data_9BY7
# 
_entry.id   9BY7 
# 
_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   9BY7         pdb_00009by7 10.2210/pdb9by7/pdb 
WWPDB D_1000284362 ?            ?                   
EMDB  EMD-45020    ?            ?                   
# 
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                        9BY7 
_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 8 model for product condition of Bacillus subtilis ribonucleotide reductase complex' EMD-45020 '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                   9BY7 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9BY7 
_struct.title                        'Class 8 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        9BY7 
_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 9BY7 A 1  ? 700 ? P50620 1 ? 700 ? 1 700 
2 1 9BY7 B 1  ? 700 ? P50620 1 ? 700 ? 1 700 
3 2 9BY7 C 22 ? 350 ? P50621 1 ? 329 ? 1 329 
4 2 9BY7 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 9BY7 MET C 1  ? UNP P50621 ? ? 'initiating methionine' -20 1  
3 9BY7 GLY C 2  ? UNP P50621 ? ? 'expression tag'        -19 2  
3 9BY7 SER C 3  ? UNP P50621 ? ? 'expression tag'        -18 3  
3 9BY7 SER C 4  ? UNP P50621 ? ? 'expression tag'        -17 4  
3 9BY7 HIS C 5  ? UNP P50621 ? ? 'expression tag'        -16 5  
3 9BY7 HIS C 6  ? UNP P50621 ? ? 'expression tag'        -15 6  
3 9BY7 HIS C 7  ? UNP P50621 ? ? 'expression tag'        -14 7  
3 9BY7 HIS C 8  ? UNP P50621 ? ? 'expression tag'        -13 8  
3 9BY7 HIS C 9  ? UNP P50621 ? ? 'expression tag'        -12 9  
3 9BY7 HIS C 10 ? UNP P50621 ? ? 'expression tag'        -11 10 
3 9BY7 SER C 11 ? UNP P50621 ? ? 'expression tag'        -10 11 
3 9BY7 SER C 12 ? UNP P50621 ? ? 'expression tag'        -9  12 
3 9BY7 GLY C 13 ? UNP P50621 ? ? 'expression tag'        -8  13 
3 9BY7 LEU C 14 ? UNP P50621 ? ? 'expression tag'        -7  14 
3 9BY7 VAL C 15 ? UNP P50621 ? ? 'expression tag'        -6  15 
3 9BY7 PRO C 16 ? UNP P50621 ? ? 'expression tag'        -5  16 
3 9BY7 ARG C 17 ? UNP P50621 ? ? 'expression tag'        -4  17 
3 9BY7 GLY C 18 ? UNP P50621 ? ? 'expression tag'        -3  18 
3 9BY7 SER C 19 ? UNP P50621 ? ? 'expression tag'        -2  19 
3 9BY7 HIS C 20 ? UNP P50621 ? ? 'expression tag'        -1  20 
3 9BY7 MET C 21 ? UNP P50621 ? ? 'expression tag'        0   21 
4 9BY7 MET D 1  ? UNP P50621 ? ? 'initiating methionine' -20 22 
4 9BY7 GLY D 2  ? UNP P50621 ? ? 'expression tag'        -19 23 
4 9BY7 SER D 3  ? UNP P50621 ? ? 'expression tag'        -18 24 
4 9BY7 SER D 4  ? UNP P50621 ? ? 'expression tag'        -17 25 
4 9BY7 HIS D 5  ? UNP P50621 ? ? 'expression tag'        -16 26 
4 9BY7 HIS D 6  ? UNP P50621 ? ? 'expression tag'        -15 27 
4 9BY7 HIS D 7  ? UNP P50621 ? ? 'expression tag'        -14 28 
4 9BY7 HIS D 8  ? UNP P50621 ? ? 'expression tag'        -13 29 
4 9BY7 HIS D 9  ? UNP P50621 ? ? 'expression tag'        -12 30 
4 9BY7 HIS D 10 ? UNP P50621 ? ? 'expression tag'        -11 31 
4 9BY7 SER D 11 ? UNP P50621 ? ? 'expression tag'        -10 32 
4 9BY7 SER D 12 ? UNP P50621 ? ? 'expression tag'        -9  33 
4 9BY7 GLY D 13 ? UNP P50621 ? ? 'expression tag'        -8  34 
4 9BY7 LEU D 14 ? UNP P50621 ? ? 'expression tag'        -7  35 
4 9BY7 VAL D 15 ? UNP P50621 ? ? 'expression tag'        -6  36 
4 9BY7 PRO D 16 ? UNP P50621 ? ? 'expression tag'        -5  37 
4 9BY7 ARG D 17 ? UNP P50621 ? ? 'expression tag'        -4  38 
4 9BY7 GLY D 18 ? UNP P50621 ? ? 'expression tag'        -3  39 
4 9BY7 SER D 19 ? UNP P50621 ? ? 'expression tag'        -2  40 
4 9BY7 HIS D 20 ? UNP P50621 ? ? 'expression tag'        -1  41 
4 9BY7 MET D 21 ? UNP P50621 ? ? 'expression tag'        0   42 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_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   ? 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 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 ? ? ? ? ? ? ? 2.342 ? ? 
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 ? ? ? ? ? ? ? 2.177 ? ? 
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 ? ? ? ? ? ? ? 1.964 ? ? 
metalc12 metalc ? ? C GLU 219 OE1 ? ? ? 1_555 M MN . MN ? ? C GLU 198 C MN 401 1_555 ? ? ? ? ? ? ? 2.173 ? ? 
metalc13 metalc ? ? C GLU 219 OE1 ? ? ? 1_555 N MN . MN ? ? C GLU 198 C MN 402 1_555 ? ? ? ? ? ? ? 2.711 ? ? 
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 ? ? ? ? ? ? ? 2.156 ? ? 
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 ? ? ? ? ? ? ? 1.990 ? ? 
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 ? ? ? ? ? ? ? 2.319 ? ? 
metalc23 metalc ? ? D GLU 219 OE1 ? ? ? 1_555 O MN . MN ? ? D GLU 198 D MN 401 1_555 ? ? ? ? ? ? ? 2.081 ? ? 
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 ? ? ? ? ? ? ? 2.330 ? ? 
# 
_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 89.6  ? 
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 97.0  ? 
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 93.4  ? 
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_555 165.6 ? 
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 96.5  ? 
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 99.6  ? 
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_555 103.0 ? 
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 1.20  
2 TYR 355 B . ? TYR 355 B PRO 356 B ? PRO 356 B 1 -0.37 
# 
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                   9BY7 
_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 NH2 D ARG 86  ? ? OE1 D GLU 211 ? ? 2.18 
5 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 ? ? 72.10   -7.44   
2  1 SER A 593 ? ? 59.74   -154.80 
3  1 SER A 653 ? ? -68.92  99.31   
4  1 ASP B 215 ? ? 79.69   -0.88   
5  1 ASP B 238 ? ? -95.45  31.32   
6  1 SER B 408 ? ? -160.51 113.55  
7  1 SER B 593 ? ? 58.45   -151.26 
8  1 THR C 72  ? ? -128.08 -59.04  
9  1 ASP C 148 ? ? 58.01   15.69   
10 1 PHE C 166 ? ? -125.60 -60.79  
11 1 THR D 72  ? ? -128.17 -58.52  
12 1 PHE D 166 ? ? -144.15 -61.21  
13 1 THR D 311 ? ? -168.67 116.03  
14 1 ASP D 317 ? ? 61.61   167.70  
15 1 ASP D 318 ? ? 67.15   -4.08   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9BY7 
_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                    9BY7 
_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                  3.67 
_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               45000 
_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                        9BY7 
_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              9BY7 
_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                9BY7 
_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              9BY7 
_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           9BY7 
_em_admin.last_update        2025-03-26 
_em_admin.map_release_date   2025-03-19 
_em_admin.title              'Class 8 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                    9BY7 
_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   ? 104.216 115.766 99.151  1.00 63.04 ?  6   VAL A N     1 
ATOM   2     C  CA    . VAL A 1 6   ? 105.504 116.303 98.731  1.00 62.74 ?  6   VAL A CA    1 
ATOM   3     C  C     . VAL A 1 6   ? 105.281 117.451 97.747  1.00 63.36 ?  6   VAL A C     1 
ATOM   4     O  O     . VAL A 1 6   ? 104.368 117.402 96.920  1.00 63.20 ?  6   VAL A O     1 
ATOM   5     C  CB    . VAL A 1 6   ? 106.400 115.185 98.130  1.00 64.24 ?  6   VAL A CB    1 
ATOM   6     C  CG1   . VAL A 1 6   ? 106.120 114.974 96.645  1.00 62.93 ?  6   VAL A CG1   1 
ATOM   7     C  CG2   . VAL A 1 6   ? 107.870 115.482 98.368  1.00 61.49 ?  6   VAL A CG2   1 
ATOM   8     N  N     . PRO A 1 7   ? 106.077 118.514 97.872  1.00 58.77 ?  7   PRO A N     1 
ATOM   9     C  CA    . PRO A 1 7   ? 105.991 119.609 96.901  1.00 54.02 ?  7   PRO A CA    1 
ATOM   10    C  C     . PRO A 1 7   ? 106.351 119.131 95.504  1.00 56.48 ?  7   PRO A C     1 
ATOM   11    O  O     . PRO A 1 7   ? 107.203 118.261 95.321  1.00 60.50 ?  7   PRO A O     1 
ATOM   12    C  CB    . PRO A 1 7   ? 107.007 120.628 97.424  1.00 55.37 ?  7   PRO A CB    1 
ATOM   13    C  CG    . PRO A 1 7   ? 107.093 120.348 98.882  1.00 57.08 ?  7   PRO A CG    1 
ATOM   14    C  CD    . PRO A 1 7   ? 106.944 118.859 99.011  1.00 57.20 ?  7   PRO A CD    1 
ATOM   15    N  N     . LYS A 1 8   ? 105.678 119.712 94.509  1.00 58.03 ?  8   LYS A N     1 
ATOM   16    C  CA    . LYS A 1 8   ? 105.921 119.310 93.128  1.00 56.12 ?  8   LYS A CA    1 
ATOM   17    C  C     . LYS A 1 8   ? 107.332 119.670 92.687  1.00 57.08 ?  8   LYS A C     1 
ATOM   18    O  O     . LYS A 1 8   ? 107.975 118.911 91.951  1.00 57.57 ?  8   LYS A O     1 
ATOM   19    C  CB    . LYS A 1 8   ? 104.891 119.954 92.202  1.00 55.64 ?  8   LYS A CB    1 
ATOM   20    C  CG    . LYS A 1 8   ? 104.739 119.243 90.868  1.00 56.25 ?  8   LYS A CG    1 
ATOM   21    C  CD    . LYS A 1 8   ? 104.449 120.221 89.746  1.00 57.80 ?  8   LYS A CD    1 
ATOM   22    C  CE    . LYS A 1 8   ? 104.650 119.575 88.387  1.00 57.13 ?  8   LYS A CE    1 
ATOM   23    N  NZ    . LYS A 1 8   ? 105.125 120.555 87.373  1.00 58.95 1  8   LYS A NZ    1 
ATOM   24    N  N     . TRP A 1 9   ? 107.831 120.828 93.124  1.00 57.42 ?  9   TRP A N     1 
ATOM   25    C  CA    . TRP A 1 9   ? 109.135 121.285 92.659  1.00 52.16 ?  9   TRP A CA    1 
ATOM   26    C  C     . TRP A 1 9   ? 110.264 120.440 93.236  1.00 54.06 ?  9   TRP A C     1 
ATOM   27    O  O     . TRP A 1 9   ? 111.238 120.145 92.534  1.00 57.94 ?  9   TRP A O     1 
ATOM   28    C  CB    . TRP A 1 9   ? 109.330 122.761 92.993  1.00 53.77 ?  9   TRP A CB    1 
ATOM   29    C  CG    . TRP A 1 9   ? 109.033 123.134 94.405  1.00 50.50 ?  9   TRP A CG    1 
ATOM   30    C  CD1   . TRP A 1 9   ? 109.894 123.097 95.455  1.00 51.38 ?  9   TRP A CD1   1 
ATOM   31    C  CD2   . TRP A 1 9   ? 107.790 123.617 94.921  1.00 51.33 ?  9   TRP A CD2   1 
ATOM   32    N  NE1   . TRP A 1 9   ? 109.266 123.519 96.600  1.00 52.90 ?  9   TRP A NE1   1 
ATOM   33    C  CE2   . TRP A 1 9   ? 107.971 123.846 96.299  1.00 52.26 ?  9   TRP A CE2   1 
ATOM   34    C  CE3   . TRP A 1 9   ? 106.539 123.874 94.354  1.00 51.69 ?  9   TRP A CE3   1 
ATOM   35    C  CZ2   . TRP A 1 9   ? 106.951 124.319 97.117  1.00 52.47 ?  9   TRP A CZ2   1 
ATOM   36    C  CZ3   . TRP A 1 9   ? 105.529 124.344 95.166  1.00 55.31 ?  9   TRP A CZ3   1 
ATOM   37    C  CH2   . TRP A 1 9   ? 105.740 124.562 96.532  1.00 54.90 ?  9   TRP A CH2   1 
ATOM   38    N  N     . ILE A 1 10  ? 110.160 120.032 94.505  1.00 54.45 ?  10  ILE A N     1 
ATOM   39    C  CA    . ILE A 1 10  ? 111.194 119.157 95.048  1.00 57.23 ?  10  ILE A CA    1 
ATOM   40    C  C     . ILE A 1 10  ? 111.041 117.730 94.542  1.00 55.75 ?  10  ILE A C     1 
ATOM   41    O  O     . ILE A 1 10  ? 112.022 116.976 94.536  1.00 59.01 ?  10  ILE A O     1 
ATOM   42    C  CB    . ILE A 1 10  ? 111.227 119.150 96.587  1.00 56.46 ?  10  ILE A CB    1 
ATOM   43    C  CG1   . ILE A 1 10  ? 110.295 118.085 97.161  1.00 58.14 ?  10  ILE A CG1   1 
ATOM   44    C  CG2   . ILE A 1 10  ? 110.894 120.513 97.152  1.00 55.14 ?  10  ILE A CG2   1 
ATOM   45    C  CD1   . ILE A 1 10  ? 110.534 117.815 98.625  1.00 58.28 ?  10  ILE A CD1   1 
ATOM   46    N  N     . GLN A 1 11  ? 109.839 117.333 94.121  1.00 57.10 ?  11  GLN A N     1 
ATOM   47    C  CA    . GLN A 1 11  ? 109.691 116.044 93.458  1.00 57.23 ?  11  GLN A CA    1 
ATOM   48    C  C     . GLN A 1 11  ? 110.371 116.055 92.096  1.00 56.41 ?  11  GLN A C     1 
ATOM   49    O  O     . GLN A 1 11  ? 111.050 115.090 91.727  1.00 58.51 ?  11  GLN A O     1 
ATOM   50    C  CB    . GLN A 1 11  ? 108.210 115.688 93.329  1.00 59.25 ?  11  GLN A CB    1 
ATOM   51    C  CG    . GLN A 1 11  ? 107.921 114.549 92.372  1.00 60.60 ?  11  GLN A CG    1 
ATOM   52    C  CD    . GLN A 1 11  ? 107.098 114.993 91.180  1.00 61.60 ?  11  GLN A CD    1 
ATOM   53    O  OE1   . GLN A 1 11  ? 106.091 115.683 91.331  1.00 60.15 ?  11  GLN A OE1   1 
ATOM   54    N  NE2   . GLN A 1 11  ? 107.527 114.601 89.986  1.00 60.38 ?  11  GLN A NE2   1 
ATOM   55    N  N     . LEU A 1 12  ? 110.208 117.145 91.343  1.00 56.36 ?  12  LEU A N     1 
ATOM   56    C  CA    . LEU A 1 12  ? 110.913 117.290 90.072  1.00 55.06 ?  12  LEU A CA    1 
ATOM   57    C  C     . LEU A 1 12  ? 112.419 117.387 90.283  1.00 57.48 ?  12  LEU A C     1 
ATOM   58    O  O     . LEU A 1 12  ? 113.200 116.863 89.481  1.00 59.89 ?  12  LEU A O     1 
ATOM   59    C  CB    . LEU A 1 12  ? 110.400 118.521 89.329  1.00 55.96 ?  12  LEU A CB    1 
ATOM   60    C  CG    . LEU A 1 12  ? 109.286 118.311 88.306  1.00 56.90 ?  12  LEU A CG    1 
ATOM   61    C  CD1   . LEU A 1 12  ? 108.486 119.590 88.130  1.00 55.45 ?  12  LEU A CD1   1 
ATOM   62    C  CD2   . LEU A 1 12  ? 109.860 117.847 86.980  1.00 57.52 ?  12  LEU A CD2   1 
ATOM   63    N  N     . ASN A 1 13  ? 112.842 118.064 91.352  1.00 56.01 ?  13  ASN A N     1 
ATOM   64    C  CA    . ASN A 1 13  ? 114.265 118.217 91.630  1.00 52.82 ?  13  ASN A CA    1 
ATOM   65    C  C     . ASN A 1 13  ? 114.910 116.891 92.007  1.00 54.86 ?  13  ASN A C     1 
ATOM   66    O  O     . ASN A 1 13  ? 116.111 116.703 91.786  1.00 60.62 ?  13  ASN A O     1 
ATOM   67    C  CB    . ASN A 1 13  ? 114.468 119.248 92.741  1.00 56.25 ?  13  ASN A CB    1 
ATOM   68    C  CG    . ASN A 1 13  ? 115.919 119.389 93.150  1.00 56.13 ?  13  ASN A CG    1 
ATOM   69    O  OD1   . ASN A 1 13  ? 116.338 118.864 94.180  1.00 54.72 ?  13  ASN A OD1   1 
ATOM   70    N  ND2   . ASN A 1 13  ? 116.693 120.104 92.343  1.00 55.92 ?  13  ASN A ND2   1 
ATOM   71    N  N     . ASN A 1 14  ? 114.137 115.964 92.571  1.00 57.72 ?  14  ASN A N     1 
ATOM   72    C  CA    . ASN A 1 14  ? 114.661 114.649 92.914  1.00 58.51 ?  14  ASN A CA    1 
ATOM   73    C  C     . ASN A 1 14  ? 114.757 113.719 91.713  1.00 57.77 ?  14  ASN A C     1 
ATOM   74    O  O     . ASN A 1 14  ? 115.374 112.656 91.824  1.00 60.03 ?  14  ASN A O     1 
ATOM   75    C  CB    . ASN A 1 14  ? 113.797 114.004 94.000  1.00 56.46 ?  14  ASN A CB    1 
ATOM   76    C  CG    . ASN A 1 14  ? 114.059 114.587 95.373  1.00 58.69 ?  14  ASN A CG    1 
ATOM   77    O  OD1   . ASN A 1 14  ? 114.360 115.771 95.509  1.00 60.90 ?  14  ASN A OD1   1 
ATOM   78    N  ND2   . ASN A 1 14  ? 113.944 113.755 96.401  1.00 59.30 ?  14  ASN A ND2   1 
ATOM   79    N  N     . GLU A 1 15  ? 114.170 114.089 90.576  1.00 57.87 ?  15  GLU A N     1 
ATOM   80    C  CA    . GLU A 1 15  ? 114.294 113.300 89.359  1.00 59.07 ?  15  GLU A CA    1 
ATOM   81    C  C     . GLU A 1 15  ? 115.643 113.484 88.676  1.00 61.72 ?  15  GLU A C     1 
ATOM   82    O  O     . GLU A 1 15  ? 115.903 112.819 87.668  1.00 63.52 ?  15  GLU A O     1 
ATOM   83    C  CB    . GLU A 1 15  ? 113.168 113.647 88.381  1.00 59.34 ?  15  GLU A CB    1 
ATOM   84    C  CG    . GLU A 1 15  ? 111.797 113.732 89.025  1.00 60.15 ?  15  GLU A CG    1 
ATOM   85    C  CD    . GLU A 1 15  ? 110.667 113.670 88.017  1.00 63.73 ?  15  GLU A CD    1 
ATOM   86    O  OE1   . GLU A 1 15  ? 110.944 113.761 86.805  1.00 63.57 ?  15  GLU A OE1   1 
ATOM   87    O  OE2   . GLU A 1 15  ? 109.500 113.532 88.440  1.00 63.84 -1 15  GLU A OE2   1 
ATOM   88    N  N     . ILE A 1 16  ? 116.493 114.376 89.190  1.00 59.98 ?  16  ILE A N     1 
ATOM   89    C  CA    . ILE A 1 16  ? 117.847 114.506 88.659  1.00 59.72 ?  16  ILE A CA    1 
ATOM   90    C  C     . ILE A 1 16  ? 118.632 113.224 88.896  1.00 59.78 ?  16  ILE A C     1 
ATOM   91    O  O     . ILE A 1 16  ? 119.353 112.745 88.012  1.00 61.09 ?  16  ILE A O     1 
ATOM   92    C  CB    . ILE A 1 16  ? 118.552 115.724 89.284  1.00 58.93 ?  16  ILE A CB    1 
ATOM   93    C  CG1   . ILE A 1 16  ? 117.781 117.008 88.979  1.00 57.54 ?  16  ILE A CG1   1 
ATOM   94    C  CG2   . ILE A 1 16  ? 119.985 115.833 88.782  1.00 59.58 ?  16  ILE A CG2   1 
ATOM   95    C  CD1   . ILE A 1 16  ? 118.249 118.201 89.778  1.00 56.90 ?  16  ILE A CD1   1 
ATOM   96    N  N     . MET A 1 17  ? 118.500 112.644 90.090  1.00 60.50 ?  17  MET A N     1 
ATOM   97    C  CA    . MET A 1 17  ? 119.256 111.451 90.442  1.00 61.98 ?  17  MET A CA    1 
ATOM   98    C  C     . MET A 1 17  ? 118.710 110.187 89.795  1.00 62.80 ?  17  MET A C     1 
ATOM   99    O  O     . MET A 1 17  ? 119.436 109.190 89.712  1.00 63.98 ?  17  MET A O     1 
ATOM   100   C  CB    . MET A 1 17  ? 119.279 111.280 91.960  1.00 61.29 ?  17  MET A CB    1 
ATOM   101   C  CG    . MET A 1 17  ? 119.710 112.529 92.693  1.00 61.55 ?  17  MET A CG    1 
ATOM   102   S  SD    . MET A 1 17  ? 121.217 113.254 92.019  1.00 68.12 ?  17  MET A SD    1 
ATOM   103   C  CE    . MET A 1 17  ? 122.466 112.311 92.888  1.00 61.05 ?  17  MET A CE    1 
ATOM   104   N  N     . ILE A 1 18  ? 117.459 110.196 89.341  1.00 62.62 ?  18  ILE A N     1 
ATOM   105   C  CA    . ILE A 1 18  ? 116.919 109.050 88.616  1.00 64.44 ?  18  ILE A CA    1 
ATOM   106   C  C     . ILE A 1 18  ? 117.637 108.985 87.272  1.00 65.28 ?  18  ILE A C     1 
ATOM   107   O  O     . ILE A 1 18  ? 117.407 109.817 86.389  1.00 66.44 ?  18  ILE A O     1 
ATOM   108   C  CB    . ILE A 1 18  ? 115.396 109.138 88.437  1.00 65.30 ?  18  ILE A CB    1 
ATOM   109   C  CG1   . ILE A 1 18  ? 114.615 108.857 89.739  1.00 64.60 ?  18  ILE A CG1   1 
ATOM   110   C  CG2   . ILE A 1 18  ? 114.927 108.167 87.359  1.00 64.87 ?  18  ILE A CG2   1 
ATOM   111   C  CD1   . ILE A 1 18  ? 115.066 109.562 91.003  1.00 64.07 ?  18  ILE A CD1   1 
ATOM   112   N  N     . GLN A 1 19  ? 118.525 108.006 87.121  1.00 68.96 ?  19  GLN A N     1 
ATOM   113   C  CA    . GLN A 1 19  ? 119.375 107.919 85.942  1.00 70.00 ?  19  GLN A CA    1 
ATOM   114   C  C     . GLN A 1 19  ? 118.591 107.313 84.786  1.00 69.78 ?  19  GLN A C     1 
ATOM   115   O  O     . GLN A 1 19  ? 118.202 106.141 84.836  1.00 71.76 ?  19  GLN A O     1 
ATOM   116   C  CB    . GLN A 1 19  ? 120.621 107.093 86.245  1.00 72.02 ?  19  GLN A CB    1 
ATOM   117   C  CG    . GLN A 1 19  ? 121.583 107.763 87.215  1.00 70.29 ?  19  GLN A CG    1 
ATOM   118   C  CD    . GLN A 1 19  ? 122.836 106.945 87.458  1.00 71.59 ?  19  GLN A CD    1 
ATOM   119   O  OE1   . GLN A 1 19  ? 122.997 105.855 86.910  1.00 71.28 ?  19  GLN A OE1   1 
ATOM   120   N  NE2   . GLN A 1 19  ? 123.732 107.469 88.286  1.00 71.39 ?  19  GLN A NE2   1 
ATOM   121   N  N     . LYS A 1 20  ? 118.359 108.111 83.750  1.00 71.28 ?  20  LYS A N     1 
ATOM   122   C  CA    . LYS A 1 20  ? 117.672 107.670 82.544  1.00 73.11 ?  20  LYS A CA    1 
ATOM   123   C  C     . LYS A 1 20  ? 118.698 107.542 81.428  1.00 73.64 ?  20  LYS A C     1 
ATOM   124   O  O     . LYS A 1 20  ? 119.410 108.506 81.125  1.00 73.55 ?  20  LYS A O     1 
ATOM   125   C  CB    . LYS A 1 20  ? 116.562 108.647 82.158  1.00 71.82 ?  20  LYS A CB    1 
ATOM   126   C  CG    . LYS A 1 20  ? 115.949 108.383 80.793  1.00 72.49 ?  20  LYS A CG    1 
ATOM   127   C  CD    . LYS A 1 20  ? 115.710 109.677 80.036  1.00 73.53 ?  20  LYS A CD    1 
ATOM   128   C  CE    . LYS A 1 20  ? 116.949 110.558 80.040  1.00 73.84 ?  20  LYS A CE    1 
ATOM   129   N  NZ    . LYS A 1 20  ? 118.105 109.892 79.382  1.00 73.93 1  20  LYS A NZ    1 
ATOM   130   N  N     . ASP A 1 21  ? 118.769 106.354 80.825  1.00 72.18 ?  21  ASP A N     1 
ATOM   131   C  CA    . ASP A 1 21  ? 119.745 106.051 79.777  1.00 73.50 ?  21  ASP A CA    1 
ATOM   132   C  C     . ASP A 1 21  ? 121.176 106.247 80.278  1.00 74.05 ?  21  ASP A C     1 
ATOM   133   O  O     . ASP A 1 21  ? 122.058 106.688 79.539  1.00 72.09 ?  21  ASP A O     1 
ATOM   134   C  CB    . ASP A 1 21  ? 119.489 106.886 78.520  1.00 73.43 ?  21  ASP A CB    1 
ATOM   135   C  CG    . ASP A 1 21  ? 118.025 106.910 78.127  1.00 74.57 ?  21  ASP A CG    1 
ATOM   136   O  OD1   . ASP A 1 21  ? 117.353 105.867 78.264  1.00 72.61 ?  21  ASP A OD1   1 
ATOM   137   O  OD2   . ASP A 1 21  ? 117.547 107.974 77.681  1.00 74.27 -1 21  ASP A OD2   1 
ATOM   138   N  N     . GLY A 1 22  ? 121.406 105.913 81.546  1.00 73.98 ?  22  GLY A N     1 
ATOM   139   C  CA    . GLY A 1 22  ? 122.735 105.979 82.120  1.00 74.01 ?  22  GLY A CA    1 
ATOM   140   C  C     . GLY A 1 22  ? 123.240 107.366 82.441  1.00 73.96 ?  22  GLY A C     1 
ATOM   141   O  O     . GLY A 1 22  ? 124.432 107.518 82.731  1.00 72.73 ?  22  GLY A O     1 
ATOM   142   N  N     . LYS A 1 23  ? 122.381 108.382 82.405  1.00 70.77 ?  23  LYS A N     1 
ATOM   143   C  CA    . LYS A 1 23  ? 122.787 109.755 82.661  1.00 68.48 ?  23  LYS A CA    1 
ATOM   144   C  C     . LYS A 1 23  ? 121.847 110.398 83.669  1.00 69.58 ?  23  LYS A C     1 
ATOM   145   O  O     . LYS A 1 23  ? 120.658 110.073 83.730  1.00 70.55 ?  23  LYS A O     1 
ATOM   146   C  CB    . LYS A 1 23  ? 122.796 110.591 81.375  1.00 68.39 ?  23  LYS A CB    1 
ATOM   147   C  CG    . LYS A 1 23  ? 123.875 110.211 80.378  1.00 68.46 ?  23  LYS A CG    1 
ATOM   148   C  CD    . LYS A 1 23  ? 123.850 111.151 79.184  1.00 68.57 ?  23  LYS A CD    1 
ATOM   149   C  CE    . LYS A 1 23  ? 124.841 110.730 78.117  1.00 68.95 ?  23  LYS A CE    1 
ATOM   150   N  NZ    . LYS A 1 23  ? 124.767 111.616 76.923  1.00 67.63 1  23  LYS A NZ    1 
ATOM   151   N  N     . PHE A 1 24  ? 122.396 111.315 84.462  1.00 63.30 ?  24  PHE A N     1 
ATOM   152   C  CA    . PHE A 1 24  ? 121.573 112.121 85.350  1.00 60.09 ?  24  PHE A CA    1 
ATOM   153   C  C     . PHE A 1 24  ? 120.663 113.031 84.537  1.00 60.84 ?  24  PHE A C     1 
ATOM   154   O  O     . PHE A 1 24  ? 121.064 113.577 83.506  1.00 59.40 ?  24  PHE A O     1 
ATOM   155   C  CB    . PHE A 1 24  ? 122.448 112.962 86.279  1.00 58.54 ?  24  PHE A CB    1 
ATOM   156   C  CG    . PHE A 1 24  ? 123.149 112.167 87.339  1.00 59.92 ?  24  PHE A CG    1 
ATOM   157   C  CD1   . PHE A 1 24  ? 122.503 111.838 88.516  1.00 60.45 ?  24  PHE A CD1   1 
ATOM   158   C  CD2   . PHE A 1 24  ? 124.458 111.754 87.160  1.00 59.89 ?  24  PHE A CD2   1 
ATOM   159   C  CE1   . PHE A 1 24  ? 123.148 111.109 89.495  1.00 60.18 ?  24  PHE A CE1   1 
ATOM   160   C  CE2   . PHE A 1 24  ? 125.107 111.026 88.135  1.00 59.21 ?  24  PHE A CE2   1 
ATOM   161   C  CZ    . PHE A 1 24  ? 124.451 110.703 89.304  1.00 60.10 ?  24  PHE A CZ    1 
ATOM   162   N  N     . GLN A 1 25  ? 119.426 113.191 85.005  1.00 61.85 ?  25  GLN A N     1 
ATOM   163   C  CA    . GLN A 1 25  ? 118.458 114.062 84.338  1.00 59.76 ?  25  GLN A CA    1 
ATOM   164   C  C     . GLN A 1 25  ? 118.658 115.481 84.862  1.00 60.95 ?  25  GLN A C     1 
ATOM   165   O  O     . GLN A 1 25  ? 117.949 115.965 85.746  1.00 61.19 ?  25  GLN A O     1 
ATOM   166   C  CB    . GLN A 1 25  ? 117.038 113.561 84.566  1.00 61.01 ?  25  GLN A CB    1 
ATOM   167   C  CG    . GLN A 1 25  ? 116.799 112.143 84.081  1.00 61.65 ?  25  GLN A CG    1 
ATOM   168   C  CD    . GLN A 1 25  ? 115.361 111.703 84.258  1.00 62.47 ?  25  GLN A CD    1 
ATOM   169   O  OE1   . GLN A 1 25  ? 114.523 111.918 83.383  1.00 62.18 ?  25  GLN A OE1   1 
ATOM   170   N  NE2   . GLN A 1 25  ? 115.068 111.082 85.394  1.00 60.78 ?  25  GLN A NE2   1 
ATOM   171   N  N     . PHE A 1 26  ? 119.659 116.155 84.292  1.00 57.38 ?  26  PHE A N     1 
ATOM   172   C  CA    . PHE A 1 26  ? 120.006 117.496 84.750  1.00 55.95 ?  26  PHE A CA    1 
ATOM   173   C  C     . PHE A 1 26  ? 118.947 118.519 84.363  1.00 57.41 ?  26  PHE A C     1 
ATOM   174   O  O     . PHE A 1 26  ? 118.776 119.524 85.062  1.00 56.88 ?  26  PHE A O     1 
ATOM   175   C  CB    . PHE A 1 26  ? 121.369 117.904 84.190  1.00 53.29 ?  26  PHE A CB    1 
ATOM   176   C  CG    . PHE A 1 26  ? 122.517 117.144 84.786  1.00 54.17 ?  26  PHE A CG    1 
ATOM   177   C  CD1   . PHE A 1 26  ? 122.715 117.123 86.156  1.00 54.44 ?  26  PHE A CD1   1 
ATOM   178   C  CD2   . PHE A 1 26  ? 123.397 116.448 83.977  1.00 55.39 ?  26  PHE A CD2   1 
ATOM   179   C  CE1   . PHE A 1 26  ? 123.770 116.423 86.705  1.00 53.11 ?  26  PHE A CE1   1 
ATOM   180   C  CE2   . PHE A 1 26  ? 124.453 115.747 84.523  1.00 54.08 ?  26  PHE A CE2   1 
ATOM   181   C  CZ    . PHE A 1 26  ? 124.640 115.735 85.889  1.00 51.66 ?  26  PHE A CZ    1 
ATOM   182   N  N     . ASP A 1 27  ? 118.229 118.287 83.261  1.00 62.63 ?  27  ASP A N     1 
ATOM   183   C  CA    . ASP A 1 27  ? 117.198 119.216 82.818  1.00 61.91 ?  27  ASP A CA    1 
ATOM   184   C  C     . ASP A 1 27  ? 116.001 119.267 83.758  1.00 62.06 ?  27  ASP A C     1 
ATOM   185   O  O     . ASP A 1 27  ? 115.164 120.165 83.615  1.00 62.82 ?  27  ASP A O     1 
ATOM   186   C  CB    . ASP A 1 27  ? 116.729 118.849 81.410  1.00 61.74 ?  27  ASP A CB    1 
ATOM   187   C  CG    . ASP A 1 27  ? 116.653 120.051 80.490  1.00 65.25 ?  27  ASP A CG    1 
ATOM   188   O  OD1   . ASP A 1 27  ? 116.635 119.858 79.255  1.00 66.74 ?  27  ASP A OD1   1 
ATOM   189   O  OD2   . ASP A 1 27  ? 116.612 121.190 81.000  1.00 65.33 -1 27  ASP A OD2   1 
ATOM   190   N  N     . LYS A 1 28  ? 115.893 118.330 84.701  1.00 58.49 ?  28  LYS A N     1 
ATOM   191   C  CA    . LYS A 1 28  ? 114.788 118.362 85.651  1.00 59.07 ?  28  LYS A CA    1 
ATOM   192   C  C     . LYS A 1 28  ? 114.864 119.577 86.564  1.00 59.76 ?  28  LYS A C     1 
ATOM   193   O  O     . LYS A 1 28  ? 113.831 120.047 87.053  1.00 62.05 ?  28  LYS A O     1 
ATOM   194   C  CB    . LYS A 1 28  ? 114.771 117.080 86.482  1.00 58.92 ?  28  LYS A CB    1 
ATOM   195   C  CG    . LYS A 1 28  ? 114.452 115.834 85.681  1.00 60.16 ?  28  LYS A CG    1 
ATOM   196   C  CD    . LYS A 1 28  ? 112.988 115.790 85.290  1.00 61.07 ?  28  LYS A CD    1 
ATOM   197   C  CE    . LYS A 1 28  ? 112.726 114.701 84.266  1.00 60.92 ?  28  LYS A CE    1 
ATOM   198   N  NZ    . LYS A 1 28  ? 111.275 114.554 83.975  1.00 61.66 1  28  LYS A NZ    1 
ATOM   199   N  N     . ASP A 1 29  ? 116.070 120.099 86.807  1.00 56.42 ?  29  ASP A N     1 
ATOM   200   C  CA    . ASP A 1 29  ? 116.211 121.250 87.691  1.00 54.47 ?  29  ASP A CA    1 
ATOM   201   C  C     . ASP A 1 29  ? 115.613 122.509 87.076  1.00 53.46 ?  29  ASP A C     1 
ATOM   202   O  O     . ASP A 1 29  ? 115.140 123.386 87.807  1.00 55.08 ?  29  ASP A O     1 
ATOM   203   C  CB    . ASP A 1 29  ? 117.682 121.471 88.035  1.00 52.84 ?  29  ASP A CB    1 
ATOM   204   C  CG    . ASP A 1 29  ? 117.901 121.710 89.514  1.00 56.37 ?  29  ASP A CG    1 
ATOM   205   O  OD1   . ASP A 1 29  ? 117.050 121.276 90.317  1.00 56.68 ?  29  ASP A OD1   1 
ATOM   206   O  OD2   . ASP A 1 29  ? 118.926 122.322 89.875  1.00 55.59 -1 29  ASP A OD2   1 
ATOM   207   N  N     . LYS A 1 30  ? 115.635 122.624 85.747  1.00 54.13 ?  30  LYS A N     1 
ATOM   208   C  CA    . LYS A 1 30  ? 114.925 123.717 85.092  1.00 56.39 ?  30  LYS A CA    1 
ATOM   209   C  C     . LYS A 1 30  ? 113.421 123.577 85.288  1.00 55.12 ?  30  LYS A C     1 
ATOM   210   O  O     . LYS A 1 30  ? 112.731 124.547 85.631  1.00 59.35 ?  30  LYS A O     1 
ATOM   211   C  CB    . LYS A 1 30  ? 115.278 123.754 83.606  1.00 55.60 ?  30  LYS A CB    1 
ATOM   212   C  CG    . LYS A 1 30  ? 114.634 124.894 82.839  1.00 57.24 ?  30  LYS A CG    1 
ATOM   213   C  CD    . LYS A 1 30  ? 115.597 125.487 81.823  1.00 57.04 ?  30  LYS A CD    1 
ATOM   214   C  CE    . LYS A 1 30  ? 114.977 126.668 81.098  1.00 57.35 ?  30  LYS A CE    1 
ATOM   215   N  NZ    . LYS A 1 30  ? 114.455 126.282 79.758  1.00 56.39 1  30  LYS A NZ    1 
ATOM   216   N  N     . GLU A 1 31  ? 112.897 122.366 85.093  1.00 52.94 ?  31  GLU A N     1 
ATOM   217   C  CA    . GLU A 1 31  ? 111.496 122.113 85.403  1.00 53.56 ?  31  GLU A CA    1 
ATOM   218   C  C     . GLU A 1 31  ? 111.232 122.280 86.892  1.00 54.66 ?  31  GLU A C     1 
ATOM   219   O  O     . GLU A 1 31  ? 110.166 122.761 87.290  1.00 56.52 ?  31  GLU A O     1 
ATOM   220   C  CB    . GLU A 1 31  ? 111.099 120.712 84.939  1.00 55.25 ?  31  GLU A CB    1 
ATOM   221   C  CG    . GLU A 1 31  ? 110.611 120.647 83.504  1.00 56.83 ?  31  GLU A CG    1 
ATOM   222   C  CD    . GLU A 1 31  ? 110.941 119.328 82.836  1.00 60.89 ?  31  GLU A CD    1 
ATOM   223   O  OE1   . GLU A 1 31  ? 111.694 118.531 83.433  1.00 60.98 ?  31  GLU A OE1   1 
ATOM   224   O  OE2   . GLU A 1 31  ? 110.448 119.088 81.714  1.00 58.42 -1 31  GLU A OE2   1 
ATOM   225   N  N     . ALA A 1 32  ? 112.198 121.896 87.729  1.00 50.02 ?  32  ALA A N     1 
ATOM   226   C  CA    . ALA A 1 32  ? 112.028 122.048 89.170  1.00 49.58 ?  32  ALA A CA    1 
ATOM   227   C  C     . ALA A 1 32  ? 111.875 123.512 89.558  1.00 52.01 ?  32  ALA A C     1 
ATOM   228   O  O     . ALA A 1 32  ? 110.985 123.860 90.338  1.00 51.91 ?  32  ALA A O     1 
ATOM   229   C  CB    . ALA A 1 32  ? 113.207 121.419 89.909  1.00 48.80 ?  32  ALA A CB    1 
ATOM   230   N  N     . VAL A 1 33  ? 112.718 124.390 89.010  1.00 53.52 ?  33  VAL A N     1 
ATOM   231   C  CA    . VAL A 1 33  ? 112.631 125.804 89.361  1.00 52.03 ?  33  VAL A CA    1 
ATOM   232   C  C     . VAL A 1 33  ? 111.393 126.441 88.735  1.00 52.95 ?  33  VAL A C     1 
ATOM   233   O  O     . VAL A 1 33  ? 110.762 127.320 89.336  1.00 54.60 ?  33  VAL A O     1 
ATOM   234   C  CB    . VAL A 1 33  ? 113.927 126.545 88.977  1.00 49.44 ?  33  VAL A CB    1 
ATOM   235   C  CG1   . VAL A 1 33  ? 114.055 126.712 87.474  1.00 51.09 ?  33  VAL A CG1   1 
ATOM   236   C  CG2   . VAL A 1 33  ? 113.991 127.894 89.671  1.00 49.46 ?  33  VAL A CG2   1 
ATOM   237   N  N     . HIS A 1 34  ? 111.017 126.006 87.529  1.00 50.73 ?  34  HIS A N     1 
ATOM   238   C  CA    . HIS A 1 34  ? 109.804 126.527 86.905  1.00 50.74 ?  34  HIS A CA    1 
ATOM   239   C  C     . HIS A 1 34  ? 108.578 126.190 87.749  1.00 52.66 ?  34  HIS A C     1 
ATOM   240   O  O     . HIS A 1 34  ? 107.723 127.051 88.003  1.00 53.04 ?  34  HIS A O     1 
ATOM   241   C  CB    . HIS A 1 34  ? 109.682 125.963 85.487  1.00 53.19 ?  34  HIS A CB    1 
ATOM   242   C  CG    . HIS A 1 34  ? 108.559 126.546 84.679  1.00 55.22 ?  34  HIS A CG    1 
ATOM   243   N  ND1   . HIS A 1 34  ? 107.319 126.832 85.207  1.00 54.82 ?  34  HIS A ND1   1 
ATOM   244   C  CD2   . HIS A 1 34  ? 108.501 126.898 83.374  1.00 54.74 ?  34  HIS A CD2   1 
ATOM   245   C  CE1   . HIS A 1 34  ? 106.543 127.330 84.261  1.00 55.21 ?  34  HIS A CE1   1 
ATOM   246   N  NE2   . HIS A 1 34  ? 107.238 127.384 83.139  1.00 55.54 ?  34  HIS A NE2   1 
ATOM   247   N  N     . SER A 1 35  ? 108.487 124.937 88.204  1.00 54.59 ?  35  SER A N     1 
ATOM   248   C  CA    . SER A 1 35  ? 107.392 124.538 89.079  1.00 51.97 ?  35  SER A CA    1 
ATOM   249   C  C     . SER A 1 35  ? 107.463 125.265 90.414  1.00 52.12 ?  35  SER A C     1 
ATOM   250   O  O     . SER A 1 35  ? 106.434 125.695 90.945  1.00 54.74 ?  35  SER A O     1 
ATOM   251   C  CB    . SER A 1 35  ? 107.416 123.025 89.293  1.00 51.86 ?  35  SER A CB    1 
ATOM   252   O  OG    . SER A 1 35  ? 106.655 122.665 90.431  1.00 54.09 ?  35  SER A OG    1 
ATOM   253   N  N     . TYR A 1 36  ? 108.668 125.413 90.968  1.00 51.70 ?  36  TYR A N     1 
ATOM   254   C  CA    . TYR A 1 36  ? 108.837 126.144 92.217  1.00 51.33 ?  36  TYR A CA    1 
ATOM   255   C  C     . TYR A 1 36  ? 108.240 127.534 92.109  1.00 48.41 ?  36  TYR A C     1 
ATOM   256   O  O     . TYR A 1 36  ? 107.429 127.942 92.946  1.00 48.38 ?  36  TYR A O     1 
ATOM   257   C  CB    . TYR A 1 36  ? 110.320 126.222 92.579  1.00 47.92 ?  36  TYR A CB    1 
ATOM   258   C  CG    . TYR A 1 36  ? 110.622 127.045 93.810  1.00 49.41 ?  36  TYR A CG    1 
ATOM   259   C  CD1   . TYR A 1 36  ? 110.092 126.703 95.047  1.00 47.81 ?  36  TYR A CD1   1 
ATOM   260   C  CD2   . TYR A 1 36  ? 111.444 128.160 93.736  1.00 48.66 ?  36  TYR A CD2   1 
ATOM   261   C  CE1   . TYR A 1 36  ? 110.372 127.450 96.172  1.00 46.14 ?  36  TYR A CE1   1 
ATOM   262   C  CE2   . TYR A 1 36  ? 111.728 128.914 94.856  1.00 46.68 ?  36  TYR A CE2   1 
ATOM   263   C  CZ    . TYR A 1 36  ? 111.189 128.554 96.070  1.00 48.10 ?  36  TYR A CZ    1 
ATOM   264   O  OH    . TYR A 1 36  ? 111.471 129.304 97.188  1.00 50.06 ?  36  TYR A OH    1 
ATOM   265   N  N     . PHE A 1 37  ? 108.584 128.253 91.043  1.00 52.38 ?  37  PHE A N     1 
ATOM   266   C  CA    . PHE A 1 37  ? 108.036 129.589 90.862  1.00 52.15 ?  37  PHE A CA    1 
ATOM   267   C  C     . PHE A 1 37  ? 106.524 129.538 90.701  1.00 53.54 ?  37  PHE A C     1 
ATOM   268   O  O     . PHE A 1 37  ? 105.792 130.019 91.571  1.00 56.56 ?  37  PHE A O     1 
ATOM   269   C  CB    . PHE A 1 37  ? 108.701 130.281 89.676  1.00 54.60 ?  37  PHE A CB    1 
ATOM   270   C  CG    . PHE A 1 37  ? 109.955 131.003 90.049  1.00 53.80 ?  37  PHE A CG    1 
ATOM   271   C  CD1   . PHE A 1 37  ? 109.896 132.269 90.603  1.00 51.23 ?  37  PHE A CD1   1 
ATOM   272   C  CD2   . PHE A 1 37  ? 111.189 130.406 89.882  1.00 53.12 ?  37  PHE A CD2   1 
ATOM   273   C  CE1   . PHE A 1 37  ? 111.044 132.933 90.962  1.00 52.41 ?  37  PHE A CE1   1 
ATOM   274   C  CE2   . PHE A 1 37  ? 112.339 131.066 90.238  1.00 52.36 ?  37  PHE A CE2   1 
ATOM   275   C  CZ    . PHE A 1 37  ? 112.267 132.329 90.783  1.00 52.98 ?  37  PHE A CZ    1 
ATOM   276   N  N     . VAL A 1 38  ? 106.040 128.873 89.647  1.00 56.41 ?  38  VAL A N     1 
ATOM   277   C  CA    . VAL A 1 38  ? 104.620 128.937 89.314  1.00 55.88 ?  38  VAL A CA    1 
ATOM   278   C  C     . VAL A 1 38  ? 103.718 128.232 90.316  1.00 55.62 ?  38  VAL A C     1 
ATOM   279   O  O     . VAL A 1 38  ? 102.493 128.283 90.161  1.00 57.68 ?  38  VAL A O     1 
ATOM   280   C  CB    . VAL A 1 38  ? 104.349 128.357 87.911  1.00 54.03 ?  38  VAL A CB    1 
ATOM   281   C  CG1   . VAL A 1 38  ? 105.247 129.022 86.886  1.00 55.29 ?  38  VAL A CG1   1 
ATOM   282   C  CG2   . VAL A 1 38  ? 104.531 126.849 87.911  1.00 52.16 ?  38  VAL A CG2   1 
ATOM   283   N  N     . ASP A 1 39  ? 104.272 127.578 91.339  1.00 54.34 ?  39  ASP A N     1 
ATOM   284   C  CA    . ASP A 1 39  ? 103.443 126.945 92.351  1.00 53.08 ?  39  ASP A CA    1 
ATOM   285   C  C     . ASP A 1 39  ? 103.639 127.487 93.758  1.00 57.49 ?  39  ASP A C     1 
ATOM   286   O  O     . ASP A 1 39  ? 102.749 127.300 94.594  1.00 61.79 ?  39  ASP A O     1 
ATOM   287   C  CB    . ASP A 1 39  ? 103.689 125.427 92.373  1.00 55.36 ?  39  ASP A CB    1 
ATOM   288   C  CG    . ASP A 1 39  ? 103.422 124.775 91.030  1.00 58.49 ?  39  ASP A CG    1 
ATOM   289   O  OD1   . ASP A 1 39  ? 102.555 125.277 90.286  1.00 59.03 ?  39  ASP A OD1   1 
ATOM   290   O  OD2   . ASP A 1 39  ? 104.075 123.757 90.720  1.00 58.25 -1 39  ASP A OD2   1 
ATOM   291   N  N     . TYR A 1 40  ? 104.762 128.141 94.054  1.00 56.20 ?  40  TYR A N     1 
ATOM   292   C  CA    . TYR A 1 40  ? 104.985 128.731 95.366  1.00 55.34 ?  40  TYR A CA    1 
ATOM   293   C  C     . TYR A 1 40  ? 105.231 130.229 95.301  1.00 59.10 ?  40  TYR A C     1 
ATOM   294   O  O     . TYR A 1 40  ? 104.616 130.986 96.059  1.00 61.95 ?  40  TYR A O     1 
ATOM   295   C  CB    . TYR A 1 40  ? 106.173 128.037 96.051  1.00 54.12 ?  40  TYR A CB    1 
ATOM   296   C  CG    . TYR A 1 40  ? 106.322 128.377 97.514  1.00 54.91 ?  40  TYR A CG    1 
