995  139.465 1.00 28.65 ?  68  GLU D C     1 
ATOM   13920 O  O     . GLU D 2 89  ? 139.305 91.618  139.743 1.00 28.44 ?  68  GLU D O     1 
ATOM   13921 C  CB    . GLU D 2 89  ? 142.386 91.066  140.744 1.00 29.32 ?  68  GLU D CB    1 
ATOM   13922 C  CG    . GLU D 2 89  ? 143.537 90.055  140.849 1.00 31.95 ?  68  GLU D CG    1 
ATOM   13923 C  CD    . GLU D 2 89  ? 143.082 88.598  140.853 1.00 35.19 ?  68  GLU D CD    1 
ATOM   13924 O  OE1   . GLU D 2 89  ? 141.885 88.315  141.082 1.00 35.47 ?  68  GLU D OE1   1 
ATOM   13925 O  OE2   . GLU D 2 89  ? 143.943 87.725  140.618 1.00 38.06 -1 68  GLU D OE2   1 
ATOM   13926 N  N     . GLN D 2 90  ? 140.721 93.258  139.165 1.00 28.45 ?  69  GLN D N     1 
ATOM   13927 C  CA    . GLN D 2 90  ? 139.686 94.293  139.192 1.00 28.47 ?  69  GLN D CA    1 
ATOM   13928 C  C     . GLN D 2 90  ? 138.619 94.066  138.113 1.00 28.97 ?  69  GLN D C     1 
ATOM   13929 O  O     . GLN D 2 90  ? 137.432 94.275  138.361 1.00 28.84 ?  69  GLN D O     1 
ATOM   13930 C  CB    . GLN D 2 90  ? 140.310 95.688  139.086 1.00 28.21 ?  69  GLN D CB    1 
ATOM   13931 C  CG    . GLN D 2 90  ? 139.391 96.830  139.520 1.00 27.75 ?  69  GLN D CG    1 
ATOM   13932 C  CD    . GLN D 2 90  ? 139.150 96.895  141.024 1.00 28.91 ?  69  GLN D CD    1 
ATOM   13933 O  OE1   . GLN D 2 90  ? 139.314 95.905  141.750 1.00 27.62 ?  69  GLN D OE1   1 
ATOM   13934 N  NE2   . GLN D 2 90  ? 138.732 98.070  141.497 1.00 28.23 ?  69  GLN D NE2   1 
ATOM   13935 N  N     . GLY D 2 91  ? 139.043 93.615  136.932 1.00 29.62 ?  70  GLY D N     1 
ATOM   13936 C  CA    . GLY D 2 91  ? 138.118 93.306  135.840 1.00 30.43 ?  70  GLY D CA    1 
ATOM   13937 C  C     . GLY D 2 91  ? 137.289 92.041  136.038 1.00 31.11 ?  70  GLY D C     1 
ATOM   13938 O  O     . GLY D 2 91  ? 136.097 92.006  135.716 1.00 30.77 ?  70  GLY D O     1 
ATOM   13939 N  N     . ASN D 2 92  ? 137.917 90.996  136.556 1.00 31.69 ?  71  ASN D N     1 
ATOM   13940 C  CA    . ASN D 2 92  ? 137.212 89.734  136.749 1.00 32.72 ?  71  ASN D CA    1 
ATOM   13941 C  C     . ASN D 2 92  ? 136.376 89.646  138.017 1.00 32.60 ?  71  ASN D C     1 
ATOM   13942 O  O     . ASN D 2 92  ? 135.365 88.939  138.035 1.00 33.12 ?  71  ASN D O     1 
ATOM   13943 C  CB    . ASN D 2 92  ? 138.181 88.562  136.670 1.00 33.68 ?  71  ASN D CB    1 
ATOM   13944 C  CG    . ASN D 2 92  ? 138.671 88.314  135.259 1.00 35.15 ?  71  ASN D CG    1 
ATOM   13945 O  OD1   . ASN D 2 92  ? 139.759 87.787  135.065 1.00 40.21 ?  71  ASN D OD1   1 
ATOM   13946 N  ND2   . ASN D 2 92  ? 137.871 88.705  134.264 1.00 36.91 ?  71  ASN D ND2   1 
ATOM   13947 N  N     . THR D 2 93  ? 136.784 90.375  139.057 1.00 31.76 ?  72  THR D N     1 
ATOM   13948 C  CA    . THR D 2 93  ? 136.142 90.273  140.362 1.00 31.47 ?  72  THR D CA    1 
ATOM   13949 C  C     . THR D 2 93  ? 135.713 91.616  140.948 1.00 30.62 ?  72  THR D C     1 
ATOM   13950 O  O     . THR D 2 93  ? 134.534 91.816  141.226 1.00 30.71 ?  72  THR D O     1 
ATOM   13951 C  CB    . THR D 2 93  ? 137.047 89.548  141.355 1.00 31.60 ?  72  THR D CB    1 
ATOM   13952 O  OG1   . THR D 2 93  ? 137.401 88.269  140.812 1.00 33.14 ?  72  THR D OG1   1 
ATOM   13953 C  CG2   . THR D 2 93  ? 136.341 89.356  142.687 1.00 31.89 ?  72  THR D CG2   1 
ATOM   13954 N  N     . GLY D 2 94  ? 136.669 92.526  141.126 1.00 29.61 ?  73  GLY D N     1 
ATOM   13955 C  CA    . GLY D 2 94  ? 136.428 93.793  141.818 1.00 28.47 ?  73  GLY D CA    1 
ATOM   13956 C  C     . GLY D 2 94  ? 135.247 94.604  141.323 1.00 27.90 ?  73  GLY D C     1 
ATOM   13957 O  O     . GLY D 2 94  ? 134.350 94.961  142.100 1.00 28.27 ?  73  GLY D O     1 
ATOM   13958 N  N     . MET D 2 95  ? 135.240 94.929  140.038 1.00 26.67 ?  74  MET D N     1 
ATOM   13959 C  CA    . MET D 2 95  ? 134.130 95.725  139.521 1.00 26.00 ?  74  MET D CA    1 
ATOM   13960 C  C     . MET D 2 95  ? 132.851 94.905  139.393 1.00 25.25 ?  74  MET D C     1 
ATOM   13961 O  O     . MET D 2 95  ? 131.791 95.395  139.759 1.00 24.97 ?  74  MET D O     1 
ATOM   13962 C  CB    . MET D 2 95  ? 134.469 96.432  138.202 1.00 26.00 ?  74  MET D CB    1 
ATOM   13963 C  CG    . MET D 2 95  ? 135.290 97.687  138.375 1.00 26.40 ?  74  MET D CG    1 
ATOM   13964 S  SD    . MET D 2 95  ? 134.473 98.974  139.352 1.00 28.10 ?  74  MET D SD    1 
ATOM   13965 C  CE    . MET D 2 95  ? 135.821 100.143 139.466 1.00 28.95 ?  74  MET D CE    1 
ATOM   13966 N  N     . PRO D 2 96  ? 132.940 93.668  138.868 1.00 24.98 ?  75  PRO D N     1 
ATOM   13967 C  CA    . PRO D 2 96  ? 131.666 92.936  138.747 1.00 24.59 ?  75  PRO D CA    1 
ATOM   13968 C  C     . PRO D 2 96  ? 131.012 92.592  140.082 1.00 23.90 ?  75  PRO D C     1 
ATOM   13969 O  O     . PRO D 2 96  ? 129.789 92.543  140.148 1.00 23.45 ?  75  PRO D O     1 
ATOM   13970 C  CB    . PRO D 2 96  ? 132.057 91.649  138.008 1.00 24.80 ?  75  PRO D CB    1 
ATOM   13971 C  CG    . PRO D 2 96  ? 133.307 92.019  137.242 1.00 25.75 ?  75  PRO D CG    1 
ATOM   13972 C  CD    . PRO D 2 96  ? 134.032 92.999  138.127 1.00 25.07 ?  75  PRO D CD    1 
ATOM   13973 N  N     . ILE D 2 97  ? 131.806 92.344  141.128 1.00 23.36 ?  76  ILE D N     1 
ATOM   13974 C  CA    . ILE D 2 97  ? 131.231 91.982  142.419 1.00 23.48 ?  76  ILE D CA    1 
ATOM   13975 C  C     . ILE D 2 97  ? 130.539 93.176  143.055 1.00 23.30 ?  76  ILE D C     1 
ATOM   13976 O  O     . ILE D 2 97  ? 129.490 93.024  143.676 1.00 23.45 ?  76  ILE D O     1 
ATOM   13977 C  CB    . ILE D 2 97  ? 132.264 91.332  143.382 1.00 23.96 ?  76  ILE D CB    1 
ATOM   13978 C  CG1   . ILE D 2 97  ? 131.565 90.430  144.393 1.00 24.71 ?  76  ILE D CG1   1 
ATOM   13979 C  CG2   . ILE D 2 97  ? 133.150 92.385  144.091 1.00 24.02 ?  76  ILE D CG2   1 
ATOM   13980 C  CD1   . ILE D 2 97  ? 132.424 89.202  144.786 1.00 29.17 ?  76  ILE D CD1   1 
ATOM   13981 N  N     . VAL D 2 98  ? 131.120 94.364  142.887 1.00 22.71 ?  77  VAL D N     1 
ATOM   13982 C  CA    . VAL D 2 98  ? 130.505 95.594  143.413 1.00 22.78 ?  77  VAL D CA    1 
ATOM   13983 C  C     . VAL D 2 98  ? 129.225 95.920  142.642 1.00 22.89 ?  77  VAL D C     1 
ATOM   13984 O  O     . VAL D 2 98  ? 128.205 96.270  143.238 1.00 23.72 ?  77  VAL D O     1 
ATOM   13985 C  CB    . VAL D 2 98  ? 131.512 96.779  143.421 1.00 22.49 ?  77  VAL D CB    1 
ATOM   13986 C  CG1   . VAL D 2 98  ? 130.817 98.114  143.749 1.00 21.91 ?  77  VAL D CG1   1 
ATOM   13987 C  CG2   . VAL D 2 98  ? 132.611 96.508  144.435 1.00 23.02 ?  77  VAL D CG2   1 
ATOM   13988 N  N     . ALA D 2 99  ? 129.265 95.769  141.319 1.00 23.19 ?  78  ALA D N     1 
ATOM   13989 C  CA    . ALA D 2 99  ? 128.070 95.978  140.489 1.00 23.05 ?  78  ALA D CA    1 
ATOM   13990 C  C     . ALA D 2 99  ? 126.935 95.043  140.914 1.00 23.52 ?  78  ALA D C     1 
ATOM   13991 O  O     . ALA D 2 99  ? 125.760 95.425  140.925 1.00 23.68 ?  78  ALA D O     1 
ATOM   13992 C  CB    . ALA D 2 99  ? 128.407 95.792  139.019 1.00 22.81 ?  78  ALA D CB    1 
ATOM   13993 N  N     . GLU D 2 100 ? 127.288 93.812  141.274 1.00 23.68 ?  79  GLU D N     1 
ATOM   13994 C  CA    . GLU D 2 100 ? 126.300 92.836  141.726 1.00 24.14 ?  79  GLU D CA    1 
ATOM   13995 C  C     . GLU D 2 100 ? 125.569 93.234  143.019 1.00 23.66 ?  79  GLU D C     1 
ATOM   13996 O  O     . GLU D 2 100 ? 124.352 93.061  143.131 1.00 22.94 ?  79  GLU D O     1 
ATOM   13997 C  CB    . GLU D 2 100 ? 126.969 91.472  141.895 1.00 24.47 ?  79  GLU D CB    1 
ATOM   13998 C  CG    . GLU D 2 100 ? 125.996 90.333  142.133 1.00 27.90 ?  79  GLU D CG    1 
ATOM   13999 C  CD    . GLU D 2 100 ? 126.696 89.029  142.472 1.00 32.30 ?  79  GLU D CD    1 
ATOM   14000 O  OE1   . GLU D 2 100 ? 127.864 88.843  142.064 1.00 32.88 ?  79  GLU D OE1   1 
ATOM   14001 O  OE2   . GLU D 2 100 ? 126.070 88.193  143.156 1.00 34.74 -1 79  GLU D OE2   1 
ATOM   14002 N  N     . HIS D 2 101 ? 126.310 93.755  143.997 1.00 23.62 ?  80  HIS D N     1 
ATOM   14003 C  CA    . HIS D 2 101 ? 125.729 94.070  145.316 1.00 23.99 ?  80  HIS D CA    1 
ATOM   14004 C  C     . HIS D 2 101 ? 125.162 95.485  145.489 1.00 24.35 ?  80  HIS D C     1 
ATOM   14005 O  O     . HIS D 2 101 ? 124.384 95.726  146.413 1.00 24.21 ?  80  HIS D O     1 
ATOM   14006 C  CB    . HIS D 2 101 ? 126.730 93.739  146.432 1.00 24.13 ?  80  HIS D CB    1 
ATOM   14007 C  CG    . HIS D 2 101 ? 127.030 92.274  146.546 1.00 24.76 ?  80  HIS D CG    1 
ATOM   14008 N  ND1   . HIS D 2 101 ? 126.350 91.439  147.409 1.00 25.68 ?  80  HIS D ND1   1 
ATOM   14009 C  CD2   . HIS D 2 101 ? 127.918 91.492  145.889 1.00 25.75 ?  80  HIS D CD2   1 
ATOM   14010 C  CE1   . HIS D 2 101 ? 126.812 90.206  147.280 1.00 26.21 ?  80  HIS D CE1   1 
ATOM   14011 N  NE2   . HIS D 2 101 ? 127.764 90.211  146.365 1.00 25.35 ?  80  HIS D NE2   1 
ATOM   14012 N  N     . VAL D 2 102 ? 125.555 96.419  144.624 1.00 24.50 ?  81  VAL D N     1 
ATOM   14013 C  CA    . VAL D 2 102 ? 125.027 97.782  144.674 1.00 25.50 ?  81  VAL D CA    1 
ATOM   14014 C  C     . VAL D 2 102 ? 123.602 97.820  144.098 1.00 26.14 ?  81  VAL D C     1 
ATOM   14015 O  O     . VAL D 2 102 ? 123.349 97.239  143.046 1.00 26.96 ?  81  VAL D O     1 
ATOM   14016 C  CB    . VAL D 2 102 ? 125.949 98.773  143.906 1.00 25.30 ?  81  VAL D CB    1 
ATOM   14017 C  CG1   . VAL D 2 102 ? 125.277 100.112 143.720 1.00 27.08 ?  81  VAL D CG1   1 
ATOM   14018 C  CG2   . VAL D 2 102 ? 127.257 98.964  144.656 1.00 25.41 ?  81  VAL D CG2   1 
ATOM   14019 N  N     . ASP D 2 103 ? 122.686 98.484  144.797 1.00 26.45 ?  82  ASP D N     1 
ATOM   14020 C  CA    . ASP D 2 103 ? 121.323 98.684  144.300 1.00 27.15 ?  82  ASP D CA    1 
ATOM   14021 C  C     . ASP D 2 103 ? 121.230 99.971  143.493 1.00 26.39 ?  82  ASP D C     1 
ATOM   14022 O  O     . ASP D 2 103 ? 121.843 100.987 143.845 1.00 26.40 ?  82  ASP D O     1 
ATOM   14023 C  CB    . ASP D 2 103 ? 120.312 98.734  145.451 1.00 27.72 ?  82  ASP D CB    1 
ATOM   14024 C  CG    . ASP D 2 103 ? 120.242 97.434  146.244 1.00 31.46 ?  82  ASP D CG    1 
ATOM   14025 O  OD1   . ASP D 2 103 ? 120.445 96.331  145.667 1.00 34.26 ?  82  ASP D OD1   1 
ATOM   14026 O  OD2   . ASP D 2 103 ? 119.972 97.515  147.464 1.00 35.52 -1 82  ASP D OD2   1 
ATOM   14027 N  N     . GLY D 2 104 ? 120.446 99.926  142.420 1.00 25.52 ?  83  GLY D N     1 
ATOM   14028 C  CA    . GLY D 2 104 ? 120.226 101.097 141.573 1.00 24.31 ?  83  GLY D CA    1 
ATOM   14029 C  C     . GLY D 2 104 ? 120.611 100.762 140.137 1.00 23.27 ?  83  GLY D C     1 
ATOM   14030 O  O     . GLY D 2 104 ? 121.735 100.338 139.870 1.00 22.38 ?  83  GLY D O     1 
ATOM   14031 N  N     . HIS D 2 105 ? 119.671 100.936 139.213 1.00 22.46 ?  84  HIS D N     1 
ATOM   14032 C  CA    . HIS D 2 105 ? 119.929 100.633 137.803 1.00 22.17 ?  84  HIS D CA    1 
ATOM   14033 C  C     . HIS D 2 105 ? 121.034 101.482 137.196 1.00 21.13 ?  84  HIS D C     1 
ATOM   14034 O  O     . HIS D 2 105 ? 121.840 100.979 136.416 1.00 20.91 ?  84  HIS D O     1 
ATOM   14035 C  CB    . HIS D 2 105 ? 118.644 100.767 136.976 1.00 22.07 ?  84  HIS D CB    1 
ATOM   14036 C  CG    . HIS D 2 105 ? 117.552 99.857  137.440 1.00 23.85 ?  84  HIS D CG    1 
ATOM   14037 N  ND1   . HIS D 2 105 ? 117.747 98.503  137.617 1.00 24.86 ?  84  HIS D ND1   1 
ATOM   14038 C  CD2   . HIS D 2 105 ? 116.271 100.104 137.798 1.00 25.19 ?  84  HIS D CD2   1 
ATOM   14039 C  CE1   . HIS D 2 105 ? 116.625 97.953  138.045 1.00 24.94 ?  84  HIS D CE1   1 
ATOM   14040 N  NE2   . HIS D 2 105 ? 115.717 98.905  138.169 1.00 26.41 ?  84  HIS D NE2   1 
ATOM   14041 N  N     . GLN D 2 106 ? 121.071 102.758 137.548 1.00 20.66 ?  85  GLN D N     1 
ATOM   14042 C  CA    . GLN D 2 106 ? 122.023 103.669 136.918 1.00 20.70 ?  85  GLN D CA    1 
ATOM   14043 C  C     . GLN D 2 106 ? 123.434 103.399 137.440 1.00 20.46 ?  85  GLN D C     1 
ATOM   14044 O  O     . GLN D 2 106 ? 124.395 103.436 136.672 1.00 20.72 ?  85  GLN D O     1 
ATOM   14045 C  CB    . GLN D 2 106 ? 121.580 105.134 137.066 1.00 20.60 ?  85  GLN D CB    1 
ATOM   14046 C  CG    . GLN D 2 106 ? 120.215 105.420 136.383 1.00 20.74 ?  85  GLN D CG    1 
ATOM   14047 C  CD    . GLN D 2 106 ? 119.641 106.813 136.674 1.00 22.11 ?  85  GLN D CD    1 
ATOM   14048 O  OE1   . GLN D 2 106 ? 120.376 107.765 136.914 1.00 22.88 ?  85  GLN D OE1   1 
ATOM   14049 N  NE2   . GLN D 2 106 ? 118.317 106.930 136.637 1.00 21.64 ?  85  GLN D NE2   1 
ATOM   14050 N  N     . ARG D 2 107 ? 123.542 103.077 138.731 1.00 20.17 ?  86  ARG D N     1 
ATOM   14051 C  CA    . ARG D 2 107 ? 124.827 102.713 139.330 1.00 20.29 ?  86  ARG D CA    1 
ATOM   14052 C  C     . ARG D 2 107 ? 125.356 101.421 138.729 1.00 20.07 ?  86  ARG D C     1 
ATOM   14053 O  O     . ARG D 2 107 ? 126.541 101.316 138.439 1.00 19.53 ?  86  ARG D O     1 
ATOM   14054 C  CB    . ARG D 2 107 ? 124.699 102.541 140.841 1.00 20.88 ?  86  ARG D CB    1 
ATOM   14055 C  CG    . ARG D 2 107 ? 124.206 103.772 141.529 1.00 22.56 ?  86  ARG D CG    1 
ATOM   14056 C  CD    . ARG D 2 107 ? 123.783 103.462 142.943 1.00 27.21 ?  86  ARG D CD    1 
ATOM   14057 N  NE    . ARG D 2 107 ? 123.822 104.715 143.673 1.00 31.70 ?  86  ARG D NE    1 
ATOM   14058 C  CZ    . ARG D 2 107 ? 123.903 104.829 144.982 1.00 32.23 ?  86  ARG D CZ    1 
ATOM   14059 N  NH1   . ARG D 2 107 ? 123.944 103.748 145.758 1.00 34.27 1  86  ARG D NH1   1 
ATOM   14060 N  NH2   . ARG D 2 107 ? 123.949 106.043 145.501 1.00 33.79 ?  86  ARG D NH2   1 
ATOM   14061 N  N     . LYS D 2 108 ? 124.475 100.434 138.557 1.00 19.61 ?  87  LYS D N     1 
ATOM   14062 C  CA    . LYS D 2 108 ? 124.880 99.177  137.930 1.00 19.92 ?  87  LYS D CA    1 
ATOM   14063 C  C     . LYS D 2 108 ? 125.402 99.396  136.507 1.00 20.08 ?  87  LYS D C     1 
ATOM   14064 O  O     . LYS D 2 108 ? 126.323 98.701  136.065 1.00 20.38 ?  87  LYS D O     1 
ATOM   14065 C  CB    . LYS D 2 108 ? 123.751 98.144  137.941 1.00 19.54 ?  87  LYS D CB    1 
ATOM   14066 C  CG    . LYS D 2 108 ? 123.371 97.649  139.324 1.00 20.55 ?  87  LYS D CG    1 
ATOM   14067 C  CD    . LYS D 2 108 ? 122.257 96.601  139.255 1.00 21.09 ?  87  LYS D CD    1 
ATOM   14068 C  CE    . LYS D 2 108 ? 121.891 96.061  140.633 1.00 22.98 ?  87  LYS D CE    1 
ATOM   14069 N  NZ    . LYS D 2 108 ? 122.981 95.159  141.169 1.00 22.30 1  87  LYS D NZ    1 
ATOM   14070 N  N     . ALA D 2 109 ? 124.810 100.352 135.790 1.00 19.72 ?  88  ALA D N     1 
ATOM   14071 C  CA    . ALA D 2 109 ? 125.235 100.643 134.427 1.00 19.83 ?  88  ALA D CA    1 
ATOM   14072 C  C     . ALA D 2 109 ? 126.629 101.273 134.400 1.00 19.84 ?  88  ALA D C     1 
ATOM   14073 O  O     . ALA D 2 109 ? 127.486 100.866 133.608 1.00 19.96 ?  88  ALA D O     1 
ATOM   14074 C  CB    . ALA D 2 109 ? 124.206 101.532 133.709 1.00 19.65 ?  88  ALA D CB    1 
ATOM   14075 N  N     . VAL D 2 110 ? 126.862 102.243 135.281 1.00 19.33 ?  89  VAL D N     1 
ATOM   14076 C  CA    . VAL D 2 110 ? 128.178 102.892 135.377 1.00 19.22 ?  89  VAL D CA    1 
ATOM   14077 C  C     . VAL D 2 110 ? 129.230 101.839 135.770 1.00 19.45 ?  89  VAL D C     1 
ATOM   14078 O  O     . VAL D 2 110 ? 130.258 101.684 135.096 1.00 18.97 ?  89  VAL D O     1 
ATOM   14079 C  CB    . VAL D 2 110 ? 128.135 104.113 136.339 1.00 19.01 ?  89  VAL D CB    1 
ATOM   14080 C  CG1   . VAL D 2 110 ? 129.554 104.694 136.606 1.00 19.90 ?  89  VAL D CG1   1 
ATOM   14081 C  CG2   . VAL D 2 110 ? 127.250 105.188 135.750 1.00 19.69 ?  89  VAL D CG2   1 
ATOM   14082 N  N     . LEU D 2 111 ? 128.932 101.066 136.815 1.00 19.27 ?  90  LEU D N     1 
ATOM   14083 C  CA    . LEU D 2 111 ? 129.833 99.991  137.236 1.00 19.96 ?  90  LEU D CA    1 
ATOM   14084 C  C     . LEU D 2 111 ? 130.124 98.969  136.129 1.00 20.30 ?  90  LEU D C     1 
ATOM   14085 O  O     . LEU D 2 111 ? 131.272 98.548  135.964 1.00 19.88 ?  90  LEU D O     1 
ATOM   14086 C  CB    . LEU D 2 111 ? 129.341 99.321  138.526 1.00 19.87 ?  90  LEU D CB    1 
ATOM   14087 C  CG    . LEU D 2 111 ? 129.398 100.246 139.744 1.00 20.24 ?  90  LEU D CG    1 
ATOM   14088 C  CD1   . LEU D 2 111 ? 128.593 99.711  140.940 1.00 21.85 ?  90  LEU D CD1   1 
ATOM   14089 C  CD2   . LEU D 2 111 ? 130.854 100.551 140.142 1.00 20.29 ?  90  LEU D CD2   1 
ATOM   14090 N  N     . ASN D 2 112 ? 129.097 98.592  135.362 1.00 20.92 ?  91  ASN D N     1 
ATOM   14091 C  CA    . ASN D 2 112 ? 129.294 97.737  134.168 1.00 20.70 ?  91  ASN D CA    1 
ATOM   14092 C  C     . ASN D 2 112 ? 130.232 98.350  133.144 1.00 20.57 ?  91  ASN D C     1 
ATOM   14093 O  O     . ASN D 2 112 ? 131.020 97.640  132.498 1.00 20.45 ?  91  ASN D O     1 
ATOM   14094 C  CB    . ASN D 2 112 ? 127.972 97.475  133.446 1.00 21.16 ?  91  ASN D CB    1 
ATOM   14095 C  CG    . ASN D 2 112 ? 127.323 96.166  133.848 1.00 21.98 ?  91  ASN D CG    1 
ATOM   14096 O  OD1   . ASN D 2 112 ? 127.792 95.460  134.746 1.00 25.37 ?  91  ASN D OD1   1 
ATOM   14097 N  ND2   . ASN D 2 112 ? 126.218 95.848  133.197 1.00 21.12 ?  91  ASN D ND2   1 
ATOM   14098 N  N     . PHE D 2 113 ? 130.085 99.656  132.933 1.00 19.70 ?  92  PHE D N     1 
ATOM   14099 C  CA    . PHE D 2 113 ? 130.950 100.359 132.011 1.00 20.02 ?  92  PHE D CA    1 
ATOM   14100 C  C     . PHE D 2 113 ? 132.410 100.311 132.487 1.00 19.97 ?  92  PHE D C     1 
ATOM   14101 O  O     . PHE D 2 113 ? 133.321 100.044 131.696 1.00 19.22 ?  92  PHE D O     1 
ATOM   14102 C  CB    . PHE D 2 113 ? 130.492 101.808 131.775 1.00 20.09 ?  92  PHE D CB    1 
ATOM   14103 C  CG    . PHE D 2 113 ? 131.264 102.490 130.700 1.00 20.54 ?  92  PHE D CG    1 
ATOM   14104 C  CD1   . PHE D 2 113 ? 130.846 102.413 129.370 1.00 20.14 ?  92  PHE D CD1   1 
ATOM   14105 C  CD2   . PHE D 2 113 ? 132.451 103.158 131.004 1.00 20.77 ?  92  PHE D CD2   1 
ATOM   14106 C  CE1   . PHE D 2 113 ? 131.588 103.020 128.360 1.00 20.54 ?  92  PHE D CE1   1 
ATOM   14107 C  CE2   . PHE D 2 113 ? 133.203 103.761 129.997 1.00 21.23 ?  92  PHE D CE2   1 
ATOM   14108 C  CZ    . PHE D 2 113 ? 132.765 103.685 128.669 1.00 20.92 ?  92  PHE D CZ    1 
ATOM   14109 N  N     . MET D 2 114 ? 132.618 100.556 133.777 1.00 19.67 ?  93  MET D N     1 
ATOM   14110 C  CA    . MET D 2 114 ? 133.952 100.472 134.357 1.00 20.55 ?  93  MET D CA    1 
ATOM   14111 C  C     . MET D 2 114 ? 134.546 99.066  134.244 1.00 20.82 ?  93  MET D C     1 
ATOM   14112 O  O     . MET D 2 114 ? 135.716 98.943  133.906 1.00 20.43 ?  93  MET D O     1 
ATOM   14113 C  CB    . MET D 2 114 ? 133.949 100.942 135.807 1.00 20.24 ?  93  MET D CB    1 
ATOM   14114 C  CG    . MET D 2 114 ? 133.430 102.360 135.925 1.00 22.05 ?  93  MET D CG    1 
ATOM   14115 S  SD    . MET D 2 114 ? 133.207 102.926 137.596 1.00 25.85 ?  93  MET D SD    1 
ATOM   14116 C  CE    . MET D 2 114 ? 133.314 104.702 137.323 1.00 27.57 ?  93  MET D CE    1 
ATOM   14117 N  N     . ALA D 2 115 ? 133.743 98.029  134.520 1.00 21.19 ?  94  ALA D N     1 
ATOM   14118 C  CA    . ALA D 2 115 ? 134.197 96.633  134.364 1.00 21.53 ?  94  ALA D CA    1 
ATOM   14119 C  C     . ALA D 2 115 ? 134.594 96.351  132.916 1.00 21.75 ?  94  ALA D C     1 
ATOM   14120 O  O     . ALA D 2 115 ? 135.628 95.729  132.669 1.00 22.18 ?  94  ALA D O     1 
ATOM   14121 C  CB    . ALA D 2 115 ? 133.131 95.640  134.840 1.00 21.32 ?  94  ALA D CB    1 
ATOM   14122 N  N     . MET D 2 116 ? 133.789 96.834  131.967 1.00 21.47 ?  95  MET D N     1 
ATOM   14123 C  CA    . MET D 2 116 ? 134.108 96.721  130.547 1.00 21.83 ?  95  MET D CA    1 
ATOM   14124 C  C     . MET D 2 116 ? 135.489 97.322  130.222 1.00 22.15 ?  95  MET D C     1 
ATOM   14125 O  O     . MET D 2 116 ? 136.287 96.698  129.525 1.00 22.09 ?  95  MET D O     1 
ATOM   14126 C  CB    . MET D 2 116 ? 133.009 97.373  129.692 1.00 21.72 ?  95  MET D CB    1 
ATOM   14127 C  CG    . MET D 2 116 ? 133.292 97.402  128.181 1.00 22.57 ?  95  MET D CG    1 
ATOM   14128 S  SD    . MET D 2 116 ? 134.429 98.710  127.652 1.00 22.75 ?  95  MET D SD    1 
ATOM   14129 C  CE    . MET D 2 116 ? 133.466 100.185 127.984 1.00 22.96 ?  95  MET D CE    1 
ATOM   14130 N  N     . MET D 2 117 ? 135.760 98.527  130.728 1.00 22.04 ?  96  MET D N     1 
ATOM   14131 C  CA    . MET D 2 117 ? 137.047 99.199  130.484 1.00 22.45 ?  96  MET D CA    1 
ATOM   14132 C  C     . MET D 2 117 ? 138.232 98.365  131.000 1.00 22.39 ?  96  MET D C     1 
ATOM   14133 O  O     . MET D 2 117 ? 139.269 98.275  130.340 1.00 21.88 ?  96  MET D O     1 
ATOM   14134 C  CB    . MET D 2 117 ? 137.062 100.617 131.091 1.00 22.00 ?  96  MET D CB    1 
ATOM   14135 C  CG    . MET D 2 117 ? 136.171 101.633 130.328 1.00 23.25 ?  96  MET D CG    1 
ATOM   14136 S  SD    . MET D 2 117 ? 136.616 101.832 128.587 1.00 24.28 ?  96  MET D SD    1 
ATOM   14137 C  CE    . MET D 2 117 ? 138.142 102.758 128.707 1.00 24.59 ?  96  MET D CE    1 
ATOM   14138 N  N     . GLU D 2 118 ? 138.065 97.740  132.165 1.00 22.66 ?  97  GLU D N     1 
ATOM   14139 C  CA    . GLU D 2 118 ? 139.108 96.869  132.721 1.00 23.52 ?  97  GLU D CA    1 
ATOM   14140 C  C     . GLU D 2 118 ? 139.415 95.704  131.796 1.00 24.25 ?  97  GLU D C     1 
ATOM   14141 O  O     . GLU D 2 118 ? 140.579 95.468  131.466 1.00 25.05 ?  97  GLU D O     1 
ATOM   14142 C  CB    . GLU D 2 118 ? 138.743 96.327  134.122 1.00 23.11 ?  97  GLU D CB    1 
ATOM   14143 C  CG    . GLU D 2 118 ? 138.150 97.339  135.112 1.00 23.08 ?  97  GLU D CG    1 
ATOM   14144 C  CD    . GLU D 2 118 ? 139.132 98.393  135.598 1.00 24.08 ?  97  GLU D CD    1 
ATOM   14145 O  OE1   . GLU D 2 118 ? 140.190 98.566  134.975 1.00 26.39 ?  97  GLU D OE1   1 
ATOM   14146 O  OE2   . GLU D 2 118 ? 138.829 99.077  136.599 1.00 27.52 -1 97  GLU D OE2   1 
ATOM   14147 N  N     . ASN D 2 119 ? 138.368 95.002  131.368 1.00 25.47 ?  98  ASN D N     1 
ATOM   14148 C  CA    . ASN D 2 119 ? 138.494 93.728  130.632 1.00 26.32 ?  98  ASN D CA    1 
ATOM   14149 C  C     . ASN D 2 119 ? 138.717 93.865  129.129 1.00 26.22 ?  98  ASN D C     1 
ATOM   14150 O  O     . ASN D 2 119 ? 139.472 93.078  128.522 1.00 26.54 ?  98  ASN D O     1 
ATOM   14151 C  CB    . ASN D 2 119 ? 137.257 92.844  130.878 1.00 26.72 ?  98  ASN D CB    1 
ATOM   14152 C  CG    . ASN D 2 119 ? 137.144 92.393  132.334 1.00 29.12 ?  98  ASN D CG    1 
ATOM   14153 O  OD1   . ASN D 2 119 ? 138.084 91.822  132.898 1.00 32.07 ?  98  ASN D OD1   1 
ATOM   14154 N  ND2   . ASN D 2 119 ? 136.003 92.676  132.954 1.00 29.12 ?  98  ASN D ND2   1 
ATOM   14155 N  N     . ALA D 2 120 ? 138.042 94.844  128.534 1.00 25.46 ?  99  ALA D N     1 
ATOM   14156 C  CA    . ALA D 2 120 ? 138.055 95.022  127.083 1.00 25.77 ?  99  ALA D CA    1 
ATOM   14157 C  C     . ALA D 2 120 ? 139.103 96.021  126.604 1.00 25.51 ?  99  ALA D C     1 
ATOM   14158 O  O     . ALA D 2 120 ? 139.577 95.922  125.469 1.00 26.64 ?  99  ALA D O     1 
ATOM   14159 C  CB    . ALA D 2 120 ? 136.662 95.431  126.576 1.00 25.75 ?  99  ALA D CB    1 
ATOM   14160 N  N     . VAL D 2 121 ? 139.458 96.983  127.450 1.00 24.40 ?  100 VAL D N     1 
ATOM   14161 C  CA    . VAL D 2 121 ? 140.336 98.064  127.015 1.00 24.15 ?  100 VAL D CA    1 
ATOM   14162 C  C     . VAL D 2 121 ? 141.696 98.009  127.716 1.00 23.94 ?  100 VAL D C     1 
ATOM   14163 O  O     . VAL D 2 121 ? 142.733 97.874  127.059 1.00 23.75 ?  100 VAL D O     1 
ATOM   14164 C  CB    . VAL D 2 121 ? 139.659 99.459  127.178 1.00 23.68 ?  100 VAL D CB    1 
ATOM   14165 C  CG1   . VAL D 2 121 ? 140.582 100.571 126.679 1.00 23.76 ?  100 VAL D CG1   1 
ATOM   14166 C  CG2   . VAL D 2 121 ? 138.335 99.495  126.409 1.00 23.99 ?  100 VAL D CG2   1 
ATOM   14167 N  N     . HIS D 2 122 ? 141.683 98.107  129.044 1.00 23.68 ?  101 HIS D N     1 
ATOM   14168 C  CA    . HIS D 2 122 ? 142.920 98.090  129.828 1.00 24.02 ?  101 HIS D CA    1 
ATOM   14169 C  C     . HIS D 2 122 ? 143.718 96.809  129.648 1.00 24.39 ?  101 HIS D C     1 
ATOM   14170 O  O     . HIS D 2 122 ? 144.924 96.869  129.426 1.00 24.71 ?  101 HIS D O     1 
ATOM   14171 C  CB    . HIS D 2 122 ? 142.658 98.346  131.317 1.00 23.20 ?  101 HIS D CB    1 
ATOM   14172 C  CG    . HIS D 2 122 ? 142.096 99.703  131.609 1.00 22.82 ?  101 HIS D CG    1 
ATOM   14173 N  ND1   . HIS D 2 122 ? 141.736 100.098 132.878 1.00 20.48 ?  101 HIS D ND1   1 
ATOM   14174 C  CD2   . HIS D 2 122 ? 141.807 100.746 130.793 1.00 21.03 ?  101 HIS D CD2   1 
ATOM   14175 C  CE1   . HIS D 2 122 ? 141.265 101.331 132.836 1.00 19.88 ?  101 HIS D CE1   1 
ATOM   14176 N  NE2   . HIS D 2 122 ? 141.299 101.749 131.583 1.00 21.62 ?  101 HIS D NE2   1 
ATOM   14177 N  N     . ALA D 2 123 ? 143.054 95.656  129.733 1.00 25.30 ?  102 ALA D N     1 
ATOM   14178 C  CA    . ALA D 2 123 ? 143.763 94.371  129.651 1.00 25.77 ?  102 ALA D CA    1 
ATOM   14179 C  C     . ALA D 2 123 ? 144.431 94.162  128.288 1.00 26.37 ?  102 ALA D C     1 
ATOM   14180 O  O     . ALA D 2 123 ? 145.555 93.651  128.206 1.00 25.87 ?  102 ALA D O     1 
ATOM   14181 C  CB    . ALA D 2 123 ? 142.825 93.204  129.985 1.00 26.43 ?  102 ALA D CB    1 
ATOM   14182 N  N     . LYS D 2 124 ? 143.732 94.562  127.225 1.00 26.51 ?  103 LYS D N     1 
ATOM   14183 C  CA    . LYS D 2 124 ? 144.269 94.475  125.875 1.00 27.22 ?  103 LYS D CA    1 