ATOM   297   C  CD1   . TYR A 1 40  ? 105.318 128.075 98.423  1.00 55.80 ?  40  TYR A CD1   1 
ATOM   298   C  CD2   . TYR A 1 40  ? 107.466 129.004 97.985  1.00 55.91 ?  40  TYR A CD2   1 
ATOM   299   C  CE1   . TYR A 1 40  ? 105.452 128.386 99.762  1.00 57.94 ?  40  TYR A CE1   1 
ATOM   300   C  CE2   . TYR A 1 40  ? 107.609 129.318 99.321  1.00 58.46 ?  40  TYR A CE2   1 
ATOM   301   C  CZ    . TYR A 1 40  ? 106.599 129.008 100.204 1.00 60.69 ?  40  TYR A CZ    1 
ATOM   302   O  OH    . TYR A 1 40  ? 106.737 129.320 101.537 1.00 61.32 ?  40  TYR A OH    1 
ATOM   303   N  N     . ILE A 1 41  ? 106.103 130.681 94.400  1.00 55.06 ?  41  ILE A N     1 
ATOM   304   C  CA    . ILE A 1 41  ? 106.643 132.031 94.509  1.00 54.10 ?  41  ILE A CA    1 
ATOM   305   C  C     . ILE A 1 41  ? 105.640 133.056 94.000  1.00 53.77 ?  41  ILE A C     1 
ATOM   306   O  O     . ILE A 1 41  ? 105.329 134.033 94.688  1.00 56.11 ?  41  ILE A O     1 
ATOM   307   C  CB    . ILE A 1 41  ? 107.984 132.129 93.758  1.00 53.23 ?  41  ILE A CB    1 
ATOM   308   C  CG1   . ILE A 1 41  ? 109.035 131.241 94.425  1.00 51.97 ?  41  ILE A CG1   1 
ATOM   309   C  CG2   . ILE A 1 41  ? 108.464 133.568 93.712  1.00 52.91 ?  41  ILE A CG2   1 
ATOM   310   C  CD1   . ILE A 1 41  ? 109.329 131.610 95.854  1.00 49.09 ?  41  ILE A CD1   1 
ATOM   311   N  N     . ASN A 1 42  ? 105.117 132.848 92.790  1.00 55.14 ?  42  ASN A N     1 
ATOM   312   C  CA    . ASN A 1 42  ? 104.120 133.767 92.254  1.00 57.04 ?  42  ASN A CA    1 
ATOM   313   C  C     . ASN A 1 42  ? 102.855 133.770 93.100  1.00 60.67 ?  42  ASN A C     1 
ATOM   314   O  O     . ASN A 1 42  ? 102.148 134.782 93.157  1.00 60.98 ?  42  ASN A O     1 
ATOM   315   C  CB    . ASN A 1 42  ? 103.798 133.400 90.805  1.00 56.57 ?  42  ASN A CB    1 
ATOM   316   C  CG    . ASN A 1 42  ? 105.023 133.428 89.912  1.00 57.49 ?  42  ASN A CG    1 
ATOM   317   O  OD1   . ASN A 1 42  ? 106.059 133.980 90.279  1.00 61.31 ?  42  ASN A OD1   1 
ATOM   318   N  ND2   . ASN A 1 42  ? 104.910 132.831 88.733  1.00 57.43 ?  42  ASN A ND2   1 
ATOM   319   N  N     . GLN A 1 43  ? 102.552 132.650 93.759  1.00 62.95 ?  43  GLN A N     1 
ATOM   320   C  CA    . GLN A 1 43  ? 101.396 132.604 94.649  1.00 61.34 ?  43  GLN A CA    1 
ATOM   321   C  C     . GLN A 1 43  ? 101.653 133.386 95.930  1.00 59.55 ?  43  GLN A C     1 
ATOM   322   O  O     . GLN A 1 43  ? 100.784 134.137 96.390  1.00 62.85 ?  43  GLN A O     1 
ATOM   323   C  CB    . GLN A 1 43  ? 101.038 131.153 94.968  1.00 60.93 ?  43  GLN A CB    1 
ATOM   324   C  CG    . GLN A 1 43  ? 101.238 130.183 93.810  1.00 61.60 ?  43  GLN A CG    1 
ATOM   325   C  CD    . GLN A 1 43  ? 100.173 130.310 92.736  1.00 64.24 ?  43  GLN A CD    1 
ATOM   326   O  OE1   . GLN A 1 43  ? 100.083 131.327 92.047  1.00 62.89 ?  43  GLN A OE1   1 
ATOM   327   N  NE2   . GLN A 1 43  ? 99.362  129.270 92.585  1.00 62.68 ?  43  GLN A NE2   1 
ATOM   328   N  N     . ASN A 1 44  ? 102.838 133.231 96.518  1.00 54.88 ?  44  ASN A N     1 
ATOM   329   C  CA    . ASN A 1 44  ? 103.174 133.870 97.783  1.00 56.20 ?  44  ASN A CA    1 
ATOM   330   C  C     . ASN A 1 44  ? 103.755 135.267 97.616  1.00 56.44 ?  44  ASN A C     1 
ATOM   331   O  O     . ASN A 1 44  ? 104.112 135.895 98.617  1.00 57.09 ?  44  ASN A O     1 
ATOM   332   C  CB    . ASN A 1 44  ? 104.159 132.996 98.567  1.00 56.48 ?  44  ASN A CB    1 
ATOM   333   C  CG    . ASN A 1 44  ? 103.493 131.789 99.197  1.00 59.38 ?  44  ASN A CG    1 
ATOM   334   O  OD1   . ASN A 1 44  ? 103.142 131.805 100.376 1.00 60.88 ?  44  ASN A OD1   1 
ATOM   335   N  ND2   . ASN A 1 44  ? 103.314 130.734 98.411  1.00 58.08 ?  44  ASN A ND2   1 
ATOM   336   N  N     . THR A 1 45  ? 103.864 135.767 96.389  1.00 58.13 ?  45  THR A N     1 
ATOM   337   C  CA    . THR A 1 45  ? 104.401 137.096 96.143  1.00 59.07 ?  45  THR A CA    1 
ATOM   338   C  C     . THR A 1 45  ? 103.299 138.138 96.267  1.00 59.02 ?  45  THR A C     1 
ATOM   339   O  O     . THR A 1 45  ? 102.249 138.019 95.627  1.00 60.05 ?  45  THR A O     1 
ATOM   340   C  CB    . THR A 1 45  ? 105.038 137.178 94.756  1.00 58.07 ?  45  THR A CB    1 
ATOM   341   O  OG1   . THR A 1 45  ? 106.130 136.253 94.676  1.00 59.58 ?  45  THR A OG1   1 
ATOM   342   C  CG2   . THR A 1 45  ? 105.548 138.584 94.485  1.00 55.65 ?  45  THR A CG2   1 
ATOM   343   N  N     . VAL A 1 46  ? 103.540 139.156 97.091  1.00 60.32 ?  46  VAL A N     1 
ATOM   344   C  CA    . VAL A 1 46  ? 102.632 140.294 97.165  1.00 60.71 ?  46  VAL A CA    1 
ATOM   345   C  C     . VAL A 1 46  ? 102.829 141.149 95.922  1.00 60.62 ?  46  VAL A C     1 
ATOM   346   O  O     . VAL A 1 46  ? 103.945 141.596 95.629  1.00 62.72 ?  46  VAL A O     1 
ATOM   347   C  CB    . VAL A 1 46  ? 102.872 141.109 98.442  1.00 60.03 ?  46  VAL A CB    1 
ATOM   348   C  CG1   . VAL A 1 46  ? 101.791 142.161 98.608  1.00 60.24 ?  46  VAL A CG1   1 
ATOM   349   C  CG2   . VAL A 1 46  ? 102.922 140.197 99.651  1.00 59.25 ?  46  VAL A CG2   1 
ATOM   350   N  N     . PHE A 1 47  ? 101.749 141.382 95.185  1.00 64.09 ?  47  PHE A N     1 
ATOM   351   C  CA    . PHE A 1 47  ? 101.790 142.173 93.964  1.00 66.23 ?  47  PHE A CA    1 
ATOM   352   C  C     . PHE A 1 47  ? 100.948 143.425 94.149  1.00 67.45 ?  47  PHE A C     1 
ATOM   353   O  O     . PHE A 1 47  ? 99.808  143.350 94.616  1.00 67.74 ?  47  PHE A O     1 
ATOM   354   C  CB    . PHE A 1 47  ? 101.293 141.368 92.761  1.00 67.11 ?  47  PHE A CB    1 
ATOM   355   C  CG    . PHE A 1 47  ? 101.385 142.111 91.458  1.00 68.09 ?  47  PHE A CG    1 
ATOM   356   C  CD1   . PHE A 1 47  ? 102.580 142.170 90.762  1.00 67.12 ?  47  PHE A CD1   1 
ATOM   357   C  CD2   . PHE A 1 47  ? 100.274 142.745 90.927  1.00 66.60 ?  47  PHE A CD2   1 
ATOM   358   C  CE1   . PHE A 1 47  ? 102.668 142.852 89.564  1.00 67.08 ?  47  PHE A CE1   1 
ATOM   359   C  CE2   . PHE A 1 47  ? 100.355 143.428 89.729  1.00 67.40 ?  47  PHE A CE2   1 
ATOM   360   C  CZ    . PHE A 1 47  ? 101.554 143.483 89.046  1.00 68.47 ?  47  PHE A CZ    1 
ATOM   361   N  N     . PHE A 1 48  ? 101.518 144.568 93.786  1.00 66.92 ?  48  PHE A N     1 
ATOM   362   C  CA    . PHE A 1 48  ? 100.863 145.858 93.907  1.00 64.94 ?  48  PHE A CA    1 
ATOM   363   C  C     . PHE A 1 48  ? 100.465 146.359 92.527  1.00 65.55 ?  48  PHE A C     1 
ATOM   364   O  O     . PHE A 1 48  ? 101.001 145.920 91.505  1.00 67.21 ?  48  PHE A O     1 
ATOM   365   C  CB    . PHE A 1 48  ? 101.775 146.877 94.601  1.00 63.60 ?  48  PHE A CB    1 
ATOM   366   C  CG    . PHE A 1 48  ? 102.256 146.438 95.959  1.00 63.28 ?  48  PHE A CG    1 
ATOM   367   C  CD1   . PHE A 1 48  ? 101.743 147.012 97.107  1.00 64.12 ?  48  PHE A CD1   1 
ATOM   368   C  CD2   . PHE A 1 48  ? 103.240 145.470 96.085  1.00 63.11 ?  48  PHE A CD2   1 
ATOM   369   C  CE1   . PHE A 1 48  ? 102.184 146.615 98.351  1.00 65.24 ?  48  PHE A CE1   1 
ATOM   370   C  CE2   . PHE A 1 48  ? 103.684 145.071 97.327  1.00 63.83 ?  48  PHE A CE2   1 
ATOM   371   C  CZ    . PHE A 1 48  ? 103.157 145.644 98.460  1.00 64.21 ?  48  PHE A CZ    1 
ATOM   372   N  N     . HIS A 1 49  ? 99.504  147.286 92.506  1.00 68.07 ?  49  HIS A N     1 
ATOM   373   C  CA    . HIS A 1 49  ? 99.008  147.803 91.234  1.00 70.19 ?  49  HIS A CA    1 
ATOM   374   C  C     . HIS A 1 49  ? 100.114 148.496 90.449  1.00 69.96 ?  49  HIS A C     1 
ATOM   375   O  O     . HIS A 1 49  ? 100.234 148.307 89.233  1.00 70.21 ?  49  HIS A O     1 
ATOM   376   C  CB    . HIS A 1 49  ? 97.837  148.755 91.474  1.00 69.80 ?  49  HIS A CB    1 
ATOM   377   C  CG    . HIS A 1 49  ? 96.707  148.141 92.239  1.00 71.45 ?  49  HIS A CG    1 
ATOM   378   N  ND1   . HIS A 1 49  ? 96.768  147.901 93.595  1.00 71.84 ?  49  HIS A ND1   1 
ATOM   379   C  CD2   . HIS A 1 49  ? 95.486  147.716 91.838  1.00 70.55 ?  49  HIS A CD2   1 
ATOM   380   C  CE1   . HIS A 1 49  ? 95.634  147.355 93.996  1.00 69.89 ?  49  HIS A CE1   1 
ATOM   381   N  NE2   . HIS A 1 49  ? 94.839  147.232 92.948  1.00 71.70 ?  49  HIS A NE2   1 
ATOM   382   N  N     . ASN A 1 50  ? 100.933 149.297 91.125  1.00 67.49 ?  50  ASN A N     1 
ATOM   383   C  CA    . ASN A 1 50  ? 102.070 149.950 90.497  1.00 66.95 ?  50  ASN A CA    1 
ATOM   384   C  C     . ASN A 1 50  ? 103.234 149.966 91.475  1.00 65.92 ?  50  ASN A C     1 
ATOM   385   O  O     . ASN A 1 50  ? 103.071 149.714 92.671  1.00 67.91 ?  50  ASN A O     1 
ATOM   386   C  CB    . ASN A 1 50  ? 101.729 151.375 90.033  1.00 66.30 ?  50  ASN A CB    1 
ATOM   387   C  CG    . ASN A 1 50  ? 101.135 152.227 91.136  1.00 66.97 ?  50  ASN A CG    1 
ATOM   388   O  OD1   . ASN A 1 50  ? 101.047 151.804 92.287  1.00 66.48 ?  50  ASN A OD1   1 
ATOM   389   N  ND2   . ASN A 1 50  ? 100.725 153.441 90.788  1.00 66.32 ?  50  ASN A ND2   1 
ATOM   390   N  N     . LEU A 1 51  ? 104.425 150.256 90.945  1.00 60.19 ?  51  LEU A N     1 
ATOM   391   C  CA    . LEU A 1 51  ? 105.620 150.287 91.781  1.00 60.44 ?  51  LEU A CA    1 
ATOM   392   C  C     . LEU A 1 51  ? 105.532 151.369 92.849  1.00 62.18 ?  51  LEU A C     1 
ATOM   393   O  O     . LEU A 1 51  ? 106.133 151.230 93.921  1.00 64.40 ?  51  LEU A O     1 
ATOM   394   C  CB    . LEU A 1 51  ? 106.860 150.494 90.911  1.00 61.12 ?  51  LEU A CB    1 
ATOM   395   C  CG    . LEU A 1 51  ? 108.208 150.587 91.630  1.00 58.98 ?  51  LEU A CG    1 
ATOM   396   C  CD1   . LEU A 1 51  ? 108.534 149.279 92.329  1.00 58.21 ?  51  LEU A CD1   1 
ATOM   397   C  CD2   . LEU A 1 51  ? 109.309 150.978 90.663  1.00 58.63 ?  51  LEU A CD2   1 
ATOM   398   N  N     . LYS A 1 52  ? 104.800 152.453 92.579  1.00 62.24 ?  52  LYS A N     1 
ATOM   399   C  CA    . LYS A 1 52  ? 104.657 153.515 93.569  1.00 60.33 ?  52  LYS A CA    1 
ATOM   400   C  C     . LYS A 1 52  ? 103.961 153.009 94.824  1.00 61.87 ?  52  LYS A C     1 
ATOM   401   O  O     . LYS A 1 52  ? 104.398 153.299 95.945  1.00 61.87 ?  52  LYS A O     1 
ATOM   402   C  CB    . LYS A 1 52  ? 103.891 154.693 92.969  1.00 59.33 ?  52  LYS A CB    1 
ATOM   403   C  CG    . LYS A 1 52  ? 104.139 156.017 93.671  1.00 62.17 ?  52  LYS A CG    1 
ATOM   404   C  CD    . LYS A 1 52  ? 103.976 157.185 92.711  1.00 63.90 ?  52  LYS A CD    1 
ATOM   405   C  CE    . LYS A 1 52  ? 104.830 158.371 93.130  1.00 63.03 ?  52  LYS A CE    1 
ATOM   406   N  NZ    . LYS A 1 52  ? 105.088 158.383 94.596  1.00 61.51 1  52  LYS A NZ    1 
ATOM   407   N  N     . GLU A 1 53  ? 102.881 152.245 94.655  1.00 65.07 ?  53  GLU A N     1 
ATOM   408   C  CA    . GLU A 1 53  ? 102.189 151.676 95.806  1.00 65.62 ?  53  GLU A CA    1 
ATOM   409   C  C     . GLU A 1 53  ? 103.094 150.711 96.560  1.00 64.75 ?  53  GLU A C     1 
ATOM   410   O  O     . GLU A 1 53  ? 103.098 150.692 97.795  1.00 65.93 ?  53  GLU A O     1 
ATOM   411   C  CB    . GLU A 1 53  ? 100.907 150.977 95.354  1.00 65.41 ?  53  GLU A CB    1 
ATOM   412   C  CG    . GLU A 1 53  ? 100.251 150.113 96.418  1.00 67.11 ?  53  GLU A CG    1 
ATOM   413   C  CD    . GLU A 1 53  ? 99.018  149.395 95.903  1.00 69.03 ?  53  GLU A CD    1 
ATOM   414   O  OE1   . GLU A 1 53  ? 98.530  149.757 94.812  1.00 69.01 ?  53  GLU A OE1   1 
ATOM   415   O  OE2   . GLU A 1 53  ? 98.538  148.469 96.589  1.00 68.53 -1 53  GLU A OE2   1 
ATOM   416   N  N     . LYS A 1 54  ? 103.877 149.914 95.832  1.00 60.53 ?  54  LYS A N     1 
ATOM   417   C  CA    . LYS A 1 54  ? 104.795 148.977 96.474  1.00 62.09 ?  54  LYS A CA    1 
ATOM   418   C  C     . LYS A 1 54  ? 105.827 149.709 97.321  1.00 58.42 ?  54  LYS A C     1 
ATOM   419   O  O     . LYS A 1 54  ? 106.068 149.349 98.481  1.00 60.89 ?  54  LYS A O     1 
ATOM   420   C  CB    . LYS A 1 54  ? 105.483 148.120 95.412  1.00 61.73 ?  54  LYS A CB    1 
ATOM   421   C  CG    . LYS A 1 54  ? 106.604 147.253 95.948  1.00 59.32 ?  54  LYS A CG    1 
ATOM   422   C  CD    . LYS A 1 54  ? 106.949 146.143 94.977  1.00 59.69 ?  54  LYS A CD    1 
ATOM   423   C  CE    . LYS A 1 54  ? 107.905 145.146 95.600  1.00 60.84 ?  54  LYS A CE    1 
ATOM   424   N  NZ    . LYS A 1 54  ? 107.873 143.835 94.897  1.00 61.90 1  54  LYS A NZ    1 
ATOM   425   N  N     . LEU A 1 55  ? 106.449 150.744 96.755  1.00 56.48 ?  55  LEU A N     1 
ATOM   426   C  CA    . LEU A 1 55  ? 107.475 151.478 97.488  1.00 58.32 ?  55  LEU A CA    1 
ATOM   427   C  C     . LEU A 1 55  ? 106.881 152.221 98.677  1.00 61.53 ?  55  LEU A C     1 
ATOM   428   O  O     . LEU A 1 55  ? 107.491 152.264 99.752  1.00 63.78 ?  55  LEU A O     1 
ATOM   429   C  CB    . LEU A 1 55  ? 108.201 152.442 96.553  1.00 59.39 ?  55  LEU A CB    1 
ATOM   430   C  CG    . LEU A 1 55  ? 109.078 151.770 95.496  1.00 59.74 ?  55  LEU A CG    1 
ATOM   431   C  CD1   . LEU A 1 55  ? 109.679 152.806 94.568  1.00 59.60 ?  55  LEU A CD1   1 
ATOM   432   C  CD2   . LEU A 1 55  ? 110.165 150.935 96.151  1.00 59.41 ?  55  LEU A CD2   1 
ATOM   433   N  N     . ASP A 1 56  ? 105.695 152.811 98.509  1.00 65.92 ?  56  ASP A N     1 
ATOM   434   C  CA    . ASP A 1 56  ? 105.043 153.477 99.630  1.00 64.75 ?  56  ASP A CA    1 
ATOM   435   C  C     . ASP A 1 56  ? 104.713 152.486 100.739 1.00 64.19 ?  56  ASP A C     1 
ATOM   436   O  O     . ASP A 1 56  ? 104.919 152.777 101.922 1.00 65.16 ?  56  ASP A O     1 
ATOM   437   C  CB    . ASP A 1 56  ? 103.780 154.191 99.149  1.00 65.50 ?  56  ASP A CB    1 
ATOM   438   C  CG    . ASP A 1 56  ? 104.088 155.429 98.330  1.00 68.31 ?  56  ASP A CG    1 
ATOM   439   O  OD1   . ASP A 1 56  ? 105.201 155.976 98.473  1.00 67.57 ?  56  ASP A OD1   1 
ATOM   440   O  OD2   . ASP A 1 56  ? 103.217 155.857 97.543  1.00 67.50 -1 56  ASP A OD2   1 
ATOM   441   N  N     . TYR A 1 57  ? 104.215 151.304 100.371 1.00 59.50 ?  57  TYR A N     1 
ATOM   442   C  CA    . TYR A 1 57  ? 103.899 150.279 101.359 1.00 62.04 ?  57  TYR A CA    1 
ATOM   443   C  C     . TYR A 1 57  ? 105.148 149.831 102.103 1.00 61.86 ?  57  TYR A C     1 
ATOM   444   O  O     . TYR A 1 57  ? 105.114 149.621 103.321 1.00 63.68 ?  57  TYR A O     1 
ATOM   445   C  CB    . TYR A 1 57  ? 103.238 149.089 100.662 1.00 61.52 ?  57  TYR A CB    1 
ATOM   446   C  CG    . TYR A 1 57  ? 103.035 147.876 101.537 1.00 62.14 ?  57  TYR A CG    1 
ATOM   447   C  CD1   . TYR A 1 57  ? 101.985 147.817 102.442 1.00 62.07 ?  57  TYR A CD1   1 
ATOM   448   C  CD2   . TYR A 1 57  ? 103.905 146.797 101.475 1.00 63.16 ?  57  TYR A CD2   1 
ATOM   449   C  CE1   . TYR A 1 57  ? 101.794 146.706 103.238 1.00 62.91 ?  57  TYR A CE1   1 
ATOM   450   C  CE2   . TYR A 1 57  ? 103.727 145.689 102.275 1.00 63.73 ?  57  TYR A CE2   1 
ATOM   451   C  CZ    . TYR A 1 57  ? 102.671 145.650 103.156 1.00 63.36 ?  57  TYR A CZ    1 
ATOM   452   O  OH    . TYR A 1 57  ? 102.491 144.545 103.955 1.00 62.05 ?  57  TYR A OH    1 
ATOM   453   N  N     . LEU A 1 58  ? 106.262 149.672 101.384 1.00 56.04 ?  58  LEU A N     1 
ATOM   454   C  CA    . LEU A 1 58  ? 107.483 149.188 102.018 1.00 54.62 ?  58  LEU A CA    1 
ATOM   455   C  C     . LEU A 1 58  ? 108.110 150.251 102.912 1.00 55.12 ?  58  LEU A C     1 
ATOM   456   O  O     . LEU A 1 58  ? 108.645 149.932 103.980 1.00 58.06 ?  58  LEU A O     1 
ATOM   457   C  CB    . LEU A 1 58  ? 108.474 148.723 100.952 1.00 56.32 ?  58  LEU A CB    1 
ATOM   458   C  CG    . LEU A 1 58  ? 108.043 147.477 100.177 1.00 56.27 ?  58  LEU A CG    1 
ATOM   459   C  CD1   . LEU A 1 58  ? 108.800 147.369 98.869  1.00 55.04 ?  58  LEU A CD1   1 
ATOM   460   C  CD2   . LEU A 1 58  ? 108.237 146.228 101.013 1.00 56.23 ?  58  LEU A CD2   1 
ATOM   461   N  N     . VAL A 1 59  ? 108.063 151.517 102.496 1.00 60.11 ?  59  VAL A N     1 
ATOM   462   C  CA    . VAL A 1 59  ? 108.630 152.584 103.316 1.00 62.24 ?  59  VAL A CA    1 
ATOM   463   C  C     . VAL A 1 59  ? 107.778 152.816 104.558 1.00 64.10 ?  59  VAL A C     1 
ATOM   464   O  O     . VAL A 1 59  ? 108.299 152.954 105.670 1.00 63.20 ?  59  VAL A O     1 
ATOM   465   C  CB    . VAL A 1 59  ? 108.787 153.872 102.488 1.00 62.74 ?  59  VAL A CB    1 
ATOM   466   C  CG1   . VAL A 1 59  ? 109.193 155.031 103.381 1.00 60.59 ?  59  VAL A CG1   1 
ATOM   467   C  CG2   . VAL A 1 59  ? 109.816 153.669 101.386 1.00 62.18 ?  59  VAL A CG2   1 
ATOM   468   N  N     . GLU A 1 60  ? 106.453 152.860 104.388 1.00 64.88 ?  60  GLU A N     1 
ATOM   469   C  CA    . GLU A 1 60  ? 105.571 153.181 105.505 1.00 64.28 ?  60  GLU A CA    1 
ATOM   470   C  C     . GLU A 1 60  ? 105.608 152.106 106.584 1.00 65.21 ?  60  GLU A C     1 
ATOM   471   O  O     . GLU A 1 60  ? 105.582 152.421 107.780 1.00 67.47 ?  60  GLU A O     1 
ATOM   472   C  CB    . GLU A 1 60  ? 104.143 153.389 105.000 1.00 64.16 ?  60  GLU A CB    1 
ATOM   473   C  CG    . GLU A 1 60  ? 103.947 154.683 104.223 1.00 65.72 ?  60  GLU A CG    1 
ATOM   474   C  CD    . GLU A 1 60  ? 102.742 154.638 103.302 1.00 69.17 ?  60  GLU A CD    1 
ATOM   475   O  OE1   . GLU A 1 60  ? 101.938 153.689 103.416 1.00 68.12 ?  60  GLU A OE1   1 
ATOM   476   O  OE2   . GLU A 1 60  ? 102.599 155.551 102.462 1.00 67.57 -1 60  GLU A OE2   1 
ATOM   477   N  N     . ASN A 1 61  ? 105.666 150.835 106.190 1.00 59.25 ?  61  ASN A N     1 
ATOM   478   C  CA    . ASN A 1 61  ? 105.643 149.738 107.152 1.00 60.01 ?  61  ASN A CA    1 
ATOM   479   C  C     . ASN A 1 61  ? 107.029 149.319 107.617 1.00 61.33 ?  61  ASN A C     1 
ATOM   480   O  O     . ASN A 1 61  ? 107.211 148.151 107.984 1.00 64.86 ?  61  ASN A O     1 
ATOM   481   C  CB    . ASN A 1 61  ? 104.898 148.536 106.573 1.00 60.81 ?  61  ASN A CB    1 
ATOM   482   C  CG    . ASN A 1 61  ? 103.519 148.899 106.076 1.00 62.46 ?  61  ASN A CG    1 
ATOM   483   O  OD1   . ASN A 1 61  ? 103.181 150.074 105.951 1.00 63.19 ?  61  ASN A OD1   1 
ATOM   484   N  ND2   . ASN A 1 61  ? 102.698 147.891 105.832 1.00 61.88 ?  61  ASN A ND2   1 
ATOM   485   N  N     . GLN A 1 62  ? 107.998 150.235 107.595 1.00 57.49 ?  62  GLN A N     1 
ATOM   486   C  CA    . GLN A 1 62  ? 109.310 150.026 108.207 1.00 58.44 ?  62  GLN A CA    1 
ATOM   487   C  C     . GLN A 1 62  ? 110.078 148.882 107.553 1.00 57.89 ?  62  GLN A C     1 
ATOM   488   O  O     . GLN A 1 62  ? 110.880 148.208 108.204 1.00 58.51 ?  62  GLN A O     1 
ATOM   489   C  CB    . GLN A 1 62  ? 109.182 149.784 109.714 1.00 58.21 ?  62  GLN A CB    1 
ATOM   490   C  CG    . GLN A 1 62  ? 108.459 150.889 110.473 1.00 57.65 ?  62  GLN A CG    1 
ATOM   491   C  CD    . GLN A 1 62  ? 109.029 152.265 110.199 1.00 60.19 ?  62  GLN A CD    1 
ATOM   492   O  OE1   . GLN A 1 62  ? 109.992 152.691 110.836 1.00 59.91 ?  62  GLN A OE1   1 
ATOM   493   N  NE2   . GLN A 1 62  ? 108.438 152.968 109.241 1.00 58.82 ?  62  GLN A NE2   1 
ATOM   494   N  N     . TYR A 1 63  ? 109.841 148.646 106.262 1.00 55.04 ?  63  TYR A N     1 
ATOM   495   C  CA    . TYR A 1 63  ? 110.607 147.643 105.534 1.00 53.55 ?  63  TYR A CA    1 
ATOM   496   C  C     . TYR A 1 63  ? 111.838 148.240 104.866 1.00 53.47 ?  63  TYR A C     1 
ATOM   497   O  O     . TYR A 1 63  ? 112.907 147.620 104.874 1.00 52.88 ?  63  TYR A O     1 
ATOM   498   C  CB    . TYR A 1 63  ? 109.728 146.960 104.482 1.00 52.78 ?  63  TYR A CB    1 
ATOM   499   C  CG    . TYR A 1 63  ? 108.720 145.996 105.060 1.00 53.89 ?  63  TYR A CG    1 
ATOM   500   C  CD1   . TYR A 1 63  ? 109.114 144.988 105.928 1.00 52.87 ?  63  TYR A CD1   1 
ATOM   501   C  CD2   . TYR A 1 63  ? 107.375 146.091 104.734 1.00 55.05 ?  63  TYR A CD2   1 
ATOM   502   C  CE1   . TYR A 1 63  ? 108.196 144.104 106.458 1.00 53.91 ?  63  TYR A CE1   1 
ATOM   503   C  CE2   . TYR A 1 63  ? 106.449 145.213 105.259 1.00 55.36 ?  63  TYR A CE2   1 
ATOM   504   C  CZ    . TYR A 1 63  ? 106.866 144.222 106.120 1.00 56.36 ?  63  TYR A CZ    1 
ATOM   505   O  OH    . TYR A 1 63  ? 105.946 143.345 106.644 1.00 55.76 ?  63  TYR A OH    1 
ATOM   506   N  N     . TYR A 1 64  ? 111.708 149.432 104.296 1.00 49.94 ?  64  TYR A N     1 
ATOM   507   C  CA    . TYR A 1 64  ? 112.799 150.114 103.621 1.00 48.26 ?  64  TYR A CA    1 
ATOM   508   C  C     . TYR A 1 64  ? 113.219 151.345 104.411 1.00 50.88 ?  64  TYR A C     1 
ATOM   509   O  O     . TYR A 1 64  ? 112.610 151.707 105.420 1.00 53.87 ?  64  TYR A O     1 
ATOM   510   C  CB    . TYR A 1 64  ? 112.392 150.520 102.201 1.00 47.96 ?  64  TYR A CB    1 
ATOM   511   C  CG    . TYR A 1 64  ? 112.447 149.396 101.198 1.00 50.04 ?  64  TYR A CG    1 
ATOM   512   C  CD1   . TYR A 1 64  ? 112.938 148.146 101.550 1.00 48.97 ?  64  TYR A CD1   1 
ATOM   513   C  CD2   . TYR A 1 64  ? 112.010 149.584 99.896  1.00 49.89 ?  64  TYR A CD2   1 
ATOM   514   C  CE1   . TYR A 1 64  ? 112.988 147.117 100.636 1.00 45.60 ?  64  TYR A CE1   1 
ATOM   515   C  CE2   . TYR A 1 64  ? 112.059 148.564 98.976  1.00 48.10 ?  64  TYR A CE2   1 
ATOM   516   C  CZ    . TYR A 1 64  ? 112.547 147.333 99.349  1.00 47.41 ?  64  TYR A CZ    1 
ATOM   517   O  OH    . TYR A 1 64  ? 112.592 146.316 98.428  1.00 50.79 ?  64  TYR A OH    1 
ATOM   518   N  N     . GLU A 1 65  ? 114.277 151.989 103.934 1.00 53.79 ?  65  GLU A N     1 
ATOM   519   C  CA    . GLU A 1 65  ? 114.733 153.259 104.479 1.00 52.12 ?  65  GLU A CA    1 
ATOM   520   C  C     . GLU A 1 65  ? 114.316 154.379 103.538 1.00 55.07 ?  65  GLU A C     1 
ATOM   521   O  O     . GLU A 1 65  ? 114.521 154.286 102.324 1.00 56.78 ?  65  GLU A O     1 
ATOM   522   C  CB    . GLU A 1 65  ? 116.249 153.265 104.675 1.00 52.60 ?  65  GLU A CB    1 
ATOM   523   C  CG    . GLU A 1 65  ? 116.780 152.075 105.451 1.00 51.39 ?  65  GLU A CG    1 
ATOM   524   C  CD    . GLU A 1 65  ? 118.294 152.054 105.518 1.00 55.09 ?  65  GLU A CD    1 
ATOM   525   O  OE1   . GLU A 1 65  ? 118.940 152.453 104.526 1.00 57.01 ?  65  GLU A OE1   1 
ATOM   526   O  OE2   . GLU A 1 65  ? 118.837 151.640 106.563 1.00 54.12 -1 65  GLU A OE2   1 
ATOM   527   N  N     . GLU A 1 66  ? 113.721 155.431 104.100 1.00 58.01 ?  66  GLU A N     1 
ATOM   528   C  CA    . GLU A 1 66  ? 113.262 156.549 103.286 1.00 56.33 ?  66  GLU A CA    1 
ATOM   529   C  C     . GLU A 1 66  ? 114.412 157.413 102.787 1.00 56.91 ?  66  GLU A C     1 
ATOM   530   O  O     . GLU A 1 66  ? 114.303 158.003 101.707 1.00 57.92 ?  66  GLU A O     1 
ATOM   531   C  CB    . GLU A 1 66  ? 112.271 157.396 104.088 1.00 57.09 ?  66  GLU A CB    1 
ATOM   532   C  CG    . GLU A 1 66  ? 111.790 158.667 103.397 1.00 59.42 ?  66  GLU A CG    1 
ATOM   533   C  CD    . GLU A 1 66  ? 110.862 158.388 102.228 1.00 61.01 ?  66  GLU A CD    1 
ATOM   534   O  OE1   . GLU A 1 66  ? 109.653 158.682 102.347 1.00 58.42 ?  66  GLU A OE1   1 
ATOM   535   O  OE2   . GLU A 1 66  ? 111.339 157.891 101.186 1.00 62.31 -1 66  GLU A OE2   1 
ATOM   536   N  N     . GLU A 1 67  ? 115.512 157.488 103.540 1.00 58.05 ?  67  GLU A N     1 
ATOM   537   C  CA    . GLU A 1 67  ? 116.578 158.433 103.221 1.00 56.47 ?  67  GLU A CA    1 
ATOM   538   C  C     . GLU A 1 67  ? 117.215 158.133 101.869 1.00 57.31 ?  67  GLU A C     1 
ATOM   539   O  O     . GLU A 1 67  ? 117.431 159.045 101.061 1.00 57.76 ?  67  GLU A O     1 
ATOM   540   C  CB    . GLU A 1 67  ? 117.632 158.421 104.328 1.00 56.92 ?  67  GLU A CB    1 
ATOM   541   C  CG    . GLU A 1 67  ? 117.786 157.078 105.022 1.00 58.91 ?  67  GLU A CG    1 
ATOM   542   C  CD    . GLU A 1 67  ? 117.007 157.001 106.320 1.00 59.42 ?  67  GLU A CD    1 
ATOM   543   O  OE1   . GLU A 1 67  ? 115.760 156.949 106.266 1.00 57.57 ?  67  GLU A OE1   1 
ATOM   544   O  OE2   . GLU A 1 67  ? 117.642 156.997 107.395 1.00 62.17 -1 67  GLU A OE2   1 
ATOM   545   N  N     . PHE A 1 68  ? 117.524 156.864 101.599 1.00 54.61 ?  68  PHE A N     1 
ATOM   546   C  CA    . PHE A 1 68  ? 118.205 156.537 100.350 1.00 52.02 ?  68  PHE A CA    1 
ATOM   547   C  C     . PHE A 1 68  ? 117.256 156.561 99.159  1.00 51.81 ?  68  PHE A C     1 
ATOM   548   O  O     . PHE A 1 68  ? 117.681 156.875 98.043  1.00 55.05 ?  68  PHE A O     1 
ATOM   549   C  CB    . PHE A 1 68  ? 118.905 155.178 100.465 1.00 51.38 ?  68  PHE A CB    1 
ATOM   550   C  CG    . PHE A 1 68  ? 118.053 154.007 100.061 1.00 50.85 ?  68  PHE A CG    1 
ATOM   551   C  CD1   . PHE A 1 68  ? 117.172 153.434 100.958 1.00 51.28 ?  68  PHE A CD1   1 
ATOM   552   C  CD2   . PHE A 1 68  ? 118.162 153.460 98.793  1.00 48.03 ?  68  PHE A CD2   1 
ATOM   553   C  CE1   . PHE A 1 68  ? 116.395 152.353 100.590 1.00 48.97 ?  68  PHE A CE1   1 
ATOM   554   C  CE2   . PHE A 1 68  ? 117.390 152.380 98.422  1.00 46.98 ?  68  PHE A CE2   1 
ATOM   555   C  CZ    . PHE A 1 68  ? 116.509 151.824 99.322  1.00 48.15 ?  68  PHE A CZ    1 
ATOM   556   N  N     . LEU A 1 69  ? 115.979 156.239 99.371  1.00 50.98 ?  69  LEU A N     1 
ATOM   557   C  CA    . LEU A 1 69  ? 115.007 156.316 98.287  1.00 53.18 ?  69  LEU A CA    1 
ATOM   558   C  C     . LEU A 1 69  ? 114.601 157.749 97.977  1.00 53.68 ?  69  LEU A C     1 
ATOM   559   O  O     . LEU A 1 69  ? 114.044 158.004 96.904  1.00 54.19 ?  69  LEU A O     1 
ATOM   560   C  CB    . LEU A 1 69  ? 113.767 155.490 98.629  1.00 54.09 ?  69  LEU A CB    1 
ATOM   561   C  CG    . LEU A 1 69  ? 113.884 153.978 98.439  1.00 52.44 ?  69  LEU A CG    1 
ATOM   562   C  CD1   . LEU A 1 69  ? 112.697 153.264 99.062  1.00 51.87 ?  69  LEU A CD1   1 
ATOM   563   C  CD2   . LEU A 1 69  ? 114.010 153.631 96.968  1.00 50.13 ?  69  LEU A CD2   1 
ATOM   564   N  N     . SER A 1 70  ? 114.866 158.688 98.886  1.00 55.83 ?  70  SER A N     1 
ATOM   565   C  CA    . SER A 1 70  ? 114.491 160.081 98.682  1.00 54.06 ?  70  SER A CA    1 
ATOM   566   C  C     . SER A 1 70  ? 115.468 160.839 97.795  1.00 53.45 ?  70  SER A C     1 
ATOM   567   O  O     . SER A 1 70  ? 115.168 161.971 97.404  1.00 56.79 ?  70  SER A O     1 
ATOM   568   C  CB    . SER A 1 70  ? 114.368 160.794 100.031 1.00 54.37 ?  70  SER A CB    1 
ATOM   569   O  OG    . SER A 1 70  ? 115.638 160.972 100.630 1.00 54.27 ?  70  SER A OG    1 
ATOM   570   N  N     . LEU A 1 71  ? 116.620 160.252 97.470  1.00 50.47 ?  71  LEU A N     1 
ATOM   571   C  CA    . LEU A 1 71  ? 117.582 160.905 96.594  1.00 50.14 ?  71  LEU A CA    1 
ATOM   572   C  C     . LEU A 1 71  ? 117.235 160.758 95.120  1.00 50.99 ?  71  LEU A C     1 
ATOM   573   O  O     . LEU A 1 71  ? 117.898 161.375 94.280  1.00 50.24 ?  71  LEU A O     1 
ATOM   574   C  CB    . LEU A 1 71  ? 118.987 160.351 96.846  1.00 48.19 ?  71  LEU A CB    1 
ATOM   575   C  CG    . LEU A 1 71  ? 119.352 160.079 98.304  1.00 49.88 ?  71  LEU A CG    1 
ATOM   576   C  CD1   . LEU A 1 71  ? 120.400 158.986 98.396  1.00 51.77 ?  71  LEU A CD1   1 
ATOM   577   C  CD2   . LEU A 1 71  ? 119.842 161.351 98.973  1.00 51.24 ?  71  LEU A CD2   1 
ATOM   578   N  N     . TYR A 1 72  ? 116.222 159.963 94.788  1.00 48.11 ?  72  TYR A N     1 
ATOM   579   C  CA    . TYR A 1 72  ? 115.782 159.771 93.416  1.00 50.38 ?  72  TYR A CA    1 
ATOM   580   C  C     . TYR A 1 72  ? 114.327 160.192 93.280  1.00 52.50 ?  72  TYR A C     1 
ATOM   581   O  O     . TYR A 1 72  ? 113.504 159.901 94.153  1.00 52.67 ?  72  TYR A O     1 
ATOM   582   C  CB    . TYR A 1 72  ? 115.912 158.308 92.973  1.00 48.01 ?  72  TYR A CB    1 
ATOM   583   C  CG    . TYR A 1 72  ? 117.227 157.644 93.296  1.00 47.76 ?  72  TYR A CG    1 
ATOM   584   C  CD1   . TYR A 1 72  ? 117.444 157.056 94.535  1.00 46.66 ?  72  TYR A CD1   1 
ATOM   585   C  CD2   . TYR A 1 72  ? 118.240 157.574 92.351  1.00 46.11 ?  72  TYR A CD2   1 
ATOM   586   C  CE1   . TYR A 1 72  ? 118.638 156.439 94.830  1.00 44.18 ?  72  TYR A CE1   1 
ATOM   587   C  CE2   . TYR A 1 72  ? 119.436 156.956 92.637  1.00 42.59 ?  72  TYR A CE2   1 
ATOM   588   C  CZ    . TYR A 1 72  ? 119.630 156.391 93.877  1.00 44.18 ?  72  TYR A CZ    1 
ATOM   589   O  OH    . TYR A 1 72  ? 120.823 155.775 94.167  1.00 49.45 ?  72  TYR A OH    1 
ATOM   590   N  N     . SER A 1 73  ? 114.015 160.877 92.185  1.00 55.03 ?  73  SER A N     1 
ATOM   591   C  CA    . SER A 1 73  ? 112.623 161.045 91.802  1.00 56.45 ?  73  SER A CA    1 
ATOM   592   C  C     . SER A 1 73  ? 112.047 159.691 91.406  1.00 57.84 ?  73  SER A C     1 
ATOM   593   O  O     . SER A 1 73  ? 112.764 158.808 90.928  1.00 58.76 ?  73  SER A O     1 
ATOM   594   C  CB    . SER A 1 73  ? 112.495 162.036 90.646  1.00 57.18 ?  73  SER A CB    1 
ATOM   595   O  OG    . SER A 1 73  ? 112.702 161.397 89.400  1.00 57.54 ?  73  SER A OG    1 
ATOM   596   N  N     . PHE A 1 74  ? 110.740 159.522 91.621  1.00 58.15 ?  74  PHE A N     1 
ATOM   597   C  CA    . PHE A 1 74  ? 110.135 158.221 91.362  1.00 55.90 ?  74  PHE A CA    1 
ATOM   598   C  C     . PHE A 1 74  ? 110.261 157.790 89.909  1.00 58.32 ?  74  PHE A C     1 
ATOM   599   O  O     . PHE A 1 74  ? 110.228 156.588 89.630  1.00 60.17 ?  74  PHE A O     1 
ATOM   600   C  CB    . PHE A 1 74  ? 108.661 158.202 91.762  1.00 58.40 ?  74  PHE A CB    1 
ATOM   601   C  CG    . PHE A 1 74  ? 108.012 156.869 91.540  1.00 58.85 ?  74  PHE A CG    1 
ATOM   602   C  CD1   . PHE A 1 74  ? 108.296 155.801 92.372  1.00 57.77 ?  74  PHE A CD1   1 
ATOM   603   C  CD2   . PHE A 1 74  ? 107.152 156.674 90.472  1.00 58.58 ?  74  PHE A CD2   1 
ATOM   604   C  CE1   . PHE A 1 74  ? 107.718 154.568 92.155  1.00 59.26 ?  74  PHE A CE1   1 
ATOM   605   C  CE2   . PHE A 1 74  ? 106.570 155.444 90.253  1.00 59.84 ?  74  PHE A CE2   1 
ATOM   606   C  CZ    . PHE A 1 74  ? 106.855 154.391 91.093  1.00 61.18 ?  74  PHE A CZ    1 
ATOM   607   N  N     . GLU A 1 75  ? 110.406 158.731 88.974  1.00 61.63 ?  75  GLU A N     1 
ATOM   608   C  CA    . GLU A 1 75  ? 110.654 158.341 87.592  1.00 61.08 ?  75  GLU A CA    1 
ATOM   609   C  C     . GLU A 1 75  ? 111.992 157.622 87.462  1.00 62.99 ?  75  GLU A C     1 
ATOM   610   O  O     . GLU A 1 75  ? 112.110 156.641 86.721  1.00 62.51 ?  75  GLU A O     1 
ATOM   611   C  CB    . GLU A 1 75  ? 110.601 159.566 86.681  1.00 60.87 ?  75  GLU A CB    1 
ATOM   612   C  CG    . GLU A 1 75  ? 109.196 160.106 86.472  1.00 62.72 ?  75  GLU A CG    1 
ATOM   613   C  CD    . GLU A 1 75  ? 108.208 159.023 86.080  1.00 65.19 ?  75  GLU A CD    1 
ATOM   614   O  OE1   . GLU A 1 75  ? 108.413 158.380 85.028  1.00 65.33 ?  75  GLU A OE1   1 
ATOM   615   O  OE2   . GLU A 1 75  ? 107.228 158.812 86.823  1.00 64.89 -1 75  GLU A OE2   1 
ATOM   616   N  N     . ASP A 1 76  ? 113.006 158.088 88.193  1.00 58.05 ?  76  ASP A N     1 
ATOM   617   C  CA    . ASP A 1 76  ? 114.308 157.427 88.167  1.00 55.77 ?  76  ASP A CA    1 
ATOM   618   C  C     . ASP A 1 76  ? 114.244 156.038 88.793  1.00 55.43 ?  76  ASP A C     1 
ATOM   619   O  O     . ASP A 1 76  ? 114.848 155.090 88.276  1.00 60.04 ?  76  ASP A O     1 
ATOM   620   C  CB    . ASP A 1 76  ? 115.340 158.293 88.883  1.00 57.42 ?  76  ASP A CB    1 
ATOM   621   C  CG    . ASP A 1 76  ? 115.489 159.662 88.250  1.00 60.39 ?  76  ASP A CG    1 
ATOM   622   O  OD1   . ASP A 1 76  ? 115.447 159.749 87.005  1.00 59.97 ?  76  ASP A OD1   1 
ATOM   623   O  OD2   . ASP A 1 76  ? 115.648 160.650 88.996  1.00 59.16 -1 76  ASP A OD2   1 
ATOM   624   N  N     . ILE A 1 77  ? 113.528 155.899 89.911  1.00 51.09 ?  77  ILE A N     1 
ATOM   625   C  CA    . ILE A 1 77  ? 113.371 154.587 90.535  1.00 51.47 ?  77  ILE A CA    1 
ATOM   626   C  C     . ILE A 1 77  ? 112.623 153.646 89.601  1.00 51.41 ?  77  ILE A C     1 
ATOM   627   O  O     . ILE A 1 77  ? 112.954 152.458 89.489  1.00 53.07 ?  77  ILE A O     1 
ATOM   628   C  CB    . ILE A 1 77  ? 112.657 154.722 91.891  1.00 52.51 ?  77  ILE A CB    1 
ATOM   629   C  CG1   . ILE A 1 77  ? 113.325 155.803 92.738  1.00 52.79 ?  77  ILE A CG1   1 
ATOM   630   C  CG2   . ILE A 1 77  ? 112.656 153.391 92.621  1.00 51.51 ?  77  ILE A CG2   1 
ATOM   631   C  CD1   . ILE A 1 77  ? 112.924 155.777 94.194  1.00 52.94 ?  77  ILE A CD1   1 
ATOM   632   N  N     . LYS A 1 78  ? 111.596 154.161 88.925  1.00 54.77 ?  78  LYS A N     1 
ATOM   633   C  CA    . LYS A 1 78  ? 110.868 153.366 87.947  1.00 54.72 ?  78  LYS A CA    1 
ATOM   634   C  C     . LYS A 1 78  ? 111.780 152.924 86.814  1.00 54.66 ?  78  LYS A C     1 
ATOM   635   O  O     . LYS A 1 78  ? 111.714 151.774 86.373  1.00 57.65 ?  78  LYS A O     1 
ATOM   636   C  CB    . LYS A 1 78  ? 109.685 154.167 87.405  1.00 57.81 ?  78  LYS A CB    1 
ATOM   637   C  CG    . LYS A 1 78  ? 108.468 153.334 87.047  1.00 56.70 ?  78  LYS A CG    1 
ATOM   638   C  CD    . LYS A 1 78  ? 107.410 154.189 86.372  1.00 56.73 ?  78  LYS A CD    1 
ATOM   639   C  CE    . LYS A 1 78  ? 106.631 153.394 85.342  1.00 57.73 ?  78  LYS A CE    1 
ATOM   640   N  NZ    . LYS A 1 78  ? 105.208 153.220 85.744  1.00 57.58 1  78  LYS A NZ    1 
ATOM   641   N  N     . GLU A 1 79  ? 112.640 153.823 86.329  1.00 55.66 ?  79  GLU A N     1 
ATOM   642   C  CA    . GLU A 1 79  ? 113.586 153.459 85.277  1.00 55.52 ?  79  GLU A CA    1 
ATOM   643   C  C     . GLU A 1 79  ? 114.542 152.372 85.750  1.00 52.99 ?  79  GLU A C     1 
ATOM   644   O  O     . GLU A 1 79  ? 114.860 151.442 84.998  1.00 55.14 ?  79  GLU A O     1 
ATOM   645   C  CB    . GLU A 1 79  ? 114.367 154.692 84.825  1.00 56.06 ?  79  GLU A CB    1 
ATOM   646   C  CG    . GLU A 1 79  ? 113.584 155.648 83.946  1.00 56.91 ?  79  GLU A CG    1 
ATOM   647   C  CD    . GLU A 1 79  ? 114.406 156.850 83.526  1.00 60.38 ?  79  GLU A CD    1 
ATOM   648   O  OE1   . GLU A 1 79  ? 115.438 156.658 82.850  1.00 60.58 ?  79  GLU A OE1   1 
ATOM   649   O  OE2   . GLU A 1 79  ? 114.025 157.986 83.875  1.00 61.84 -1 79  GLU A OE2   1 
ATOM   650   N  N     . VAL A 1 80  ? 115.014 152.476 86.992  1.00 45.61 ?  80  VAL A N     1 
ATOM   651   C  CA    . VAL A 1 80  ? 115.905 151.457 87.543  1.00 43.99 ?  80  VAL A CA    1 
ATOM   652   C  C     . VAL A 1 80  ? 115.199 150.106 87.605  1.00 48.77 ?  80  VAL A C     1 
ATOM   653   O  O     . VAL A 1 80  ? 115.763 149.070 87.224  1.00 49.84 ?  80  VAL A O     1 
ATOM   654   C  CB    . VAL A 1 80  ? 116.415 151.899 88.927  1.00 43.52 ?  80  VAL A CB    1 
ATOM   655   C  CG1   . VAL A 1 80  ? 117.035 150.735 89.671  1.00 45.04 ?  80  VAL A CG1   1 
ATOM   656   C  CG2   . VAL A 1 80  ? 117.415 153.031 88.779  1.00 44.18 ?  80  VAL A CG2   1 
ATOM   657   N  N     . PHE A 1 81  ? 113.951 150.097 88.077  1.00 48.14 ?  81  PHE A N     1 
ATOM   658   C  CA    . PHE A 1 81  ? 113.206 148.845 88.169  1.00 44.30 ?  81  PHE A CA    1 
ATOM   659   C  C     . PHE A 1 81  ? 112.908 148.268 86.789  1.00 47.34 ?  81  PHE A C     1 
ATOM   660   O  O     . PHE A 1 81  ? 112.910 147.046 86.609  1.00 49.22 ?  81  PHE A O     1 
ATOM   661   C  CB    . PHE A 1 81  ? 111.920 149.059 88.962  1.00 44.78 ?  81  PHE A CB    1 
ATOM   662   C  CG    . PHE A 1 81  ? 112.073 148.824 90.437  1.00 44.53 ?  81  PHE A CG    1 
ATOM   663   C  CD1   . PHE A 1 81  ? 112.660 149.782 91.244  1.00 45.67 ?  81  PHE A CD1   1 
ATOM   664   C  CD2   . PHE A 1 81  ? 111.630 147.649 91.016  1.00 46.79 ?  81  PHE A CD2   1 
ATOM   665   C  CE1   . PHE A 1 81  ? 112.803 149.571 92.602  1.00 45.99 ?  81  PHE A CE1   1 
ATOM   666   C  CE2   . PHE A 1 81  ? 111.770 147.434 92.372  1.00 45.17 ?  81  PHE A CE2   1 