ATOM   14184 C  C     . LYS D 2 124 ? 145.441 95.452  125.695 1.00 26.63 ?  103 LYS D C     1 
ATOM   14185 O  O     . LYS D 2 124 ? 146.412 95.134  125.009 1.00 26.07 ?  103 LYS D O     1 
ATOM   14186 C  CB    . LYS D 2 124 ? 143.163 94.735  124.832 1.00 27.51 ?  103 LYS D CB    1 
ATOM   14187 C  CG    . LYS D 2 124 ? 143.629 94.757  123.360 1.00 30.58 ?  103 LYS D CG    1 
ATOM   14188 C  CD    . LYS D 2 124 ? 144.094 93.390  122.879 1.00 35.72 ?  103 LYS D CD    1 
ATOM   14189 C  CE    . LYS D 2 124 ? 144.585 93.421  121.430 1.00 37.33 ?  103 LYS D CE    1 
ATOM   14190 N  NZ    . LYS D 2 124 ? 143.464 93.728  120.503 1.00 40.73 1  103 LYS D NZ    1 
ATOM   14191 N  N     . SER D 2 125 ? 145.343 96.621  126.334 1.00 26.02 ?  104 SER D N     1 
ATOM   14192 C  CA    . SER D 2 125 ? 146.376 97.657  126.257 1.00 26.16 ?  104 SER D CA    1 
ATOM   14193 C  C     . SER D 2 125 ? 147.690 97.214  126.901 1.00 26.18 ?  104 SER D C     1 
ATOM   14194 O  O     . SER D 2 125 ? 148.767 97.442  126.337 1.00 26.06 ?  104 SER D O     1 
ATOM   14195 C  CB    . SER D 2 125 ? 145.897 98.962  126.896 1.00 26.10 ?  104 SER D CB    1 
ATOM   14196 O  OG    . SER D 2 125 ? 144.818 99.504  126.155 1.00 26.58 ?  104 SER D OG    1 
ATOM   14197 N  N     . TYR D 2 126 ? 147.593 96.587  128.071 1.00 25.68 ?  105 TYR D N     1 
ATOM   14198 C  CA    . TYR D 2 126 ? 148.771 96.053  128.767 1.00 26.12 ?  105 TYR D CA    1 
ATOM   14199 C  C     . TYR D 2 126 ? 149.426 94.939  127.944 1.00 26.38 ?  105 TYR D C     1 
ATOM   14200 O  O     . TYR D 2 126 ? 150.649 94.895  127.800 1.00 26.83 ?  105 TYR D O     1 
ATOM   14201 C  CB    . TYR D 2 126 ? 148.404 95.522  130.167 1.00 25.35 ?  105 TYR D CB    1 
ATOM   14202 C  CG    . TYR D 2 126 ? 148.228 96.585  131.234 1.00 25.46 ?  105 TYR D CG    1 
ATOM   14203 C  CD1   . TYR D 2 126 ? 149.246 97.501  131.505 1.00 25.41 ?  105 TYR D CD1   1 
ATOM   14204 C  CD2   . TYR D 2 126 ? 147.056 96.657  132.001 1.00 24.77 ?  105 TYR D CD2   1 
ATOM   14205 C  CE1   . TYR D 2 126 ? 149.099 98.479  132.486 1.00 25.89 ?  105 TYR D CE1   1 
ATOM   14206 C  CE2   . TYR D 2 126 ? 146.898 97.639  132.991 1.00 23.11 ?  105 TYR D CE2   1 
ATOM   14207 C  CZ    . TYR D 2 126 ? 147.930 98.535  133.235 1.00 25.38 ?  105 TYR D CZ    1 
ATOM   14208 O  OH    . TYR D 2 126 ? 147.811 99.511  134.200 1.00 23.31 ?  105 TYR D OH    1 
ATOM   14209 N  N     . SER D 2 127 ? 148.602 94.055  127.391 1.00 27.16 ?  106 SER D N     1 
ATOM   14210 C  CA    . SER D 2 127 ? 149.087 92.967  126.535 1.00 27.83 ?  106 SER D CA    1 
ATOM   14211 C  C     . SER D 2 127 ? 149.839 93.517  125.314 1.00 28.21 ?  106 SER D C     1 
ATOM   14212 O  O     . SER D 2 127 ? 150.946 93.055  125.007 1.00 28.30 ?  106 SER D O     1 
ATOM   14213 C  CB    . SER D 2 127 ? 147.924 92.056  126.111 1.00 28.37 ?  106 SER D CB    1 
ATOM   14214 O  OG    . SER D 2 127 ? 148.352 91.056  125.189 1.00 29.33 ?  106 SER D OG    1 
ATOM   14215 N  N     . ASN D 2 128 ? 149.238 94.502  124.640 1.00 28.27 ?  107 ASN D N     1 
ATOM   14216 C  CA    . ASN D 2 128 ? 149.855 95.203  123.503 1.00 28.79 ?  107 ASN D CA    1 
ATOM   14217 C  C     . ASN D 2 128 ? 151.218 95.812  123.820 1.00 28.53 ?  107 ASN D C     1 
ATOM   14218 O  O     . ASN D 2 128 ? 152.155 95.679  123.025 1.00 28.03 ?  107 ASN D O     1 
ATOM   14219 C  CB    . ASN D 2 128 ? 148.931 96.300  122.944 1.00 29.05 ?  107 ASN D CB    1 
ATOM   14220 C  CG    . ASN D 2 128 ? 147.704 95.735  122.223 1.00 30.48 ?  107 ASN D CG    1 
ATOM   14221 O  OD1   . ASN D 2 128 ? 147.619 94.538  121.959 1.00 32.19 ?  107 ASN D OD1   1 
ATOM   14222 N  ND2   . ASN D 2 128 ? 146.742 96.601  121.922 1.00 31.59 ?  107 ASN D ND2   1 
ATOM   14223 N  N     . ILE D 2 129 ? 151.322 96.500  124.959 1.00 28.21 ?  108 ILE D N     1 
ATOM   14224 C  CA    . ILE D 2 129 ? 152.611 97.058  125.390 1.00 28.76 ?  108 ILE D CA    1 
ATOM   14225 C  C     . ILE D 2 129 ? 153.662 95.947  125.550 1.00 29.83 ?  108 ILE D C     1 
ATOM   14226 O  O     . ILE D 2 129 ? 154.783 96.061  125.035 1.00 29.99 ?  108 ILE D O     1 
ATOM   14227 C  CB    . ILE D 2 129 ? 152.495 97.913  126.693 1.00 28.28 ?  108 ILE D CB    1 
ATOM   14228 C  CG1   . ILE D 2 129 ? 151.603 99.142  126.464 1.00 27.94 ?  108 ILE D CG1   1 
ATOM   14229 C  CG2   . ILE D 2 129 ? 153.884 98.363  127.168 1.00 27.52 ?  108 ILE D CG2   1 
ATOM   14230 C  CD1   . ILE D 2 129 ? 151.138 99.824  127.746 1.00 27.98 ?  108 ILE D CD1   1 
ATOM   14231 N  N     . PHE D 2 130 ? 153.300 94.878  126.255 1.00 30.86 ?  109 PHE D N     1 
ATOM   14232 C  CA    . PHE D 2 130 ? 154.199 93.744  126.445 1.00 32.76 ?  109 PHE D CA    1 
ATOM   14233 C  C     . PHE D 2 130 ? 154.688 93.130  125.129 1.00 34.37 ?  109 PHE D C     1 
ATOM   14234 O  O     . PHE D 2 130 ? 155.890 92.982  124.926 1.00 34.61 ?  109 PHE D O     1 
ATOM   14235 C  CB    . PHE D 2 130 ? 153.543 92.665  127.304 1.00 32.81 ?  109 PHE D CB    1 
ATOM   14236 C  CG    . PHE D 2 130 ? 153.899 92.748  128.761 1.00 33.84 ?  109 PHE D CG    1 
ATOM   14237 C  CD1   . PHE D 2 130 ? 155.195 92.474  129.191 1.00 34.61 ?  109 PHE D CD1   1 
ATOM   14238 C  CD2   . PHE D 2 130 ? 152.930 93.066  129.705 1.00 35.74 ?  109 PHE D CD2   1 
ATOM   14239 C  CE1   . PHE D 2 130 ? 155.530 92.537  130.543 1.00 36.99 ?  109 PHE D CE1   1 
ATOM   14240 C  CE2   . PHE D 2 130 ? 153.251 93.133  131.067 1.00 36.96 ?  109 PHE D CE2   1 
ATOM   14241 C  CZ    . PHE D 2 130 ? 154.554 92.868  131.487 1.00 36.91 ?  109 PHE D CZ    1 
ATOM   14242 N  N     . MET D 2 131 ? 153.747 92.795  124.245 1.00 35.90 ?  110 MET D N     1 
ATOM   14243 C  CA    . MET D 2 131 ? 154.051 92.160  122.962 1.00 37.94 ?  110 MET D CA    1 
ATOM   14244 C  C     . MET D 2 131 ? 154.948 93.023  122.086 1.00 38.05 ?  110 MET D C     1 
ATOM   14245 O  O     . MET D 2 131 ? 155.703 92.499  121.274 1.00 38.20 ?  110 MET D O     1 
ATOM   14246 C  CB    . MET D 2 131 ? 152.765 91.800  122.199 1.00 38.63 ?  110 MET D CB    1 
ATOM   14247 C  CG    . MET D 2 131 ? 151.929 90.681  122.842 1.00 42.34 ?  110 MET D CG    1 
ATOM   14248 S  SD    . MET D 2 131 ? 150.411 90.250  121.930 1.00 50.15 ?  110 MET D SD    1 
ATOM   14249 C  CE    . MET D 2 131 ? 149.374 91.698  122.169 1.00 48.14 ?  110 MET D CE    1 
ATOM   14250 N  N     . THR D 2 132 ? 154.862 94.342  122.255 1.00 38.12 ?  111 THR D N     1 
ATOM   14251 C  CA    . THR D 2 132 ? 155.705 95.271  121.502 1.00 38.79 ?  111 THR D CA    1 
ATOM   14252 C  C     . THR D 2 132 ? 157.161 95.273  122.001 1.00 38.81 ?  111 THR D C     1 
ATOM   14253 O  O     . THR D 2 132 ? 158.094 95.283  121.192 1.00 39.26 ?  111 THR D O     1 
ATOM   14254 C  CB    . THR D 2 132 ? 155.123 96.699  121.525 1.00 38.78 ?  111 THR D CB    1 
ATOM   14255 O  OG1   . THR D 2 132 ? 153.789 96.676  121.005 1.00 39.32 ?  111 THR D OG1   1 
ATOM   14256 C  CG2   . THR D 2 132 ? 155.958 97.646  120.669 1.00 39.75 ?  111 THR D CG2   1 
ATOM   14257 N  N     . LEU D 2 133 ? 157.340 95.249  123.323 1.00 38.34 ?  112 LEU D N     1 
ATOM   14258 C  CA    . LEU D 2 133 ? 158.652 95.431  123.952 1.00 38.36 ?  112 LEU D CA    1 
ATOM   14259 C  C     . LEU D 2 133 ? 159.442 94.145  124.200 1.00 38.94 ?  112 LEU D C     1 
ATOM   14260 O  O     . LEU D 2 133 ? 160.671 94.160  124.174 1.00 39.14 ?  112 LEU D O     1 
ATOM   14261 C  CB    . LEU D 2 133 ? 158.511 96.197  125.278 1.00 37.62 ?  112 LEU D CB    1 
ATOM   14262 C  CG    . LEU D 2 133 ? 157.804 97.555  125.267 1.00 36.50 ?  112 LEU D CG    1 
ATOM   14263 C  CD1   . LEU D 2 133 ? 157.546 98.034  126.699 1.00 35.80 ?  112 LEU D CD1   1 
ATOM   14264 C  CD2   . LEU D 2 133 ? 158.573 98.597  124.473 1.00 35.32 ?  112 LEU D CD2   1 
ATOM   14265 N  N     . ALA D 2 134 ? 158.754 93.039  124.455 1.00 39.41 ?  113 ALA D N     1 
ATOM   14266 C  CA    . ALA D 2 134 ? 159.461 91.791  124.768 1.00 40.33 ?  113 ALA D CA    1 
ATOM   14267 C  C     . ALA D 2 134 ? 159.045 90.635  123.864 1.00 41.05 ?  113 ALA D C     1 
ATOM   14268 O  O     . ALA D 2 134 ? 157.909 90.602  123.403 1.00 40.81 ?  113 ALA D O     1 
ATOM   14269 C  CB    . ALA D 2 134 ? 159.257 91.426  126.227 1.00 40.15 ?  113 ALA D CB    1 
ATOM   14270 N  N     . PRO D 2 135 ? 159.968 89.687  123.596 1.00 42.21 ?  114 PRO D N     1 
ATOM   14271 C  CA    . PRO D 2 135 ? 159.552 88.468  122.890 1.00 43.27 ?  114 PRO D CA    1 
ATOM   14272 C  C     . PRO D 2 135 ? 158.718 87.557  123.803 1.00 43.89 ?  114 PRO D C     1 
ATOM   14273 O  O     . PRO D 2 135 ? 158.785 87.684  125.029 1.00 43.31 ?  114 PRO D O     1 
ATOM   14274 C  CB    . PRO D 2 135 ? 160.880 87.799  122.525 1.00 43.69 ?  114 PRO D CB    1 
ATOM   14275 C  CG    . PRO D 2 135 ? 161.836 88.282  123.547 1.00 43.01 ?  114 PRO D CG    1 
ATOM   14276 C  CD    . PRO D 2 135 ? 161.412 89.681  123.900 1.00 42.16 ?  114 PRO D CD    1 
ATOM   14277 N  N     . THR D 2 136 ? 157.956 86.647  123.198 1.00 45.26 ?  115 THR D N     1 
ATOM   14278 C  CA    . THR D 2 136 ? 157.005 85.786  123.922 1.00 46.11 ?  115 THR D CA    1 
ATOM   14279 C  C     . THR D 2 136 ? 157.616 85.097  125.146 1.00 46.35 ?  115 THR D C     1 
ATOM   14280 O  O     . THR D 2 136 ? 157.015 85.105  126.225 1.00 46.25 ?  115 THR D O     1 
ATOM   14281 C  CB    . THR D 2 136 ? 156.340 84.743  122.982 1.00 46.59 ?  115 THR D CB    1 
ATOM   14282 O  OG1   . THR D 2 136 ? 155.760 85.418  121.861 1.00 47.80 ?  115 THR D OG1   1 
ATOM   14283 C  CG2   . THR D 2 136 ? 155.229 83.975  123.696 1.00 46.94 ?  115 THR D CG2   1 
ATOM   14284 N  N     . GLU D 2 137 ? 158.811 84.528  124.984 1.00 46.92 ?  116 GLU D N     1 
ATOM   14285 C  CA    . GLU D 2 137 ? 159.475 83.812  126.072 1.00 47.37 ?  116 GLU D CA    1 
ATOM   14286 C  C     . GLU D 2 137 ? 159.802 84.708  127.269 1.00 46.64 ?  116 GLU D C     1 
ATOM   14287 O  O     . GLU D 2 137 ? 159.674 84.275  128.416 1.00 46.89 ?  116 GLU D O     1 
ATOM   14288 C  CB    . GLU D 2 137 ? 160.733 83.083  125.575 1.00 48.04 ?  116 GLU D CB    1 
ATOM   14289 C  CG    . GLU D 2 137 ? 161.426 82.199  126.630 1.00 49.86 ?  116 GLU D CG    1 
ATOM   14290 C  CD    . GLU D 2 137 ? 160.645 80.928  126.996 1.00 52.40 ?  116 GLU D CD    1 
ATOM   14291 O  OE1   . GLU D 2 137 ? 159.452 81.021  127.364 1.00 52.97 ?  116 GLU D OE1   1 
ATOM   14292 O  OE2   . GLU D 2 137 ? 161.240 79.826  126.939 1.00 54.12 -1 116 GLU D OE2   1 
ATOM   14293 N  N     . THR D 2 138 ? 160.216 85.945  126.996 1.00 46.09 ?  117 THR D N     1 
ATOM   14294 C  CA    . THR D 2 138 ? 160.508 86.932  128.047 1.00 45.30 ?  117 THR D CA    1 
ATOM   14295 C  C     . THR D 2 138 ? 159.247 87.342  128.818 1.00 44.63 ?  117 THR D C     1 
ATOM   14296 O  O     . THR D 2 138 ? 159.283 87.494  130.042 1.00 44.51 ?  117 THR D O     1 
ATOM   14297 C  CB    . THR D 2 138 ? 161.205 88.186  127.468 1.00 45.20 ?  117 THR D CB    1 
ATOM   14298 O  OG1   . THR D 2 138 ? 162.398 87.793  126.781 1.00 45.69 ?  117 THR D OG1   1 
ATOM   14299 C  CG2   . THR D 2 138 ? 161.577 89.178  128.570 1.00 44.67 ?  117 THR D CG2   1 
ATOM   14300 N  N     . ILE D 2 139 ? 158.136 87.511  128.100 1.00 44.24 ?  118 ILE D N     1 
ATOM   14301 C  CA    . ILE D 2 139 ? 156.853 87.843  128.726 1.00 43.65 ?  118 ILE D CA    1 
ATOM   14302 C  C     . ILE D 2 139 ? 156.422 86.736  129.699 1.00 43.87 ?  118 ILE D C     1 
ATOM   14303 O  O     . ILE D 2 139 ? 156.081 87.013  130.853 1.00 43.36 ?  118 ILE D O     1 
ATOM   14304 C  CB    . ILE D 2 139 ? 155.761 88.139  127.666 1.00 43.68 ?  118 ILE D CB    1 
ATOM   14305 C  CG1   . ILE D 2 139 ? 156.101 89.430  126.905 1.00 43.30 ?  118 ILE D CG1   1 
ATOM   14306 C  CG2   . ILE D 2 139 ? 154.368 88.242  128.315 1.00 43.11 ?  118 ILE D CG2   1 
ATOM   14307 C  CD1   . ILE D 2 139 ? 155.347 89.626  125.596 1.00 43.41 ?  118 ILE D CD1   1 
ATOM   14308 N  N     . ASN D 2 140 ? 156.470 85.488  129.236 1.00 44.52 ?  119 ASN D N     1 
ATOM   14309 C  CA    . ASN D 2 140 ? 156.118 84.332  130.068 1.00 45.00 ?  119 ASN D CA    1 
ATOM   14310 C  C     . ASN D 2 140 ? 156.962 84.231  131.355 1.00 44.99 ?  119 ASN D C     1 
ATOM   14311 O  O     . ASN D 2 140 ? 156.432 83.920  132.429 1.00 44.61 ?  119 ASN D O     1 
ATOM   14312 C  CB    . ASN D 2 140 ? 156.192 83.029  129.251 1.00 45.74 ?  119 ASN D CB    1 
ATOM   14313 C  CG    . ASN D 2 140 ? 155.219 83.009  128.066 1.00 46.40 ?  119 ASN D CG    1 
ATOM   14314 O  OD1   . ASN D 2 140 ? 154.288 83.817  127.982 1.00 46.85 ?  119 ASN D OD1   1 
ATOM   14315 N  ND2   . ASN D 2 140 ? 155.433 82.068  127.148 1.00 48.16 ?  119 ASN D ND2   1 
ATOM   14316 N  N     . GLU D 2 141 ? 158.261 84.522  131.247 1.00 45.09 ?  120 GLU D N     1 
ATOM   14317 C  CA    . GLU D 2 141 ? 159.169 84.474  132.398 1.00 45.27 ?  120 GLU D CA    1 
ATOM   14318 C  C     . GLU D 2 141 ? 158.922 85.590  133.423 1.00 44.75 ?  120 GLU D C     1 
ATOM   14319 O  O     . GLU D 2 141 ? 158.946 85.344  134.634 1.00 44.37 ?  120 GLU D O     1 
ATOM   14320 C  CB    . GLU D 2 141 ? 160.629 84.487  131.944 1.00 45.75 ?  120 GLU D CB    1 
ATOM   14321 C  CG    . GLU D 2 141 ? 161.068 83.213  131.221 1.00 48.17 ?  120 GLU D CG    1 
ATOM   14322 C  CD    . GLU D 2 141 ? 162.533 83.222  130.834 1.00 50.15 ?  120 GLU D CD    1 
ATOM   14323 O  OE1   . GLU D 2 141 ? 163.386 83.514  131.699 1.00 50.90 ?  120 GLU D OE1   1 
ATOM   14324 O  OE2   . GLU D 2 141 ? 162.834 82.930  129.658 1.00 52.25 -1 120 GLU D OE2   1 
ATOM   14325 N  N     . VAL D 2 142 ? 158.703 86.810  132.932 1.00 44.31 ?  121 VAL D N     1 
ATOM   14326 C  CA    . VAL D 2 142 ? 158.387 87.951  133.793 1.00 43.91 ?  121 VAL D CA    1 
ATOM   14327 C  C     . VAL D 2 142 ? 157.099 87.692  134.581 1.00 43.71 ?  121 VAL D C     1 
ATOM   14328 O  O     . VAL D 2 142 ? 157.035 87.963  135.779 1.00 43.44 ?  121 VAL D O     1 
ATOM   14329 C  CB    . VAL D 2 142 ? 158.278 89.276  132.989 1.00 43.65 ?  121 VAL D CB    1 
ATOM   14330 C  CG1   . VAL D 2 142 ? 157.820 90.424  133.888 1.00 43.40 ?  121 VAL D CG1   1 
ATOM   14331 C  CG2   . VAL D 2 142 ? 159.618 89.623  132.349 1.00 43.96 ?  121 VAL D CG2   1 
ATOM   14332 N  N     . PHE D 2 143 ? 156.085 87.154  133.908 1.00 44.03 ?  122 PHE D N     1 
ATOM   14333 C  CA    . PHE D 2 143 ? 154.826 86.840  134.573 1.00 44.42 ?  122 PHE D CA    1 
ATOM   14334 C  C     . PHE D 2 143 ? 154.953 85.695  135.572 1.00 45.38 ?  122 PHE D C     1 
ATOM   14335 O  O     . PHE D 2 143 ? 154.314 85.724  136.621 1.00 45.50 ?  122 PHE D O     1 
ATOM   14336 C  CB    . PHE D 2 143 ? 153.697 86.602  133.567 1.00 44.27 ?  122 PHE D CB    1 
ATOM   14337 C  CG    . PHE D 2 143 ? 153.000 87.866  133.162 1.00 43.28 ?  122 PHE D CG    1 
ATOM   14338 C  CD1   . PHE D 2 143 ? 152.005 88.414  133.969 1.00 42.17 ?  122 PHE D CD1   1 
ATOM   14339 C  CD2   . PHE D 2 143 ? 153.360 88.530  131.997 1.00 42.76 ?  122 PHE D CD2   1 
ATOM   14340 C  CE1   . PHE D 2 143 ? 151.366 89.595  133.613 1.00 42.16 ?  122 PHE D CE1   1 
ATOM   14341 C  CE2   . PHE D 2 143 ? 152.728 89.713  131.631 1.00 42.77 ?  122 PHE D CE2   1 
ATOM   14342 C  CZ    . PHE D 2 143 ? 151.727 90.248  132.440 1.00 42.28 ?  122 PHE D CZ    1 
ATOM   14343 N  N     . GLU D 2 144 ? 155.791 84.711  135.257 1.00 46.18 ?  123 GLU D N     1 
ATOM   14344 C  CA    . GLU D 2 144 ? 156.135 83.657  136.211 1.00 47.19 ?  123 GLU D CA    1 
ATOM   14345 C  C     . GLU D 2 144 ? 156.785 84.241  137.475 1.00 46.99 ?  123 GLU D C     1 
ATOM   14346 O  O     . GLU D 2 144 ? 156.419 83.854  138.589 1.00 46.94 ?  123 GLU D O     1 
ATOM   14347 C  CB    . GLU D 2 144 ? 157.056 82.619  135.555 1.00 47.80 ?  123 GLU D CB    1 
ATOM   14348 C  CG    . GLU D 2 144 ? 157.371 81.385  136.408 1.00 49.54 ?  123 GLU D CG    1 
ATOM   14349 C  CD    . GLU D 2 144 ? 158.385 80.447  135.747 1.00 52.37 ?  123 GLU D CD    1 
ATOM   14350 O  OE1   . GLU D 2 144 ? 159.421 80.929  135.231 1.00 52.92 ?  123 GLU D OE1   1 
ATOM   14351 O  OE2   . GLU D 2 144 ? 158.151 79.219  135.750 1.00 53.55 -1 123 GLU D OE2   1 
ATOM   14352 N  N     . TRP D 2 145 ? 157.735 85.165  137.292 1.00 47.02 ?  124 TRP D N     1 
ATOM   14353 C  CA    . TRP D 2 145 ? 158.449 85.821  138.402 1.00 46.93 ?  124 TRP D CA    1 
ATOM   14354 C  C     . TRP D 2 145 ? 157.507 86.660  139.252 1.00 46.55 ?  124 TRP D C     1 
ATOM   14355 O  O     . TRP D 2 145 ? 157.470 86.514  140.471 1.00 46.42 ?  124 TRP D O     1 
ATOM   14356 C  CB    . TRP D 2 145 ? 159.590 86.711  137.881 1.00 47.07 ?  124 TRP D CB    1 
ATOM   14357 C  CG    . TRP D 2 145 ? 160.520 87.275  138.959 1.00 47.82 ?  124 TRP D CG    1 
ATOM   14358 C  CD1   . TRP D 2 145 ? 161.695 86.724  139.398 1.00 48.78 ?  124 TRP D CD1   1 
ATOM   14359 C  CD2   . TRP D 2 145 ? 160.356 88.501  139.701 1.00 47.80 ?  124 TRP D CD2   1 
ATOM   14360 N  NE1   . TRP D 2 145 ? 162.266 87.520  140.366 1.00 49.06 ?  124 TRP D NE1   1 
ATOM   14361 C  CE2   . TRP D 2 145 ? 161.467 88.614  140.574 1.00 48.24 ?  124 TRP D CE2   1 
ATOM   14362 C  CE3   . TRP D 2 145 ? 159.381 89.507  139.719 1.00 47.65 ?  124 TRP D CE3   1 
ATOM   14363 C  CZ2   . TRP D 2 145 ? 161.626 89.695  141.457 1.00 47.74 ?  124 TRP D CZ2   1 
ATOM   14364 C  CZ3   . TRP D 2 145 ? 159.538 90.583  140.597 1.00 46.92 ?  124 TRP D CZ3   1 
ATOM   14365 C  CH2   . TRP D 2 145 ? 160.656 90.665  141.453 1.00 47.88 ?  124 TRP D CH2   1 
ATOM   14366 N  N     . VAL D 2 146 ? 156.749 87.541  138.605 1.00 46.09 ?  125 VAL D N     1 
ATOM   14367 C  CA    . VAL D 2 146 ? 155.859 88.451  139.315 1.00 45.36 ?  125 VAL D CA    1 
ATOM   14368 C  C     . VAL D 2 146 ? 154.717 87.672  139.988 1.00 45.28 ?  125 VAL D C     1 
ATOM   14369 O  O     . VAL D 2 146 ? 154.260 88.046  141.074 1.00 45.29 ?  125 VAL D O     1 
ATOM   14370 C  CB    . VAL D 2 146 ? 155.399 89.625  138.391 1.00 45.33 ?  125 VAL D CB    1 
ATOM   14371 C  CG1   . VAL D 2 146 ? 154.362 90.489  139.061 1.00 44.97 ?  125 VAL D CG1   1 
ATOM   14372 C  CG2   . VAL D 2 146 ? 156.600 90.493  138.012 1.00 44.52 ?  125 VAL D CG2   1 
ATOM   14373 N  N     . LYS D 2 147 ? 154.302 86.567  139.370 1.00 44.98 ?  126 LYS D N     1 
ATOM   14374 C  CA    . LYS D 2 147 ? 153.292 85.677  139.959 1.00 44.65 ?  126 LYS D CA    1 
ATOM   14375 C  C     . LYS D 2 147 ? 153.761 85.021  141.268 1.00 44.06 ?  126 LYS D C     1 
ATOM   14376 O  O     . LYS D 2 147 ? 152.948 84.716  142.142 1.00 44.65 ?  126 LYS D O     1 
ATOM   14377 C  CB    . LYS D 2 147 ? 152.868 84.589  138.968 1.00 45.31 ?  126 LYS D CB    1 
ATOM   14378 C  CG    . LYS D 2 147 ? 151.362 84.379  138.902 1.00 46.54 ?  126 LYS D CG    1 
ATOM   14379 C  CD    . LYS D 2 147 ? 150.972 82.901  138.847 1.00 49.06 ?  126 LYS D CD    1 
ATOM   14380 C  CE    . LYS D 2 147 ? 150.831 82.310  140.257 1.00 50.46 ?  126 LYS D CE    1 
ATOM   14381 N  NZ    . LYS D 2 147 ? 149.894 81.147  140.305 1.00 51.33 1  126 LYS D NZ    1 
ATOM   14382 N  N     . GLN D 2 148 ? 155.068 84.808  141.396 1.00 42.58 ?  127 GLN D N     1 
ATOM   14383 C  CA    . GLN D 2 148 ? 155.650 84.209  142.596 1.00 41.39 ?  127 GLN D CA    1 
ATOM   14384 C  C     . GLN D 2 148 ? 156.126 85.257  143.610 1.00 39.56 ?  127 GLN D C     1 
ATOM   14385 O  O     . GLN D 2 148 ? 156.370 84.930  144.770 1.00 39.77 ?  127 GLN D O     1 
ATOM   14386 C  CB    . GLN D 2 148 ? 156.784 83.244  142.197 1.00 42.11 ?  127 GLN D CB    1 
ATOM   14387 C  CG    . GLN D 2 148 ? 157.973 83.163  143.150 1.00 44.08 ?  127 GLN D CG    1 
ATOM   14388 C  CD    . GLN D 2 148 ? 159.159 84.030  142.722 1.00 46.12 ?  127 GLN D CD    1 
ATOM   14389 O  OE1   . GLN D 2 148 ? 158.994 85.175  142.278 1.00 46.47 ?  127 GLN D OE1   1 
ATOM   14390 N  NE2   . GLN D 2 148 ? 160.367 83.487  142.870 1.00 45.69 ?  127 GLN D NE2   1 
ATOM   14391 N  N     . ASN D 2 149 ? 156.242 86.512  143.166 1.00 36.99 ?  128 ASN D N     1 
ATOM   14392 C  CA    . ASN D 2 149 ? 156.746 87.599  144.004 1.00 34.54 ?  128 ASN D CA    1 
ATOM   14393 C  C     . ASN D 2 149 ? 155.923 87.848  145.271 1.00 33.13 ?  128 ASN D C     1 
ATOM   14394 O  O     . ASN D 2 149 ? 154.714 88.061  145.208 1.00 32.62 ?  128 ASN D O     1 
ATOM   14395 C  CB    . ASN D 2 149 ? 156.861 88.895  143.198 1.00 34.24 ?  128 ASN D CB    1 
ATOM   14396 C  CG    . ASN D 2 149 ? 157.490 90.016  144.001 1.00 33.83 ?  128 ASN D CG    1 
ATOM   14397 O  OD1   . ASN D 2 149 ? 156.793 90.887  144.525 1.00 32.21 ?  128 ASN D OD1   1 
ATOM   14398 N  ND2   . ASN D 2 149 ? 158.814 89.979  144.130 1.00 33.26 ?  128 ASN D ND2   1 
ATOM   14399 N  N     . LYS D 2 150 ? 156.604 87.851  146.413 1.00 31.49 ?  129 LYS D N     1 
ATOM   14400 C  CA    . LYS D 2 150 ? 155.965 87.946  147.724 1.00 30.68 ?  129 LYS D CA    1 
ATOM   14401 C  C     . LYS D 2 150 ? 155.151 89.243  147.947 1.00 28.95 ?  129 LYS D C     1 
ATOM   14402 O  O     . LYS D 2 150 ? 154.052 89.202  148.513 1.00 27.90 ?  129 LYS D O     1 
ATOM   14403 C  CB    . LYS D 2 150 ? 157.041 87.753  148.804 1.00 31.17 ?  129 LYS D CB    1 
ATOM   14404 C  CG    . LYS D 2 150 ? 156.687 88.155  150.221 1.00 33.66 ?  129 LYS D CG    1 
ATOM   14405 C  CD    . LYS D 2 150 ? 157.898 87.913  151.135 1.00 38.08 ?  129 LYS D CD    1 
ATOM   14406 C  CE    . LYS D 2 150 ? 157.883 88.822  152.370 1.00 40.20 ?  129 LYS D CE    1 
ATOM   14407 N  NZ    . LYS D 2 150 ? 157.206 88.189  153.535 1.00 42.60 1  129 LYS D NZ    1 
ATOM   14408 N  N     . TYR D 2 151 ? 155.688 90.381  147.509 1.00 27.36 ?  130 TYR D N     1 
ATOM   14409 C  CA    . TYR D 2 151 ? 155.047 91.682  147.775 1.00 26.56 ?  130 TYR D CA    1 
ATOM   14410 C  C     . TYR D 2 151 ? 153.867 91.944  146.853 1.00 25.66 ?  130 TYR D C     1 
ATOM   14411 O  O     . TYR D 2 151 ? 152.859 92.505  147.293 1.00 25.61 ?  130 TYR D O     1 
ATOM   14412 C  CB    . TYR D 2 151 ? 156.069 92.836  147.742 1.00 26.32 ?  130 TYR D CB    1 
ATOM   14413 C  CG    . TYR D 2 151 ? 157.331 92.494  148.511 1.00 27.20 ?  130 TYR D CG    1 
ATOM   14414 C  CD1   . TYR D 2 151 ? 157.310 92.400  149.902 1.00 27.31 ?  130 TYR D CD1   1 
ATOM   14415 C  CD2   . TYR D 2 151 ? 158.524 92.211  147.848 1.00 27.22 ?  130 TYR D CD2   1 
ATOM   14416 C  CE1   . TYR D 2 151 ? 158.454 92.054  150.619 1.00 29.65 ?  130 TYR D CE1   1 
ATOM   14417 C  CE2   . TYR D 2 151 ? 159.683 91.862  148.559 1.00 28.75 ?  130 TYR D CE2   1 
ATOM   14418 C  CZ    . TYR D 2 151 ? 159.628 91.797  149.954 1.00 29.17 ?  130 TYR D CZ    1 
ATOM   14419 O  OH    . TYR D 2 151 ? 160.739 91.460  150.694 1.00 30.61 ?  130 TYR D OH    1 
ATOM   14420 N  N     . LEU D 2 152 ? 153.992 91.538  145.588 1.00 24.87 ?  131 LEU D N     1 
ATOM   14421 C  CA    . LEU D 2 152 ? 152.870 91.611  144.658 1.00 24.37 ?  131 LEU D CA    1 
ATOM   14422 C  C     . LEU D 2 152 ? 151.733 90.695  145.126 1.00 24.18 ?  131 LEU D C     1 
ATOM   14423 O  O     . LEU D 2 152 ? 150.590 91.138  145.235 1.00 23.16 ?  131 LEU D O     1 
ATOM   14424 C  CB    . LEU D 2 152 ? 153.268 91.278  143.216 1.00 24.45 ?  131 LEU D CB    1 
ATOM   14425 C  CG    . LEU D 2 152 ? 151.990 91.451  142.376 1.00 26.33 ?  131 LEU D CG    1 
ATOM   14426 C  CD1   . LEU D 2 152 ? 151.660 92.937  142.178 1.00 25.00 ?  131 LEU D CD1   1 
ATOM   14427 C  CD2   . LEU D 2 152 ? 152.004 90.703  141.075 1.00 29.15 ?  131 LEU D CD2   1 
ATOM   14428 N  N     . GLN D 2 153 ? 152.057 89.436  145.430 1.00 24.07 ?  132 GLN D N     1 
ATOM   14429 C  CA    . GLN D 2 153 ? 151.046 88.493  145.953 1.00 24.99 ?  132 GLN D CA    1 
ATOM   14430 C  C     . GLN D 2 153 ? 150.370 88.968  147.236 1.00 24.24 ?  132 GLN D C     1 
ATOM   14431 O  O     . GLN D 2 153 ? 149.136 88.878  147.373 1.00 23.75 ?  132 GLN D O     1 
ATOM   14432 C  CB    . GLN D 2 153 ? 151.622 87.078  146.127 1.00 25.84 ?  132 GLN D CB    1 
ATOM   14433 C  CG    . GLN D 2 153 ? 151.903 86.352  144.784 1.00 28.48 ?  132 GLN D CG    1 
ATOM   14434 C  CD    . GLN D 2 153 ? 150.650 86.150  143.916 1.00 30.95 ?  132 GLN D CD    1 
ATOM   14435 O  OE1   . GLN D 2 153 ? 149.564 85.907  144.427 1.00 31.78 ?  132 GLN D OE1   1 
ATOM   14436 N  NE2   . GLN D 2 153 ? 150.815 86.239  142.595 1.00 32.81 ?  132 GLN D NE2   1 
ATOM   14437 N  N     . LYS D 2 154 ? 151.152 89.487  148.179 1.00 24.00 ?  133 LYS D N     1 
ATOM   14438 C  CA    . LYS D 2 154 ? 150.549 89.939  149.433 1.00 24.43 ?  133 LYS D CA    1 
ATOM   14439 C  C     . LYS D 2 154 ? 149.411 90.937  149.177 1.00 23.40 ?  133 LYS D C     1 
ATOM   14440 O  O     . LYS D 2 154 ? 148.289 90.741  149.650 1.00 22.68 ?  133 LYS D O     1 
ATOM   14441 C  CB    . LYS D 2 154 ? 151.569 90.550  150.400 1.00 24.64 ?  133 LYS D CB    1 
ATOM   14442 C  CG    . LYS D 2 154 ? 150.895 90.974  151.717 1.00 28.01 ?  133 LYS D CG    1 
ATOM   14443 C  CD    . LYS D 2 154 ? 151.858 91.425  152.790 1.00 32.56 ?  133 LYS D CD    1 
ATOM   14444 C  CE    . LYS D 2 154 ? 152.666 90.269  153.328 1.00 34.45 ?  133 LYS D CE    1 
ATOM   14445 N  NZ    . LYS D 2 154 ? 153.619 90.739  154.381 1.00 36.11 1  133 LYS D NZ    1 
ATOM   14446 N  N     . LYS D 2 155 ? 149.698 92.001  148.427 1.00 23.07 ?  134 LYS D N     1 
ATOM   14447 C  CA    . LYS D 2 155 ? 148.663 92.992  148.144 1.00 22.70 ?  134 LYS D CA    1 
ATOM   14448 C  C     . LYS D 2 155 ? 147.546 92.438  147.260 1.00 21.96 ?  134 LYS D C     1 
ATOM   14449 O  O     . LYS D 2 155 ? 146.379 92.691  147.537 1.00 22.25 ?  134 LYS D O     1 
ATOM   14450 C  CB    . LYS D 2 155 ? 149.241 94.311  147.597 1.00 22.70 ?  134 LYS D CB    1 
ATOM   14451 C  CG    . LYS D 2 155 ? 149.923 94.245  146.245 1.00 23.62 ?  134 LYS D CG    1 
ATOM   14452 C  CD    . LYS D 2 155 ? 150.359 95.651  145.836 1.00 25.32 ?  134 LYS D CD    1 
ATOM   14453 C  CE    . LYS D 2 155 ? 151.665 95.599  145.048 1.00 27.09 ?  134 LYS D CE    1 
ATOM   14454 N  NZ    . LYS D 2 155 ? 152.053 96.963  144.586 1.00 26.65 1  134 LYS D NZ    1 
ATOM   14455 N  N     . ALA D 2 156 ? 147.879 91.663  146.227 1.00 21.76 ?  135 ALA D N     1 
ATOM   14456 C  CA    . ALA D 2 156 ? 146.827 91.115  145.351 1.00 21.83 ?  135 ALA D CA    1 
ATOM   14457 C  C     . ALA D 2 156 ? 145.829 90.263  146.152 1.00 22.30 ?  135 ALA D C     1 
ATOM   14458 O  O     . ALA D 2 156 ? 144.612 90.423  146.013 1.00 21.92 ?  135 ALA D O     1 
ATOM   14459 C  CB    . ALA D 2 156 ? 147.430 90.300  144.193 1.00 22.30 ?  135 ALA D CB    1 
ATOM   14460 N  N     . GLN D 2 157 ? 146.343 89.379  147.008 1.00 22.15 ?  136 GLN D N     1 
ATOM   14461 C  CA    . GLN D 2 157 ? 145.472 88.493  147.788 1.00 22.38 ?  136 GLN D CA    1 
ATOM   14462 C  C     . GLN D 2 157 ? 144.709 89.206  148.912 1.00 21.59 ?  136 GLN D C     1 
ATOM   14463 O  O     . GLN D 2 157 ? 143.593 88.811  149.247 1.00 21.44 ?  136 GLN D O     1 
ATOM   14464 C  CB    . GLN D 2 157 ? 146.240 87.275  148.333 1.00 22.94 ?  136 GLN D CB    1 
ATOM   14465 C  CG    . GLN D 2 157 ? 146.918 86.403  147.264 1.00 25.31 ?  136 GLN D CG    1 
ATOM   14466 C  CD    . GLN D 2 157 ? 146.024 86.091  146.059 1.00 28.02 ?  136 GLN D CD    1 
ATOM   14467 O  OE1   . GLN D 2 157 ? 144.822 85.844  146.195 1.00 27.14 ?  136 GLN D OE1   1 
ATOM   14468 N  NE2   . GLN D 2 157 ? 146.626 86.093  144.871 1.00 29.47 ?  136 GLN D NE2   1 
ATOM   14469 N  N     . MET D 2 158 ? 145.302 90.240  149.498 1.00 21.52 ?  137 MET D N     1 
ATOM   14470 C  CA    . MET D 2 158 ? 144.590 91.054  150.498 1.00 22.20 ?  137 MET D CA    1 
ATOM   14471 C  C     . MET D 2 158 ? 143.327 91.700  149.915 1.00 21.84 ?  137 MET D C     1 
ATOM   14472 O  O     . MET D 2 158 ? 142.264 91.680  150.540 1.00 21.91 ?  137 MET D O     1 
ATOM   14473 C  CB    . MET D 2 158 ? 145.497 92.135  151.087 1.00 22.52 ?  137 MET D CB    1 
ATOM   14474 C  CG    . MET D 2 158 ? 146.492 91.608  152.131 1.00 25.81 ?  137 MET D CG    1 
ATOM   14475 S  SD    . MET D 2 158 ? 147.569 92.896  152.816 1.00 31.19 ?  137 MET D SD    1 
ATOM   14476 C  CE    . MET D 2 158 ? 146.326 93.891  153.599 1.00 23.91 ?  137 MET D CE    1 
ATOM   14477 N  N     . ILE D 2 159 ? 143.461 92.264  148.716 1.00 21.41 ?  138 ILE D N     1 
ATOM   14478 C  CA    . ILE D 2 159 ? 142.354 92.927  148.034 1.00 21.51 ?  138 ILE D CA    1 
ATOM   14479 C  C     . ILE D 2 159 ? 141.274 91.904  147.646 1.00 21.77 ?  138 ILE D C     1 
ATOM   14480 O  O     . ILE D 2 159 ? 140.084 92.107  147.933 1.00 21.44 ?  138 ILE D O     1 
ATOM   14481 C  CB    . ILE D 2 159 ? 142.880 93.752  146.796 1.00 21.49 ?  138 ILE D CB    1 
ATOM   14482 C  CG1   . ILE D 2 159 ? 143.838 94.869  147.238 1.00 21.16 ?  138 ILE D CG1   1 
ATOM   14483 C  CG2   . ILE D 2 159 ? 141.731 94.320  145.953 1.00 22.34 ?  138 ILE D CG2   1 
ATOM   14484 C  CD1   . ILE D 2 159 ? 143.215 95.941  148.156 1.00 23.85 ?  138 ILE D CD1   1 
ATOM   14485 N  N     . VAL D 2 160 ? 141.705 90.808  147.010 1.00 21.96 ?  139 VAL D N     1 
ATOM   14486 C  CA    . VAL D 2 160 ? 140.816 89.732  146.546 1.00 22.59 ?  139 VAL D CA    1 
ATOM   14487 C  C     . VAL D 2 160 ? 140.071 89.093  147.725 1.00 22.36 ?  139 VAL D C     1 
ATOM   14488 O  O     . VAL D 2 160 ? 138.891 88.748  147.605 1.00 21.64 ?  139 VAL D O     1 
ATOM   14489 C  CB    . VAL D 2 160 ? 141.606 88.657  145.724 1.00 23.08 ?  139 VAL D CB    1 
ATOM   14490 C  CG1   . VAL D 2 160 ? 140.811 87.349  145.553 1.00 24.33 ?  139 VAL D CG1   1 
ATOM   14491 C  CG2   . VAL D 2 160 ? 142.006 89.216  144.349 1.00 22.87 ?  139 VAL D CG2   1 
ATOM   14492 N  N     . GLY D 2 161 ? 140.764 88.947  148.858 1.00 22.21 ?  140 GLY D N     1 
ATOM   14493 C  CA    . GLY D 2 161 ? 140.153 88.423  150.078 1.00 22.50 ?  140 GLY D CA    1 
ATOM   14494 C  C     . GLY D 2 161 ? 138.936 89.232  150.514 1.00 22.88 ?  140 GLY D C     1 
ATOM   14495 O  O     . GLY D 2 161 ? 137.900 88.660  150.882 1.00 23.54 ?  140 GLY D O     1 
ATOM   14496 N  N     . LEU D 2 162 ? 139.047 90.559  150.462 1.00 22.25 ?  141 LEU D N     1 
ATOM   14497 C  CA    . LEU D 2 162 ? 137.923 91.427  150.823 1.00 22.48 ?  141 LEU D CA    1 
ATOM   14498 C  C     . LEU D 2 162 ? 136.764 91.360  149.825 1.00 22.27 ?  141 LEU D C     1 
ATOM   14499 O  O     . LEU D 2 162 ? 135.604 91.442  150.232 1.00 22.31 ?  141 LEU D O     1 
ATOM   14500 C  CB    . LEU D 2 162 ? 138.377 92.877  151.085 1.00 22.07 ?  141 LEU D CB    1 
ATOM   14501 C  CG    . LEU D 2 162 ? 139.115 93.071  152.428 1.00 22.81 ?  141 LEU D CG    1 
ATOM   14502 C  CD1   . LEU D 2 162 ? 139.978 94.331  152.435 1.00 21.65 ?  141 LEU D CD1   1 
ATOM   14503 C  CD2   . LEU D 2 162 ? 138.174 93.023  153.637 1.00 23.35 ?  141 LEU D CD2   1 
ATOM   14504 N  N     . TYR D 2 163 ? 137.066 91.213  148.533 1.00 22.63 ?  142 TYR D N     1 
ATOM   14505 C  CA    . TYR D 2 163 ? 136.010 91.001  147.523 1.00 23.30 ?  142 TYR D CA    1 
ATOM   14506 C  C     . TYR D 2 163 ? 135.272 89.686  147.740 1.00 23.40 ?  142 TYR D C     1 
ATOM   14507 O  O     . TYR D 2 163 ? 134.062 89.624  147.583 1.00 23.75 ?  142 TYR D O     1 
ATOM   14508 C  CB    . TYR D 2 163 ? 136.572 90.968  146.108 1.00 23.22 ?  142 TYR D CB    1 
ATOM   14509 C  CG    . TYR D 2 163 ? 137.252 92.224  145.636 1.00 24.01 ?  142 TYR D CG    1 
ATOM   14510 C  CD1   . TYR D 2 163 ? 136.972 93.456  146.211 1.00 24.47 ?  142 TYR D CD1   1 
ATOM   14511 C  CD2   . TYR D 2 163 ? 138.177 92.171  144.597 1.00 24.62 ?  142 TYR D CD2   1 
ATOM   14512 C  CE1   . TYR D 2 163 ? 137.596 94.605  145.772 1.00 26.33 ?  142 TYR D CE1   1 
ATOM   14513 C  CE2   . TYR D 2 163 ? 138.801 93.319  144.139 1.00 26.07 ?  142 TYR D CE2   1 
ATOM   14514 C  CZ    . TYR D 2 163 ? 138.498 94.536  144.736 1.00 26.65 ?  142 TYR D CZ    1 
ATOM   14515 O  OH    . TYR D 2 163 ? 139.115 95.688  144.306 1.00 31.13 ?  142 TYR D OH    1 
ATOM   14516 N  N     . LYS D 2 164 ? 136.005 88.638  148.091 1.00 23.70 ?  143 LYS D N     1 
ATOM   14517 C  CA    . LYS D 2 164 ? 135.397 87.323  148.348 1.00 24.47 ?  143 LYS D CA    1 
ATOM   14518 C  C     . LYS D 2 164 ? 134.552 87.276  149.632 1.00 24.55 ?  143 LYS D C     1 
ATOM   14519 O  O     . LYS D 2 164 ? 133.733 86.372  149.809 1.00 24.49 ?  143 LYS D O     1 
ATOM   14520 C  CB    . LYS D 2 164 ? 136.483 86.246  148.396 1.00 24.98 ?  143 LYS D CB    1 
ATOM   14521 C  CG    . LYS D 2 164 ? 137.053 85.849  147.026 1.00 27.10 ?  143 LYS D CG    1 
ATOM   14522 C  CD    . LYS D 2 164 ? 138.028 84.692  147.190 1.00 30.75 ?  143 LYS D CD    1 
ATOM   14523 C  CE    . LYS D 2 164 ? 138.559 84.172  145.855 1.00 32.81 ?  143 LYS D CE    1 
ATOM   14524 N  NZ    . LYS D 2 164 ? 139.610 83.093  146.044 1.00 33.68 1  143 LYS D NZ    1 
ATOM   14525 N  N     . ALA D 2 165 ? 134.762 88.238  150.526 1.00 24.18 ?  144 ALA D N     1 
ATOM   14526 C  CA    . ALA D 2 165 ? 134.069 88.260  151.817 1.00 25.04 ?  144 ALA D CA    1 
ATOM   14527 C  C     . ALA D 2 165 ? 132.754 89.052  151.823 1.00 25.00 ?  144 ALA D C     1 
ATOM   14528 O  O     . ALA D 2 165 ? 132.070 89.107  152.856 1.00 25.50 ?  144 ALA D O     1 
ATOM   14529 C  CB    . ALA D 2 165 ? 135.007 88.774  152.924 1.00 25.02 ?  144 ALA D CB    1 
ATOM   14530 N  N     . ILE D 2 166 ? 132.397 89.665  150.692 1.00 24.60 ?  145 ILE D N     1 
ATOM   14531 C  CA    . ILE D 2 166 ? 131.122 90.377  150.588 1.00 24.40 ?  145 ILE D CA    1 
ATOM   14532 C  C     . ILE D 2 166 ? 129.969 89.377  150.759 1.00 25.75 ?  145 ILE D C     1 
ATOM   14533 O  O     . ILE D 2 166 ? 129.970 88.303  150.148 1.00 25.84 ?  145 ILE D O     1 
ATOM   14534 C  CB    . ILE D 2 166 ? 130.945 91.125  149.236 1.00 24.15 ?  145 ILE D CB    1 
ATOM   14535 C  CG1   . ILE D 2 166 ? 132.158 92.000  148.927 1.00 23.15 ?  145 ILE D CG1   1 
ATOM   14536 C  CG2   . ILE D 2 166 ? 129.671 91.970  149.259 1.00 22.72 ?  145 ILE D CG2   1 
ATOM   14537 C  CD1   . ILE D 2 166 ? 132.158 92.574  147.525 1.00 21.70 ?  145 ILE D CD1   1 
ATOM   14538 N  N     . GLN D 2 167 ? 129.016 89.724  151.614 1.00 26.52 ?  146 GLN D N     1 
ATOM   14539 C  CA    . GLN D 2 167 ? 127.837 88.894  151.822 1.00 28.77 ?  146 GLN D CA    1 
ATOM   14540 C  C     . GLN D 2 167 ? 126.590 89.596  151.303 1.00 29.20 ?  146 GLN D C     1 
ATOM   14541 O  O     . GLN D 2 167 ? 126.442 90.818  151.453 1.00 28.89 ?  146 GLN D O     1 
ATOM   14542 C  CB    . GLN D 2 167 ? 127.677 88.566  153.304 1.00 29.04 ?  146 GLN D CB    1 
ATOM   14543 C  CG    . GLN D 2 167 ? 128.800 87.708  153.853 1.00 31.87 ?  146 GLN D CG    1 
ATOM   14544 C  CD    . GLN D 2 167 ? 129.273 88.190  155.198 1.00 35.35 ?  146 GLN D CD    1 
ATOM   14545 O  OE1   . GLN D 2 167 ? 128.552 88.096  156.195 1.00 36.91 ?  146 GLN D OE1   1 
ATOM   14546 N  NE2   . GLN D 2 167 ? 130.497 88.713  155.241 1.00 36.19 ?  146 GLN D NE2   1 
ATOM   14547 N  N     . LYS D 2 168 ? 125.695 88.820  150.695 1.00 30.29 ?  147 LYS D N     1 
ATOM   14548 C  CA    . LYS D 2 168 ? 124.425 89.352  150.206 1.00 31.24 ?  147 LYS D CA    1 
ATOM   14549 C  C     . LYS D 2 168 ? 123.700 90.145  151.293 1.00 31.73 ?  147 LYS D C     1 
ATOM   14550 O  O     . LYS D 2 168 ? 123.644 89.710  152.443 1.00 31.46 ?  147 LYS D O     1 
ATOM   14551 C  CB    . LYS D 2 168 ? 123.538 88.227  149.679 1.00 31.92 ?  147 LYS D CB    1 
ATOM   14552 C  CG    . LYS D 2 168 ? 122.231 88.717  149.074 1.00 33.23 ?  147 LYS D CG    1 
ATOM   14553 C  CD    . LYS D 2 168 ? 121.493 87.601  148.351 1.00 36.06 ?  147 LYS D CD    1 
ATOM   14554 C  CE    . LYS D 2 168 ? 120.161 88.082  147.816 1.00 35.46 ?  147 LYS D CE    1 
ATOM   14555 N  NZ    . LYS D 2 168 ? 120.319 89.014  146.668 1.00 38.24 1  147 LYS D NZ    1 
ATOM   14556 N  N     . ASP D 2 169 ? 123.171 91.314  150.920 1.00 32.28 ?  148 ASP D N     1 
ATOM   14557 C  CA    . ASP D 2 169 ? 122.436 92.201  151.837 1.00 33.45 ?  148 ASP D CA    1 
ATOM   14558 C  C     . ASP D 2 169 ? 123.196 92.637  153.089 1.00 33.30 ?  148 ASP D C     1 
ATOM   14559 O  O     . ASP D 2 169 ? 122.584 92.975  154.104 1.00 34.32 ?  148 ASP D O     1 
ATOM   14560 C  CB    . ASP D 2 169 ? 121.106 91.563  152.273 1.00 34.63 ?  148 ASP D CB    1 
ATOM   14561 C  CG    . ASP D 2 169 ? 120.066 91.550  151.173 1.00 36.09 ?  148 ASP D CG    1 
ATOM   14562 O  OD1   . ASP D 2 169 ? 120.239 92.233  150.142 1.00 37.80 ?  148 ASP D OD1   1 
ATOM   14563 O  OD2   . ASP D 2 169 ? 119.054 90.843  151.360 1.00 40.47 -1 148 ASP D OD2   1 
ATOM   14564 N  N     . ASP D 2 170 ? 124.519 92.611  153.043 1.00 32.58 ?  149 ASP D N     1 
ATOM   14565 C  CA    . ASP D 2 170 ? 125.306 93.129  154.160 1.00 32.01 ?  149 ASP D CA    1 
ATOM   14566 C  C     . ASP D 2 170 ? 126.156 94.293  153.665 1.00 30.59 ?  149 ASP D C     1 
ATOM   14567 O  O     . ASP D 2 170 ? 127.171 94.098  152.997 1.00 29.11 ?  149 ASP D O     1 
ATOM   14568 C  CB    . ASP D 2 170 ? 126.157 92.029  154.800 1.00 32.93 ?  149 ASP D CB    1 
ATOM   14569 C  CG    . ASP D 2 170 ? 127.171 92.568  155.801 1.00 35.05 ?  149 ASP D CG    1 
ATOM   14570 O  OD1   . ASP D 2 170 ? 126.936 93.619  156.437 1.00 39.25 ?  149 ASP D OD1   1 
ATOM   14571 O  OD2   . ASP D 2 170 ? 128.213 91.921  155.968 1.00 39.22 -1 149 ASP D OD2   1 
ATOM   14572 N  N     . GLU D 2 171 ? 125.710 95.502  153.998 1.00 29.34 ?  150 GLU D N     1 
ATOM   14573 C  CA    . GLU D 2 171 ? 126.349 96.725  153.520 1.00 28.51 ?  150 GLU D CA    1 
ATOM   14574 C  C     . GLU D 2 171 ? 127.712 96.997  154.171 1.00 27.27 ?  150 GLU D C     1 
ATOM   14575 O  O     . GLU D 2 171 ? 128.529 97.704  153.602 1.00 26.62 ?  150 GLU D O     1 
ATOM   14576 C  CB    . GLU D 2 171 ? 125.405 97.925  153.679 1.00 29.09 ?  150 GLU D CB    1 
ATOM   14577 C  CG    . GLU D 2 171 ? 125.132 98.360  155.117 1.00 30.68 ?  150 GLU D CG    1 
ATOM   14578 C  CD    . GLU D 2 171 ? 124.055 99.429  155.207 1.00 33.92 ?  150 GLU D CD    1 
ATOM   14579 O  OE1   . GLU D 2 171 ? 123.550 99.862  154.142 1.00 36.31 ?  150 GLU D OE1   1 
ATOM   14580 O  OE2   . GLU D 2 171 ? 123.710 99.849  156.333 1.00 34.02 -1 150 GLU D OE2   1 
ATOM   14581 N  N     . ILE D 2 172 ? 127.961 96.416  155.343 1.00 26.19 ?  151 ILE D N     1 
ATOM   14582 C  CA    . ILE D 2 172 ? 129.257 96.562  156.007 1.00 25.49 ?  151 ILE D CA    1 
ATOM   14583 C  C     . ILE D 2 172 ? 130.354 95.850  155.210 1.00 24.61 ?  151 ILE D C     1 
ATOM   14584 O  O     . ILE D 2 172 ? 131.413 96.429  154.942 1.00 24.09 ?  151 ILE D O     1 
ATOM   14585 C  CB    . ILE D 2 172 ? 129.217 96.075  157.483 1.00 25.98 ?  151 ILE D CB    1 
ATOM   14586 C  CG1   . ILE D 2 172 ? 128.257 96.929  158.312 1.00 26.86 ?  151 ILE D CG1   1 
ATOM   14587 C  CG2   . ILE D 2 172 ? 130.626 96.053  158.134 1.00 26.50 ?  151 ILE D CG2   1 
ATOM   14588 C  CD1   . ILE D 2 172 ? 128.623 98.405  158.376 1.00 27.81 ?  151 ILE D CD1   1 
ATOM   14589 N  N     . SER D 2 173 ? 130.082 94.609  154.816 1.00 23.71 ?  152 SER D N     1 
ATOM   14590 C  CA    . SER D 2 173 ? 131.028 93.833  154.017 1.00 23.38 ?  152 SER D CA    1 
ATOM   14591 C  C     . SER D 2 173 ? 131.213 94.454  152.620 1.00 22.41 ?  152 SER D C     1 
ATOM   14592 O  O     . SER D 2 173 ? 132.307 94.416  152.050 1.00 21.43 ?  152 SER D O     1 
ATOM   14593 C  CB    . SER D 2 173 ? 130.600 92.362  153.928 1.00 23.90 ?  152 SER D CB    1 
ATOM   14594 O  OG    . SER D 2 173 ? 129.437 92.161  153.125 1.00 23.74 ?  152 SER D OG    1 
ATOM   14595 N  N     . LEU D 2 174 ? 130.147 95.042  152.087 1.00 21.63 ?  153 LEU D N     1 
ATOM   14596 C  CA    . LEU D 2 174 ? 130.242 95.741  150.803 1.00 20.75 ?  153 LEU D CA    1 
ATOM   14597 C  C     . LEU D 2 174 ? 131.153 96.960  150.942 1.00 20.96 ?  153 LEU D C     1 
ATOM   14598 O  O     . LEU D 2 174 ? 132.010 97.198  150.091 1.00 20.41 ?  153 LEU D O     1 
ATOM   14599 C  CB    . LEU D 2 174 ? 128.851 96.155  150.284 1.00 20.62 ?  153 LEU D CB    1 
ATOM   14600 C  CG    . LEU D 2 174 ? 128.814 96.938  148.954 1.00 19.55 ?  153 LEU D CG    1 
ATOM   14601 C  CD1   . LEU D 2 174 ? 129.575 96.187  147.855 1.00 20.44 ?  153 LEU D CD1   1 
ATOM   14602 C  CD2   . LEU D 2 174 ? 127.360 97.205  148.541 1.00 20.99 ?  153 LEU D CD2   1 
ATOM   14603 N  N     . PHE D 2 175 ? 130.968 97.724  152.018 1.00 21.07 ?  154 PHE D N     1 
ATOM   14604 C  CA    . PHE D 2 175 ? 131.791 98.905  152.268 1.00 21.32 ?  154 PHE D CA    1 
ATOM   14605 C  C     . PHE D 2 175 ? 133.280 98.546  152.350 1.00 21.08 ?  154 PHE D C     1 
ATOM   14606 O  O     . PHE D 2 175 ? 134.125 99.222  151.761 1.00 20.85 ?  154 PHE D O     1 
ATOM   14607 C  CB    . PHE D 2 175 ? 131.347 99.607  153.556 1.00 21.20 ?  154 PHE D CB    1 
ATOM   14608 C  CG    . PHE D 2 175 ? 132.300 100.664 154.030 1.00 22.46 ?  154 PHE D CG    1 
ATOM   14609 C  CD1   . PHE D 2 175 ? 132.150 101.987 153.617 1.00 21.21 ?  154 PHE D CD1   1 
ATOM   14610 C  CD2   . PHE D 2 175 ? 133.347 100.346 154.900 1.00 22.53 ?  154 PHE D CD2   1 
ATOM   14611 C  CE1   . PHE D 2 175 ? 133.014 102.969 154.056 1.00 22.11 ?  154 PHE D CE1   1 
ATOM   14612 C  CE2   . PHE D 2 175 ? 134.234 101.326 155.334 1.00 23.26 ?  154 PHE D CE2   1 
ATOM   14613 C  CZ    . PHE D 2 175 ? 134.067 102.643 154.918 1.00 22.08 ?  154 PHE D CZ    1 
ATOM   14614 N  N     . LYS D 2 176 ? 133.590 97.488  153.092 1.00 21.14 ?  155 LYS D N     1 
ATOM   14615 C  CA    . LYS D 2 176 ? 134.974 97.024  153.235 1.00 20.93 ?  155 LYS D CA    1 
ATOM   14616 C  C     . LYS D 2 176 ? 135.609 96.679  151.890 1.00 20.61 ?  155 LYS D C     1 
ATOM   14617 O  O     . LYS D 2 176 ? 136.766 97.025  151.629 1.00 20.62 ?  155 LYS D O     1 
ATOM   14618 C  CB    . LYS D 2 176 ? 135.024 95.830  154.175 1.00 21.27 ?  155 LYS D CB    1 
ATOM   14619 C  CG    . LYS D 2 176 ? 134.808 96.233  155.607 1.00 22.04 ?  155 LYS D CG    1 
ATOM   14620 C  CD    . LYS D 2 176 ? 134.750 95.042  156.550 1.00 25.24 ?  155 LYS D CD    1 
ATOM   14621 C  CE    . LYS D 2 176 ? 134.596 95.539  157.965 1.00 25.83 ?  155 LYS D CE    1 
ATOM   14622 N  NZ    . LYS D 2 176 ? 134.548 94.435  158.967 1.00 26.64 1  155 LYS D NZ    1 
ATOM   14623 N  N     . ALA D 2 177 ? 134.836 96.022  151.032 1.00 20.02 ?  156 ALA D N     1 
ATOM   14624 C  CA    . ALA D 2 177 ? 135.281 95.722  149.672 1.00 19.86 ?  156 ALA D CA    1 
ATOM   14625 C  C     . ALA D 2 177 ? 135.471 96.994  148.833 1.00 19.61 ?  156 ALA D C     1 
ATOM   14626 O  O     . ALA D 2 177 ? 136.370 97.069  147.993 1.00 19.69 ?  156 ALA D O     1 
ATOM   14627 C  CB    . ALA D 2 177 ? 134.298 94.809  149.019 1.00 19.99 ?  156 ALA D CB    1 
ATOM   14628 N  N     . MET D 2 178 ? 134.615 97.989  149.053 1.00 19.75 ?  157 MET D N     1 
ATOM   14629 C  CA    . MET D 2 178 ? 134.712 99.261  148.307 1.00 18.89 ?  157 MET D CA    1 
ATOM   14630 C  C     . MET D 2 178 ? 135.973 100.011 148.708 1.00 18.62 ?  157 MET D C     1 
ATOM   14631 O  O     . MET D 2 178 ? 136.649 100.603 147.859 1.00 18.10 ?  157 MET D O     1 
ATOM   14632 C  CB    . MET D 2 178 ? 133.481 100.130 148.545 1.00 18.82 ?  157 MET D CB    1 
ATOM   14633 C  CG    . MET D 2 178 ? 132.247 99.638  147.806 1.00 20.20 ?  157 MET D CG    1 
ATOM   14634 S  SD    . MET D 2 178 ? 130.816 100.627 148.262 1.00 23.78 ?  157 MET D SD    1 
ATOM   14635 C  CE    . MET D 2 178 ? 129.620 100.004 147.083 1.00 22.62 ?  157 MET D CE    1 
ATOM   14636 N  N     . VAL D 2 179 ? 136.293 99.956  150.002 1.00 18.34 ?  158 VAL D N     1 
ATOM   14637 C  CA    . VAL D 2 179 ? 137.529 100.523 150.519 1.00 18.75 ?  158 VAL D CA    1 
ATOM   14638 C  C     . VAL D 2 179 ? 138.731 99.866  149.852 1.00 18.86 ?  158 VAL D C     1 
ATOM   14639 O  O     . VAL D 2 179 ? 139.655 100.570 149.406 1.00 18.79 ?  158 VAL D O     1 
ATOM   14640 C  CB    . VAL D 2 179 ? 137.648 100.397 152.061 1.00 19.02 ?  158 VAL D CB    1 
ATOM   14641 C  CG1   . VAL D 2 179 ? 139.057 100.802 152.518 1.00 19.10 ?  158 VAL D CG1   1 
ATOM   14642 C  CG2   . VAL D 2 179 ? 136.577 101.248 152.761 1.00 18.94 ?  158 VAL D CG2   1 
ATOM   14643 N  N     . ALA D 2 180 ? 138.718 98.528  149.799 1.00 18.96 ?  159 ALA D N     1 
ATOM   14644 C  CA    . ALA D 2 180 ? 139.753 97.768  149.096 1.00 19.05 ?  159 ALA D CA    1 
ATOM   14645 C  C     . ALA D 2 180 ? 139.856 98.199  147.631 1.00 18.67 ?  159 ALA D C     1 
ATOM   14646 O  O     . ALA D 2 180 ? 140.960 98.425  147.121 1.00 17.72 ?  159 ALA D O     1 
ATOM   14647 C  CB    . ALA D 2 180 ? 139.487 96.255  149.199 1.00 19.43 ?  159 ALA D CB    1 
ATOM   14648 N  N     . SER D 2 181 ? 138.701 98.344  146.974 1.00 18.49 ?  160 SER D N     1 
ATOM   14649 C  CA    . SER D 2 181 ? 138.672 98.768  145.573 1.00 18.51 ?  160 SER D CA    1 
ATOM   14650 C  C     . SER D 2 181 ? 139.256 100.167 145.372 1.00 18.23 ?  160 SER D C     1 
ATOM   14651 O  O     . SER D 2 181 ? 140.066 100.380 144.479 1.00 18.18 ?  160 SER D O     1 
ATOM   14652 C  CB    . SER D 2 181 ? 137.250 98.715  145.006 1.00 18.51 ?  160 SER D CB    1 
ATOM   14653 O  OG    . SER D 2 181 ? 137.292 98.966  143.615 1.00 19.42 ?  160 SER D OG    1 
ATOM   14654 N  N     . VAL D 2 182 ? 138.847 101.114 146.213 1.00 18.43 ?  161 VAL D N     1 
ATOM   14655 C  CA    . VAL D 2 182 ? 139.408 102.468 146.154 1.00 18.09 ?  161 VAL D CA    1 
ATOM   14656 C  C     . VAL D 2 182 ? 140.921 102.452 146.399 1.00 18.41 ?  161 VAL D C     1 
ATOM   14657 O  O     . VAL D 2 182 ? 141.672 103.134 145.699 1.00 18.52 ?  161 VAL D O     1 
ATOM   14658 C  CB    . VAL D 2 182 ? 138.698 103.426 147.119 1.00 17.71 ?  161 VAL D CB    1 
ATOM   14659 C  CG1   . VAL D 2 182 ? 139.440 104.782 147.196 1.00 16.02 ?  161 VAL D CG1   1 
ATOM   14660 C  CG2   . VAL D 2 182 ? 137.250 103.637 146.653 1.00 17.78 ?  161 VAL D CG2   1 
ATOM   14661 N  N     . TYR D 2 183 ? 141.368 101.639 147.358 1.00 19.06 ?  162 TYR D N     1 
ATOM   14662 C  CA    . TYR D 2 183 ? 142.801 101.530 147.614 1.00 19.73 ?  162 TYR D CA    1 
ATOM   14663 C  C     . TYR D 2 183 ? 143.546 100.989 146.402 1.00 19.90 ?  162 TYR D C     1 
ATOM   14664 O  O     . TYR D 2 183 ? 144.657 101.417 146.135 1.00 20.73 ?  162 TYR D O     1 
ATOM   14665 C  CB    . TYR D 2 183 ? 143.120 100.703 148.873 1.00 19.84 ?  162 TYR D CB    1 
ATOM   14666 C  CG    . TYR D 2 183 ? 142.807 101.405 150.179 1.00 20.24 ?  162 TYR D CG    1 
ATOM   14667 C  CD1   . TYR D 2 183 ? 142.525 102.768 150.215 1.00 21.51 ?  162 TYR D CD1   1 
ATOM   14668 C  CD2   . TYR D 2 183 ? 142.813 100.703 151.391 1.00 20.45 ?  162 TYR D CD2   1 
ATOM   14669 C  CE1   . TYR D 2 183 ? 142.242 103.416 151.424 1.00 21.68 ?  162 TYR D CE1   1 
ATOM   14670 C  CE2   . TYR D 2 183 ? 142.553 101.347 152.608 1.00 19.97 ?  162 TYR D CE2   1 
ATOM   14671 C  CZ    . TYR D 2 183 ? 142.263 102.701 152.613 1.00 21.83 ?  162 TYR D CZ    1 
ATOM   14672 O  OH    . TYR D 2 183 ? 141.994 103.346 153.804 1.00 21.96 ?  162 TYR D OH    1 
ATOM   14673 N  N     . LEU D 2 184 ? 142.940 100.074 145.659 1.00 20.22 ?  163 LEU D N     1 
ATOM   14674 C  CA    . LEU D 2 184 ? 143.592 99.564  144.456 1.00 20.89 ?  163 LEU D CA    1 
ATOM   14675 C  C     . LEU D 2 184 ? 143.626 100.649 143.370 1.00 20.72 ?  163 LEU D C     1 
ATOM   14676 O  O     . LEU D 2 184 ? 144.693 100.986 142.866 1.00 21.07 ?  163 LEU D O     1 
ATOM   14677 C  CB    . LEU D 2 184 ? 142.942 98.253  143.971 1.00 21.16 ?  163 LEU D CB    1 
ATOM   14678 C  CG    . LEU D 2 184 ? 143.468 97.584  142.684 1.00 22.77 ?  163 LEU D CG    1 
ATOM   14679 C  CD1   . LEU D 2 184 ? 144.999 97.380  142.696 1.00 22.44 ?  163 LEU D CD1   1 
ATOM   14680 C  CD2   . LEU D 2 184 ? 142.765 96.260  142.423 1.00 24.75 ?  163 LEU D CD2   1 
ATOM   14681 N  N     . GLU D 2 185 ? 142.463 101.215 143.053 1.00 20.65 ?  164 GLU D N     1 
ATOM   14682 C  CA    . GLU D 2 185 ? 142.327 102.226 141.994 1.00 20.69 ?  164 GLU D CA    1 
ATOM   14683 C  C     . GLU D 2 185 ? 143.140 103.500 142.226 1.00 20.64 ?  164 GLU D C     1 
ATOM   14684 O  O     . GLU D 2 185 ? 143.711 104.065 141.281 1.00 20.25 ?  164 GLU D O     1 
ATOM   14685 C  CB    . GLU D 2 185 ? 140.854 102.623 141.821 1.00 21.03 ?  164 GLU D CB    1 
ATOM   14686 C  CG    . GLU D 2 185 ? 139.910 101.468 141.471 1.00 22.19 ?  164 GLU D CG    1 
ATOM   14687 C  CD    . GLU D 2 185 ? 139.875 101.127 139.983 1.00 24.19 ?  164 GLU D CD    1 
ATOM   14688 O  OE1   . GLU D 2 185 ? 140.640 101.696 139.185 1.00 27.97 ?  164 GLU D OE1   1 
ATOM   14689 O  OE2   . GLU D 2 185 ? 139.055 100.294 139.595 1.00 25.47 -1 164 GLU D OE2   1 
ATOM   14690 N  N     . SER D 2 186 ? 143.160 103.966 143.470 1.00 20.42 ?  165 SER D N     1 
ATOM   14691 C  CA    . SER D 2 186 ? 143.682 105.295 143.786 1.00 20.70 ?  165 SER D CA    1 
ATOM   14692 C  C     . SER D 2 186 ? 145.015 105.284 144.532 1.00 20.88 ?  165 SER D C     1 
ATOM   14693 O  O     . SER D 2 186 ? 145.549 106.345 144.856 1.00 21.21 ?  165 SER D O     1 
ATOM   14694 C  CB    . SER D 2 186 ? 142.650 106.102 144.594 1.00 21.25 ?  165 SER D CB    1 
ATOM   14695 O  OG    . SER D 2 186 ? 141.379 106.123 143.960 1.00 20.97 ?  165 SER D OG    1 
ATOM   14696 N  N     . PHE D 2 187 ? 145.567 104.101 144.802 1.00 20.94 ?  166 PHE D N     1 
ATOM   14697 C  CA    . PHE D 2 187 ? 146.740 104.026 145.661 1.00 21.19 ?  166 PHE D CA    1 
ATOM   14698 C  C     . PHE D 2 187 ? 147.716 102.935 145.223 1.00 21.22 ?  166 PHE D C     1 
ATOM   14699 O  O     . PHE D 2 187 ? 148.847 103.257 144.840 1.00 21.10 ?  166 PHE D O     1 
ATOM   14700 C  CB    . PHE D 2 187 ? 146.301 103.941 147.150 1.00 21.63 ?  166 PHE D CB    1 
ATOM   14701 C  CG    . PHE D 2 187 ? 147.338 103.390 148.093 1.00 24.05 ?  166 PHE D CG    1 
ATOM   14702 C  CD1   . PHE D 2 187 ? 148.584 104.000 148.236 1.00 25.52 ?  166 PHE D CD1   1 
ATOM   14703 C  CD2   . PHE D 2 187 ? 147.045 102.280 148.882 1.00 27.03 ?  166 PHE D CD2   1 
ATOM   14704 C  CE1   . PHE D 2 187 ? 149.522 103.496 149.128 1.00 26.73 ?  166 PHE D CE1   1 
ATOM   14705 C  CE2   . PHE D 2 187 ? 147.996 101.763 149.775 1.00 27.36 ?  166 PHE D CE2   1 
ATOM   14706 C  CZ    . PHE D 2 187 ? 149.229 102.373 149.890 1.00 27.87 ?  166 PHE D CZ    1 
ATOM   14707 N  N     . LEU D 2 188 ? 147.277 101.679 145.222 1.00 20.78 ?  167 LEU D N     1 
ATOM   14708 C  CA    . LEU D 2 188 ? 148.176 100.543 144.934 1.00 21.78 ?  167 LEU D CA    1 
ATOM   14709 C  C     . LEU D 2 188 ? 148.776 100.530 143.522 1.00 21.91 ?  167 LEU D C     1 
ATOM   14710 O  O     . LEU D 2 188 ? 149.902 100.067 143.340 1.00 22.87 ?  167 LEU D O     1 
ATOM   14711 C  CB    . LEU D 2 188 ? 147.479 99.210  145.203 1.00 22.32 ?  167 LEU D CB    1 
ATOM   14712 C  CG    . LEU D 2 188 ? 147.095 98.814  146.629 1.00 23.33 ?  167 LEU D CG    1 
ATOM   14713 C  CD1   . LEU D 2 188 ? 146.401 97.464  146.588 1.00 22.43 ?  167 LEU D CD1   1 