ATOM   667   C  CZ    . PHE A 1 81  ? 112.358 148.395 93.165  1.00 43.40 ?  81  PHE A CZ    1 
ATOM   668   N  N     . LYS A 1 82  ? 112.642 149.129 85.802  1.00 47.06 ?  82  LYS A N     1 
ATOM   669   C  CA    . LYS A 1 82  ? 112.497 148.651 84.429  1.00 50.44 ?  82  LYS A CA    1 
ATOM   670   C  C     . LYS A 1 82  ? 113.788 148.018 83.934  1.00 50.45 ?  82  LYS A C     1 
ATOM   671   O  O     . LYS A 1 82  ? 113.763 146.975 83.273  1.00 52.83 ?  82  LYS A O     1 
ATOM   672   C  CB    . LYS A 1 82  ? 112.085 149.790 83.494  1.00 51.75 ?  82  LYS A CB    1 
ATOM   673   C  CG    . LYS A 1 82  ? 110.783 150.491 83.836  1.00 53.41 ?  82  LYS A CG    1 
ATOM   674   C  CD    . LYS A 1 82  ? 109.614 149.533 83.866  1.00 53.59 ?  82  LYS A CD    1 
ATOM   675   C  CE    . LYS A 1 82  ? 108.504 149.995 82.937  1.00 54.29 ?  82  LYS A CE    1 
ATOM   676   N  NZ    . LYS A 1 82  ? 109.010 150.255 81.560  1.00 52.75 1  82  LYS A NZ    1 
ATOM   677   N  N     . THR A 1 83  ? 114.927 148.639 84.246  1.00 43.33 ?  83  THR A N     1 
ATOM   678   C  CA    . THR A 1 83  ? 116.211 148.075 83.845  1.00 45.07 ?  83  THR A CA    1 
ATOM   679   C  C     . THR A 1 83  ? 116.422 146.701 84.468  1.00 46.81 ?  83  THR A C     1 
ATOM   680   O  O     . THR A 1 83  ? 116.931 145.785 83.811  1.00 47.75 ?  83  THR A O     1 
ATOM   681   C  CB    . THR A 1 83  ? 117.344 149.025 84.236  1.00 46.72 ?  83  THR A CB    1 
ATOM   682   O  OG1   . THR A 1 83  ? 117.084 150.324 83.694  1.00 50.88 ?  83  THR A OG1   1 
ATOM   683   C  CG2   . THR A 1 83  ? 118.671 148.523 83.696  1.00 46.24 ?  83  THR A CG2   1 
ATOM   684   N  N     . ALA A 1 84  ? 116.033 146.537 85.733  1.00 46.18 ?  84  ALA A N     1 
ATOM   685   C  CA    . ALA A 1 84  ? 116.151 145.229 86.372  1.00 41.53 ?  84  ALA A CA    1 
ATOM   686   C  C     . ALA A 1 84  ? 115.249 144.198 85.708  1.00 42.96 ?  84  ALA A C     1 
ATOM   687   O  O     . ALA A 1 84  ? 115.676 143.070 85.439  1.00 47.86 ?  84  ALA A O     1 
ATOM   688   C  CB    . ALA A 1 84  ? 115.829 145.339 87.859  1.00 43.85 ?  84  ALA A CB    1 
ATOM   689   N  N     . TYR A 1 85  ? 113.996 144.566 85.431  1.00 47.92 ?  85  TYR A N     1 
ATOM   690   C  CA    . TYR A 1 85  ? 113.044 143.621 84.865  1.00 47.31 ?  85  TYR A CA    1 
ATOM   691   C  C     . TYR A 1 85  ? 113.199 143.444 83.360  1.00 46.51 ?  85  TYR A C     1 
ATOM   692   O  O     . TYR A 1 85  ? 112.670 142.474 82.810  1.00 49.04 ?  85  TYR A O     1 
ATOM   693   C  CB    . TYR A 1 85  ? 111.614 144.058 85.187  1.00 47.59 ?  85  TYR A CB    1 
ATOM   694   C  CG    . TYR A 1 85  ? 111.170 143.710 86.590  1.00 48.42 ?  85  TYR A CG    1 
ATOM   695   C  CD1   . TYR A 1 85  ? 111.396 144.579 87.648  1.00 47.29 ?  85  TYR A CD1   1 
ATOM   696   C  CD2   . TYR A 1 85  ? 110.528 142.509 86.856  1.00 46.70 ?  85  TYR A CD2   1 
ATOM   697   C  CE1   . TYR A 1 85  ? 110.992 144.264 88.929  1.00 46.62 ?  85  TYR A CE1   1 
ATOM   698   C  CE2   . TYR A 1 85  ? 110.122 142.185 88.134  1.00 46.81 ?  85  TYR A CE2   1 
ATOM   699   C  CZ    . TYR A 1 85  ? 110.357 143.065 89.166  1.00 47.28 ?  85  TYR A CZ    1 
ATOM   700   O  OH    . TYR A 1 85  ? 109.953 142.745 90.440  1.00 49.55 ?  85  TYR A OH    1 
ATOM   701   N  N     . ALA A 1 86  ? 113.907 144.353 82.683  1.00 45.11 ?  86  ALA A N     1 
ATOM   702   C  CA    . ALA A 1 86  ? 114.113 144.202 81.247  1.00 44.63 ?  86  ALA A CA    1 
ATOM   703   C  C     . ALA A 1 86  ? 114.989 143.000 80.927  1.00 47.07 ?  86  ALA A C     1 
ATOM   704   O  O     . ALA A 1 86  ? 114.848 142.399 79.856  1.00 48.77 ?  86  ALA A O     1 
ATOM   705   C  CB    . ALA A 1 86  ? 114.730 145.472 80.661  1.00 44.19 ?  86  ALA A CB    1 
ATOM   706   N  N     . LYS A 1 87  ? 115.899 142.641 81.835  1.00 46.25 ?  87  LYS A N     1 
ATOM   707   C  CA    . LYS A 1 87  ? 116.756 141.484 81.610  1.00 45.97 ?  87  LYS A CA    1 
ATOM   708   C  C     . LYS A 1 87  ? 115.949 140.192 81.576  1.00 45.92 ?  87  LYS A C     1 
ATOM   709   O  O     . LYS A 1 87  ? 116.333 139.240 80.887  1.00 45.76 ?  87  LYS A O     1 
ATOM   710   C  CB    . LYS A 1 87  ? 117.837 141.426 82.692  1.00 42.62 ?  87  LYS A CB    1 
ATOM   711   C  CG    . LYS A 1 87  ? 118.472 140.060 82.902  1.00 44.03 ?  87  LYS A CG    1 
ATOM   712   C  CD    . LYS A 1 87  ? 119.835 139.968 82.236  1.00 45.15 ?  87  LYS A CD    1 
ATOM   713   C  CE    . LYS A 1 87  ? 120.501 138.636 82.538  1.00 45.16 ?  87  LYS A CE    1 
ATOM   714   N  NZ    . LYS A 1 87  ? 121.838 138.522 81.894  1.00 42.00 1  87  LYS A NZ    1 
ATOM   715   N  N     . LYS A 1 88  ? 114.818 140.154 82.281  1.00 48.62 ?  88  LYS A N     1 
ATOM   716   C  CA    . LYS A 1 88  ? 114.010 138.945 82.426  1.00 47.59 ?  88  LYS A CA    1 
ATOM   717   C  C     . LYS A 1 88  ? 114.862 137.793 82.949  1.00 43.20 ?  88  LYS A C     1 
ATOM   718   O  O     . LYS A 1 88  ? 114.936 136.716 82.355  1.00 46.03 ?  88  LYS A O     1 
ATOM   719   C  CB    . LYS A 1 88  ? 113.326 138.573 81.109  1.00 49.47 ?  88  LYS A CB    1 
ATOM   720   C  CG    . LYS A 1 88  ? 111.990 139.265 80.884  1.00 49.24 ?  88  LYS A CG    1 
ATOM   721   C  CD    . LYS A 1 88  ? 111.553 139.182 79.429  1.00 47.96 ?  88  LYS A CD    1 
ATOM   722   C  CE    . LYS A 1 88  ? 112.733 139.295 78.478  1.00 49.54 ?  88  LYS A CE    1 
ATOM   723   N  NZ    . LYS A 1 88  ? 112.303 139.234 77.055  1.00 47.96 1  88  LYS A NZ    1 
ATOM   724   N  N     . PHE A 1 89  ? 115.524 138.041 84.077  1.00 42.48 ?  89  PHE A N     1 
ATOM   725   C  CA    . PHE A 1 89  ? 116.404 137.044 84.665  1.00 38.98 ?  89  PHE A CA    1 
ATOM   726   C  C     . PHE A 1 89  ? 115.609 135.826 85.112  1.00 41.01 ?  89  PHE A C     1 
ATOM   727   O  O     . PHE A 1 89  ? 114.534 135.945 85.703  1.00 44.65 ?  89  PHE A O     1 
ATOM   728   C  CB    . PHE A 1 89  ? 117.165 137.642 85.850  1.00 35.95 ?  89  PHE A CB    1 
ATOM   729   C  CG    . PHE A 1 89  ? 117.910 136.628 86.670  1.00 37.82 ?  89  PHE A CG    1 
ATOM   730   C  CD1   . PHE A 1 89  ? 119.183 136.229 86.309  1.00 35.27 ?  89  PHE A CD1   1 
ATOM   731   C  CD2   . PHE A 1 89  ? 117.337 136.074 87.803  1.00 35.78 ?  89  PHE A CD2   1 
ATOM   732   C  CE1   . PHE A 1 89  ? 119.869 135.298 87.058  1.00 37.73 ?  89  PHE A CE1   1 
ATOM   733   C  CE2   . PHE A 1 89  ? 118.019 135.142 88.554  1.00 35.76 ?  89  PHE A CE2   1 
ATOM   734   C  CZ    . PHE A 1 89  ? 119.285 134.754 88.182  1.00 38.16 ?  89  PHE A CZ    1 
ATOM   735   N  N     . ARG A 1 90  ? 116.150 134.645 84.826  1.00 41.13 ?  90  ARG A N     1 
ATOM   736   C  CA    . ARG A 1 90  ? 115.557 133.387 85.249  1.00 40.95 ?  90  ARG A CA    1 
ATOM   737   C  C     . ARG A 1 90  ? 116.605 132.576 85.991  1.00 41.23 ?  90  ARG A C     1 
ATOM   738   O  O     . ARG A 1 90  ? 117.727 132.411 85.501  1.00 43.62 ?  90  ARG A O     1 
ATOM   739   C  CB    . ARG A 1 90  ? 115.015 132.593 84.056  1.00 42.51 ?  90  ARG A CB    1 
ATOM   740   C  CG    . ARG A 1 90  ? 114.015 133.354 83.207  1.00 42.59 ?  90  ARG A CG    1 
ATOM   741   C  CD    . ARG A 1 90  ? 112.613 133.252 83.782  1.00 45.13 ?  90  ARG A CD    1 
ATOM   742   N  NE    . ARG A 1 90  ? 111.690 134.169 83.126  1.00 45.28 ?  90  ARG A NE    1 
ATOM   743   C  CZ    . ARG A 1 90  ? 111.433 135.401 83.544  1.00 47.41 ?  90  ARG A CZ    1 
ATOM   744   N  NH1   . ARG A 1 90  ? 111.998 135.893 84.633  1.00 46.93 1  90  ARG A NH1   1 
ATOM   745   N  NH2   . ARG A 1 90  ? 110.586 136.157 82.851  1.00 44.82 ?  90  ARG A NH2   1 
ATOM   746   N  N     . PHE A 1 91  ? 116.243 132.084 87.165  1.00 36.44 ?  91  PHE A N     1 
ATOM   747   C  CA    . PHE A 1 91  ? 117.145 131.229 87.921  1.00 36.22 ?  91  PHE A CA    1 
ATOM   748   C  C     . PHE A 1 91  ? 117.352 129.919 87.169  1.00 42.87 ?  91  PHE A C     1 
ATOM   749   O  O     . PHE A 1 91  ? 116.373 129.277 86.772  1.00 45.07 ?  91  PHE A O     1 
ATOM   750   C  CB    . PHE A 1 91  ? 116.583 130.964 89.313  1.00 35.20 ?  91  PHE A CB    1 
ATOM   751   C  CG    . PHE A 1 91  ? 116.653 132.152 90.229  1.00 39.44 ?  91  PHE A CG    1 
ATOM   752   C  CD1   . PHE A 1 91  ? 117.804 132.424 90.948  1.00 42.42 ?  91  PHE A CD1   1 
ATOM   753   C  CD2   . PHE A 1 91  ? 115.570 132.999 90.369  1.00 39.20 ?  91  PHE A CD2   1 
ATOM   754   C  CE1   . PHE A 1 91  ? 117.871 133.513 91.791  1.00 38.91 ?  91  PHE A CE1   1 
ATOM   755   C  CE2   . PHE A 1 91  ? 115.630 134.091 91.211  1.00 39.18 ?  91  PHE A CE2   1 
ATOM   756   C  CZ    . PHE A 1 91  ? 116.782 134.348 91.923  1.00 38.29 ?  91  PHE A CZ    1 
ATOM   757   N  N     . PRO A 1 92  ? 118.599 129.491 86.947  1.00 41.57 ?  92  PRO A N     1 
ATOM   758   C  CA    . PRO A 1 92  ? 118.823 128.272 86.160  1.00 37.12 ?  92  PRO A CA    1 
ATOM   759   C  C     . PRO A 1 92  ? 118.563 126.991 86.927  1.00 38.04 ?  92  PRO A C     1 
ATOM   760   O  O     . PRO A 1 92  ? 118.429 125.933 86.299  1.00 40.67 ?  92  PRO A O     1 
ATOM   761   C  CB    . PRO A 1 92  ? 120.299 128.387 85.766  1.00 38.47 ?  92  PRO A CB    1 
ATOM   762   C  CG    . PRO A 1 92  ? 120.912 129.127 86.905  1.00 39.59 ?  92  PRO A CG    1 
ATOM   763   C  CD    . PRO A 1 92  ? 119.860 130.071 87.442  1.00 40.78 ?  92  PRO A CD    1 
ATOM   764   N  N     . SER A 1 93  ? 118.488 127.048 88.253  1.00 39.30 ?  93  SER A N     1 
ATOM   765   C  CA    . SER A 1 93  ? 118.328 125.859 89.071  1.00 42.91 ?  93  SER A CA    1 
ATOM   766   C  C     . SER A 1 93  ? 117.358 126.157 90.203  1.00 44.00 ?  93  SER A C     1 
ATOM   767   O  O     . SER A 1 93  ? 117.121 127.313 90.558  1.00 46.31 ?  93  SER A O     1 
ATOM   768   C  CB    . SER A 1 93  ? 119.674 125.382 89.633  1.00 41.29 ?  93  SER A CB    1 
ATOM   769   O  OG    . SER A 1 93  ? 120.089 126.192 90.718  1.00 40.49 ?  93  SER A OG    1 
ATOM   770   N  N     . PHE A 1 94  ? 116.790 125.089 90.766  1.00 41.93 ?  94  PHE A N     1 
ATOM   771   C  CA    . PHE A 1 94  ? 115.872 125.253 91.887  1.00 42.32 ?  94  PHE A CA    1 
ATOM   772   C  C     . PHE A 1 94  ? 116.589 125.790 93.117  1.00 43.88 ?  94  PHE A C     1 
ATOM   773   O  O     . PHE A 1 94  ? 116.020 126.582 93.875  1.00 46.67 ?  94  PHE A O     1 
ATOM   774   C  CB    . PHE A 1 94  ? 115.178 123.930 92.207  1.00 41.55 ?  94  PHE A CB    1 
ATOM   775   C  CG    . PHE A 1 94  ? 114.555 123.895 93.572  1.00 43.53 ?  94  PHE A CG    1 
ATOM   776   C  CD1   . PHE A 1 94  ? 113.430 124.650 93.852  1.00 44.19 ?  94  PHE A CD1   1 
ATOM   777   C  CD2   . PHE A 1 94  ? 115.094 123.111 94.577  1.00 44.94 ?  94  PHE A CD2   1 
ATOM   778   C  CE1   . PHE A 1 94  ? 112.858 124.627 95.106  1.00 43.92 ?  94  PHE A CE1   1 
ATOM   779   C  CE2   . PHE A 1 94  ? 114.524 123.083 95.833  1.00 46.60 ?  94  PHE A CE2   1 
ATOM   780   C  CZ    . PHE A 1 94  ? 113.405 123.842 96.097  1.00 44.64 ?  94  PHE A CZ    1 
ATOM   781   N  N     . MET A 1 95  ? 117.833 125.360 93.343  1.00 41.38 ?  95  MET A N     1 
ATOM   782   C  CA    . MET A 1 95  ? 118.557 125.788 94.536  1.00 36.23 ?  95  MET A CA    1 
ATOM   783   C  C     . MET A 1 95  ? 118.807 127.288 94.536  1.00 39.46 ?  95  MET A C     1 
ATOM   784   O  O     . MET A 1 95  ? 118.736 127.929 95.587  1.00 45.02 ?  95  MET A O     1 
ATOM   785   C  CB    . MET A 1 95  ? 119.877 125.029 94.659  1.00 42.26 ?  95  MET A CB    1 
ATOM   786   C  CG    . MET A 1 95  ? 120.323 124.670 96.085  1.00 44.32 ?  95  MET A CG    1 
ATOM   787   S  SD    . MET A 1 95  ? 119.101 124.350 97.384  1.00 53.46 ?  95  MET A SD    1 
ATOM   788   C  CE    . MET A 1 95  ? 117.966 123.208 96.598  1.00 45.67 ?  95  MET A CE    1 
ATOM   789   N  N     . SER A 1 96  ? 119.113 127.867 93.374  1.00 35.10 ?  96  SER A N     1 
ATOM   790   C  CA    . SER A 1 96  ? 119.367 129.303 93.310  1.00 33.05 ?  96  SER A CA    1 
ATOM   791   C  C     . SER A 1 96  ? 118.161 130.096 93.797  1.00 34.07 ?  96  SER A C     1 
ATOM   792   O  O     . SER A 1 96  ? 118.267 130.923 94.715  1.00 34.98 ?  96  SER A O     1 
ATOM   793   C  CB    . SER A 1 96  ? 119.723 129.696 91.878  1.00 35.24 ?  96  SER A CB    1 
ATOM   794   O  OG    . SER A 1 96  ? 120.518 128.700 91.264  1.00 38.59 ?  96  SER A OG    1 
ATOM   795   N  N     . ALA A 1 97  ? 116.995 129.829 93.206  1.00 40.03 ?  97  ALA A N     1 
ATOM   796   C  CA    . ALA A 1 97  ? 115.783 130.546 93.581  1.00 37.07 ?  97  ALA A CA    1 
ATOM   797   C  C     . ALA A 1 97  ? 115.370 130.227 95.009  1.00 37.56 ?  97  ALA A C     1 
ATOM   798   O  O     . ALA A 1 97  ? 114.913 131.112 95.739  1.00 45.57 ?  97  ALA A O     1 
ATOM   799   C  CB    . ALA A 1 97  ? 114.658 130.206 92.609  1.00 36.46 ?  97  ALA A CB    1 
ATOM   800   N  N     . PHE A 1 98  ? 115.507 128.966 95.421  1.00 33.25 ?  98  PHE A N     1 
ATOM   801   C  CA    . PHE A 1 98  ? 115.128 128.588 96.775  1.00 35.49 ?  98  PHE A CA    1 
ATOM   802   C  C     . PHE A 1 98  ? 115.978 129.322 97.802  1.00 37.06 ?  98  PHE A C     1 
ATOM   803   O  O     . PHE A 1 98  ? 115.456 129.877 98.775  1.00 45.07 ?  98  PHE A O     1 
ATOM   804   C  CB    . PHE A 1 98  ? 115.255 127.075 96.952  1.00 40.98 ?  98  PHE A CB    1 
ATOM   805   C  CG    . PHE A 1 98  ? 115.112 126.620 98.373  1.00 42.29 ?  98  PHE A CG    1 
ATOM   806   C  CD1   . PHE A 1 98  ? 113.860 126.503 98.950  1.00 41.66 ?  98  PHE A CD1   1 
ATOM   807   C  CD2   . PHE A 1 98  ? 116.226 126.317 99.135  1.00 42.38 ?  98  PHE A CD2   1 
ATOM   808   C  CE1   . PHE A 1 98  ? 113.723 126.091 100.257 1.00 41.14 ?  98  PHE A CE1   1 
ATOM   809   C  CE2   . PHE A 1 98  ? 116.095 125.905 100.444 1.00 42.94 ?  98  PHE A CE2   1 
ATOM   810   C  CZ    . PHE A 1 98  ? 114.841 125.790 101.005 1.00 42.27 ?  98  PHE A CZ    1 
ATOM   811   N  N     . LYS A 1 99  ? 117.294 129.346 97.591  1.00 39.01 ?  99  LYS A N     1 
ATOM   812   C  CA    . LYS A 1 99  ? 118.180 130.041 98.512  1.00 38.77 ?  99  LYS A CA    1 
ATOM   813   C  C     . LYS A 1 99  ? 117.886 131.532 98.533  1.00 39.03 ?  99  LYS A C     1 
ATOM   814   O  O     . LYS A 1 99  ? 117.852 132.144 99.608  1.00 41.24 ?  99  LYS A O     1 
ATOM   815   C  CB    . LYS A 1 99  ? 119.639 129.783 98.135  1.00 38.86 ?  99  LYS A CB    1 
ATOM   816   C  CG    . LYS A 1 99  ? 120.120 128.382 98.470  1.00 41.35 ?  99  LYS A CG    1 
ATOM   817   C  CD    . LYS A 1 99  ? 119.752 127.994 99.890  1.00 43.43 ?  99  LYS A CD    1 
ATOM   818   C  CE    . LYS A 1 99  ? 120.937 127.392 100.619 1.00 41.25 ?  99  LYS A CE    1 
ATOM   819   N  NZ    . LYS A 1 99  ? 120.842 127.606 102.088 1.00 42.13 1  99  LYS A NZ    1 
ATOM   820   N  N     . PHE A 1 100 ? 117.646 132.137 97.365  1.00 34.65 ?  100 PHE A N     1 
ATOM   821   C  CA    . PHE A 1 100 ? 117.334 133.562 97.362  1.00 34.54 ?  100 PHE A CA    1 
ATOM   822   C  C     . PHE A 1 100 ? 116.051 133.846 98.130  1.00 36.68 ?  100 PHE A C     1 
ATOM   823   O  O     . PHE A 1 100 ? 116.033 134.679 99.041  1.00 42.14 ?  100 PHE A O     1 
ATOM   824   C  CB    . PHE A 1 100 ? 117.218 134.102 95.940  1.00 36.23 ?  100 PHE A CB    1 
ATOM   825   C  CG    . PHE A 1 100 ? 116.765 135.531 95.900  1.00 36.68 ?  100 PHE A CG    1 
ATOM   826   C  CD1   . PHE A 1 100 ? 117.626 136.548 96.274  1.00 37.98 ?  100 PHE A CD1   1 
ATOM   827   C  CD2   . PHE A 1 100 ? 115.471 135.856 95.535  1.00 36.45 ?  100 PHE A CD2   1 
ATOM   828   C  CE1   . PHE A 1 100 ? 117.213 137.862 96.263  1.00 38.96 ?  100 PHE A CE1   1 
ATOM   829   C  CE2   . PHE A 1 100 ? 115.053 137.169 95.522  1.00 39.45 ?  100 PHE A CE2   1 
ATOM   830   C  CZ    . PHE A 1 100 ? 115.925 138.173 95.887  1.00 39.03 ?  100 PHE A CZ    1 
ATOM   831   N  N     . TYR A 1 101 ? 114.968 133.148 97.793  1.00 41.22 ?  101 TYR A N     1 
ATOM   832   C  CA    . TYR A 1 101 ? 113.677 133.442 98.396  1.00 38.44 ?  101 TYR A CA    1 
ATOM   833   C  C     . TYR A 1 101 ? 113.550 132.919 99.818  1.00 40.02 ?  101 TYR A C     1 
ATOM   834   O  O     . TYR A 1 101 ? 112.548 133.212 100.478 1.00 46.64 ?  101 TYR A O     1 
ATOM   835   C  CB    . TYR A 1 101 ? 112.553 132.889 97.517  1.00 38.76 ?  101 TYR A CB    1 
ATOM   836   C  CG    . TYR A 1 101 ? 112.360 133.690 96.250  1.00 36.64 ?  101 TYR A CG    1 
ATOM   837   C  CD1   . TYR A 1 101 ? 111.802 134.959 96.290  1.00 39.62 ?  101 TYR A CD1   1 
ATOM   838   C  CD2   . TYR A 1 101 ? 112.761 133.190 95.021  1.00 35.22 ?  101 TYR A CD2   1 
ATOM   839   C  CE1   . TYR A 1 101 ? 111.634 135.701 95.138  1.00 39.29 ?  101 TYR A CE1   1 
ATOM   840   C  CE2   . TYR A 1 101 ? 112.598 133.924 93.866  1.00 39.50 ?  101 TYR A CE2   1 
ATOM   841   C  CZ    . TYR A 1 101 ? 112.035 135.179 93.929  1.00 41.13 ?  101 TYR A CZ    1 
ATOM   842   O  OH    . TYR A 1 101 ? 111.871 135.913 92.778  1.00 39.45 ?  101 TYR A OH    1 
ATOM   843   N  N     . ASN A 1 102 ? 114.529 132.158 100.306 1.00 40.55 ?  102 ASN A N     1 
ATOM   844   C  CA    . ASN A 1 102 ? 114.539 131.743 101.700 1.00 41.46 ?  102 ASN A CA    1 
ATOM   845   C  C     . ASN A 1 102 ? 115.494 132.550 102.569 1.00 43.05 ?  102 ASN A C     1 
ATOM   846   O  O     . ASN A 1 102 ? 115.276 132.629 103.783 1.00 45.65 ?  102 ASN A O     1 
ATOM   847   C  CB    . ASN A 1 102 ? 114.905 130.258 101.807 1.00 42.60 ?  102 ASN A CB    1 
ATOM   848   C  CG    . ASN A 1 102 ? 113.686 129.358 101.829 1.00 44.82 ?  102 ASN A CG    1 
ATOM   849   O  OD1   . ASN A 1 102 ? 112.770 129.514 101.023 1.00 46.40 ?  102 ASN A OD1   1 
ATOM   850   N  ND2   . ASN A 1 102 ? 113.668 128.411 102.759 1.00 44.73 ?  102 ASN A ND2   1 
ATOM   851   N  N     . ASP A 1 103 ? 116.538 133.147 101.997 1.00 43.44 ?  103 ASP A N     1 
ATOM   852   C  CA    . ASP A 1 103 ? 117.544 133.850 102.783 1.00 41.09 ?  103 ASP A CA    1 
ATOM   853   C  C     . ASP A 1 103 ? 117.579 135.351 102.549 1.00 41.31 ?  103 ASP A C     1 
ATOM   854   O  O     . ASP A 1 103 ? 117.774 136.108 103.500 1.00 47.96 ?  103 ASP A O     1 
ATOM   855   C  CB    . ASP A 1 103 ? 118.934 133.272 102.491 1.00 44.45 ?  103 ASP A CB    1 
ATOM   856   C  CG    . ASP A 1 103 ? 119.084 131.841 102.965 1.00 46.42 ?  103 ASP A CG    1 
ATOM   857   O  OD1   . ASP A 1 103 ? 118.099 131.276 103.484 1.00 47.25 ?  103 ASP A OD1   1 
ATOM   858   O  OD2   . ASP A 1 103 ? 120.189 131.278 102.816 1.00 48.74 -1 103 ASP A OD2   1 
ATOM   859   N  N     . TYR A 1 104 ? 117.397 135.810 101.309 1.00 31.26 ?  104 TYR A N     1 
ATOM   860   C  CA    . TYR A 1 104 ? 117.619 137.207 100.971 1.00 37.51 ?  104 TYR A CA    1 
ATOM   861   C  C     . TYR A 1 104 ? 116.368 137.951 100.530 1.00 39.68 ?  104 TYR A C     1 
ATOM   862   O  O     . TYR A 1 104 ? 116.339 139.181 100.636 1.00 44.70 ?  104 TYR A O     1 
ATOM   863   C  CB    . TYR A 1 104 ? 118.675 137.321 99.862  1.00 36.23 ?  104 TYR A CB    1 
ATOM   864   C  CG    . TYR A 1 104 ? 119.977 136.637 100.205 1.00 39.20 ?  104 TYR A CG    1 
ATOM   865   C  CD1   . TYR A 1 104 ? 120.949 137.290 100.947 1.00 34.99 ?  104 TYR A CD1   1 
ATOM   866   C  CD2   . TYR A 1 104 ? 120.228 135.335 99.796  1.00 34.27 ?  104 TYR A CD2   1 
ATOM   867   C  CE1   . TYR A 1 104 ? 122.137 136.667 101.269 1.00 36.30 ?  104 TYR A CE1   1 
ATOM   868   C  CE2   . TYR A 1 104 ? 121.412 134.703 100.114 1.00 34.79 ?  104 TYR A CE2   1 
ATOM   869   C  CZ    . TYR A 1 104 ? 122.364 135.374 100.851 1.00 39.47 ?  104 TYR A CZ    1 
ATOM   870   O  OH    . TYR A 1 104 ? 123.547 134.752 101.171 1.00 37.58 ?  104 TYR A OH    1 
ATOM   871   N  N     . ALA A 1 105 ? 115.348 137.256 100.039 1.00 39.31 ?  105 ALA A N     1 
ATOM   872   C  CA    . ALA A 1 105 ? 114.133 137.934 99.611  1.00 40.02 ?  105 ALA A CA    1 
ATOM   873   C  C     . ALA A 1 105 ? 113.394 138.511 100.810 1.00 43.24 ?  105 ALA A C     1 
ATOM   874   O  O     . ALA A 1 105 ? 113.253 137.857 101.847 1.00 41.64 ?  105 ALA A O     1 
ATOM   875   C  CB    . ALA A 1 105 ? 113.224 136.976 98.847  1.00 37.86 ?  105 ALA A CB    1 
ATOM   876   N  N     . LEU A 1 106 ? 112.929 139.748 100.666 1.00 47.41 ?  106 LEU A N     1 
ATOM   877   C  CA    . LEU A 1 106 ? 112.179 140.391 101.734 1.00 45.87 ?  106 LEU A CA    1 
ATOM   878   C  C     . LEU A 1 106 ? 110.827 139.715 101.916 1.00 47.88 ?  106 LEU A C     1 
ATOM   879   O  O     . LEU A 1 106 ? 110.121 139.425 100.947 1.00 46.17 ?  106 LEU A O     1 
ATOM   880   C  CB    . LEU A 1 106 ? 111.989 141.876 101.434 1.00 46.17 ?  106 LEU A CB    1 
ATOM   881   C  CG    . LEU A 1 106 ? 111.342 142.721 102.532 1.00 44.92 ?  106 LEU A CG    1 
ATOM   882   C  CD1   . LEU A 1 106 ? 112.262 142.834 103.734 1.00 43.99 ?  106 LEU A CD1   1 
ATOM   883   C  CD2   . LEU A 1 106 ? 110.993 144.095 101.999 1.00 45.17 ?  106 LEU A CD2   1 
ATOM   884   N  N     . LYS A 1 107 ? 110.469 139.471 103.171 1.00 54.76 ?  107 LYS A N     1 
ATOM   885   C  CA    . LYS A 1 107 ? 109.204 138.853 103.525 1.00 53.91 ?  107 LYS A CA    1 
ATOM   886   C  C     . LYS A 1 107 ? 108.445 139.759 104.484 1.00 54.18 ?  107 LYS A C     1 
ATOM   887   O  O     . LYS A 1 107 ? 109.020 140.645 105.121 1.00 54.39 ?  107 LYS A O     1 
ATOM   888   C  CB    . LYS A 1 107 ? 109.416 137.472 104.160 1.00 51.79 ?  107 LYS A CB    1 
ATOM   889   C  CG    . LYS A 1 107 ? 109.854 136.403 103.178 1.00 50.81 ?  107 LYS A CG    1 
ATOM   890   C  CD    . LYS A 1 107 ? 110.196 135.106 103.889 1.00 55.44 ?  107 LYS A CD    1 
ATOM   891   C  CE    . LYS A 1 107 ? 110.592 134.025 102.900 1.00 54.96 ?  107 LYS A CE    1 
ATOM   892   N  NZ    . LYS A 1 107 ? 111.247 132.866 103.569 1.00 51.84 1  107 LYS A NZ    1 
ATOM   893   N  N     . THR A 1 108 ? 107.137 139.531 104.571 1.00 60.48 ?  108 THR A N     1 
ATOM   894   C  CA    . THR A 1 108 ? 106.302 140.305 105.471 1.00 61.10 ?  108 THR A CA    1 
ATOM   895   C  C     . THR A 1 108 ? 106.733 140.076 106.921 1.00 62.03 ?  108 THR A C     1 
ATOM   896   O  O     . THR A 1 108 ? 107.505 139.168 107.236 1.00 60.42 ?  108 THR A O     1 
ATOM   897   C  CB    . THR A 1 108 ? 104.831 139.939 105.284 1.00 60.24 ?  108 THR A CB    1 
ATOM   898   O  OG1   . THR A 1 108 ? 104.702 138.519 105.153 1.00 62.28 ?  108 THR A OG1   1 
ATOM   899   C  CG2   . THR A 1 108 ? 104.273 140.609 104.037 1.00 59.01 ?  108 THR A CG2   1 
ATOM   900   N  N     . ASN A 1 109 ? 106.214 140.924 107.813 1.00 63.53 ?  109 ASN A N     1 
ATOM   901   C  CA    . ASN A 1 109 ? 106.657 140.906 109.203 1.00 62.62 ?  109 ASN A CA    1 
ATOM   902   C  C     . ASN A 1 109 ? 106.373 139.571 109.878 1.00 64.06 ?  109 ASN A C     1 
ATOM   903   O  O     . ASN A 1 109 ? 107.072 139.196 110.826 1.00 65.05 ?  109 ASN A O     1 
ATOM   904   C  CB    . ASN A 1 109 ? 105.993 142.044 109.977 1.00 62.62 ?  109 ASN A CB    1 
ATOM   905   C  CG    . ASN A 1 109 ? 106.703 143.366 109.784 1.00 62.85 ?  109 ASN A CG    1 
ATOM   906   O  OD1   . ASN A 1 109 ? 107.923 143.412 109.634 1.00 64.74 ?  109 ASN A OD1   1 
ATOM   907   N  ND2   . ASN A 1 109 ? 105.941 144.453 109.783 1.00 63.04 ?  109 ASN A ND2   1 
ATOM   908   N  N     . ASP A 1 110 ? 105.363 138.841 109.410 1.00 68.70 ?  110 ASP A N     1 
ATOM   909   C  CA    . ASP A 1 110 ? 105.031 137.531 109.948 1.00 67.94 ?  110 ASP A CA    1 
ATOM   910   C  C     . ASP A 1 110 ? 105.698 136.396 109.181 1.00 68.31 ?  110 ASP A C     1 
ATOM   911   O  O     . ASP A 1 110 ? 105.372 135.229 109.417 1.00 69.86 ?  110 ASP A O     1 
ATOM   912   C  CB    . ASP A 1 110 ? 103.514 137.334 109.962 1.00 67.40 ?  110 ASP A CB    1 
ATOM   913   C  CG    . ASP A 1 110 ? 102.848 137.861 108.707 1.00 68.90 ?  110 ASP A CG    1 
ATOM   914   O  OD1   . ASP A 1 110 ? 103.439 138.735 108.042 1.00 69.20 ?  110 ASP A OD1   1 
ATOM   915   O  OD2   . ASP A 1 110 ? 101.733 137.402 108.387 1.00 70.98 -1 110 ASP A OD2   1 
ATOM   916   N  N     . LYS A 1 111 ? 106.624 136.716 108.272 1.00 66.46 ?  111 LYS A N     1 
ATOM   917   C  CA    . LYS A 1 111 ? 107.320 135.718 107.455 1.00 65.58 ?  111 LYS A CA    1 
ATOM   918   C  C     . LYS A 1 111 ? 106.331 134.857 106.674 1.00 65.91 ?  111 LYS A C     1 
ATOM   919   O  O     . LYS A 1 111 ? 106.511 133.648 106.527 1.00 67.92 ?  111 LYS A O     1 
ATOM   920   C  CB    . LYS A 1 111 ? 108.243 134.841 108.306 1.00 65.10 ?  111 LYS A CB    1 
ATOM   921   C  CG    . LYS A 1 111 ? 109.390 135.574 108.995 1.00 65.13 ?  111 LYS A CG    1 
ATOM   922   C  CD    . LYS A 1 111 ? 109.904 136.747 108.176 1.00 66.65 ?  111 LYS A CD    1 
ATOM   923   C  CE    . LYS A 1 111 ? 109.878 138.034 108.985 1.00 66.83 ?  111 LYS A CE    1 
ATOM   924   N  NZ    . LYS A 1 111 ? 110.322 139.206 108.180 1.00 64.70 1  111 LYS A NZ    1 
ATOM   925   N  N     . LYS A 1 112 ? 105.274 135.488 106.163 1.00 64.63 ?  112 LYS A N     1 
ATOM   926   C  CA    . LYS A 1 112 ? 104.186 134.776 105.504 1.00 66.88 ?  112 LYS A CA    1 
ATOM   927   C  C     . LYS A 1 112 ? 104.261 134.859 103.985 1.00 66.69 ?  112 LYS A C     1 
ATOM   928   O  O     . LYS A 1 112 ? 104.246 133.828 103.307 1.00 68.00 ?  112 LYS A O     1 
ATOM   929   C  CB    . LYS A 1 112 ? 102.838 135.320 105.990 1.00 66.48 ?  112 LYS A CB    1 
ATOM   930   C  CG    . LYS A 1 112 ? 101.653 134.429 105.659 1.00 67.80 ?  112 LYS A CG    1 
ATOM   931   C  CD    . LYS A 1 112 ? 101.694 133.131 106.452 1.00 68.20 ?  112 LYS A CD    1 
ATOM   932   C  CE    . LYS A 1 112 ? 101.859 133.390 107.943 1.00 68.46 ?  112 LYS A CE    1 
ATOM   933   N  NZ    . LYS A 1 112 ? 100.825 134.323 108.469 1.00 66.80 1  112 LYS A NZ    1 
ATOM   934   N  N     . LYS A 1 113 ? 104.339 136.065 103.438 1.00 59.74 ?  113 LYS A N     1 
ATOM   935   C  CA    . LYS A 1 113 ? 104.366 136.287 102.002 1.00 57.63 ?  113 LYS A CA    1 
ATOM   936   C  C     . LYS A 1 113 ? 105.720 136.862 101.591 1.00 57.10 ?  113 LYS A C     1 
ATOM   937   O  O     . LYS A 1 113 ? 106.593 137.121 102.422 1.00 58.08 ?  113 LYS A O     1 
ATOM   938   C  CB    . LYS A 1 113 ? 103.219 137.209 101.584 1.00 58.63 ?  113 LYS A CB    1 
ATOM   939   C  CG    . LYS A 1 113 ? 101.840 136.589 101.730 1.00 58.57 ?  113 LYS A CG    1 
ATOM   940   C  CD    . LYS A 1 113 ? 101.575 135.566 100.639 1.00 61.20 ?  113 LYS A CD    1 
ATOM   941   C  CE    . LYS A 1 113 ? 100.176 134.987 100.748 1.00 59.99 ?  113 LYS A CE    1 
ATOM   942   N  NZ    . LYS A 1 113 ? 99.934  133.933 99.725  1.00 58.80 1  113 LYS A NZ    1 
ATOM   943   N  N     . ILE A 1 114 ? 105.883 137.065 100.288 1.00 53.70 ?  114 ILE A N     1 
ATOM   944   C  CA    . ILE A 1 114 ? 107.138 137.525 99.703  1.00 52.40 ?  114 ILE A CA    1 
ATOM   945   C  C     . ILE A 1 114 ? 106.910 138.914 99.124  1.00 50.13 ?  114 ILE A C     1 
ATOM   946   O  O     . ILE A 1 114 ? 106.004 139.113 98.305  1.00 52.75 ?  114 ILE A O     1 
ATOM   947   C  CB    . ILE A 1 114 ? 107.650 136.554 98.628  1.00 52.98 ?  114 ILE A CB    1 
ATOM   948   C  CG1   . ILE A 1 114 ? 108.222 135.294 99.278  1.00 51.59 ?  114 ILE A CG1   1 
ATOM   949   C  CG2   . ILE A 1 114 ? 108.697 137.220 97.753  1.00 52.71 ?  114 ILE A CG2   1 
ATOM   950   C  CD1   . ILE A 1 114 ? 108.321 134.120 98.336  1.00 51.35 ?  114 ILE A CD1   1 
ATOM   951   N  N     . LEU A 1 115 ? 107.730 139.873 99.548  1.00 49.22 ?  115 LEU A N     1 
ATOM   952   C  CA    . LEU A 1 115 ? 107.632 141.250 99.080  1.00 51.09 ?  115 LEU A CA    1 
ATOM   953   C  C     . LEU A 1 115 ? 108.585 141.561 97.936  1.00 51.90 ?  115 LEU A C     1 
ATOM   954   O  O     . LEU A 1 115 ? 108.215 142.291 97.013  1.00 52.05 ?  115 LEU A O     1 
ATOM   955   C  CB    . LEU A 1 115 ? 107.897 142.222 100.234 1.00 50.85 ?  115 LEU A CB    1 
ATOM   956   C  CG    . LEU A 1 115 ? 106.860 142.221 101.355 1.00 49.79 ?  115 LEU A CG    1 
ATOM   957   C  CD1   . LEU A 1 115 ? 107.488 142.664 102.663 1.00 50.56 ?  115 LEU A CD1   1 
ATOM   958   C  CD2   . LEU A 1 115 ? 105.690 143.111 100.984 1.00 50.74 ?  115 LEU A CD2   1 
ATOM   959   N  N     . GLU A 1 116 ? 109.797 141.021 97.971  1.00 49.12 ?  116 GLU A N     1 
ATOM   960   C  CA    . GLU A 1 116 ? 110.828 141.326 96.989  1.00 45.80 ?  116 GLU A CA    1 
ATOM   961   C  C     . GLU A 1 116 ? 111.052 140.134 96.072  1.00 46.41 ?  116 GLU A C     1 
ATOM   962   O  O     . GLU A 1 116 ? 111.155 138.996 96.539  1.00 50.13 ?  116 GLU A O     1 
ATOM   963   C  CB    . GLU A 1 116 ? 112.144 141.696 97.673  1.00 44.75 ?  116 GLU A CB    1 
ATOM   964   C  CG    . GLU A 1 116 ? 112.389 143.181 97.807  1.00 44.63 ?  116 GLU A CG    1 
ATOM   965   C  CD    . GLU A 1 116 ? 113.632 143.486 98.613  1.00 47.03 ?  116 GLU A CD    1 
ATOM   966   O  OE1   . GLU A 1 116 ? 114.167 142.557 99.250  1.00 46.08 ?  116 GLU A OE1   1 
ATOM   967   O  OE2   . GLU A 1 116 ? 114.077 144.653 98.607  1.00 48.24 -1 116 GLU A OE2   1 
ATOM   968   N  N     . ARG A 1 117 ? 111.124 140.399 94.773  1.00 42.37 ?  117 ARG A N     1 
ATOM   969   C  CA    . ARG A 1 117 ? 111.645 139.434 93.821  1.00 42.21 ?  117 ARG A CA    1 
ATOM   970   C  C     . ARG A 1 117 ? 113.157 139.631 93.723  1.00 43.77 ?  117 ARG A C     1 
ATOM   971   O  O     . ARG A 1 117 ? 113.747 140.432 94.452  1.00 47.51 ?  117 ARG A O     1 
ATOM   972   C  CB    . ARG A 1 117 ? 110.951 139.585 92.468  1.00 42.43 ?  117 ARG A CB    1 
ATOM   973   C  CG    . ARG A 1 117 ? 109.434 139.540 92.532  1.00 44.77 ?  117 ARG A CG    1 
ATOM   974   C  CD    . ARG A 1 117 ? 108.945 138.323 93.303  1.00 49.50 ?  117 ARG A CD    1 
ATOM   975   N  NE    . ARG A 1 117 ? 109.076 137.091 92.535  1.00 47.61 ?  117 ARG A NE    1 
ATOM   976   C  CZ    . ARG A 1 117 ? 108.259 136.723 91.557  1.00 47.19 ?  117 ARG A CZ    1 
ATOM   977   N  NH1   . ARG A 1 117 ? 107.227 137.470 91.201  1.00 48.28 1  117 ARG A NH1   1 
ATOM   978   N  NH2   . ARG A 1 117 ? 108.480 135.575 90.924  1.00 47.65 ?  117 ARG A NH2   1 
ATOM   979   N  N     . TYR A 1 118 ? 113.809 138.890 92.826  1.00 42.19 ?  118 TYR A N     1 
ATOM   980   C  CA    . TYR A 1 118 ? 115.234 139.104 92.605  1.00 36.17 ?  118 TYR A CA    1 
ATOM   981   C  C     . TYR A 1 118 ? 115.490 140.485 92.015  1.00 37.76 ?  118 TYR A C     1 
ATOM   982   O  O     . TYR A 1 118 ? 116.424 141.186 92.426  1.00 40.66 ?  118 TYR A O     1 
ATOM   983   C  CB    . TYR A 1 118 ? 115.787 138.011 91.691  1.00 36.88 ?  118 TYR A CB    1 
ATOM   984   C  CG    . TYR A 1 118 ? 117.291 137.903 91.686  1.00 36.73 ?  118 TYR A CG    1 
ATOM   985   C  CD1   . TYR A 1 118 ? 117.998 137.739 92.869  1.00 36.21 ?  118 TYR A CD1   1 
ATOM   986   C  CD2   . TYR A 1 118 ? 118.006 137.958 90.500  1.00 36.96 ?  118 TYR A CD2   1 
ATOM   987   C  CE1   . TYR A 1 118 ? 119.371 137.637 92.868  1.00 35.71 ?  118 TYR A CE1   1 
ATOM   988   C  CE2   . TYR A 1 118 ? 119.378 137.851 90.488  1.00 31.19 ?  118 TYR A CE2   1 
ATOM   989   C  CZ    . TYR A 1 118 ? 120.056 137.692 91.674  1.00 35.72 ?  118 TYR A CZ    1 
ATOM   990   O  OH    . TYR A 1 118 ? 121.427 137.591 91.666  1.00 45.66 ?  118 TYR A OH    1 
ATOM   991   N  N     . GLU A 1 119 ? 114.653 140.899 91.062  1.00 41.38 ?  119 GLU A N     1 
ATOM   992   C  CA    . GLU A 1 119 ? 114.810 142.210 90.446  1.00 38.57 ?  119 GLU A CA    1 
ATOM   993   C  C     . GLU A 1 119 ? 114.575 143.330 91.450  1.00 40.41 ?  119 GLU A C     1 
ATOM   994   O  O     . GLU A 1 119 ? 115.270 144.350 91.416  1.00 43.54 ?  119 GLU A O     1 
ATOM   995   C  CB    . GLU A 1 119 ? 113.863 142.345 89.256  1.00 40.57 ?  119 GLU A CB    1 
ATOM   996   C  CG    . GLU A 1 119 ? 114.330 141.616 88.012  1.00 41.16 ?  119 GLU A CG    1 
ATOM   997   C  CD    . GLU A 1 119 ? 113.808 140.196 87.932  1.00 43.69 ?  119 GLU A CD    1 
ATOM   998   O  OE1   . GLU A 1 119 ? 113.418 139.641 88.981  1.00 43.92 ?  119 GLU A OE1   1 
ATOM   999   O  OE2   . GLU A 1 119 ? 113.794 139.632 86.819  1.00 44.72 -1 119 GLU A OE2   1 
ATOM   1000  N  N     . ASP A 1 120 ? 113.604 143.165 92.349  1.00 42.16 ?  120 ASP A N     1 
ATOM   1001  C  CA    . ASP A 1 120 ? 113.343 144.194 93.350  1.00 38.20 ?  120 ASP A CA    1 
ATOM   1002  C  C     . ASP A 1 120 ? 114.527 144.356 94.293  1.00 38.64 ?  120 ASP A C     1 
ATOM   1003  O  O     . ASP A 1 120 ? 114.961 145.480 94.576  1.00 45.44 ?  120 ASP A O     1 
ATOM   1004  C  CB    . ASP A 1 120 ? 112.076 143.855 94.137  1.00 42.51 ?  120 ASP A CB    1 
ATOM   1005  C  CG    . ASP A 1 120 ? 110.895 143.564 93.239  1.00 47.73 ?  120 ASP A CG    1 
ATOM   1006  O  OD1   . ASP A 1 120 ? 110.774 144.222 92.185  1.00 46.98 ?  120 ASP A OD1   1 
ATOM   1007  O  OD2   . ASP A 1 120 ? 110.087 142.679 93.585  1.00 51.12 -1 120 ASP A OD2   1 
ATOM   1008  N  N     . ARG A 1 121 ? 115.064 143.240 94.792  1.00 33.43 ?  121 ARG A N     1 
ATOM   1009  C  CA    . ARG A 1 121 ? 116.221 143.302 95.676  1.00 32.95 ?  121 ARG A CA    1 
ATOM   1010  C  C     . ARG A 1 121 ? 117.421 143.916 94.968  1.00 34.25 ?  121 ARG A C     1 
ATOM   1011  O  O     . ARG A 1 121 ? 118.128 144.753 95.541  1.00 41.31 ?  121 ARG A O     1 
ATOM   1012  C  CB    . ARG A 1 121 ? 116.562 141.904 96.191  1.00 34.34 ?  121 ARG A CB    1 
ATOM   1013  C  CG    . ARG A 1 121 ? 117.736 141.860 97.153  1.00 32.95 ?  121 ARG A CG    1 
ATOM   1014  C  CD    . ARG A 1 121 ? 117.271 141.991 98.591  1.00 33.48 ?  121 ARG A CD    1 
ATOM   1015  N  NE    . ARG A 1 121 ? 118.118 142.892 99.361  1.00 38.02 ?  121 ARG A NE    1 
ATOM   1016  C  CZ    . ARG A 1 121 ? 117.802 144.143 99.666  1.00 37.23 ?  121 ARG A CZ    1 
ATOM   1017  N  NH1   . ARG A 1 121 ? 116.662 144.683 99.270  1.00 36.19 1  121 ARG A NH1   1 
ATOM   1018  N  NH2   . ARG A 1 121 ? 118.652 144.870 100.384 1.00 34.72 ?  121 ARG A NH2   1 
ATOM   1019  N  N     . ILE A 1 122 ? 117.659 143.521 93.716  1.00 33.17 ?  122 ILE A N     1 
ATOM   1020  C  CA    . ILE A 1 122 ? 118.795 144.060 92.976  1.00 29.12 ?  122 ILE A CA    1 
ATOM   1021  C  C     . ILE A 1 122 ? 118.623 145.554 92.738  1.00 30.95 ?  122 ILE A C     1 
ATOM   1022  O  O     . ILE A 1 122 ? 119.576 146.327 92.875  1.00 36.66 ?  122 ILE A O     1 
ATOM   1023  C  CB    . ILE A 1 122 ? 118.990 143.283 91.662  1.00 32.31 ?  122 ILE A CB    1 
ATOM   1024  C  CG1   . ILE A 1 122 ? 119.777 142.002 91.933  1.00 27.19 ?  122 ILE A CG1   1 
ATOM   1025  C  CG2   . ILE A 1 122 ? 119.703 144.136 90.624  1.00 33.57 ?  122 ILE A CG2   1 
ATOM   1026  C  CD1   . ILE A 1 122 ? 120.099 141.226 90.699  1.00 33.73 ?  122 ILE A CD1   1 
ATOM   1027  N  N     . SER A 1 123 ? 117.411 145.990 92.386  1.00 34.94 ?  123 SER A N     1 
ATOM   1028  C  CA    . SER A 1 123 ? 117.167 147.410 92.162  1.00 32.04 ?  123 SER A CA    1 
ATOM   1029  C  C     . SER A 1 123 ? 117.359 148.214 93.439  1.00 31.85 ?  123 SER A C     1 
ATOM   1030  O  O     . SER A 1 123 ? 117.917 149.316 93.408  1.00 39.19 ?  123 SER A O     1 
ATOM   1031  C  CB    . SER A 1 123 ? 115.756 147.620 91.615  1.00 34.60 ?  123 SER A CB    1 
ATOM   1032  O  OG    . SER A 1 123 ? 115.426 146.624 90.669  1.00 39.38 ?  123 SER A OG    1 
ATOM   1033  N  N     . ILE A 1 124 ? 116.891 147.687 94.572  1.00 31.75 ?  124 ILE A N     1 
ATOM   1034  C  CA    . ILE A 1 124 ? 117.067 148.395 95.835  1.00 34.84 ?  124 ILE A CA    1 
ATOM   1035  C  C     . ILE A 1 124 ? 118.545 148.491 96.195  1.00 36.09 ?  124 ILE A C     1 
ATOM   1036  O  O     . ILE A 1 124 ? 119.025 149.549 96.620  1.00 39.49 ?  124 ILE A O     1 
ATOM   1037  C  CB    . ILE A 1 124 ? 116.247 147.718 96.945  1.00 38.69 ?  124 ILE A CB    1 
ATOM   1038  C  CG1   . ILE A 1 124 ? 114.754 147.921 96.685  1.00 39.24 ?  124 ILE A CG1   1 
ATOM   1039  C  CG2   . ILE A 1 124 ? 116.625 148.268 98.307  1.00 33.39 ?  124 ILE A CG2   1 
ATOM   1040  C  CD1   . ILE A 1 124 ? 114.384 149.350 96.344  1.00 37.19 ?  124 ILE A CD1   1 
ATOM   1041  N  N     . VAL A 1 125 ? 119.292 147.398 96.019  1.00 32.10 ?  125 VAL A N     1 
ATOM   1042  C  CA    . VAL A 1 125 ? 120.724 147.422 96.306  1.00 29.01 ?  125 VAL A CA    1 
ATOM   1043  C  C     . VAL A 1 125 ? 121.440 148.405 95.385  1.00 28.32 ?  125 VAL A C     1 
ATOM   1044  O  O     . VAL A 1 125 ? 122.354 149.120 95.807  1.00 39.80 ?  125 VAL A O     1 
ATOM   1045  C  CB    . VAL A 1 125 ? 121.310 146.001 96.198  1.00 33.53 ?  125 VAL A CB    1 
ATOM   1046  C  CG1   . VAL A 1 125 ? 122.816 146.032 96.314  1.00 30.75 ?  125 VAL A CG1   1 
ATOM   1047  C  CG2   . VAL A 1 125 ? 120.729 145.110 97.279  1.00 28.67 ?  125 VAL A CG2   1 
ATOM   1048  N  N     . ALA A 1 126 ? 121.020 148.473 94.121  1.00 26.22 ?  126 ALA A N     1 
ATOM   1049  C  CA    . ALA A 1 126 ? 121.655 149.380 93.172  1.00 26.65 ?  126 ALA A CA    1 
ATOM   1050  C  C     . ALA A 1 126 ? 121.361 150.835 93.504  1.00 34.15 ?  126 ALA A C     1 
ATOM   1051  O  O     . ALA A 1 126 ? 122.253 151.689 93.419  1.00 39.43 ?  126 ALA A O     1 
ATOM   1052  C  CB    . ALA A 1 126 ? 121.188 149.056 91.757  1.00 29.39 ?  126 ALA A CB    1 
ATOM   1053  N  N     . LEU A 1 127 ? 120.115 151.143 93.868  1.00 36.11 ?  127 LEU A N     1 
ATOM   1054  C  CA    . LEU A 1 127 ? 119.776 152.504 94.265  1.00 32.17 ?  127 LEU A CA    1 
ATOM   1055  C  C     . LEU A 1 127 ? 120.480 152.894 95.557  1.00 30.19 ?  127 LEU A C     1 
ATOM   1056  O  O     . LEU A 1 127 ? 120.827 154.066 95.742  1.00 35.16 ?  127 LEU A O     1 
ATOM   1057  C  CB    . LEU A 1 127 ? 118.262 152.646 94.415  1.00 33.59 ?  127 LEU A CB    1 
ATOM   1058  C  CG    . LEU A 1 127 ? 117.451 152.563 93.121  1.00 34.25 ?  127 LEU A CG    1 
ATOM   1059  C  CD1   . LEU A 1 127 ? 116.032 152.110 93.406  1.00 36.24 ?  127 LEU A CD1   1 
ATOM   1060  C  CD2   . LEU A 1 127 ? 117.451 153.893 92.392  1.00 34.84 ?  127 LEU A CD2   1 
ATOM   1061  N  N     . PHE A 1 128 ? 120.689 151.934 96.459  1.00 32.75 ?  128 PHE A N     1 
ATOM   1062  C  CA    . PHE A 1 128 ? 121.489 152.194 97.649  1.00 32.86 ?  128 PHE A CA    1 
ATOM   1063  C  C     . PHE A 1 128 ? 122.940 152.488 97.285  1.00 30.93 ?  128 PHE A C     1 
ATOM   1064  O  O     . PHE A 1 128 ? 123.550 153.409 97.839  1.00 38.78 ?  128 PHE A O     1 
ATOM   1065  C  CB    . PHE A 1 128 ? 121.396 150.999 98.598  1.00 30.53 ?  128 PHE A CB    1 
ATOM   1066  C  CG    . PHE A 1 128 ? 122.280 151.106 99.804  1.00 35.69 ?  128 PHE A CG    1 
ATOM   1067  C  CD1   . PHE A 1 128 ? 121.847 151.774 100.936 1.00 37.91 ?  128 PHE A CD1   1 
ATOM   1068  C  CD2   . PHE A 1 128 ? 123.537 150.527 99.814  1.00 33.56 ?  128 PHE A CD2   1 
ATOM   1069  C  CE1   . PHE A 1 128 ? 122.655 151.870 102.049 1.00 38.80 ?  128 PHE A CE1   1 
ATOM   1070  C  CE2   . PHE A 1 128 ? 124.349 150.625 100.920 1.00 33.60 ?  128 PHE A CE2   1 
ATOM   1071  C  CZ    . PHE A 1 128 ? 123.908 151.294 102.040 1.00 35.48 ?  128 PHE A CZ    1 
ATOM   1072  N  N     . PHE A 1 129 ? 123.508 151.714 96.357  1.00 28.02 ?  129 PHE A N     1 
ATOM   1073  C  CA    . PHE A 1 129 ? 124.898 151.916 95.960  1.00 25.55 ?  129 PHE A CA    1 
ATOM   1074  C  C     . PHE A 1 129 ? 125.101 153.259 95.273  1.00 29.30 ?  129 PHE A C     1 
ATOM   1075  O  O     . PHE A 1 129 ? 126.083 153.959 95.543  1.00 33.20 ?  129 PHE A O     1 
ATOM   1076  C  CB    . PHE A 1 129 ? 125.353 150.790 95.033  1.00 26.16 ?  129 PHE A CB    1 
ATOM   1077  C  CG    . PHE A 1 129 ? 125.636 149.497 95.732  1.00 25.05 ?  129 PHE A CG    1 
ATOM   1078  C  CD1   . PHE A 1 129 ? 125.812 149.456 97.101  1.00 27.59 ?  129 PHE A CD1   1 
ATOM   1079  C  CD2   . PHE A 1 129 ? 125.742 148.321 95.011  1.00 26.52 ?  129 PHE A CD2   1 
ATOM   1080  C  CE1   . PHE A 1 129 ? 126.073 148.264 97.741  1.00 24.89 ?  129 PHE A CE1   1 
ATOM   1081  C  CE2   . PHE A 1 129 ? 126.009 147.128 95.644  1.00 26.00 ?  129 PHE A CE2   1 
ATOM   1082  C  CZ    . PHE A 1 129 ? 126.174 147.100 97.011  1.00 27.59 ?  129 PHE A CZ    1 
ATOM   1083  N  N     . ALA A 1 130 ? 124.186 153.633 94.376  1.00 35.43 ?  130 ALA A N     1 
ATOM   1084  C  CA    . ALA A 1 130 ? 124.410 154.801 93.532  1.00 35.20 ?  130 ALA A CA    1 
ATOM   1085  C  C     . ALA A 1 130 ? 124.342 156.103 94.319  1.00 42.34 ?  130 ALA A C     1 
ATOM   1086  O  O     . ALA A 1 130 ? 125.010 157.077 93.955  1.00 47.09 ?  130 ALA A O     1 
ATOM   1087  C  CB    . ALA A 1 130 ? 123.399 154.819 92.392  1.00 34.43 ?  130 ALA A CB    1 
ATOM   1088  N  N     . ASN A 1 131 ? 123.537 156.144 95.383  1.00 42.79 ?  131 ASN A N     1 
ATOM   1089  C  CA    . ASN A 1 131 ? 123.446 157.306 96.268  1.00 43.74 ?  131 ASN A CA    1 
ATOM   1090  C  C     . ASN A 1 131 ? 123.012 158.559 95.505  1.00 43.29 ?  131 ASN A C     1 
ATOM   1091  O  O     . ASN A 1 131 ? 123.656 159.608 95.566  1.00 47.94 ?  131 ASN A O     1 
ATOM   1092  C  CB    . ASN A 1 131 ? 124.770 157.536 97.002  1.00 43.48 ?  131 ASN A CB    1 
ATOM   1093  C  CG    . ASN A 1 131 ? 124.613 158.410 98.229  1.00 48.16 ?  131 ASN A CG    1 
ATOM   1094  O  OD1   . ASN A 1 131 ? 123.679 158.239 99.012  1.00 44.83 ?  131 ASN A OD1   1 
ATOM   1095  N  ND2   . ASN A 1 131 ? 125.529 159.353 98.403  1.00 46.49 ?  131 ASN A ND2   1 
ATOM   1096  N  N     . GLY A 1 132 ? 121.903 158.441 94.778  1.00 41.46 ?  132 GLY A N     1 
ATOM   1097  C  CA    . GLY A 1 132 ? 121.305 159.555 94.081  1.00 41.96 ?  132 GLY A CA    1 
ATOM   1098  C  C     . GLY A 1 132 ? 121.538 159.583 92.583  1.00 44.87 ?  132 GLY A C     1 
ATOM   1099  O  O     . GLY A 1 132 ? 120.836 160.317 91.879  1.00 49.08 ?  132 GLY A O     1 
ATOM   1100  N  N     . ASP A 1 133 ? 122.493 158.808 92.077  1.00 47.04 ?  133 ASP A N     1 
ATOM   1101  C  CA    . ASP A 1 133 ? 122.815 158.803 90.655  1.00 46.05 ?  133 ASP A CA    1 
ATOM   1102  C  C     . ASP A 1 133 ? 121.947 157.775 89.939  1.00 49.14 ?  133 ASP A C     1 
ATOM   1103  O  O     . ASP A 1 133 ? 121.976 156.588 90.275  1.00 49.71 ?  133 ASP A O     1 
ATOM   1104  C  CB    . ASP A 1 133 ? 124.298 158.501 90.442  1.00 48.23 ?  133 ASP A CB    1 
ATOM   1105  C  CG    . ASP A 1 133 ? 124.821 159.036 89.123  1.00 53.27 ?  133 ASP A CG    1 
ATOM   1106  O  OD1   . ASP A 1 133 ? 124.016 159.201 88.182  1.00 52.24 ?  133 ASP A OD1   1 
ATOM   1107  O  OD2   . ASP A 1 133 ? 126.039 159.292 89.028  1.00 52.57 -1 133 ASP A OD2   1 
ATOM   1108  N  N     . THR A 1 134 ? 121.174 158.232 88.953  1.00 48.73 ?  134 THR A N     1 
ATOM   1109  C  CA    . THR A 1 134 ? 120.293 157.321 88.227  1.00 47.99 ?  134 THR A CA    1 
ATOM   1110  C  C     . THR A 1 134 ? 121.077 156.434 87.267  1.00 49.88 ?  134 THR A C     1 
ATOM   1111  O  O     . THR A 1 134 ? 120.834 155.223 87.190  1.00 51.80 ?  134 THR A O     1 
ATOM   1112  C  CB    . THR A 1 134 ? 119.232 158.119 87.474  1.00 52.41 ?  134 THR A CB    1 
ATOM   1113  O  OG1   . THR A 1 134 ? 118.382 158.779 88.418  1.00 53.72 ?  134 THR A OG1   1 
ATOM   1114  C  CG2   . THR A 1 134 ? 118.388 157.202 86.603  1.00 51.31 ?  134 THR A CG2   1 
ATOM   1115  N  N     . GLU A 1 135 ? 122.024 157.018 86.528  1.00 47.24 ?  135 GLU A N     1 
ATOM   1116  C  CA    . GLU A 1 135 ? 122.818 156.236 85.586  1.00 47.75 ?  135 GLU A CA    1 
ATOM   1117  C  C     . GLU A 1 135 ? 123.688 155.218 86.311  1.00 48.60 ?  135 GLU A C     1 
ATOM   1118  O  O     . GLU A 1 135 ? 123.835 154.080 85.851  1.00 51.03 ?  135 GLU A O     1 
ATOM   1119  C  CB    . GLU A 1 135 ? 123.676 157.164 84.729  1.00 49.48 ?  135 GLU A CB    1 
ATOM   1120  C  CG    . GLU A 1 135 ? 122.873 158.143 83.893  1.00 48.79 ?  135 GLU A CG    1 
ATOM   1121  C  CD    . GLU A 1 135 ? 121.777 157.463 83.099  1.00 54.08 ?  135 GLU A CD    1 
ATOM   1122  O  OE1   . GLU A 1 135 ? 122.097 156.574 82.283  1.00 54.31 ?  135 GLU A OE1   1 
ATOM   1123  O  OE2   . GLU A 1 135 ? 120.594 157.816 83.293  1.00 55.23 -1 135 GLU A OE2   1 
ATOM   1124  N  N     . LYS A 1 136 ? 124.275 155.609 87.443  1.00 40.59 ?  136 LYS A N     1 
ATOM   1125  C  CA    . LYS A 1 136 ? 125.056 154.665 88.233  1.00 40.58 ?  136 LYS A CA    1 
ATOM   1126  C  C     . LYS A 1 136 ? 124.174 153.554 88.787  1.00 41.54 ?  136 LYS A C     1 
ATOM   1127  O  O     . LYS A 1 136 ? 124.596 152.395 88.861  1.00 44.71 ?  136 LYS A O     1 
ATOM   1128  C  CB    . LYS A 1 136 ? 125.778 155.400 89.361  1.00 45.00 ?  136 LYS A CB    1 
ATOM   1129  C  CG    . LYS A 1 136 ? 126.971 154.656 89.929  1.00 42.10 ?  136 LYS A CG    1 
ATOM   1130  C  CD    . LYS A 1 136 ? 128.164 154.742 88.999  1.00 43.50 ?  136 LYS A CD    1 
ATOM   1131  C  CE    . LYS A 1 136 ? 129.464 154.503 89.746  1.00 46.23 ?  136 LYS A CE    1 
ATOM   1132  N  NZ    . LYS A 1 136 ? 130.647 154.745 88.875  1.00 47.84 1  136 LYS A NZ    1 
ATOM   1133  N  N     . ALA A 1 137 ? 122.945 153.890 89.186  1.00 39.31 ?  137 ALA A N     1 
ATOM   1134  C  CA    . ALA A 1 137 ? 122.016 152.866 89.653  1.00 34.47 ?  137 ALA A CA    1 
ATOM   1135  C  C     . ALA A 1 137 ? 121.681 151.881 88.542  1.00 36.75 ?  137 ALA A C     1 
ATOM   1136  O  O     . ALA A 1 137 ? 121.604 150.670 88.778  1.00 39.98 ?  137 ALA A O     1 
ATOM   1137  C  CB    . ALA A 1 137 ? 120.747 153.517 90.199  1.00 36.06 ?  137 ALA A CB    1 
ATOM   1138  N  N     . LYS A 1 138 ? 121.480 152.382 87.321  1.00 40.72 ?  138 LYS A N     1 
ATOM   1139  C  CA    . LYS A 1 138 ? 121.239 151.491 86.189  1.00 40.87 ?  138 LYS A CA    1 
ATOM   1140  C  C     . LYS A 1 138 ? 122.457 150.624 85.895  1.00 41.41 ?  138 LYS A C     1 
ATOM   1141  O  O     . LYS A 1 138 ? 122.319 149.446 85.548  1.00 43.37 ?  138 LYS A O     1 
ATOM   1142  C  CB    . LYS A 1 138 ? 120.843 152.303 84.957  1.00 45.21 ?  138 LYS A CB    1 
ATOM   1143  C  CG    . LYS A 1 138 ? 119.410 152.803 84.979  1.00 44.02 ?  138 LYS A CG    1 
ATOM   1144  C  CD    . LYS A 1 138 ? 119.249 154.053 84.135  1.00 43.87 ?  138 LYS A CD    1 
ATOM   1145  C  CE    . LYS A 1 138 ? 118.984 153.703 82.682  1.00 47.11 ?  138 LYS A CE    1 
ATOM   1146  N  NZ    . LYS A 1 138 ? 118.949 154.914 81.818  1.00 48.97 1  138 LYS A NZ    1 
ATOM   1147  N  N     . GLU A 1 139 ? 123.658 151.192 86.019  1.00 40.08 ?  139 GLU A N     1 
ATOM   1148  C  CA    . GLU A 1 139 ? 124.874 150.407 85.828  1.00 36.52 ?  139 GLU A CA    1 
ATOM   1149  C  C     . GLU A 1 139 ? 124.983 149.292 86.863  1.00 34.97 ?  139 GLU A C     1 
ATOM   1150  O  O     . GLU A 1 139 ? 125.342 148.158 86.530  1.00 40.47 ?  139 GLU A O     1 
ATOM   1151  C  CB    . GLU A 1 139 ? 126.100 151.317 85.890  1.00 38.10 ?  139 GLU A CB    1 
ATOM   1152  C  CG    . GLU A 1 139 ? 126.425 152.015 84.582  1.00 41.30 ?  139 GLU A CG    1 
ATOM   1153  C  CD    . GLU A 1 139 ? 127.514 153.056 84.733  1.00 48.31 ?  139 GLU A CD    1 
ATOM   1154  O  OE1   . GLU A 1 139 ? 127.568 153.713 85.794  1.00 45.67 ?  139 GLU A OE1   1 
ATOM   1155  O  OE2   . GLU A 1 139 ? 128.318 153.221 83.793  1.00 48.32 -1 139 GLU A OE2   1 
ATOM   1156  N  N     . TYR A 1 140 ? 124.678 149.598 88.125  1.00 32.51 ?  140 TYR A N     1 
ATOM   1157  C  CA    . TYR A 1 140 ? 124.696 148.575 89.167  1.00 30.56 ?  140 TYR A CA    1 
ATOM   1158  C  C     . TYR A 1 140 ? 123.636 147.510 88.910  1.00 33.75 ?  140 TYR A C     1 
ATOM   1159  O  O     . TYR A 1 140 ? 123.867 146.320 89.153  1.00 34.13 ?  140 TYR A O     1 
ATOM   1160  C  CB    . TYR A 1 140 ? 124.478 149.211 90.536  1.00 32.61 ?  140 TYR A CB    1 
ATOM   1161  C  CG    . TYR A 1 140 ? 125.679 149.915 91.114  1.00 32.42 ?  140 TYR A CG    1 
ATOM   1162  C  CD1   . TYR A 1 140 ? 126.879 149.244 91.306  1.00 34.45 ?  140 TYR A CD1   1 
ATOM   1163  C  CD2   . TYR A 1 140 ? 125.607 151.247 91.484  1.00 33.15 ?  140 TYR A CD2   1 
ATOM   1164  C  CE1   . TYR A 1 140 ? 127.973 149.889 91.843  1.00 34.20 ?  140 TYR A CE1   1 
ATOM   1165  C  CE2   . TYR A 1 140 ? 126.693 151.898 92.017  1.00 35.74 ?  140 TYR A CE2   1 
ATOM   1166  C  CZ    . TYR A 1 140 ? 127.872 151.218 92.195  1.00 30.78 ?  140 TYR A CZ    1 
ATOM   1167  O  OH    . TYR A 1 140 ? 128.949 151.877 92.730  1.00 33.69 ?  140 TYR A OH    1 
ATOM   1168  N  N     . VAL A 1 141 ? 122.459 147.928 88.439  1.00 33.86 ?  141 VAL A N     1 
ATOM   1169  C  CA    . VAL A 1 141 ? 121.408 146.975 88.096  1.00 33.00 ?  141 VAL A CA    1 
ATOM   1170  C  C     . VAL A 1 141 ? 121.880 146.035 86.999  1.00 35.02 ?  141 VAL A C     1 
ATOM   1171  O  O     . VAL A 1 141 ? 121.681 144.820 87.076  1.00 39.42 ?  141 VAL A O     1 
ATOM   1172  C  CB    . VAL A 1 141 ? 120.124 147.717 87.684  1.00 36.37 ?  141 VAL A CB    1 
ATOM   1173  C  CG1   . VAL A 1 141 ? 119.244 146.814 86.858  1.00 36.42 ?  141 VAL A CG1   1 
ATOM   1174  C  CG2   . VAL A 1 141 ? 119.372 148.170 88.905  1.00 35.34 ?  141 VAL A CG2   1 
ATOM   1175  N  N     . ASN A 1 142 ? 122.513 146.580 85.960  1.00 35.68 ?  142 ASN A N     1 
ATOM   1176  C  CA    . ASN A 1 142 ? 123.039 145.735 84.894  1.00 31.75 ?  142 ASN A CA    1 
ATOM   1177  C  C     . ASN A 1 142 ? 124.116 144.798 85.422  1.00 33.91 ?  142 ASN A C     1 
ATOM   1178  O  O     . ASN A 1 142 ? 124.183 143.630 85.027  1.00 40.10 ?  142 ASN A O     1 
ATOM   1179  C  CB    . ASN A 1 142 ? 123.586 146.599 83.761  1.00 32.37 ?  142 ASN A CB    1 
ATOM   1180  C  CG    . ASN A 1 142 ? 122.498 147.110 82.846  1.00 38.00 ?  142 ASN A CG    1 
ATOM   1181  O  OD1   . ASN A 1 142 ? 121.624 146.356 82.421  1.00 37.20 ?  142 ASN A OD1   1 
ATOM   1182  N  ND2   . ASN A 1 142 ? 122.541 148.400 82.540  1.00 36.90 ?  142 ASN A ND2   1 
ATOM   1183  N  N     . LEU A 1 143 ? 124.971 145.298 86.315  1.00 34.59 ?  143 LEU A N     1 
ATOM   1184  C  CA    . LEU A 1 143 ? 126.049 144.480 86.858  1.00 27.88 ?  143 LEU A CA    1 
ATOM   1185  C  C     . LEU A 1 143 ? 125.513 143.304 87.666  1.00 29.22 ?  143 LEU A C     1 
ATOM   1186  O  O     . LEU A 1 143 ? 126.024 142.184 87.556  1.00 29.56 ?  143 LEU A O     1 
ATOM   1187  C  CB    . LEU A 1 143 ? 126.967 145.348 87.717  1.00 27.94 ?  143 LEU A CB    1 
ATOM   1188  C  CG    . LEU A 1 143 ? 128.411 144.884 87.874  1.00 32.99 ?  143 LEU A CG    1 
ATOM   1189  C  CD1   . LEU A 1 143 ? 129.171 145.134 86.589  1.00 33.82 ?  143 LEU A CD1   1 
ATOM   1190  C  CD2   . LEU A 1 143 ? 129.057 145.617 89.028  1.00 28.96 ?  143 LEU A CD2   1 
ATOM   1191  N  N     . MET A 1 144 ? 124.491 143.536 88.490  1.00 33.23 ?  144 MET A N     1 
ATOM   1192  C  CA    . MET A 1 144 ? 124.012 142.471 89.366  1.00 27.56 ?  144 MET A CA    1 
ATOM   1193  C  C     . MET A 1 144 ? 122.997 141.561 88.678  1.00 28.03 ?  144 MET A C     1 
ATOM   1194  O  O     . MET A 1 144 ? 122.949 140.362 88.968  1.00 31.91 ?  144 MET A O     1 
ATOM   1195  C  CB    . MET A 1 144 ? 123.421 143.058 90.646  1.00 28.77 ?  144 MET A CB    1 
ATOM   1196  C  CG    . MET A 1 144 ? 124.399 143.902 91.445  1.00 30.13 ?  144 MET A CG    1 
ATOM   1197  S  SD    . MET A 1 144 ? 123.722 144.419 93.029  1.00 44.79 ?  144 MET A SD    1 
ATOM   1198  C  CE    . MET A 1 144 ? 122.911 145.940 92.563  1.00 33.81 ?  144 MET A CE    1 
ATOM   1199  N  N     . ILE A 1 145 ? 122.166 142.106 87.785  1.00 28.21 ?  145 ILE A N     1 
ATOM   1200  C  CA    . ILE A 1 145 ? 121.201 141.271 87.075  1.00 30.79 ?  145 ILE A CA    1 
ATOM   1201  C  C     . ILE A 1 145 ? 121.908 140.375 86.066  1.00 33.87 ?  145 ILE A C     1 
ATOM   1202  O  O     . ILE A 1 145 ? 121.461 139.251 85.807  1.00 37.32 ?  145 ILE A O     1 
ATOM   1203  C  CB    . ILE A 1 145 ? 120.105 142.138 86.421  1.00 31.53 ?  145 ILE A CB    1 
ATOM   1204  C  CG1   . ILE A 1 145 ? 118.802 141.346 86.304  1.00 30.46 ?  145 ILE A CG1   1 
ATOM   1205  C  CG2   . ILE A 1 145 ? 120.530 142.652 85.052  1.00 30.98 ?  145 ILE A CG2   1 
ATOM   1206  C  CD1   . ILE A 1 145 ? 118.164 141.008 87.630  1.00 28.31 ?  145 ILE A CD1   1 
ATOM   1207  N  N     . ASN A 1 146 ? 123.013 140.842 85.481  1.00 29.04 ?  146 ASN A N     1 
ATOM   1208  C  CA    . ASN A 1 146 ? 123.878 139.960 84.714  1.00 27.56 ?  146 ASN A CA    1 
ATOM   1209  C  C     . ASN A 1 146 ? 124.670 139.027 85.615  1.00 29.54 ?  146 ASN A C     1 
ATOM   1210  O  O     . ASN A 1 146 ? 125.338 138.121 85.108  1.00 36.63 ?  146 ASN A O     1 
ATOM   1211  C  CB    . ASN A 1 146 ? 124.839 140.771 83.844  1.00 29.11 ?  146 ASN A CB    1 
ATOM   1212  C  CG    . ASN A 1 146 ? 124.121 141.593 82.795  1.00 33.00 ?  146 ASN A CG    1 
ATOM   1213  O  OD1   . ASN A 1 146 ? 122.957 141.347 82.488  1.00 34.73 ?  146 ASN A OD1   1 
ATOM   1214  N  ND2   . ASN A 1 146 ? 124.816 142.577 82.239  1.00 35.28 ?  146 ASN A ND2   1 
ATOM   1215  N  N     . GLN A 1 147 ? 124.608 139.242 86.929  1.00 28.22 ?  147 GLN A N     1 
ATOM   1216  C  CA    . GLN A 1 147 ? 125.312 138.435 87.919  1.00 24.26 ?  147 GLN A CA    1 
ATOM   1217  C  C     . GLN A 1 147 ? 126.816 138.454 87.689  1.00 27.66 ?  147 GLN A C     1 
ATOM   1218  O  O     . GLN A 1 147 ? 127.501 137.462 87.925  1.00 34.10 ?  147 GLN A O     1 
ATOM   1219  C  CB    . GLN A 1 147 ? 124.775 137.001 87.946  1.00 24.18 ?  147 GLN A CB    1 
ATOM   1220  C  CG    . GLN A 1 147 ? 123.344 136.906 88.445  1.00 23.63 ?  147 GLN A CG    1 
ATOM   1221  C  CD    . GLN A 1 147 ? 122.959 135.507 88.864  1.00 27.67 ?  147 GLN A CD    1 
ATOM   1222  O  OE1   . GLN A 1 147 ? 122.326 135.309 89.899  1.00 31.18 ?  147 GLN A OE1   1 
ATOM   1223  N  NE2   . GLN A 1 147 ? 123.330 134.526 88.053  1.00 35.38 ?  147 GLN A NE2   1 
ATOM   1224  N  N     . GLU A 1 148 ? 127.336 139.585 87.208  1.00 26.16 ?  148 GLU A N     1 
ATOM   1225  C  CA    . GLU A 1 148 ? 128.777 139.764 87.095  1.00 22.83 ?  148 GLU A CA    1 
ATOM   1226  C  C     . GLU A 1 148 ? 129.413 140.074 88.442  1.00 26.73 ?  148 GLU A C     1 
ATOM   1227  O  O     . GLU A 1 148 ? 130.551 139.667 88.697  1.00 28.77 ?  148 GLU A O     1 
ATOM   1228  C  CB    . GLU A 1 148 ? 129.090 140.879 86.099  1.00 21.54 ?  148 GLU A CB    1 
ATOM   1229  C  CG    . GLU A 1 148 ? 128.552 140.626 84.706  1.00 25.93 ?  148 GLU A CG    1 
ATOM   1230  C  CD    . GLU A 1 148 ? 128.648 141.846 83.817  1.00 32.88 ?  148 GLU A CD    1 
ATOM   1231  O  OE1   . GLU A 1 148 ? 127.695 142.651 83.801  1.00 33.79 ?  148 GLU A OE1   1 
ATOM   1232  O  OE2   . GLU A 1 148 ? 129.682 142.003 83.135  1.00 36.84 -1 148 GLU A OE2   1 
ATOM   1233  N  N     . TYR A 1 149 ? 128.701 140.791 89.306  1.00 24.71 ?  149 TYR A N     1 
ATOM   1234  C  CA    . TYR A 1 149 ? 129.170 141.115 90.644  1.00 19.22 ?  149 TYR A CA    1 
ATOM   1235  C  C     . TYR A 1 149 ? 128.074 140.798 91.646  1.00 22.08 ?  149 TYR A C     1 
ATOM   1236  O  O     . TYR A 1 149 ? 126.894 141.055 91.391  1.00 27.63 ?  149 TYR A O     1 
ATOM   1237  C  CB    . TYR A 1 149 ? 129.572 142.588 90.752  1.00 19.77 ?  149 TYR A CB    1 
ATOM   1238  C  CG    . TYR A 1 149 ? 129.775 143.077 92.168  1.00 24.10 ?  149 TYR A CG    1 
ATOM   1239  C  CD1   . TYR A 1 149 ? 130.810 142.588 92.951  1.00 16.11 ?  149 TYR A CD1   1 
ATOM   1240  C  CD2   . TYR A 1 149 ? 128.929 144.027 92.719  1.00 21.98 ?  149 TYR A CD2   1 
ATOM   1241  C  CE1   . TYR A 1 149 ? 130.997 143.035 94.242  1.00 16.16 ?  149 TYR A CE1   1 
ATOM   1242  C  CE2   . TYR A 1 149 ? 129.107 144.477 94.008  1.00 21.75 ?  149 TYR A CE2   1 
ATOM   1243  C  CZ    . TYR A 1 149 ? 130.144 143.979 94.765  1.00 18.88 ?  149 TYR A CZ    1 
ATOM   1244  O  OH    . TYR A 1 149 ? 130.323 144.425 96.052  1.00 21.26 ?  149 TYR A OH    1 
ATOM   1245  N  N     . GLN A 1 150 ? 128.467 140.234 92.778  1.00 18.57 ?  150 GLN A N     1 
ATOM   1246  C  CA    . GLN A 1 150 ? 127.530 139.895 93.846  1.00 14.00 ?  150 GLN A CA    1 
ATOM   1247  C  C     . GLN A 1 150 ? 127.978 140.535 95.149  1.00 16.18 ?  150 GLN A C     1 
ATOM   1248  O  O     . GLN A 1 150 ? 129.040 140.165 95.684  1.00 23.41 ?  150 GLN A O     1 
ATOM   1249  C  CB    . GLN A 1 150 ? 127.425 138.379 94.004  1.00 19.28 ?  150 GLN A CB    1 
ATOM   1250  C  CG    . GLN A 1 150 ? 126.709 137.916 95.259  1.00 21.38 ?  150 GLN A CG    1 
ATOM   1251  C  CD    . GLN A 1 150 ? 125.262 138.355 95.308  1.00 16.86 ?  150 GLN A CD    1 
ATOM   1252  O  OE1   . GLN A 1 150 ? 124.439 137.907 94.512  1.00 29.61 ?  150 GLN A OE1   1 
ATOM   1253  N  NE2   . GLN A 1 150 ? 124.944 139.233 96.247  1.00 14.13 ?  150 GLN A NE2   1 
ATOM   1254  N  N     . PRO A 1 151 ? 127.229 141.495 95.688  1.00 25.42 ?  151 PRO A N     1 
ATOM   1255  C  CA    . PRO A 1 151 ? 127.546 142.007 97.025  1.00 16.72 ?  151 PRO A CA    1 
ATOM   1256  C  C     . PRO A 1 151 ? 127.428 140.904 98.066  1.00 18.06 ?  151 PRO A C     1 
ATOM   1257  O  O     . PRO A 1 151 ? 126.663 139.951 97.909  1.00 24.62 ?  151 PRO A O     1 
ATOM   1258  C  CB    . PRO A 1 151 ? 126.498 143.103 97.245  1.00 15.05 ?  151 PRO A CB    1 
ATOM   1259  C  CG    . PRO A 1 151 ? 126.034 143.471 95.876  1.00 20.42 ?  151 PRO A CG    1 
ATOM   1260  C  CD    . PRO A 1 151 ? 126.113 142.221 95.065  1.00 22.10 ?  151 PRO A CD    1 
ATOM   1261  N  N     . SER A 1 152 ? 128.210 141.039 99.132  1.00 20.26 ?  152 SER A N     1 
ATOM   1262  C  CA    . SER A 1 152 ? 128.242 140.024 100.172 1.00 16.72 ?  152 SER A CA    1 
ATOM   1263  C  C     . SER A 1 152 ? 126.865 139.849 100.806 1.00 23.77 ?  152 SER A C     1 
ATOM   1264  O  O     . SER A 1 152 ? 125.959 140.668 100.635 1.00 26.90 ?  152 SER A O     1 
ATOM   1265  C  CB    . SER A 1 152 ? 129.266 140.389 101.243 1.00 25.81 ?  152 SER A CB    1 
ATOM   1266  O  OG    . SER A 1 152 ? 128.835 141.507 101.996 1.00 28.95 ?  152 SER A OG    1 
ATOM   1267  N  N     . THR A 1 153 ? 126.716 138.749 101.543 1.00 30.12 ?  153 THR A N     1 
ATOM   1268  C  CA    . THR A 1 153 ? 125.456 138.453 102.224 1.00 23.96 ?  153 THR A CA    1 
ATOM   1269  C  C     . THR A 1 153 ? 124.964 139.593 103.108 1.00 30.26 ?  153 THR A C     1 
ATOM   1270  O  O     . THR A 1 153 ? 123.771 139.926 103.028 1.00 27.34 ?  153 THR A O     1 
ATOM   1271  C  CB    . THR A 1 153 ? 125.608 137.151 103.024 1.00 23.09 ?  153 THR A CB    1 
ATOM   1272  O  OG1   . THR A 1 153 ? 125.676 136.040 102.122 1.00 35.60 ?  153 THR A OG1   1 
ATOM   1273  C  CG2   . THR A 1 153 ? 124.437 136.952 103.973 1.00 24.13 ?  153 THR A CG2   1 
ATOM   1274  N  N     . PRO A 1 154 ? 125.791 140.238 103.942 1.00 29.45 ?  154 PRO A N     1 
ATOM   1275  C  CA    . PRO A 1 154 ? 125.273 141.386 104.710 1.00 21.01 ?  154 PRO A CA    1 
ATOM   1276  C  C     . PRO A 1 154 ? 124.779 142.522 103.831 1.00 22.76 ?  154 PRO A C     1 
ATOM   1277  O  O     . PRO A 1 154 ? 123.671 143.030 104.043 1.00 30.56 ?  154 PRO A O     1 
ATOM   1278  C  CB    . PRO A 1 154 ? 126.478 141.804 105.563 1.00 23.98 ?  154 PRO A CB    1 
ATOM   1279  C  CG    . PRO A 1 154 ? 127.330 140.608 105.626 1.00 21.87 ?  154 PRO A CG    1 
ATOM   1280  C  CD    . PRO A 1 154 ? 127.182 139.928 104.318 1.00 22.33 ?  154 PRO A CD    1 
ATOM   1281  N  N     . THR A 1 155 ? 125.572 142.931 102.840 1.00 22.52 ?  155 THR A N     1 
ATOM   1282  C  CA    . THR A 1 155 ? 125.171 144.037 101.977 1.00 22.76 ?  155 THR A CA    1 
ATOM   1283  C  C     . THR A 1 155 ? 123.954 143.668 101.138 1.00 25.20 ?  155 THR A C     1 
ATOM   1284  O  O     . THR A 1 155 ? 122.970 144.411 101.098 1.00 25.43 ?  155 THR A O     1 
ATOM   1285  C  CB    . THR A 1 155 ? 126.336 144.453 101.081 1.00 21.27 ?  155 THR A CB    1 
ATOM   1286  O  OG1   . THR A 1 155 ? 127.462 144.804 101.890 1.00 27.97 ?  155 THR A OG1   1 
ATOM   1287  C  CG2   . THR A 1 155 ? 125.947 145.643 100.227 1.00 16.40 ?  155 THR A CG2   1 
ATOM   1288  N  N     . PHE A 1 156 ? 124.000 142.515 100.469 1.00 27.54 ?  156 PHE A N     1 
ATOM   1289  C  CA    . PHE A 1 156 ? 122.888 142.111 99.614  1.00 25.07 ?  156 PHE A CA    1 
ATOM   1290  C  C     . PHE A 1 156 ? 121.612 141.907 100.420 1.00 27.98 ?  156 PHE A C     1 
ATOM   1291  O  O     . PHE A 1 156 ? 120.509 142.164 99.928  1.00 29.53 ?  156 PHE A O     1 
ATOM   1292  C  CB    . PHE A 1 156 ? 123.251 140.835 98.854  1.00 25.40 ?  156 PHE A CB    1 
ATOM   1293  C  CG    . PHE A 1 156 ? 122.366 140.560 97.675  1.00 27.47 ?  156 PHE A CG    1 
ATOM   1294  C  CD1   . PHE A 1 156 ? 122.225 141.495 96.664  1.00 24.32 ?  156 PHE A CD1   1 
ATOM   1295  C  CD2   . PHE A 1 156 ? 121.677 139.364 97.575  1.00 26.19 ?  156 PHE A CD2   1 
ATOM   1296  C  CE1   . PHE A 1 156 ? 121.413 141.242 95.578  1.00 28.99 ?  156 PHE A CE1   1 
ATOM   1297  C  CE2   . PHE A 1 156 ? 120.865 139.106 96.491  1.00 24.92 ?  156 PHE A CE2   1 
ATOM   1298  C  CZ    . PHE A 1 156 ? 120.733 140.047 95.492  1.00 29.97 ?  156 PHE A CZ    1 
ATOM   1299  N  N     . LEU A 1 157 ? 121.745 141.447 101.664 1.00 31.66 ?  157 LEU A N     1 
ATOM   1300  C  CA    . LEU A 1 157 ? 120.583 141.182 102.502 1.00 28.13 ?  157 LEU A CA    1 
ATOM   1301  C  C     . LEU A 1 157 ? 120.009 142.445 103.129 1.00 29.68 ?  157 LEU A C     1 
ATOM   1302  O  O     . LEU A 1 157 ? 118.792 142.535 103.314 1.00 37.88 ?  157 LEU A O     1 
ATOM   1303  C  CB    . LEU A 1 157 ? 120.956 140.177 103.593 1.00 31.34 ?  157 LEU A CB    1 
ATOM   1304  C  CG    . LEU A 1 157 ? 119.885 139.806 104.619 1.00 31.00 ?  157 LEU A CG    1 
ATOM   1305  C  CD1   . LEU A 1 157 ? 118.695 139.166 103.940 1.00 29.27 ?  157 LEU A CD1   1 
ATOM   1306  C  CD2   . LEU A 1 157 ? 120.460 138.882 105.678 1.00 28.33 ?  157 LEU A CD2   1 
ATOM   1307  N  N     . ASN A 1 158 ? 120.846 143.427 103.455 1.00 32.61 ?  158 ASN A N     1 
ATOM   1308  C  CA    . ASN A 1 158 ? 120.416 144.553 104.270 1.00 26.65 ?  158 ASN A CA    1 
ATOM   1309  C  C     . ASN A 1 158 ? 120.436 145.892 103.543 1.00 31.48 ?  158 ASN A C     1 
ATOM   1310  O  O     . ASN A 1 158 ? 120.020 146.895 104.128 1.00 38.42 ?  158 ASN A O     1 
ATOM   1311  C  CB    . ASN A 1 158 ? 121.285 144.642 105.529 1.00 29.21 ?  158 ASN A CB    1 
ATOM   1312  C  CG    . ASN A 1 158 ? 121.316 143.342 106.307 1.00 36.03 ?  158 ASN A CG    1 
ATOM   1313  O  OD1   . ASN A 1 158 ? 120.302 142.658 106.434 1.00 38.85 ?  158 ASN A OD1   1 
ATOM   1314  N  ND2   . ASN A 1 158 ? 122.484 142.994 106.829 1.00 32.53 ?  158 ASN A ND2   1 
ATOM   1315  N  N     . ALA A 1 159 ? 120.902 145.946 102.296 1.00 33.82 ?  159 ALA A N     1 
ATOM   1316  C  CA    . ALA A 1 159 ? 120.982 147.222 101.595 1.00 29.94 ?  159 ALA A CA    1 
ATOM   1317  C  C     . ALA A 1 159 ? 119.599 147.823 101.383 1.00 36.52 ?  159 ALA A C     1 
ATOM   1318  O  O     . ALA A 1 159 ? 118.781 147.271 100.640 1.00 42.82 ?  159 ALA A O     1 
ATOM   1319  C  CB    . ALA A 1 159 ? 121.694 147.067 100.252 1.00 34.55 ?  159 ALA A CB    1 
ATOM   1320  N  N     . GLY A 1 160 ? 119.332 148.952 102.032 1.00 43.17 ?  160 GLY A N     1 
ATOM   1321  C  CA    . GLY A 1 160 ? 118.068 149.639 101.885 1.00 40.60 ?  160 GLY A CA    1 
ATOM   1322  C  C     . GLY A 1 160 ? 116.959 149.188 102.805 1.00 44.10 ?  160 GLY A C     1 
ATOM   1323  O  O     . GLY A 1 160 ? 115.823 149.644 102.642 1.00 45.10 ?  160 GLY A O     1 
ATOM   1324  N  N     . ARG A 1 161 ? 117.243 148.310 103.762 1.00 44.10 ?  161 ARG A N     1 
ATOM   1325  C  CA    . ARG A 1 161 ? 116.246 147.837 104.711 1.00 43.77 ?  161 ARG A CA    1 
ATOM   1326  C  C     . ARG A 1 161 ? 116.354 148.617 106.014 1.00 45.82 ?  161 ARG A C     1 
ATOM   1327  O  O     . ARG A 1 161 ? 117.455 148.953 106.458 1.00 48.53 ?  161 ARG A O     1 
ATOM   1328  C  CB    . ARG A 1 161 ? 116.411 146.340 104.976 1.00 41.51 ?  161 ARG A CB    1 
ATOM   1329  C  CG    . ARG A 1 161 ? 116.164 145.474 103.754 1.00 42.22 ?  161 ARG A CG    1 
ATOM   1330  C  CD    . ARG A 1 161 ? 115.984 144.015 104.126 1.00 41.57 ?  161 ARG A CD    1 
ATOM   1331  N  NE    . ARG A 1 161 ? 116.009 143.155 102.950 1.00 45.49 ?  161 ARG A NE    1 
ATOM   1332  C  CZ    . ARG A 1 161 ? 115.925 141.832 102.983 1.00 45.46 ?  161 ARG A CZ    1 
ATOM   1333  N  NH1   . ARG A 1 161 ? 115.804 141.175 104.125 1.00 43.98 1  161 ARG A NH1   1 
ATOM   1334  N  NH2   . ARG A 1 161 ? 115.969 141.151 101.843 1.00 42.72 ?  161 ARG A NH2   1 
ATOM   1335  N  N     . LYS A 1 162 ? 115.201 148.908 106.621 1.00 53.82 ?  162 LYS A N     1 
ATOM   1336  C  CA    . LYS A 1 162 ? 115.189 149.702 107.846 1.00 52.61 ?  162 LYS A CA    1 
ATOM   1337  C  C     . LYS A 1 162 ? 115.696 148.894 109.034 1.00 54.80 ?  162 LYS A C     1 
ATOM   1338  O  O     . LYS A 1 162 ? 116.715 149.238 109.643 1.00 55.62 ?  162 LYS A O     1 
ATOM   1339  C  CB    . LYS A 1 162 ? 113.778 150.224 108.118 1.00 52.45 ?  162 LYS A CB    1 
ATOM   1340  C  CG    . LYS A 1 162 ? 113.731 151.652 108.632 1.00 55.20 ?  162 LYS A CG    1 
ATOM   1341  C  CD    . LYS A 1 162 ? 112.330 152.229 108.535 1.00 55.29 ?  162 LYS A CD    1 
ATOM   1342  C  CE    . LYS A 1 162 ? 112.355 153.748 108.536 1.00 54.69 ?  162 LYS A CE    1 
ATOM   1343  N  NZ    . LYS A 1 162 ? 113.561 154.280 109.229 1.00 55.20 1  162 LYS A NZ    1 
ATOM   1344  N  N     . ARG A 1 163 ? 114.998 147.814 109.375 1.00 57.23 ?  163 ARG A N     1 
ATOM   1345  C  CA    . ARG A 1 163 ? 115.385 146.962 110.498 1.00 57.25 ?  163 ARG A CA    1 
ATOM   1346  C  C     . ARG A 1 163 ? 116.415 145.942 110.019 1.00 58.83 ?  163 ARG A C     1 
ATOM   1347  O  O     . ARG A 1 163 ? 116.121 144.777 109.744 1.00 57.95 ?  163 ARG A O     1 
ATOM   1348  C  CB    . ARG A 1 163 ? 114.154 146.295 111.103 1.00 60.18 ?  163 ARG A CB    1 
ATOM   1349  C  CG    . ARG A 1 163 ? 113.158 147.280 111.694 1.00 58.41 ?  163 ARG A CG    1 
ATOM   1350  C  CD    . ARG A 1 163 ? 111.830 146.613 111.997 1.00 58.40 ?  163 ARG A CD    1 
ATOM   1351  N  NE    . ARG A 1 163 ? 111.166 146.162 110.781 1.00 60.59 ?  163 ARG A NE    1 
ATOM   1352  C  CZ    . ARG A 1 163 ? 110.079 145.402 110.758 1.00 62.32 ?  163 ARG A CZ    1 
ATOM   1353  N  NH1   . ARG A 1 163 ? 109.496 144.998 111.875 1.00 61.42 1  163 ARG A NH1   1 
ATOM   1354  N  NH2   . ARG A 1 163 ? 109.564 145.041 109.586 1.00 59.59 ?  163 ARG A NH2   1 
ATOM   1355  N  N     . ARG A 1 164 ? 117.651 146.419 109.925 1.00 53.64 ?  164 ARG A N     1 
ATOM   1356  C  CA    . ARG A 1 164 ? 118.744 145.680 109.319 1.00 50.73 ?  164 ARG A CA    1 
ATOM   1357  C  C     . ARG A 1 164 ? 119.949 145.652 110.248 1.00 51.26 ?  164 ARG A C     1 
ATOM   1358  O  O     . ARG A 1 164 ? 120.094 146.487 111.145 1.00 52.65 ?  164 ARG A O     1 
ATOM   1359  C  CB    . ARG A 1 164 ? 119.154 146.308 107.983 1.00 49.66 ?  164 ARG A CB    1 
ATOM   1360  C  CG    . ARG A 1 164 ? 119.871 147.644 108.139 1.00 46.69 ?  164 ARG A CG    1 
ATOM   1361  C  CD    . ARG A 1 164 ? 120.742 147.949 106.937 1.00 49.28 ?  164 ARG A CD    1 
ATOM   1362  N  NE    . ARG A 1 164 ? 121.502 149.184 107.090 1.00 50.57 ?  164 ARG A NE    1 
ATOM   1363  C  CZ    . ARG A 1 164 ? 121.683 150.074 106.124 1.00 51.84 ?  164 ARG A CZ    1 
ATOM   1364  N  NH1   . ARG A 1 164 ? 121.158 149.903 104.920 1.00 47.62 1  164 ARG A NH1   1 
ATOM   1365  N  NH2   . ARG A 1 164 ? 122.408 151.161 106.369 1.00 50.81 ?  164 ARG A NH2   1 
ATOM   1366  N  N     . GLY A 1 165 ? 120.815 144.669 110.021 1.00 45.41 ?  165 GLY A N     1 
ATOM   1367  C  CA    . GLY A 1 165 ? 122.129 144.658 110.619 1.00 42.70 ?  165 GLY A CA    1 
ATOM   1368  C  C     . GLY A 1 165 ? 123.097 145.497 109.809 1.00 47.81 ?  165 GLY A C     1 
ATOM   1369  O  O     . GLY A 1 165 ? 122.726 146.215 108.878 1.00 44.98 ?  165 GLY A O     1 
ATOM   1370  N  N     . GLU A 1 166 ? 124.369 145.403 110.177 1.00 45.86 ?  166 GLU A N     1 
ATOM   1371  C  CA    . GLU A 1 166 ? 125.387 146.138 109.448 1.00 39.66 ?  166 GLU A CA    1 
ATOM   1372  C  C     . GLU A 1 166 ? 125.685 145.460 108.114 1.00 37.91 ?  166 GLU A C     1 
ATOM   1373  O  O     . GLU A 1 166 ? 125.433 144.268 107.919 1.00 38.58 ?  166 GLU A O     1 
ATOM   1374  C  CB    . GLU A 1 166 ? 126.666 146.258 110.275 1.00 37.81 ?  166 GLU A CB    1 
ATOM   1375  C  CG    . GLU A 1 166 ? 126.589 147.291 111.386 1.00 41.94 ?  166 GLU A CG    1 
ATOM   1376  C  CD    . GLU A 1 166 ? 126.311 148.693 110.873 1.00 47.92 ?  166 GLU A CD    1 
ATOM   1377  O  OE1   . GLU A 1 166 ? 126.718 149.010 109.735 1.00 46.33 ?  166 GLU A OE1   1 
ATOM   1378  O  OE2   . GLU A 1 166 ? 125.684 149.481 111.612 1.00 45.41 -1 166 GLU A OE2   1 
ATOM   1379  N  N     . LEU A 1 167 ? 126.226 146.245 107.184 1.00 33.25 ?  167 LEU A N     1 
ATOM   1380  C  CA    . LEU A 1 167 ? 126.635 145.719 105.889 1.00 25.75 ?  167 LEU A CA    1 
ATOM   1381  C  C     . LEU A 1 167 ? 127.998 145.048 105.935 1.00 30.06 ?  167 LEU A C     1 
ATOM   1382  O  O     . LEU A 1 167 ? 128.403 144.435 104.943 1.00 32.58 ?  167 LEU A O     1 
ATOM   1383  C  CB    . LEU A 1 167 ? 126.649 146.838 104.846 1.00 27.51 ?  167 LEU A CB    1 
ATOM   1384  C  CG    . LEU A 1 167 ? 125.332 147.558 104.553 1.00 28.18 ?  167 LEU A CG    1 
ATOM   1385  C  CD1   . LEU A 1 167 ? 125.384 148.197 103.183 1.00 31.34 ?  167 LEU A CD1   1 
ATOM   1386  C  CD2   . LEU A 1 167 ? 124.154 146.610 104.643 1.00 28.89 ?  167 LEU A CD2   1 
ATOM   1387  N  N     . VAL A 1 168 ? 128.708 145.151 107.053 1.00 33.17 ?  168 VAL A N     1 
ATOM   1388  C  CA    . VAL A 1 168 ? 129.987 144.486 107.258 1.00 26.44 ?  168 VAL A CA    1 
ATOM   1389  C  C     . VAL A 1 168 ? 129.797 143.413 108.320 1.00 30.61 ?  168 VAL A C     1 
ATOM   1390  O  O     . VAL A 1 168 ? 129.162 143.655 109.352 1.00 36.41 ?  168 VAL A O     1 
ATOM   1391  C  CB    . VAL A 1 168 ? 131.082 145.488 107.676 1.00 26.26 ?  168 VAL A CB    1 
ATOM   1392  C  CG1   . VAL A 1 168 ? 132.418 144.785 107.834 1.00 29.07 ?  168 VAL A CG1   1 
ATOM   1393  C  CG2   . VAL A 1 168 ? 131.185 146.610 106.660 1.00 31.34 ?  168 VAL A CG2   1 
ATOM   1394  N  N     . SER A 1 169 ? 130.342 142.225 108.066 1.00 29.13 ?  169 SER A N     1 
ATOM   1395  C  CA    . SER A 1 169 ? 130.213 141.116 108.998 1.00 30.02 ?  169 SER A CA    1 
ATOM   1396  C  C     . SER A 1 169 ? 131.545 140.551 109.467 1.00 25.74 ?  169 SER A C     1 
ATOM   1397  O  O     . SER A 1 169 ? 131.548 139.644 110.307 1.00 31.17 ?  169 SER A O     1 
ATOM   1398  C  CB    . SER A 1 169 ? 129.378 139.988 108.380 1.00 33.72 ?  169 SER A CB    1 
ATOM   1399  O  OG    . SER A 1 169 ? 128.010 140.130 108.722 1.00 37.71 ?  169 SER A OG    1 
ATOM   1400  N  N     . CYS A 1 170 ? 132.667 141.042 108.958 1.00 28.39 ?  170 CYS A N     1 
ATOM   1401  C  CA    . CYS A 1 170 ? 133.980 140.603 109.408 1.00 26.92 ?  170 CYS A CA    1 
ATOM   1402  C  C     . CYS A 1 170 ? 134.636 141.742 110.175 1.00 25.20 ?  170 CYS A C     1 
ATOM   1403  O  O     . CYS A 1 170 ? 134.775 142.852 109.651 1.00 27.42 ?  170 CYS A O     1 
ATOM   1404  C  CB    . CYS A 1 170 ? 134.849 140.146 108.232 1.00 33.70 ?  170 CYS A CB    1 
ATOM   1405  S  SG    . CYS A 1 170 ? 135.349 141.422 107.049 1.00 51.33 ?  170 CYS A SG    1 
ATOM   1406  N  N     . PHE A 1 171 ? 135.007 141.472 111.423 1.00 22.44 ?  171 PHE A N     1 