ATOM   14714 C  CD2   . LEU D 2 188 ? 148.298 98.776  147.579 1.00 25.71 ?  167 LEU D CD2   1 
ATOM   14715 N  N     . PHE D 2 189 ? 148.025 101.014 142.531 1.00 21.56 ?  168 PHE D N     1 
ATOM   14716 C  CA    . PHE D 2 189 ? 148.526 101.118 141.158 1.00 21.86 ?  168 PHE D CA    1 
ATOM   14717 C  C     . PHE D 2 189 ? 149.716 102.093 141.029 1.00 21.87 ?  168 PHE D C     1 
ATOM   14718 O  O     . PHE D 2 189 ? 150.513 101.992 140.093 1.00 21.79 ?  168 PHE D O     1 
ATOM   14719 C  CB    . PHE D 2 189 ? 147.421 101.600 140.200 1.00 21.79 ?  168 PHE D CB    1 
ATOM   14720 C  CG    . PHE D 2 189 ? 146.447 100.528 139.770 1.00 21.88 ?  168 PHE D CG    1 
ATOM   14721 C  CD1   . PHE D 2 189 ? 146.871 99.226  139.496 1.00 21.44 ?  168 PHE D CD1   1 
ATOM   14722 C  CD2   . PHE D 2 189 ? 145.098 100.841 139.606 1.00 22.82 ?  168 PHE D CD2   1 
ATOM   14723 C  CE1   . PHE D 2 189 ? 145.958 98.243  139.092 1.00 22.35 ?  168 PHE D CE1   1 
ATOM   14724 C  CE2   . PHE D 2 189 ? 144.175 99.876  139.202 1.00 22.08 ?  168 PHE D CE2   1 
ATOM   14725 C  CZ    . PHE D 2 189 ? 144.603 98.568  138.954 1.00 22.60 ?  168 PHE D CZ    1 
ATOM   14726 N  N     . TYR D 2 190 ? 149.820 103.047 141.948 1.00 21.91 ?  169 TYR D N     1 
ATOM   14727 C  CA    . TYR D 2 190 ? 150.725 104.186 141.727 1.00 22.52 ?  169 TYR D CA    1 
ATOM   14728 C  C     . TYR D 2 190 ? 152.214 103.913 141.945 1.00 22.75 ?  169 TYR D C     1 
ATOM   14729 O  O     . TYR D 2 190 ? 153.038 104.583 141.338 1.00 21.93 ?  169 TYR D O     1 
ATOM   14730 C  CB    . TYR D 2 190 ? 150.237 105.442 142.455 1.00 22.67 ?  169 TYR D CB    1 
ATOM   14731 C  CG    . TYR D 2 190 ? 149.065 106.063 141.723 1.00 24.77 ?  169 TYR D CG    1 
ATOM   14732 C  CD1   . TYR D 2 190 ? 147.789 105.495 141.795 1.00 25.65 ?  169 TYR D CD1   1 
ATOM   14733 C  CD2   . TYR D 2 190 ? 149.242 107.186 140.920 1.00 25.94 ?  169 TYR D CD2   1 
ATOM   14734 C  CE1   . TYR D 2 190 ? 146.714 106.050 141.092 1.00 26.62 ?  169 TYR D CE1   1 
ATOM   14735 C  CE2   . TYR D 2 190 ? 148.175 107.756 140.229 1.00 26.91 ?  169 TYR D CE2   1 
ATOM   14736 C  CZ    . TYR D 2 190 ? 146.920 107.184 140.315 1.00 27.39 ?  169 TYR D CZ    1 
ATOM   14737 O  OH    . TYR D 2 190 ? 145.876 107.761 139.616 1.00 27.50 ?  169 TYR D OH    1 
ATOM   14738 N  N     . SER D 2 191 ? 152.554 102.919 142.772 1.00 22.74 ?  170 SER D N     1 
ATOM   14739 C  CA    . SER D 2 191 ? 153.948 102.462 142.850 1.00 23.43 ?  170 SER D CA    1 
ATOM   14740 C  C     . SER D 2 191 ? 154.379 101.933 141.482 1.00 23.08 ?  170 SER D C     1 
ATOM   14741 O  O     . SER D 2 191 ? 155.541 102.006 141.122 1.00 23.67 ?  170 SER D O     1 
ATOM   14742 C  CB    . SER D 2 191 ? 154.144 101.387 143.930 1.00 23.39 ?  170 SER D CB    1 
ATOM   14743 O  OG    . SER D 2 191 ? 153.368 100.229 143.661 1.00 24.10 ?  170 SER D OG    1 
ATOM   14744 N  N     . GLY D 2 192 ? 153.417 101.439 140.715 1.00 22.82 ?  171 GLY D N     1 
ATOM   14745 C  CA    . GLY D 2 192 ? 153.656 100.953 139.362 1.00 22.08 ?  171 GLY D CA    1 
ATOM   14746 C  C     . GLY D 2 192 ? 153.626 102.048 138.308 1.00 22.12 ?  171 GLY D C     1 
ATOM   14747 O  O     . GLY D 2 192 ? 154.548 102.149 137.496 1.00 22.86 ?  171 GLY D O     1 
ATOM   14748 N  N     . PHE D 2 193 ? 152.577 102.869 138.319 1.00 21.48 ?  172 PHE D N     1 
ATOM   14749 C  CA    . PHE D 2 193 ? 152.438 103.982 137.360 1.00 21.06 ?  172 PHE D CA    1 
ATOM   14750 C  C     . PHE D 2 193 ? 153.650 104.914 137.369 1.00 21.13 ?  172 PHE D C     1 
ATOM   14751 O  O     . PHE D 2 193 ? 153.962 105.529 136.348 1.00 21.18 ?  172 PHE D O     1 
ATOM   14752 C  CB    . PHE D 2 193 ? 151.191 104.812 137.656 1.00 21.33 ?  172 PHE D CB    1 
ATOM   14753 C  CG    . PHE D 2 193 ? 149.886 104.132 137.316 1.00 20.93 ?  172 PHE D CG    1 
ATOM   14754 C  CD1   . PHE D 2 193 ? 149.795 103.204 136.279 1.00 20.88 ?  172 PHE D CD1   1 
ATOM   14755 C  CD2   . PHE D 2 193 ? 148.732 104.469 138.011 1.00 19.83 ?  172 PHE D CD2   1 
ATOM   14756 C  CE1   . PHE D 2 193 ? 148.570 102.601 135.970 1.00 22.31 ?  172 PHE D CE1   1 
ATOM   14757 C  CE2   . PHE D 2 193 ? 147.501 103.880 137.700 1.00 20.67 ?  172 PHE D CE2   1 
ATOM   14758 C  CZ    . PHE D 2 193 ? 147.422 102.945 136.678 1.00 21.00 ?  172 PHE D CZ    1 
ATOM   14759 N  N     . TYR D 2 194 ? 154.331 105.006 138.513 1.00 20.48 ?  173 TYR D N     1 
ATOM   14760 C  CA    . TYR D 2 194 ? 155.472 105.906 138.665 1.00 20.76 ?  173 TYR D CA    1 
ATOM   14761 C  C     . TYR D 2 194 ? 156.460 105.786 137.499 1.00 20.53 ?  173 TYR D C     1 
ATOM   14762 O  O     . TYR D 2 194 ? 156.857 106.782 136.887 1.00 19.89 ?  173 TYR D O     1 
ATOM   14763 C  CB    . TYR D 2 194 ? 156.200 105.667 140.011 1.00 20.94 ?  173 TYR D CB    1 
ATOM   14764 C  CG    . TYR D 2 194 ? 157.243 106.732 140.305 1.00 21.56 ?  173 TYR D CG    1 
ATOM   14765 C  CD1   . TYR D 2 194 ? 156.960 107.795 141.167 1.00 22.23 ?  173 TYR D CD1   1 
ATOM   14766 C  CD2   . TYR D 2 194 ? 158.506 106.690 139.703 1.00 22.00 ?  173 TYR D CD2   1 
ATOM   14767 C  CE1   . TYR D 2 194 ? 157.906 108.786 141.420 1.00 21.58 ?  173 TYR D CE1   1 
ATOM   14768 C  CE2   . TYR D 2 194 ? 159.452 107.665 139.955 1.00 20.52 ?  173 TYR D CE2   1 
ATOM   14769 C  CZ    . TYR D 2 194 ? 159.148 108.710 140.811 1.00 21.66 ?  173 TYR D CZ    1 
ATOM   14770 O  OH    . TYR D 2 194 ? 160.081 109.693 141.040 1.00 21.37 ?  173 TYR D OH    1 
ATOM   14771 N  N     . TYR D 2 195 ? 156.832 104.559 137.174 1.00 20.77 ?  174 TYR D N     1 
ATOM   14772 C  CA    . TYR D 2 195 ? 157.920 104.352 136.234 1.00 21.12 ?  174 TYR D CA    1 
ATOM   14773 C  C     . TYR D 2 195 ? 157.572 104.775 134.796 1.00 21.49 ?  174 TYR D C     1 
ATOM   14774 O  O     . TYR D 2 195 ? 158.328 105.547 134.199 1.00 21.60 ?  174 TYR D O     1 
ATOM   14775 C  CB    . TYR D 2 195 ? 158.454 102.921 136.343 1.00 21.23 ?  174 TYR D CB    1 
ATOM   14776 C  CG    . TYR D 2 195 ? 159.921 102.760 136.013 1.00 21.77 ?  174 TYR D CG    1 
ATOM   14777 C  CD1   . TYR D 2 195 ? 160.863 103.721 136.394 1.00 23.28 ?  174 TYR D CD1   1 
ATOM   14778 C  CD2   . TYR D 2 195 ? 160.372 101.628 135.338 1.00 22.87 ?  174 TYR D CD2   1 
ATOM   14779 C  CE1   . TYR D 2 195 ? 162.222 103.555 136.088 1.00 23.81 ?  174 TYR D CE1   1 
ATOM   14780 C  CE2   . TYR D 2 195 ? 161.721 101.454 135.040 1.00 24.09 ?  174 TYR D CE2   1 
ATOM   14781 C  CZ    . TYR D 2 195 ? 162.635 102.419 135.410 1.00 23.51 ?  174 TYR D CZ    1 
ATOM   14782 O  OH    . TYR D 2 195 ? 163.971 102.245 135.102 1.00 25.36 ?  174 TYR D OH    1 
ATOM   14783 N  N     . PRO D 2 196 ? 156.432 104.292 134.238 1.00 21.86 ?  175 PRO D N     1 
ATOM   14784 C  CA    . PRO D 2 196 ? 156.014 104.779 132.914 1.00 22.03 ?  175 PRO D CA    1 
ATOM   14785 C  C     . PRO D 2 196 ? 155.855 106.297 132.861 1.00 22.18 ?  175 PRO D C     1 
ATOM   14786 O  O     . PRO D 2 196 ? 156.217 106.905 131.850 1.00 23.00 ?  175 PRO D O     1 
ATOM   14787 C  CB    . PRO D 2 196 ? 154.652 104.109 132.688 1.00 21.50 ?  175 PRO D CB    1 
ATOM   14788 C  CG    . PRO D 2 196 ? 154.633 102.955 133.561 1.00 22.47 ?  175 PRO D CG    1 
ATOM   14789 C  CD    . PRO D 2 196 ? 155.618 103.144 134.676 1.00 20.91 ?  175 PRO D CD    1 
ATOM   14790 N  N     . LEU D 2 197 ? 155.335 106.903 133.930 1.00 21.70 ?  176 LEU D N     1 
ATOM   14791 C  CA    . LEU D 2 197 ? 155.218 108.367 134.002 1.00 22.40 ?  176 LEU D CA    1 
ATOM   14792 C  C     . LEU D 2 197 ? 156.581 109.061 134.043 1.00 22.58 ?  176 LEU D C     1 
ATOM   14793 O  O     . LEU D 2 197 ? 156.759 110.133 133.449 1.00 22.15 ?  176 LEU D O     1 
ATOM   14794 C  CB    . LEU D 2 197 ? 154.406 108.794 135.218 1.00 22.15 ?  176 LEU D CB    1 
ATOM   14795 C  CG    . LEU D 2 197 ? 152.895 108.535 135.241 1.00 23.08 ?  176 LEU D CG    1 
ATOM   14796 C  CD1   . LEU D 2 197 ? 152.402 108.712 136.668 1.00 21.62 ?  176 LEU D CD1   1 
ATOM   14797 C  CD2   . LEU D 2 197 ? 152.151 109.476 134.272 1.00 21.94 ?  176 LEU D CD2   1 
ATOM   14798 N  N     . TYR D 2 198 ? 157.525 108.440 134.755 1.00 22.76 ?  177 TYR D N     1 
ATOM   14799 C  CA    . TYR D 2 198 ? 158.912 108.903 134.833 1.00 23.23 ?  177 TYR D CA    1 
ATOM   14800 C  C     . TYR D 2 198 ? 159.569 108.914 133.453 1.00 23.91 ?  177 TYR D C     1 
ATOM   14801 O  O     . TYR D 2 198 ? 160.200 109.910 133.069 1.00 24.20 ?  177 TYR D O     1 
ATOM   14802 C  CB    . TYR D 2 198 ? 159.703 108.040 135.830 1.00 23.19 ?  177 TYR D CB    1 
ATOM   14803 C  CG    . TYR D 2 198 ? 161.152 108.435 136.044 1.00 23.52 ?  177 TYR D CG    1 
ATOM   14804 C  CD1   . TYR D 2 198 ? 161.482 109.635 136.658 1.00 24.85 ?  177 TYR D CD1   1 
ATOM   14805 C  CD2   . TYR D 2 198 ? 162.193 107.577 135.667 1.00 25.30 ?  177 TYR D CD2   1 
ATOM   14806 C  CE1   . TYR D 2 198 ? 162.815 109.994 136.875 1.00 26.05 ?  177 TYR D CE1   1 
ATOM   14807 C  CE2   . TYR D 2 198 ? 163.537 107.927 135.885 1.00 26.38 ?  177 TYR D CE2   1 
ATOM   14808 C  CZ    . TYR D 2 198 ? 163.830 109.135 136.489 1.00 26.68 ?  177 TYR D CZ    1 
ATOM   14809 O  OH    . TYR D 2 198 ? 165.139 109.501 136.717 1.00 30.01 ?  177 TYR D OH    1 
ATOM   14810 N  N     . PHE D 2 199 ? 159.419 107.826 132.696 1.00 24.84 ?  178 PHE D N     1 
ATOM   14811 C  CA    . PHE D 2 199 ? 159.908 107.814 131.314 1.00 25.81 ?  178 PHE D CA    1 
ATOM   14812 C  C     . PHE D 2 199 ? 159.180 108.805 130.414 1.00 26.23 ?  178 PHE D C     1 
ATOM   14813 O  O     . PHE D 2 199 ? 159.812 109.532 129.646 1.00 26.58 ?  178 PHE D O     1 
ATOM   14814 C  CB    . PHE D 2 199 ? 159.852 106.415 130.716 1.00 26.08 ?  178 PHE D CB    1 
ATOM   14815 C  CG    . PHE D 2 199 ? 160.936 105.507 131.215 1.00 28.71 ?  178 PHE D CG    1 
ATOM   14816 C  CD1   . PHE D 2 199 ? 162.252 105.945 131.282 1.00 32.03 ?  178 PHE D CD1   1 
ATOM   14817 C  CD2   . PHE D 2 199 ? 160.647 104.216 131.624 1.00 31.77 ?  178 PHE D CD2   1 
ATOM   14818 C  CE1   . PHE D 2 199 ? 163.273 105.108 131.759 1.00 32.29 ?  178 PHE D CE1   1 
ATOM   14819 C  CE2   . PHE D 2 199 ? 161.661 103.373 132.092 1.00 32.72 ?  178 PHE D CE2   1 
ATOM   14820 C  CZ    . PHE D 2 199 ? 162.974 103.827 132.156 1.00 31.91 ?  178 PHE D CZ    1 
ATOM   14821 N  N     . TYR D 2 200 ? 157.854 108.817 130.524 1.00 26.46 ?  179 TYR D N     1 
ATOM   14822 C  CA    . TYR D 2 200 ? 156.971 109.690 129.734 1.00 27.43 ?  179 TYR D CA    1 
ATOM   14823 C  C     . TYR D 2 200 ? 157.343 111.157 129.924 1.00 27.68 ?  179 TYR D C     1 
ATOM   14824 O  O     . TYR D 2 200 ? 157.342 111.930 128.967 1.00 28.71 ?  179 TYR D O     1 
ATOM   14825 C  CB    . TYR D 2 200 ? 155.535 109.452 130.190 1.00 27.27 ?  179 TYR D CB    1 
ATOM   14826 C  CG    . TYR D 2 200 ? 154.426 109.924 129.282 1.00 28.90 ?  179 TYR D CG    1 
ATOM   14827 C  CD1   . TYR D 2 200 ? 154.432 109.644 127.922 1.00 29.00 ?  179 TYR D CD1   1 
ATOM   14828 C  CD2   . TYR D 2 200 ? 153.324 110.600 129.815 1.00 30.14 ?  179 TYR D CD2   1 
ATOM   14829 C  CE1   . TYR D 2 200 ? 153.387 110.057 127.100 1.00 31.26 ?  179 TYR D CE1   1 
ATOM   14830 C  CE2   . TYR D 2 200 ? 152.273 111.007 129.010 1.00 31.86 ?  179 TYR D CE2   1 
ATOM   14831 C  CZ    . TYR D 2 200 ? 152.311 110.738 127.652 1.00 32.51 ?  179 TYR D CZ    1 
ATOM   14832 O  OH    . TYR D 2 200 ? 151.271 111.146 126.853 1.00 33.77 ?  179 TYR D OH    1 
ATOM   14833 N  N     . GLY D 2 201 ? 157.666 111.531 131.161 1.00 27.68 ?  180 GLY D N     1 
ATOM   14834 C  CA    . GLY D 2 201 ? 158.101 112.888 131.473 1.00 28.02 ?  180 GLY D CA    1 
ATOM   14835 C  C     . GLY D 2 201 ? 159.485 113.261 130.947 1.00 28.60 ?  180 GLY D C     1 
ATOM   14836 O  O     . GLY D 2 201 ? 159.832 114.435 130.930 1.00 28.44 ?  180 GLY D O     1 
ATOM   14837 N  N     . GLN D 2 202 ? 160.267 112.257 130.540 1.00 29.34 ?  181 GLN D N     1 
ATOM   14838 C  CA    . GLN D 2 202 ? 161.622 112.435 129.990 1.00 30.39 ?  181 GLN D CA    1 
ATOM   14839 C  C     . GLN D 2 202 ? 161.683 112.314 128.467 1.00 30.55 ?  181 GLN D C     1 
ATOM   14840 O  O     . GLN D 2 202 ? 162.760 112.457 127.880 1.00 31.23 ?  181 GLN D O     1 
ATOM   14841 C  CB    . GLN D 2 202 ? 162.554 111.334 130.502 1.00 30.31 ?  181 GLN D CB    1 
ATOM   14842 C  CG    . GLN D 2 202 ? 162.908 111.332 131.941 1.00 32.40 ?  181 GLN D CG    1 
ATOM   14843 C  CD    . GLN D 2 202 ? 163.825 110.168 132.254 1.00 33.85 ?  181 GLN D CD    1 
ATOM   14844 O  OE1   . GLN D 2 202 ? 163.412 109.175 132.847 1.00 33.94 ?  181 GLN D OE1   1 
ATOM   14845 N  NE2   . GLN D 2 202 ? 165.067 110.266 131.811 1.00 34.92 ?  181 GLN D NE2   1 
ATOM   14846 N  N     . GLY D 2 203 ? 160.564 111.981 127.834 1.00 30.57 ?  182 GLY D N     1 
ATOM   14847 C  CA    . GLY D 2 203 ? 160.542 111.775 126.385 1.00 30.83 ?  182 GLY D CA    1 
ATOM   14848 C  C     . GLY D 2 203 ? 160.854 110.350 125.953 1.00 30.80 ?  182 GLY D C     1 
ATOM   14849 O  O     . GLY D 2 203 ? 161.065 110.090 124.765 1.00 30.86 ?  182 GLY D O     1 
ATOM   14850 N  N     . LYS D 2 204 ? 160.877 109.425 126.913 1.00 30.14 ?  183 LYS D N     1 
ATOM   14851 C  CA    . LYS D 2 204 ? 161.131 108.010 126.625 1.00 30.35 ?  183 LYS D CA    1 
ATOM   14852 C  C     . LYS D 2 204 ? 159.850 107.181 126.681 1.00 29.52 ?  183 LYS D C     1 
ATOM   14853 O  O     . LYS D 2 204 ? 158.959 107.470 127.476 1.00 28.60 ?  183 LYS D O     1 
ATOM   14854 C  CB    . LYS D 2 204 ? 162.166 107.446 127.596 1.00 30.76 ?  183 LYS D CB    1 
ATOM   14855 C  CG    . LYS D 2 204 ? 163.557 108.068 127.437 1.00 32.95 ?  183 LYS D CG    1 
ATOM   14856 C  CD    . LYS D 2 204 ? 164.435 107.675 128.601 1.00 36.37 ?  183 LYS D CD    1 
ATOM   14857 C  CE    . LYS D 2 204 ? 165.829 108.265 128.492 1.00 38.47 ?  183 LYS D CE    1 
ATOM   14858 N  NZ    . LYS D 2 204 ? 166.535 108.040 129.789 1.00 40.21 1  183 LYS D NZ    1 
ATOM   14859 N  N     . LEU D 2 205 ? 159.774 106.146 125.839 1.00 29.47 ?  184 LEU D N     1 
ATOM   14860 C  CA    . LEU D 2 205 ? 158.605 105.257 125.761 1.00 29.06 ?  184 LEU D CA    1 
ATOM   14861 C  C     . LEU D 2 205 ? 157.281 106.048 125.800 1.00 28.96 ?  184 LEU D C     1 
ATOM   14862 O  O     . LEU D 2 205 ? 156.401 105.803 126.635 1.00 27.68 ?  184 LEU D O     1 
ATOM   14863 C  CB    . LEU D 2 205 ? 158.652 104.185 126.861 1.00 28.63 ?  184 LEU D CB    1 
ATOM   14864 C  CG    . LEU D 2 205 ? 159.893 103.280 126.933 1.00 29.00 ?  184 LEU D CG    1 
ATOM   14865 C  CD1   . LEU D 2 205 ? 159.792 102.336 128.134 1.00 28.90 ?  184 LEU D CD1   1 
ATOM   14866 C  CD2   . LEU D 2 205 ? 160.076 102.481 125.650 1.00 28.67 ?  184 LEU D CD2   1 
ATOM   14867 N  N     . MET D 2 206 ? 157.174 106.994 124.871 1.00 29.02 ?  185 MET D N     1 
ATOM   14868 C  CA    . MET D 2 206 ? 156.056 107.920 124.778 1.00 29.72 ?  185 MET D CA    1 
ATOM   14869 C  C     . MET D 2 206 ? 154.722 107.302 124.374 1.00 29.54 ?  185 MET D C     1 
ATOM   14870 O  O     . MET D 2 206 ? 153.676 107.774 124.813 1.00 29.47 ?  185 MET D O     1 
ATOM   14871 C  CB    . MET D 2 206 ? 156.409 109.061 123.816 1.00 30.69 ?  185 MET D CB    1 
ATOM   14872 C  CG    . MET D 2 206 ? 157.648 109.834 124.242 1.00 32.03 ?  185 MET D CG    1 
ATOM   14873 S  SD    . MET D 2 206 ? 157.447 110.542 125.886 1.00 36.63 ?  185 MET D SD    1 
ATOM   14874 C  CE    . MET D 2 206 ? 156.598 112.059 125.487 1.00 33.80 ?  185 MET D CE    1 
ATOM   14875 N  N     . GLN D 2 207 ? 154.756 106.276 123.526 1.00 29.56 ?  186 GLN D N     1 
ATOM   14876 C  CA    . GLN D 2 207 ? 153.530 105.626 123.051 1.00 29.17 ?  186 GLN D CA    1 
ATOM   14877 C  C     . GLN D 2 207 ? 152.894 104.799 124.164 1.00 28.26 ?  186 GLN D C     1 
ATOM   14878 O  O     . GLN D 2 207 ? 151.695 104.903 124.405 1.00 27.98 ?  186 GLN D O     1 
ATOM   14879 C  CB    . GLN D 2 207 ? 153.799 104.751 121.815 1.00 29.80 ?  186 GLN D CB    1 
ATOM   14880 C  CG    . GLN D 2 207 ? 154.489 105.474 120.660 1.00 31.75 ?  186 GLN D CG    1 
ATOM   14881 C  CD    . GLN D 2 207 ? 153.779 106.759 120.282 1.00 34.93 ?  186 GLN D CD    1 
ATOM   14882 O  OE1   . GLN D 2 207 ? 152.680 106.739 119.712 1.00 36.91 ?  186 GLN D OE1   1 
ATOM   14883 N  NE2   . GLN D 2 207 ? 154.398 107.887 120.610 1.00 36.09 ?  186 GLN D NE2   1 
ATOM   14884 N  N     . SER D 2 208 ? 153.698 103.981 124.841 0.50 27.75 ?  187 SER D N     1 
ATOM   14885 C  CA    . SER D 2 208 ? 153.197 103.189 125.959 0.50 27.12 ?  187 SER D CA    1 
ATOM   14886 C  C     . SER D 2 208 ? 152.866 104.084 127.150 0.50 26.72 ?  187 SER D C     1 
ATOM   14887 O  O     . SER D 2 208 ? 151.943 103.785 127.906 0.50 26.30 ?  187 SER D O     1 
ATOM   14888 C  CB    . SER D 2 208 ? 154.193 102.100 126.359 0.50 26.88 ?  187 SER D CB    1 
ATOM   14889 O  OG    . SER D 2 208 ? 155.474 102.651 126.571 0.50 26.59 ?  187 SER D OG    1 
ATOM   14890 N  N     . GLY D 2 209 ? 153.617 105.175 127.305 1.00 26.64 ?  188 GLY D N     1 
ATOM   14891 C  CA    . GLY D 2 209 ? 153.342 106.178 128.354 1.00 26.43 ?  188 GLY D CA    1 
ATOM   14892 C  C     . GLY D 2 209 ? 152.014 106.895 128.144 1.00 26.66 ?  188 GLY D C     1 
ATOM   14893 O  O     . GLY D 2 209 ? 151.311 107.217 129.102 1.00 26.57 ?  188 GLY D O     1 
ATOM   14894 N  N     . GLU D 2 210 ? 151.671 107.153 126.886 1.00 27.42 ?  189 GLU D N     1 
ATOM   14895 C  CA    . GLU D 2 210 ? 150.371 107.734 126.554 1.00 27.73 ?  189 GLU D CA    1 
ATOM   14896 C  C     . GLU D 2 210 ? 149.250 106.753 126.929 1.00 27.04 ?  189 GLU D C     1 
ATOM   14897 O  O     . GLU D 2 210 ? 148.261 107.139 127.553 1.00 26.57 ?  189 GLU D O     1 
ATOM   14898 C  CB    . GLU D 2 210 ? 150.299 108.126 125.067 1.00 28.28 ?  189 GLU D CB    1 
ATOM   14899 C  CG    . GLU D 2 210 ? 148.989 108.833 124.684 1.00 30.71 ?  189 GLU D CG    1 
ATOM   14900 C  CD    . GLU D 2 210 ? 148.998 109.463 123.292 1.00 35.43 ?  189 GLU D CD    1 
ATOM   14901 O  OE1   . GLU D 2 210 ? 149.957 109.242 122.511 1.00 36.89 ?  189 GLU D OE1   1 
ATOM   14902 O  OE2   . GLU D 2 210 ? 148.032 110.198 122.984 1.00 37.04 -1 189 GLU D OE2   1 
ATOM   14903 N  N     . ILE D 2 211 ? 149.421 105.488 126.559 1.00 26.80 ?  190 ILE D N     1 
ATOM   14904 C  CA    . ILE D 2 211 ? 148.479 104.444 126.951 1.00 26.92 ?  190 ILE D CA    1 
ATOM   14905 C  C     . ILE D 2 211 ? 148.324 104.382 128.464 1.00 26.45 ?  190 ILE D C     1 
ATOM   14906 O  O     . ILE D 2 211 ? 147.201 104.354 128.964 1.00 26.65 ?  190 ILE D O     1 
ATOM   14907 C  CB    . ILE D 2 211 ? 148.866 103.059 126.370 1.00 27.00 ?  190 ILE D CB    1 
ATOM   14908 C  CG1   . ILE D 2 211 ? 148.643 103.059 124.852 1.00 28.77 ?  190 ILE D CG1   1 
ATOM   14909 C  CG2   . ILE D 2 211 ? 148.042 101.941 127.029 1.00 26.82 ?  190 ILE D CG2   1 
ATOM   14910 C  CD1   . ILE D 2 211 ? 149.129 101.809 124.131 1.00 30.88 ?  190 ILE D CD1   1 
ATOM   14911 N  N     . ILE D 2 212 ? 149.442 104.392 129.197 1.00 26.49 ?  191 ILE D N     1 
ATOM   14912 C  CA    . ILE D 2 212 ? 149.388 104.289 130.655 1.00 25.73 ?  191 ILE D CA    1 
ATOM   14913 C  C     . ILE D 2 212 ? 148.651 105.487 131.258 1.00 25.48 ?  191 ILE D C     1 
ATOM   14914 O  O     . ILE D 2 212 ? 147.871 105.336 132.202 1.00 24.95 ?  191 ILE D O     1 
ATOM   14915 C  CB    . ILE D 2 212 ? 150.800 104.117 131.292 1.00 26.44 ?  191 ILE D CB    1 
ATOM   14916 C  CG1   . ILE D 2 212 ? 151.426 102.780 130.875 1.00 26.71 ?  191 ILE D CG1   1 
ATOM   14917 C  CG2   . ILE D 2 212 ? 150.738 104.242 132.830 1.00 26.01 ?  191 ILE D CG2   1 
ATOM   14918 C  CD1   . ILE D 2 212 ? 150.682 101.533 131.316 1.00 30.50 ?  191 ILE D CD1   1 
ATOM   14919 N  N     . ASN D 2 213 ? 148.884 106.666 130.690 1.00 24.79 ?  192 ASN D N     1 
ATOM   14920 C  CA    . ASN D 2 213 ? 148.213 107.875 131.147 1.00 24.80 ?  192 ASN D CA    1 
ATOM   14921 C  C     . ASN D 2 213 ? 146.683 107.808 130.965 1.00 24.44 ?  192 ASN D C     1 
ATOM   14922 O  O     . ASN D 2 213 ? 145.926 108.334 131.789 1.00 23.25 ?  192 ASN D O     1 
ATOM   14923 C  CB    . ASN D 2 213 ? 148.803 109.101 130.448 1.00 25.68 ?  192 ASN D CB    1 
ATOM   14924 C  CG    . ASN D 2 213 ? 148.897 110.307 131.363 1.00 27.89 ?  192 ASN D CG    1 
ATOM   14925 O  OD1   . ASN D 2 213 ? 149.070 110.179 132.572 1.00 31.05 ?  192 ASN D OD1   1 
ATOM   14926 N  ND2   . ASN D 2 213 ? 148.791 111.494 130.781 1.00 31.70 ?  192 ASN D ND2   1 
ATOM   14927 N  N     . LEU D 2 214 ? 146.236 107.148 129.896 1.00 23.60 ?  193 LEU D N     1 
ATOM   14928 C  CA    . LEU D 2 214 ? 144.802 106.984 129.649 1.00 23.84 ?  193 LEU D CA    1 
ATOM   14929 C  C     . LEU D 2 214 ? 144.209 105.997 130.637 1.00 23.48 ?  193 LEU D C     1 
ATOM   14930 O  O     . LEU D 2 214 ? 143.115 106.219 131.163 1.00 24.12 ?  193 LEU D O     1 
ATOM   14931 C  CB    . LEU D 2 214 ? 144.549 106.516 128.216 1.00 23.71 ?  193 LEU D CB    1 
ATOM   14932 C  CG    . LEU D 2 214 ? 144.755 107.579 127.128 1.00 25.29 ?  193 LEU D CG    1 
ATOM   14933 C  CD1   . LEU D 2 214 ? 144.619 106.955 125.738 1.00 25.41 ?  193 LEU D CD1   1 
ATOM   14934 C  CD2   . LEU D 2 214 ? 143.784 108.738 127.284 1.00 25.80 ?  193 LEU D CD2   1 
ATOM   14935 N  N     . ILE D 2 215 ? 144.944 104.914 130.892 1.00 22.89 ?  194 ILE D N     1 
ATOM   14936 C  CA    . ILE D 2 215 ? 144.543 103.914 131.870 1.00 22.25 ?  194 ILE D CA    1 
ATOM   14937 C  C     . ILE D 2 215 ? 144.432 104.574 133.241 1.00 22.55 ?  194 ILE D C     1 
ATOM   14938 O  O     . ILE D 2 215 ? 143.410 104.441 133.930 1.00 22.53 ?  194 ILE D O     1 
ATOM   14939 C  CB    . ILE D 2 215 ? 145.543 102.742 131.937 1.00 22.37 ?  194 ILE D CB    1 
ATOM   14940 C  CG1   . ILE D 2 215 ? 145.519 101.946 130.626 1.00 21.89 ?  194 ILE D CG1   1 
ATOM   14941 C  CG2   . ILE D 2 215 ? 145.247 101.847 133.157 1.00 20.25 ?  194 ILE D CG2   1 
ATOM   14942 C  CD1   . ILE D 2 215 ? 146.492 100.762 130.584 1.00 20.48 ?  194 ILE D CD1   1 
ATOM   14943 N  N     . LEU D 2 216 ? 145.480 105.298 133.625 1.00 22.35 ?  195 LEU D N     1 
ATOM   14944 C  CA    . LEU D 2 216 ? 145.532 105.944 134.933 1.00 22.51 ?  195 LEU D CA    1 
ATOM   14945 C  C     . LEU D 2 216 ? 144.355 106.909 135.101 1.00 22.30 ?  195 LEU D C     1 
ATOM   14946 O  O     . LEU D 2 216 ? 143.744 106.960 136.177 1.00 21.62 ?  195 LEU D O     1 
ATOM   14947 C  CB    . LEU D 2 216 ? 146.873 106.678 135.091 1.00 23.06 ?  195 LEU D CB    1 
ATOM   14948 C  CG    . LEU D 2 216 ? 147.220 107.567 136.295 1.00 23.98 ?  195 LEU D CG    1 
ATOM   14949 C  CD1   . LEU D 2 216 ? 148.710 107.788 136.300 1.00 24.44 ?  195 LEU D CD1   1 
ATOM   14950 C  CD2   . LEU D 2 216 ? 146.496 108.922 136.251 1.00 25.00 ?  195 LEU D CD2   1 
ATOM   14951 N  N     . ARG D 2 217 ? 144.050 107.668 134.043 1.00 21.64 ?  196 ARG D N     1 
ATOM   14952 C  CA    . ARG D 2 217 ? 142.915 108.598 134.056 1.00 22.49 ?  196 ARG D CA    1 
ATOM   14953 C  C     . ARG D 2 217 ? 141.574 107.862 134.300 1.00 21.56 ?  196 ARG D C     1 
ATOM   14954 O  O     . ARG D 2 217 ? 140.725 108.364 135.025 1.00 21.32 ?  196 ARG D O     1 
ATOM   14955 C  CB    . ARG D 2 217 ? 142.864 109.464 132.782 1.00 23.07 ?  196 ARG D CB    1 
ATOM   14956 C  CG    . ARG D 2 217 ? 141.796 110.580 132.821 1.00 25.64 ?  196 ARG D CG    1 
ATOM   14957 C  CD    . ARG D 2 217 ? 141.611 111.287 131.466 1.00 32.11 ?  196 ARG D CD    1 
ATOM   14958 N  NE    . ARG D 2 217 ? 141.218 110.356 130.399 1.00 35.06 ?  196 ARG D NE    1 
ATOM   14959 C  CZ    . ARG D 2 217 ? 140.786 110.720 129.196 1.00 37.65 ?  196 ARG D CZ    1 
ATOM   14960 N  NH1   . ARG D 2 217 ? 140.658 112.006 128.888 1.00 40.20 1  196 ARG D NH1   1 
ATOM   14961 N  NH2   . ARG D 2 217 ? 140.466 109.794 128.296 1.00 38.20 ?  196 ARG D NH2   1 
ATOM   14962 N  N     . ASP D 2 218 ? 141.396 106.682 133.704 1.00 21.34 ?  197 ASP D N     1 
ATOM   14963 C  CA    . ASP D 2 218 ? 140.239 105.828 134.015 1.00 21.09 ?  197 ASP D CA    1 
ATOM   14964 C  C     . ASP D 2 218 ? 140.247 105.360 135.484 1.00 20.65 ?  197 ASP D C     1 
ATOM   14965 O  O     . ASP D 2 218 ? 139.220 105.441 136.163 1.00 20.16 ?  197 ASP D O     1 
ATOM   14966 C  CB    . ASP D 2 218 ? 140.173 104.607 133.086 1.00 21.58 ?  197 ASP D CB    1 
ATOM   14967 C  CG    . ASP D 2 218 ? 139.884 104.973 131.630 1.00 22.60 ?  197 ASP D CG    1 
ATOM   14968 O  OD1   . ASP D 2 218 ? 139.309 106.054 131.362 1.00 24.72 ?  197 ASP D OD1   1 
ATOM   14969 O  OD2   . ASP D 2 218 ? 140.252 104.167 130.745 1.00 22.64 -1 197 ASP D OD2   1 
ATOM   14970 N  N     . GLU D 2 219 ? 141.385 104.871 135.981 1.00 20.59 ?  198 GLU D N     1 
ATOM   14971 C  CA    . GLU D 2 219 ? 141.433 104.370 137.372 1.00 20.66 ?  198 GLU D CA    1 
ATOM   14972 C  C     . GLU D 2 219 ? 141.130 105.477 138.385 1.00 20.45 ?  198 GLU D C     1 
ATOM   14973 O  O     . GLU D 2 219 ? 140.485 105.228 139.408 1.00 20.59 ?  198 GLU D O     1 
ATOM   14974 C  CB    . GLU D 2 219 ? 142.770 103.690 137.709 1.00 20.55 ?  198 GLU D CB    1 
ATOM   14975 C  CG    . GLU D 2 219 ? 143.364 102.752 136.612 1.00 21.99 ?  198 GLU D CG    1 
ATOM   14976 C  CD    . GLU D 2 219 ? 142.489 101.553 136.226 1.00 24.00 ?  198 GLU D CD    1 
ATOM   14977 O  OE1   . GLU D 2 219 ? 141.250 101.579 136.392 1.00 25.06 ?  198 GLU D OE1   1 
ATOM   14978 O  OE2   . GLU D 2 219 ? 143.046 100.569 135.713 1.00 24.49 -1 198 GLU D OE2   1 
ATOM   14979 N  N     . ALA D 2 220 ? 141.579 106.694 138.090 1.00 20.47 ?  199 ALA D N     1 
ATOM   14980 C  CA    . ALA D 2 220 ? 141.282 107.863 138.944 1.00 21.10 ?  199 ALA D CA    1 
ATOM   14981 C  C     . ALA D 2 220 ? 139.782 108.077 139.122 1.00 21.34 ?  199 ALA D C     1 
ATOM   14982 O  O     . ALA D 2 220 ? 139.299 108.134 140.251 1.00 21.19 ?  199 ALA D O     1 
ATOM   14983 C  CB    . ALA D 2 220 ? 141.958 109.129 138.411 1.00 21.09 ?  199 ALA D CB    1 
ATOM   14984 N  N     . ILE D 2 221 ? 139.045 108.165 138.011 1.00 21.31 ?  200 ILE D N     1 
ATOM   14985 C  CA    . ILE D 2 221 ? 137.591 108.284 138.089 1.00 21.80 ?  200 ILE D CA    1 
ATOM   14986 C  C     . ILE D 2 221 ? 136.903 107.045 138.703 1.00 20.90 ?  200 ILE D C     1 
ATOM   14987 O  O     . ILE D 2 221 ? 135.927 107.189 139.439 1.00 20.54 ?  200 ILE D O     1 
ATOM   14988 C  CB    . ILE D 2 221 ? 136.941 108.729 136.748 1.00 22.75 ?  200 ILE D CB    1 
ATOM   14989 C  CG1   . ILE D 2 221 ? 135.525 109.230 137.005 1.00 24.63 ?  200 ILE D CG1   1 
ATOM   14990 C  CG2   . ILE D 2 221 ? 136.906 107.591 135.730 1.00 23.38 ?  200 ILE D CG2   1 
ATOM   14991 C  CD1   . ILE D 2 221 ? 134.995 110.139 135.935 1.00 26.91 ?  200 ILE D CD1   1 
ATOM   14992 N  N     . HIS D 2 222 ? 137.428 105.843 138.441 1.00 20.31 ?  201 HIS D N     1 
ATOM   14993 C  CA    . HIS D 2 222 ? 136.893 104.640 139.087 1.00 20.25 ?  201 HIS D CA    1 
ATOM   14994 C  C     . HIS D 2 222 ? 136.996 104.764 140.606 1.00 20.51 ?  201 HIS D C     1 
ATOM   14995 O  O     . HIS D 2 222 ? 136.014 104.546 141.325 1.00 20.99 ?  201 HIS D O     1 
ATOM   14996 C  CB    . HIS D 2 222 ? 137.606 103.365 138.623 1.00 19.79 ?  201 HIS D CB    1 
ATOM   14997 C  CG    . HIS D 2 222 ? 137.471 103.071 137.160 1.00 19.25 ?  201 HIS D CG    1 
ATOM   14998 N  ND1   . HIS D 2 222 ? 138.177 102.057 136.549 1.00 18.35 ?  201 HIS D ND1   1 
ATOM   14999 C  CD2   . HIS D 2 222 ? 136.731 103.657 136.185 1.00 17.64 ?  201 HIS D CD2   1 
ATOM   15000 C  CE1   . HIS D 2 222 ? 137.869 102.017 135.264 1.00 18.28 ?  201 HIS D CE1   1 
ATOM   15001 N  NE2   . HIS D 2 222 ? 137.001 102.983 135.016 1.00 20.01 ?  201 HIS D NE2   1 
ATOM   15002 N  N     . GLY D 2 223 ? 138.183 105.140 141.086 1.00 20.33 ?  202 GLY D N     1 
ATOM   15003 C  CA    . GLY D 2 223 ? 138.422 105.346 142.520 1.00 19.94 ?  202 GLY D CA    1 
ATOM   15004 C  C     . GLY D 2 223 ? 137.508 106.391 143.149 1.00 19.80 ?  202 GLY D C     1 
ATOM   15005 O  O     . GLY D 2 223 ? 136.955 106.162 144.224 1.00 19.96 ?  202 GLY D O     1 
ATOM   15006 N  N     . VAL D 2 224 ? 137.319 107.525 142.472 1.00 19.49 ?  203 VAL D N     1 
ATOM   15007 C  CA    . VAL D 2 224 ? 136.424 108.580 142.975 1.00 18.88 ?  203 VAL D CA    1 
ATOM   15008 C  C     . VAL D 2 224 ? 134.970 108.097 143.070 1.00 18.55 ?  203 VAL D C     1 
ATOM   15009 O  O     . VAL D 2 224 ? 134.284 108.333 144.077 1.00 17.65 ?  203 VAL D O     1 
ATOM   15010 C  CB    . VAL D 2 224 ? 136.513 109.897 142.118 1.00 19.22 ?  203 VAL D CB    1 
ATOM   15011 C  CG1   . VAL D 2 224 ? 135.542 110.969 142.654 1.00 18.51 ?  203 VAL D CG1   1 
ATOM   15012 C  CG2   . VAL D 2 224 ? 137.955 110.446 142.109 1.00 19.69 ?  203 VAL D CG2   1 
ATOM   15013 N  N     . TYR D 2 225 ? 134.515 107.399 142.031 1.00 18.17 ?  204 TYR D N     1 
ATOM   15014 C  CA    . TYR D 2 225 ? 133.138 106.904 141.967 1.00 18.76 ?  204 TYR D CA    1 
ATOM   15015 C  C     . TYR D 2 225 ? 132.852 105.854 143.055 1.00 18.93 ?  204 TYR D C     1 
ATOM   15016 O  O     . TYR D 2 225 ? 131.889 105.981 143.823 1.00 18.77 ?  204 TYR D O     1 
ATOM   15017 C  CB    . TYR D 2 225 ? 132.813 106.340 140.569 1.00 18.96 ?  204 TYR D CB    1 
ATOM   15018 C  CG    . TYR D 2 225 ? 131.346 105.946 140.443 1.00 20.06 ?  204 TYR D CG    1 
ATOM   15019 C  CD1   . TYR D 2 225 ? 130.341 106.922 140.483 1.00 21.79 ?  204 TYR D CD1   1 
ATOM   15020 C  CD2   . TYR D 2 225 ? 130.963 104.607 140.320 1.00 19.51 ?  204 TYR D CD2   1 
ATOM   15021 C  CE1   . TYR D 2 225 ? 128.992 106.573 140.398 1.00 20.38 ?  204 TYR D CE1   1 
ATOM   15022 C  CE2   . TYR D 2 225 ? 129.600 104.246 140.227 1.00 19.38 ?  204 TYR D CE2   1 
ATOM   15023 C  CZ    . TYR D 2 225 ? 128.629 105.243 140.272 1.00 20.84 ?  204 TYR D CZ    1 
ATOM   15024 O  OH    . TYR D 2 225 ? 127.290 104.928 140.199 1.00 20.77 ?  204 TYR D OH    1 
ATOM   15025 N  N     . VAL D 2 226 ? 133.693 104.824 143.126 1.00 18.76 ?  205 VAL D N     1 
ATOM   15026 C  CA    . VAL D 2 226 ? 133.525 103.797 144.151 1.00 18.85 ?  205 VAL D CA    1 
ATOM   15027 C  C     . VAL D 2 226 ? 133.625 104.426 145.540 1.00 19.19 ?  205 VAL D C     1 
ATOM   15028 O  O     . VAL D 2 226 ? 132.899 104.025 146.452 1.00 19.87 ?  205 VAL D O     1 
ATOM   15029 C  CB    . VAL D 2 226 ? 134.519 102.643 143.976 1.00 19.28 ?  205 VAL D CB    1 
ATOM   15030 C  CG1   . VAL D 2 226 ? 134.364 101.599 145.115 1.00 18.22 ?  205 VAL D CG1   1 
ATOM   15031 C  CG2   . VAL D 2 226 ? 134.297 101.995 142.599 1.00 18.40 ?  205 VAL D CG2   1 
ATOM   15032 N  N     . GLY D 2 227 ? 134.499 105.425 145.681 1.00 18.53 ?  206 GLY D N     1 
ATOM   15033 C  CA    . GLY D 2 227 ? 134.607 106.201 146.931 1.00 18.74 ?  206 GLY D CA    1 
ATOM   15034 C  C     . GLY D 2 227 ? 133.308 106.852 147.374 1.00 19.17 ?  206 GLY D C     1 
ATOM   15035 O  O     . GLY D 2 227 ? 132.977 106.862 148.568 1.00 18.66 ?  206 GLY D O     1 
ATOM   15036 N  N     . LEU D 2 228 ? 132.575 107.417 146.416 1.00 19.00 ?  207 LEU D N     1 
ATOM   15037 C  CA    . LEU D 2 228 ? 131.284 108.038 146.721 1.00 19.73 ?  207 LEU D CA    1 
ATOM   15038 C  C     . LEU D 2 228 ? 130.253 106.986 147.151 1.00 19.76 ?  207 LEU D C     1 
ATOM   15039 O  O     . LEU D 2 228 ? 129.485 107.217 148.084 1.00 20.07 ?  207 LEU D O     1 
ATOM   15040 C  CB    . LEU D 2 228 ? 130.786 108.870 145.537 1.00 19.36 ?  207 LEU D CB    1 
ATOM   15041 C  CG    . LEU D 2 228 ? 131.588 110.149 145.247 1.00 20.50 ?  207 LEU D CG    1 
ATOM   15042 C  CD1   . LEU D 2 228 ? 131.181 110.743 143.911 1.00 19.87 ?  207 LEU D CD1   1 
ATOM   15043 C  CD2   . LEU D 2 228 ? 131.422 111.198 146.384 1.00 22.38 ?  207 LEU D CD2   1 
ATOM   15044 N  N     . LEU D 2 229 ? 130.268 105.821 146.504 1.00 19.27 ?  208 LEU D N     1 
ATOM   15045 C  CA    . LEU D 2 229 ? 129.399 104.702 146.916 1.00 19.47 ?  208 LEU D CA    1 
ATOM   15046 C  C     . LEU D 2 229 ? 129.715 104.192 148.327 1.00 19.67 ?  208 LEU D C     1 
ATOM   15047 O  O     . LEU D 2 229 ? 128.805 103.812 149.075 1.00 19.82 ?  208 LEU D O     1 
ATOM   15048 C  CB    . LEU D 2 229 ? 129.471 103.538 145.906 1.00 19.51 ?  208 LEU D CB    1 
ATOM   15049 C  CG    . LEU D 2 229 ? 129.044 103.772 144.447 1.00 19.48 ?  208 LEU D CG    1 
ATOM   15050 C  CD1   . LEU D 2 229 ? 129.349 102.526 143.597 1.00 20.14 ?  208 LEU D CD1   1 
ATOM   15051 C  CD2   . LEU D 2 229 ? 127.563 104.188 144.308 1.00 19.95 ?  208 LEU D CD2   1 
ATOM   15052 N  N     . ALA D 2 230 ? 130.998 104.172 148.689 1.00 19.43 ?  209 ALA D N     1 
ATOM   15053 C  CA    . ALA D 2 230 ? 131.416 103.799 150.047 1.00 20.29 ?  209 ALA D CA    1 
ATOM   15054 C  C     . ALA D 2 230 ? 130.971 104.826 151.090 1.00 21.17 ?  209 ALA D C     1 
ATOM   15055 O  O     . ALA D 2 230 ? 130.488 104.456 152.155 1.00 21.73 ?  209 ALA D O     1 
ATOM   15056 C  CB    . ALA D 2 230 ? 132.928 103.594 150.107 1.00 19.99 ?  209 ALA D CB    1 
ATOM   15057 N  N     . GLN D 2 231 ? 131.127 106.113 150.780 1.00 22.26 ?  210 GLN D N     1 
ATOM   15058 C  CA    . GLN D 2 231 ? 130.678 107.191 151.682 1.00 23.33 ?  210 GLN D CA    1 
ATOM   15059 C  C     . GLN D 2 231 ? 129.168 107.138 151.935 1.00 23.85 ?  210 GLN D C     1 
ATOM   15060 O  O     . GLN D 2 231 ? 128.715 107.409 153.043 1.00 24.91 ?  210 GLN D O     1 
ATOM   15061 C  CB    . GLN D 2 231 ? 131.051 108.570 151.129 1.00 23.49 ?  210 GLN D CB    1 
ATOM   15062 C  CG    . GLN D 2 231 ? 132.553 108.865 151.058 1.00 23.05 ?  210 GLN D CG    1 
ATOM   15063 C  CD    . GLN D 2 231 ? 132.835 110.247 150.472 1.00 24.65 ?  210 GLN D CD    1 
ATOM   15064 O  OE1   . GLN D 2 231 ? 132.268 111.242 150.924 1.00 25.85 ?  210 GLN D OE1   1 
ATOM   15065 N  NE2   . GLN D 2 231 ? 133.696 110.311 149.456 1.00 22.30 ?  210 GLN D NE2   1 
ATOM   15066 N  N     . GLU D 2 232 ? 128.397 106.808 150.903 1.00 24.36 ?  211 GLU D N     1 
ATOM   15067 C  CA    . GLU D 2 232 ? 126.958 106.600 151.051 1.00 24.83 ?  211 GLU D CA    1 
ATOM   15068 C  C     . GLU D 2 232 ? 126.638 105.547 152.118 1.00 24.34 ?  211 GLU D C     1 
ATOM   15069 O  O     . GLU D 2 232 ? 125.765 105.767 152.959 1.00 24.20 ?  211 GLU D O     1 
ATOM   15070 C  CB    . GLU D 2 232 ? 126.333 106.198 149.720 1.00 25.15 ?  211 GLU D CB    1 
ATOM   15071 C  CG    . GLU D 2 232 ? 124.827 106.219 149.720 1.00 28.55 ?  211 GLU D CG    1 
ATOM   15072 C  CD    . GLU D 2 232 ? 124.274 105.838 148.374 1.00 33.83 ?  211 GLU D CD    1 
ATOM   15073 O  OE1   . GLU D 2 232 ? 124.039 106.755 147.560 1.00 35.09 ?  211 GLU D OE1   1 
ATOM   15074 O  OE2   . GLU D 2 232 ? 124.117 104.625 148.114 1.00 35.51 -1 211 GLU D OE2   1 
ATOM   15075 N  N     . ILE D 2 233 ? 127.343 104.417 152.090 1.00 23.39 ?  212 ILE D N     1 
ATOM   15076 C  CA    . ILE D 2 233 ? 127.167 103.377 153.117 1.00 23.42 ?  212 ILE D CA    1 
ATOM   15077 C  C     . ILE D 2 233 ? 127.633 103.876 154.486 1.00 23.74 ?  212 ILE D C     1 
ATOM   15078 O  O     . ILE D 2 233 ? 126.915 103.754 155.477 1.00 24.61 ?  212 ILE D O     1 
ATOM   15079 C  CB    . ILE D 2 233 ? 127.874 102.047 152.742 1.00 22.81 ?  212 ILE D CB    1 
ATOM   15080 C  CG1   . ILE D 2 233 ? 127.214 101.419 151.506 1.00 22.94 ?  212 ILE D CG1   1 
ATOM   15081 C  CG2   . ILE D 2 233 ? 127.833 101.053 153.911 1.00 22.45 ?  212 ILE D CG2   1 
ATOM   15082 C  CD1   . ILE D 2 233 ? 128.048 100.298 150.848 1.00 22.21 ?  212 ILE D CD1   1 
ATOM   15083 N  N     . TYR D 2 234 ? 128.829 104.456 154.529 1.00 24.19 ?  213 TYR D N     1 
ATOM   15084 C  CA    . TYR D 2 234 ? 129.409 104.991 155.752 1.00 24.59 ?  213 TYR D CA    1 
ATOM   15085 C  C     . TYR D 2 234 ? 128.453 105.959 156.458 1.00 25.15 ?  213 TYR D C     1 
ATOM   15086 O  O     . TYR D 2 234 ? 128.306 105.902 157.682 1.00 24.94 ?  213 TYR D O     1 
ATOM   15087 C  CB    . TYR D 2 234 ? 130.728 105.699 155.431 1.00 24.41 ?  213 TYR D CB    1 
ATOM   15088 C  CG    . TYR D 2 234 ? 131.433 106.320 156.619 1.00 25.93 ?  213 TYR D CG    1 
ATOM   15089 C  CD1   . TYR D 2 234 ? 132.287 105.564 157.415 1.00 24.70 ?  213 TYR D CD1   1 
ATOM   15090 C  CD2   . TYR D 2 234 ? 131.251 107.672 156.938 1.00 26.11 ?  213 TYR D CD2   1 
ATOM   15091 C  CE1   . TYR D 2 234 ? 132.944 106.130 158.504 1.00 27.90 ?  213 TYR D CE1   1 
ATOM   15092 C  CE2   . TYR D 2 234 ? 131.907 108.245 158.020 1.00 27.70 ?  213 TYR D CE2   1 
ATOM   15093 C  CZ    . TYR D 2 234 ? 132.752 107.472 158.795 1.00 27.89 ?  213 TYR D CZ    1 
ATOM   15094 O  OH    . TYR D 2 234 ? 133.402 108.033 159.870 1.00 32.34 ?  213 TYR D OH    1 
ATOM   15095 N  N     . ASN D 2 235 ? 127.819 106.838 155.680 1.00 25.43 ?  214 ASN D N     1 
ATOM   15096 C  CA    . ASN D 2 235 ? 126.918 107.868 156.223 1.00 26.77 ?  214 ASN D CA    1 
ATOM   15097 C  C     . ASN D 2 235 ? 125.593 107.323 156.756 1.00 27.06 ?  214 ASN D C     1 
ATOM   15098 O  O     . ASN D 2 235 ? 124.855 108.031 157.433 1.00 27.42 ?  214 ASN D O     1 
ATOM   15099 C  CB    . ASN D 2 235 ? 126.624 108.951 155.183 1.00 26.80 ?  214 ASN D CB    1 
ATOM   15100 C  CG    . ASN D 2 235 ? 127.853 109.719 154.775 1.00 28.19 ?  214 ASN D CG    1 
ATOM   15101 O  OD1   . ASN D 2 235 ? 128.755 109.954 155.576 1.00 29.35 ?  214 ASN D OD1   1 
ATOM   15102 N  ND2   . ASN D 2 235 ? 127.891 110.128 153.518 1.00 30.84 ?  214 ASN D ND2   1 
ATOM   15103 N  N     . LYS D 2 236 ? 125.298 106.071 156.442 1.00 26.87 ?  215 LYS D N     1 
ATOM   15104 C  CA    . LYS D 2 236 ? 124.090 105.428 156.944 1.00 27.86 ?  215 LYS D CA    1 
ATOM   15105 C  C     . LYS D 2 236 ? 124.330 104.760 158.305 1.00 28.07 ?  215 LYS D C     1 
ATOM   15106 O  O     . LYS D 2 236 ? 123.406 104.211 158.903 1.00 28.22 ?  215 LYS D O     1 
ATOM   15107 C  CB    . LYS D 2 236 ? 123.566 104.409 155.932 1.00 27.52 ?  215 LYS D CB    1 
ATOM   15108 C  CG    . LYS D 2 236 ? 123.106 105.012 154.627 1.00 29.60 ?  215 LYS D CG    1 
ATOM   15109 C  CD    . LYS D 2 236 ? 122.071 104.139 153.936 1.00 34.24 ?  215 LYS D CD    1 
ATOM   15110 C  CE    . LYS D 2 236 ? 122.651 103.277 152.831 1.00 36.75 ?  215 LYS D CE    1 
ATOM   15111 N  NZ    . LYS D 2 236 ? 123.592 102.266 153.360 1.00 40.41 1  215 LYS D NZ    1 
ATOM   15112 N  N     . GLN D 2 237 ? 125.568 104.820 158.791 1.00 28.33 ?  216 GLN D N     1 
ATOM   15113 C  CA    . GLN D 2 237 ? 125.951 104.102 160.009 1.00 29.60 ?  216 GLN D CA    1 
ATOM   15114 C  C     . GLN D 2 237 ? 125.880 104.977 161.256 1.00 30.69 ?  216 GLN D C     1 
ATOM   15115 O  O     . GLN D 2 237 ? 125.923 106.208 161.164 1.00 30.85 ?  216 GLN D O     1 
ATOM   15116 C  CB    . GLN D 2 237 ? 127.370 103.509 159.881 1.00 29.08 ?  216 GLN D CB    1 
ATOM   15117 C  CG    . GLN D 2 237 ? 127.618 102.645 158.641 1.00 27.78 ?  216 GLN D CG    1 
ATOM   15118 C  CD    . GLN D 2 237 ? 126.554 101.580 158.424 1.00 28.38 ?  216 GLN D CD    1 
ATOM   15119 O  OE1   . GLN D 2 237 ? 126.227 100.818 159.332 1.00 29.30 ?  216 GLN D OE1   1 
ATOM   15120 N  NE2   . GLN D 2 237 ? 126.019 101.516 157.209 1.00 26.88 ?  216 GLN D NE2   1 
ATOM   15121 N  N     . THR D 2 238 ? 125.785 104.328 162.415 1.00 32.02 ?  217 THR D N     1 
ATOM   15122 C  CA    . THR D 2 238 ? 125.876 105.014 163.708 1.00 33.47 ?  217 THR D CA    1 
ATOM   15123 C  C     . THR D 2 238 ? 127.275 105.601 163.923 1.00 34.29 ?  217 THR D C     1 
ATOM   15124 O  O     . THR D 2 238 ? 128.216 105.306 163.168 1.00 33.78 ?  217 THR D O     1 
ATOM   15125 C  CB    . THR D 2 238 ? 125.545 104.054 164.885 1.00 34.00 ?  217 THR D CB    1 
ATOM   15126 O  OG1   . THR D 2 238 ? 126.547 103.030 164.971 1.00 34.33 ?  217 THR D OG1   1 
ATOM   15127 C  CG2   . THR D 2 238 ? 124.164 103.405 164.695 1.00 33.53 ?  217 THR D CG2   1 
ATOM   15128 N  N     . GLU D 2 239 ? 127.422 106.420 164.960 1.00 35.45 ?  218 GLU D N     1 
ATOM   15129 C  CA    . GLU D 2 239 ? 128.718 107.017 165.266 1.00 36.37 ?  218 GLU D CA    1 
ATOM   15130 C  C     . GLU D 2 239 ? 129.754 105.981 165.696 1.00 36.29 ?  218 GLU D C     1 
ATOM   15131 O  O     . GLU D 2 239 ? 130.920 106.069 165.300 1.00 36.18 ?  218 GLU D O     1 
ATOM   15132 C  CB    . GLU D 2 239 ? 128.585 108.139 166.299 1.00 37.27 ?  218 GLU D CB    1 
ATOM   15133 C  CG    . GLU D 2 239 ? 127.869 109.390 165.757 1.00 39.45 ?  218 GLU D CG    1 
ATOM   15134 C  CD    . GLU D 2 239 ? 128.530 109.970 164.508 1.00 41.22 ?  218 GLU D CD    1 
ATOM   15135 O  OE1   . GLU D 2 239 ? 129.771 110.118 164.488 1.00 42.62 ?  218 GLU D OE1   1 
ATOM   15136 O  OE2   . GLU D 2 239 ? 127.803 110.280 163.539 1.00 41.24 -1 218 GLU D OE2   1 
ATOM   15137 N  N     . GLU D 2 240 ? 129.328 104.995 166.483 1.00 36.66 ?  219 GLU D N     1 
ATOM   15138 C  CA    . GLU D 2 240 ? 130.228 103.923 166.916 1.00 37.01 ?  219 GLU D CA    1 
ATOM   15139 C  C     . GLU D 2 240 ? 130.658 103.057 165.732 1.00 35.85 ?  219 GLU D C     1 
ATOM   15140 O  O     . GLU D 2 240 ? 131.830 102.685 165.629 1.00 35.62 ?  219 GLU D O     1 
ATOM   15141 C  CB    . GLU D 2 240 ? 129.590 103.054 168.011 1.00 37.98 ?  219 GLU D CB    1 
ATOM   15142 C  CG    . GLU D 2 240 ? 130.545 101.984 168.563 1.00 40.87 ?  219 GLU D CG    1 
ATOM   15143 C  CD    . GLU D 2 240 ? 129.937 101.094 169.645 1.00 44.58 ?  219 GLU D CD    1 
ATOM   15144 O  OE1   . GLU D 2 240 ? 130.719 100.567 170.473 1.00 45.86 ?  219 GLU D OE1   1 
ATOM   15145 O  OE2   . GLU D 2 240 ? 128.694 100.915 169.670 1.00 45.75 -1 219 GLU D OE2   1 
ATOM   15146 N  N     . LYS D 2 241 ? 129.704 102.742 164.855 1.00 34.54 ?  220 LYS D N     1 
ATOM   15147 C  CA    . LYS D 2 241 ? 129.977 101.947 163.657 1.00 33.65 ?  220 LYS D CA    1 
ATOM   15148 C  C     . LYS D 2 241 ? 130.897 102.704 162.691 1.00 32.67 ?  220 LYS D C     1 
ATOM   15149 O  O     . LYS D 2 241 ? 131.774 102.099 162.081 1.00 32.05 ?  220 LYS D O     1 
ATOM   15150 C  CB    . LYS D 2 241 ? 128.675 101.526 162.967 1.00 33.30 ?  220 LYS D CB    1 
ATOM   15151 C  CG    . LYS D 2 241 ? 128.835 100.553 161.783 1.00 34.50 ?  220 LYS D CG    1 
ATOM   15152 C  CD    . LYS D 2 241 ? 129.484 99.222  162.183 1.00 36.30 ?  220 LYS D CD    1 
ATOM   15153 C  CE    . LYS D 2 241 ? 128.549 98.367  163.030 1.00 38.44 ?  220 LYS D CE    1 
ATOM   15154 N  NZ    . LYS D 2 241 ? 129.311 97.389  163.853 1.00 39.28 1  220 LYS D NZ    1 
ATOM   15155 N  N     . LYS D 2 242 ? 130.691 104.019 162.566 1.00 31.90 ?  221 LYS D N     1 
ATOM   15156 C  CA    . LYS D 2 242 ? 131.566 104.872 161.761 1.00 31.28 ?  221 LYS D CA    1 
ATOM   15157 C  C     . LYS D 2 242 ? 133.011 104.819 162.257 1.00 31.32 ?  221 LYS D C     1 
ATOM   15158 O  O     . LYS D 2 242 ? 133.921 104.602 161.466 1.00 30.72 ?  221 LYS D O     1 
ATOM   15159 C  CB    . LYS D 2 242 ? 131.077 106.328 161.746 1.00 31.38 ?  221 LYS D CB    1 
ATOM   15160 C  CG    . LYS D 2 242 ? 129.963 106.616 160.745 1.00 30.64 ?  221 LYS D CG    1 
ATOM   15161 C  CD    . LYS D 2 242 ? 129.561 108.089 160.809 1.00 32.51 ?  221 LYS D CD    1 
ATOM   15162 C  CE    . LYS D 2 242 ? 128.478 108.403 159.801 1.00 32.66 ?  221 LYS D CE    1 
ATOM   15163 N  NZ    . LYS D 2 242 ? 127.925 109.757 160.026 1.00 35.31 1  221 LYS D NZ    1 
ATOM   15164 N  N     . ALA D 2 243 ? 133.209 105.023 163.563 1.00 31.62 ?  222 ALA D N     1 
ATOM   15165 C  CA    . ALA D 2 243 ? 134.541 104.955 164.174 1.00 31.66 ?  222 ALA D CA    1 
ATOM   15166 C  C     . ALA D 2 243 ? 135.223 103.605 163.915 1.00 31.52 ?  222 ALA D C     1 
ATOM   15167 O  O     . ALA D 2 243 ? 136.439 103.537 163.715 1.00 31.41 ?  222 ALA D O     1 
ATOM   15168 C  CB    . ALA D 2 243 ? 134.457 105.246 165.677 1.00 31.89 ?  222 ALA D CB    1 
ATOM   15169 N  N     . GLU D 2 244 ? 134.416 102.548 163.902 1.00 31.35 ?  223 GLU D N     1 
ATOM   15170 C  CA    . GLU D 2 244 ? 134.867 101.189 163.653 1.00 31.54 ?  223 GLU D CA    1 
ATOM   15171 C  C     . GLU D 2 244 ? 135.278 100.984 162.177 1.00 30.63 ?  223 GLU D C     1 
ATOM   15172 O  O     . GLU D 2 244 ? 136.278 100.315 161.878 1.00 29.47 ?  223 GLU D O     1 
ATOM   15173 C  CB    . GLU D 2 244 ? 133.734 100.252 164.041 1.00 32.45 ?  223 GLU D CB    1 
ATOM   15174 C  CG    . GLU D 2 244 ? 134.068 98.797  164.160 1.00 35.31 ?  223 GLU D CG    1 
ATOM   15175 C  CD    . GLU D 2 244 ? 132.954 98.040  164.855 1.00 38.36 ?  223 GLU D CD    1 
ATOM   15176 O  OE1   . GLU D 2 244 ? 132.749 98.260  166.067 1.00 41.93 ?  223 GLU D OE1   1 
ATOM   15177 O  OE2   . GLU D 2 244 ? 132.273 97.232  164.192 1.00 39.37 -1 223 GLU D OE2   1 
ATOM   15178 N  N     . LEU D 2 245 ? 134.503 101.569 161.270 1.00 29.62 ?  224 LEU D N     1 
ATOM   15179 C  CA    . LEU D 2 245 ? 134.826 101.554 159.845 1.00 29.44 ?  224 LEU D CA    1 
ATOM   15180 C  C     . LEU D 2 245 ? 136.057 102.401 159.517 1.00 28.99 ?  224 LEU D C     1 
ATOM   15181 O  O     . LEU D 2 245 ? 136.830 102.038 158.635 1.00 28.63 ?  224 LEU D O     1 
ATOM   15182 C  CB    . LEU D 2 245 ? 133.620 102.001 159.013 1.00 29.06 ?  224 LEU D CB    1 
ATOM   15183 C  CG    . LEU D 2 245 ? 132.411 101.059 159.000 1.00 29.27 ?  224 LEU D CG    1 
ATOM   15184 C  CD1   . LEU D 2 245 ? 131.331 101.632 158.086 1.00 30.76 ?  224 LEU D CD1   1 
ATOM   15185 C  CD2   . LEU D 2 245 ? 132.787 99.652  158.549 1.00 28.11 ?  224 LEU D CD2   1 
ATOM   15186 N  N     . ARG D 2 246 ? 136.232 103.519 160.223 1.00 29.31 ?  225 ARG D N     1 
ATOM   15187 C  CA    . ARG D 2 246 ? 137.441 104.339 160.083 1.00 29.86 ?  225 ARG D CA    1 
ATOM   15188 C  C     . ARG D 2 246 ? 138.679 103.567 160.518 1.00 29.23 ?  225 ARG D C     1 
ATOM   15189 O  O     . ARG D 2 246 ? 139.700 103.604 159.846 1.00 28.95 ?  225 ARG D O     1 
ATOM   15190 C  CB    . ARG D 2 246 ? 137.360 105.633 160.901 1.00 30.56 ?  225 ARG D CB    1 
ATOM   15191 C  CG    . ARG D 2 246 ? 136.489 106.709 160.297 1.00 33.71 ?  225 ARG D CG    1 
ATOM   15192 C  CD    . ARG D 2 246 ? 136.849 108.115 160.816 1.00 37.42 ?  225 ARG D CD    1 
ATOM   15193 N  NE    . ARG D 2 246 ? 136.809 108.228 162.279 1.00 39.17 ?  225 ARG D NE    1 
ATOM   15194 C  CZ    . ARG D 2 246 ? 135.703 108.360 163.012 1.00 40.68 ?  225 ARG D CZ    1 
ATOM   15195 N  NH1   . ARG D 2 246 ? 134.500 108.386 162.443 1.00 40.28 1  225 ARG D NH1   1 
ATOM   15196 N  NH2   . ARG D 2 246 ? 135.801 108.456 164.334 1.00 41.65 ?  225 ARG D NH2   1 
ATOM   15197 N  N     . GLU D 2 247 ? 138.581 102.887 161.654 1.00 28.89 ?  226 GLU D N     1 
ATOM   15198 C  CA    . GLU D 2 247 ? 139.679 102.060 162.146 1.00 29.27 ?  226 GLU D CA    1 
ATOM   15199 C  C     . GLU D 2 247 ? 140.019 100.959 161.142 1.00 27.84 ?  226 GLU D C     1 
ATOM   15200 O  O     . GLU D 2 247 ? 141.199 100.713 160.883 1.00 27.37 ?  226 GLU D O     1 
ATOM   15201 C  CB    . GLU D 2 247 ? 139.363 101.474 163.532 1.00 30.21 ?  226 GLU D CB    1 
ATOM   15202 C  CG    . GLU D 2 247 ? 140.418 100.491 164.077 1.00 34.46 ?  226 GLU D CG    1 
ATOM   15203 C  CD    . GLU D 2 247 ? 141.804 101.116 164.214 1.00 40.77 ?  226 GLU D CD    1 
ATOM   15204 O  OE1   . GLU D 2 247 ? 141.950 102.071 165.013 1.00 44.03 ?  226 GLU D OE1   1 
ATOM   15205 O  OE2   . GLU D 2 247 ? 142.750 100.658 163.523 1.00 42.98 -1 226 GLU D OE2   1 
ATOM   15206 N  N     . PHE D 2 248 ? 138.993 100.316 160.577 1.00 26.73 ?  227 PHE D N     1 
ATOM   15207 C  CA    . PHE D 2 248 ? 139.190 99.319  159.517 1.00 26.15 ?  227 PHE D CA    1 
ATOM   15208 C  C     . PHE D 2 248 ? 139.987 99.894  158.343 1.00 25.33 ?  227 PHE D C     1 
ATOM   15209 O  O     . PHE D 2 248 ? 140.952 99.280  157.894 1.00 24.70 ?  227 PHE D O     1 
ATOM   15210 C  CB    . PHE D 2 248 ? 137.868 98.733  158.984 1.00 26.02 ?  227 PHE D CB    1 
ATOM   15211 C  CG    . PHE D 2 248 ? 138.024 97.999  157.652 1.00 25.61 ?  227 PHE D CG    1 
ATOM   15212 C  CD1   . PHE D 2 248 ? 138.398 96.660  157.618 1.00 26.51 ?  227 PHE D CD1   1 
ATOM   15213 C  CD2   . PHE D 2 248 ? 137.835 98.669  156.440 1.00 26.21 ?  227 PHE D CD2   1 
ATOM   15214 C  CE1   . PHE D 2 248 ? 138.569 95.987  156.408 1.00 26.16 ?  227 PHE D CE1   1 
ATOM   15215 C  CE2   . PHE D 2 248 ? 138.005 98.007  155.216 1.00 26.07 ?  227 PHE D CE2   1 
ATOM   15216 C  CZ    . PHE D 2 248 ? 138.377 96.660  155.205 1.00 25.82 ?  227 PHE D CZ    1 
ATOM   15217 N  N     . ALA D 2 249 ? 139.559 101.057 157.849 1.00 24.83 ?  228 ALA D N     1 
ATOM   15218 C  CA    . ALA D 2 249 ? 140.170 101.695 156.675 1.00 24.08 ?  228 ALA D CA    1 
ATOM   15219 C  C     . ALA D 2 249 ? 141.636 102.075 156.925 1.00 23.93 ?  228 ALA D C     1 
ATOM   15220 O  O     . ALA D 2 249 ? 142.496 101.854 156.070 1.00 22.51 ?  228 ALA D O     1 
ATOM   15221 C  CB    . ALA D 2 249 ? 139.363 102.934 156.273 1.00 24.18 ?  228 ALA D CB    1 
ATOM   15222 N  N     . ILE D 2 250 ? 141.908 102.651 158.096 1.00 24.20 ?  229 ILE D N     1 
ATOM   15223 C  CA    . ILE D 2 250 ? 143.266 103.064 158.454 1.00 24.86 ?  229 ILE D CA    1 
ATOM   15224 C  C     . ILE D 2 250 ? 144.170 101.845 158.670 1.00 24.68 ?  229 ILE D C     1 
ATOM   15225 O  O     . ILE D 2 250 ? 145.312 101.834 158.225 1.00 24.30 ?  229 ILE D O     1 
ATOM   15226 C  CB    . ILE D 2 250 ? 143.284 104.023 159.697 1.00 25.44 ?  229 ILE D CB    1 
ATOM   15227 C  CG1   . ILE D 2 250 ? 142.452 105.296 159.448 1.00 26.49 ?  229 ILE D CG1   1 
ATOM   15228 C  CG2   . ILE D 2 250 ? 144.717 104.387 160.110 1.00 27.13 ?  229 ILE D CG2   1 
ATOM   15229 C  CD1   . ILE D 2 250 ? 142.806 106.083 158.184 1.00 28.58 ?  229 ILE D CD1   1 
ATOM   15230 N  N     . ASP D 2 251 ? 143.651 100.821 159.348 1.00 24.90 ?  230 ASP D N     1 
ATOM   15231 C  CA    . ASP D 2 251 ? 144.387 99.581  159.572 1.00 25.04 ?  230 ASP D CA    1 
ATOM   15232 C  C     . ASP D 2 251 ? 144.747 98.908  158.236 1.00 24.25 ?  230 ASP D C     1 
ATOM   15233 O  O     . ASP D 2 251 ? 145.891 98.496  158.030 1.00 23.60 ?  230 ASP D O     1 
ATOM   15234 C  CB    . ASP D 2 251 ? 143.562 98.640  160.456 1.00 26.23 ?  230 ASP D CB    1 
ATOM   15235 C  CG    . ASP D 2 251 ? 144.201 97.279  160.628 1.00 28.91 ?  230 ASP D CG    1 
ATOM   15236 O  OD1   . ASP D 2 251 ? 145.262 97.179  161.280 1.00 32.03 ?  230 ASP D OD1   1 
ATOM   15237 O  OD2   . ASP D 2 251 ? 143.621 96.295  160.126 1.00 33.16 -1 230 ASP D OD2   1 
ATOM   15238 N  N     . LEU D 2 252 ? 143.766 98.796  157.343 1.00 23.43 ?  231 LEU D N     1 
ATOM   15239 C  CA    . LEU D 2 252 ? 144.004 98.254  156.008 1.00 22.79 ?  231 LEU D CA    1 
ATOM   15240 C  C     . LEU D 2 252 ? 145.048 99.083  155.252 1.00 22.71 ?  231 LEU D C     1 
ATOM   15241 O  O     . LEU D 2 252 ? 145.965 98.526  154.637 1.00 21.58 ?  231 LEU D O     1 
ATOM   15242 C  CB    . LEU D 2 252 ? 142.704 98.186  155.199 1.00 22.48 ?  231 LEU D CB    1 