ATOM   1407  C  CA    . PHE A 1 171 ? 135.690 142.433 112.272 1.00 16.13 ?  171 PHE A CA    1 
ATOM   1408  C  C     . PHE A 1 171 ? 136.882 141.759 112.930 1.00 16.35 ?  171 PHE A C     1 
ATOM   1409  O  O     . PHE A 1 171 ? 136.813 140.586 113.307 1.00 27.33 ?  171 PHE A O     1 
ATOM   1410  C  CB    . PHE A 1 171 ? 134.755 143.006 113.342 1.00 17.63 ?  171 PHE A CB    1 
ATOM   1411  C  CG    . PHE A 1 171 ? 133.500 143.610 112.787 1.00 17.41 ?  171 PHE A CG    1 
ATOM   1412  C  CD1   . PHE A 1 171 ? 133.505 144.892 112.269 1.00 16.60 ?  171 PHE A CD1   1 
ATOM   1413  C  CD2   . PHE A 1 171 ? 132.315 142.896 112.786 1.00 16.10 ?  171 PHE A CD2   1 
ATOM   1414  C  CE1   . PHE A 1 171 ? 132.355 145.448 111.757 1.00 15.99 ?  171 PHE A CE1   1 
ATOM   1415  C  CE2   . PHE A 1 171 ? 131.163 143.450 112.275 1.00 16.69 ?  171 PHE A CE2   1 
ATOM   1416  C  CZ    . PHE A 1 171 ? 131.183 144.726 111.761 1.00 14.78 ?  171 PHE A CZ    1 
ATOM   1417  N  N     . LEU A 1 172 ? 137.975 142.505 113.056 1.00 17.80 ?  172 LEU A N     1 
ATOM   1418  C  CA    . LEU A 1 172 ? 139.202 142.017 113.667 1.00 7.46  ?  172 LEU A CA    1 
ATOM   1419  C  C     . LEU A 1 172 ? 139.582 142.964 114.792 1.00 13.17 ?  172 LEU A C     1 
ATOM   1420  O  O     . LEU A 1 172 ? 139.709 144.171 114.570 1.00 17.99 ?  172 LEU A O     1 
ATOM   1421  C  CB    . LEU A 1 172 ? 140.338 141.922 112.642 1.00 12.46 ?  172 LEU A CB    1 
ATOM   1422  C  CG    . LEU A 1 172 ? 140.266 140.852 111.553 1.00 7.26  ?  172 LEU A CG    1 
ATOM   1423  C  CD1   . LEU A 1 172 ? 139.342 141.281 110.426 1.00 11.37 ?  172 LEU A CD1   1 
ATOM   1424  C  CD2   . LEU A 1 172 ? 141.652 140.561 111.018 1.00 11.04 ?  172 LEU A CD2   1 
ATOM   1425  N  N     . LEU A 1 173 ? 139.764 142.421 115.992 1.00 22.03 ?  173 LEU A N     1 
ATOM   1426  C  CA    . LEU A 1 173 ? 140.040 143.219 117.178 1.00 9.24  ?  173 LEU A CA    1 
ATOM   1427  C  C     . LEU A 1 173 ? 141.396 142.853 117.760 1.00 16.79 ?  173 LEU A C     1 
ATOM   1428  O  O     . LEU A 1 173 ? 141.730 141.672 117.890 1.00 26.59 ?  173 LEU A O     1 
ATOM   1429  C  CB    . LEU A 1 173 ? 138.965 143.020 118.248 1.00 14.56 ?  173 LEU A CB    1 
ATOM   1430  C  CG    . LEU A 1 173 ? 137.498 143.199 117.864 1.00 16.55 ?  173 LEU A CG    1 
ATOM   1431  C  CD1   . LEU A 1 173 ? 136.632 143.041 119.098 1.00 20.59 ?  173 LEU A CD1   1 
ATOM   1432  C  CD2   . LEU A 1 173 ? 137.258 144.543 117.203 1.00 15.88 ?  173 LEU A CD2   1 
ATOM   1433  N  N     . GLU A 1 174 ? 142.171 143.872 118.111 1.00 23.22 ?  174 GLU A N     1 
ATOM   1434  C  CA    . GLU A 1 174 ? 143.417 143.698 118.843 1.00 19.58 ?  174 GLU A CA    1 
ATOM   1435  C  C     . GLU A 1 174 ? 143.140 143.924 120.324 1.00 17.36 ?  174 GLU A C     1 
ATOM   1436  O  O     . GLU A 1 174 ? 142.581 144.958 120.702 1.00 29.19 ?  174 GLU A O     1 
ATOM   1437  C  CB    . GLU A 1 174 ? 144.489 144.664 118.344 1.00 22.04 ?  174 GLU A CB    1 
ATOM   1438  C  CG    . GLU A 1 174 ? 145.025 144.348 116.966 1.00 20.41 ?  174 GLU A CG    1 
ATOM   1439  C  CD    . GLU A 1 174 ? 146.513 144.074 116.975 1.00 19.96 ?  174 GLU A CD    1 
ATOM   1440  O  OE1   . GLU A 1 174 ? 147.297 145.044 116.959 1.00 22.11 ?  174 GLU A OE1   1 
ATOM   1441  O  OE2   . GLU A 1 174 ? 146.898 142.888 116.995 1.00 32.00 -1 174 GLU A OE2   1 
ATOM   1442  N  N     . VAL A 1 175 ? 143.529 142.963 121.155 1.00 18.09 ?  175 VAL A N     1 
ATOM   1443  C  CA    . VAL A 1 175 ? 143.299 143.027 122.593 1.00 21.78 ?  175 VAL A CA    1 
ATOM   1444  C  C     . VAL A 1 175 ? 144.622 143.337 123.278 1.00 19.70 ?  175 VAL A C     1 
ATOM   1445  O  O     . VAL A 1 175 ? 145.601 142.598 123.119 1.00 21.46 ?  175 VAL A O     1 
ATOM   1446  C  CB    . VAL A 1 175 ? 142.697 141.717 123.125 1.00 21.89 ?  175 VAL A CB    1 
ATOM   1447  C  CG1   . VAL A 1 175 ? 142.054 141.940 124.484 1.00 15.48 ?  175 VAL A CG1   1 
ATOM   1448  C  CG2   . VAL A 1 175 ? 141.690 141.155 122.137 1.00 17.38 ?  175 VAL A CG2   1 
ATOM   1449  N  N     . ASN A 1 176 ? 144.654 144.426 124.039 1.00 15.24 ?  176 ASN A N     1 
ATOM   1450  C  CA    . ASN A 1 176 ? 145.841 144.785 124.795 1.00 18.20 ?  176 ASN A CA    1 
ATOM   1451  C  C     . ASN A 1 176 ? 145.899 143.999 126.102 1.00 21.81 ?  176 ASN A C     1 
ATOM   1452  O  O     . ASN A 1 176 ? 144.905 143.437 126.567 1.00 21.13 ?  176 ASN A O     1 
ATOM   1453  C  CB    . ASN A 1 176 ? 145.866 146.286 125.078 1.00 18.41 ?  176 ASN A CB    1 
ATOM   1454  C  CG    . ASN A 1 176 ? 147.248 146.878 124.952 1.00 23.52 ?  176 ASN A CG    1 
ATOM   1455  O  OD1   . ASN A 1 176 ? 148.249 146.175 125.066 1.00 27.38 ?  176 ASN A OD1   1 
ATOM   1456  N  ND2   . ASN A 1 176 ? 147.313 148.180 124.708 1.00 21.82 ?  176 ASN A ND2   1 
ATOM   1457  N  N     . ASP A 1 177 ? 147.089 143.975 126.699 1.00 29.34 ?  177 ASP A N     1 
ATOM   1458  C  CA    . ASP A 1 177 ? 147.350 143.162 127.887 1.00 22.42 ?  177 ASP A CA    1 
ATOM   1459  C  C     . ASP A 1 177 ? 146.931 143.923 129.147 1.00 22.88 ?  177 ASP A C     1 
ATOM   1460  O  O     . ASP A 1 177 ? 147.746 144.372 129.953 1.00 27.43 ?  177 ASP A O     1 
ATOM   1461  C  CB    . ASP A 1 177 ? 148.819 142.760 127.936 1.00 21.20 ?  177 ASP A CB    1 
ATOM   1462  C  CG    . ASP A 1 177 ? 149.106 141.733 129.008 1.00 27.82 ?  177 ASP A CG    1 
ATOM   1463  O  OD1   . ASP A 1 177 ? 148.237 140.875 129.256 1.00 30.56 ?  177 ASP A OD1   1 
ATOM   1464  O  OD2   . ASP A 1 177 ? 150.206 141.782 129.596 1.00 29.71 -1 177 ASP A OD2   1 
ATOM   1465  N  N     . SER A 1 178 ? 145.618 144.059 129.304 1.00 22.26 ?  178 SER A N     1 
ATOM   1466  C  CA    . SER A 1 178 ? 145.064 144.712 130.481 1.00 18.11 ?  178 SER A CA    1 
ATOM   1467  C  C     . SER A 1 178 ? 143.640 144.222 130.691 1.00 20.63 ?  178 SER A C     1 
ATOM   1468  O  O     . SER A 1 178 ? 142.980 143.759 129.759 1.00 29.47 ?  178 SER A O     1 
ATOM   1469  C  CB    . SER A 1 178 ? 145.100 146.237 130.348 1.00 19.31 ?  178 SER A CB    1 
ATOM   1470  O  OG    . SER A 1 178 ? 143.862 146.741 129.891 1.00 25.10 ?  178 SER A OG    1 
ATOM   1471  N  N     . LEU A 1 179 ? 143.176 144.329 131.938 1.00 27.75 ?  179 LEU A N     1 
ATOM   1472  C  CA    . LEU A 1 179 ? 141.803 143.944 132.251 1.00 20.46 ?  179 LEU A CA    1 
ATOM   1473  C  C     . LEU A 1 179 ? 140.805 144.922 131.648 1.00 22.67 ?  179 LEU A C     1 
ATOM   1474  O  O     . LEU A 1 179 ? 139.713 144.522 131.231 1.00 27.44 ?  179 LEU A O     1 
ATOM   1475  C  CB    . LEU A 1 179 ? 141.610 143.852 133.765 1.00 23.33 ?  179 LEU A CB    1 
ATOM   1476  C  CG    . LEU A 1 179 ? 140.283 143.257 134.237 1.00 22.04 ?  179 LEU A CG    1 
ATOM   1477  C  CD1   . LEU A 1 179 ? 140.228 141.768 133.943 1.00 24.32 ?  179 LEU A CD1   1 
ATOM   1478  C  CD2   . LEU A 1 179 ? 140.071 143.528 135.715 1.00 21.57 ?  179 LEU A CD2   1 
ATOM   1479  N  N     . ASN A 1 180 ? 141.155 146.210 131.607 1.00 23.10 ?  180 ASN A N     1 
ATOM   1480  C  CA    . ASN A 1 180 ? 140.298 147.184 130.940 1.00 21.89 ?  180 ASN A CA    1 
ATOM   1481  C  C     . ASN A 1 180 ? 140.147 146.848 129.464 1.00 26.71 ?  180 ASN A C     1 
ATOM   1482  O  O     . ASN A 1 180 ? 139.040 146.890 128.915 1.00 30.16 ?  180 ASN A O     1 
ATOM   1483  C  CB    . ASN A 1 180 ? 140.870 148.590 131.108 1.00 22.57 ?  180 ASN A CB    1 
ATOM   1484  C  CG    . ASN A 1 180 ? 140.510 149.214 132.436 1.00 27.08 ?  180 ASN A CG    1 
ATOM   1485  O  OD1   . ASN A 1 180 ? 139.505 148.860 133.052 1.00 33.00 ?  180 ASN A OD1   1 
ATOM   1486  N  ND2   . ASN A 1 180 ? 141.330 150.155 132.886 1.00 27.92 ?  180 ASN A ND2   1 
ATOM   1487  N  N     . ASP A 1 181 ? 141.253 146.488 128.812 1.00 25.42 ?  181 ASP A N     1 
ATOM   1488  C  CA    . ASP A 1 181 ? 141.203 146.139 127.399 1.00 16.89 ?  181 ASP A CA    1 
ATOM   1489  C  C     . ASP A 1 181 ? 140.487 144.816 127.167 1.00 20.98 ?  181 ASP A C     1 
ATOM   1490  O  O     . ASP A 1 181 ? 139.808 144.661 126.152 1.00 25.91 ?  181 ASP A O     1 
ATOM   1491  C  CB    . ASP A 1 181 ? 142.616 146.101 126.826 1.00 20.00 ?  181 ASP A CB    1 
ATOM   1492  C  CG    . ASP A 1 181 ? 143.195 147.486 126.626 1.00 32.71 ?  181 ASP A CG    1 
ATOM   1493  O  OD1   . ASP A 1 181 ? 142.821 148.150 125.638 1.00 36.80 ?  181 ASP A OD1   1 
ATOM   1494  O  OD2   . ASP A 1 181 ? 144.026 147.913 127.455 1.00 30.19 -1 181 ASP A OD2   1 
ATOM   1495  N  N     . ILE A 1 182 ? 140.609 143.863 128.090 1.00 21.36 ?  182 ILE A N     1 
ATOM   1496  C  CA    . ILE A 1 182 ? 139.885 142.602 127.946 1.00 21.47 ?  182 ILE A CA    1 
ATOM   1497  C  C     . ILE A 1 182 ? 138.385 142.824 128.106 1.00 18.86 ?  182 ILE A C     1 
ATOM   1498  O  O     . ILE A 1 182 ? 137.575 142.262 127.357 1.00 24.47 ?  182 ILE A O     1 
ATOM   1499  C  CB    . ILE A 1 182 ? 140.425 141.565 128.948 1.00 24.51 ?  182 ILE A CB    1 
ATOM   1500  C  CG1   . ILE A 1 182 ? 141.792 141.059 128.491 1.00 20.55 ?  182 ILE A CG1   1 
ATOM   1501  C  CG2   . ILE A 1 182 ? 139.453 140.405 129.105 1.00 26.74 ?  182 ILE A CG2   1 
ATOM   1502  C  CD1   . ILE A 1 182 ? 142.524 140.267 129.534 1.00 22.39 ?  182 ILE A CD1   1 
ATOM   1503  N  N     . SER A 1 183 ? 137.991 143.649 129.079 1.00 22.49 ?  183 SER A N     1 
ATOM   1504  C  CA    . SER A 1 183 ? 136.581 143.981 129.245 1.00 21.31 ?  183 SER A CA    1 
ATOM   1505  C  C     . SER A 1 183 ? 136.040 144.709 128.023 1.00 24.12 ?  183 SER A C     1 
ATOM   1506  O  O     . SER A 1 183 ? 134.931 144.419 127.557 1.00 30.09 ?  183 SER A O     1 
ATOM   1507  C  CB    . SER A 1 183 ? 136.388 144.830 130.499 1.00 21.24 ?  183 SER A CB    1 
ATOM   1508  O  OG    . SER A 1 183 ? 137.035 144.253 131.617 1.00 32.18 ?  183 SER A OG    1 
ATOM   1509  N  N     . ARG A 1 184 ? 136.811 145.658 127.488 1.00 23.49 ?  184 ARG A N     1 
ATOM   1510  C  CA    . ARG A 1 184 ? 136.383 146.349 126.279 1.00 23.99 ?  184 ARG A CA    1 
ATOM   1511  C  C     . ARG A 1 184 ? 136.312 145.406 125.088 1.00 28.93 ?  184 ARG A C     1 
ATOM   1512  O  O     . ARG A 1 184 ? 135.434 145.559 124.237 1.00 33.36 ?  184 ARG A O     1 
ATOM   1513  C  CB    . ARG A 1 184 ? 137.316 147.517 125.976 1.00 23.38 ?  184 ARG A CB    1 
ATOM   1514  C  CG    . ARG A 1 184 ? 136.667 148.605 125.146 1.00 27.12 ?  184 ARG A CG    1 
ATOM   1515  C  CD    . ARG A 1 184 ? 136.078 149.686 126.027 1.00 31.20 ?  184 ARG A CD    1 
ATOM   1516  N  NE    . ARG A 1 184 ? 134.634 149.794 125.862 1.00 31.34 ?  184 ARG A NE    1 
ATOM   1517  C  CZ    . ARG A 1 184 ? 133.876 150.686 126.484 1.00 35.55 ?  184 ARG A CZ    1 
ATOM   1518  N  NH1   . ARG A 1 184 ? 134.395 151.569 127.320 1.00 33.29 1  184 ARG A NH1   1 
ATOM   1519  N  NH2   . ARG A 1 184 ? 132.565 150.693 126.260 1.00 29.20 ?  184 ARG A NH2   1 
ATOM   1520  N  N     . ALA A 1 185 ? 137.221 144.434 125.005 1.00 28.47 ?  185 ALA A N     1 
ATOM   1521  C  CA    . ALA A 1 185 ? 137.161 143.452 123.931 1.00 15.38 ?  185 ALA A CA    1 
ATOM   1522  C  C     . ALA A 1 185 ? 135.901 142.608 124.031 1.00 21.04 ?  185 ALA A C     1 
ATOM   1523  O  O     . ALA A 1 185 ? 135.246 142.341 123.020 1.00 25.07 ?  185 ALA A O     1 
ATOM   1524  C  CB    . ALA A 1 185 ? 138.405 142.567 123.957 1.00 17.48 ?  185 ALA A CB    1 
ATOM   1525  N  N     . ILE A 1 186 ? 135.542 142.184 125.244 1.00 24.51 ?  186 ILE A N     1 
ATOM   1526  C  CA    . ILE A 1 186 ? 134.307 141.424 125.430 1.00 20.17 ?  186 ILE A CA    1 
ATOM   1527  C  C     . ILE A 1 186 ? 133.100 142.266 125.037 1.00 20.92 ?  186 ILE A C     1 
ATOM   1528  O  O     . ILE A 1 186 ? 132.192 141.796 124.336 1.00 27.02 ?  186 ILE A O     1 
ATOM   1529  C  CB    . ILE A 1 186 ? 134.198 140.931 126.886 1.00 27.30 ?  186 ILE A CB    1 
ATOM   1530  C  CG1   . ILE A 1 186 ? 135.232 139.844 127.167 1.00 24.05 ?  186 ILE A CG1   1 
ATOM   1531  C  CG2   . ILE A 1 186 ? 132.796 140.420 127.179 1.00 27.00 ?  186 ILE A CG2   1 
ATOM   1532  C  CD1   . ILE A 1 186 ? 135.470 139.613 128.641 1.00 25.30 ?  186 ILE A CD1   1 
ATOM   1533  N  N     . ASP A 1 187 ? 133.076 143.526 125.477 1.00 27.48 ?  187 ASP A N     1 
ATOM   1534  C  CA    . ASP A 1 187 ? 131.959 144.410 125.159 1.00 23.22 ?  187 ASP A CA    1 
ATOM   1535  C  C     . ASP A 1 187 ? 131.834 144.622 123.656 1.00 27.24 ?  187 ASP A C     1 
ATOM   1536  O  O     . ASP A 1 187 ? 130.739 144.519 123.095 1.00 32.57 ?  187 ASP A O     1 
ATOM   1537  C  CB    . ASP A 1 187 ? 132.133 145.746 125.881 1.00 22.13 ?  187 ASP A CB    1 
ATOM   1538  C  CG    . ASP A 1 187 ? 131.238 146.834 125.321 1.00 34.84 ?  187 ASP A CG    1 
ATOM   1539  O  OD1   . ASP A 1 187 ? 130.013 146.612 125.222 1.00 36.41 ?  187 ASP A OD1   1 
ATOM   1540  O  OD2   . ASP A 1 187 ? 131.761 147.915 124.977 1.00 37.56 -1 187 ASP A OD2   1 
ATOM   1541  N  N     . ILE A 1 188 ? 132.952 144.911 122.988 1.00 25.83 ?  188 ILE A N     1 
ATOM   1542  C  CA    . ILE A 1 188 ? 132.928 145.171 121.553 1.00 22.68 ?  188 ILE A CA    1 
ATOM   1543  C  C     . ILE A 1 188 ? 132.567 143.906 120.787 1.00 22.53 ?  188 ILE A C     1 
ATOM   1544  O  O     . ILE A 1 188 ? 131.860 143.960 119.776 1.00 28.19 ?  188 ILE A O     1 
ATOM   1545  C  CB    . ILE A 1 188 ? 134.279 145.752 121.097 1.00 25.08 ?  188 ILE A CB    1 
ATOM   1546  C  CG1   . ILE A 1 188 ? 134.477 147.155 121.669 1.00 23.81 ?  188 ILE A CG1   1 
ATOM   1547  C  CG2   . ILE A 1 188 ? 134.365 145.807 119.585 1.00 21.04 ?  188 ILE A CG2   1 
ATOM   1548  C  CD1   . ILE A 1 188 ? 135.804 147.770 121.314 1.00 23.99 ?  188 ILE A CD1   1 
ATOM   1549  N  N     . SER A 1 189 ? 133.041 142.750 121.254 1.00 24.80 ?  189 SER A N     1 
ATOM   1550  C  CA    . SER A 1 189 ? 132.680 141.492 120.615 1.00 14.85 ?  189 SER A CA    1 
ATOM   1551  C  C     . SER A 1 189 ? 131.182 141.247 120.701 1.00 21.48 ?  189 SER A C     1 
ATOM   1552  O  O     . SER A 1 189 ? 130.559 140.842 119.715 1.00 28.50 ?  189 SER A O     1 
ATOM   1553  C  CB    . SER A 1 189 ? 133.451 140.339 121.257 1.00 20.15 ?  189 SER A CB    1 
ATOM   1554  O  OG    . SER A 1 189 ? 134.837 140.619 121.309 1.00 24.99 ?  189 SER A OG    1 
ATOM   1555  N  N     . MET A 1 190 ? 130.583 141.494 121.868 1.00 24.96 ?  190 MET A N     1 
ATOM   1556  C  CA    . MET A 1 190 ? 129.137 141.334 121.983 1.00 25.46 ?  190 MET A CA    1 
ATOM   1557  C  C     . MET A 1 190 ? 128.390 142.358 121.135 1.00 24.52 ?  190 MET A C     1 
ATOM   1558  O  O     . MET A 1 190 ? 127.366 142.033 120.527 1.00 25.65 ?  190 MET A O     1 
ATOM   1559  C  CB    . MET A 1 190 ? 128.699 141.420 123.445 1.00 24.20 ?  190 MET A CB    1 
ATOM   1560  C  CG    . MET A 1 190 ? 128.921 140.132 124.220 1.00 25.61 ?  190 MET A CG    1 
ATOM   1561  S  SD    . MET A 1 190 ? 128.726 140.290 126.004 1.00 39.39 ?  190 MET A SD    1 
ATOM   1562  C  CE    . MET A 1 190 ? 128.875 142.057 126.212 1.00 30.50 ?  190 MET A CE    1 
ATOM   1563  N  N     . GLN A 1 191 ? 128.886 143.596 121.078 1.00 20.97 ?  191 GLN A N     1 
ATOM   1564  C  CA    . GLN A 1 191 ? 128.231 144.616 120.262 1.00 27.46 ?  191 GLN A CA    1 
ATOM   1565  C  C     . GLN A 1 191 ? 128.260 144.253 118.783 1.00 26.57 ?  191 GLN A C     1 
ATOM   1566  O  O     . GLN A 1 191 ? 127.263 144.429 118.074 1.00 30.30 ?  191 GLN A O     1 
ATOM   1567  C  CB    . GLN A 1 191 ? 128.885 145.980 120.486 1.00 28.45 ?  191 GLN A CB    1 
ATOM   1568  C  CG    . GLN A 1 191 ? 128.746 146.525 121.895 1.00 26.96 ?  191 GLN A CG    1 
ATOM   1569  C  CD    . GLN A 1 191 ? 127.320 146.888 122.252 1.00 29.87 ?  191 GLN A CD    1 
ATOM   1570  O  OE1   . GLN A 1 191 ? 126.931 146.837 123.417 1.00 30.00 ?  191 GLN A OE1   1 
ATOM   1571  N  NE2   . GLN A 1 191 ? 126.535 147.271 121.252 1.00 30.62 ?  191 GLN A NE2   1 
ATOM   1572  N  N     . LEU A 1 192 ? 129.398 143.752 118.297 1.00 26.64 ?  192 LEU A N     1 
ATOM   1573  C  CA    . LEU A 1 192 ? 129.521 143.414 116.884 1.00 21.91 ?  192 LEU A CA    1 
ATOM   1574  C  C     . LEU A 1 192 ? 128.804 142.116 116.540 1.00 24.46 ?  192 LEU A C     1 
ATOM   1575  O  O     . LEU A 1 192 ? 128.256 141.993 115.440 1.00 33.12 ?  192 LEU A O     1 
ATOM   1576  C  CB    . LEU A 1 192 ? 130.996 143.326 116.492 1.00 21.31 ?  192 LEU A CB    1 
ATOM   1577  C  CG    . LEU A 1 192 ? 131.786 144.636 116.526 1.00 20.35 ?  192 LEU A CG    1 
ATOM   1578  C  CD1   . LEU A 1 192 ? 133.274 144.370 116.393 1.00 20.92 ?  192 LEU A CD1   1 
ATOM   1579  C  CD2   . LEU A 1 192 ? 131.311 145.586 115.442 1.00 18.19 ?  192 LEU A CD2   1 
ATOM   1580  N  N     . SER A 1 193 ? 128.797 141.142 117.453 1.00 29.05 ?  193 SER A N     1 
ATOM   1581  C  CA    . SER A 1 193 ? 128.011 139.932 117.243 1.00 26.96 ?  193 SER A CA    1 
ATOM   1582  C  C     . SER A 1 193 ? 126.521 140.245 117.248 1.00 30.56 ?  193 SER A C     1 
ATOM   1583  O  O     . SER A 1 193 ? 125.744 139.606 116.531 1.00 34.58 ?  193 SER A O     1 
ATOM   1584  C  CB    . SER A 1 193 ? 128.352 138.899 118.315 1.00 28.66 ?  193 SER A CB    1 
ATOM   1585  O  OG    . SER A 1 193 ? 127.626 137.699 118.118 1.00 37.95 ?  193 SER A OG    1 
ATOM   1586  N  N     . LYS A 1 194 ? 126.107 141.222 118.057 1.00 33.77 ?  194 LYS A N     1 
ATOM   1587  C  CA    . LYS A 1 194 ? 124.719 141.670 118.042 1.00 31.64 ?  194 LYS A CA    1 
ATOM   1588  C  C     . LYS A 1 194 ? 124.346 142.246 116.683 1.00 36.17 ?  194 LYS A C     1 
ATOM   1589  O  O     . LYS A 1 194 ? 123.226 142.044 116.199 1.00 39.77 ?  194 LYS A O     1 
ATOM   1590  C  CB    . LYS A 1 194 ? 124.505 142.697 119.153 1.00 29.29 ?  194 LYS A CB    1 
ATOM   1591  C  CG    . LYS A 1 194 ? 123.278 143.568 118.993 1.00 33.70 ?  194 LYS A CG    1 
ATOM   1592  C  CD    . LYS A 1 194 ? 123.347 144.771 119.916 1.00 36.36 ?  194 LYS A CD    1 
ATOM   1593  C  CE    . LYS A 1 194 ? 121.998 145.457 120.039 1.00 34.10 ?  194 LYS A CE    1 
ATOM   1594  N  NZ    . LYS A 1 194 ? 122.055 146.619 120.967 1.00 34.07 1  194 LYS A NZ    1 
ATOM   1595  N  N     . LEU A 1 195 ? 125.276 142.959 116.046 1.00 34.21 ?  195 LEU A N     1 
ATOM   1596  C  CA    . LEU A 1 195 ? 125.054 143.477 114.703 1.00 31.80 ?  195 LEU A CA    1 
ATOM   1597  C  C     . LEU A 1 195 ? 125.048 142.383 113.645 1.00 34.40 ?  195 LEU A C     1 
ATOM   1598  O  O     . LEU A 1 195 ? 124.701 142.663 112.493 1.00 38.44 ?  195 LEU A O     1 
ATOM   1599  C  CB    . LEU A 1 195 ? 126.122 144.515 114.358 1.00 33.76 ?  195 LEU A CB    1 
ATOM   1600  C  CG    . LEU A 1 195 ? 126.157 145.758 115.244 1.00 34.19 ?  195 LEU A CG    1 
ATOM   1601  C  CD1   . LEU A 1 195 ? 127.383 146.597 114.928 1.00 30.68 ?  195 LEU A CD1   1 
ATOM   1602  C  CD2   . LEU A 1 195 ? 124.884 146.568 115.079 1.00 36.49 ?  195 LEU A CD2   1 
ATOM   1603  N  N     . GLY A 1 196 ? 125.426 141.159 114.001 1.00 31.78 ?  196 GLY A N     1 
ATOM   1604  C  CA    . GLY A 1 196 ? 125.453 140.054 113.070 1.00 30.65 ?  196 GLY A CA    1 
ATOM   1605  C  C     . GLY A 1 196 ? 126.813 139.735 112.494 1.00 35.94 ?  196 GLY A C     1 
ATOM   1606  O  O     . GLY A 1 196 ? 126.926 138.786 111.710 1.00 40.43 ?  196 GLY A O     1 
ATOM   1607  N  N     . GLY A 1 197 ? 127.844 140.489 112.856 1.00 30.13 ?  197 GLY A N     1 
ATOM   1608  C  CA    . GLY A 1 197 ? 129.161 140.282 112.299 1.00 24.75 ?  197 GLY A CA    1 
ATOM   1609  C  C     . GLY A 1 197 ? 129.961 139.213 113.022 1.00 24.86 ?  197 GLY A C     1 
ATOM   1610  O  O     . GLY A 1 197 ? 129.760 138.947 114.203 1.00 30.82 ?  197 GLY A O     1 
ATOM   1611  N  N     . GLY A 1 198 ? 130.880 138.596 112.282 1.00 20.05 ?  198 GLY A N     1 
ATOM   1612  C  CA    . GLY A 1 198 ? 131.839 137.679 112.865 1.00 17.92 ?  198 GLY A CA    1 
ATOM   1613  C  C     . GLY A 1 198 ? 133.051 138.449 113.347 1.00 16.53 ?  198 GLY A C     1 
ATOM   1614  O  O     . GLY A 1 198 ? 133.582 139.301 112.630 1.00 22.13 ?  198 GLY A O     1 
ATOM   1615  N  N     . VAL A 1 199 ? 133.486 138.148 114.566 1.00 20.68 ?  199 VAL A N     1 
ATOM   1616  C  CA    . VAL A 1 199 ? 134.531 138.909 115.238 1.00 16.18 ?  199 VAL A CA    1 
ATOM   1617  C  C     . VAL A 1 199 ? 135.744 138.015 115.434 1.00 11.98 ?  199 VAL A C     1 
ATOM   1618  O  O     . VAL A 1 199 ? 135.624 136.900 115.953 1.00 15.18 ?  199 VAL A O     1 
ATOM   1619  C  CB    . VAL A 1 199 ? 134.045 139.469 116.587 1.00 14.84 ?  199 VAL A CB    1 
ATOM   1620  C  CG1   . VAL A 1 199 ? 135.083 140.402 117.175 1.00 14.75 ?  199 VAL A CG1   1 
ATOM   1621  C  CG2   . VAL A 1 199 ? 132.718 140.180 116.415 1.00 18.84 ?  199 VAL A CG2   1 
ATOM   1622  N  N     . SER A 1 200 ? 136.907 138.505 115.022 1.00 16.69 ?  200 SER A N     1 
ATOM   1623  C  CA    . SER A 1 200 ? 138.177 137.846 115.274 1.00 7.23  ?  200 SER A CA    1 
ATOM   1624  C  C     . SER A 1 200 ? 138.988 138.689 116.246 1.00 12.61 ?  200 SER A C     1 
ATOM   1625  O  O     . SER A 1 200 ? 139.001 139.920 116.154 1.00 19.88 ?  200 SER A O     1 
ATOM   1626  C  CB    . SER A 1 200 ? 138.961 137.639 113.980 1.00 14.12 ?  200 SER A CB    1 
ATOM   1627  O  OG    . SER A 1 200 ? 139.935 136.626 114.133 1.00 19.62 ?  200 SER A OG    1 
ATOM   1628  N  N     . LEU A 1 201 ? 139.659 138.026 117.181 1.00 18.50 ?  201 LEU A N     1 
ATOM   1629  C  CA    . LEU A 1 201 ? 140.433 138.705 118.206 1.00 10.78 ?  201 LEU A CA    1 
ATOM   1630  C  C     . LEU A 1 201 ? 141.853 138.164 118.230 1.00 10.09 ?  201 LEU A C     1 
ATOM   1631  O  O     . LEU A 1 201 ? 142.068 136.952 118.158 1.00 15.23 ?  201 LEU A O     1 
ATOM   1632  C  CB    . LEU A 1 201 ? 139.790 138.543 119.589 1.00 14.87 ?  201 LEU A CB    1 
ATOM   1633  C  CG    . LEU A 1 201 ? 138.373 139.101 119.736 1.00 15.59 ?  201 LEU A CG    1 
ATOM   1634  C  CD1   . LEU A 1 201 ? 137.357 137.974 119.807 1.00 20.18 ?  201 LEU A CD1   1 
ATOM   1635  C  CD2   . LEU A 1 201 ? 138.273 139.995 120.956 1.00 12.72 ?  201 LEU A CD2   1 
ATOM   1636  N  N     . ASN A 1 202 ? 142.818 139.073 118.326 1.00 10.92 ?  202 ASN A N     1 
ATOM   1637  C  CA    . ASN A 1 202 ? 144.214 138.709 118.519 1.00 8.56  ?  202 ASN A CA    1 
ATOM   1638  C  C     . ASN A 1 202 ? 144.490 138.614 120.012 1.00 18.53 ?  202 ASN A C     1 
ATOM   1639  O  O     . ASN A 1 202 ? 144.303 139.589 120.747 1.00 29.15 ?  202 ASN A O     1 
ATOM   1640  C  CB    . ASN A 1 202 ? 145.139 139.732 117.864 1.00 9.92  ?  202 ASN A CB    1 
ATOM   1641  C  CG    . ASN A 1 202 ? 146.544 139.206 117.673 1.00 12.50 ?  202 ASN A CG    1 
ATOM   1642  O  OD1   . ASN A 1 202 ? 146.757 138.002 117.546 1.00 17.38 ?  202 ASN A OD1   1 
ATOM   1643  N  ND2   . ASN A 1 202 ? 147.515 140.109 117.653 1.00 10.64 ?  202 ASN A ND2   1 
ATOM   1644  N  N     . LEU A 1 203 ? 144.936 137.441 120.462 1.00 13.46 ?  203 LEU A N     1 
ATOM   1645  C  CA    . LEU A 1 203 ? 145.217 137.204 121.870 1.00 11.52 ?  203 LEU A CA    1 
ATOM   1646  C  C     . LEU A 1 203 ? 146.711 137.092 122.149 1.00 13.48 ?  203 LEU A C     1 
ATOM   1647  O  O     . LEU A 1 203 ? 147.105 136.628 123.222 1.00 21.45 ?  203 LEU A O     1 
ATOM   1648  C  CB    . LEU A 1 203 ? 144.489 135.946 122.346 1.00 17.29 ?  203 LEU A CB    1 
ATOM   1649  C  CG    . LEU A 1 203 ? 142.965 135.944 122.220 1.00 16.61 ?  203 LEU A CG    1 
ATOM   1650  C  CD1   . LEU A 1 203 ? 142.369 134.839 123.069 1.00 17.98 ?  203 LEU A CD1   1 
ATOM   1651  C  CD2   . LEU A 1 203 ? 142.377 137.291 122.610 1.00 13.98 ?  203 LEU A CD2   1 
ATOM   1652  N  N     . SER A 1 204 ? 147.550 137.518 121.205 1.00 12.80 ?  204 SER A N     1 
ATOM   1653  C  CA    . SER A 1 204 ? 148.991 137.369 121.363 1.00 15.21 ?  204 SER A CA    1 
ATOM   1654  C  C     . SER A 1 204 ? 149.576 138.376 122.344 1.00 20.30 ?  204 SER A C     1 
ATOM   1655  O  O     . SER A 1 204 ? 150.542 138.058 123.045 1.00 27.24 ?  204 SER A O     1 
ATOM   1656  C  CB    . SER A 1 204 ? 149.681 137.497 120.008 1.00 15.24 ?  204 SER A CB    1 
ATOM   1657  O  OG    . SER A 1 204 ? 149.124 136.597 119.069 1.00 22.85 ?  204 SER A OG    1 
ATOM   1658  N  N     . LYS A 1 205 ? 149.021 139.588 122.404 1.00 19.51 ?  205 LYS A N     1 
ATOM   1659  C  CA    . LYS A 1 205 ? 149.528 140.585 123.340 1.00 16.00 ?  205 LYS A CA    1 
ATOM   1660  C  C     . LYS A 1 205 ? 149.198 140.244 124.783 1.00 18.09 ?  205 LYS A C     1 
ATOM   1661  O  O     . LYS A 1 205 ? 149.856 140.758 125.692 1.00 22.70 ?  205 LYS A O     1 
ATOM   1662  C  CB    . LYS A 1 205 ? 148.979 141.968 122.996 1.00 16.09 ?  205 LYS A CB    1 
ATOM   1663  C  CG    . LYS A 1 205 ? 149.541 142.548 121.719 1.00 18.07 ?  205 LYS A CG    1 
ATOM   1664  C  CD    . LYS A 1 205 ? 148.997 143.935 121.455 1.00 23.59 ?  205 LYS A CD    1 
ATOM   1665  C  CE    . LYS A 1 205 ? 149.710 144.585 120.285 1.00 26.62 ?  205 LYS A CE    1 
ATOM   1666  N  NZ    . LYS A 1 205 ? 149.532 143.814 119.027 1.00 19.06 1  205 LYS A NZ    1 
ATOM   1667  N  N     . LEU A 1 206 ? 148.202 139.392 125.012 1.00 17.87 ?  206 LEU A N     1 
ATOM   1668  C  CA    . LEU A 1 206 ? 147.858 138.981 126.364 1.00 12.12 ?  206 LEU A CA    1 
ATOM   1669  C  C     . LEU A 1 206 ? 148.973 138.128 126.952 1.00 17.25 ?  206 LEU A C     1 
ATOM   1670  O  O     . LEU A 1 206 ? 149.502 137.234 126.283 1.00 21.62 ?  206 LEU A O     1 
ATOM   1671  C  CB    . LEU A 1 206 ? 146.546 138.203 126.359 1.00 19.76 ?  206 LEU A CB    1 
ATOM   1672  C  CG    . LEU A 1 206 ? 145.309 138.989 125.930 1.00 20.73 ?  206 LEU A CG    1 
ATOM   1673  C  CD1   . LEU A 1 206 ? 144.086 138.097 125.962 1.00 16.80 ?  206 LEU A CD1   1 
ATOM   1674  C  CD2   . LEU A 1 206 ? 145.118 140.202 126.819 1.00 23.23 ?  206 LEU A CD2   1 
ATOM   1675  N  N     . ARG A 1 207 ? 149.328 138.400 128.203 1.00 24.80 ?  207 ARG A N     1 
ATOM   1676  C  CA    . ARG A 1 207 ? 150.399 137.651 128.842 1.00 22.16 ?  207 ARG A CA    1 
ATOM   1677  C  C     . ARG A 1 207 ? 149.943 136.234 129.167 1.00 27.34 ?  207 ARG A C     1 
ATOM   1678  O  O     . ARG A 1 207 ? 148.755 135.963 129.362 1.00 27.88 ?  207 ARG A O     1 
ATOM   1679  C  CB    . ARG A 1 207 ? 150.880 138.366 130.102 1.00 22.25 ?  207 ARG A CB    1 
ATOM   1680  C  CG    . ARG A 1 207 ? 149.882 138.435 131.234 1.00 23.35 ?  207 ARG A CG    1 
ATOM   1681  C  CD    . ARG A 1 207 ? 150.394 139.356 132.323 1.00 26.39 ?  207 ARG A CD    1 
ATOM   1682  N  NE    . ARG A 1 207 ? 150.387 140.750 131.898 1.00 28.94 ?  207 ARG A NE    1 
ATOM   1683  C  CZ    . ARG A 1 207 ? 150.377 141.786 132.725 1.00 24.31 ?  207 ARG A CZ    1 
ATOM   1684  N  NH1   . ARG A 1 207 ? 150.400 141.623 134.036 1.00 28.75 1  207 ARG A NH1   1 
ATOM   1685  N  NH2   . ARG A 1 207 ? 150.340 143.016 132.222 1.00 20.66 ?  207 ARG A NH2   1 
ATOM   1686  N  N     . ALA A 1 208 ? 150.910 135.325 129.219 1.00 33.04 ?  208 ALA A N     1 
ATOM   1687  C  CA    . ALA A 1 208 ? 150.632 133.904 129.312 1.00 24.77 ?  208 ALA A CA    1 
ATOM   1688  C  C     . ALA A 1 208 ? 150.211 133.514 130.727 1.00 31.73 ?  208 ALA A C     1 
ATOM   1689  O  O     . ALA A 1 208 ? 150.207 134.324 131.657 1.00 36.14 ?  208 ALA A O     1 
ATOM   1690  C  CB    . ALA A 1 208 ? 151.854 133.100 128.878 1.00 25.67 ?  208 ALA A CB    1 
ATOM   1691  N  N     . LYS A 1 209 ? 149.838 132.246 130.877 1.00 32.25 ?  209 LYS A N     1 
ATOM   1692  C  CA    . LYS A 1 209 ? 149.465 131.718 132.180 1.00 29.35 ?  209 LYS A CA    1 
ATOM   1693  C  C     . LYS A 1 209 ? 150.678 131.657 133.098 1.00 33.86 ?  209 LYS A C     1 
ATOM   1694  O  O     . LYS A 1 209 ? 151.766 131.241 132.690 1.00 34.76 ?  209 LYS A O     1 
ATOM   1695  C  CB    . LYS A 1 209 ? 148.847 130.328 132.029 1.00 29.71 ?  209 LYS A CB    1 
ATOM   1696  C  CG    . LYS A 1 209 ? 147.940 129.919 133.173 1.00 32.21 ?  209 LYS A CG    1 
ATOM   1697  C  CD    . LYS A 1 209 ? 147.672 128.424 133.154 1.00 31.43 ?  209 LYS A CD    1 
ATOM   1698  C  CE    . LYS A 1 209 ? 148.936 127.635 132.848 1.00 35.68 ?  209 LYS A CE    1 
ATOM   1699  N  NZ    . LYS A 1 209 ? 148.632 126.237 132.436 1.00 36.68 1  209 LYS A NZ    1 
ATOM   1700  N  N     . GLY A 1 210 ? 150.484 132.074 134.346 1.00 35.89 ?  210 GLY A N     1 
ATOM   1701  C  CA    . GLY A 1 210 ? 151.573 132.092 135.299 1.00 34.31 ?  210 GLY A CA    1 
ATOM   1702  C  C     . GLY A 1 210 ? 152.425 133.336 135.274 1.00 36.82 ?  210 GLY A C     1 
ATOM   1703  O  O     . GLY A 1 210 ? 153.554 133.310 135.773 1.00 38.71 ?  210 GLY A O     1 
ATOM   1704  N  N     . GLU A 1 211 ? 151.928 134.426 134.702 1.00 37.12 ?  211 GLU A N     1 
ATOM   1705  C  CA    . GLU A 1 211 ? 152.627 135.701 134.715 1.00 33.53 ?  211 GLU A CA    1 
ATOM   1706  C  C     . GLU A 1 211 ? 152.089 136.582 135.836 1.00 36.61 ?  211 GLU A C     1 
ATOM   1707  O  O     . GLU A 1 211 ? 150.988 136.374 136.350 1.00 37.11 ?  211 GLU A O     1 
ATOM   1708  C  CB    . GLU A 1 211 ? 152.491 136.412 133.368 1.00 32.02 ?  211 GLU A CB    1 
ATOM   1709  C  CG    . GLU A 1 211 ? 153.049 135.618 132.205 1.00 32.88 ?  211 GLU A CG    1 
ATOM   1710  C  CD    . GLU A 1 211 ? 153.964 136.440 131.326 1.00 37.46 ?  211 GLU A CD    1 
ATOM   1711  O  OE1   . GLU A 1 211 ? 155.073 136.785 131.785 1.00 41.10 ?  211 GLU A OE1   1 
ATOM   1712  O  OE2   . GLU A 1 211 ? 153.586 136.730 130.173 1.00 30.94 -1 211 GLU A OE2   1 
ATOM   1713  N  N     . ALA A 1 212 ? 152.887 137.575 136.210 1.00 34.70 ?  212 ALA A N     1 
ATOM   1714  C  CA    . ALA A 1 212 ? 152.552 138.433 137.336 1.00 31.46 ?  212 ALA A CA    1 
ATOM   1715  C  C     . ALA A 1 212 ? 151.554 139.511 136.933 1.00 36.01 ?  212 ALA A C     1 
ATOM   1716  O  O     . ALA A 1 212 ? 151.593 140.031 135.815 1.00 39.23 ?  212 ALA A O     1 
ATOM   1717  C  CB    . ALA A 1 212 ? 153.813 139.081 137.905 1.00 35.89 ?  212 ALA A CB    1 
ATOM   1718  N  N     . ILE A 1 213 ? 150.656 139.838 137.854 1.00 34.91 ?  213 ILE A N     1 
ATOM   1719  C  CA    . ILE A 1 213 ? 149.753 140.979 137.717 1.00 33.44 ?  213 ILE A CA    1 
ATOM   1720  C  C     . ILE A 1 213 ? 150.098 141.932 138.854 1.00 35.43 ?  213 ILE A C     1 
ATOM   1721  O  O     . ILE A 1 213 ? 149.575 141.808 139.964 1.00 40.52 ?  213 ILE A O     1 
ATOM   1722  C  CB    . ILE A 1 213 ? 148.278 140.578 137.758 1.00 35.77 ?  213 ILE A CB    1 
ATOM   1723  C  CG1   . ILE A 1 213 ? 148.014 139.371 136.861 1.00 37.06 ?  213 ILE A CG1   1 
ATOM   1724  C  CG2   . ILE A 1 213 ? 147.400 141.746 137.347 1.00 32.96 ?  213 ILE A CG2   1 
ATOM   1725  C  CD1   . ILE A 1 213 ? 146.698 138.691 137.149 1.00 30.23 ?  213 ILE A CD1   1 
ATOM   1726  N  N     . LYS A 1 214 ? 150.968 142.905 138.578 1.00 41.20 ?  214 LYS A N     1 
ATOM   1727  C  CA    . LYS A 1 214 ? 151.434 143.869 139.575 1.00 40.66 ?  214 LYS A CA    1 
ATOM   1728  C  C     . LYS A 1 214 ? 152.124 143.154 140.742 1.00 44.42 ?  214 LYS A C     1 
ATOM   1729  O  O     . LYS A 1 214 ? 151.632 143.101 141.869 1.00 46.37 ?  214 LYS A O     1 
ATOM   1730  C  CB    . LYS A 1 214 ? 150.282 144.758 140.063 1.00 39.51 ?  214 LYS A CB    1 
ATOM   1731  C  CG    . LYS A 1 214 ? 150.394 146.207 139.624 1.00 42.74 ?  214 LYS A CG    1 
ATOM   1732  C  CD    . LYS A 1 214 ? 149.216 147.029 140.116 1.00 42.94 ?  214 LYS A CD    1 
ATOM   1733  C  CE    . LYS A 1 214 ? 149.086 148.319 139.324 1.00 45.18 ?  214 LYS A CE    1 
ATOM   1734  N  NZ    . LYS A 1 214 ? 147.701 148.865 139.367 1.00 43.21 1  214 LYS A NZ    1 
ATOM   1735  N  N     . ASP A 1 215 ? 153.262 142.550 140.400 1.00 45.21 ?  215 ASP A N     1 
ATOM   1736  C  CA    . ASP A 1 215 ? 154.265 141.986 141.303 1.00 50.42 ?  215 ASP A CA    1 
ATOM   1737  C  C     . ASP A 1 215 ? 153.750 140.835 142.166 1.00 50.21 ?  215 ASP A C     1 
ATOM   1738  O  O     . ASP A 1 215 ? 154.426 140.443 143.126 1.00 52.51 ?  215 ASP A O     1 
ATOM   1739  C  CB    . ASP A 1 215 ? 154.919 143.070 142.186 1.00 49.52 ?  215 ASP A CB    1 
ATOM   1740  C  CG    . ASP A 1 215 ? 154.016 143.568 143.306 1.00 52.69 ?  215 ASP A CG    1 
ATOM   1741  O  OD1   . ASP A 1 215 ? 153.787 142.830 144.285 1.00 51.32 ?  215 ASP A OD1   1 
ATOM   1742  O  OD2   . ASP A 1 215 ? 153.536 144.717 143.205 1.00 51.14 -1 215 ASP A OD2   1 
ATOM   1743  N  N     . VAL A 1 216 ? 152.594 140.260 141.852 1.00 43.00 ?  216 VAL A N     1 
ATOM   1744  C  CA    . VAL A 1 216 ? 152.182 138.985 142.433 1.00 45.82 ?  216 VAL A CA    1 
ATOM   1745  C  C     . VAL A 1 216 ? 152.236 137.933 141.332 1.00 47.78 ?  216 VAL A C     1 
ATOM   1746  O  O     . VAL A 1 216 ? 151.544 138.046 140.313 1.00 50.41 ?  216 VAL A O     1 
ATOM   1747  C  CB    . VAL A 1 216 ? 150.790 139.067 143.085 1.00 45.53 ?  216 VAL A CB    1 
ATOM   1748  C  CG1   . VAL A 1 216 ? 149.781 139.699 142.161 1.00 44.93 ?  216 VAL A CG1   1 
ATOM   1749  C  CG2   . VAL A 1 216 ? 150.322 137.683 143.501 1.00 45.66 ?  216 VAL A CG2   1 
ATOM   1750  N  N     . GLU A 1 217 ? 153.066 136.917 141.532 1.00 48.05 ?  217 GLU A N     1 
ATOM   1751  C  CA    . GLU A 1 217 ? 153.441 135.993 140.474 1.00 46.87 ?  217 GLU A CA    1 
ATOM   1752  C  C     . GLU A 1 217 ? 152.438 134.852 140.345 1.00 48.29 ?  217 GLU A C     1 
ATOM   1753  O  O     . GLU A 1 217 ? 151.649 134.576 141.252 1.00 49.42 ?  217 GLU A O     1 
ATOM   1754  C  CB    . GLU A 1 217 ? 154.840 135.435 140.735 1.00 48.30 ?  217 GLU A CB    1 
ATOM   1755  C  CG    . GLU A 1 217 ? 155.811 136.468 141.284 1.00 49.23 ?  217 GLU A CG    1 
ATOM   1756  C  CD    . GLU A 1 217 ? 156.656 137.106 140.201 1.00 51.51 ?  217 GLU A CD    1 
ATOM   1757  O  OE1   . GLU A 1 217 ? 157.168 136.369 139.332 1.00 53.39 ?  217 GLU A OE1   1 
ATOM   1758  O  OE2   . GLU A 1 217 ? 156.803 138.346 140.215 1.00 49.38 -1 217 GLU A OE2   1 
ATOM   1759  N  N     . ASN A 1 218 ? 152.488 134.185 139.189 1.00 45.48 ?  218 ASN A N     1 
ATOM   1760  C  CA    . ASN A 1 218 ? 151.599 133.067 138.872 1.00 43.90 ?  218 ASN A CA    1 
ATOM   1761  C  C     . ASN A 1 218 ? 150.137 133.462 139.044 1.00 47.78 ?  218 ASN A C     1 
ATOM   1762  O  O     . ASN A 1 218 ? 149.304 132.681 139.510 1.00 49.11 ?  218 ASN A O     1 
ATOM   1763  C  CB    . ASN A 1 218 ? 151.939 131.838 139.715 1.00 45.70 ?  218 ASN A CB    1 
ATOM   1764  C  CG    . ASN A 1 218 ? 153.138 131.082 139.181 1.00 48.95 ?  218 ASN A CG    1 
ATOM   1765  O  OD1   . ASN A 1 218 ? 153.000 130.198 138.336 1.00 48.93 ?  218 ASN A OD1   1 
ATOM   1766  N  ND2   . ASN A 1 218 ? 154.323 131.431 139.667 1.00 46.74 ?  218 ASN A ND2   1 
ATOM   1767  N  N     . ALA A 1 219 ? 149.821 134.696 138.660 1.00 40.88 ?  219 ALA A N     1 
ATOM   1768  C  CA    . ALA A 1 219 ? 148.498 135.261 138.877 1.00 38.59 ?  219 ALA A CA    1 
ATOM   1769  C  C     . ALA A 1 219 ? 147.631 135.273 137.628 1.00 40.39 ?  219 ALA A C     1 
ATOM   1770  O  O     . ALA A 1 219 ? 146.405 135.179 137.740 1.00 41.10 ?  219 ALA A O     1 
ATOM   1771  C  CB    . ALA A 1 219 ? 148.625 136.689 139.415 1.00 37.28 ?  219 ALA A CB    1 
ATOM   1772  N  N     . THR A 1 220 ? 148.234 135.380 136.449 1.00 37.47 ?  220 THR A N     1 
ATOM   1773  C  CA    . THR A 1 220 ? 147.472 135.486 135.215 1.00 34.68 ?  220 THR A CA    1 
ATOM   1774  C  C     . THR A 1 220 ? 146.957 134.114 134.796 1.00 35.72 ?  220 THR A C     1 
ATOM   1775  O  O     . THR A 1 220 ? 147.679 133.116 134.865 1.00 37.02 ?  220 THR A O     1 
ATOM   1776  C  CB    . THR A 1 220 ? 148.342 136.094 134.113 1.00 33.58 ?  220 THR A CB    1 