ATOM   15243 C  CG    . LEU D 2 252 ? 142.836 97.624  153.771 1.00 21.05 ?  231 LEU D CG    1 
ATOM   15244 C  CD1   . LEU D 2 252 ? 143.431 96.199  153.767 1.00 22.94 ?  231 LEU D CD1   1 
ATOM   15245 C  CD2   . LEU D 2 252 ? 141.493 97.627  153.057 1.00 19.31 ?  231 LEU D CD2   1 
ATOM   15246 N  N     . LEU D 2 253 ? 144.900 100.407 155.299 1.00 22.90 ?  232 LEU D N     1 
ATOM   15247 C  CA    . LEU D 2 253 ? 145.857 101.295 154.623 1.00 23.78 ?  232 LEU D CA    1 
ATOM   15248 C  C     . LEU D 2 253 ? 147.284 101.054 155.130 1.00 23.75 ?  232 LEU D C     1 
ATOM   15249 O  O     . LEU D 2 253 ? 148.219 100.953 154.335 1.00 23.26 ?  232 LEU D O     1 
ATOM   15250 C  CB    . LEU D 2 253 ? 145.489 102.768 154.820 1.00 24.03 ?  232 LEU D CB    1 
ATOM   15251 C  CG    . LEU D 2 253 ? 146.562 103.765 154.346 1.00 26.46 ?  232 LEU D CG    1 
ATOM   15252 C  CD1   . LEU D 2 253 ? 146.615 103.794 152.837 1.00 26.52 ?  232 LEU D CD1   1 
ATOM   15253 C  CD2   . LEU D 2 253 ? 146.313 105.173 154.893 1.00 27.50 ?  232 LEU D CD2   1 
ATOM   15254 N  N     . ASN D 2 254 ? 147.435 100.989 156.454 1.00 24.63 ?  233 ASN D N     1 
ATOM   15255 C  CA    . ASN D 2 254 ? 148.726 100.697 157.081 1.00 25.49 ?  233 ASN D CA    1 
ATOM   15256 C  C     . ASN D 2 254 ? 149.363 99.383  156.605 1.00 24.94 ?  233 ASN D C     1 
ATOM   15257 O  O     . ASN D 2 254 ? 150.562 99.353  156.316 1.00 24.64 ?  233 ASN D O     1 
ATOM   15258 C  CB    . ASN D 2 254 ? 148.601 100.679 158.602 1.00 26.98 ?  233 ASN D CB    1 
ATOM   15259 C  CG    . ASN D 2 254 ? 148.741 102.055 159.213 1.00 29.94 ?  233 ASN D CG    1 
ATOM   15260 O  OD1   . ASN D 2 254 ? 149.579 102.862 158.789 1.00 34.55 ?  233 ASN D OD1   1 
ATOM   15261 N  ND2   . ASN D 2 254 ? 147.931 102.332 160.226 1.00 33.81 ?  233 ASN D ND2   1 
ATOM   15262 N  N     . GLN D 2 255 ? 148.569 98.314  156.539 1.00 24.08 ?  234 GLN D N     1 
ATOM   15263 C  CA    . GLN D 2 255 ? 149.079 97.016  156.088 1.00 24.35 ?  234 GLN D CA    1 
ATOM   15264 C  C     . GLN D 2 255 ? 149.566 97.117  154.654 1.00 23.26 ?  234 GLN D C     1 
ATOM   15265 O  O     . GLN D 2 255 ? 150.673 96.664  154.344 1.00 23.12 ?  234 GLN D O     1 
ATOM   15266 C  CB    . GLN D 2 255 ? 148.016 95.914  156.166 1.00 24.84 ?  234 GLN D CB    1 
ATOM   15267 C  CG    . GLN D 2 255 ? 147.656 95.437  157.555 1.00 27.45 ?  234 GLN D CG    1 
ATOM   15268 C  CD    . GLN D 2 255 ? 148.857 94.951  158.349 1.00 32.02 ?  234 GLN D CD    1 
ATOM   15269 O  OE1   . GLN D 2 255 ? 149.175 95.512  159.395 1.00 35.80 ?  234 GLN D OE1   1 
ATOM   15270 N  NE2   . GLN D 2 255 ? 149.525 93.905  157.859 1.00 32.12 ?  234 GLN D NE2   1 
ATOM   15271 N  N     . LEU D 2 256 ? 148.739 97.712  153.793 1.00 21.77 ?  235 LEU D N     1 
ATOM   15272 C  CA    . LEU D 2 256 ? 149.076 97.863  152.376 1.00 21.68 ?  235 LEU D CA    1 
ATOM   15273 C  C     . LEU D 2 256 ? 150.279 98.782  152.195 1.00 21.49 ?  235 LEU D C     1 
ATOM   15274 O  O     . LEU D 2 256 ? 151.154 98.506  151.380 1.00 20.89 ?  235 LEU D O     1 
ATOM   15275 C  CB    . LEU D 2 256 ? 147.883 98.398  151.560 1.00 20.49 ?  235 LEU D CB    1 
ATOM   15276 C  CG    . LEU D 2 256 ? 146.679 97.458  151.401 1.00 21.52 ?  235 LEU D CG    1 
ATOM   15277 C  CD1   . LEU D 2 256 ? 145.474 98.175  150.769 1.00 20.71 ?  235 LEU D CD1   1 
ATOM   15278 C  CD2   . LEU D 2 256 ? 147.033 96.221  150.587 1.00 20.74 ?  235 LEU D CD2   1 
ATOM   15279 N  N     . TYR D 2 257 ? 150.317 99.869  152.964 1.00 21.42 ?  236 TYR D N     1 
ATOM   15280 C  CA    . TYR D 2 257 ? 151.420 100.824 152.865 1.00 22.02 ?  236 TYR D CA    1 
ATOM   15281 C  C     . TYR D 2 257 ? 152.767 100.204 153.237 1.00 22.61 ?  236 TYR D C     1 
ATOM   15282 O  O     . TYR D 2 257 ? 153.765 100.423 152.550 1.00 22.19 ?  236 TYR D O     1 
ATOM   15283 C  CB    . TYR D 2 257 ? 151.146 102.071 153.700 1.00 22.06 ?  236 TYR D CB    1 
ATOM   15284 C  CG    . TYR D 2 257 ? 152.314 103.029 153.772 1.00 23.44 ?  236 TYR D CG    1 
ATOM   15285 C  CD1   . TYR D 2 257 ? 152.750 103.721 152.636 1.00 24.01 ?  236 TYR D CD1   1 
ATOM   15286 C  CD2   . TYR D 2 257 ? 152.975 103.250 154.978 1.00 25.22 ?  236 TYR D CD2   1 
ATOM   15287 C  CE1   . TYR D 2 257 ? 153.823 104.607 152.706 1.00 25.14 ?  236 TYR D CE1   1 
ATOM   15288 C  CE2   . TYR D 2 257 ? 154.055 104.126 155.056 1.00 26.71 ?  236 TYR D CE2   1 
ATOM   15289 C  CZ    . TYR D 2 257 ? 154.467 104.801 153.921 1.00 25.35 ?  236 TYR D CZ    1 
ATOM   15290 O  OH    . TYR D 2 257 ? 155.524 105.670 154.015 1.00 26.77 ?  236 TYR D OH    1 
ATOM   15291 N  N     . GLU D 2 258 ? 152.796 99.421  154.313 1.00 23.09 ?  237 GLU D N     1 
ATOM   15292 C  CA    . GLU D 2 258 ? 154.056 98.807  154.737 1.00 23.98 ?  237 GLU D CA    1 
ATOM   15293 C  C     . GLU D 2 258 ? 154.565 97.798  153.708 1.00 23.13 ?  237 GLU D C     1 
ATOM   15294 O  O     . GLU D 2 258 ? 155.764 97.726  153.450 1.00 23.02 ?  237 GLU D O     1 
ATOM   15295 C  CB    . GLU D 2 258 ? 153.943 98.194  156.140 1.00 25.20 ?  237 GLU D CB    1 
ATOM   15296 C  CG    . GLU D 2 258 ? 153.716 99.236  157.249 1.00 28.82 ?  237 GLU D CG    1 
ATOM   15297 C  CD    . GLU D 2 258 ? 154.934 100.124 157.540 1.00 34.48 ?  237 GLU D CD    1 
ATOM   15298 O  OE1   . GLU D 2 258 ? 156.095 99.677  157.344 1.00 37.75 ?  237 GLU D OE1   1 
ATOM   15299 O  OE2   . GLU D 2 258 ? 154.731 101.281 157.984 1.00 37.16 -1 237 GLU D OE2   1 
ATOM   15300 N  N     . ASN D 2 259 ? 153.651 97.051  153.103 1.00 22.12 ?  238 ASN D N     1 
ATOM   15301 C  CA    . ASN D 2 259 ? 153.994 96.167  151.988 1.00 22.35 ?  238 ASN D CA    1 
ATOM   15302 C  C     . ASN D 2 259 ? 154.432 96.927  150.708 1.00 22.11 ?  238 ASN D C     1 
ATOM   15303 O  O     . ASN D 2 259 ? 155.330 96.471  149.997 1.00 22.24 ?  238 ASN D O     1 
ATOM   15304 C  CB    . ASN D 2 259 ? 152.835 95.207  151.691 1.00 21.69 ?  238 ASN D CB    1 
ATOM   15305 C  CG    . ASN D 2 259 ? 153.158 94.232  150.573 1.00 23.38 ?  238 ASN D CG    1 
ATOM   15306 O  OD1   . ASN D 2 259 ? 153.952 93.296  150.750 1.00 23.95 ?  238 ASN D OD1   1 
ATOM   15307 N  ND2   . ASN D 2 259 ? 152.557 94.451  149.412 1.00 21.14 ?  238 ASN D ND2   1 
ATOM   15308 N  N     . GLU D 2 260 ? 153.804 98.075  150.429 1.00 21.95 ?  239 GLU D N     1 
ATOM   15309 C  CA    . GLU D 2 260 ? 154.206 98.942  149.302 1.00 22.50 ?  239 GLU D CA    1 
ATOM   15310 C  C     . GLU D 2 260 ? 155.646 99.437  149.436 1.00 22.03 ?  239 GLU D C     1 
ATOM   15311 O  O     . GLU D 2 260 ? 156.355 99.564  148.443 1.00 22.03 ?  239 GLU D O     1 
ATOM   15312 C  CB    . GLU D 2 260 ? 153.300 100.180 149.171 1.00 22.90 ?  239 GLU D CB    1 
ATOM   15313 C  CG    . GLU D 2 260 ? 151.984 99.981  148.403 1.00 25.84 ?  239 GLU D CG    1 
ATOM   15314 C  CD    . GLU D 2 260 ? 152.148 99.262  147.068 1.00 28.59 ?  239 GLU D CD    1 
ATOM   15315 O  OE1   . GLU D 2 260 ? 152.254 98.018  147.074 1.00 28.18 ?  239 GLU D OE1   1 
ATOM   15316 O  OE2   . GLU D 2 260 ? 152.130 99.935  146.010 1.00 30.32 -1 239 GLU D OE2   1 
ATOM   15317 N  N     . LEU D 2 261 ? 156.057 99.750  150.660 1.00 21.50 ?  240 LEU D N     1 
ATOM   15318 C  CA    . LEU D 2 261 ? 157.424 100.204 150.896 1.00 22.03 ?  240 LEU D CA    1 
ATOM   15319 C  C     . LEU D 2 261 ? 158.404 99.103  150.530 1.00 21.52 ?  240 LEU D C     1 
ATOM   15320 O  O     . LEU D 2 261 ? 159.412 99.368  149.873 1.00 21.44 ?  240 LEU D O     1 
ATOM   15321 C  CB    . LEU D 2 261 ? 157.634 100.643 152.343 1.00 21.57 ?  240 LEU D CB    1 
ATOM   15322 C  CG    . LEU D 2 261 ? 156.795 101.809 152.867 1.00 23.22 ?  240 LEU D CG    1 
ATOM   15323 C  CD1   . LEU D 2 261 ? 157.141 102.050 154.325 1.00 23.06 ?  240 LEU D CD1   1 
ATOM   15324 C  CD2   . LEU D 2 261 ? 157.023 103.074 152.039 1.00 23.52 ?  240 LEU D CD2   1 
ATOM   15325 N  N     . GLU D 2 262 ? 158.092 97.873  150.937 1.00 21.69 ?  241 GLU D N     1 
ATOM   15326 C  CA    . GLU D 2 262 ? 158.928 96.712  150.591 1.00 22.31 ?  241 GLU D CA    1 
ATOM   15327 C  C     . GLU D 2 262 ? 158.897 96.416  149.090 1.00 21.69 ?  241 GLU D C     1 
ATOM   15328 O  O     . GLU D 2 262 ? 159.933 96.139  148.480 1.00 21.75 ?  241 GLU D O     1 
ATOM   15329 C  CB    . GLU D 2 262 ? 158.492 95.466  151.368 1.00 22.46 ?  241 GLU D CB    1 
ATOM   15330 C  CG    . GLU D 2 262 ? 158.597 95.561  152.892 1.00 25.63 ?  241 GLU D CG    1 
ATOM   15331 C  CD    . GLU D 2 262 ? 158.233 94.238  153.553 1.00 29.83 ?  241 GLU D CD    1 
ATOM   15332 O  OE1   . GLU D 2 262 ? 157.026 93.940  153.681 1.00 33.22 ?  241 GLU D OE1   1 
ATOM   15333 O  OE2   . GLU D 2 262 ? 159.148 93.479  153.917 1.00 33.36 -1 241 GLU D OE2   1 
ATOM   15334 N  N     . TYR D 2 263 ? 157.702 96.455  148.504 1.00 21.42 ?  242 TYR D N     1 
ATOM   15335 C  CA    . TYR D 2 263 ? 157.518 96.279  147.059 1.00 21.04 ?  242 TYR D CA    1 
ATOM   15336 C  C     . TYR D 2 263 ? 158.371 97.298  146.292 1.00 21.15 ?  242 TYR D C     1 
ATOM   15337 O  O     . TYR D 2 263 ? 159.010 96.968  145.291 1.00 20.32 ?  242 TYR D O     1 
ATOM   15338 C  CB    . TYR D 2 263 ? 156.033 96.461  146.707 1.00 20.95 ?  242 TYR D CB    1 
ATOM   15339 C  CG    . TYR D 2 263 ? 155.695 96.408  145.228 1.00 21.86 ?  242 TYR D CG    1 
ATOM   15340 C  CD1   . TYR D 2 263 ? 155.566 95.185  144.568 1.00 23.53 ?  242 TYR D CD1   1 
ATOM   15341 C  CD2   . TYR D 2 263 ? 155.503 97.579  144.489 1.00 21.20 ?  242 TYR D CD2   1 
ATOM   15342 C  CE1   . TYR D 2 263 ? 155.254 95.130  143.217 1.00 23.34 ?  242 TYR D CE1   1 
ATOM   15343 C  CE2   . TYR D 2 263 ? 155.191 97.531  143.134 1.00 23.11 ?  242 TYR D CE2   1 
ATOM   15344 C  CZ    . TYR D 2 263 ? 155.075 96.302  142.506 1.00 23.27 ?  242 TYR D CZ    1 
ATOM   15345 O  OH    . TYR D 2 263 ? 154.765 96.250  141.163 1.00 27.07 ?  242 TYR D OH    1 
ATOM   15346 N  N     . THR D 2 264 ? 158.350 98.538  146.777 1.00 21.12 ?  243 THR D N     1 
ATOM   15347 C  CA    . THR D 2 264 ? 159.049 99.656  146.152 1.00 21.98 ?  243 THR D CA    1 
ATOM   15348 C  C     . THR D 2 264 ? 160.562 99.448  146.164 1.00 22.32 ?  243 THR D C     1 
ATOM   15349 O  O     . THR D 2 264 ? 161.205 99.545  145.121 1.00 21.78 ?  243 THR D O     1 
ATOM   15350 C  CB    . THR D 2 264 ? 158.657 100.995 146.817 1.00 21.68 ?  243 THR D CB    1 
ATOM   15351 O  OG1   . THR D 2 264 ? 157.274 101.252 146.557 1.00 23.29 ?  243 THR D OG1   1 
ATOM   15352 C  CG2   . THR D 2 264 ? 159.504 102.173 146.297 1.00 23.16 ?  243 THR D CG2   1 
ATOM   15353 N  N     . GLU D 2 265 ? 161.121 99.136  147.333 1.00 22.48 ?  244 GLU D N     1 
ATOM   15354 C  CA    . GLU D 2 265 ? 162.563 98.891  147.424 1.00 23.73 ?  244 GLU D CA    1 
ATOM   15355 C  C     . GLU D 2 265 ? 162.985 97.721  146.549 1.00 23.85 ?  244 GLU D C     1 
ATOM   15356 O  O     . GLU D 2 265 ? 164.013 97.791  145.888 1.00 24.40 ?  244 GLU D O     1 
ATOM   15357 C  CB    . GLU D 2 265 ? 162.989 98.656  148.865 1.00 23.19 ?  244 GLU D CB    1 
ATOM   15358 C  CG    . GLU D 2 265 ? 162.984 99.929  149.668 1.00 25.08 ?  244 GLU D CG    1 
ATOM   15359 C  CD    . GLU D 2 265 ? 163.236 99.702  151.144 1.00 27.30 ?  244 GLU D CD    1 
ATOM   15360 O  OE1   . GLU D 2 265 ? 163.619 98.581  151.531 1.00 27.77 ?  244 GLU D OE1   1 
ATOM   15361 O  OE2   . GLU D 2 265 ? 163.048 100.659 151.917 1.00 28.63 -1 244 GLU D OE2   1 
ATOM   15362 N  N     . ASP D 2 266 ? 162.163 96.671  146.527 1.00 24.13 ?  245 ASP D N     1 
ATOM   15363 C  CA    . ASP D 2 266 ? 162.426 95.464  145.739 1.00 25.22 ?  245 ASP D CA    1 
ATOM   15364 C  C     . ASP D 2 266 ? 162.580 95.758  144.230 1.00 24.84 ?  245 ASP D C     1 
ATOM   15365 O  O     . ASP D 2 266 ? 163.409 95.140  143.555 1.00 25.64 ?  245 ASP D O     1 
ATOM   15366 C  CB    . ASP D 2 266 ? 161.307 94.440  145.990 1.00 25.79 ?  245 ASP D CB    1 
ATOM   15367 C  CG    . ASP D 2 266 ? 161.562 93.096  145.322 1.00 27.71 ?  245 ASP D CG    1 
ATOM   15368 O  OD1   . ASP D 2 266 ? 162.618 92.497  145.577 1.00 31.57 ?  245 ASP D OD1   1 
ATOM   15369 O  OD2   . ASP D 2 266 ? 160.694 92.622  144.559 1.00 30.29 -1 245 ASP D OD2   1 
ATOM   15370 N  N     . LEU D 2 267 ? 161.801 96.708  143.719 1.00 24.07 ?  246 LEU D N     1 
ATOM   15371 C  CA    . LEU D 2 267 ? 161.800 97.036  142.291 1.00 23.98 ?  246 LEU D CA    1 
ATOM   15372 C  C     . LEU D 2 267 ? 162.685 98.223  141.908 1.00 22.83 ?  246 LEU D C     1 
ATOM   15373 O  O     . LEU D 2 267 ? 163.330 98.199  140.852 1.00 23.00 ?  246 LEU D O     1 
ATOM   15374 C  CB    . LEU D 2 267 ? 160.368 97.312  141.798 1.00 23.82 ?  246 LEU D CB    1 
ATOM   15375 C  CG    . LEU D 2 267 ? 159.417 96.109  141.739 1.00 26.05 ?  246 LEU D CG    1 
ATOM   15376 C  CD1   . LEU D 2 267 ? 158.157 96.466  141.000 1.00 26.74 ?  246 LEU D CD1   1 
ATOM   15377 C  CD2   . LEU D 2 267 ? 160.071 94.907  141.083 1.00 28.00 ?  246 LEU D CD2   1 
ATOM   15378 N  N     . TYR D 2 268 ? 162.705 99.248  142.760 1.00 21.68 ?  247 TYR D N     1 
ATOM   15379 C  CA    . TYR D 2 268 ? 163.292 100.543 142.399 1.00 20.95 ?  247 TYR D CA    1 
ATOM   15380 C  C     . TYR D 2 268 ? 164.691 100.850 142.947 1.00 21.43 ?  247 TYR D C     1 
ATOM   15381 O  O     . TYR D 2 268 ? 165.342 101.766 142.447 1.00 20.73 ?  247 TYR D O     1 
ATOM   15382 C  CB    . TYR D 2 268 ? 162.346 101.689 142.769 1.00 20.27 ?  247 TYR D CB    1 
ATOM   15383 C  CG    . TYR D 2 268 ? 161.100 101.785 141.908 1.00 19.54 ?  247 TYR D CG    1 
ATOM   15384 C  CD1   . TYR D 2 268 ? 159.875 101.314 142.370 1.00 18.52 ?  247 TYR D CD1   1 
ATOM   15385 C  CD2   . TYR D 2 268 ? 161.154 102.346 140.623 1.00 20.62 ?  247 TYR D CD2   1 
ATOM   15386 C  CE1   . TYR D 2 268 ? 158.703 101.412 141.575 1.00 18.33 ?  247 TYR D CE1   1 
ATOM   15387 C  CE2   . TYR D 2 268 ? 159.995 102.447 139.820 1.00 20.79 ?  247 TYR D CE2   1 
ATOM   15388 C  CZ    . TYR D 2 268 ? 158.781 101.986 140.311 1.00 20.23 ?  247 TYR D CZ    1 
ATOM   15389 O  OH    . TYR D 2 268 ? 157.656 102.089 139.517 1.00 20.50 ?  247 TYR D OH    1 
ATOM   15390 N  N     . ASP D 2 269 ? 165.153 100.121 143.970 1.00 21.65 ?  248 ASP D N     1 
ATOM   15391 C  CA    . ASP D 2 269 ? 166.533 100.317 144.427 1.00 22.30 ?  248 ASP D CA    1 
ATOM   15392 C  C     . ASP D 2 269 ? 167.569 100.135 143.293 1.00 22.54 ?  248 ASP D C     1 
ATOM   15393 O  O     . ASP D 2 269 ? 168.552 100.879 143.229 1.00 22.49 ?  248 ASP D O     1 
ATOM   15394 C  CB    . ASP D 2 269 ? 166.874 99.418  145.617 1.00 22.83 ?  248 ASP D CB    1 
ATOM   15395 C  CG    . ASP D 2 269 ? 166.375 99.981  146.944 1.00 23.55 ?  248 ASP D CG    1 
ATOM   15396 O  OD1   . ASP D 2 269 ? 165.901 101.135 146.973 1.00 24.95 ?  248 ASP D OD1   1 
ATOM   15397 O  OD2   . ASP D 2 269 ? 166.456 99.263  147.966 1.00 24.47 -1 248 ASP D OD2   1 
ATOM   15398 N  N     . GLN D 2 270 ? 167.343 99.163  142.407 1.00 22.79 ?  249 GLN D N     1 
ATOM   15399 C  CA    . GLN D 2 270 ? 168.285 98.881  141.316 1.00 23.41 ?  249 GLN D CA    1 
ATOM   15400 C  C     . GLN D 2 270 ? 168.381 100.005 140.279 1.00 22.83 ?  249 GLN D C     1 
ATOM   15401 O  O     . GLN D 2 270 ? 169.322 100.034 139.488 1.00 23.75 ?  249 GLN D O     1 
ATOM   15402 C  CB    . GLN D 2 270 ? 167.975 97.548  140.628 1.00 24.02 ?  249 GLN D CB    1 
ATOM   15403 C  CG    . GLN D 2 270 ? 166.681 97.534  139.794 1.00 25.40 ?  249 GLN D CG    1 
ATOM   15404 C  CD    . GLN D 2 270 ? 166.257 96.131  139.397 1.00 29.23 ?  249 GLN D CD    1 
ATOM   15405 O  OE1   . GLN D 2 270 ? 166.504 95.167  140.124 1.00 31.31 ?  249 GLN D OE1   1 
ATOM   15406 N  NE2   . GLN D 2 270 ? 165.602 96.008  138.244 1.00 30.04 ?  249 GLN D NE2   1 
ATOM   15407 N  N     . VAL D 2 271 ? 167.404 100.911 140.273 1.00 21.93 ?  250 VAL D N     1 
ATOM   15408 C  CA    . VAL D 2 271 ? 167.451 102.087 139.398 1.00 21.29 ?  250 VAL D CA    1 
ATOM   15409 C  C     . VAL D 2 271 ? 167.483 103.406 140.193 1.00 21.16 ?  250 VAL D C     1 
ATOM   15410 O  O     . VAL D 2 271 ? 167.307 104.487 139.624 1.00 21.54 ?  250 VAL D O     1 
ATOM   15411 C  CB    . VAL D 2 271 ? 166.292 102.068 138.350 1.00 21.62 ?  250 VAL D CB    1 
ATOM   15412 C  CG1   . VAL D 2 271 ? 166.451 100.882 137.401 1.00 21.36 ?  250 VAL D CG1   1 
ATOM   15413 C  CG2   . VAL D 2 271 ? 164.914 102.038 139.037 1.00 21.17 ?  250 VAL D CG2   1 
ATOM   15414 N  N     . GLY D 2 272 ? 167.686 103.304 141.512 1.00 20.92 ?  251 GLY D N     1 
ATOM   15415 C  CA    . GLY D 2 272 ? 167.927 104.465 142.391 1.00 20.61 ?  251 GLY D CA    1 
ATOM   15416 C  C     . GLY D 2 272 ? 166.773 105.434 142.639 1.00 20.77 ?  251 GLY D C     1 
ATOM   15417 O  O     . GLY D 2 272 ? 166.999 106.613 142.954 1.00 20.28 ?  251 GLY D O     1 
ATOM   15418 N  N     . LEU D 2 273 ? 165.541 104.946 142.525 1.00 19.85 ?  252 LEU D N     1 
ATOM   15419 C  CA    . LEU D 2 273 ? 164.383 105.842 142.555 1.00 20.09 ?  252 LEU D CA    1 
ATOM   15420 C  C     . LEU D 2 273 ? 163.474 105.736 143.782 1.00 19.88 ?  252 LEU D C     1 
ATOM   15421 O  O     . LEU D 2 273 ? 162.541 106.522 143.912 1.00 20.04 ?  252 LEU D O     1 
ATOM   15422 C  CB    . LEU D 2 273 ? 163.534 105.620 141.293 1.00 19.97 ?  252 LEU D CB    1 
ATOM   15423 C  CG    . LEU D 2 273 ? 164.218 105.847 139.953 1.00 20.26 ?  252 LEU D CG    1 
ATOM   15424 C  CD1   . LEU D 2 273 ? 163.181 105.682 138.865 1.00 18.98 ?  252 LEU D CD1   1 
ATOM   15425 C  CD2   . LEU D 2 273 ? 164.892 107.245 139.869 1.00 21.03 ?  252 LEU D CD2   1 
ATOM   15426 N  N     . SER D 2 274 ? 163.759 104.784 144.672 0.50 19.54 ?  253 SER D N     1 
ATOM   15427 C  CA    . SER D 2 274 ? 162.823 104.402 145.742 0.50 19.34 ?  253 SER D CA    1 
ATOM   15428 C  C     . SER D 2 274 ? 162.352 105.552 146.639 0.50 20.05 ?  253 SER D C     1 
ATOM   15429 O  O     . SER D 2 274 ? 161.172 105.622 146.981 0.50 20.31 ?  253 SER D O     1 
ATOM   15430 C  CB    . SER D 2 274 ? 163.392 103.257 146.590 0.50 18.97 ?  253 SER D CB    1 
ATOM   15431 O  OG    . SER D 2 274 ? 163.726 102.138 145.789 0.50 15.35 ?  253 SER D OG    1 
ATOM   15432 N  N     . HIS D 2 275 ? 163.270 106.438 147.024 1.00 20.77 ?  254 HIS D N     1 
ATOM   15433 C  CA    . HIS D 2 275 ? 162.921 107.616 147.845 1.00 21.18 ?  254 HIS D CA    1 
ATOM   15434 C  C     . HIS D 2 275 ? 161.772 108.433 147.230 1.00 21.50 ?  254 HIS D C     1 
ATOM   15435 O  O     . HIS D 2 275 ? 160.782 108.747 147.913 1.00 19.88 ?  254 HIS D O     1 
ATOM   15436 C  CB    . HIS D 2 275 ? 164.143 108.515 148.095 1.00 21.60 ?  254 HIS D CB    1 
ATOM   15437 C  CG    . HIS D 2 275 ? 163.810 109.788 148.815 1.00 22.43 ?  254 HIS D CG    1 
ATOM   15438 N  ND1   . HIS D 2 275 ? 163.796 109.887 150.192 1.00 22.77 ?  254 HIS D ND1   1 
ATOM   15439 C  CD2   . HIS D 2 275 ? 163.462 111.011 148.345 1.00 22.50 ?  254 HIS D CD2   1 
ATOM   15440 C  CE1   . HIS D 2 275 ? 163.459 111.119 150.537 1.00 24.05 ?  254 HIS D CE1   1 
ATOM   15441 N  NE2   . HIS D 2 275 ? 163.245 111.818 149.435 1.00 23.22 ?  254 HIS D NE2   1 
ATOM   15442 N  N     . ASP D 2 276 ? 161.904 108.756 145.943 1.00 22.34 ?  255 ASP D N     1 
ATOM   15443 C  CA    . ASP D 2 276 ? 160.890 109.541 145.244 1.00 23.19 ?  255 ASP D CA    1 
ATOM   15444 C  C     . ASP D 2 276 ? 159.602 108.763 145.016 1.00 22.17 ?  255 ASP D C     1 
ATOM   15445 O  O     . ASP D 2 276 ? 158.527 109.345 145.051 1.00 21.87 ?  255 ASP D O     1 
ATOM   15446 C  CB    . ASP D 2 276 ? 161.414 110.072 143.900 1.00 24.33 ?  255 ASP D CB    1 
ATOM   15447 C  CG    . ASP D 2 276 ? 162.137 111.415 144.025 1.00 27.58 ?  255 ASP D CG    1 
ATOM   15448 O  OD1   . ASP D 2 276 ? 161.876 112.174 144.985 1.00 31.10 ?  255 ASP D OD1   1 
ATOM   15449 O  OD2   . ASP D 2 276 ? 162.979 111.708 143.146 1.00 29.88 -1 255 ASP D OD2   1 
ATOM   15450 N  N     . VAL D 2 277 ? 159.713 107.462 144.747 1.00 21.21 ?  256 VAL D N     1 
ATOM   15451 C  CA    . VAL D 2 277 ? 158.523 106.620 144.590 1.00 20.51 ?  256 VAL D CA    1 
ATOM   15452 C  C     . VAL D 2 277 ? 157.701 106.578 145.884 1.00 20.32 ?  256 VAL D C     1 
ATOM   15453 O  O     . VAL D 2 277 ? 156.475 106.642 145.840 1.00 19.81 ?  256 VAL D O     1 
ATOM   15454 C  CB    . VAL D 2 277 ? 158.868 105.178 144.122 1.00 20.30 ?  256 VAL D CB    1 
ATOM   15455 C  CG1   . VAL D 2 277 ? 157.613 104.325 144.046 1.00 21.16 ?  256 VAL D CG1   1 
ATOM   15456 C  CG2   . VAL D 2 277 ? 159.552 105.211 142.766 1.00 19.06 ?  256 VAL D CG2   1 
ATOM   15457 N  N     . LYS D 2 278 ? 158.388 106.491 147.023 1.00 19.84 ?  257 LYS D N     1 
ATOM   15458 C  CA    . LYS D 2 278 ? 157.730 106.498 148.329 1.00 20.27 ?  257 LYS D CA    1 
ATOM   15459 C  C     . LYS D 2 278 ? 156.910 107.772 148.569 1.00 20.16 ?  257 LYS D C     1 
ATOM   15460 O  O     . LYS D 2 278 ? 155.797 107.687 149.081 1.00 19.88 ?  257 LYS D O     1 
ATOM   15461 C  CB    . LYS D 2 278 ? 158.734 106.257 149.460 1.00 20.20 ?  257 LYS D CB    1 
ATOM   15462 C  CG    . LYS D 2 278 ? 159.219 104.813 149.534 1.00 21.60 ?  257 LYS D CG    1 
ATOM   15463 C  CD    . LYS D 2 278 ? 160.407 104.661 150.476 1.00 21.53 ?  257 LYS D CD    1 
ATOM   15464 C  CE    . LYS D 2 278 ? 160.956 103.258 150.387 1.00 24.52 ?  257 LYS D CE    1 
ATOM   15465 N  NZ    . LYS D 2 278 ? 162.104 103.076 151.335 1.00 26.32 1  257 LYS D NZ    1 
ATOM   15466 N  N     . LYS D 2 279 ? 157.447 108.932 148.175 1.00 19.67 ?  258 LYS D N     1 
ATOM   15467 C  CA    . LYS D 2 279 ? 156.689 110.189 148.259 1.00 20.10 ?  258 LYS D CA    1 
ATOM   15468 C  C     . LYS D 2 279 ? 155.406 110.120 147.423 1.00 19.12 ?  258 LYS D C     1 
ATOM   15469 O  O     . LYS D 2 279 ? 154.354 110.590 147.861 1.00 18.59 ?  258 LYS D O     1 
ATOM   15470 C  CB    . LYS D 2 279 ? 157.536 111.403 147.830 1.00 20.54 ?  258 LYS D CB    1 
ATOM   15471 C  CG    . LYS D 2 279 ? 158.780 111.653 148.680 1.00 22.84 ?  258 LYS D CG    1 
ATOM   15472 C  CD    . LYS D 2 279 ? 159.258 113.122 148.608 1.00 24.16 ?  258 LYS D CD    1 
ATOM   15473 C  CE    . LYS D 2 279 ? 159.766 113.510 147.222 1.00 25.61 ?  258 LYS D CE    1 
ATOM   15474 N  NZ    . LYS D 2 279 ? 160.237 114.948 147.163 1.00 24.70 1  258 LYS D NZ    1 
ATOM   15475 N  N     . PHE D 2 280 ? 155.507 109.512 146.237 1.00 19.04 ?  259 PHE D N     1 
ATOM   15476 C  CA    . PHE D 2 280 ? 154.377 109.357 145.301 1.00 19.31 ?  259 PHE D CA    1 
ATOM   15477 C  C     . PHE D 2 280 ? 153.292 108.410 145.825 1.00 19.25 ?  259 PHE D C     1 
ATOM   15478 O  O     . PHE D 2 280 ? 152.093 108.656 145.641 1.00 19.71 ?  259 PHE D O     1 
ATOM   15479 C  CB    . PHE D 2 280 ? 154.889 108.858 143.950 1.00 19.04 ?  259 PHE D CB    1 
ATOM   15480 C  CG    . PHE D 2 280 ? 153.913 109.028 142.802 1.00 20.15 ?  259 PHE D CG    1 
ATOM   15481 C  CD1   . PHE D 2 280 ? 153.385 110.271 142.489 1.00 21.63 ?  259 PHE D CD1   1 
ATOM   15482 C  CD2   . PHE D 2 280 ? 153.572 107.933 142.004 1.00 19.95 ?  259 PHE D CD2   1 
ATOM   15483 C  CE1   . PHE D 2 280 ? 152.509 110.427 141.392 1.00 22.56 ?  259 PHE D CE1   1 
ATOM   15484 C  CE2   . PHE D 2 280 ? 152.708 108.069 140.918 1.00 20.29 ?  259 PHE D CE2   1 
ATOM   15485 C  CZ    . PHE D 2 280 ? 152.172 109.321 140.612 1.00 21.30 ?  259 PHE D CZ    1 
ATOM   15486 N  N     . ILE D 2 281 ? 153.710 107.320 146.461 1.00 19.36 ?  260 ILE D N     1 
ATOM   15487 C  CA    . ILE D 2 281 ? 152.780 106.420 147.151 1.00 19.45 ?  260 ILE D CA    1 
ATOM   15488 C  C     . ILE D 2 281 ? 151.961 107.144 148.242 1.00 19.61 ?  260 ILE D C     1 
ATOM   15489 O  O     . ILE D 2 281 ? 150.739 106.994 148.291 1.00 19.72 ?  260 ILE D O     1 
ATOM   15490 C  CB    . ILE D 2 281 ? 153.548 105.205 147.734 1.00 19.49 ?  260 ILE D CB    1 
ATOM   15491 C  CG1   . ILE D 2 281 ? 154.115 104.359 146.590 1.00 20.10 ?  260 ILE D CG1   1 
ATOM   15492 C  CG2   . ILE D 2 281 ? 152.684 104.370 148.704 1.00 20.53 ?  260 ILE D CG2   1 
ATOM   15493 C  CD1   . ILE D 2 281 ? 155.159 103.348 147.075 1.00 21.17 ?  260 ILE D CD1   1 
ATOM   15494 N  N     . ARG D 2 282 ? 152.627 107.927 149.093 1.00 19.75 ?  261 ARG D N     1 
ATOM   15495 C  CA    . ARG D 2 282 ? 151.948 108.621 150.204 1.00 20.34 ?  261 ARG D CA    1 
ATOM   15496 C  C     . ARG D 2 282 ? 150.971 109.677 149.702 1.00 21.18 ?  261 ARG D C     1 
ATOM   15497 O  O     . ARG D 2 282 ? 149.862 109.830 150.234 1.00 21.68 ?  261 ARG D O     1 
ATOM   15498 C  CB    . ARG D 2 282 ? 152.958 109.239 151.179 1.00 20.20 ?  261 ARG D CB    1 
ATOM   15499 C  CG    . ARG D 2 282 ? 153.710 108.219 152.014 1.00 20.57 ?  261 ARG D CG    1 
ATOM   15500 C  CD    . ARG D 2 282 ? 154.574 108.899 153.079 1.00 23.15 ?  261 ARG D CD    1 
ATOM   15501 N  NE    . ARG D 2 282 ? 155.774 109.541 152.539 1.00 23.46 ?  261 ARG D NE    1 
ATOM   15502 C  CZ    . ARG D 2 282 ? 156.948 108.935 152.372 1.00 22.84 ?  261 ARG D CZ    1 
ATOM   15503 N  NH1   . ARG D 2 282 ? 157.094 107.649 152.667 1.00 23.37 1  261 ARG D NH1   1 
ATOM   15504 N  NH2   . ARG D 2 282 ? 157.981 109.617 151.896 1.00 22.27 ?  261 ARG D NH2   1 
ATOM   15505 N  N     . TYR D 2 283 ? 151.403 110.416 148.686 1.00 21.46 ?  262 TYR D N     1 
ATOM   15506 C  CA    . TYR D 2 283 ? 150.569 111.423 148.033 1.00 22.97 ?  262 TYR D CA    1 
ATOM   15507 C  C     . TYR D 2 283 ? 149.288 110.773 147.464 1.00 22.12 ?  262 TYR D C     1 