ATOM   1777  O  OG1   . THR A 1 220 ? 148.555 137.483 134.386 1.00 36.06 ?  220 THR A OG1   1 
ATOM   1778  C  CG2   . THR A 1 220 ? 147.663 135.980 132.766 1.00 35.48 ?  220 THR A CG2   1 
ATOM   1779  N  N     . LYS A 1 221 ? 145.696 134.069 134.368 1.00 37.24 ?  221 LYS A N     1 
ATOM   1780  C  CA    . LYS A 1 221 ? 145.075 132.829 133.921 1.00 32.88 ?  221 LYS A CA    1 
ATOM   1781  C  C     . LYS A 1 221 ? 145.424 132.475 132.483 1.00 38.04 ?  221 LYS A C     1 
ATOM   1782  O  O     . LYS A 1 221 ? 145.001 131.418 132.002 1.00 43.49 ?  221 LYS A O     1 
ATOM   1783  C  CB    . LYS A 1 221 ? 143.555 132.914 134.066 1.00 33.02 ?  221 LYS A CB    1 
ATOM   1784  C  CG    . LYS A 1 221 ? 143.084 133.540 135.360 1.00 37.07 ?  221 LYS A CG    1 
ATOM   1785  C  CD    . LYS A 1 221 ? 141.597 133.320 135.557 1.00 36.66 ?  221 LYS A CD    1 
ATOM   1786  C  CE    . LYS A 1 221 ? 141.301 131.923 136.069 1.00 35.69 ?  221 LYS A CE    1 
ATOM   1787  N  NZ    . LYS A 1 221 ? 142.129 131.582 137.255 1.00 37.36 1  221 LYS A NZ    1 
ATOM   1788  N  N     . GLY A 1 222 ? 146.172 133.324 131.792 1.00 32.91 ?  222 GLY A N     1 
ATOM   1789  C  CA    . GLY A 1 222 ? 146.552 133.059 130.426 1.00 30.90 ?  222 GLY A CA    1 
ATOM   1790  C  C     . GLY A 1 222 ? 145.484 133.469 129.433 1.00 30.75 ?  222 GLY A C     1 
ATOM   1791  O  O     . GLY A 1 222 ? 144.475 134.096 129.766 1.00 31.07 ?  222 GLY A O     1 
ATOM   1792  N  N     . VAL A 1 223 ? 145.723 133.096 128.175 1.00 31.96 ?  223 VAL A N     1 
ATOM   1793  C  CA    . VAL A 1 223 ? 144.775 133.430 127.119 1.00 26.30 ?  223 VAL A CA    1 
ATOM   1794  C  C     . VAL A 1 223 ? 143.548 132.533 127.143 1.00 22.89 ?  223 VAL A C     1 
ATOM   1795  O  O     . VAL A 1 223 ? 142.540 132.871 126.517 1.00 31.06 ?  223 VAL A O     1 
ATOM   1796  C  CB    . VAL A 1 223 ? 145.437 133.362 125.731 1.00 25.90 ?  223 VAL A CB    1 
ATOM   1797  C  CG1   . VAL A 1 223 ? 146.744 134.133 125.726 1.00 25.11 ?  223 VAL A CG1   1 
ATOM   1798  C  CG2   . VAL A 1 223 ? 145.656 131.920 125.305 1.00 26.84 ?  223 VAL A CG2   1 
ATOM   1799  N  N     . VAL A 1 224 ? 143.598 131.400 127.845 1.00 25.50 ?  224 VAL A N     1 
ATOM   1800  C  CA    . VAL A 1 224 ? 142.455 130.493 127.865 1.00 25.72 ?  224 VAL A CA    1 
ATOM   1801  C  C     . VAL A 1 224 ? 141.313 131.050 128.712 1.00 27.40 ?  224 VAL A C     1 
ATOM   1802  O  O     . VAL A 1 224 ? 140.139 130.821 128.401 1.00 30.19 ?  224 VAL A O     1 
ATOM   1803  C  CB    . VAL A 1 224 ? 142.896 129.100 128.344 1.00 32.71 ?  224 VAL A CB    1 
ATOM   1804  C  CG1   . VAL A 1 224 ? 141.716 128.145 128.386 1.00 31.81 ?  224 VAL A CG1   1 
ATOM   1805  C  CG2   . VAL A 1 224 ? 143.978 128.557 127.429 1.00 29.46 ?  224 VAL A CG2   1 
ATOM   1806  N  N     . GLY A 1 225 ? 141.617 131.790 129.779 1.00 24.18 ?  225 GLY A N     1 
ATOM   1807  C  CA    . GLY A 1 225 ? 140.559 132.445 130.530 1.00 21.73 ?  225 GLY A CA    1 
ATOM   1808  C  C     . GLY A 1 225 ? 139.840 133.503 129.715 1.00 22.30 ?  225 GLY A C     1 
ATOM   1809  O  O     . GLY A 1 225 ? 138.607 133.588 129.732 1.00 31.46 ?  225 GLY A O     1 
ATOM   1810  N  N     . VAL A 1 226 ? 140.601 134.316 128.980 1.00 19.34 ?  226 VAL A N     1 
ATOM   1811  C  CA    . VAL A 1 226 ? 140.000 135.275 128.061 1.00 20.35 ?  226 VAL A CA    1 
ATOM   1812  C  C     . VAL A 1 226 ? 139.239 134.552 126.964 1.00 24.85 ?  226 VAL A C     1 
ATOM   1813  O  O     . VAL A 1 226 ? 138.214 135.040 126.481 1.00 26.82 ?  226 VAL A O     1 
ATOM   1814  C  CB    . VAL A 1 226 ? 141.083 136.205 127.483 1.00 18.19 ?  226 VAL A CB    1 
ATOM   1815  C  CG1   . VAL A 1 226 ? 140.451 137.323 126.668 1.00 25.76 ?  226 VAL A CG1   1 
ATOM   1816  C  CG2   . VAL A 1 226 ? 141.939 136.765 128.599 1.00 20.82 ?  226 VAL A CG2   1 
ATOM   1817  N  N     . MET A 1 227 ? 139.728 133.383 126.550 1.00 28.39 ?  227 MET A N     1 
ATOM   1818  C  CA    . MET A 1 227 ? 139.031 132.585 125.550 1.00 22.22 ?  227 MET A CA    1 
ATOM   1819  C  C     . MET A 1 227 ? 137.671 132.131 126.058 1.00 22.95 ?  227 MET A C     1 
ATOM   1820  O  O     . MET A 1 227 ? 136.684 132.165 125.322 1.00 29.97 ?  227 MET A O     1 
ATOM   1821  C  CB    . MET A 1 227 ? 139.892 131.383 125.167 1.00 19.68 ?  227 MET A CB    1 
ATOM   1822  C  CG    . MET A 1 227 ? 140.933 131.676 124.109 1.00 17.85 ?  227 MET A CG    1 
ATOM   1823  S  SD    . MET A 1 227 ? 141.654 130.175 123.432 1.00 33.28 ?  227 MET A SD    1 
ATOM   1824  C  CE    . MET A 1 227 ? 140.356 129.659 122.326 1.00 29.81 ?  227 MET A CE    1 
ATOM   1825  N  N     . LYS A 1 228 ? 137.605 131.692 127.317 1.00 26.79 ?  228 LYS A N     1 
ATOM   1826  C  CA    . LYS A 1 228 ? 136.324 131.309 127.907 1.00 23.10 ?  228 LYS A CA    1 
ATOM   1827  C  C     . LYS A 1 228 ? 135.393 132.508 128.031 1.00 24.38 ?  228 LYS A C     1 
ATOM   1828  O  O     . LYS A 1 228 ? 134.189 132.404 127.753 1.00 26.05 ?  228 LYS A O     1 
ATOM   1829  C  CB    . LYS A 1 228 ? 136.545 130.663 129.274 1.00 23.32 ?  228 LYS A CB    1 
ATOM   1830  C  CG    . LYS A 1 228 ? 137.371 129.393 129.235 1.00 29.04 ?  228 LYS A CG    1 
ATOM   1831  C  CD    . LYS A 1 228 ? 137.479 128.765 130.612 1.00 36.78 ?  228 LYS A CD    1 
ATOM   1832  C  CE    . LYS A 1 228 ? 138.599 129.393 131.425 1.00 36.15 ?  228 LYS A CE    1 
ATOM   1833  N  NZ    . LYS A 1 228 ? 139.792 128.507 131.507 1.00 30.76 1  228 LYS A NZ    1 
ATOM   1834  N  N     . LEU A 1 229 ? 135.935 133.655 128.450 1.00 24.46 ?  229 LEU A N     1 
ATOM   1835  C  CA    . LEU A 1 229 ? 135.138 134.876 128.513 1.00 21.84 ?  229 LEU A CA    1 
ATOM   1836  C  C     . LEU A 1 229 ? 134.546 135.214 127.150 1.00 21.51 ?  229 LEU A C     1 
ATOM   1837  O  O     . LEU A 1 229 ? 133.354 135.513 127.033 1.00 22.24 ?  229 LEU A O     1 
ATOM   1838  C  CB    . LEU A 1 229 ? 135.993 136.036 129.017 1.00 24.43 ?  229 LEU A CB    1 
ATOM   1839  C  CG    . LEU A 1 229 ? 136.392 136.096 130.489 1.00 23.02 ?  229 LEU A CG    1 
ATOM   1840  C  CD1   . LEU A 1 229 ? 137.499 137.114 130.654 1.00 24.40 ?  229 LEU A CD1   1 
ATOM   1841  C  CD2   . LEU A 1 229 ? 135.203 136.452 131.358 1.00 18.49 ?  229 LEU A CD2   1 
ATOM   1842  N  N     . LEU A 1 230 ? 135.374 135.167 126.106 1.00 26.92 ?  230 LEU A N     1 
ATOM   1843  C  CA    . LEU A 1 230 ? 134.914 135.494 124.760 1.00 18.66 ?  230 LEU A CA    1 
ATOM   1844  C  C     . LEU A 1 230 ? 133.920 134.462 124.249 1.00 17.88 ?  230 LEU A C     1 
ATOM   1845  O  O     . LEU A 1 230 ? 132.960 134.810 123.554 1.00 29.69 ?  230 LEU A O     1 
ATOM   1846  C  CB    . LEU A 1 230 ? 136.106 135.603 123.813 1.00 20.57 ?  230 LEU A CB    1 
ATOM   1847  C  CG    . LEU A 1 230 ? 136.972 136.850 123.975 1.00 27.78 ?  230 LEU A CG    1 
ATOM   1848  C  CD1   . LEU A 1 230 ? 138.310 136.663 123.280 1.00 28.12 ?  230 LEU A CD1   1 
ATOM   1849  C  CD2   . LEU A 1 230 ? 136.246 138.074 123.443 1.00 21.05 ?  230 LEU A CD2   1 
ATOM   1850  N  N     . ASP A 1 231 ? 134.136 133.188 124.572 1.00 20.37 ?  231 ASP A N     1 
ATOM   1851  C  CA    . ASP A 1 231 ? 133.211 132.147 124.146 1.00 24.19 ?  231 ASP A CA    1 
ATOM   1852  C  C     . ASP A 1 231 ? 131.832 132.360 124.752 1.00 28.73 ?  231 ASP A C     1 
ATOM   1853  O  O     . ASP A 1 231 ? 130.815 132.244 124.058 1.00 33.36 ?  231 ASP A O     1 
ATOM   1854  C  CB    . ASP A 1 231 ? 133.767 130.775 124.522 1.00 27.44 ?  231 ASP A CB    1 
ATOM   1855  C  CG    . ASP A 1 231 ? 132.854 129.642 124.110 1.00 35.91 ?  231 ASP A CG    1 
ATOM   1856  O  OD1   . ASP A 1 231 ? 132.700 129.414 122.893 1.00 39.62 ?  231 ASP A OD1   1 
ATOM   1857  O  OD2   . ASP A 1 231 ? 132.292 128.975 125.003 1.00 38.47 -1 231 ASP A OD2   1 
ATOM   1858  N  N     . ASN A 1 232 ? 131.773 132.700 126.041 1.00 29.49 ?  232 ASN A N     1 
ATOM   1859  C  CA    . ASN A 1 232 ? 130.474 132.982 126.645 1.00 27.94 ?  232 ASN A CA    1 
ATOM   1860  C  C     . ASN A 1 232 ? 129.884 134.294 126.147 1.00 28.52 ?  232 ASN A C     1 
ATOM   1861  O  O     . ASN A 1 232 ? 128.658 134.416 126.043 1.00 33.99 ?  232 ASN A O     1 
ATOM   1862  C  CB    . ASN A 1 232 ? 130.579 132.985 128.165 1.00 29.32 ?  232 ASN A CB    1 
ATOM   1863  C  CG    . ASN A 1 232 ? 130.489 131.597 128.743 1.00 36.30 ?  232 ASN A CG    1 
ATOM   1864  O  OD1   . ASN A 1 232 ? 131.406 130.790 128.600 1.00 38.87 ?  232 ASN A OD1   1 
ATOM   1865  N  ND2   . ASN A 1 232 ? 129.372 131.302 129.398 1.00 33.39 ?  232 ASN A ND2   1 
ATOM   1866  N  N     . ALA A 1 233 ? 130.725 135.279 125.830 1.00 25.87 ?  233 ALA A N     1 
ATOM   1867  C  CA    . ALA A 1 233 ? 130.220 136.521 125.259 1.00 17.88 ?  233 ALA A CA    1 
ATOM   1868  C  C     . ALA A 1 233 ? 129.585 136.280 123.896 1.00 30.07 ?  233 ALA A C     1 
ATOM   1869  O  O     . ALA A 1 233 ? 128.569 136.896 123.556 1.00 36.37 ?  233 ALA A O     1 
ATOM   1870  C  CB    . ALA A 1 233 ? 131.347 137.547 125.156 1.00 23.66 ?  233 ALA A CB    1 
ATOM   1871  N  N     . PHE A 1 234 ? 130.176 135.390 123.098 1.00 32.09 ?  234 PHE A N     1 
ATOM   1872  C  CA    . PHE A 1 234 ? 129.617 135.066 121.792 1.00 25.48 ?  234 PHE A CA    1 
ATOM   1873  C  C     . PHE A 1 234 ? 128.400 134.160 121.902 1.00 23.30 ?  234 PHE A C     1 
ATOM   1874  O  O     . PHE A 1 234 ? 127.491 134.250 121.070 1.00 29.86 ?  234 PHE A O     1 
ATOM   1875  C  CB    . PHE A 1 234 ? 130.689 134.426 120.911 1.00 24.96 ?  234 PHE A CB    1 
ATOM   1876  C  CG    . PHE A 1 234 ? 131.664 135.412 120.339 1.00 24.03 ?  234 PHE A CG    1 
ATOM   1877  C  CD1   . PHE A 1 234 ? 131.225 136.467 119.560 1.00 27.38 ?  234 PHE A CD1   1 
ATOM   1878  C  CD2   . PHE A 1 234 ? 133.018 135.296 120.592 1.00 23.01 ?  234 PHE A CD2   1 
ATOM   1879  C  CE1   . PHE A 1 234 ? 132.118 137.380 119.041 1.00 26.14 ?  234 PHE A CE1   1 
ATOM   1880  C  CE2   . PHE A 1 234 ? 133.915 136.207 120.079 1.00 24.47 ?  234 PHE A CE2   1 
ATOM   1881  C  CZ    . PHE A 1 234 ? 133.465 137.249 119.301 1.00 26.41 ?  234 PHE A CZ    1 
ATOM   1882  N  N     . ARG A 1 235 ? 128.360 133.283 122.906 1.00 31.26 ?  235 ARG A N     1 
ATOM   1883  C  CA    . ARG A 1 235 ? 127.141 132.523 123.160 1.00 26.90 ?  235 ARG A CA    1 
ATOM   1884  C  C     . ARG A 1 235 ? 125.995 133.426 123.588 1.00 32.93 ?  235 ARG A C     1 
ATOM   1885  O  O     . ARG A 1 235 ? 124.842 133.176 123.220 1.00 39.75 ?  235 ARG A O     1 
ATOM   1886  C  CB    . ARG A 1 235 ? 127.386 131.449 124.216 1.00 23.83 ?  235 ARG A CB    1 
ATOM   1887  C  CG    . ARG A 1 235 ? 127.332 130.039 123.669 1.00 35.16 ?  235 ARG A CG    1 
ATOM   1888  C  CD    . ARG A 1 235 ? 127.066 129.016 124.767 1.00 37.47 ?  235 ARG A CD    1 
ATOM   1889  N  NE    . ARG A 1 235 ? 127.980 129.116 125.902 1.00 36.06 ?  235 ARG A NE    1 
ATOM   1890  C  CZ    . ARG A 1 235 ? 129.297 128.984 125.831 1.00 36.85 ?  235 ARG A CZ    1 
ATOM   1891  N  NH1   . ARG A 1 235 ? 129.907 128.694 124.693 1.00 35.35 1  235 ARG A NH1   1 
ATOM   1892  N  NH2   . ARG A 1 235 ? 130.024 129.126 126.936 1.00 33.99 ?  235 ARG A NH2   1 
ATOM   1893  N  N     . TYR A 1 236 ? 126.283 134.468 124.369 1.00 29.33 ?  236 TYR A N     1 
ATOM   1894  C  CA    . TYR A 1 236 ? 125.225 135.370 124.807 1.00 27.39 ?  236 TYR A CA    1 
ATOM   1895  C  C     . TYR A 1 236 ? 124.672 136.181 123.641 1.00 26.88 ?  236 TYR A C     1 
ATOM   1896  O  O     . TYR A 1 236 ? 123.454 136.277 123.460 1.00 32.69 ?  236 TYR A O     1 
ATOM   1897  C  CB    . TYR A 1 236 ? 125.744 136.298 125.904 1.00 28.09 ?  236 TYR A CB    1 
ATOM   1898  C  CG    . TYR A 1 236 ? 124.675 137.199 126.466 1.00 29.84 ?  236 TYR A CG    1 
ATOM   1899  C  CD1   . TYR A 1 236 ? 123.686 136.690 127.294 1.00 26.03 ?  236 TYR A CD1   1 
ATOM   1900  C  CD2   . TYR A 1 236 ? 124.643 138.551 126.158 1.00 29.81 ?  236 TYR A CD2   1 
ATOM   1901  C  CE1   . TYR A 1 236 ? 122.705 137.500 127.806 1.00 30.09 ?  236 TYR A CE1   1 
ATOM   1902  C  CE2   . TYR A 1 236 ? 123.662 139.371 126.669 1.00 23.27 ?  236 TYR A CE2   1 
ATOM   1903  C  CZ    . TYR A 1 236 ? 122.696 138.837 127.494 1.00 24.22 ?  236 TYR A CZ    1 
ATOM   1904  O  OH    . TYR A 1 236 ? 121.711 139.639 128.012 1.00 29.49 ?  236 TYR A OH    1 
ATOM   1905  N  N     . ALA A 1 237 ? 125.555 136.775 122.838 1.00 30.76 ?  237 ALA A N     1 
ATOM   1906  C  CA    . ALA A 1 237 ? 125.140 137.585 121.694 1.00 33.92 ?  237 ALA A CA    1 
ATOM   1907  C  C     . ALA A 1 237 ? 125.030 136.672 120.477 1.00 38.01 ?  237 ALA A C     1 
ATOM   1908  O  O     . ALA A 1 237 ? 125.961 136.512 119.686 1.00 37.56 ?  237 ALA A O     1 
ATOM   1909  C  CB    . ALA A 1 237 ? 126.114 138.732 121.464 1.00 31.93 ?  237 ALA A CB    1 
ATOM   1910  N  N     . ASP A 1 238 ? 123.858 136.058 120.336 1.00 54.09 ?  238 ASP A N     1 
ATOM   1911  C  CA    . ASP A 1 238 ? 123.619 135.065 119.299 1.00 57.14 ?  238 ASP A CA    1 
ATOM   1912  C  C     . ASP A 1 238 ? 122.488 135.437 118.350 1.00 59.65 ?  238 ASP A C     1 
ATOM   1913  O  O     . ASP A 1 238 ? 122.206 134.668 117.424 1.00 62.01 ?  238 ASP A O     1 
ATOM   1914  C  CB    . ASP A 1 238 ? 123.326 133.704 119.937 1.00 56.12 ?  238 ASP A CB    1 
ATOM   1915  C  CG    . ASP A 1 238 ? 122.106 133.733 120.835 1.00 59.17 ?  238 ASP A CG    1 
ATOM   1916  O  OD1   . ASP A 1 238 ? 121.712 134.834 121.271 1.00 58.79 ?  238 ASP A OD1   1 
ATOM   1917  O  OD2   . ASP A 1 238 ? 121.540 132.652 121.103 1.00 61.73 -1 238 ASP A OD2   1 
ATOM   1918  N  N     . GLN A 1 239 ? 121.832 136.582 118.552 1.00 61.84 ?  239 GLN A N     1 
ATOM   1919  C  CA    . GLN A 1 239 ? 120.786 137.080 117.657 1.00 63.57 ?  239 GLN A CA    1 
ATOM   1920  C  C     . GLN A 1 239 ? 119.669 136.043 117.494 1.00 64.40 ?  239 GLN A C     1 
ATOM   1921  O  O     . GLN A 1 239 ? 119.481 135.452 116.428 1.00 64.50 ?  239 GLN A O     1 
ATOM   1922  C  CB    . GLN A 1 239 ? 121.366 137.462 116.289 1.00 62.58 ?  239 GLN A CB    1 
ATOM   1923  C  CG    . GLN A 1 239 ? 122.732 138.117 116.333 1.00 60.47 ?  239 GLN A CG    1 
ATOM   1924  C  CD    . GLN A 1 239 ? 123.476 137.950 115.025 1.00 63.61 ?  239 GLN A CD    1 
ATOM   1925  O  OE1   . GLN A 1 239 ? 124.648 137.575 115.005 1.00 63.04 ?  239 GLN A OE1   1 
ATOM   1926  N  NE2   . GLN A 1 239 ? 122.794 138.226 113.920 1.00 62.96 ?  239 GLN A NE2   1 
ATOM   1927  N  N     . MET A 1 240 ? 118.969 135.803 118.610 1.00 72.88 ?  240 MET A N     1 
ATOM   1928  C  CA    . MET A 1 240 ? 117.874 134.837 118.693 1.00 74.86 ?  240 MET A CA    1 
ATOM   1929  C  C     . MET A 1 240 ? 118.375 133.397 118.648 1.00 74.66 ?  240 MET A C     1 
ATOM   1930  O  O     . MET A 1 240 ? 117.603 132.458 118.865 1.00 76.79 ?  240 MET A O     1 
ATOM   1931  C  CB    . MET A 1 240 ? 116.852 135.058 117.568 1.00 75.37 ?  240 MET A CB    1 
ATOM   1932  C  CG    . MET A 1 240 ? 115.495 134.414 117.799 1.00 74.25 ?  240 MET A CG    1 
ATOM   1933  S  SD    . MET A 1 240 ? 114.084 135.481 117.493 1.00 82.10 ?  240 MET A SD    1 
ATOM   1934  C  CE    . MET A 1 240 ? 112.756 134.288 117.655 1.00 74.95 ?  240 MET A CE    1 
ATOM   1935  N  N     . GLY A 1 241 ? 119.665 133.208 118.392 1.00 73.27 ?  241 GLY A N     1 
ATOM   1936  C  CA    . GLY A 1 241 ? 120.189 131.886 118.146 1.00 72.70 ?  241 GLY A CA    1 
ATOM   1937  C  C     . GLY A 1 241 ? 119.978 131.380 116.736 1.00 75.66 ?  241 GLY A C     1 
ATOM   1938  O  O     . GLY A 1 241 ? 120.416 130.265 116.425 1.00 74.83 ?  241 GLY A O     1 
ATOM   1939  N  N     . GLN A 1 242 ? 119.313 132.160 115.878 1.00 79.13 ?  242 GLN A N     1 
ATOM   1940  C  CA    . GLN A 1 242 ? 119.161 131.773 114.479 1.00 78.63 ?  242 GLN A CA    1 
ATOM   1941  C  C     . GLN A 1 242 ? 120.523 131.604 113.821 1.00 80.35 ?  242 GLN A C     1 
ATOM   1942  O  O     . GLN A 1 242 ? 120.780 130.608 113.134 1.00 79.65 ?  242 GLN A O     1 
ATOM   1943  C  CB    . GLN A 1 242 ? 118.333 132.822 113.735 1.00 77.99 ?  242 GLN A CB    1 
ATOM   1944  C  CG    . GLN A 1 242 ? 116.831 132.699 113.925 1.00 79.49 ?  242 GLN A CG    1 
ATOM   1945  C  CD    . GLN A 1 242 ? 116.050 133.531 112.925 1.00 79.66 ?  242 GLN A CD    1 
ATOM   1946  O  OE1   . GLN A 1 242 ? 116.631 134.185 112.059 1.00 78.67 ?  242 GLN A OE1   1 
ATOM   1947  N  NE2   . GLN A 1 242 ? 114.728 133.512 113.043 1.00 79.18 ?  242 GLN A NE2   1 
ATOM   1948  N  N     . ARG A 1 243 ? 121.411 132.574 114.027 1.00 67.57 ?  243 ARG A N     1 
ATOM   1949  C  CA    . ARG A 1 243 ? 122.824 132.452 113.691 1.00 64.53 ?  243 ARG A CA    1 
ATOM   1950  C  C     . ARG A 1 243 ? 123.603 132.806 114.948 1.00 65.13 ?  243 ARG A C     1 
ATOM   1951  O  O     . ARG A 1 243 ? 123.793 133.989 115.250 1.00 64.19 ?  243 ARG A O     1 
ATOM   1952  C  CB    . ARG A 1 243 ? 123.209 133.369 112.529 1.00 63.99 ?  243 ARG A CB    1 
ATOM   1953  C  CG    . ARG A 1 243 ? 124.624 133.150 112.021 1.00 65.11 ?  243 ARG A CG    1 
ATOM   1954  C  CD    . ARG A 1 243 ? 125.374 134.465 111.885 1.00 63.87 ?  243 ARG A CD    1 
ATOM   1955  N  NE    . ARG A 1 243 ? 125.689 135.042 113.187 1.00 65.64 ?  243 ARG A NE    1 
ATOM   1956  C  CZ    . ARG A 1 243 ? 126.741 135.811 113.432 1.00 62.31 ?  243 ARG A CZ    1 
ATOM   1957  N  NH1   . ARG A 1 243 ? 127.613 136.112 112.484 1.00 61.32 1  243 ARG A NH1   1 
ATOM   1958  N  NH2   . ARG A 1 243 ? 126.924 136.288 114.660 1.00 59.64 ?  243 ARG A NH2   1 
ATOM   1959  N  N     . GLN A 1 244 ? 124.045 131.785 115.681 1.00 62.49 ?  244 GLN A N     1 
ATOM   1960  C  CA    . GLN A 1 244 ? 124.708 132.010 116.957 1.00 60.92 ?  244 GLN A CA    1 
ATOM   1961  C  C     . GLN A 1 244 ? 125.986 132.816 116.763 1.00 61.50 ?  244 GLN A C     1 
ATOM   1962  O  O     . GLN A 1 244 ? 126.586 132.826 115.684 1.00 59.07 ?  244 GLN A O     1 
ATOM   1963  C  CB    . GLN A 1 244 ? 125.021 130.677 117.640 1.00 59.61 ?  244 GLN A CB    1 
ATOM   1964  C  CG    . GLN A 1 244 ? 126.292 129.998 117.155 1.00 61.35 ?  244 GLN A CG    1 
ATOM   1965  C  CD    . GLN A 1 244 ? 126.180 129.493 115.731 1.00 63.43 ?  244 GLN A CD    1 
ATOM   1966  O  OE1   . GLN A 1 244 ? 125.084 129.228 115.238 1.00 62.60 ?  244 GLN A OE1   1 
ATOM   1967  N  NE2   . GLN A 1 244 ? 127.318 129.356 115.060 1.00 60.79 ?  244 GLN A NE2   1 
ATOM   1968  N  N     . GLY A 1 245 ? 126.388 133.517 117.822 1.00 51.77 ?  245 GLY A N     1 
ATOM   1969  C  CA    . GLY A 1 245 ? 127.566 134.359 117.768 1.00 44.75 ?  245 GLY A CA    1 
ATOM   1970  C  C     . GLY A 1 245 ? 128.815 133.590 117.402 1.00 44.79 ?  245 GLY A C     1 
ATOM   1971  O  O     . GLY A 1 245 ? 129.159 132.598 118.050 1.00 45.23 ?  245 GLY A O     1 
ATOM   1972  N  N     . SER A 1 246 ? 129.499 134.039 116.355 1.00 39.42 ?  246 SER A N     1 
ATOM   1973  C  CA    . SER A 1 246 ? 130.688 133.374 115.846 1.00 34.17 ?  246 SER A CA    1 
ATOM   1974  C  C     . SER A 1 246 ? 131.904 134.245 116.117 1.00 31.18 ?  246 SER A C     1 
ATOM   1975  O  O     . SER A 1 246 ? 131.947 135.409 115.705 1.00 27.05 ?  246 SER A O     1 
ATOM   1976  C  CB    . SER A 1 246 ? 130.560 133.092 114.349 1.00 31.85 ?  246 SER A CB    1 
ATOM   1977  O  OG    . SER A 1 246 ? 129.588 132.093 114.101 1.00 41.80 ?  246 SER A OG    1 
ATOM   1978  N  N     . GLY A 1 247 ? 132.888 133.677 116.809 1.00 24.77 ?  247 GLY A N     1 
ATOM   1979  C  CA    . GLY A 1 247 ? 134.112 134.383 117.098 1.00 11.06 ?  247 GLY A CA    1 
ATOM   1980  C  C     . GLY A 1 247 ? 135.317 133.546 116.723 1.00 15.76 ?  247 GLY A C     1 
ATOM   1981  O  O     . GLY A 1 247 ? 135.247 132.323 116.613 1.00 22.75 ?  247 GLY A O     1 
ATOM   1982  N  N     . ALA A 1 248 ? 136.430 134.237 116.514 1.00 19.37 ?  248 ALA A N     1 
ATOM   1983  C  CA    . ALA A 1 248 ? 137.709 133.603 116.251 1.00 16.42 ?  248 ALA A CA    1 
ATOM   1984  C  C     . ALA A 1 248 ? 138.761 134.221 117.154 1.00 12.25 ?  248 ALA A C     1 
ATOM   1985  O  O     . ALA A 1 248 ? 138.757 135.431 117.388 1.00 20.81 ?  248 ALA A O     1 
ATOM   1986  C  CB    . ALA A 1 248 ? 138.124 133.745 114.783 1.00 9.18  ?  248 ALA A CB    1 
ATOM   1987  N  N     . ALA A 1 249 ? 139.652 133.384 117.669 1.00 17.17 ?  249 ALA A N     1 
ATOM   1988  C  CA    . ALA A 1 249 ? 140.787 133.831 118.457 1.00 11.41 ?  249 ALA A CA    1 
ATOM   1989  C  C     . ALA A 1 249 ? 142.066 133.443 117.735 1.00 10.22 ?  249 ALA A C     1 
ATOM   1990  O  O     . ALA A 1 249 ? 142.169 132.346 117.185 1.00 19.58 ?  249 ALA A O     1 
ATOM   1991  C  CB    . ALA A 1 249 ? 140.767 133.228 119.863 1.00 13.14 ?  249 ALA A CB    1 
ATOM   1992  N  N     . TYR A 1 250 ? 143.033 134.350 117.727 1.00 11.19 ?  250 TYR A N     1 
ATOM   1993  C  CA    . TYR A 1 250 ? 144.309 134.105 117.079 1.00 7.84  ?  250 TYR A CA    1 
ATOM   1994  C  C     . TYR A 1 250 ? 145.431 134.239 118.092 1.00 8.84  ?  250 TYR A C     1 
ATOM   1995  O  O     . TYR A 1 250 ? 145.430 135.155 118.920 1.00 13.20 ?  250 TYR A O     1 
ATOM   1996  C  CB    . TYR A 1 250 ? 144.535 135.066 115.911 1.00 10.59 ?  250 TYR A CB    1 
ATOM   1997  C  CG    . TYR A 1 250 ? 143.901 134.608 114.620 1.00 19.08 ?  250 TYR A CG    1 
ATOM   1998  C  CD1   . TYR A 1 250 ? 142.541 134.764 114.398 1.00 8.70  ?  250 TYR A CD1   1 
ATOM   1999  C  CD2   . TYR A 1 250 ? 144.660 134.003 113.626 1.00 12.91 ?  250 TYR A CD2   1 
ATOM   2000  C  CE1   . TYR A 1 250 ? 141.958 134.343 113.225 1.00 0.00  ?  250 TYR A CE1   1 
ATOM   2001  C  CE2   . TYR A 1 250 ? 144.083 133.579 112.448 1.00 7.59  ?  250 TYR A CE2   1 
ATOM   2002  C  CZ    . TYR A 1 250 ? 142.731 133.751 112.255 1.00 7.54  ?  250 TYR A CZ    1 
ATOM   2003  O  OH    . TYR A 1 250 ? 142.145 133.332 111.084 1.00 22.46 ?  250 TYR A OH    1 
ATOM   2004  N  N     . LEU A 1 251 ? 146.381 133.314 118.027 1.00 10.93 ?  251 LEU A N     1 
ATOM   2005  C  CA    . LEU A 1 251 ? 147.548 133.327 118.891 1.00 12.86 ?  251 LEU A CA    1 
ATOM   2006  C  C     . LEU A 1 251 ? 148.793 133.069 118.063 1.00 11.61 ?  251 LEU A C     1 
ATOM   2007  O  O     . LEU A 1 251 ? 148.803 132.187 117.199 1.00 17.27 ?  251 LEU A O     1 
ATOM   2008  C  CB    . LEU A 1 251 ? 147.436 132.278 119.998 1.00 18.54 ?  251 LEU A CB    1 
ATOM   2009  C  CG    . LEU A 1 251 ? 148.200 132.605 121.279 1.00 14.33 ?  251 LEU A CG    1 
ATOM   2010  C  CD1   . LEU A 1 251 ? 147.449 133.638 122.090 1.00 16.35 ?  251 LEU A CD1   1 
ATOM   2011  C  CD2   . LEU A 1 251 ? 148.436 131.353 122.093 1.00 13.33 ?  251 LEU A CD2   1 
ATOM   2012  N  N     . ASN A 1 252 ? 149.836 133.850 118.320 1.00 12.05 ?  252 ASN A N     1 
ATOM   2013  C  CA    . ASN A 1 252 ? 151.128 133.586 117.706 1.00 12.86 ?  252 ASN A CA    1 
ATOM   2014  C  C     . ASN A 1 252 ? 151.686 132.269 118.230 1.00 17.68 ?  252 ASN A C     1 
ATOM   2015  O  O     . ASN A 1 252 ? 151.538 131.938 119.408 1.00 23.42 ?  252 ASN A O     1 
ATOM   2016  C  CB    . ASN A 1 252 ? 152.096 134.732 117.992 1.00 15.86 ?  252 ASN A CB    1 
ATOM   2017  C  CG    . ASN A 1 252 ? 153.340 134.672 117.134 1.00 20.25 ?  252 ASN A CG    1 
ATOM   2018  O  OD1   . ASN A 1 252 ? 154.331 134.045 117.503 1.00 25.80 ?  252 ASN A OD1   1 
ATOM   2019  N  ND2   . ASN A 1 252 ? 153.293 135.319 115.978 1.00 15.68 ?  252 ASN A ND2   1 
ATOM   2020  N  N     . ILE A 1 253 ? 152.327 131.510 117.338 1.00 15.99 ?  253 ILE A N     1 
ATOM   2021  C  CA    . ILE A 1 253 ? 152.833 130.194 117.708 1.00 14.48 ?  253 ILE A CA    1 
ATOM   2022  C  C     . ILE A 1 253 ? 153.933 130.282 118.760 1.00 19.81 ?  253 ILE A C     1 
ATOM   2023  O  O     . ILE A 1 253 ? 154.210 129.293 119.445 1.00 23.62 ?  253 ILE A O     1 
ATOM   2024  C  CB    . ILE A 1 253 ? 153.317 129.446 116.450 1.00 17.64 ?  253 ILE A CB    1 
ATOM   2025  C  CG1   . ILE A 1 253 ? 153.428 127.946 116.726 1.00 19.79 ?  253 ILE A CG1   1 
ATOM   2026  C  CG2   . ILE A 1 253 ? 154.642 130.010 115.962 1.00 14.47 ?  253 ILE A CG2   1 
ATOM   2027  C  CD1   . ILE A 1 253 ? 152.924 127.083 115.599 1.00 16.32 ?  253 ILE A CD1   1 
ATOM   2028  N  N     . PHE A 1 254 ? 154.559 131.445 118.917 1.00 23.04 ?  254 PHE A N     1 
ATOM   2029  C  CA    . PHE A 1 254 ? 155.606 131.641 119.909 1.00 20.04 ?  254 PHE A CA    1 
ATOM   2030  C  C     . PHE A 1 254 ? 155.069 132.132 121.246 1.00 19.83 ?  254 PHE A C     1 
ATOM   2031  O  O     . PHE A 1 254 ? 155.856 132.370 122.166 1.00 29.11 ?  254 PHE A O     1 
ATOM   2032  C  CB    . PHE A 1 254 ? 156.656 132.617 119.376 1.00 23.31 ?  254 PHE A CB    1 
ATOM   2033  C  CG    . PHE A 1 254 ? 157.626 131.990 118.419 1.00 23.76 ?  254 PHE A CG    1 
ATOM   2034  C  CD1   . PHE A 1 254 ? 158.525 131.033 118.854 1.00 25.73 ?  254 PHE A CD1   1 
ATOM   2035  C  CD2   . PHE A 1 254 ? 157.629 132.345 117.083 1.00 24.41 ?  254 PHE A CD2   1 
ATOM   2036  C  CE1   . PHE A 1 254 ? 159.417 130.451 117.976 1.00 24.63 ?  254 PHE A CE1   1 
ATOM   2037  C  CE2   . PHE A 1 254 ? 158.518 131.764 116.201 1.00 28.73 ?  254 PHE A CE2   1 
ATOM   2038  C  CZ    . PHE A 1 254 ? 159.414 130.817 116.650 1.00 26.32 ?  254 PHE A CZ    1 
ATOM   2039  N  N     . HIS A 1 255 ? 153.756 132.301 121.368 1.00 22.21 ?  255 HIS A N     1 
ATOM   2040  C  CA    . HIS A 1 255 ? 153.146 132.562 122.662 1.00 22.02 ?  255 HIS A CA    1 
ATOM   2041  C  C     . HIS A 1 255 ? 153.286 131.332 123.550 1.00 23.79 ?  255 HIS A C     1 
ATOM   2042  O  O     . HIS A 1 255 ? 153.183 130.197 123.084 1.00 27.87 ?  255 HIS A O     1 
ATOM   2043  C  CB    . HIS A 1 255 ? 151.670 132.920 122.480 1.00 23.90 ?  255 HIS A CB    1 
ATOM   2044  C  CG    . HIS A 1 255 ? 151.070 133.653 123.639 1.00 19.97 ?  255 HIS A CG    1 
ATOM   2045  N  ND1   . HIS A 1 255 ? 150.727 133.030 124.818 1.00 16.34 ?  255 HIS A ND1   1 
ATOM   2046  C  CD2   . HIS A 1 255 ? 150.722 134.953 123.786 1.00 17.37 ?  255 HIS A CD2   1 
ATOM   2047  C  CE1   . HIS A 1 255 ? 150.212 133.917 125.649 1.00 17.98 ?  255 HIS A CE1   1 
ATOM   2048  N  NE2   . HIS A 1 255 ? 150.195 135.092 125.046 1.00 17.01 ?  255 HIS A NE2   1 
ATOM   2049  N  N     . ARG A 1 256 ? 153.539 131.564 124.841 1.00 23.57 ?  256 ARG A N     1 
ATOM   2050  C  CA    . ARG A 1 256 ? 153.710 130.447 125.764 1.00 26.08 ?  256 ARG A CA    1 
ATOM   2051  C  C     . ARG A 1 256 ? 152.436 129.623 125.896 1.00 25.39 ?  256 ARG A C     1 
ATOM   2052  O  O     . ARG A 1 256 ? 152.501 128.403 126.084 1.00 31.14 ?  256 ARG A O     1 
ATOM   2053  C  CB    . ARG A 1 256 ? 154.151 130.961 127.132 1.00 28.03 ?  256 ARG A CB    1 
ATOM   2054  C  CG    . ARG A 1 256 ? 154.457 129.863 128.126 1.00 29.43 ?  256 ARG A CG    1 
ATOM   2055  C  CD    . ARG A 1 256 ? 153.543 129.937 129.334 1.00 29.65 ?  256 ARG A CD    1 
ATOM   2056  N  NE    . ARG A 1 256 ? 152.299 129.206 129.138 1.00 31.35 ?  256 ARG A NE    1 
ATOM   2057  C  CZ    . ARG A 1 256 ? 152.097 127.956 129.527 1.00 34.72 ?  256 ARG A CZ    1 
ATOM   2058  N  NH1   . ARG A 1 256 ? 153.045 127.261 130.135 1.00 33.44 1  256 ARG A NH1   1 
ATOM   2059  N  NH2   . ARG A 1 256 ? 150.917 127.387 129.300 1.00 30.56 ?  256 ARG A NH2   1 
ATOM   2060  N  N     . ASP A 1 257 ? 151.274 130.263 125.792 1.00 23.03 ?  257 ASP A N     1 
ATOM   2061  C  CA    . ASP A 1 257 ? 149.990 129.593 125.935 1.00 19.77 ?  257 ASP A CA    1 
ATOM   2062  C  C     . ASP A 1 257 ? 149.555 128.854 124.679 1.00 23.50 ?  257 ASP A C     1 
ATOM   2063  O  O     . ASP A 1 257 ? 148.377 128.496 124.584 1.00 29.98 ?  257 ASP A O     1 
ATOM   2064  C  CB    . ASP A 1 257 ? 148.908 130.604 126.320 1.00 25.21 ?  257 ASP A CB    1 
ATOM   2065  C  CG    . ASP A 1 257 ? 149.016 131.056 127.756 1.00 31.90 ?  257 ASP A CG    1 
ATOM   2066  O  OD1   . ASP A 1 257 ? 149.765 130.427 128.532 1.00 32.69 ?  257 ASP A OD1   1 
ATOM   2067  O  OD2   . ASP A 1 257 ? 148.343 132.041 128.110 1.00 32.98 -1 257 ASP A OD2   1 
ATOM   2068  N  N     . ILE A 1 258 ? 150.456 128.616 123.724 1.00 24.69 ?  258 ILE A N     1 
ATOM   2069  C  CA    . ILE A 1 258 ? 150.043 128.049 122.443 1.00 21.61 ?  258 ILE A CA    1 
ATOM   2070  C  C     . ILE A 1 258 ? 149.502 126.636 122.624 1.00 20.20 ?  258 ILE A C     1 
ATOM   2071  O  O     . ILE A 1 258 ? 148.527 126.246 121.973 1.00 27.04 ?  258 ILE A O     1 
ATOM   2072  C  CB    . ILE A 1 258 ? 151.205 128.099 121.431 1.00 24.23 ?  258 ILE A CB    1 
ATOM   2073  C  CG1   . ILE A 1 258 ? 150.739 127.614 120.055 1.00 22.62 ?  258 ILE A CG1   1 
ATOM   2074  C  CG2   . ILE A 1 258 ? 152.407 127.299 121.919 1.00 17.77 ?  258 ILE A CG2   1 
ATOM   2075  C  CD1   . ILE A 1 258 ? 149.685 128.494 119.423 1.00 17.72 ?  258 ILE A CD1   1 
ATOM   2076  N  N     . ASN A 1 259 ? 150.112 125.848 123.512 1.00 31.20 ?  259 ASN A N     1 
ATOM   2077  C  CA    . ASN A 1 259 ? 149.645 124.482 123.719 1.00 25.53 ?  259 ASN A CA    1 
ATOM   2078  C  C     . ASN A 1 259 ? 148.289 124.460 124.414 1.00 29.96 ?  259 ASN A C     1 
ATOM   2079  O  O     . ASN A 1 259 ? 147.411 123.675 124.043 1.00 34.90 ?  259 ASN A O     1 
ATOM   2080  C  CB    . ASN A 1 259 ? 150.680 123.694 124.515 1.00 30.04 ?  259 ASN A CB    1 
ATOM   2081  C  CG    . ASN A 1 259 ? 151.971 123.496 123.749 1.00 34.90 ?  259 ASN A CG    1 
ATOM   2082  O  OD1   . ASN A 1 259 ? 152.003 122.803 122.734 1.00 34.38 ?  259 ASN A OD1   1 
ATOM   2083  N  ND2   . ASN A 1 259 ? 153.045 124.108 124.231 1.00 36.03 ?  259 ASN A ND2   1 
ATOM   2084  N  N     . ASP A 1 260 ? 148.098 125.313 125.423 1.00 29.27 ?  260 ASP A N     1 
ATOM   2085  C  CA    . ASP A 1 260 ? 146.783 125.436 126.041 1.00 25.18 ?  260 ASP A CA    1 
ATOM   2086  C  C     . ASP A 1 260 ? 145.775 126.052 125.080 1.00 26.78 ?  260 ASP A C     1 
ATOM   2087  O  O     . ASP A 1 260 ? 144.588 125.716 125.128 1.00 35.48 ?  260 ASP A O     1 
ATOM   2088  C  CB    . ASP A 1 260 ? 146.874 126.269 127.318 1.00 27.48 ?  260 ASP A CB    1 
ATOM   2089  C  CG    . ASP A 1 260 ? 148.031 125.854 128.203 1.00 39.93 ?  260 ASP A CG    1 
ATOM   2090  O  OD1   . ASP A 1 260 ? 148.221 124.637 128.406 1.00 37.41 ?  260 ASP A OD1   1 
ATOM   2091  O  OD2   . ASP A 1 260 ? 148.753 126.748 128.694 1.00 39.68 -1 260 ASP A OD2   1 
ATOM   2092  N  N     . PHE A 1 261 ? 146.230 126.963 124.217 1.00 31.54 ?  261 PHE A N     1 
ATOM   2093  C  CA    . PHE A 1 261 ? 145.363 127.540 123.197 1.00 22.38 ?  261 PHE A CA    1 
ATOM   2094  C  C     . PHE A 1 261 ? 144.852 126.464 122.249 1.00 21.58 ?  261 PHE A C     1 
ATOM   2095  O  O     . PHE A 1 261 ? 143.674 126.464 121.873 1.00 24.08 ?  261 PHE A O     1 
ATOM   2096  C  CB    . PHE A 1 261 ? 146.133 128.624 122.440 1.00 15.65 ?  261 PHE A CB    1 
ATOM   2097  C  CG    . PHE A 1 261 ? 145.376 129.251 121.305 1.00 22.10 ?  261 PHE A CG    1 
ATOM   2098  C  CD1   . PHE A 1 261 ? 144.497 130.291 121.536 1.00 20.48 ?  261 PHE A CD1   1 
ATOM   2099  C  CD2   . PHE A 1 261 ? 145.582 128.834 120.002 1.00 24.42 ?  261 PHE A CD2   1 
ATOM   2100  C  CE1   . PHE A 1 261 ? 143.813 130.882 120.496 1.00 14.82 ?  261 PHE A CE1   1 
ATOM   2101  C  CE2   . PHE A 1 261 ? 144.901 129.422 118.959 1.00 20.16 ?  261 PHE A CE2   1 
ATOM   2102  C  CZ    . PHE A 1 261 ? 144.018 130.449 119.208 1.00 14.38 ?  261 PHE A CZ    1 
ATOM   2103  N  N     . LEU A 1 262 ? 145.724 125.535 121.857 1.00 26.28 ?  262 LEU A N     1 
ATOM   2104  C  CA    . LEU A 1 262 ? 145.325 124.439 120.983 1.00 22.74 ?  262 LEU A CA    1 
ATOM   2105  C  C     . LEU A 1 262 ? 144.524 123.373 121.718 1.00 30.54 ?  262 LEU A C     1 
ATOM   2106  O  O     . LEU A 1 262 ? 143.680 122.710 121.107 1.00 34.37 ?  262 LEU A O     1 
ATOM   2107  C  CB    . LEU A 1 262 ? 146.557 123.806 120.338 1.00 26.69 ?  262 LEU A CB    1 
ATOM   2108  C  CG    . LEU A 1 262 ? 147.387 124.712 119.432 1.00 23.46 ?  262 LEU A CG    1 
ATOM   2109  C  CD1   . LEU A 1 262 ? 148.666 124.010 119.021 1.00 24.29 ?  262 LEU A CD1   1 
ATOM   2110  C  CD2   . LEU A 1 262 ? 146.585 125.136 118.218 1.00 22.16 ?  262 LEU A CD2   1 
ATOM   2111  N  N     . ASP A 1 263 ? 144.770 123.187 123.017 1.00 38.57 ?  263 ASP A N     1 
ATOM   2112  C  CA    . ASP A 1 263 ? 144.053 122.174 123.782 1.00 30.89 ?  263 ASP A CA    1 
ATOM   2113  C  C     . ASP A 1 263 ? 142.585 122.515 123.988 1.00 32.35 ?  263 ASP A C     1 
ATOM   2114  O  O     . ASP A 1 263 ? 141.821 121.643 124.413 1.00 41.94 ?  263 ASP A O     1 
ATOM   2115  C  CB    . ASP A 1 263 ? 144.723 121.960 125.139 1.00 33.94 ?  263 ASP A CB    1 
ATOM   2116  C  CG    . ASP A 1 263 ? 146.038 121.217 125.031 1.00 40.92 ?  263 ASP A CG    1 
ATOM   2117  O  OD1   . ASP A 1 263 ? 146.284 120.595 123.977 1.00 37.88 ?  263 ASP A OD1   1 
ATOM   2118  O  OD2   . ASP A 1 263 ? 146.823 121.256 126.000 1.00 42.51 -1 263 ASP A OD2   1 
ATOM   2119  N  N     . THR A 1 264 ? 142.172 123.753 123.711 1.00 37.53 ?  264 THR A N     1 
ATOM   2120  C  CA    . THR A 1 264 ? 140.762 124.110 123.795 1.00 36.65 ?  264 THR A CA    1 
ATOM   2121  C  C     . THR A 1 264 ? 139.929 123.470 122.693 1.00 38.27 ?  264 THR A C     1 
ATOM   2122  O  O     . THR A 1 264 ? 138.698 123.474 122.792 1.00 42.43 ?  264 THR A O     1 
ATOM   2123  C  CB    . THR A 1 264 ? 140.598 125.631 123.741 1.00 37.79 ?  264 THR A CB    1 
ATOM   2124  O  OG1   . THR A 1 264 ? 141.126 126.130 122.507 1.00 41.67 ?  264 THR A OG1   1 
ATOM   2125  C  CG2   . THR A 1 264 ? 141.330 126.287 124.900 1.00 33.19 ?  264 THR A CG2   1 
ATOM   2126  N  N     . LYS A 1 265 ? 140.563 122.924 121.658 1.00 34.74 ?  265 LYS A N     1 
ATOM   2127  C  CA    . LYS A 1 265 ? 139.859 122.300 120.547 1.00 38.69 ?  265 LYS A CA    1 
ATOM   2128  C  C     . LYS A 1 265 ? 139.970 120.784 120.541 1.00 38.10 ?  265 LYS A C     1 
ATOM   2129  O  O     . LYS A 1 265 ? 139.375 120.138 119.672 1.00 42.13 ?  265 LYS A O     1 
ATOM   2130  C  CB    . LYS A 1 265 ? 140.374 122.857 119.216 1.00 37.22 ?  265 LYS A CB    1 
ATOM   2131  C  CG    . LYS A 1 265 ? 139.806 124.212 118.858 1.00 37.99 ?  265 LYS A CG    1 
ATOM   2132  C  CD    . LYS A 1 265 ? 138.320 124.268 119.131 1.00 38.69 ?  265 LYS A CD    1 
ATOM   2133  C  CE    . LYS A 1 265 ? 137.737 125.589 118.688 1.00 36.61 ?  265 LYS A CE    1 
ATOM   2134  N  NZ    . LYS A 1 265 ? 136.356 125.778 119.202 1.00 42.06 1  265 LYS A NZ    1 
ATOM   2135  N  N     . LYS A 1 266 ? 140.714 120.199 121.474 1.00 40.85 ?  266 LYS A N     1 
ATOM   2136  C  CA    . LYS A 1 266 ? 140.800 118.749 121.552 1.00 45.78 ?  266 LYS A CA    1 
ATOM   2137  C  C     . LYS A 1 266 ? 139.453 118.158 121.952 1.00 51.25 ?  266 LYS A C     1 
ATOM   2138  O  O     . LYS A 1 266 ? 138.691 118.747 122.724 1.00 51.79 ?  266 LYS A O     1 
ATOM   2139  C  CB    . LYS A 1 266 ? 141.877 118.327 122.549 1.00 44.22 ?  266 LYS A CB    1 
ATOM   2140  C  CG    . LYS A 1 266 ? 143.286 118.367 121.985 1.00 46.23 ?  266 LYS A CG    1 
ATOM   2141  C  CD    . LYS A 1 266 ? 144.310 117.915 123.010 1.00 48.71 ?  266 LYS A CD    1 
ATOM   2142  C  CE    . LYS A 1 266 ? 145.664 117.673 122.363 1.00 49.28 ?  266 LYS A CE    1 
ATOM   2143  N  NZ    . LYS A 1 266 ? 146.761 117.602 123.367 1.00 47.87 1  266 LYS A NZ    1 
ATOM   2144  N  N     . ILE A 1 267 ? 139.158 116.979 121.403 1.00 54.28 ?  267 ILE A N     1 
ATOM   2145  C  CA    . ILE A 1 267 ? 137.895 116.312 121.706 1.00 55.14 ?  267 ILE A CA    1 
ATOM   2146  C  C     . ILE A 1 267 ? 137.834 115.918 123.176 1.00 57.07 ?  267 ILE A C     1 