ATOM   15508 O  O     . TYR D 2 283 ? 148.187 111.306 147.620 1.00 22.00 ?  262 TYR D O     1 
ATOM   15509 C  CB    . TYR D 2 283 ? 151.406 112.126 146.959 1.00 23.37 ?  262 TYR D CB    1 
ATOM   15510 C  CG    . TYR D 2 283 ? 150.652 112.952 145.943 1.00 27.31 ?  262 TYR D CG    1 
ATOM   15511 C  CD1   . TYR D 2 283 ? 150.343 114.289 146.194 1.00 30.79 ?  262 TYR D CD1   1 
ATOM   15512 C  CD2   . TYR D 2 283 ? 150.289 112.407 144.712 1.00 30.31 ?  262 TYR D CD2   1 
ATOM   15513 C  CE1   . TYR D 2 283 ? 149.649 115.060 145.247 1.00 33.18 ?  262 TYR D CE1   1 
ATOM   15514 C  CE2   . TYR D 2 283 ? 149.608 113.167 143.756 1.00 33.20 ?  262 TYR D CE2   1 
ATOM   15515 C  CZ    . TYR D 2 283 ? 149.298 114.494 144.031 1.00 34.74 ?  262 TYR D CZ    1 
ATOM   15516 O  OH    . TYR D 2 283 ? 148.632 115.245 143.082 1.00 37.63 ?  262 TYR D OH    1 
ATOM   15517 N  N     . ASN D 2 284 ? 149.426 109.599 146.854 1.00 21.63 ?  263 ASN D N     1 
ATOM   15518 C  CA    . ASN D 2 284 ? 148.266 108.905 146.299 1.00 21.41 ?  263 ASN D CA    1 
ATOM   15519 C  C     . ASN D 2 284 ? 147.413 108.197 147.356 1.00 20.86 ?  263 ASN D C     1 
ATOM   15520 O  O     . ASN D 2 284 ? 146.202 108.091 147.193 1.00 20.92 ?  263 ASN D O     1 
ATOM   15521 C  CB    . ASN D 2 284 ? 148.670 107.977 145.152 1.00 21.15 ?  263 ASN D CB    1 
ATOM   15522 C  CG    . ASN D 2 284 ? 148.993 108.749 143.880 1.00 22.59 ?  263 ASN D CG    1 
ATOM   15523 O  OD1   . ASN D 2 284 ? 148.097 109.287 143.224 1.00 22.35 ?  263 ASN D OD1   1 
ATOM   15524 N  ND2   . ASN D 2 284 ? 150.275 108.821 143.534 1.00 22.93 ?  263 ASN D ND2   1 
ATOM   15525 N  N     . ALA D 2 285 ? 148.042 107.727 148.433 1.00 20.92 ?  264 ALA D N     1 
ATOM   15526 C  CA    . ALA D 2 285 ? 147.306 107.235 149.611 1.00 20.77 ?  264 ALA D CA    1 
ATOM   15527 C  C     . ALA D 2 285 ? 146.359 108.302 150.173 1.00 21.13 ?  264 ALA D C     1 
ATOM   15528 O  O     . ALA D 2 285 ? 145.204 108.005 150.503 1.00 19.92 ?  264 ALA D O     1 
ATOM   15529 C  CB    . ALA D 2 285 ? 148.274 106.743 150.696 1.00 20.68 ?  264 ALA D CB    1 
ATOM   15530 N  N     . ASN D 2 286 ? 146.853 109.541 150.271 1.00 21.38 ?  265 ASN D N     1 
ATOM   15531 C  CA    . ASN D 2 286 ? 146.042 110.679 150.709 1.00 21.94 ?  265 ASN D CA    1 
ATOM   15532 C  C     . ASN D 2 286 ? 144.851 110.947 149.771 1.00 22.13 ?  265 ASN D C     1 
ATOM   15533 O  O     . ASN D 2 286 ? 143.761 111.263 150.231 1.00 21.95 ?  265 ASN D O     1 
ATOM   15534 C  CB    . ASN D 2 286 ? 146.894 111.944 150.832 1.00 22.22 ?  265 ASN D CB    1 
ATOM   15535 C  CG    . ASN D 2 286 ? 147.718 111.997 152.115 1.00 22.80 ?  265 ASN D CG    1 
ATOM   15536 O  OD1   . ASN D 2 286 ? 147.512 111.225 153.058 1.00 22.57 ?  265 ASN D OD1   1 
ATOM   15537 N  ND2   . ASN D 2 286 ? 148.670 112.923 152.145 1.00 23.91 ?  265 ASN D ND2   1 
ATOM   15538 N  N     . LYS D 2 287 ? 145.062 110.812 148.464 1.00 22.51 ?  266 LYS D N     1 
ATOM   15539 C  CA    . LYS D 2 287 ? 143.961 110.967 147.502 1.00 22.91 ?  266 LYS D CA    1 
ATOM   15540 C  C     . LYS D 2 287 ? 142.895 109.881 147.697 1.00 22.33 ?  266 LYS D C     1 
ATOM   15541 O  O     . LYS D 2 287 ? 141.706 110.173 147.660 1.00 22.24 ?  266 LYS D O     1 
ATOM   15542 C  CB    . LYS D 2 287 ? 144.475 110.962 146.056 1.00 23.65 ?  266 LYS D CB    1 
ATOM   15543 C  CG    . LYS D 2 287 ? 145.176 112.258 145.646 1.00 26.50 ?  266 LYS D CG    1 
ATOM   15544 C  CD    . LYS D 2 287 ? 145.650 112.182 144.182 1.00 31.30 ?  266 LYS D CD    1 
ATOM   15545 C  CE    . LYS D 2 287 ? 145.875 113.577 143.627 1.00 35.08 ?  266 LYS D CE    1 
ATOM   15546 N  NZ    . LYS D 2 287 ? 146.302 113.593 142.196 1.00 37.66 1  266 LYS D NZ    1 
ATOM   15547 N  N     . ALA D 2 288 ? 143.337 108.642 147.919 1.00 21.41 ?  267 ALA D N     1 
ATOM   15548 C  CA    . ALA D 2 288 ? 142.449 107.506 148.174 1.00 21.53 ?  267 ALA D CA    1 
ATOM   15549 C  C     . ALA D 2 288 ? 141.598 107.724 149.437 1.00 21.77 ?  267 ALA D C     1 
ATOM   15550 O  O     . ALA D 2 288 ? 140.379 107.479 149.441 1.00 21.59 ?  267 ALA D O     1 
ATOM   15551 C  CB    . ALA D 2 288 ? 143.261 106.207 148.277 1.00 21.33 ?  267 ALA D CB    1 
ATOM   15552 N  N     . LEU D 2 289 ? 142.235 108.206 150.495 1.00 21.71 ?  268 LEU D N     1 
ATOM   15553 C  CA    . LEU D 2 289 ? 141.513 108.555 151.713 1.00 22.36 ?  268 LEU D CA    1 
ATOM   15554 C  C     . LEU D 2 289 ? 140.496 109.657 151.451 1.00 23.01 ?  268 LEU D C     1 
ATOM   15555 O  O     . LEU D 2 289 ? 139.343 109.557 151.877 1.00 23.14 ?  268 LEU D O     1 
ATOM   15556 C  CB    . LEU D 2 289 ? 142.482 108.940 152.837 1.00 22.61 ?  268 LEU D CB    1 
ATOM   15557 C  CG    . LEU D 2 289 ? 143.317 107.780 153.420 1.00 21.22 ?  268 LEU D CG    1 
ATOM   15558 C  CD1   . LEU D 2 289 ? 144.450 108.308 154.287 1.00 20.77 ?  268 LEU D CD1   1 
ATOM   15559 C  CD2   . LEU D 2 289 ? 142.445 106.782 154.216 1.00 21.40 ?  268 LEU D CD2   1 
ATOM   15560 N  N     . MET D 2 290 ? 140.899 110.698 150.729 1.00 23.87 ?  269 MET D N     1 
ATOM   15561 C  CA    . MET D 2 290 ? 139.952 111.764 150.418 1.00 25.26 ?  269 MET D CA    1 
ATOM   15562 C  C     . MET D 2 290 ? 138.765 111.254 149.582 1.00 24.37 ?  269 MET D C     1 
ATOM   15563 O  O     . MET D 2 290 ? 137.636 111.667 149.824 1.00 23.97 ?  269 MET D O     1 
ATOM   15564 C  CB    . MET D 2 290 ? 140.655 112.980 149.823 1.00 25.94 ?  269 MET D CB    1 
ATOM   15565 C  CG    . MET D 2 290 ? 141.329 113.823 150.923 1.00 31.08 ?  269 MET D CG    1 
ATOM   15566 S  SD    . MET D 2 290 ? 142.219 115.274 150.316 1.00 41.28 ?  269 MET D SD    1 
ATOM   15567 C  CE    . MET D 2 290 ? 140.946 116.085 149.313 1.00 38.56 ?  269 MET D CE    1 
ATOM   15568 N  N     . ASN D 2 291 ? 139.013 110.326 148.652 1.00 23.66 ?  270 ASN D N     1 
ATOM   15569 C  CA    . ASN D 2 291 ? 137.918 109.649 147.919 1.00 23.17 ?  270 ASN D CA    1 
ATOM   15570 C  C     . ASN D 2 291 ? 136.895 108.950 148.819 1.00 23.22 ?  270 ASN D C     1 
ATOM   15571 O  O     . ASN D 2 291 ? 135.721 108.842 148.464 1.00 22.68 ?  270 ASN D O     1 
ATOM   15572 C  CB    . ASN D 2 291 ? 138.459 108.640 146.894 1.00 22.41 ?  270 ASN D CB    1 
ATOM   15573 C  CG    . ASN D 2 291 ? 139.152 109.307 145.729 1.00 21.93 ?  270 ASN D CG    1 
ATOM   15574 O  OD1   . ASN D 2 291 ? 139.033 110.520 145.529 1.00 20.94 ?  270 ASN D OD1   1 
ATOM   15575 N  ND2   . ASN D 2 291 ? 139.886 108.518 144.948 1.00 19.20 ?  270 ASN D ND2   1 
ATOM   15576 N  N     . LEU D 2 292 ? 137.360 108.478 149.975 1.00 23.53 ?  271 LEU D N     1 
ATOM   15577 C  CA    . LEU D 2 292 ? 136.510 107.805 150.959 1.00 24.21 ?  271 LEU D CA    1 
ATOM   15578 C  C     . LEU D 2 292 ? 135.974 108.774 152.017 1.00 25.14 ?  271 LEU D C     1 
ATOM   15579 O  O     . LEU D 2 292 ? 135.390 108.353 153.029 1.00 25.14 ?  271 LEU D O     1 
ATOM   15580 C  CB    . LEU D 2 292 ? 137.277 106.640 151.621 1.00 23.71 ?  271 LEU D CB    1 
ATOM   15581 C  CG    . LEU D 2 292 ? 137.705 105.470 150.723 1.00 23.37 ?  271 LEU D CG    1 
ATOM   15582 C  CD1   . LEU D 2 292 ? 138.776 104.616 151.409 1.00 23.28 ?  271 LEU D CD1   1 
ATOM   15583 C  CD2   . LEU D 2 292 ? 136.502 104.603 150.302 1.00 23.06 ?  271 LEU D CD2   1 
ATOM   15584 N  N     . GLY D 2 293 ? 136.165 110.072 151.773 1.00 25.82 ?  272 GLY D N     1 
ATOM   15585 C  CA    . GLY D 2 293 ? 135.702 111.116 152.679 1.00 27.13 ?  272 GLY D CA    1 
ATOM   15586 C  C     . GLY D 2 293 ? 136.478 111.211 153.977 1.00 27.99 ?  272 GLY D C     1 
ATOM   15587 O  O     . GLY D 2 293 ? 135.989 111.787 154.945 1.00 27.97 ?  272 GLY D O     1 
ATOM   15588 N  N     . PHE D 2 294 ? 137.688 110.646 154.000 1.00 28.02 ?  273 PHE D N     1 
ATOM   15589 C  CA    . PHE D 2 294 ? 138.550 110.676 155.189 1.00 28.75 ?  273 PHE D CA    1 
ATOM   15590 C  C     . PHE D 2 294 ? 139.663 111.726 155.078 1.00 29.00 ?  273 PHE D C     1 
ATOM   15591 O  O     . PHE D 2 294 ? 140.006 112.160 153.981 1.00 28.74 ?  273 PHE D O     1 
ATOM   15592 C  CB    . PHE D 2 294 ? 139.176 109.293 155.434 1.00 28.32 ?  273 PHE D CB    1 
ATOM   15593 C  CG    . PHE D 2 294 ? 138.178 108.220 155.770 1.00 28.66 ?  273 PHE D CG    1 
ATOM   15594 C  CD1   . PHE D 2 294 ? 137.116 108.478 156.638 1.00 30.23 ?  273 PHE D CD1   1 
ATOM   15595 C  CD2   . PHE D 2 294 ? 138.308 106.947 155.231 1.00 26.94 ?  273 PHE D CD2   1 
ATOM   15596 C  CE1   . PHE D 2 294 ? 136.188 107.479 156.951 1.00 31.04 ?  273 PHE D CE1   1 
ATOM   15597 C  CE2   . PHE D 2 294 ? 137.399 105.944 155.537 1.00 27.39 ?  273 PHE D CE2   1 
ATOM   15598 C  CZ    . PHE D 2 294 ? 136.338 106.201 156.397 1.00 29.80 ?  273 PHE D CZ    1 
ATOM   15599 N  N     . ASP D 2 295 ? 140.217 112.126 156.221 1.00 29.60 ?  274 ASP D N     1 
ATOM   15600 C  CA    . ASP D 2 295 ? 141.329 113.072 156.260 1.00 30.40 ?  274 ASP D CA    1 
ATOM   15601 C  C     . ASP D 2 295 ? 142.629 112.442 155.722 1.00 29.58 ?  274 ASP D C     1 
ATOM   15602 O  O     . ASP D 2 295 ? 142.814 111.228 155.814 1.00 28.68 ?  274 ASP D O     1 
ATOM   15603 C  CB    . ASP D 2 295 ? 141.558 113.583 157.688 1.00 31.44 ?  274 ASP D CB    1 
ATOM   15604 C  CG    . ASP D 2 295 ? 140.394 114.411 158.219 1.00 34.27 ?  274 ASP D CG    1 
ATOM   15605 O  OD1   . ASP D 2 295 ? 139.676 115.055 157.417 1.00 36.43 ?  274 ASP D OD1   1 
ATOM   15606 O  OD2   . ASP D 2 295 ? 140.206 114.417 159.455 1.00 38.03 -1 274 ASP D OD2   1 
ATOM   15607 N  N     . PRO D 2 296 ? 143.536 113.272 155.171 1.00 29.59 ?  275 PRO D N     1 
ATOM   15608 C  CA    . PRO D 2 296 ? 144.823 112.721 154.737 1.00 29.09 ?  275 PRO D CA    1 
ATOM   15609 C  C     . PRO D 2 296 ? 145.593 112.138 155.921 1.00 29.26 ?  275 PRO D C     1 
ATOM   15610 O  O     . PRO D 2 296 ? 145.506 112.654 157.036 1.00 29.36 ?  275 PRO D O     1 
ATOM   15611 C  CB    . PRO D 2 296 ? 145.563 113.937 154.162 1.00 29.49 ?  275 PRO D CB    1 
ATOM   15612 C  CG    . PRO D 2 296 ? 144.853 115.142 154.719 1.00 30.28 ?  275 PRO D CG    1 
ATOM   15613 C  CD    . PRO D 2 296 ? 143.430 114.722 154.915 1.00 29.63 ?  275 PRO D CD    1 
ATOM   15614 N  N     . TYR D 2 297 ? 146.321 111.058 155.681 1.00 28.97 ?  276 TYR D N     1 
ATOM   15615 C  CA    . TYR D 2 297 ? 147.064 110.379 156.735 1.00 29.63 ?  276 TYR D CA    1 
ATOM   15616 C  C     . TYR D 2 297 ? 148.513 110.886 156.816 1.00 29.55 ?  276 TYR D C     1 
ATOM   15617 O  O     . TYR D 2 297 ? 149.104 110.965 157.901 1.00 30.12 ?  276 TYR D O     1 
ATOM   15618 C  CB    . TYR D 2 297 ? 147.051 108.877 156.454 1.00 29.49 ?  276 TYR D CB    1 
ATOM   15619 C  CG    . TYR D 2 297 ? 147.495 108.003 157.597 1.00 31.19 ?  276 TYR D CG    1 
ATOM   15620 C  CD1   . TYR D 2 297 ? 146.782 107.980 158.800 1.00 31.93 ?  276 TYR D CD1   1 
ATOM   15621 C  CD2   . TYR D 2 297 ? 148.613 107.176 157.472 1.00 31.98 ?  276 TYR D CD2   1 
ATOM   15622 C  CE1   . TYR D 2 297 ? 147.179 107.171 159.856 1.00 33.86 ?  276 TYR D CE1   1 
ATOM   15623 C  CE2   . TYR D 2 297 ? 149.017 106.354 158.525 1.00 33.88 ?  276 TYR D CE2   1 
ATOM   15624 C  CZ    . TYR D 2 297 ? 148.288 106.359 159.709 1.00 34.42 ?  276 TYR D CZ    1 
ATOM   15625 O  OH    . TYR D 2 297 ? 148.672 105.564 160.759 1.00 37.63 ?  276 TYR D OH    1 
ATOM   15626 N  N     . PHE D 2 298 ? 149.066 111.220 155.655 1.00 29.10 ?  277 PHE D N     1 
ATOM   15627 C  CA    . PHE D 2 298 ? 150.471 111.586 155.510 1.00 28.97 ?  277 PHE D CA    1 
ATOM   15628 C  C     . PHE D 2 298 ? 150.623 113.097 155.302 1.00 29.77 ?  277 PHE D C     1 
ATOM   15629 O  O     . PHE D 2 298 ? 149.751 113.741 154.710 1.00 29.07 ?  277 PHE D O     1 
ATOM   15630 C  CB    . PHE D 2 298 ? 151.086 110.842 154.320 1.00 27.99 ?  277 PHE D CB    1 
ATOM   15631 C  CG    . PHE D 2 298 ? 151.060 109.338 154.452 1.00 27.61 ?  277 PHE D CG    1 
ATOM   15632 C  CD1   . PHE D 2 298 ? 150.194 108.573 153.681 1.00 25.91 ?  277 PHE D CD1   1 
ATOM   15633 C  CD2   . PHE D 2 298 ? 151.920 108.687 155.339 1.00 27.32 ?  277 PHE D CD2   1 
ATOM   15634 C  CE1   . PHE D 2 298 ? 150.177 107.194 153.796 1.00 26.65 ?  277 PHE D CE1   1 
ATOM   15635 C  CE2   . PHE D 2 298 ? 151.914 107.310 155.463 1.00 25.38 ?  277 PHE D CE2   1 
ATOM   15636 C  CZ    . PHE D 2 298 ? 151.040 106.557 154.702 1.00 26.20 ?  277 PHE D CZ    1 
ATOM   15637 N  N     . GLU D 2 299 ? 151.729 113.651 155.797 1.00 31.10 ?  278 GLU D N     1 
ATOM   15638 C  CA    . GLU D 2 299 ? 152.074 115.055 155.559 1.00 32.86 ?  278 GLU D CA    1 
ATOM   15639 C  C     . GLU D 2 299 ? 152.252 115.301 154.054 1.00 33.04 ?  278 GLU D C     1 
ATOM   15640 O  O     . GLU D 2 299 ? 152.640 114.395 153.311 1.00 32.23 ?  278 GLU D O     1 
ATOM   15641 C  CB    . GLU D 2 299 ? 153.349 115.442 156.328 1.00 33.45 ?  278 GLU D CB    1 
ATOM   15642 C  CG    . GLU D 2 299 ? 154.592 114.647 155.901 1.00 36.27 ?  278 GLU D CG    1 
ATOM   15643 C  CD    . GLU D 2 299 ? 155.890 115.105 156.549 1.00 40.47 ?  278 GLU D CD    1 
ATOM   15644 O  OE1   . GLU D 2 299 ? 155.900 115.421 157.761 1.00 41.72 ?  278 GLU D OE1   1 
ATOM   15645 O  OE2   . GLU D 2 299 ? 156.916 115.114 155.833 1.00 42.65 -1 278 GLU D OE2   1 
ATOM   15646 N  N     . GLU D 2 300 ? 151.958 116.526 153.625 1.00 34.09 ?  279 GLU D N     1 
ATOM   15647 C  CA    . GLU D 2 300 ? 152.099 116.929 152.232 1.00 35.06 ?  279 GLU D CA    1 
ATOM   15648 C  C     . GLU D 2 300 ? 153.574 116.938 151.829 1.00 34.97 ?  279 GLU D C     1 
ATOM   15649 O  O     . GLU D 2 300 ? 154.429 117.427 152.570 1.00 34.96 ?  279 GLU D O     1 
ATOM   15650 C  CB    . GLU D 2 300 ? 151.463 118.313 152.015 1.00 35.81 ?  279 GLU D CB    1 
ATOM   15651 C  CG    . GLU D 2 300 ? 151.386 118.749 150.550 1.00 38.58 ?  279 GLU D CG    1 
ATOM   15652 C  CD    . GLU D 2 300 ? 150.280 119.767 150.283 1.00 43.09 ?  279 GLU D CD    1 
ATOM   15653 O  OE1   . GLU D 2 300 ? 149.416 119.492 149.419 1.00 44.69 ?  279 GLU D OE1   1 
ATOM   15654 O  OE2   . GLU D 2 300 ? 150.266 120.835 150.938 1.00 44.94 -1 279 GLU D OE2   1 
ATOM   15655 N  N     . GLU D 2 301 ? 153.858 116.369 150.662 1.00 34.73 ?  280 GLU D N     1 
ATOM   15656 C  CA    . GLU D 2 301 ? 155.208 116.325 150.113 1.00 35.16 ?  280 GLU D CA    1 
ATOM   15657 C  C     . GLU D 2 301 ? 155.161 116.753 148.656 1.00 35.23 ?  280 GLU D C     1 
ATOM   15658 O  O     . GLU D 2 301 ? 154.140 116.583 147.983 1.00 34.92 ?  280 GLU D O     1 
ATOM   15659 C  CB    . GLU D 2 301 ? 155.781 114.905 150.208 1.00 35.10 ?  280 GLU D CB    1 
ATOM   15660 C  CG    . GLU D 2 301 ? 156.342 114.527 151.577 1.00 36.62 ?  280 GLU D CG    1 
ATOM   15661 C  CD    . GLU D 2 301 ? 156.648 113.035 151.703 1.00 37.59 ?  280 GLU D CD    1 
ATOM   15662 O  OE1   . GLU D 2 301 ? 155.732 112.209 151.503 1.00 38.10 ?  280 GLU D OE1   1 
ATOM   15663 O  OE2   . GLU D 2 301 ? 157.799 112.685 152.027 1.00 38.93 -1 280 GLU D OE2   1 
ATOM   15664 N  N     . ASP D 2 302 ? 156.263 117.308 148.166 1.00 35.60 ?  281 ASP D N     1 
ATOM   15665 C  CA    . ASP D 2 302 ? 156.360 117.640 146.749 1.00 35.96 ?  281 ASP D CA    1 
ATOM   15666 C  C     . ASP D 2 302 ? 156.688 116.370 145.976 1.00 35.01 ?  281 ASP D C     1 
ATOM   15667 O  O     . ASP D 2 302 ? 157.284 115.445 146.526 1.00 35.52 ?  281 ASP D O     1 
ATOM   15668 C  CB    . ASP D 2 302 ? 157.391 118.757 146.505 1.00 36.82 ?  281 ASP D CB    1 
ATOM   15669 C  CG    . ASP D 2 302 ? 158.829 118.356 146.882 1.00 39.01 ?  281 ASP D CG    1 
ATOM   15670 O  OD1   . ASP D 2 302 ? 159.041 117.413 147.685 1.00 40.83 ?  281 ASP D OD1   1 
ATOM   15671 O  OD2   . ASP D 2 302 ? 159.759 119.021 146.380 1.00 41.13 -1 281 ASP D OD2   1 
ATOM   15672 N  N     . ILE D 2 303 ? 156.268 116.302 144.720 1.00 33.94 ?  282 ILE D N     1 
ATOM   15673 C  CA    . ILE D 2 303 ? 156.520 115.117 143.902 1.00 33.00 ?  282 ILE D CA    1 
ATOM   15674 C  C     . ILE D 2 303 ? 157.613 115.361 142.853 1.00 31.59 ?  282 ILE D C     1 
ATOM   15675 O  O     . ILE D 2 303 ? 157.813 116.493 142.408 1.00 31.14 ?  282 ILE D O     1 
ATOM   15676 C  CB    . ILE D 2 303 ? 155.198 114.560 143.283 1.00 33.44 ?  282 ILE D CB    1 
ATOM   15677 C  CG1   . ILE D 2 303 ? 155.442 113.869 141.936 1.00 34.29 ?  282 ILE D CG1   1 
ATOM   15678 C  CG2   . ILE D 2 303 ? 154.155 115.660 143.161 1.00 35.47 ?  282 ILE D CG2   1 
ATOM   15679 C  CD1   . ILE D 2 303 ? 154.176 113.487 141.195 1.00 36.30 ?  282 ILE D CD1   1 
ATOM   15680 N  N     . ASN D 2 304 ? 158.329 114.298 142.489 1.00 29.53 ?  283 ASN D N     1 
ATOM   15681 C  CA    . ASN D 2 304 ? 159.340 114.365 141.437 1.00 28.49 ?  283 ASN D CA    1 
ATOM   15682 C  C     . ASN D 2 304 ? 158.818 115.121 140.197 1.00 27.87 ?  283 ASN D C     1 
ATOM   15683 O  O     . ASN D 2 304 ? 157.777 114.761 139.648 1.00 27.02 ?  283 ASN D O     1 
ATOM   15684 C  CB    . ASN D 2 304 ? 159.790 112.953 141.054 1.00 28.20 ?  283 ASN D CB    1 
ATOM   15685 C  CG    . ASN D 2 304 ? 160.900 112.960 140.038 1.00 28.17 ?  283 ASN D CG    1 
ATOM   15686 O  OD1   . ASN D 2 304 ? 160.650 113.034 138.839 1.00 29.01 ?  283 ASN D OD1   1 
ATOM   15687 N  ND2   . ASN D 2 304 ? 162.136 112.882 140.506 1.00 27.24 ?  283 ASN D ND2   1 
ATOM   15688 N  N     . PRO D 2 305 ? 159.532 116.180 139.764 1.00 28.00 ?  284 PRO D N     1 
ATOM   15689 C  CA    . PRO D 2 305 ? 159.039 117.023 138.664 1.00 27.58 ?  284 PRO D CA    1 
ATOM   15690 C  C     . PRO D 2 305 ? 158.966 116.322 137.306 1.00 27.01 ?  284 PRO D C     1 
ATOM   15691 O  O     . PRO D 2 305 ? 158.179 116.726 136.455 1.00 26.66 ?  284 PRO D O     1 
ATOM   15692 C  CB    . PRO D 2 305 ? 160.048 118.179 138.614 1.00 28.21 ?  284 PRO D CB    1 
ATOM   15693 C  CG    . PRO D 2 305 ? 161.247 117.689 139.298 1.00 28.80 ?  284 PRO D CG    1 
ATOM   15694 C  CD    . PRO D 2 305 ? 160.753 116.744 140.371 1.00 28.11 ?  284 PRO D CD    1 
ATOM   15695 N  N     . ILE D 2 306 ? 159.771 115.283 137.108 1.00 26.52 ?  285 ILE D N     1 
ATOM   15696 C  CA    . ILE D 2 306 ? 159.727 114.521 135.866 1.00 26.50 ?  285 ILE D CA    1 
ATOM   15697 C  C     . ILE D 2 306 ? 158.420 113.720 135.790 1.00 26.43 ?  285 ILE D C     1 
ATOM   15698 O  O     . ILE D 2 306 ? 157.708 113.750 134.776 1.00 26.00 ?  285 ILE D O     1 
ATOM   15699 C  CB    . ILE D 2 306 ? 160.977 113.623 135.694 1.00 26.88 ?  285 ILE D CB    1 
ATOM   15700 C  CG1   . ILE D 2 306 ? 162.245 114.496 135.665 1.00 26.98 ?  285 ILE D CG1   1 
ATOM   15701 C  CG2   . ILE D 2 306 ? 160.841 112.771 134.432 1.00 24.94 ?  285 ILE D CG2   1 
ATOM   15702 C  CD1   . ILE D 2 306 ? 163.544 113.737 135.691 1.00 26.65 ?  285 ILE D CD1   1 
ATOM   15703 N  N     . VAL D 2 307 ? 158.097 113.035 136.882 1.00 26.36 ?  286 VAL D N     1 
ATOM   15704 C  CA    . VAL D 2 307 ? 156.810 112.364 137.016 1.00 26.71 ?  286 VAL D CA    1 
ATOM   15705 C  C     . VAL D 2 307 ? 155.643 113.351 136.909 1.00 27.68 ?  286 VAL D C     1 
ATOM   15706 O  O     . VAL D 2 307 ? 154.658 113.054 136.234 1.00 27.92 ?  286 VAL D O     1 
ATOM   15707 C  CB    . VAL D 2 307 ? 156.744 111.504 138.307 1.00 26.37 ?  286 VAL D CB    1 
ATOM   15708 C  CG1   . VAL D 2 307 ? 155.317 111.001 138.579 1.00 25.48 ?  286 VAL D CG1   1 
ATOM   15709 C  CG2   . VAL D 2 307 ? 157.671 110.340 138.163 1.00 25.55 ?  286 VAL D CG2   1 
ATOM   15710 N  N     . LEU D 2 308 ? 155.761 114.529 137.529 1.00 28.80 ?  287 LEU D N     1 
ATOM   15711 C  CA    . LEU D 2 308 ? 154.733 115.570 137.362 1.00 30.07 ?  287 LEU D CA    1 
ATOM   15712 C  C     . LEU D 2 308 ? 154.537 115.973 135.896 1.00 30.38 ?  287 LEU D C     1 
ATOM   15713 O  O     . LEU D 2 308 ? 153.405 116.151 135.435 1.00 30.71 ?  287 LEU D O     1 
ATOM   15714 C  CB    . LEU D 2 308 ? 155.039 116.807 138.211 1.00 30.86 ?  287 LEU D CB    1 
ATOM   15715 C  CG    . LEU D 2 308 ? 154.574 116.746 139.670 1.00 32.62 ?  287 LEU D CG    1 
ATOM   15716 C  CD1   . LEU D 2 308 ? 155.109 117.925 140.453 1.00 33.97 ?  287 LEU D CD1   1 
ATOM   15717 C  CD2   . LEU D 2 308 ? 153.039 116.676 139.771 1.00 34.73 ?  287 LEU D CD2   1 
ATOM   15718 N  N     . ASN D 2 309 ? 155.637 116.106 135.163 1.00 30.81 ?  288 ASN D N     1 
ATOM   15719 C  CA    . ASN D 2 309 ? 155.558 116.438 133.745 1.00 31.25 ?  288 ASN D CA    1 
ATOM   15720 C  C     . ASN D 2 309 ? 154.871 115.332 132.942 1.00 31.83 ?  288 ASN D C     1 
ATOM   15721 O  O     . ASN D 2 309 ? 154.161 115.610 131.972 1.00 31.73 ?  288 ASN D O     1 
ATOM   15722 C  CB    . ASN D 2 309 ? 156.939 116.766 133.166 1.00 31.21 ?  288 ASN D CB    1 
ATOM   15723 C  CG    . ASN D 2 309 ? 156.856 117.307 131.747 1.00 31.41 ?  288 ASN D CG    1 
ATOM   15724 O  OD1   . ASN D 2 309 ? 156.010 118.156 131.444 1.00 31.88 ?  288 ASN D OD1   1 
ATOM   15725 N  ND2   . ASN D 2 309 ? 157.724 116.814 130.870 1.00 29.12 ?  288 ASN D ND2   1 
ATOM   15726 N  N     . GLY D 2 310 ? 155.083 114.084 133.360 1.00 32.04 ?  289 GLY D N     1 
ATOM   15727 C  CA    . GLY D 2 310 ? 154.374 112.942 132.793 1.00 33.04 ?  289 GLY D CA    1 
ATOM   15728 C  C     . GLY D 2 310 ? 152.883 113.006 133.096 1.00 33.85 ?  289 GLY D C     1 
ATOM   15729 O  O     . GLY D 2 310 ? 152.058 112.829 132.199 1.00 34.05 ?  289 GLY D O     1 
ATOM   15730 N  N     . LEU D 2 311 ? 152.543 113.261 134.359 1.00 34.33 ?  290 LEU D N     1 
ATOM   15731 C  CA    . LEU D 2 311 ? 151.150 113.332 134.810 1.00 35.77 ?  290 LEU D CA    1 
ATOM   15732 C  C     . LEU D 2 311 ? 150.350 114.438 134.129 1.00 37.01 ?  290 LEU D C     1 
ATOM   15733 O  O     . LEU D 2 311 ? 149.185 114.243 133.779 1.00 37.18 ?  290 LEU D O     1 
ATOM   15734 C  CB    . LEU D 2 311 ? 151.084 113.545 136.327 1.00 35.50 ?  290 LEU D CB    1 
ATOM   15735 C  CG    . LEU D 2 311 ? 151.034 112.371 137.300 1.00 35.45 ?  290 LEU D CG    1 
ATOM   15736 C  CD1   . LEU D 2 311 ? 151.167 112.901 138.737 1.00 35.28 ?  290 LEU D CD1   1 
ATOM   15737 C  CD2   . LEU D 2 311 ? 149.754 111.546 137.150 1.00 34.16 ?  290 LEU D CD2   1 
ATOM   15738 N  N     . LYS D 2 330 ? 117.722 117.668 149.367 1.00 61.72 ?  309 LYS D N     1 
ATOM   15739 C  CA    . LYS D 2 330 ? 116.424 117.007 149.366 1.00 61.83 ?  309 LYS D CA    1 
ATOM   15740 C  C     . LYS D 2 330 ? 116.085 116.471 150.750 1.00 62.21 ?  309 LYS D C     1 
ATOM   15741 O  O     . LYS D 2 330 ? 116.335 115.299 151.036 1.00 61.32 ?  309 LYS D O     1 
ATOM   15742 C  CB    . LYS D 2 330 ? 116.402 115.853 148.359 1.00 59.60 ?  309 LYS D CB    1 
ATOM   15743 C  CG    . LYS D 2 330 ? 116.973 116.177 146.992 1.00 60.95 ?  309 LYS D CG    1 
ATOM   15744 C  CD    . LYS D 2 330 ? 115.948 115.939 145.896 1.00 60.77 ?  309 LYS D CD    1 
ATOM   15745 C  CE    . LYS D 2 330 ? 116.363 116.607 144.596 1.00 61.40 ?  309 LYS D CE    1 
ATOM   15746 N  NZ    . LYS D 2 330 ? 115.551 117.819 144.304 1.00 62.04 1  309 LYS D NZ    1 
ATOM   15747 N  N     . ALA D 2 331 ? 115.529 117.312 151.621 1.00 57.72 ?  310 ALA D N     1 
ATOM   15748 C  CA    . ALA D 2 331 ? 115.148 116.828 152.940 1.00 58.04 ?  310 ALA D CA    1 
ATOM   15749 C  C     . ALA D 2 331 ? 113.793 116.132 152.932 1.00 58.14 ?  310 ALA D C     1 
ATOM   15750 O  O     . ALA D 2 331 ? 113.730 114.909 153.094 1.00 58.87 ?  310 ALA D O     1 
ATOM   15751 C  CB    . ALA D 2 331 ? 115.135 117.988 153.942 1.00 56.57 ?  310 ALA D CB    1 
ATOM   15752 N  N     . THR D 2 332 ? 112.707 116.886 152.742 1.00 46.15 ?  311 THR D N     1 
ATOM   15753 C  CA    . THR D 2 332 ? 111.392 116.338 152.422 1.00 42.78 ?  311 THR D CA    1 
ATOM   15754 C  C     . THR D 2 332 ? 110.438 117.450 151.995 1.00 42.27 ?  311 THR D C     1 
ATOM   15755 O  O     . THR D 2 332 ? 110.116 118.336 152.794 1.00 45.09 ?  311 THR D O     1 
ATOM   15756 C  CB    . THR D 2 332 ? 110.824 115.541 153.604 1.00 46.86 ?  311 THR D CB    1 
ATOM   15757 O  OG1   . THR D 2 332 ? 109.639 114.842 153.201 1.00 46.97 ?  311 THR D OG1   1 
ATOM   15758 C  CG2   . THR D 2 332 ? 110.548 116.437 154.795 1.00 43.65 ?  311 THR D CG2   1 
ATOM   15759 N  N     . VAL D 2 333 ? 109.977 117.417 150.746 1.00 39.49 ?  312 VAL D N     1 
ATOM   15760 C  CA    . VAL D 2 333 ? 109.030 118.413 150.257 1.00 35.97 ?  312 VAL D CA    1 
ATOM   15761 C  C     . VAL D 2 333 ? 107.692 118.228 150.961 1.00 40.19 ?  312 VAL D C     1 
ATOM   15762 O  O     . VAL D 2 333 ? 107.117 117.133 150.945 1.00 43.38 ?  312 VAL D O     1 
ATOM   15763 C  CB    . VAL D 2 333 ? 108.866 118.326 148.728 1.00 38.60 ?  312 VAL D CB    1 
ATOM   15764 C  CG1   . VAL D 2 333 ? 107.534 118.924 148.294 1.00 39.63 ?  312 VAL D CG1   1 
ATOM   15765 C  CG2   . VAL D 2 333 ? 110.020 119.025 148.030 1.00 39.03 ?  312 VAL D CG2   1 
ATOM   15766 N  N     . GLU D 2 334 ? 107.191 119.290 151.590 1.00 39.20 ?  313 GLU D N     1 
ATOM   15767 C  CA    . GLU D 2 334 ? 105.867 119.285 152.205 1.00 36.81 ?  313 GLU D CA    1 
ATOM   15768 C  C     . GLU D 2 334 ? 105.154 120.568 151.798 1.00 37.73 ?  313 GLU D C     1 
ATOM   15769 O  O     . GLU D 2 334 ? 105.744 121.662 151.906 1.00 40.12 ?  313 GLU D O     1 
ATOM   15770 C  CB    . GLU D 2 334 ? 105.946 119.162 153.728 1.00 34.61 ?  313 GLU D CB    1 
ATOM   15771 C  CG    . GLU D 2 334 ? 104.586 118.981 154.384 1.00 37.90 ?  313 GLU D CG    1 
ATOM   15772 C  CD    . GLU D 2 334 ? 104.662 118.834 155.890 1.00 39.43 ?  313 GLU D CD    1 
ATOM   15773 O  OE1   . GLU D 2 334 ? 105.783 118.752 156.426 1.00 37.54 ?  313 GLU D OE1   1 
ATOM   15774 O  OE2   . GLU D 2 334 ? 103.597 118.796 156.539 1.00 39.69 -1 313 GLU D OE2   1 
ATOM   15775 N  N     . PRO D 2 335 ? 103.912 120.495 151.326 1.00 38.18 ?  314 PRO D N     1 
ATOM   15776 C  CA    . PRO D 2 335 ? 103.215 121.710 150.895 1.00 40.62 ?  314 PRO D CA    1 
ATOM   15777 C  C     . PRO D 2 335 ? 102.826 122.595 152.068 1.00 40.02 ?  314 PRO D C     1 
ATOM   15778 O  O     . PRO D 2 335 ? 102.675 122.138 153.203 1.00 41.11 ?  314 PRO D O     1 
ATOM   15779 C  CB    . PRO D 2 335 ? 101.975 121.167 150.178 1.00 37.91 ?  314 PRO D CB    1 
ATOM   15780 C  CG    . PRO D 2 335 ? 101.731 119.847 150.828 1.00 34.58 ?  314 PRO D CG    1 
ATOM   15781 C  CD    . PRO D 2 335 ? 103.095 119.287 151.120 1.00 36.60 ?  314 PRO D CD    1 
ATOM   15782 N  N     . LEU D 2 336 ? 102.674 123.885 151.778 1.00 34.57 ?  315 LEU D N     1 
ATOM   15783 C  CA    . LEU D 2 336 ? 102.126 124.824 152.745 1.00 30.08 ?  315 LEU D CA    1 
ATOM   15784 C  C     . LEU D 2 336 ? 100.612 124.668 152.792 1.00 33.20 ?  315 LEU D C     1 
ATOM   15785 O  O     . LEU D 2 336 ? 99.926  124.884 151.788 1.00 37.22 ?  315 LEU D O     1 
ATOM   15786 C  CB    . LEU D 2 336 ? 102.504 126.257 152.369 1.00 28.04 ?  315 LEU D CB    1 
ATOM   15787 C  CG    . LEU D 2 336 ? 103.923 126.714 152.709 1.00 27.76 ?  315 LEU D CG    1 
ATOM   15788 C  CD1   . LEU D 2 336 ? 104.351 127.850 151.794 1.00 24.11 ?  315 LEU D CD1   1 
ATOM   15789 C  CD2   . LEU D 2 336 ? 104.010 127.136 154.164 1.00 29.08 ?  315 LEU D CD2   1 
ATOM   15790 N  N     . LYS D 2 337 ? 100.090 124.295 153.959 1.00 36.25 ?  316 LYS D N     1 
ATOM   15791 C  CA    . LYS D 2 337 ? 98.684  123.935 154.108 1.00 47.76 ?  316 LYS D CA    1 
ATOM   15792 C  C     . LYS D 2 337 ? 97.889  125.034 154.804 1.00 47.26 ?  316 LYS D C     1 
ATOM   15793 O  O     . LYS D 2 337 ? 96.970  124.745 155.575 1.00 51.37 ?  316 LYS D O     1 
ATOM   15794 C  CB    . LYS D 2 337 ? 98.545  122.617 154.866 1.00 44.37 ?  316 LYS D CB    1 
ATOM   15795 C  CG    . LYS D 2 337 ? 99.510  122.474 156.030 1.00 46.03 ?  316 LYS D CG    1 
ATOM   15796 C  CD    . LYS D 2 337 ? 99.949  121.031 156.215 1.00 46.40 ?  316 LYS D CD    1 
ATOM   15797 C  CE    . LYS D 2 337 ? 100.481 120.447 154.917 1.00 45.29 ?  316 LYS D CE    1 
ATOM   15798 N  NZ    . LYS D 2 337 ? 101.329 119.249 155.153 1.00 42.09 1  316 LYS D NZ    1 
ATOM   15799 N  N     . ASP D 2 338 ? 98.240  126.295 154.542 1.00 29.55 ?  317 ASP D N     1 
ATOM   15800 C  CA    . ASP D 2 338 ? 97.603  127.458 155.153 1.00 32.48 ?  317 ASP D CA    1 
ATOM   15801 C  C     . ASP D 2 338 ? 97.776  127.465 156.668 1.00 37.94 ?  317 ASP D C     1 
ATOM   15802 O  O     . ASP D 2 338 ? 98.236  126.479 157.255 1.00 40.84 ?  317 ASP D O     1 
ATOM   15803 C  CB    . ASP D 2 338 ? 96.118  127.526 154.785 1.00 36.01 ?  317 ASP D CB    1 
ATOM   15804 C  CG    . ASP D 2 338 ? 95.591  128.944 154.768 1.00 38.86 ?  317 ASP D CG    1 
ATOM   15805 O  OD1   . ASP D 2 338 ? 96.391  129.875 155.002 1.00 36.19 ?  317 ASP D OD1   1 
ATOM   15806 O  OD2   . ASP D 2 338 ? 94.381  129.130 154.522 1.00 34.94 -1 317 ASP D OD2   1 
ATOM   15807 N  N     . ASP D 2 339 ? 97.459  128.601 157.297 1.00 32.37 ?  318 ASP D N     1 
ATOM   15808 C  CA    . ASP D 2 339 ? 97.660  128.829 158.727 1.00 28.49 ?  318 ASP D CA    1 
ATOM   15809 C  C     . ASP D 2 339 ? 99.148  128.873 159.056 1.00 28.80 ?  318 ASP D C     1 
ATOM   15810 O  O     . ASP D 2 339 ? 99.531  129.132 160.201 1.00 36.28 ?  318 ASP D O     1 
ATOM   15811 C  CB    . ASP D 2 339 ? 96.947  127.768 159.570 1.00 30.55 ?  318 ASP D CB    1 
ATOM   15812 C  CG    . ASP D 2 339 ? 96.095  128.375 160.668 1.00 37.05 ?  318 ASP D CG    1 
ATOM   15813 O  OD1   . ASP D 2 339 ? 96.468  129.449 161.186 1.00 32.14 ?  318 ASP D OD1   1 
ATOM   15814 O  OD2   . ASP D 2 339 ? 95.052  127.779 161.013 1.00 39.30 -1 318 ASP D OD2   1 
ATOM   15815 N  N     . ASP D 2 340 ? 99.991  128.622 158.055 1.00 24.72 ?  319 ASP D N     1 
ATOM   15816 C  CA    . ASP D 2 340 ? 101.420 128.867 158.145 1.00 24.52 ?  319 ASP D CA    1 
ATOM   15817 C  C     . ASP D 2 340 ? 101.775 130.302 157.793 1.00 21.51 ?  319 ASP D C     1 
ATOM   15818 O  O     . ASP D 2 340 ? 102.915 130.720 158.019 1.00 32.71 ?  319 ASP D O     1 
ATOM   15819 C  CB    . ASP D 2 340 ? 102.179 127.908 157.222 1.00 23.05 ?  319 ASP D CB    1 
ATOM   15820 C  CG    . ASP D 2 340 ? 102.083 126.465 157.674 1.00 28.00 ?  319 ASP D CG    1 
ATOM   15821 O  OD1   . ASP D 2 340 ? 101.983 126.226 158.896 1.00 34.28 ?  319 ASP D OD1   1 
ATOM   15822 O  OD2   . ASP D 2 340 ? 102.106 125.566 156.808 1.00 31.08 -1 319 ASP D OD2   1 
ATOM   15823 N  N     . PHE D 2 341 ? 100.825 131.054 157.241 1.00 10.52 ?  320 PHE D N     1 
ATOM   15824 C  CA    . PHE D 2 341 ? 100.989 132.468 156.948 1.00 15.27 ?  320 PHE D CA    1 
ATOM   15825 C  C     . PHE D 2 341 ? 100.440 133.352 158.055 1.00 12.85 ?  320 PHE D C     1 
ATOM   15826 O  O     . PHE D 2 341 ? 100.483 134.580 157.931 1.00 22.40 ?  320 PHE D O     1 
ATOM   15827 C  CB    . PHE D 2 341 ? 100.298 132.812 155.625 1.00 21.01 ?  320 PHE D CB    1 
ATOM   15828 C  CG    . PHE D 2 341 ? 100.860 132.085 154.435 1.00 15.79 ?  320 PHE D CG    1 
ATOM   15829 C  CD1   . PHE D 2 341 ? 100.425 130.811 154.119 1.00 11.88 ?  320 PHE D CD1   1 
ATOM   15830 C  CD2   . PHE D 2 341 ? 101.815 132.679 153.631 1.00 9.87  ?  320 PHE D CD2   1 
ATOM   15831 C  CE1   . PHE D 2 341 ? 100.937 130.141 153.028 1.00 13.02 ?  320 PHE D CE1   1 
ATOM   15832 C  CE2   . PHE D 2 341 ? 102.330 132.013 152.537 1.00 10.78 ?  320 PHE D CE2   1 
ATOM   15833 C  CZ    . PHE D 2 341 ? 101.891 130.743 152.237 1.00 4.79  ?  320 PHE D CZ    1 
ATOM   15834 N  N     . TYR D 2 342 ? 99.926  132.758 159.128 1.00 12.46 ?  321 TYR D N     1 
ATOM   15835 C  CA    . TYR D 2 342 ? 99.336  133.490 160.237 1.00 17.95 ?  321 TYR D CA    1 
ATOM   15836 C  C     . TYR D 2 342 ? 100.031 133.081 161.524 1.00 22.41 ?  321 TYR D C     1 
ATOM   15837 O  O     . TYR D 2 342 ? 100.351 131.905 161.719 1.00 24.04 ?  321 TYR D O     1 
ATOM   15838 C  CB    . TYR D 2 342 ? 97.833  133.221 160.339 1.00 13.28 ?  321 TYR D CB    1 
ATOM   15839 C  CG    . TYR D 2 342 ? 97.052  133.683 159.131 1.00 11.63 ?  321 TYR D CG    1 
ATOM   15840 C  CD1   . TYR D 2 342 ? 96.636  135.002 159.011 1.00 16.81 ?  321 TYR D CD1   1 
ATOM   15841 C  CD2   . TYR D 2 342 ? 96.737  132.801 158.107 1.00 15.94 ?  321 TYR D CD2   1 
ATOM   15842 C  CE1   . TYR D 2 342 ? 95.924  135.427 157.906 1.00 20.80 ?  321 TYR D CE1   1 
ATOM   15843 C  CE2   . TYR D 2 342 ? 96.027  133.216 156.999 1.00 15.55 ?  321 TYR D CE2   1 
ATOM   15844 C  CZ    . TYR D 2 342 ? 95.623  134.530 156.904 1.00 24.69 ?  321 TYR D CZ    1 
ATOM   15845 O  OH    . TYR D 2 342 ? 94.913  134.951 155.802 1.00 21.45 ?  321 TYR D OH    1 
ATOM   15846 N  N     . PHE D 2 343 ? 100.270 134.054 162.395 1.00 12.93 ?  322 PHE D N     1 
ATOM   15847 C  CA    . PHE D 2 343 ? 100.996 133.807 163.635 1.00 18.66 ?  322 PHE D CA    1 
ATOM   15848 C  C     . PHE D 2 343 ? 100.337 134.523 164.808 1.00 24.79 ?  322 PHE D C     1 
ATOM   15849 O  O     . PHE D 2 343 ? 100.023 135.709 164.730 1.00 23.91 ?  322 PHE D O     1 
ATOM   15850 C  CB    . PHE D 2 343 ? 102.457 134.249 163.496 1.00 13.99 ?  322 PHE D CB    1 
ATOM   15851 C  CG    . PHE D 2 343 ? 103.098 133.824 162.206 1.00 14.21 ?  322 PHE D CG    1 
ATOM   15852 C  CD1   . PHE D 2 343 ? 103.049 134.639 161.088 1.00 13.48 ?  322 PHE D CD1   1 
ATOM   15853 C  CD2   . PHE D 2 343 ? 103.746 132.606 162.110 1.00 16.65 ?  322 PHE D CD2   1 
ATOM   15854 C  CE1   . PHE D 2 343 ? 103.633 134.246 159.902 1.00 9.34  ?  322 PHE D CE1   1 
ATOM   15855 C  CE2   . PHE D 2 343 ? 104.330 132.209 160.925 1.00 9.50  ?  322 PHE D CE2   1 
ATOM   15856 C  CZ    . PHE D 2 343 ? 104.273 133.031 159.822 1.00 5.03  ?  322 PHE D CZ    1 
HETATM 15857 P  PA    . TTP E 3 .   ? 146.143 143.923 134.214 1.00 19.37 ?  801 TTP A PA    1 
HETATM 15858 O  O1A   . TTP E 3 .   ? 144.721 144.410 134.125 1.00 21.91 -1 801 TTP A O1A   1 
HETATM 15859 O  O2A   . TTP E 3 .   ? 147.039 144.717 133.297 1.00 26.56 ?  801 TTP A O2A   1 
HETATM 15860 O  O3A   . TTP E 3 .   ? 146.649 143.926 135.738 1.00 35.02 ?  801 TTP A O3A   1 
HETATM 15861 P  PB    . TTP E 3 .   ? 147.762 144.961 136.263 1.00 29.77 ?  801 TTP A PB    1 
HETATM 15862 O  O1B   . TTP E 3 .   ? 147.426 145.395 137.666 1.00 33.96 -1 801 TTP A O1B   1 
HETATM 15863 O  O2B   . TTP E 3 .   ? 147.918 146.164 135.369 1.00 25.37 ?  801 TTP A O2B   1 
HETATM 15864 O  O3B   . TTP E 3 .   ? 149.066 144.019 136.245 1.00 28.38 ?  801 TTP A O3B   1 
HETATM 15865 P  PG    . TTP E 3 .   ? 150.421 144.450 135.494 1.00 32.16 ?  801 TTP A PG    1 
HETATM 15866 O  O1G   . TTP E 3 .   ? 150.104 144.995 134.123 1.00 33.52 ?  801 TTP A O1G   1 
HETATM 15867 O  O2G   . TTP E 3 .   ? 151.301 143.235 135.354 1.00 23.47 -1 801 TTP A O2G   1 
HETATM 15868 O  O3G   . TTP E 3 .   ? 151.145 145.501 136.296 1.00 34.78 ?  801 TTP A O3G   1 
HETATM 15869 O  "O5'" . TTP E 3 .   ? 146.236 142.365 133.851 1.00 18.77 ?  801 TTP A "O5'" 1 
HETATM 15870 C  "C5'" . TTP E 3 .   ? 147.146 141.960 132.836 1.00 25.04 ?  801 TTP A "C5'" 1 
HETATM 15871 C  "C4'" . TTP E 3 .   ? 146.908 140.504 132.474 1.00 26.93 ?  801 TTP A "C4'" 1 
HETATM 15872 O  "O4'" . TTP E 3 .   ? 146.578 139.760 133.645 1.00 30.38 ?  801 TTP A "O4'" 1 
HETATM 15873 C  "C3'" . TTP E 3 .   ? 145.741 140.370 131.517 1.00 25.75 ?  801 TTP A "C3'" 1 
HETATM 15874 O  "O3'" . TTP E 3 .   ? 146.210 140.047 130.206 1.00 30.86 ?  801 TTP A "O3'" 1 
HETATM 15875 C  "C2'" . TTP E 3 .   ? 144.900 139.235 132.058 1.00 28.56 ?  801 TTP A "C2'" 1 
HETATM 15876 C  "C1'" . TTP E 3 .   ? 145.569 138.793 133.349 1.00 25.58 ?  801 TTP A "C1'" 1 
HETATM 15877 N  N1    . TTP E 3 .   ? 144.587 138.747 134.432 1.00 26.58 ?  801 TTP A N1    1 
HETATM 15878 C  C2    . TTP E 3 .   ? 143.998 137.514 134.785 1.00 30.61 ?  801 TTP A C2    1 
HETATM 15879 O  O2    . TTP E 3 .   ? 144.331 136.480 134.169 1.00 27.38 ?  801 TTP A O2    1 
HETATM 15880 N  N3    . TTP E 3 .   ? 143.097 137.426 135.771 1.00 28.52 ?  801 TTP A N3    1 
HETATM 15881 C  C4    . TTP E 3 .   ? 142.728 138.516 136.446 1.00 31.97 ?  801 TTP A C4    1 
HETATM 15882 O  O4    . TTP E 3 .   ? 141.887 138.436 137.365 1.00 33.14 ?  801 TTP A O4    1 
HETATM 15883 C  C5    . TTP E 3 .   ? 143.329 139.822 136.092 1.00 26.42 ?  801 TTP A C5    1 
HETATM 15884 C  C5M   . TTP E 3 .   ? 142.939 141.071 136.832 1.00 26.94 ?  801 TTP A C5M   1 
HETATM 15885 C  C6    . TTP E 3 .   ? 144.260 139.874 135.067 1.00 25.12 ?  801 TTP A C6    1 
HETATM 15886 MG MG    . MG  F 4 .   ? 148.330 146.265 132.935 1.00 24.14 ?  802 MG  A MG    1 
HETATM 15887 P  PG    . ATP G 5 .   ? 108.453 133.672 77.989  1.00 73.57 ?  803 ATP A PG    1 
HETATM 15888 O  O1G   . ATP G 5 .   ? 108.917 134.582 76.904  1.00 63.77 ?  803 ATP A O1G   1 
HETATM 15889 O  O2G   . ATP G 5 .   ? 107.920 132.328 77.480  1.00 64.13 -1 803 ATP A O2G   1 
HETATM 15890 O  O3G   . ATP G 5 .   ? 109.508 133.416 79.071  1.00 61.47 ?  803 ATP A O3G   1 
HETATM 15891 P  PB    . ATP G 5 .   ? 106.922 135.134 80.111  1.00 71.75 ?  803 ATP A PB    1 
HETATM 15892 O  O1B   . ATP G 5 .   ? 107.734 136.364 80.196  1.00 63.94 -1 803 ATP A O1B   1 
HETATM 15893 O  O2B   . ATP G 5 .   ? 105.409 135.343 80.188  1.00 62.90 ?  803 ATP A O2B   1 
HETATM 15894 O  O3B   . ATP G 5 .   ? 107.220 134.319 78.777  1.00 66.82 ?  803 ATP A O3B   1 
HETATM 15895 P  PA    . ATP G 5 .   ? 106.564 132.988 82.123  1.00 70.68 ?  803 ATP A PA    1 
HETATM 15896 O  O1A   . ATP G 5 .   ? 107.207 131.662 82.018  1.00 64.00 -1 803 ATP A O1A   1 
HETATM 15897 O  O2A   . ATP G 5 .   ? 105.089 133.014 81.724  1.00 62.49 ?  803 ATP A O2A   1 
HETATM 15898 O  O3A   . ATP G 5 .   ? 107.316 134.077 81.235  1.00 63.22 ?  803 ATP A O3A   1 
HETATM 15899 O  "O5'" . ATP G 5 .   ? 106.692 133.581 83.581  1.00 62.47 ?  803 ATP A "O5'" 1 
HETATM 15900 C  "C5'" . ATP G 5 .   ? 105.816 134.633 84.039  1.00 61.67 ?  803 ATP A "C5'" 1 
HETATM 15901 C  "C4'" . ATP G 5 .   ? 106.533 135.446 85.086  1.00 61.88 ?  803 ATP A "C4'" 1 
HETATM 15902 O  "O4'" . ATP G 5 .   ? 107.025 134.573 86.125  1.00 63.84 ?  803 ATP A "O4'" 1 
HETATM 15903 C  "C3'" . ATP G 5 .   ? 107.758 136.207 84.593  1.00 60.84 ?  803 ATP A "C3'" 1 
HETATM 15904 O  "O3'" . ATP G 5 .   ? 107.393 137.481 84.075  1.00 63.01 ?  803 ATP A "O3'" 1 
HETATM 15905 C  "C2'" . ATP G 5 .   ? 108.592 136.339 85.867  1.00 62.28 ?  803 ATP A "C2'" 1 
HETATM 15906 O  "O2'" . ATP G 5 .   ? 108.157 137.430 86.670  1.00 61.13 ?  803 ATP A "O2'" 1 
HETATM 15907 C  "C1'" . ATP G 5 .   ? 108.301 135.008 86.567  1.00 61.93 ?  803 ATP A "C1'" 1 
HETATM 15908 N  N9    . ATP G 5 .   ? 109.271 133.957 86.282  1.00 60.22 ?  803 ATP A N9    1 
HETATM 15909 C  C8    . ATP G 5 .   ? 109.025 132.738 85.706  1.00 60.42 ?  803 ATP A C8    1 
HETATM 15910 N  N7    . ATP G 5 .   ? 110.089 131.986 85.569  1.00 60.85 ?  803 ATP A N7    1 
HETATM 15911 C  C5    . ATP G 5 .   ? 111.110 132.763 86.093  1.00 61.63 ?  803 ATP A C5    1 
HETATM 15912 C  C6    . ATP G 5 .   ? 112.492 132.541 86.248  1.00 58.03 ?  803 ATP A C6    1 
HETATM 15913 N  N6    . ATP G 5 .   ? 113.112 131.419 85.869  1.00 57.72 ?  803 ATP A N6    1 
HETATM 15914 N  N1    . ATP G 5 .   ? 113.226 133.523 86.812  1.00 58.44 ?  803 ATP A N1    1 
HETATM 15915 C  C2    . ATP G 5 .   ? 112.616 134.649 87.188  1.00 58.37 ?  803 ATP A C2    1 
HETATM 15916 N  N3    . ATP G 5 .   ? 111.324 134.969 87.098  1.00 61.94 ?  803 ATP A N3    1 
HETATM 15917 C  C4    . ATP G 5 .   ? 110.620 133.981 86.538  1.00 62.47 ?  803 ATP A C4    1 
HETATM 15918 O  O1B   . DGI H 6 .   ? 104.580 150.738 83.939  1.00 65.79 ?  804 DGI A O1B   1 
HETATM 15919 P  PB    . DGI H 6 .   ? 104.708 152.207 84.271  1.00 74.95 ?  804 DGI A PB    1 
HETATM 15920 O  O2B   . DGI H 6 .   ? 103.379 152.934 84.267  1.00 66.56 -1 804 DGI A O2B   1 
HETATM 15921 O  O3B   . DGI H 6 .   ? 105.764 152.912 83.446  1.00 66.82 ?  804 DGI A O3B   1 
HETATM 15922 O  O3A   . DGI H 6 .   ? 105.235 152.206 85.811  1.00 67.64 ?  804 DGI A O3A   1 
HETATM 15923 P  PA    . DGI H 6 .   ? 105.137 151.365 87.168  1.00 72.66 ?  804 DGI A PA    1 
HETATM 15924 O  O1A   . DGI H 6 .   ? 105.279 152.283 88.317  1.00 65.42 -1 804 DGI A O1A   1 
HETATM 15925 O  O2A   . DGI H 6 .   ? 103.955 150.473 87.096  1.00 66.08 ?  804 DGI A O2A   1 
HETATM 15926 O  "O5'" . DGI H 6 .   ? 106.466 150.485 87.084  1.00 64.30 ?  804 DGI A "O5'" 1 
HETATM 15927 C  "C5'" . DGI H 6 .   ? 107.729 151.118 86.797  1.00 63.95 ?  804 DGI A "C5'" 1 
HETATM 15928 C  "C4'" . DGI H 6 .   ? 108.844 150.140 87.067  1.00 63.55 ?  804 DGI A "C4'" 1 
HETATM 15929 O  "O4'" . DGI H 6 .   ? 108.781 149.700 88.443  1.00 62.06 ?  804 DGI A "O4'" 1 
HETATM 15930 C  "C3'" . DGI H 6 .   ? 108.821 148.876 86.200  1.00 64.87 ?  804 DGI A "C3'" 1 
HETATM 15931 O  "O3'" . DGI H 6 .   ? 110.121 148.613 85.672  1.00 62.86 ?  804 DGI A "O3'" 1 
HETATM 15932 C  "C2'" . DGI H 6 .   ? 108.404 147.781 87.174  1.00 62.93 ?  804 DGI A "C2'" 1 
HETATM 15933 C  "C1'" . DGI H 6 .   ? 108.945 148.298 88.491  1.00 59.66 ?  804 DGI A "C1'" 1 
HETATM 15934 N  N9    . DGI H 6 .   ? 108.232 147.792 89.680  1.00 62.34 ?  804 DGI A N9    1 
HETATM 15935 C  C8    . DGI H 6 .   ? 108.779 147.162 90.764  1.00 63.25 ?  804 DGI A C8    1 
HETATM 15936 N  N7    . DGI H 6 .   ? 107.890 146.810 91.662  1.00 62.94 ?  804 DGI A N7    1 
HETATM 15937 C  C5    . DGI H 6 .   ? 106.683 147.236 91.135  1.00 64.85 ?  804 DGI A C5    1 
HETATM 15938 C  C4    . DGI H 6 .   ? 106.877 147.844 89.913  1.00 64.28 ?  804 DGI A C4    1 
HETATM 15939 N  N3    . DGI H 6 .   ? 105.955 148.387 89.099  1.00 64.32 ?  804 DGI A N3    1 
HETATM 15940 C  C2    . DGI H 6 .   ? 104.721 148.295 89.586  1.00 62.71 ?  804 DGI A C2    1 
HETATM 15941 N  N2    . DGI H 6 .   ? 103.696 148.792 88.891  1.00 63.01 ?  804 DGI A N2    1 
HETATM 15942 N  N1    . DGI H 6 .   ? 104.428 147.708 90.788  1.00 63.42 ?  804 DGI A N1    1 
HETATM 15943 C  C6    . DGI H 6 .   ? 105.353 147.143 91.645  1.00 64.23 ?  804 DGI A C6    1 
HETATM 15944 O  O6    . DGI H 6 .   ? 104.995 146.635 92.707  1.00 64.17 ?  804 DGI A O6    1 
HETATM 15945 P  PA    . TTP I 3 .   ? 119.635 146.801 124.136 1.00 22.87 ?  801 TTP B PA    1 
HETATM 15946 O  O1A   . TTP I 3 .   ? 120.993 146.315 123.703 1.00 21.90 -1 801 TTP B O1A   1 
HETATM 15947 O  O2A   . TTP I 3 .   ? 119.722 148.195 124.703 1.00 27.07 ?  801 TTP B O2A   1 
HETATM 15948 O  O3A   . TTP I 3 .   ? 118.576 146.751 122.927 1.00 36.80 ?  801 TTP B O3A   1 
HETATM 15949 P  PB    . TTP I 3 .   ? 118.537 147.865 121.769 1.00 32.44 ?  801 TTP B PB    1 
HETATM 15950 O  O1B   . TTP I 3 .   ? 119.358 147.433 120.582 1.00 35.04 -1 801 TTP B O1B   1 
HETATM 15951 O  O2B   . TTP I 3 .   ? 118.989 149.215 122.261 1.00 28.12 ?  801 TTP B O2B   1 
HETATM 15952 O  O3B   . TTP I 3 .   ? 116.975 147.891 121.398 1.00 37.21 ?  801 TTP B O3B   1 
HETATM 15953 P  PG    . TTP I 3 .   ? 115.880 148.154 122.548 1.00 30.08 ?  801 TTP B PG    1 
HETATM 15954 O  O1G   . TTP I 3 .   ? 115.404 146.826 123.074 1.00 20.36 ?  801 TTP B O1G   1 
HETATM 15955 O  O2G   . TTP I 3 .   ? 114.700 148.901 121.980 1.00 33.83 -1 801 TTP B O2G   1 
HETATM 15956 O  O3G   . TTP I 3 .   ? 116.499 148.948 123.672 1.00 27.09 ?  801 TTP B O3G   1 
HETATM 15957 O  "O5'" . TTP I 3 .   ? 118.973 145.795 125.199 1.00 24.10 ?  801 TTP B "O5'" 1 
HETATM 15958 C  "C5'" . TTP I 3 .   ? 118.219 144.680 124.737 1.00 22.09 ?  801 TTP B "C5'" 1 
HETATM 15959 C  "C4'" . TTP I 3 .   ? 118.114 143.648 125.847 1.00 23.21 ?  801 TTP B "C4'" 1 
HETATM 15960 O  "O4'" . TTP I 3 .   ? 118.173 142.355 125.247 1.00 35.77 ?  801 TTP B "O4'" 1 
HETATM 15961 C  "C3'" . TTP I 3 .   ? 119.279 143.769 126.809 1.00 25.49 ?  801 TTP B "C3'" 1 
HETATM 15962 O  "O3'" . TTP I 3 .   ? 118.797 143.896 128.148 1.00 27.76 ?  801 TTP B "O3'" 1 
HETATM 15963 C  "C2'" . TTP I 3 .   ? 120.073 142.489 126.676 1.00 25.02 ?  801 TTP B "C2'" 1 
HETATM 15964 C  "C1'" . TTP I 3 .   ? 119.264 141.588 125.758 1.00 28.60 ?  801 TTP B "C1'" 1 
HETATM 15965 N  N1    . TTP I 3 .   ? 120.090 141.127 124.643 1.00 27.06 ?  801 TTP B N1    1 
HETATM 15966 C  C2    . TTP I 3 .   ? 120.214 139.743 124.388 1.00 29.68 ?  801 TTP B C2    1 
HETATM 15967 O  O2    . TTP I 3 .   ? 119.615 138.930 125.123 1.00 27.86 ?  801 TTP B O2    1 
HETATM 15968 N  N3    . TTP I 3 .   ? 120.960 139.286 123.376 1.00 27.67 ?  801 TTP B N3    1 
HETATM 15969 C  C4    . TTP I 3 .   ? 121.610 140.135 122.577 1.00 32.29 ?  801 TTP B C4    1 
HETATM 15970 O  O4    . TTP I 3 .   ? 122.305 139.707 121.633 1.00 35.26 ?  801 TTP B O4    1 
HETATM 15971 C  C5    . TTP I 3 .   ? 121.495 141.591 122.824 1.00 27.29 ?  801 TTP B C5    1 
HETATM 15972 C  C5M   . TTP I 3 .   ? 122.211 142.580 121.946 1.00 27.10 ?  801 TTP B C5M   1 
HETATM 15973 C  C6    . TTP I 3 .   ? 120.714 142.027 123.879 1.00 25.61 ?  801 TTP B C6    1 
HETATM 15974 MG MG    . MG  J 4 .   ? 117.917 149.645 125.061 1.00 27.32 ?  802 MG  B MG    1 
HETATM 15975 P  PG    . ATP K 5 .   ? 155.406 137.807 179.165 1.00 78.28 ?  803 ATP B PG    1 
HETATM 15976 O  O1G   . ATP K 5 .   ? 155.200 138.304 180.555 1.00 64.48 ?  803 ATP B O1G   1 
HETATM 15977 O  O2G   . ATP K 5 .   ? 154.110 137.680 178.359 1.00 66.98 -1 803 ATP B O2G   1 
HETATM 15978 O  O3G   . ATP K 5 .   ? 156.417 138.630 178.360 1.00 64.37 ?  803 ATP B O3G   1 
HETATM 15979 P  PB    . ATP K 5 .   ? 157.369 135.578 179.537 1.00 74.62 ?  803 ATP B PB    1 
HETATM 15980 O  O1B   . ATP K 5 .   ? 158.505 136.083 178.740 1.00 63.94 -1 803 ATP B O1B   1 
HETATM 15981 O  O2B   . ATP K 5 .   ? 157.537 135.647 181.054 1.00 65.48 ?  803 ATP B O2B   1 
HETATM 15982 O  O3B   . ATP K 5 .   ? 156.015 136.330 179.180 1.00 67.90 ?  803 ATP B O3B   1 
HETATM 15983 P  PA    . ATP K 5 .   ? 156.241 133.318 177.999 1.00 74.99 ?  803 ATP B PA    1 
HETATM 15984 O  O1A   . ATP K 5 .   ? 154.892 132.897 178.429 1.00 65.28 -1 803 ATP B O1A   1 
HETATM 15985 O  O2A   . ATP K 5 .   ? 157.152 132.188 177.523 1.00 66.62 ?  803 ATP B O2A   1 
HETATM 15986 O  O3A   . ATP K 5 .   ? 157.008 134.073 179.168 1.00 66.93 ?  803 ATP B O3A   1 
HETATM 15987 O  "O5'" . ATP K 5 .   ? 156.166 134.408 176.860 1.00 63.34 ?  803 ATP B "O5'" 1 
HETATM 15988 C  "C5'" . ATP K 5 .   ? 157.203 134.522 175.864 1.00 62.23 ?  803 ATP B "C5'" 1 
HETATM 15989 C  "C4'" . ATP K 5 .   ? 156.723 135.430 174.761 1.00 64.37 ?  803 ATP B "C4'" 1 
HETATM 15990 O  "O4'" . ATP K 5 .   ? 155.953 134.667 173.807 1.00 66.78 ?  803 ATP B "O4'" 1 
HETATM 15991 C  "C3'" . ATP K 5 .   ? 155.799 136.559 175.204 1.00 61.93 ?  803 ATP B "C3'" 1 
HETATM 15992 O  "O3'" . ATP K 5 .   ? 156.545 137.700 175.610 1.00 65.20 ?  803 ATP B "O3'" 1 
HETATM 15993 C  "C2'" . ATP K 5 .   ? 154.994 136.837 173.934 1.00 61.89 ?  803 ATP B "C2'" 1 
HETATM 15994 O  "O2'" . ATP K 5 .   ? 155.699 137.688 173.039 1.00 64.23 ?  803 ATP B "O2'" 1 
HETATM 15995 C  "C1'" . ATP K 5 .   ? 154.855 135.432 173.339 1.00 63.64 ?  803 ATP B "C1'" 1 
HETATM 15996 N  N9    . ATP K 5 .   ? 153.622 134.745 173.708 1.00 61.39 ?  803 ATP B N9    1 
HETATM 15997 C  C8    . ATP K 5 .   ? 153.501 133.581 174.422 1.00 60.31 ?  803 ATP B C8    1 
HETATM 15998 N  N7    . ATP K 5 .   ? 152.263 133.188 174.602 1.00 61.85 ?  803 ATP B N7    1 
HETATM 15999 C  C5    . ATP K 5 .   ? 151.514 134.162 173.958 1.00 64.90 ?  803 ATP B C5    1 
HETATM 16000 C  C6    . ATP K 5 .   ? 150.128 134.333 173.780 1.00 60.15 ?  803 ATP B C6    1 
HETATM 16001 N  N6    . ATP K 5 .   ? 149.206 133.490 174.257 1.00 59.38 ?  803 ATP B N6    1 
HETATM 16002 N  N1    . ATP K 5 .   ? 149.712 135.414 173.087 1.00 59.56 ?  803 ATP B N1    1 
HETATM 16003 C  C2    . ATP K 5 .   ? 150.625 136.263 172.611 1.00 58.45 ?  803 ATP B C2    1 
HETATM 16004 N  N3    . ATP K 5 .   ? 151.954 136.206 172.713 1.00 61.55 ?  803 ATP B N3    1 
HETATM 16005 C  C4    . ATP K 5 .   ? 152.338 135.127 173.402 1.00 64.32 ?  803 ATP B C4    1 
HETATM 16006 O  O1B   . DGI L 6 .   ? 162.870 152.880 173.269 1.00 62.73 -1 804 DGI B O1B   1 
HETATM 16007 P  PB    . DGI L 6 .   ? 163.097 151.407 172.996 1.00 78.16 ?  804 DGI B PB    1 
HETATM 16008 O  O2B   . DGI L 6 .   ? 164.537 151.080 172.670 1.00 66.34 ?  804 DGI B O2B   1 
HETATM 16009 O  O3B   . DGI L 6 .   ? 162.516 150.515 174.072 1.00 63.38 ?  804 DGI B O3B   1 
HETATM 16010 O  O3A   . DGI L 6 .   ? 162.301 151.056 171.620 1.00 65.58 ?  804 DGI B O3A   1 
HETATM 16011 P  PA    . DGI L 6 .   ? 162.313 150.030 170.393 1.00 72.25 ?  804 DGI B PA    1 
HETATM 16012 O  O1A   . DGI L 6 .   ? 163.173 148.876 170.745 1.00 65.11 ?  804 DGI B O1A   1 
HETATM 16013 O  O2A   . DGI L 6 .   ? 162.582 150.775 169.146 1.00 63.88 -1 804 DGI B O2A   1 
HETATM 16014 O  "O5'" . DGI L 6 .   ? 160.788 149.561 170.361 1.00 64.69 ?  804 DGI B "O5'" 1 
HETATM 16015 C  "C5'" . DGI L 6 .   ? 159.736 150.547 170.413 1.00 61.37 ?  804 DGI B "C5'" 1 
HETATM 16016 C  "C4'" . DGI L 6 .   ? 158.402 149.853 170.292 1.00 62.25 ?  804 DGI B "C4'" 1 
HETATM 16017 O  "O4'" . DGI L 6 .   ? 158.330 149.157 169.028 1.00 62.79 ?  804 DGI B "O4'" 1 
HETATM 16018 C  "C3'" . DGI L 6 .   ? 158.105 148.820 171.383 1.00 63.26 ?  804 DGI B "C3'" 1 
HETATM 16019 O  "O3'" . DGI L 6 .   ? 156.795 149.020 171.915 1.00 62.44 ?  804 DGI B "O3'" 1 
HETATM 16020 C  "C2'" . DGI L 6 .   ? 158.192 147.487 170.648 1.00 58.79 ?  804 DGI B "C2'" 1 
HETATM 16021 C  "C1'" . DGI L 6 .   ? 157.792 147.869 169.237 1.00 58.08 ?  804 DGI B "C1'" 1 
HETATM 16022 N  N9    . DGI L 6 .   ? 158.322 146.974 168.189 1.00 59.64 ?  804 DGI B N9    1 
HETATM 16023 C  C8    . DGI L 6 .   ? 157.608 146.348 167.202 1.00 62.54 ?  804 DGI B C8    1 
HETATM 16024 N  N7    . DGI L 6 .   ? 158.352 145.609 166.414 1.00 61.46 ?  804 DGI B N7    1 
HETATM 16025 C  C5    . DGI L 6 .   ? 159.635 145.757 166.913 1.00 64.08 ?  804 DGI B C5    1 
HETATM 16026 C  C4    . DGI L 6 .   ? 159.632 146.595 168.007 1.00 62.76 ?  804 DGI B C4    1 
HETATM 16027 N  N3    . DGI L 6 .   ? 160.679 146.980 168.762 1.00 63.02 ?  804 DGI B N3    1 
HETATM 16028 C  C2    . DGI L 6 .   ? 161.829 146.451 168.352 1.00 61.32 ?  804 DGI B C2    1 
HETATM 16029 N  N2    . DGI L 6 .   ? 162.957 146.736 169.007 1.00 62.38 ?  804 DGI B N2    1 
HETATM 16030 N  N1    . DGI L 6 .   ? 161.930 145.609 167.277 1.00 60.59 ?  804 DGI B N1    1 
HETATM 16031 C  C6    . DGI L 6 .   ? 160.876 145.198 166.485 1.00 62.82 ?  804 DGI B C6    1 
HETATM 16032 O  O6    . DGI L 6 .   ? 161.064 144.438 165.536 1.00 61.55 ?  804 DGI B O6    1 
HETATM 16033 MN MN    . MN  M 7 .   ? 121.776 91.834  123.881 0.85 25.05 ?  401 MN  C MN    1 
HETATM 16034 MN MN    . MN  N 7 .   ? 120.167 95.168  124.381 0.85 26.37 ?  402 MN  C MN    1 
HETATM 16035 MN MN    . MN  O 7 .   ? 139.743 100.553 137.397 1.00 22.51 ?  401 MN  D MN    1 
HETATM 16036 MN MN    . MN  P 7 .   ? 142.110 99.012  134.692 1.00 24.72 ?  402 MN  D MN    1 
# 