ATOM   2147  O  O     . ILE A 1 267 ? 136.765 115.955 123.798 1.00 54.69 ?  267 ILE A O     1 
ATOM   2148  C  CB    . ILE A 1 267 ? 137.698 115.100 120.777 1.00 55.54 ?  267 ILE A CB    1 
ATOM   2149  C  CG1   . ILE A 1 267 ? 139.000 114.304 120.658 1.00 57.04 ?  267 ILE A CG1   1 
ATOM   2150  C  CG2   . ILE A 1 267 ? 137.212 115.551 119.410 1.00 55.23 ?  267 ILE A CG2   1 
ATOM   2151  C  CD1   . ILE A 1 267 ? 138.878 113.057 119.814 1.00 55.54 ?  267 ILE A CD1   1 
ATOM   2152  N  N     . SER A 1 268 ? 138.972 115.542 123.756 1.00 60.16 ?  268 SER A N     1 
ATOM   2153  C  CA    . SER A 1 268 ? 139.052 115.152 125.158 1.00 61.20 ?  268 SER A CA    1 
ATOM   2154  C  C     . SER A 1 268 ? 139.212 116.341 126.102 1.00 63.52 ?  268 SER A C     1 
ATOM   2155  O  O     . SER A 1 268 ? 139.623 116.148 127.253 1.00 63.03 ?  268 SER A O     1 
ATOM   2156  C  CB    . SER A 1 268 ? 140.205 114.168 125.361 1.00 63.43 ?  268 SER A CB    1 
ATOM   2157  O  OG    . SER A 1 268 ? 141.423 114.703 124.875 1.00 62.04 ?  268 SER A OG    1 
ATOM   2158  N  N     . ALA A 1 269 ? 138.905 117.555 125.653 1.00 67.34 ?  269 ALA A N     1 
ATOM   2159  C  CA    . ALA A 1 269 ? 139.060 118.726 126.503 1.00 66.38 ?  269 ALA A CA    1 
ATOM   2160  C  C     . ALA A 1 269 ? 137.942 118.797 127.535 1.00 67.63 ?  269 ALA A C     1 
ATOM   2161  O  O     . ALA A 1 269 ? 136.790 118.455 127.254 1.00 65.73 ?  269 ALA A O     1 
ATOM   2162  C  CB    . ALA A 1 269 ? 139.077 120.000 125.658 1.00 63.69 ?  269 ALA A CB    1 
ATOM   2163  N  N     . ASP A 1 270 ? 138.290 119.247 128.737 1.00 75.07 ?  270 ASP A N     1 
ATOM   2164  C  CA    . ASP A 1 270 ? 137.315 119.371 129.809 1.00 75.00 ?  270 ASP A CA    1 
ATOM   2165  C  C     . ASP A 1 270 ? 136.420 120.588 129.584 1.00 74.74 ?  270 ASP A C     1 
ATOM   2166  O  O     . ASP A 1 270 ? 136.742 121.501 128.819 1.00 75.33 ?  270 ASP A O     1 
ATOM   2167  C  CB    . ASP A 1 270 ? 138.019 119.476 131.162 1.00 75.61 ?  270 ASP A CB    1 
ATOM   2168  C  CG    . ASP A 1 270 ? 137.127 119.064 132.318 1.00 77.85 ?  270 ASP A CG    1 
ATOM   2169  O  OD1   . ASP A 1 270 ? 136.083 119.715 132.530 1.00 77.52 ?  270 ASP A OD1   1 
ATOM   2170  O  OD2   . ASP A 1 270 ? 137.471 118.086 133.016 1.00 76.02 -1 270 ASP A OD2   1 
ATOM   2171  N  N     . GLU A 1 271 ? 135.275 120.588 130.270 1.00 75.70 ?  271 GLU A N     1 
ATOM   2172  C  CA    . GLU A 1 271 ? 134.320 121.682 130.135 1.00 76.74 ?  271 GLU A CA    1 
ATOM   2173  C  C     . GLU A 1 271 ? 134.854 122.997 130.691 1.00 76.23 ?  271 GLU A C     1 
ATOM   2174  O  O     . GLU A 1 271 ? 134.355 124.062 130.311 1.00 75.27 ?  271 GLU A O     1 
ATOM   2175  C  CB    . GLU A 1 271 ? 133.007 121.319 130.827 1.00 75.14 ?  271 GLU A CB    1 
ATOM   2176  C  CG    . GLU A 1 271 ? 132.311 120.106 130.233 1.00 75.56 ?  271 GLU A CG    1 
ATOM   2177  C  CD    . GLU A 1 271 ? 131.893 120.323 128.792 1.00 76.58 ?  271 GLU A CD    1 
ATOM   2178  O  OE1   . GLU A 1 271 ? 131.430 121.437 128.468 1.00 76.79 ?  271 GLU A OE1   1 
ATOM   2179  O  OE2   . GLU A 1 271 ? 132.030 119.381 127.983 1.00 75.92 -1 271 GLU A OE2   1 
ATOM   2180  N  N     . ASP A 1 272 ? 135.848 122.950 131.576 1.00 74.59 ?  272 ASP A N     1 
ATOM   2181  C  CA    . ASP A 1 272 ? 136.444 124.161 132.124 1.00 75.23 ?  272 ASP A CA    1 
ATOM   2182  C  C     . ASP A 1 272 ? 137.536 124.739 131.234 1.00 73.89 ?  272 ASP A C     1 
ATOM   2183  O  O     . ASP A 1 272 ? 138.107 125.779 131.578 1.00 71.80 ?  272 ASP A O     1 
ATOM   2184  C  CB    . ASP A 1 272 ? 137.014 123.885 133.518 1.00 74.63 ?  272 ASP A CB    1 
ATOM   2185  C  CG    . ASP A 1 272 ? 135.958 123.950 134.605 1.00 76.48 ?  272 ASP A CG    1 
ATOM   2186  O  OD1   . ASP A 1 272 ? 134.861 124.485 134.339 1.00 76.29 ?  272 ASP A OD1   1 
ATOM   2187  O  OD2   . ASP A 1 272 ? 136.228 123.470 135.725 1.00 74.73 -1 272 ASP A OD2   1 
ATOM   2188  N  N     . VAL A 1 273 ? 137.846 124.089 130.112 1.00 64.46 ?  273 VAL A N     1 
ATOM   2189  C  CA    . VAL A 1 273 ? 138.876 124.539 129.185 1.00 63.69 ?  273 VAL A CA    1 
ATOM   2190  C  C     . VAL A 1 273 ? 138.321 124.710 127.775 1.00 61.79 ?  273 VAL A C     1 
ATOM   2191  O  O     . VAL A 1 273 ? 138.595 125.708 127.102 1.00 62.73 ?  273 VAL A O     1 
ATOM   2192  C  CB    . VAL A 1 273 ? 140.088 123.579 129.182 1.00 64.13 ?  273 VAL A CB    1 
ATOM   2193  C  CG1   . VAL A 1 273 ? 140.985 123.847 127.984 1.00 60.73 ?  273 VAL A CG1   1 
ATOM   2194  C  CG2   . VAL A 1 273 ? 140.869 123.708 130.479 1.00 62.17 ?  273 VAL A CG2   1 
ATOM   2195  N  N     . ARG A 1 274 ? 137.528 123.744 127.315 1.00 58.79 ?  274 ARG A N     1 
ATOM   2196  C  CA    . ARG A 1 274 ? 137.081 123.723 125.928 1.00 56.27 ?  274 ARG A CA    1 
ATOM   2197  C  C     . ARG A 1 274 ? 136.191 124.919 125.609 1.00 56.31 ?  274 ARG A C     1 
ATOM   2198  O  O     . ARG A 1 274 ? 135.321 125.299 126.398 1.00 59.27 ?  274 ARG A O     1 
ATOM   2199  C  CB    . ARG A 1 274 ? 136.334 122.419 125.642 1.00 58.56 ?  274 ARG A CB    1 
ATOM   2200  C  CG    . ARG A 1 274 ? 135.159 122.558 124.688 1.00 56.98 ?  274 ARG A CG    1 
ATOM   2201  C  CD    . ARG A 1 274 ? 134.639 121.198 124.241 1.00 57.29 ?  274 ARG A CD    1 
ATOM   2202  N  NE    . ARG A 1 274 ? 135.552 120.495 123.343 1.00 60.77 ?  274 ARG A NE    1 
ATOM   2203  C  CZ    . ARG A 1 274 ? 135.966 120.943 122.164 1.00 60.46 ?  274 ARG A CZ    1 
ATOM   2204  N  NH1   . ARG A 1 274 ? 135.532 122.089 121.663 1.00 59.29 1  274 ARG A NH1   1 
ATOM   2205  N  NH2   . ARG A 1 274 ? 136.825 120.213 121.460 1.00 56.10 ?  274 ARG A NH2   1 
ATOM   2206  N  N     . VAL A 1 275 ? 136.423 125.514 124.442 1.00 47.22 ?  275 VAL A N     1 
ATOM   2207  C  CA    . VAL A 1 275 ? 135.577 126.565 123.892 1.00 47.42 ?  275 VAL A CA    1 
ATOM   2208  C  C     . VAL A 1 275 ? 134.880 126.007 122.659 1.00 47.78 ?  275 VAL A C     1 
ATOM   2209  O  O     . VAL A 1 275 ? 135.491 125.284 121.864 1.00 49.68 ?  275 VAL A O     1 
ATOM   2210  C  CB    . VAL A 1 275 ? 136.381 127.835 123.550 1.00 45.57 ?  275 VAL A CB    1 
ATOM   2211  C  CG1   . VAL A 1 275 ? 136.871 128.508 124.820 1.00 42.16 ?  275 VAL A CG1   1 
ATOM   2212  C  CG2   . VAL A 1 275 ? 137.549 127.500 122.644 1.00 46.32 ?  275 VAL A CG2   1 
ATOM   2213  N  N     . LYS A 1 276 ? 133.598 126.323 122.514 1.00 47.35 ?  276 LYS A N     1 
ATOM   2214  C  CA    . LYS A 1 276 ? 132.771 125.736 121.467 1.00 48.92 ?  276 LYS A CA    1 
ATOM   2215  C  C     . LYS A 1 276 ? 132.405 126.706 120.356 1.00 45.86 ?  276 LYS A C     1 
ATOM   2216  O  O     . LYS A 1 276 ? 132.430 126.328 119.183 1.00 51.39 ?  276 LYS A O     1 
ATOM   2217  C  CB    . LYS A 1 276 ? 131.489 125.163 122.082 1.00 49.48 ?  276 LYS A CB    1 
ATOM   2218  C  CG    . LYS A 1 276 ? 131.744 124.021 123.054 1.00 50.86 ?  276 LYS A CG    1 
ATOM   2219  C  CD    . LYS A 1 276 ? 130.471 123.567 123.745 1.00 51.93 ?  276 LYS A CD    1 
ATOM   2220  C  CE    . LYS A 1 276 ? 130.755 122.426 124.711 1.00 52.38 ?  276 LYS A CE    1 
ATOM   2221  N  NZ    . LYS A 1 276 ? 129.617 122.182 125.640 1.00 54.84 1  276 LYS A NZ    1 
ATOM   2222  N  N     . THR A 1 277 ? 132.067 127.950 120.688 1.00 37.03 ?  277 THR A N     1 
ATOM   2223  C  CA    . THR A 1 277 ? 131.653 128.940 119.706 1.00 38.81 ?  277 THR A CA    1 
ATOM   2224  C  C     . THR A 1 277 ? 132.810 129.787 119.194 1.00 40.67 ?  277 THR A C     1 
ATOM   2225  O  O     . THR A 1 277 ? 132.584 130.726 118.424 1.00 39.52 ?  277 THR A O     1 
ATOM   2226  C  CB    . THR A 1 277 ? 130.572 129.847 120.295 1.00 39.99 ?  277 THR A CB    1 
ATOM   2227  O  OG1   . THR A 1 277 ? 131.188 130.957 120.961 1.00 38.24 ?  277 THR A OG1   1 
ATOM   2228  C  CG2   . THR A 1 277 ? 129.728 129.077 121.288 1.00 38.90 ?  277 THR A CG2   1 
ATOM   2229  N  N     . LEU A 1 278 ? 134.038 129.479 119.600 1.00 36.61 ?  278 LEU A N     1 
ATOM   2230  C  CA    . LEU A 1 278 ? 135.203 130.294 119.276 1.00 30.45 ?  278 LEU A CA    1 
ATOM   2231  C  C     . LEU A 1 278 ? 136.134 129.493 118.377 1.00 24.23 ?  278 LEU A C     1 
ATOM   2232  O  O     . LEU A 1 278 ? 136.756 128.527 118.827 1.00 32.43 ?  278 LEU A O     1 
ATOM   2233  C  CB    . LEU A 1 278 ? 135.923 130.740 120.547 1.00 30.01 ?  278 LEU A CB    1 
ATOM   2234  C  CG    . LEU A 1 278 ? 136.770 132.008 120.456 1.00 28.95 ?  278 LEU A CG    1 
ATOM   2235  C  CD1   . LEU A 1 278 ? 135.890 133.237 120.353 1.00 23.64 ?  278 LEU A CD1   1 
ATOM   2236  C  CD2   . LEU A 1 278 ? 137.686 132.113 121.658 1.00 26.19 ?  278 LEU A CD2   1 
ATOM   2237  N  N     . SER A 1 279 ? 136.228 129.895 117.113 1.00 24.49 ?  279 SER A N     1 
ATOM   2238  C  CA    . SER A 1 279 ? 137.249 129.357 116.231 1.00 15.83 ?  279 SER A CA    1 
ATOM   2239  C  C     . SER A 1 279 ? 138.621 129.843 116.682 1.00 17.60 ?  279 SER A C     1 
ATOM   2240  O  O     . SER A 1 279 ? 138.754 130.855 117.372 1.00 28.53 ?  279 SER A O     1 
ATOM   2241  C  CB    . SER A 1 279 ? 136.991 129.776 114.785 1.00 18.86 ?  279 SER A CB    1 
ATOM   2242  O  OG    . SER A 1 279 ? 135.701 129.380 114.357 1.00 26.41 ?  279 SER A OG    1 
ATOM   2243  N  N     . ILE A 1 280 ? 139.655 129.102 116.301 1.00 15.31 ?  280 ILE A N     1 
ATOM   2244  C  CA    . ILE A 1 280 ? 141.014 129.423 116.711 1.00 16.70 ?  280 ILE A CA    1 
ATOM   2245  C  C     . ILE A 1 280 ? 141.913 129.460 115.484 1.00 15.46 ?  280 ILE A C     1 
ATOM   2246  O  O     . ILE A 1 280 ? 141.756 128.657 114.559 1.00 20.73 ?  280 ILE A O     1 
ATOM   2247  C  CB    . ILE A 1 280 ? 141.555 128.432 117.764 1.00 17.82 ?  280 ILE A CB    1 
ATOM   2248  C  CG1   . ILE A 1 280 ? 141.601 127.005 117.221 1.00 23.63 ?  280 ILE A CG1   1 
ATOM   2249  C  CG2   . ILE A 1 280 ? 140.716 128.486 119.019 1.00 18.85 ?  280 ILE A CG2   1 
ATOM   2250  C  CD1   . ILE A 1 280 ? 142.627 126.141 117.915 1.00 18.27 ?  280 ILE A CD1   1 
ATOM   2251  N  N     . GLY A 1 281 ? 142.829 130.418 115.470 1.00 9.44  ?  281 GLY A N     1 
ATOM   2252  C  CA    . GLY A 1 281 ? 143.846 130.483 114.442 1.00 4.46  ?  281 GLY A CA    1 
ATOM   2253  C  C     . GLY A 1 281 ? 145.213 130.639 115.072 1.00 11.28 ?  281 GLY A C     1 
ATOM   2254  O  O     . GLY A 1 281 ? 145.362 131.204 116.154 1.00 21.39 ?  281 GLY A O     1 
ATOM   2255  N  N     . VAL A 1 282 ? 146.219 130.117 114.380 1.00 18.47 ?  282 VAL A N     1 
ATOM   2256  C  CA    . VAL A 1 282 ? 147.600 130.170 114.840 1.00 16.31 ?  282 VAL A CA    1 
ATOM   2257  C  C     . VAL A 1 282 ? 148.417 130.939 113.815 1.00 14.87 ?  282 VAL A C     1 
ATOM   2258  O  O     . VAL A 1 282 ? 148.391 130.617 112.622 1.00 19.62 ?  282 VAL A O     1 
ATOM   2259  C  CB    . VAL A 1 282 ? 148.184 128.765 115.068 1.00 12.54 ?  282 VAL A CB    1 
ATOM   2260  C  CG1   . VAL A 1 282 ? 149.684 128.841 115.260 1.00 19.43 ?  282 VAL A CG1   1 
ATOM   2261  C  CG2   . VAL A 1 282 ? 147.541 128.126 116.277 1.00 20.97 ?  282 VAL A CG2   1 
ATOM   2262  N  N     . VAL A 1 283 ? 149.136 131.953 114.281 1.00 12.30 ?  283 VAL A N     1 
ATOM   2263  C  CA    . VAL A 1 283 ? 149.997 132.766 113.436 1.00 8.37  ?  283 VAL A CA    1 
ATOM   2264  C  C     . VAL A 1 283 ? 151.406 132.199 113.528 1.00 13.12 ?  283 VAL A C     1 
ATOM   2265  O  O     . VAL A 1 283 ? 151.992 132.144 114.615 1.00 25.22 ?  283 VAL A O     1 
ATOM   2266  C  CB    . VAL A 1 283 ? 149.957 134.241 113.857 1.00 9.54  ?  283 VAL A CB    1 
ATOM   2267  C  CG1   . VAL A 1 283 ? 150.685 135.105 112.848 1.00 12.39 ?  283 VAL A CG1   1 
ATOM   2268  C  CG2   . VAL A 1 283 ? 148.519 134.690 114.015 1.00 9.73  ?  283 VAL A CG2   1 
ATOM   2269  N  N     . ILE A 1 284 ? 151.947 131.772 112.392 1.00 15.63 ?  284 ILE A N     1 
ATOM   2270  C  CA    . ILE A 1 284 ? 153.242 131.099 112.364 1.00 15.39 ?  284 ILE A CA    1 
ATOM   2271  C  C     . ILE A 1 284 ? 154.251 131.941 111.593 1.00 21.61 ?  284 ILE A C     1 
ATOM   2272  O  O     . ILE A 1 284 ? 154.161 132.044 110.362 1.00 21.50 ?  284 ILE A O     1 
ATOM   2273  C  CB    . ILE A 1 284 ? 153.124 129.693 111.757 1.00 15.46 ?  284 ILE A CB    1 
ATOM   2274  C  CG1   . ILE A 1 284 ? 151.997 128.915 112.435 1.00 12.76 ?  284 ILE A CG1   1 
ATOM   2275  C  CG2   . ILE A 1 284 ? 154.440 128.950 111.885 1.00 16.89 ?  284 ILE A CG2   1 
ATOM   2276  C  CD1   . ILE A 1 284 ? 151.859 127.495 111.950 1.00 16.53 ?  284 ILE A CD1   1 
ATOM   2277  N  N     . PRO A 1 285 ? 155.215 132.562 112.266 1.00 25.53 ?  285 PRO A N     1 
ATOM   2278  C  CA    . PRO A 1 285 ? 156.296 133.240 111.548 1.00 25.30 ?  285 PRO A CA    1 
ATOM   2279  C  C     . PRO A 1 285 ? 157.220 132.240 110.869 1.00 25.79 ?  285 PRO A C     1 
ATOM   2280  O  O     . PRO A 1 285 ? 157.259 131.055 111.204 1.00 25.01 ?  285 PRO A O     1 
ATOM   2281  C  CB    . PRO A 1 285 ? 157.029 134.012 112.650 1.00 26.35 ?  285 PRO A CB    1 
ATOM   2282  C  CG    . PRO A 1 285 ? 156.061 134.076 113.790 1.00 23.82 ?  285 PRO A CG    1 
ATOM   2283  C  CD    . PRO A 1 285 ? 155.280 132.808 113.714 1.00 19.89 ?  285 PRO A CD    1 
ATOM   2284  N  N     . ASP A 1 286 ? 157.969 132.745 109.886 1.00 31.22 ?  286 ASP A N     1 
ATOM   2285  C  CA    . ASP A 1 286 ? 158.948 131.916 109.192 1.00 25.97 ?  286 ASP A CA    1 
ATOM   2286  C  C     . ASP A 1 286 ? 159.985 131.335 110.143 1.00 34.55 ?  286 ASP A C     1 
ATOM   2287  O  O     . ASP A 1 286 ? 160.582 130.297 109.834 1.00 35.11 ?  286 ASP A O     1 
ATOM   2288  C  CB    . ASP A 1 286 ? 159.645 132.729 108.101 1.00 27.60 ?  286 ASP A CB    1 
ATOM   2289  C  CG    . ASP A 1 286 ? 159.088 132.452 106.721 1.00 38.61 ?  286 ASP A CG    1 
ATOM   2290  O  OD1   . ASP A 1 286 ? 157.858 132.286 106.596 1.00 42.79 ?  286 ASP A OD1   1 
ATOM   2291  O  OD2   . ASP A 1 286 ? 159.882 132.405 105.758 1.00 42.45 -1 286 ASP A OD2   1 
ATOM   2292  N  N     . LYS A 1 287 ? 160.210 131.983 111.288 1.00 32.80 ?  287 LYS A N     1 
ATOM   2293  C  CA    . LYS A 1 287 ? 161.163 131.467 112.264 1.00 27.94 ?  287 LYS A CA    1 
ATOM   2294  C  C     . LYS A 1 287 ? 160.743 130.098 112.782 1.00 27.59 ?  287 LYS A C     1 
ATOM   2295  O  O     . LYS A 1 287 ? 161.582 129.207 112.940 1.00 35.74 ?  287 LYS A O     1 
ATOM   2296  C  CB    . LYS A 1 287 ? 161.313 132.454 113.421 1.00 28.97 ?  287 LYS A CB    1 
ATOM   2297  C  CG    . LYS A 1 287 ? 162.457 132.127 114.365 1.00 27.77 ?  287 LYS A CG    1 
ATOM   2298  C  CD    . LYS A 1 287 ? 163.755 131.961 113.598 1.00 31.66 ?  287 LYS A CD    1 
ATOM   2299  C  CE    . LYS A 1 287 ? 164.917 131.684 114.529 1.00 32.61 ?  287 LYS A CE    1 
ATOM   2300  N  NZ    . LYS A 1 287 ? 166.216 131.701 113.806 1.00 33.85 1  287 LYS A NZ    1 
ATOM   2301  N  N     . PHE A 1 288 ? 159.451 129.915 113.065 1.00 27.34 ?  288 PHE A N     1 
ATOM   2302  C  CA    . PHE A 1 288 ? 158.984 128.625 113.563 1.00 22.62 ?  288 PHE A CA    1 
ATOM   2303  C  C     . PHE A 1 288 ? 159.163 127.527 112.521 1.00 25.80 ?  288 PHE A C     1 
ATOM   2304  O  O     . PHE A 1 288 ? 159.578 126.410 112.853 1.00 34.63 ?  288 PHE A O     1 
ATOM   2305  C  CB    . PHE A 1 288 ? 157.521 128.721 113.987 1.00 24.92 ?  288 PHE A CB    1 
ATOM   2306  C  CG    . PHE A 1 288 ? 157.003 127.481 114.653 1.00 27.45 ?  288 PHE A CG    1 
ATOM   2307  C  CD1   . PHE A 1 288 ? 157.197 127.275 116.008 1.00 23.19 ?  288 PHE A CD1   1 
ATOM   2308  C  CD2   . PHE A 1 288 ? 156.331 126.516 113.925 1.00 26.73 ?  288 PHE A CD2   1 
ATOM   2309  C  CE1   . PHE A 1 288 ? 156.726 126.136 116.621 1.00 27.14 ?  288 PHE A CE1   1 
ATOM   2310  C  CE2   . PHE A 1 288 ? 155.858 125.374 114.535 1.00 24.01 ?  288 PHE A CE2   1 
ATOM   2311  C  CZ    . PHE A 1 288 ? 156.056 125.185 115.883 1.00 27.79 ?  288 PHE A CZ    1 
ATOM   2312  N  N     . VAL A 1 289 ? 158.844 127.822 111.261 1.00 32.00 ?  289 VAL A N     1 
ATOM   2313  C  CA    . VAL A 1 289 ? 159.009 126.832 110.202 1.00 29.47 ?  289 VAL A CA    1 
ATOM   2314  C  C     . VAL A 1 289 ? 160.482 126.494 110.018 1.00 30.02 ?  289 VAL A C     1 
ATOM   2315  O  O     . VAL A 1 289 ? 160.843 125.336 109.785 1.00 35.14 ?  289 VAL A O     1 
ATOM   2316  C  CB    . VAL A 1 289 ? 158.373 127.340 108.894 1.00 30.34 ?  289 VAL A CB    1 
ATOM   2317  C  CG1   . VAL A 1 289 ? 158.566 126.328 107.778 1.00 30.45 ?  289 VAL A CG1   1 
ATOM   2318  C  CG2   . VAL A 1 289 ? 156.898 127.633 109.107 1.00 23.88 ?  289 VAL A CG2   1 
ATOM   2319  N  N     . GLU A 1 290 ? 161.355 127.499 110.121 1.00 37.54 ?  290 GLU A N     1 
ATOM   2320  C  CA    . GLU A 1 290 ? 162.788 127.244 110.030 1.00 34.55 ?  290 GLU A CA    1 
ATOM   2321  C  C     . GLU A 1 290 ? 163.271 126.375 111.187 1.00 35.20 ?  290 GLU A C     1 
ATOM   2322  O  O     . GLU A 1 290 ? 164.071 125.455 110.989 1.00 41.82 ?  290 GLU A O     1 
ATOM   2323  C  CB    . GLU A 1 290 ? 163.550 128.569 109.987 1.00 34.45 ?  290 GLU A CB    1 
ATOM   2324  C  CG    . GLU A 1 290 ? 164.911 128.538 110.660 1.00 39.30 ?  290 GLU A CG    1 
ATOM   2325  C  CD    . GLU A 1 290 ? 165.605 129.884 110.629 1.00 45.41 ?  290 GLU A CD    1 
ATOM   2326  O  OE1   . GLU A 1 290 ? 164.902 130.917 110.632 1.00 46.66 ?  290 GLU A OE1   1 
ATOM   2327  O  OE2   . GLU A 1 290 ? 166.853 129.912 110.604 1.00 43.61 -1 290 GLU A OE2   1 
ATOM   2328  N  N     . LEU A 1 291 ? 162.792 126.652 112.403 1.00 28.22 ?  291 LEU A N     1 
ATOM   2329  C  CA    . LEU A 1 291 ? 163.195 125.863 113.563 1.00 26.89 ?  291 LEU A CA    1 
ATOM   2330  C  C     . LEU A 1 291 ? 162.726 124.420 113.442 1.00 35.32 ?  291 LEU A C     1 
ATOM   2331  O  O     . LEU A 1 291 ? 163.465 123.490 113.780 1.00 38.89 ?  291 LEU A O     1 
ATOM   2332  C  CB    . LEU A 1 291 ? 162.647 126.494 114.844 1.00 31.08 ?  291 LEU A CB    1 
ATOM   2333  C  CG    . LEU A 1 291 ? 163.289 127.804 115.301 1.00 33.94 ?  291 LEU A CG    1 
ATOM   2334  C  CD1   . LEU A 1 291 ? 162.417 128.491 116.336 1.00 28.25 ?  291 LEU A CD1   1 
ATOM   2335  C  CD2   . LEU A 1 291 ? 164.681 127.557 115.846 1.00 31.72 ?  291 LEU A CD2   1 
ATOM   2336  N  N     . ALA A 1 292 ? 161.493 124.216 112.974 1.00 37.20 ?  292 ALA A N     1 
ATOM   2337  C  CA    . ALA A 1 292 ? 160.994 122.858 112.780 1.00 30.50 ?  292 ALA A CA    1 
ATOM   2338  C  C     . ALA A 1 292 ? 161.747 122.149 111.661 1.00 32.10 ?  292 ALA A C     1 
ATOM   2339  O  O     . ALA A 1 292 ? 161.990 120.940 111.738 1.00 35.83 ?  292 ALA A O     1 
ATOM   2340  C  CB    . ALA A 1 292 ? 159.495 122.887 112.489 1.00 26.04 ?  292 ALA A CB    1 
ATOM   2341  N  N     . ARG A 1 293 ? 162.121 122.885 110.613 1.00 32.95 ?  293 ARG A N     1 
ATOM   2342  C  CA    . ARG A 1 293 ? 162.852 122.291 109.499 1.00 33.13 ?  293 ARG A CA    1 
ATOM   2343  C  C     . ARG A 1 293 ? 164.212 121.770 109.941 1.00 39.16 ?  293 ARG A C     1 
ATOM   2344  O  O     . ARG A 1 293 ? 164.636 120.686 109.523 1.00 41.45 ?  293 ARG A O     1 
ATOM   2345  C  CB    . ARG A 1 293 ? 163.003 123.316 108.376 1.00 34.94 ?  293 ARG A CB    1 
ATOM   2346  C  CG    . ARG A 1 293 ? 163.870 122.863 107.217 1.00 35.23 ?  293 ARG A CG    1 
ATOM   2347  C  CD    . ARG A 1 293 ? 164.236 124.038 106.333 1.00 37.62 ?  293 ARG A CD    1 
ATOM   2348  N  NE    . ARG A 1 293 ? 163.076 124.873 106.045 1.00 42.26 ?  293 ARG A NE    1 
ATOM   2349  C  CZ    . ARG A 1 293 ? 163.055 126.193 106.169 1.00 40.70 ?  293 ARG A CZ    1 
ATOM   2350  N  NH1   . ARG A 1 293 ? 164.117 126.866 106.579 1.00 41.69 1  293 ARG A NH1   1 
ATOM   2351  N  NH2   . ARG A 1 293 ? 161.939 126.854 105.876 1.00 35.59 ?  293 ARG A NH2   1 
ATOM   2352  N  N     . GLU A 1 294 ? 164.909 122.524 110.786 1.00 44.74 ?  294 GLU A N     1 
ATOM   2353  C  CA    . GLU A 1 294 ? 166.220 122.123 111.279 1.00 43.18 ?  294 GLU A CA    1 
ATOM   2354  C  C     . GLU A 1 294 ? 166.140 121.176 112.467 1.00 44.44 ?  294 GLU A C     1 
ATOM   2355  O  O     . GLU A 1 294 ? 167.189 120.743 112.959 1.00 48.04 ?  294 GLU A O     1 
ATOM   2356  C  CB    . GLU A 1 294 ? 167.037 123.362 111.658 1.00 41.64 ?  294 GLU A CB    1 
ATOM   2357  C  CG    . GLU A 1 294 ? 167.099 124.417 110.565 1.00 43.84 ?  294 GLU A CG    1 
ATOM   2358  C  CD    . GLU A 1 294 ? 167.373 125.804 111.110 1.00 52.67 ?  294 GLU A CD    1 
ATOM   2359  O  OE1   . GLU A 1 294 ? 166.935 126.096 112.242 1.00 50.44 ?  294 GLU A OE1   1 
ATOM   2360  O  OE2   . GLU A 1 294 ? 168.025 126.603 110.406 1.00 51.67 -1 294 GLU A OE2   1 
ATOM   2361  N  N     . ASP A 1 295 ? 164.933 120.853 112.934 1.00 44.22 ?  295 ASP A N     1 
ATOM   2362  C  CA    . ASP A 1 295 ? 164.722 119.974 114.085 1.00 43.82 ?  295 ASP A CA    1 
ATOM   2363  C  C     . ASP A 1 295 ? 165.403 120.514 115.338 1.00 48.16 ?  295 ASP A C     1 
ATOM   2364  O  O     . ASP A 1 295 ? 165.790 119.753 116.227 1.00 51.21 ?  295 ASP A O     1 
ATOM   2365  C  CB    . ASP A 1 295 ? 165.191 118.546 113.794 1.00 46.89 ?  295 ASP A CB    1 
ATOM   2366  C  CG    . ASP A 1 295 ? 164.291 117.499 114.422 1.00 51.48 ?  295 ASP A CG    1 
ATOM   2367  O  OD1   . ASP A 1 295 ? 163.550 117.838 115.367 1.00 49.59 ?  295 ASP A OD1   1 
ATOM   2368  O  OD2   . ASP A 1 295 ? 164.323 116.335 113.967 1.00 50.75 -1 295 ASP A OD2   1 
ATOM   2369  N  N     . LYS A 1 296 ? 165.552 121.833 115.415 1.00 45.61 ?  296 LYS A N     1 
ATOM   2370  C  CA    . LYS A 1 296 ? 166.165 122.466 116.568 1.00 45.38 ?  296 LYS A CA    1 
ATOM   2371  C  C     . LYS A 1 296 ? 165.143 122.623 117.690 1.00 44.84 ?  296 LYS A C     1 
ATOM   2372  O  O     . LYS A 1 296 ? 163.949 122.370 117.521 1.00 45.52 ?  296 LYS A O     1 
ATOM   2373  C  CB    . LYS A 1 296 ? 166.758 123.819 116.179 1.00 45.77 ?  296 LYS A CB    1 
ATOM   2374  C  CG    . LYS A 1 296 ? 167.948 123.714 115.241 1.00 45.88 ?  296 LYS A CG    1 
ATOM   2375  C  CD    . LYS A 1 296 ? 168.532 125.079 114.926 1.00 46.45 ?  296 LYS A CD    1 
ATOM   2376  C  CE    . LYS A 1 296 ? 169.871 124.948 114.217 1.00 45.56 ?  296 LYS A CE    1 
ATOM   2377  N  NZ    . LYS A 1 296 ? 170.337 126.248 113.661 1.00 46.99 1  296 LYS A NZ    1 
ATOM   2378  N  N     . ALA A 1 297 ? 165.629 123.038 118.855 1.00 46.02 ?  297 ALA A N     1 
ATOM   2379  C  CA    . ALA A 1 297 ? 164.762 123.258 120.004 1.00 44.58 ?  297 ALA A CA    1 
ATOM   2380  C  C     . ALA A 1 297 ? 164.223 124.682 119.967 1.00 44.70 ?  297 ALA A C     1 
ATOM   2381  O  O     . ALA A 1 297 ? 164.982 125.644 120.114 1.00 46.57 ?  297 ALA A O     1 
ATOM   2382  C  CB    . ALA A 1 297 ? 165.521 123.001 121.303 1.00 44.33 ?  297 ALA A CB    1 
ATOM   2383  N  N     . ALA A 1 298 ? 162.916 124.814 119.769 1.00 38.12 ?  298 ALA A N     1 
ATOM   2384  C  CA    . ALA A 1 298 ? 162.275 126.117 119.752 1.00 36.96 ?  298 ALA A CA    1 
ATOM   2385  C  C     . ALA A 1 298 ? 161.858 126.517 121.163 1.00 35.89 ?  298 ALA A C     1 
ATOM   2386  O  O     . ALA A 1 298 ? 161.819 125.703 122.086 1.00 36.72 ?  298 ALA A O     1 
ATOM   2387  C  CB    . ALA A 1 298 ? 161.067 126.111 118.817 1.00 36.58 ?  298 ALA A CB    1 
ATOM   2388  N  N     . TYR A 1 299 ? 161.544 127.799 121.324 1.00 35.49 ?  299 TYR A N     1 
ATOM   2389  C  CA    . TYR A 1 299 ? 161.131 128.342 122.609 1.00 28.47 ?  299 TYR A CA    1 
ATOM   2390  C  C     . TYR A 1 299 ? 159.874 129.175 122.425 1.00 31.38 ?  299 TYR A C     1 
ATOM   2391  O  O     . TYR A 1 299 ? 159.815 130.024 121.532 1.00 40.14 ?  299 TYR A O     1 
ATOM   2392  C  CB    . TYR A 1 299 ? 162.237 129.201 123.229 1.00 34.24 ?  299 TYR A CB    1 
ATOM   2393  C  CG    . TYR A 1 299 ? 163.307 128.407 123.937 1.00 37.70 ?  299 TYR A CG    1 
ATOM   2394  C  CD1   . TYR A 1 299 ? 163.149 128.022 125.258 1.00 35.43 ?  299 TYR A CD1   1 
ATOM   2395  C  CD2   . TYR A 1 299 ? 164.481 128.056 123.287 1.00 37.20 ?  299 TYR A CD2   1 
ATOM   2396  C  CE1   . TYR A 1 299 ? 164.124 127.303 125.912 1.00 35.26 ?  299 TYR A CE1   1 
ATOM   2397  C  CE2   . TYR A 1 299 ? 165.463 127.335 123.932 1.00 37.25 ?  299 TYR A CE2   1 
ATOM   2398  C  CZ    . TYR A 1 299 ? 165.279 126.961 125.245 1.00 40.47 ?  299 TYR A CZ    1 
ATOM   2399  O  OH    . TYR A 1 299 ? 166.252 126.242 125.898 1.00 45.23 ?  299 TYR A OH    1 
ATOM   2400  N  N     . VAL A 1 300 ? 158.878 128.929 123.257 1.00 31.06 ?  300 VAL A N     1 
ATOM   2401  C  CA    . VAL A 1 300 ? 157.737 129.826 123.378 1.00 24.27 ?  300 VAL A CA    1 
ATOM   2402  C  C     . VAL A 1 300 ? 158.031 130.793 124.513 1.00 29.18 ?  300 VAL A C     1 
ATOM   2403  O  O     . VAL A 1 300 ? 158.738 130.462 125.470 1.00 29.35 ?  300 VAL A O     1 
ATOM   2404  C  CB    . VAL A 1 300 ? 156.423 129.053 123.610 1.00 26.12 ?  300 VAL A CB    1 
ATOM   2405  C  CG1   . VAL A 1 300 ? 156.035 128.284 122.359 1.00 29.40 ?  300 VAL A CG1   1 
ATOM   2406  C  CG2   . VAL A 1 300 ? 156.555 128.118 124.798 1.00 29.28 ?  300 VAL A CG2   1 
ATOM   2407  N  N     . PHE A 1 301 ? 157.497 132.003 124.412 1.00 27.32 ?  301 PHE A N     1 
ATOM   2408  C  CA    . PHE A 1 301 ? 157.894 133.087 125.293 1.00 25.15 ?  301 PHE A CA    1 
ATOM   2409  C  C     . PHE A 1 301 ? 156.708 133.619 126.082 1.00 25.22 ?  301 PHE A C     1 
ATOM   2410  O  O     . PHE A 1 301 ? 155.556 133.529 125.649 1.00 31.04 ?  301 PHE A O     1 
ATOM   2411  C  CB    . PHE A 1 301 ? 158.537 134.226 124.500 1.00 27.97 ?  301 PHE A CB    1 
ATOM   2412  C  CG    . PHE A 1 301 ? 159.699 133.789 123.661 1.00 31.39 ?  301 PHE A CG    1 
ATOM   2413  C  CD1   . PHE A 1 301 ? 160.947 133.606 124.228 1.00 29.04 ?  301 PHE A CD1   1 
ATOM   2414  C  CD2   . PHE A 1 301 ? 159.542 133.551 122.309 1.00 26.23 ?  301 PHE A CD2   1 
ATOM   2415  C  CE1   . PHE A 1 301 ? 162.015 133.198 123.463 1.00 31.76 ?  301 PHE A CE1   1 
ATOM   2416  C  CE2   . PHE A 1 301 ? 160.607 133.144 121.540 1.00 28.48 ?  301 PHE A CE2   1 
ATOM   2417  C  CZ    . PHE A 1 301 ? 161.846 132.969 122.118 1.00 32.52 ?  301 PHE A CZ    1 
ATOM   2418  N  N     . TYR A 1 302 ? 157.013 134.167 127.256 1.00 26.97 ?  302 TYR A N     1 
ATOM   2419  C  CA    . TYR A 1 302 ? 156.022 134.847 128.074 1.00 27.45 ?  302 TYR A CA    1 
ATOM   2420  C  C     . TYR A 1 302 ? 155.927 136.285 127.590 1.00 30.56 ?  302 TYR A C     1 
ATOM   2421  O  O     . TYR A 1 302 ? 156.911 137.031 127.709 1.00 29.62 ?  302 TYR A O     1 
ATOM   2422  C  CB    . TYR A 1 302 ? 156.413 134.799 129.542 1.00 28.30 ?  302 TYR A CB    1 
ATOM   2423  C  CG    . TYR A 1 302 ? 156.281 133.432 130.176 1.00 26.25 ?  302 TYR A CG    1 
ATOM   2424  C  CD1   . TYR A 1 302 ? 157.160 132.409 129.855 1.00 27.65 ?  302 TYR A CD1   1 
ATOM   2425  C  CD2   . TYR A 1 302 ? 155.283 133.170 131.102 1.00 27.48 ?  302 TYR A CD2   1 
ATOM   2426  C  CE1   . TYR A 1 302 ? 157.044 131.162 130.431 1.00 30.31 ?  302 TYR A CE1   1 
ATOM   2427  C  CE2   . TYR A 1 302 ? 155.161 131.927 131.686 1.00 30.14 ?  302 TYR A CE2   1 
ATOM   2428  C  CZ    . TYR A 1 302 ? 156.045 130.927 131.348 1.00 33.71 ?  302 TYR A CZ    1 
ATOM   2429  O  OH    . TYR A 1 302 ? 155.926 129.686 131.927 1.00 37.78 ?  302 TYR A OH    1 
ATOM   2430  N  N     . PRO A 1 303 ? 154.793 136.715 127.034 1.00 29.03 ?  303 PRO A N     1 
ATOM   2431  C  CA    . PRO A 1 303 ? 154.734 138.051 126.416 1.00 24.96 ?  303 PRO A CA    1 
ATOM   2432  C  C     . PRO A 1 303 ? 155.009 139.192 127.376 1.00 27.56 ?  303 PRO A C     1 
ATOM   2433  O  O     . PRO A 1 303 ? 155.590 140.205 126.965 1.00 30.61 ?  303 PRO A O     1 
ATOM   2434  C  CB    . PRO A 1 303 ? 153.301 138.117 125.868 1.00 24.83 ?  303 PRO A CB    1 
ATOM   2435  C  CG    . PRO A 1 303 ? 152.859 136.708 125.779 1.00 24.18 ?  303 PRO A CG    1 
ATOM   2436  C  CD    . PRO A 1 303 ? 153.527 135.984 126.893 1.00 25.44 ?  303 PRO A CD    1 
ATOM   2437  N  N     . HIS A 1 304 ? 154.602 139.071 128.642 1.00 32.27 ?  304 HIS A N     1 
ATOM   2438  C  CA    . HIS A 1 304 ? 154.793 140.176 129.572 1.00 27.96 ?  304 HIS A CA    1 
ATOM   2439  C  C     . HIS A 1 304 ? 156.264 140.407 129.878 1.00 32.41 ?  304 HIS A C     1 
ATOM   2440  O  O     . HIS A 1 304 ? 156.681 141.554 130.054 1.00 40.50 ?  304 HIS A O     1 
ATOM   2441  C  CB    . HIS A 1 304 ? 154.022 139.933 130.866 1.00 29.89 ?  304 HIS A CB    1 
ATOM   2442  C  CG    . HIS A 1 304 ? 153.874 141.159 131.710 1.00 32.74 ?  304 HIS A CG    1 
ATOM   2443  N  ND1   . HIS A 1 304 ? 153.560 142.391 131.178 1.00 31.93 ?  304 HIS A ND1   1 
ATOM   2444  C  CD2   . HIS A 1 304 ? 154.005 141.348 133.044 1.00 35.88 ?  304 HIS A CD2   1 
ATOM   2445  C  CE1   . HIS A 1 304 ? 153.500 143.285 132.148 1.00 33.55 ?  304 HIS A CE1   1 
ATOM   2446  N  NE2   . HIS A 1 304 ? 153.765 142.678 133.290 1.00 34.35 ?  304 HIS A NE2   1 
ATOM   2447  N  N     . THR A 1 305 ? 157.062 139.341 129.947 1.00 25.74 ?  305 THR A N     1 
ATOM   2448  C  CA    . THR A 1 305 ? 158.496 139.512 130.151 1.00 29.41 ?  305 THR A CA    1 
ATOM   2449  C  C     . THR A 1 305 ? 159.132 140.256 128.984 1.00 28.69 ?  305 THR A C     1 
ATOM   2450  O  O     . THR A 1 305 ? 159.968 141.144 129.186 1.00 37.07 ?  305 THR A O     1 
ATOM   2451  C  CB    . THR A 1 305 ? 159.162 138.152 130.350 1.00 33.48 ?  305 THR A CB    1 
ATOM   2452  O  OG1   . THR A 1 305 ? 159.033 137.376 129.153 1.00 32.73 ?  305 THR A OG1   1 
ATOM   2453  C  CG2   . THR A 1 305 ? 158.506 137.412 131.500 1.00 30.50 ?  305 THR A CG2   1 
ATOM   2454  N  N     . ILE A 1 306 ? 158.737 139.917 127.756 1.00 32.69 ?  306 ILE A N     1 
ATOM   2455  C  CA    . ILE A 1 306 ? 159.261 140.615 126.587 1.00 28.02 ?  306 ILE A CA    1 
ATOM   2456  C  C     . ILE A 1 306 ? 158.833 142.076 126.601 1.00 29.49 ?  306 ILE A C     1 
ATOM   2457  O  O     . ILE A 1 306 ? 159.627 142.972 126.293 1.00 35.55 ?  306 ILE A O     1 
ATOM   2458  C  CB    . ILE A 1 306 ? 158.812 139.904 125.297 1.00 30.36 ?  306 ILE A CB    1 
ATOM   2459  C  CG1   . ILE A 1 306 ? 159.516 138.556 125.163 1.00 28.05 ?  306 ILE A CG1   1 
ATOM   2460  C  CG2   . ILE A 1 306 ? 159.093 140.767 124.078 1.00 30.85 ?  306 ILE A CG2   1 
ATOM   2461  C  CD1   . ILE A 1 306 ? 159.028 137.735 124.005 1.00 31.24 ?  306 ILE A CD1   1 
ATOM   2462  N  N     . TYR A 1 307 ? 157.574 142.343 126.950 1.00 33.59 ?  307 TYR A N     1 
ATOM   2463  C  CA    . TYR A 1 307 ? 157.101 143.723 126.995 1.00 31.54 ?  307 TYR A CA    1 
ATOM   2464  C  C     . TYR A 1 307 ? 157.833 144.527 128.061 1.00 35.23 ?  307 TYR A C     1 
ATOM   2465  O  O     . TYR A 1 307 ? 158.178 145.694 127.839 1.00 36.72 ?  307 TYR A O     1 
ATOM   2466  C  CB    . TYR A 1 307 ? 155.593 143.755 127.236 1.00 29.33 ?  307 TYR A CB    1 
ATOM   2467  C  CG    . TYR A 1 307 ? 155.006 145.146 127.202 1.00 33.59 ?  307 TYR A CG    1 
ATOM   2468  C  CD1   . TYR A 1 307 ? 154.674 145.747 125.997 1.00 29.32 ?  307 TYR A CD1   1 
ATOM   2469  C  CD2   . TYR A 1 307 ? 154.785 145.857 128.372 1.00 34.47 ?  307 TYR A CD2   1 
ATOM   2470  C  CE1   . TYR A 1 307 ? 154.140 147.017 125.958 1.00 33.46 ?  307 TYR A CE1   1 
ATOM   2471  C  CE2   . TYR A 1 307 ? 154.251 147.128 128.344 1.00 34.77 ?  307 TYR A CE2   1 
ATOM   2472  C  CZ    . TYR A 1 307 ? 153.930 147.703 127.133 1.00 35.97 ?  307 TYR A CZ    1 
ATOM   2473  O  OH    . TYR A 1 307 ? 153.398 148.970 127.099 1.00 38.80 ?  307 TYR A OH    1 
ATOM   2474  N  N     . LYS A 1 308 ? 158.070 143.927 129.230 1.00 35.92 ?  308 LYS A N     1 
ATOM   2475  C  CA    . LYS A 1 308 ? 158.801 144.617 130.287 1.00 33.02 ?  308 LYS A CA    1 
ATOM   2476  C  C     . LYS A 1 308 ? 160.245 144.878 129.882 1.00 32.74 ?  308 LYS A C     1 
ATOM   2477  O  O     . LYS A 1 308 ? 160.788 145.955 130.154 1.00 39.07 ?  308 LYS A O     1 
ATOM   2478  C  CB    . LYS A 1 308 ? 158.747 143.800 131.577 1.00 34.34 ?  308 LYS A CB    1 
ATOM   2479  C  CG    . LYS A 1 308 ? 157.393 143.813 132.265 1.00 34.02 ?  308 LYS A CG    1 
ATOM   2480  C  CD    . LYS A 1 308 ? 157.451 143.118 133.613 1.00 34.74 ?  308 LYS A CD    1 
ATOM   2481  C  CE    . LYS A 1 308 ? 158.030 141.718 133.494 1.00 38.99 ?  308 LYS A CE    1 
ATOM   2482  N  NZ    . LYS A 1 308 ? 157.060 140.675 133.927 1.00 36.46 1  308 LYS A NZ    1 
ATOM   2483  N  N     . GLU A 1 309 ? 160.882 143.907 129.228 1.00 30.34 ?  309 GLU A N     1 
ATOM   2484  C  CA    . GLU A 1 309 ? 162.294 144.041 128.892 1.00 35.08 ?  309 GLU A CA    1 
ATOM   2485  C  C     . GLU A 1 309 ? 162.522 145.008 127.735 1.00 36.49 ?  309 GLU A C     1 
ATOM   2486  O  O     . GLU A 1 309 ? 163.478 145.790 127.761 1.00 39.85 ?  309 GLU A O     1 
ATOM   2487  C  CB    . GLU A 1 309 ? 162.877 142.666 128.562 1.00 32.16 ?  309 GLU A CB    1 
ATOM   2488  C  CG    . GLU A 1 309 ? 164.276 142.705 127.986 1.00 36.68 ?  309 GLU A CG    1 
ATOM   2489  C  CD    . GLU A 1 309 ? 165.324 143.072 129.013 1.00 43.34 ?  309 GLU A CD    1 
ATOM   2490  O  OE1   . GLU A 1 309 ? 165.007 143.061 130.219 1.00 44.25 ?  309 GLU A OE1   1 
ATOM   2491  O  OE2   . GLU A 1 309 ? 166.468 143.373 128.612 1.00 42.50 -1 309 GLU A OE2   1 
ATOM   2492  N  N     . TYR A 1 310 ? 161.659 144.977 126.721 1.00 34.65 ?  310 TYR A N     1 
ATOM   2493  C  CA    . TYR A 1 310 ? 161.891 145.717 125.490 1.00 35.73 ?  310 TYR A CA    1 
ATOM   2494  C  C     . TYR A 1 310 ? 160.943 146.888 125.283 1.00 33.98 ?  310 TYR A C     1 
ATOM   2495  O  O     . TYR A 1 310 ? 161.204 147.722 124.411 1.00 35.70 ?  310 TYR A O     1 
ATOM   2496  C  CB    . TYR A 1 310 ? 161.790 144.771 124.284 1.00 34.26 ?  310 TYR A CB    1 
ATOM   2497  C  CG    . TYR A 1 310 ? 162.860 143.707 124.262 1.00 34.23 ?  310 TYR A CG    1 
ATOM   2498  C  CD1   . TYR A 1 310 ? 164.102 143.956 123.700 1.00 33.53 ?  310 TYR A CD1   1 
ATOM   2499  C  CD2   . TYR A 1 310 ? 162.630 142.455 124.815 1.00 32.13 ?  310 TYR A CD2   1 
ATOM   2500  C  CE1   . TYR A 1 310 ? 165.083 142.988 123.682 1.00 36.62 ?  310 TYR A CE1   1 
ATOM   2501  C  CE2   . TYR A 1 310 ? 163.605 141.482 124.803 1.00 33.39 ?  310 TYR A CE2   1 
ATOM   2502  C  CZ    . TYR A 1 310 ? 164.830 141.754 124.235 1.00 36.69 ?  310 TYR A CZ    1 
ATOM   2503  O  OH    . TYR A 1 310 ? 165.804 140.786 124.220 1.00 35.81 ?  310 TYR A OH    1 
ATOM   2504  N  N     . GLY A 1 311 ? 159.861 146.977 126.049 1.00 31.00 ?  311 GLY A N     1 
ATOM   2505  C  CA    . GLY A 1 311 ? 158.904 148.047 125.875 1.00 32.53 ?  311 GLY A CA    1 
ATOM   2506  C  C     . GLY A 1 311 ? 157.927 147.850 124.739 1.00 35.66 ?  311 GLY A C     1 
ATOM   2507  O  O     . GLY A 1 311 ? 157.086 148.728 124.509 1.00 39.25 ?  311 GLY A O     1 
ATOM   2508  N  N     . GLN A 1 312 ? 158.009 146.733 124.021 1.00 36.16 ?  312 GLN A N     1 
ATOM   2509  C  CA    . GLN A 1 312 ? 157.106 146.428 122.924 1.00 32.63 ?  312 GLN A CA    1 
ATOM   2510  C  C     . GLN A 1 312 ? 156.521 145.040 123.128 1.00 33.64 ?  312 GLN A C     1 
ATOM   2511  O  O     . GLN A 1 312 ? 157.134 144.179 123.762 1.00 38.49 ?  312 GLN A O     1 
ATOM   2512  C  CB    . GLN A 1 312 ? 157.819 146.490 121.567 1.00 32.24 ?  312 GLN A CB    1 
ATOM   2513  C  CG    . GLN A 1 312 ? 158.451 147.829 121.248 1.00 35.80 ?  312 GLN A CG    1 
ATOM   2514  C  CD    . GLN A 1 312 ? 159.738 147.688 120.461 1.00 40.31 ?  312 GLN A CD    1 
ATOM   2515  O  OE1   . GLN A 1 312 ? 159.737 147.743 119.231 1.00 39.60 ?  312 GLN A OE1   1 
ATOM   2516  N  NE2   . GLN A 1 312 ? 160.847 147.503 121.168 1.00 37.60 ?  312 GLN A NE2   1 
ATOM   2517  N  N     . HIS A 1 313 ? 155.325 144.834 122.586 1.00 30.44 ?  313 HIS A N     1 
ATOM   2518  C  CA    . HIS A 1 313 ? 154.716 143.516 122.615 1.00 28.09 ?  313 HIS A CA    1 
ATOM   2519  C  C     . HIS A 1 313 ? 155.494 142.557 121.718 1.00 32.02 ?  313 HIS A C     1 
ATOM   2520  O  O     . HIS A 1 313 ? 156.171 142.962 120.769 1.00 32.61 ?  313 HIS A O     1 
ATOM   2521  C  CB    . HIS A 1 313 ? 153.256 143.588 122.172 1.00 25.78 ?  313 HIS A CB    1 
ATOM   2522  C  CG    . HIS A 1 313 ? 152.389 144.404 123.081 1.00 31.16 ?  313 HIS A CG    1 
ATOM   2523  N  ND1   . HIS A 1 313 ? 151.949 143.942 124.301 1.00 29.95 ?  313 HIS A ND1   1 
ATOM   2524  C  CD2   . HIS A 1 313 ? 151.880 145.651 122.945 1.00 30.97 ?  313 HIS A CD2   1 
ATOM   2525  C  CE1   . HIS A 1 313 ? 151.205 144.868 124.878 1.00 29.39 ?  313 HIS A CE1   1 
ATOM   2526  N  NE2   . HIS A 1 313 ? 151.148 145.915 124.076 1.00 31.94 ?  313 HIS A NE2   1 
ATOM   2527  N  N     . MET A 1 314 ? 155.400 141.266 122.041 1.00 35.83 ?  314 MET A N     1 
ATOM   2528  C  CA    . MET A 1 314 ? 156.131 140.263 121.274 1.00 29.72 ?  314 MET A CA    1 
ATOM   2529  C  C     . MET A 1 314 ? 155.653 140.210 119.829 1.00 35.52 ?  314 MET A C     1 
ATOM   2530  O  O     . MET A 1 314 ? 156.467 140.120 118.902 1.00 38.07 ?  314 MET A O     1 
ATOM   2531  C  CB    . MET A 1 314 ? 155.992 138.890 121.930 1.00 27.22 ?  314 MET A CB    1 
ATOM   2532  C  CG    . MET A 1 314 ? 156.651 137.772 121.144 1.00 32.36 ?  314 MET A CG    1 
ATOM   2533  S  SD    . MET A 1 314 ? 156.494 136.140 121.891 1.00 41.78 ?  314 MET A SD    1 
ATOM   2534  C  CE    . MET A 1 314 ? 155.144 136.411 123.029 1.00 30.24 ?  314 MET A CE    1 
ATOM   2535  N  N     . ASP A 1 315 ? 154.339 140.268 119.613 1.00 33.93 ?  315 ASP A N     1 
ATOM   2536  C  CA    . ASP A 1 315 ? 153.804 140.192 118.260 1.00 38.13 ?  315 ASP A CA    1 
ATOM   2537  C  C     . ASP A 1 315 ? 153.996 141.482 117.476 1.00 31.39 ?  315 ASP A C     1 
ATOM   2538  O  O     . ASP A 1 315 ? 153.793 141.482 116.258 1.00 39.47 ?  315 ASP A O     1 
ATOM   2539  C  CB    . ASP A 1 315 ? 152.318 139.825 118.293 1.00 31.26 ?  315 ASP A CB    1 
ATOM   2540  C  CG    . ASP A 1 315 ? 151.517 140.727 119.201 1.00 35.74 ?  315 ASP A CG    1 
ATOM   2541  O  OD1   . ASP A 1 315 ? 152.101 141.269 120.160 1.00 39.29 ?  315 ASP A OD1   1 
ATOM   2542  O  OD2   . ASP A 1 315 ? 150.304 140.894 118.954 1.00 32.58 -1 315 ASP A OD2   1 
ATOM   2543  N  N     . GLU A 1 316 ? 154.377 142.572 118.135 1.00 24.36 ?  316 GLU A N     1 
ATOM   2544  C  CA    . GLU A 1 316 ? 154.736 143.803 117.446 1.00 28.82 ?  316 GLU A CA    1 
ATOM   2545  C  C     . GLU A 1 316 ? 156.195 143.827 117.015 1.00 33.83 ?  316 GLU A C     1 
ATOM   2546  O  O     . GLU A 1 316 ? 156.625 144.803 116.392 1.00 32.98 ?  316 GLU A O     1 
ATOM   2547  C  CB    . GLU A 1 316 ? 154.443 145.012 118.338 1.00 31.77 ?  316 GLU A CB    1 
ATOM   2548  C  CG    . GLU A 1 316 ? 152.973 145.202 118.656 1.00 31.04 ?  316 GLU A CG    1 
ATOM   2549  C  CD    . GLU A 1 316 ? 152.259 146.045 117.621 1.00 38.93 ?  316 GLU A CD    1 
ATOM   2550  O  OE1   . GLU A 1 316 ? 151.102 146.444 117.871 1.00 41.23 ?  316 GLU A OE1   1 
ATOM   2551  O  OE2   . GLU A 1 316 ? 152.854 146.311 116.557 1.00 41.62 -1 316 GLU A OE2   1 
ATOM   2552  N  N     . MET A 1 317 ? 156.958 142.788 117.333 1.00 39.09 ?  317 MET A N     1 
ATOM   2553  C  CA    . MET A 1 317 ? 158.370 142.701 117.003 1.00 35.78 ?  317 MET A CA    1 
ATOM   2554  C  C     . MET A 1 317 ? 158.597 141.622 115.953 1.00 34.44 ?  317 MET A C     1 
ATOM   2555  O  O     . MET A 1 317 ? 157.780 140.716 115.772 1.00 36.95 ?  317 MET A O     1 
ATOM   2556  C  CB    . MET A 1 317 ? 159.206 142.401 118.252 1.00 34.12 ?  317 MET A CB    1 
ATOM   2557  C  CG    . MET A 1 317 ? 159.087 143.448 119.345 1.00 34.36 ?  317 MET A CG    1 
ATOM   2558  S  SD    . MET A 1 317 ? 159.964 142.990 120.848 1.00 44.92 ?  317 MET A SD    1 
ATOM   2559  C  CE    . MET A 1 317 ? 161.419 144.021 120.715 1.00 38.89 ?  317 MET A CE    1 
ATOM   2560  N  N     . ASP A 1 318 ? 159.728 141.731 115.262 1.00 41.30 ?  318 ASP A N     1 
ATOM   2561  C  CA    . ASP A 1 318 ? 160.096 140.764 114.234 1.00 38.66 ?  318 ASP A CA    1 
ATOM   2562  C  C     . ASP A 1 318 ? 160.724 139.553 114.907 1.00 37.96 ?  318 ASP A C     1 
ATOM   2563  O  O     . ASP A 1 318 ? 161.814 139.645 115.476 1.00 41.69 ?  318 ASP A O     1 
ATOM   2564  C  CB    . ASP A 1 318 ? 161.056 141.394 113.230 1.00 36.96 ?  318 ASP A CB    1 
ATOM   2565  C  CG    . ASP A 1 318 ? 161.200 140.571 111.968 1.00 46.58 ?  318 ASP A CG    1 
ATOM   2566  O  OD1   . ASP A 1 318 ? 160.257 139.825 111.631 1.00 43.51 ?  318 ASP A OD1   1 
ATOM   2567  O  OD2   . ASP A 1 318 ? 162.258 140.668 111.313 1.00 49.50 -1 318 ASP A OD2   1 
ATOM   2568  N  N     . MET A 1 319 ? 160.036 138.411 114.844 1.00 34.59 ?  319 MET A N     1 
ATOM   2569  C  CA    . MET A 1 319 ? 160.561 137.213 115.488 1.00 35.93 ?  319 MET A CA    1 
ATOM   2570  C  C     . MET A 1 319 ? 161.786 136.672 114.764 1.00 33.84 ?  319 MET A C     1 
ATOM   2571  O  O     . MET A 1 319 ? 162.695 136.142 115.409 1.00 37.29 ?  319 MET A O     1 
ATOM   2572  C  CB    . MET A 1 319 ? 159.478 136.140 115.578 1.00 33.86 ?  319 MET A CB    1 
ATOM   2573  C  CG    . MET A 1 319 ? 159.853 134.980 116.478 1.00 35.19 ?  319 MET A CG    1 
ATOM   2574  S  SD    . MET A 1 319 ? 160.201 135.486 118.172 1.00 43.77 ?  319 MET A SD    1 
ATOM   2575  C  CE    . MET A 1 319 ? 158.544 135.692 118.811 1.00 36.00 ?  319 MET A CE    1 
ATOM   2576  N  N     . ASN A 1 320 ? 161.841 136.811 113.440 1.00 39.08 ?  320 ASN A N     1 
ATOM   2577  C  CA    . ASN A 1 320 ? 162.993 136.323 112.692 1.00 40.11 ?  320 ASN A CA    1 
ATOM   2578  C  C     . ASN A 1 320 ? 164.268 137.087 113.024 1.00 41.59 ?  320 ASN A C     1 
ATOM   2579  O  O     . ASN A 1 320 ? 165.362 136.606 112.707 1.00 41.30 ?  320 ASN A O     1 
ATOM   2580  C  CB    . ASN A 1 320 ? 162.710 136.395 111.192 1.00 42.00 ?  320 ASN A CB    1 
ATOM   2581  C  CG    . ASN A 1 320 ? 161.755 135.314 110.732 1.00 43.63 ?  320 ASN A CG    1 
ATOM   2582  O  OD1   . ASN A 1 320 ? 160.542 135.522 110.680 1.00 38.11 ?  320 ASN A OD1   1 
ATOM   2583  N  ND2   . ASN A 1 320 ? 162.297 134.151 110.393 1.00 40.53 ?  320 ASN A ND2   1 
ATOM   2584  N  N     . GLU A 1 321 ? 164.157 138.261 113.648 1.00 42.57 ?  321 GLU A N     1 
ATOM   2585  C  CA    . GLU A 1 321 ? 165.322 139.029 114.057 1.00 41.38 ?  321 GLU A CA    1 
ATOM   2586  C  C     . GLU A 1 321 ? 165.474 139.158 115.565 1.00 43.34 ?  321 GLU A C     1 
ATOM   2587  O  O     . GLU A 1 321 ? 166.558 139.521 116.029 1.00 46.03 ?  321 GLU A O     1 
ATOM   2588  C  CB    . GLU A 1 321 ? 165.279 140.434 113.434 1.00 41.68 ?  321 GLU A CB    1 
ATOM   2589  C  CG    . GLU A 1 321 ? 164.724 141.512 114.350 1.00 44.45 ?  321 GLU A CG    1 
ATOM   2590  C  CD    . GLU A 1 321 ? 164.323 142.770 113.605 1.00 47.32 ?  321 GLU A CD    1 
ATOM   2591  O  OE1   . GLU A 1 321 ? 164.174 142.708 112.367 1.00 47.11 ?  321 GLU A OE1   1 
ATOM   2592  O  OE2   . GLU A 1 321 ? 164.154 143.821 114.260 1.00 43.73 -1 321 GLU A OE2   1 
ATOM   2593  N  N     . MET A 1 322 ? 164.430 138.860 116.340 1.00 40.61 ?  322 MET A N     1 
ATOM   2594  C  CA    . MET A 1 322 ? 164.472 139.007 117.788 1.00 38.13 ?  322 MET A CA    1 
ATOM   2595  C  C     . MET A 1 322 ? 164.338 137.692 118.542 1.00 35.74 ?  322 MET A C     1 
ATOM   2596  O  O     . MET A 1 322 ? 164.378 137.706 119.774 1.00 41.25 ?  322 MET A O     1 
ATOM   2597  C  CB    . MET A 1 322 ? 163.377 139.972 118.261 1.00 37.48 ?  322 MET A CB    1 
ATOM   2598  C  CG    . MET A 1 322 ? 163.459 141.362 117.660 1.00 38.97 ?  322 MET A CG    1 
ATOM   2599  S  SD    . MET A 1 322 ? 164.603 142.462 118.517 1.00 48.56 ?  322 MET A SD    1 
ATOM   2600  C  CE    . MET A 1 322 ? 164.442 141.892 120.203 1.00 39.49 ?  322 MET A CE    1 
ATOM   2601  N  N     . TYR A 1 323 ? 164.165 136.563 117.851 1.00 33.93 ?  323 TYR A N     1 
ATOM   2602  C  CA    . TYR A 1 323 ? 164.016 135.289 118.548 1.00 32.83 ?  323 TYR A CA    1 
ATOM   2603  C  C     . TYR A 1 323 ? 165.281 134.935 119.319 1.00 36.92 ?  323 TYR A C     1 
ATOM   2604  O  O     . TYR A 1 323 ? 165.221 134.517 120.481 1.00 39.12 ?  323 TYR A O     1 
ATOM   2605  C  CB    . TYR A 1 323 ? 163.665 134.182 117.553 1.00 33.05 ?  323 TYR A CB    1 
ATOM   2606  C  CG    . TYR A 1 323 ? 163.696 132.793 118.149 1.00 34.69 ?  323 TYR A CG    1 
ATOM   2607  C  CD1   . TYR A 1 323 ? 162.601 132.285 118.831 1.00 33.75 ?  323 TYR A CD1   1 
ATOM   2608  C  CD2   . TYR A 1 323 ? 164.821 131.987 118.029 1.00 32.20 ?  323 TYR A CD2   1 
ATOM   2609  C  CE1   . TYR A 1 323 ? 162.625 131.019 119.378 1.00 32.07 ?  323 TYR A CE1   1 
ATOM   2610  C  CE2   . TYR A 1 323 ? 164.854 130.723 118.574 1.00 32.37 ?  323 TYR A CE2   1 
ATOM   2611  C  CZ    . TYR A 1 323 ? 163.755 130.243 119.246 1.00 31.69 ?  323 TYR A CZ    1 
ATOM   2612  O  OH    . TYR A 1 323 ? 163.787 128.982 119.789 1.00 31.64 ?  323 TYR A OH    1 
ATOM   2613  N  N     . ASP A 1 324 ? 166.441 135.101 118.683 1.00 38.72 ?  324 ASP A N     1 
ATOM   2614  C  CA    . ASP A 1 324 ? 167.701 134.802 119.350 1.00 35.27 ?  324 ASP A CA    1 
ATOM   2615  C  C     . ASP A 1 324 ? 167.951 135.757 120.508 1.00 40.31 ?  324 ASP A C     1 
ATOM   2616  O  O     . ASP A 1 324 ? 168.495 135.356 121.542 1.00 47.00 ?  324 ASP A O     1 
ATOM   2617  C  CB    . ASP A 1 324 ? 168.850 134.856 118.345 1.00 41.26 ?  324 ASP A CB    1 
ATOM   2618  C  CG    . ASP A 1 324 ? 168.749 133.776 117.289 1.00 44.72 ?  324 ASP A CG    1 
ATOM   2619  O  OD1   . ASP A 1 324 ? 168.585 132.594 117.659 1.00 41.76 ?  324 ASP A OD1   1 
ATOM   2620  O  OD2   . ASP A 1 324 ? 168.832 134.107 116.088 1.00 44.08 -1 324 ASP A OD2   1 
ATOM   2621  N  N     . LYS A 1 325 ? 167.570 137.026 120.350 1.00 38.81 ?  325 LYS A N     1 
ATOM   2622  C  CA    . LYS A 1 325 ? 167.703 137.978 121.447 1.00 35.53 ?  325 LYS A CA    1 
ATOM   2623  C  C     . LYS A 1 325 ? 166.803 137.603 122.617 1.00 38.86 ?  325 LYS A C     1 
ATOM   2624  O  O     . LYS A 1 325 ? 167.210 137.714 123.779 1.00 43.73 ?  325 LYS A O     1 
ATOM   2625  C  CB    . LYS A 1 325 ? 167.392 139.390 120.951 1.00 37.33 ?  325 LYS A CB    1 
ATOM   2626  C  CG    . LYS A 1 325 ? 168.366 139.896 119.903 1.00 37.87 ?  325 LYS A CG    1 
ATOM   2627  C  CD    . LYS A 1 325 ? 167.979 141.275 119.407 1.00 41.16 ?  325 LYS A CD    1 
ATOM   2628  C  CE    . LYS A 1 325 ? 168.906 141.739 118.296 1.00 42.11 ?  325 LYS A CE    1 
ATOM   2629  N  NZ    . LYS A 1 325 ? 168.356 142.913 117.566 1.00 43.60 1  325 LYS A NZ    1 
ATOM   2630  N  N     . PHE A 1 326 ? 165.575 137.161 122.333 1.00 39.16 ?  326 PHE A N     1 
ATOM   2631  C  CA    . PHE A 1 326 ? 164.684 136.704 123.393 1.00 33.41 ?  326 PHE A CA    1 
ATOM   2632  C  C     . PHE A 1 326 ? 165.256 135.486 124.103 1.00 36.37 ?  326 PHE A C     1 
ATOM   2633  O  O     . PHE A 1 326 ? 165.185 135.382 125.334 1.00 40.55 ?  326 PHE A O     1 
ATOM   2634  C  CB    . PHE A 1 326 ? 163.304 136.370 122.822 1.00 32.69 ?  326 PHE A CB    1 
ATOM   2635  C  CG    . PHE A 1 326 ? 162.568 137.550 122.259 1.00 35.56 ?  326 PHE A CG    1 
ATOM   2636  C  CD1   . PHE A 1 326 ? 162.925 138.842 122.598 1.00 35.09 ?  326 PHE A CD1   1 
ATOM   2637  C  CD2   . PHE A 1 326 ? 161.509 137.359 121.389 1.00 34.20 ?  326 PHE A CD2   1 
ATOM   2638  C  CE1   . PHE A 1 326 ? 162.241 139.919 122.076 1.00 33.20 ?  326 PHE A CE1   1 
ATOM   2639  C  CE2   . PHE A 1 326 ? 160.823 138.433 120.865 1.00 37.15 ?  326 PHE A CE2   1 
ATOM   2640  C  CZ    . PHE A 1 326 ? 161.190 139.715 121.209 1.00 38.91 ?  326 PHE A CZ    1 
ATOM   2641  N  N     . VAL A 1 327 ? 165.815 134.545 123.340 1.00 39.05 ?  327 VAL A N     1 
ATOM   2642  C  CA    . VAL A 1 327 ? 166.374 133.335 123.938 1.00 38.24 ?  327 VAL A CA    1 
ATOM   2643  C  C     . VAL A 1 327 ? 167.583 133.672 124.800 1.00 40.04 ?  327 VAL A C     1 
ATOM   2644  O  O     . VAL A 1 327 ? 167.733 133.155 125.914 1.00 45.64 ?  327 VAL A O     1 
ATOM   2645  C  CB    . VAL A 1 327 ? 166.721 132.315 122.838 1.00 36.91 ?  327 VAL A CB    1 
ATOM   2646  C  CG1   . VAL A 1 327 ? 167.561 131.184 123.404 1.00 40.92 ?  327 VAL A CG1   1 
ATOM   2647  C  CG2   . VAL A 1 327 ? 165.453 131.771 122.210 1.00 33.27 ?  327 VAL A CG2   1 
ATOM   2648  N  N     . ASP A 1 328 ? 168.459 134.549 124.309 1.00 38.45 ?  328 ASP A N     1 
ATOM   2649  C  CA    . ASP A 1 328 ? 169.660 134.920 125.045 1.00 36.87 ?  328 ASP A CA    1 
ATOM   2650  C  C     . ASP A 1 328 ? 169.377 135.855 126.211 1.00 40.52 ?  328 ASP A C     1 
ATOM   2651  O  O     . ASP A 1 328 ? 170.217 135.972 127.109 1.00 45.52 ?  328 ASP A O     1 
ATOM   2652  C  CB    . ASP A 1 328 ? 170.672 135.575 124.102 1.00 38.98 ?  328 ASP A CB    1 
ATOM   2653  C  CG    . ASP A 1 328 ? 171.155 134.631 123.024 1.00 44.83 ?  328 ASP A CG    1 
ATOM   2654  O  OD1   . ASP A 1 328 ? 171.029 133.403 123.207 1.00 48.01 ?  328 ASP A OD1   1 
ATOM   2655  O  OD2   . ASP A 1 328 ? 171.664 135.118 121.991 1.00 44.15 -1 328 ASP A OD2   1 
ATOM   2656  N  N     . ASN A 1 329 ? 168.228 136.521 126.218 1.00 41.66 ?  329 ASN A N     1 
ATOM   2657  C  CA    . ASN A 1 329 ? 167.914 137.470 127.279 1.00 38.80 ?  329 ASN A CA    1 
ATOM   2658  C  C     . ASN A 1 329 ? 167.533 136.722 128.549 1.00 42.53 ?  329 ASN A C     1 
ATOM   2659  O  O     . ASN A 1 329 ? 166.569 135.950 128.534 1.00 42.49 ?  329 ASN A O     1 
ATOM   2660  C  CB    . ASN A 1 329 ? 166.779 138.389 126.849 1.00 33.89 ?  329 ASN A CB    1 
ATOM   2661  C  CG    . ASN A 1 329 ? 166.723 139.667 127.659 1.00 40.78 ?  329 ASN A CG    1 
ATOM   2662  O  OD1   . ASN A 1 329 ? 166.673 139.636 128.887 1.00 45.18 ?  329 ASN A OD1   1 
ATOM   2663  N  ND2   . ASN A 1 329 ? 166.738 140.801 126.972 1.00 41.09 ?  329 ASN A ND2   1 
ATOM   2664  N  N     . PRO A 1 330 ? 168.254 136.911 129.658 1.00 44.27 ?  330 PRO A N     1 
ATOM   2665  C  CA    . PRO A 1 330 ? 167.858 136.235 130.902 1.00 40.96 ?  330 PRO A CA    1 
ATOM   2666  C  C     . PRO A 1 330 ? 166.574 136.782 131.500 1.00 39.46 ?  330 PRO A C     1 
ATOM   2667  O  O     . PRO A 1 330 ? 165.850 136.032 132.166 1.00 40.15 ?  330 PRO A O     1 
ATOM   2668  C  CB    . PRO A 1 330 ? 169.058 136.473 131.827 1.00 39.08 ?  330 PRO A CB    1 
ATOM   2669  C  CG    . PRO A 1 330 ? 169.685 137.717 131.305 1.00 36.96 ?  330 PRO A CG    1 
ATOM   2670  C  CD    . PRO A 1 330 ? 169.496 137.684 129.818 1.00 38.41 ?  330 PRO A CD    1 
ATOM   2671  N  N     . ARG A 1 331 ? 166.269 138.061 131.284 1.00 38.41 ?  331 ARG A N     1 
ATOM   2672  C  CA    . ARG A 1 331 ? 165.073 138.665 131.855 1.00 40.80 ?  331 ARG A CA    1 
ATOM   2673  C  C     . ARG A 1 331 ? 163.805 138.295 131.100 1.00 41.59 ?  331 ARG A C     1 
ATOM   2674  O  O     . ARG A 1 331 ? 162.706 138.533 131.612 1.00 40.35 ?  331 ARG A O     1 
ATOM   2675  C  CB    . ARG A 1 331 ? 165.227 140.187 131.900 1.00 39.81 ?  331 ARG A CB    1 
ATOM   2676  C  CG    . ARG A 1 331 ? 166.186 140.669 132.977 1.00 40.33 ?  331 ARG A CG    1 
ATOM   2677  C  CD    . ARG A 1 331 ? 166.756 142.036 132.645 1.00 42.11 ?  331 ARG A CD    1 
ATOM   2678  N  NE    . ARG A 1 331 ? 167.354 142.073 131.315 1.00 41.88 ?  331 ARG A NE    1 
ATOM   2679  C  CZ    . ARG A 1 331 ? 168.540 141.566 131.012 1.00 43.13 ?  331 ARG A CZ    1 
ATOM   2680  N  NH1   . ARG A 1 331 ? 169.299 140.984 131.925 1.00 42.61 1  331 ARG A NH1   1 
ATOM   2681  N  NH2   . ARG A 1 331 ? 168.978 141.648 129.759 1.00 43.39 ?  331 ARG A NH2   1 
ATOM   2682  N  N     . VAL A 1 332 ? 163.928 137.728 129.907 1.00 37.30 ?  332 VAL A N     1 
ATOM   2683  C  CA    . VAL A 1 332 ? 162.789 137.187 129.177 1.00 32.98 ?  332 VAL A CA    1 
ATOM   2684  C  C     . VAL A 1 332 ? 162.566 135.757 129.645 1.00 37.43 ?  332 VAL A C     1 
ATOM   2685  O  O     . VAL A 1 332 ? 163.514 134.970 129.735 1.00 38.83 ?  332 VAL A O     1 
ATOM   2686  C  CB    . VAL A 1 332 ? 163.028 137.245 127.659 1.00 33.47 ?  332 VAL A CB    1 
ATOM   2687  C  CG1   . VAL A 1 332 ? 161.965 136.454 126.918 1.00 33.96 ?  332 VAL A CG1   1 
ATOM   2688  C  CG2   . VAL A 1 332 ? 163.052 138.687 127.181 1.00 34.85 ?  332 VAL A CG2   1 
ATOM   2689  N  N     . LYS A 1 333 ? 161.321 135.424 129.971 1.00 35.97 ?  333 LYS A N     1 
ATOM   2690  C  CA    . LYS A 1 333 ? 160.974 134.072 130.386 1.00 29.96 ?  333 LYS A CA    1 
ATOM   2691  C  C     . LYS A 1 333 ? 160.522 133.273 129.171 1.00 32.69 ?  333 LYS A C     1 
ATOM   2692  O  O     . LYS A 1 333 ? 159.664 133.723 128.407 1.00 35.64 ?  333 LYS A O     1 
ATOM   2693  C  CB    . LYS A 1 333 ? 159.878 134.091 131.450 1.00 28.38 ?  333 LYS A CB    1 
ATOM   2694  C  CG    . LYS A 1 333 ? 159.817 132.833 132.297 1.00 34.79 ?  333 LYS A CG    1 
ATOM   2695  C  CD    . LYS A 1 333 ? 158.636 132.865 133.249 1.00 35.04 ?  333 LYS A CD    1 
ATOM   2696  C  CE    . LYS A 1 333 ? 158.434 131.518 133.925 1.00 37.13 ?  333 LYS A CE    1 
ATOM   2697  N  NZ    . LYS A 1 333 ? 157.272 131.525 134.857 1.00 37.74 1  333 LYS A NZ    1 
ATOM   2698  N  N     . LYS A 1 334 ? 161.108 132.093 128.995 1.00 38.85 ?  334 LYS A N     1 
ATOM   2699  C  CA    . LYS A 1 334 ? 160.828 131.258 127.838 1.00 34.29 ?  334 LYS A CA    1 
ATOM   2700  C  C     . LYS A 1 334 ? 160.643 129.816 128.282 1.00 36.06 ?  334 LYS A C     1 
ATOM   2701  O  O     . LYS A 1 334 ? 161.174 129.393 129.310 1.00 39.70 ?  334 LYS A O     1 
ATOM   2702  C  CB    . LYS A 1 334 ? 161.950 131.350 126.796 1.00 32.87 ?  334 LYS A CB    1 
ATOM   2703  C  CG    . LYS A 1 334 ? 163.265 130.750 127.249 1.00 35.31 ?  334 LYS A CG    1 
ATOM   2704  C  CD    . LYS A 1 334 ? 164.441 131.625 126.866 1.00 35.92 ?  334 LYS A CD    1 
ATOM   2705  C  CE    . LYS A 1 334 ? 164.363 132.974 127.546 1.00 38.84 ?  334 LYS A CE    1 
ATOM   2706  N  NZ    . LYS A 1 334 ? 165.619 133.752 127.398 1.00 39.45 1  334 LYS A NZ    1 
ATOM   2707  N  N     . GLU A 1 335 ? 159.872 129.068 127.497 1.00 38.00 ?  335 GLU A N     1 
ATOM   2708  C  CA    . GLU A 1 335 ? 159.632 127.654 127.735 1.00 36.54 ?  335 GLU A CA    1 
ATOM   2709  C  C     . GLU A 1 335 ? 160.071 126.852 126.518 1.00 36.29 ?  335 GLU A C     1 
ATOM   2710  O  O     . GLU A 1 335 ? 159.783 127.228 125.378 1.00 40.84 ?  335 GLU A O     1 
ATOM   2711  C  CB    . GLU A 1 335 ? 158.157 127.378 128.037 1.00 36.06 ?  335 GLU A CB    1 
ATOM   2712  C  CG    . GLU A 1 335 ? 157.936 126.407 129.182 1.00 38.94 ?  335 GLU A CG    1 
ATOM   2713  C  CD    . GLU A 1 335 ? 156.665 126.689 129.955 1.00 44.57 ?  335 GLU A CD    1 
ATOM   2714  O  OE1   . GLU A 1 335 ? 156.618 126.366 131.160 1.00 44.53 ?  335 GLU A OE1   1 
ATOM   2715  O  OE2   . GLU A 1 335 ? 155.710 127.226 129.357 1.00 42.08 -1 335 GLU A OE2   1 
ATOM   2716  N  N     . LYS A 1 336 ? 160.769 125.749 126.767 1.00 37.35 ?  336 LYS A N     1 
ATOM   2717  C  CA    . LYS A 1 336 ? 161.284 124.912 125.694 1.00 32.44 ?  336 LYS A CA    1 
ATOM   2718  C  C     . LYS A 1 336 ? 160.167 124.064 125.101 1.00 37.58 ?  336 LYS A C     1 
ATOM   2719  O  O     . LYS A 1 336 ? 159.405 123.424 125.832 1.00 40.53 ?  336 LYS A O     1 
ATOM   2720  C  CB    . LYS A 1 336 ? 162.407 124.019 126.218 1.00 38.26 ?  336 LYS A CB    1 
ATOM   2721  C  CG    . LYS A 1 336 ? 163.312 123.442 125.146 1.00 43.11 ?  336 LYS A CG    1 
ATOM   2722  C  CD    . LYS A 1 336 ? 164.308 122.471 125.759 1.00 41.37 ?  336 LYS A CD    1 
ATOM   2723  C  CE    . LYS A 1 336 ? 165.499 122.238 124.846 1.00 41.46 ?  336 LYS A CE    1 
ATOM   2724  N  NZ    . LYS A 1 336 ? 165.347 120.997 124.039 1.00 42.28 1  336 LYS A NZ    1 
ATOM   2725  N  N     . ILE A 1 337 ? 160.070 124.065 123.772 1.00 34.86 ?  337 ILE A N     1 
ATOM   2726  C  CA    . ILE A 1 337 ? 159.102 123.255 123.050 1.00 30.93 ?  337 ILE A CA    1 
ATOM   2727  C  C     . ILE A 1 337 ? 159.806 122.586 121.879 1.00 34.73 ?  337 ILE A C     1 
ATOM   2728  O  O     . ILE A 1 337 ? 160.896 122.985 121.467 1.00 42.14 ?  337 ILE A O     1 
ATOM   2729  C  CB    . ILE A 1 337 ? 157.895 124.076 122.545 1.00 32.72 ?  337 ILE A CB    1 
ATOM   2730  C  CG1   . ILE A 1 337 ? 158.370 125.239 121.673 1.00 35.14 ?  337 ILE A CG1   1 
ATOM   2731  C  CG2   . ILE A 1 337 ? 157.059 124.578 123.709 1.00 36.24 ?  337 ILE A CG2   1 
ATOM   2732  C  CD1   . ILE A 1 337 ? 157.541 125.444 120.431 1.00 32.24 ?  337 ILE A CD1   1 
ATOM   2733  N  N     . ASN A 1 338 ? 159.162 121.550 121.343 1.00 36.42 ?  338 ASN A N     1 
ATOM   2734  C  CA    . ASN A 1 338 ? 159.642 120.905 120.132 1.00 31.75 ?  338 ASN A CA    1 
ATOM   2735  C  C     . ASN A 1 338 ? 158.821 121.416 118.960 1.00 33.43 ?  338 ASN A C     1 
ATOM   2736  O  O     . ASN A 1 338 ? 157.624 121.107 118.877 1.00 36.67 ?  338 ASN A O     1 
ATOM   2737  C  CB    . ASN A 1 338 ? 159.533 119.387 120.242 1.00 33.95 ?  338 ASN A CB    1 
ATOM   2738  C  CG    . ASN A 1 338 ? 160.254 118.669 119.120 1.00 36.09 ?  338 ASN A CG    1 
ATOM   2739  O  OD1   . ASN A 1 338 ? 159.627 118.133 118.207 1.00 38.24 ?  338 ASN A OD1   1 
ATOM   2740  N  ND2   . ASN A 1 338 ? 161.580 118.657 119.181 1.00 35.46 ?  338 ASN A ND2   1 
ATOM   2741  N  N     . PRO A 1 339 ? 159.400 122.203 118.050 1.00 35.15 ?  339 PRO A N     1 
ATOM   2742  C  CA    . PRO A 1 339 ? 158.600 122.763 116.949 1.00 29.42 ?  339 PRO A CA    1 
ATOM   2743  C  C     . PRO A 1 339 ? 157.978 121.712 116.047 1.00 32.59 ?  339 PRO A C     1 
ATOM   2744  O  O     . PRO A 1 339 ? 156.859 121.915 115.562 1.00 37.75 ?  339 PRO A O     1 
ATOM   2745  C  CB    . PRO A 1 339 ? 159.611 123.634 116.191 1.00 33.56 ?  339 PRO A CB    1 
ATOM   2746  C  CG    . PRO A 1 339 ? 160.943 123.081 116.556 1.00 36.27 ?  339 PRO A CG    1 
ATOM   2747  C  CD    . PRO A 1 339 ? 160.817 122.589 117.962 1.00 36.81 ?  339 PRO A CD    1 
ATOM   2748  N  N     . ARG A 1 340 ? 158.664 120.593 115.806 1.00 35.29 ?  340 ARG A N     1 
ATOM   2749  C  CA    . ARG A 1 340 ? 158.075 119.535 114.991 1.00 28.41 ?  340 ARG A CA    1 
ATOM   2750  C  C     . ARG A 1 340 ? 156.922 118.858 115.720 1.00 30.40 ?  340 ARG A C     1 
ATOM   2751  O  O     . ARG A 1 340 ? 155.921 118.487 115.098 1.00 37.55 ?  340 ARG A O     1 
ATOM   2752  C  CB    . ARG A 1 340 ? 159.140 118.515 114.597 1.00 28.21 ?  340 ARG A CB    1 
ATOM   2753  C  CG    . ARG A 1 340 ? 160.060 119.002 113.499 1.00 29.17 ?  340 ARG A CG    1 
ATOM   2754  C  CD    . ARG A 1 340 ? 160.732 117.849 112.784 1.00 33.78 ?  340 ARG A CD    1 
ATOM   2755  N  NE    . ARG A 1 340 ? 161.750 118.320 111.854 1.00 35.44 ?  340 ARG A NE    1 
ATOM   2756  C  CZ    . ARG A 1 340 ? 162.500 117.529 111.101 1.00 32.17 ?  340 ARG A CZ    1 
ATOM   2757  N  NH1   . ARG A 1 340 ? 162.374 116.214 111.141 1.00 30.86 1  340 ARG A NH1   1 
ATOM   2758  N  NH2   . ARG A 1 340 ? 163.398 118.072 110.285 1.00 33.45 ?  340 ARG A NH2   1 
ATOM   2759  N  N     . LYS A 1 341 ? 157.042 118.690 117.037 1.00 32.09 ?  341 LYS A N     1 
ATOM   2760  C  CA    . LYS A 1 341 ? 155.925 118.162 117.812 1.00 30.76 ?  341 LYS A CA    1 
ATOM   2761  C  C     . LYS A 1 341 ? 154.738 119.115 117.771 1.00 33.23 ?  341 LYS A C     1 
ATOM   2762  O  O     . LYS A 1 341 ? 153.586 118.678 117.683 1.00 36.39 ?  341 LYS A O     1 
ATOM   2763  C  CB    . LYS A 1 341 ? 156.359 117.904 119.253 1.00 35.55 ?  341 LYS A CB    1 
ATOM   2764  C  CG    . LYS A 1 341 ? 156.330 116.442 119.653 1.00 35.82 ?  341 LYS A CG    1 
ATOM   2765  C  CD    . LYS A 1 341 ? 157.107 115.588 118.665 1.00 38.75 ?  341 LYS A CD    1 
ATOM   2766  C  CE    . LYS A 1 341 ? 157.195 114.145 119.134 1.00 41.67 ?  341 LYS A CE    1 
ATOM   2767  N  NZ    . LYS A 1 341 ? 158.293 113.952 120.121 1.00 36.89 1  341 LYS A NZ    1 
ATOM   2768  N  N     . LEU A 1 342 ? 155.000 120.422 117.829 1.00 30.62 ?  342 LEU A N     1 
ATOM   2769  C  CA    . LEU A 1 342 ? 153.923 121.399 117.715 1.00 27.32 ?  342 LEU A CA    1 
ATOM   2770  C  C     . LEU A 1 342 ? 153.272 121.345 116.338 1.00 29.90 ?  342 LEU A C     1 
ATOM   2771  O  O     . LEU A 1 342 ? 152.049 121.466 116.221 1.00 33.99 ?  342 LEU A O     1 
ATOM   2772  C  CB    . LEU A 1 342 ? 154.456 122.801 118.008 1.00 31.11 ?  342 LEU A CB    1 
ATOM   2773  C  CG    . LEU A 1 342 ? 153.423 123.891 118.299 1.00 30.19 ?  342 LEU A CG    1 
ATOM   2774  C  CD1   . LEU A 1 342 ? 152.295 123.342 119.153 1.00 28.04 ?  342 LEU A CD1   1 
ATOM   2775  C  CD2   . LEU A 1 342 ? 154.081 125.076 118.982 1.00 26.81 ?  342 LEU A CD2   1 
ATOM   2776  N  N     . LEU A 1 343 ? 154.073 121.167 115.285 1.00 31.54 ?  343 LEU A N     1 
ATOM   2777  C  CA    . LEU A 1 343 ? 153.517 121.036 113.942 1.00 25.59 ?  343 LEU A CA    1 
ATOM   2778  C  C     . LEU A 1 343 ? 152.653 119.786 113.819 1.00 26.60 ?  343 LEU A C     1 
ATOM   2779  O  O     . LEU A 1 343 ? 151.575 119.821 113.213 1.00 37.59 ?  343 LEU A O     1 
ATOM   2780  C  CB    . LEU A 1 343 ? 154.644 121.008 112.912 1.00 30.44 ?  343 LEU A CB    1 
ATOM   2781  C  CG    . LEU A 1 343 ? 154.918 122.296 112.137 1.00 29.59 ?  343 LEU A CG    1 
ATOM   2782  C  CD1   . LEU A 1 343 ? 155.933 122.041 111.039 1.00 25.32 ?  343 LEU A CD1   1 
ATOM   2783  C  CD2   . LEU A 1 343 ? 153.631 122.861 111.563 1.00 33.56 ?  343 LEU A CD2   1 
ATOM   2784  N  N     . GLU A 1 344 ? 153.120 118.669 114.378 1.00 33.26 ?  344 GLU A N     1 
ATOM   2785  C  CA    . GLU A 1 344 ? 152.330 117.443 114.356 1.00 33.22 ?  344 GLU A CA    1 
ATOM   2786  C  C     . GLU A 1 344 ? 151.037 117.610 115.144 1.00 31.00 ?  344 GLU A C     1 
ATOM   2787  O  O     . GLU A 1 344 ? 149.988 117.093 114.745 1.00 34.27 ?  344 GLU A O     1 
ATOM   2788  C  CB    . GLU A 1 344 ? 153.153 116.278 114.906 1.00 30.91 ?  344 GLU A CB    1 
ATOM   2789  C  CG    . GLU A 1 344 ? 154.339 115.895 114.034 1.00 34.30 ?  344 GLU A CG    1 
ATOM   2790  C  CD    . GLU A 1 344 ? 155.452 115.228 114.818 1.00 41.97 ?  344 GLU A CD    1 
ATOM   2791  O  OE1   . GLU A 1 344 ? 155.211 114.833 115.978 1.00 44.43 ?  344 GLU A OE1   1 
ATOM   2792  O  OE2   . GLU A 1 344 ? 156.569 115.100 114.275 1.00 38.74 -1 344 GLU A OE2   1 
ATOM   2793  N  N     . LYS A 1 345 ? 151.095 118.320 116.272 1.00 29.36 ?  345 LYS A N     1 
ATOM   2794  C  CA    . LYS A 1 345 ? 149.883 118.595 117.037 1.00 28.66 ?  345 LYS A CA    1 
ATOM   2795  C  C     . LYS A 1 345 ? 148.916 119.460 116.240 1.00 31.02 ?  345 LYS A C     1 
ATOM   2796  O  O     . LYS A 1 345 ? 147.701 119.237 116.278 1.00 36.42 ?  345 LYS A O     1 
ATOM   2797  C  CB    . LYS A 1 345 ? 150.240 119.266 118.362 1.00 29.68 ?  345 LYS A CB    1 
ATOM   2798  C  CG    . LYS A 1 345 ? 149.035 119.700 119.176 1.00 30.37 ?  345 LYS A CG    1 
ATOM   2799  C  CD    . LYS A 1 345 ? 149.438 120.140 120.570 1.00 32.15 ?  345 LYS A CD    1 
ATOM   2800  C  CE    . LYS A 1 345 ? 148.225 120.540 121.389 1.00 36.64 ?  345 LYS A CE    1 
ATOM   2801  N  NZ    . LYS A 1 345 ? 148.588 120.863 122.795 1.00 33.99 1  345 LYS A NZ    1 
ATOM   2802  N  N     . LEU A 1 346 ? 149.437 120.455 115.520 1.00 30.76 ?  346 LEU A N     1 
ATOM   2803  C  CA    . LEU A 1 346 ? 148.590 121.268 114.652 1.00 25.94 ?  346 LEU A CA    1 
ATOM   2804  C  C     . LEU A 1 346 ? 147.908 120.407 113.599 1.00 28.41 ?  346 LEU A C     1 
ATOM   2805  O  O     . LEU A 1 346 ? 146.703 120.537 113.357 1.00 29.87 ?  346 LEU A O     1 
ATOM   2806  C  CB    . LEU A 1 346 ? 149.421 122.364 113.982 1.00 27.27 ?  346 LEU A CB    1 
ATOM   2807  C  CG    . LEU A 1 346 ? 149.985 123.497 114.837 1.00 29.07 ?  346 LEU A CG    1 
ATOM   2808  C  CD1   . LEU A 1 346 ? 150.920 124.358 114.009 1.00 29.73 ?  346 LEU A CD1   1 
ATOM   2809  C  CD2   . LEU A 1 346 ? 148.871 124.333 115.417 1.00 29.79 ?  346 LEU A CD2   1 
ATOM   2810  N  N     . ALA A 1 347 ? 148.670 119.516 112.962 1.00 30.42 ?  347 ALA A N     1 
ATOM   2811  C  CA    . ALA A 1 347 ? 148.096 118.649 111.937 1.00 26.76 ?  347 ALA A CA    1 
ATOM   2812  C  C     . ALA A 1 347 ? 147.032 117.729 112.520 1.00 32.78 ?  347 ALA A C     1 
ATOM   2813  O  O     . ALA A 1 347 ? 145.970 117.537 111.918 1.00 34.48 ?  347 ALA A O     1 
ATOM   2814  C  CB    . ALA A 1 347 ? 149.196 117.834 111.260 1.00 28.67 ?  347 ALA A CB    1 
ATOM   2815  N  N     . MET A 1 348 ? 147.299 117.151 113.692 1.00 35.83 ?  348 MET A N     1 
ATOM   2816  C  CA    . MET A 1 348 ? 146.326 116.271 114.331 1.00 34.31 ?  348 MET A CA    1 
ATOM   2817  C  C     . MET A 1 348 ? 145.057 117.027 114.703 1.00 34.62 ?  348 MET A C     1 
ATOM   2818  O  O     . MET A 1 348 ? 143.944 116.518 114.522 1.00 39.98 ?  348 MET A O     1 
ATOM   2819  C  CB    . MET A 1 348 ? 146.951 115.620 115.566 1.00 35.33 ?  348 MET A CB    1 
ATOM   2820  C  CG    . MET A 1 348 ? 145.971 114.866 116.444 1.00 42.25 ?  348 MET A CG    1 
ATOM   2821  S  SD    . MET A 1 348 ? 145.766 115.633 118.063 1.00 54.03 ?  348 MET A SD    1 
ATOM   2822  C  CE    . MET A 1 348 ? 147.457 115.630 118.653 1.00 37.83 ?  348 MET A CE    1 
ATOM   2823  N  N     . LEU A 1 349 ? 145.205 118.246 115.224 1.00 30.71 ?  349 LEU A N     1 
ATOM   2824  C  CA    . LEU A 1 349 ? 144.043 119.044 115.597 1.00 28.89 ?  349 LEU A CA    1 
ATOM   2825  C  C     . LEU A 1 349 ? 143.226 119.439 114.374 1.00 24.96 ?  349 LEU A C     1 
ATOM   2826  O  O     . LEU A 1 349 ? 141.994 119.468 114.433 1.00 29.91 ?  349 LEU A O     1 
ATOM   2827  C  CB    . LEU A 1 349 ? 144.490 120.282 116.373 1.00 31.98 ?  349 LEU A CB    1 
ATOM   2828  C  CG    . LEU A 1 349 ? 143.485 120.848 117.375 1.00 32.78 ?  349 LEU A CG    1 
ATOM   2829  C  CD1   . LEU A 1 349 ? 143.292 119.890 118.538 1.00 35.13 ?  349 LEU A CD1   1 
ATOM   2830  C  CD2   . LEU A 1 349 ? 143.933 122.213 117.867 1.00 28.86 ?  349 LEU A CD2   1 
ATOM   2831  N  N     . ARG A 1 350 ? 143.892 119.761 113.263 1.00 27.26 ?  350 ARG A N     1 
ATOM   2832  C  CA    . ARG A 1 350 ? 143.153 120.075 112.043 1.00 26.52 ?  350 ARG A CA    1 
ATOM   2833  C  C     . ARG A 1 350 ? 142.467 118.842 111.472 1.00 31.57 ?  350 ARG A C     1 
ATOM   2834  O  O     . ARG A 1 350 ? 141.372 118.950 110.909 1.00 35.26 ?  350 ARG A O     1 
ATOM   2835  C  CB    . ARG A 1 350 ? 144.081 120.698 111.000 1.00 24.25 ?  350 ARG A CB    1 
ATOM   2836  C  CG    . ARG A 1 350 ? 144.772 121.967 111.459 1.00 27.97 ?  350 ARG A CG    1 
ATOM   2837  C  CD    . ARG A 1 350 ? 145.430 122.688 110.301 1.00 29.70 ?  350 ARG A CD    1 
ATOM   2838  N  NE    . ARG A 1 350 ? 144.543 123.697 109.737 1.00 36.09 ?  350 ARG A NE    1 
ATOM   2839  C  CZ    . ARG A 1 350 ? 144.382 123.916 108.441 1.00 34.03 ?  350 ARG A CZ    1 
ATOM   2840  N  NH1   . ARG A 1 350 ? 145.038 123.212 107.534 1.00 30.09 1  350 ARG A NH1   1 
ATOM   2841  N  NH2   . ARG A 1 350 ? 143.535 124.862 108.044 1.00 30.10 ?  350 ARG A NH2   1 
ATOM   2842  N  N     . SER A 1 351 ? 143.095 117.672 111.594 1.00 35.31 ?  351 SER A N     1 
ATOM   2843  C  CA    . SER A 1 351 ? 142.455 116.441 111.144 1.00 32.15 ?  351 SER A CA    1 
ATOM   2844  C  C     . SER A 1 351 ? 141.217 116.124 111.973 1.00 37.40 ?  351 SER A C     1 
ATOM   2845  O  O     . SER A 1 351 ? 140.186 115.715 111.429 1.00 43.54 ?  351 SER A O     1 
ATOM   2846  C  CB    . SER A 1 351 ? 143.449 115.283 111.205 1.00 34.90 ?  351 SER A CB    1 
ATOM   2847  O  OG    . SER A 1 351 ? 144.481 115.445 110.251 1.00 45.11 ?  351 SER A OG    1 
ATOM   2848  N  N     . GLU A 1 352 ? 141.299 116.305 113.290 1.00 34.86 ?  352 GLU A N     1 
ATOM   2849  C  CA    . GLU A 1 352 ? 140.208 115.908 114.170 1.00 32.54 ?  352 GLU A CA    1 
ATOM   2850  C  C     . GLU A 1 352 ? 139.115 116.962 114.304 1.00 37.94 ?  352 GLU A C     1 
ATOM   2851  O  O     . GLU A 1 352 ? 137.978 116.610 114.636 1.00 46.70 ?  352 GLU A O     1 
ATOM   2852  C  CB    . GLU A 1 352 ? 140.754 115.553 115.558 1.00 38.24 ?  352 GLU A CB    1 
ATOM   2853  C  CG    . GLU A 1 352 ? 140.812 116.711 116.537 1.00 41.92 ?  352 GLU A CG    1 
ATOM   2854  C  CD    . GLU A 1 352 ? 141.401 116.312 117.875 1.00 45.83 ?  352 GLU A CD    1 
ATOM   2855  O  OE1   . GLU A 1 352 ? 142.461 115.653 117.886 1.00 43.39 ?  352 GLU A OE1   1 
ATOM   2856  O  OE2   . GLU A 1 352 ? 140.803 116.657 118.916 1.00 46.21 -1 352 GLU A OE2   1 
ATOM   2857  N  N     . SER A 1 353 ? 139.419 118.238 114.061 1.00 35.27 ?  353 SER A N     1 
ATOM   2858  C  CA    . SER A 1 353 ? 138.426 119.292 114.232 1.00 36.63 ?  353 SER A CA    1 
ATOM   2859  C  C     . SER A 1 353 ? 138.421 120.347 113.137 1.00 32.80 ?  353 SER A C     1 
ATOM   2860  O  O     . SER A 1 353 ? 137.463 121.123 113.077 1.00 32.09 ?  353 SER A O     1 
ATOM   2861  C  CB    . SER A 1 353 ? 138.627 119.992 115.584 1.00 35.94 ?  353 SER A CB    1 
ATOM   2862  O  OG    . SER A 1 353 ? 139.889 120.632 115.644 1.00 33.36 ?  353 SER A OG    1 
ATOM   2863  N  N     . GLY A 1 354 ? 139.437 120.416 112.279 1.00 25.10 ?  354 GLY A N     1 
ATOM   2864  C  CA    . GLY A 1 354 ? 139.543 121.472 111.298 1.00 27.40 ?  354 GLY A CA    1 
ATOM   2865  C  C     . GLY A 1 354 ? 140.241 122.721 111.787 1.00 23.52 ?  354 GLY A C     1 
ATOM   2866  O  O     . GLY A 1 354 ? 140.500 123.623 110.980 1.00 29.14 ?  354 GLY A O     1 
ATOM   2867  N  N     . TYR A 1 355 ? 140.563 122.800 113.074 1.00 22.42 ?  355 TYR A N     1 
ATOM   2868  C  CA    . TYR A 1 355 ? 141.217 123.920 113.721 1.00 16.59 ?  355 TYR A CA    1 
ATOM   2869  C  C     . TYR A 1 355 ? 142.649 123.554 114.093 1.00 22.01 ?  355 TYR A C     1 
ATOM   2870  O  O     . TYR A 1 355 ? 142.958 122.378 114.292 1.00 27.95 ?  355 TYR A O     1 
ATOM   2871  C  CB    . TYR A 1 355 ? 140.455 124.344 114.982 1.00 23.87 ?  355 TYR A CB    1 
ATOM   2872  C  CG    . TYR A 1 355 ? 139.092 124.924 114.702 1.00 28.43 ?  355 TYR A CG    1 
ATOM   2873  C  CD1   . TYR A 1 355 ? 138.940 126.002 113.842 1.00 21.92 ?  355 TYR A CD1   1 
ATOM   2874  C  CD2   . TYR A 1 355 ? 137.956 124.393 115.295 1.00 30.32 ?  355 TYR A CD2   1 
ATOM   2875  C  CE1   . TYR A 1 355 ? 137.697 126.533 113.581 1.00 28.77 ?  355 TYR A CE1   1 
ATOM   2876  C  CE2   . TYR A 1 355 ? 136.708 124.919 115.040 1.00 26.19 ?  355 TYR A CE2   1 
ATOM   2877  C  CZ    . TYR A 1 355 ? 136.584 125.989 114.183 1.00 29.94 ?  355 TYR A CZ    1 
ATOM   2878  O  OH    . TYR A 1 355 ? 135.341 126.516 113.927 1.00 31.97 ?  355 TYR A OH    1 
ATOM   2879  N  N     . PRO A 1 356 ? 143.554 124.533 114.205 1.00 30.72 ?  356 PRO A N     1 
ATOM   2880  C  CA    . PRO A 1 356 ? 143.371 125.978 114.040 1.00 15.39 ?  356 PRO A CA    1 
ATOM   2881  C  C     . PRO A 1 356 ? 143.480 126.453 112.600 1.00 15.29 ?  356 PRO A C     1 
ATOM   2882  O  O     . PRO A 1 356 ? 143.947 125.730 111.727 1.00 24.86 ?  356 PRO A O     1 
ATOM   2883  C  CB    . PRO A 1 356 ? 144.506 126.548 114.892 1.00 17.74 ?  356 PRO A CB    1 
ATOM   2884  C  CG    . PRO A 1 356 ? 145.612 125.563 114.680 1.00 22.45 ?  356 PRO A CG    1 
ATOM   2885  C  CD    . PRO A 1 356 ? 144.941 124.211 114.583 1.00 19.53 ?  356 PRO A CD    1 
ATOM   2886  N  N     . TYR A 1 357 ? 143.033 127.676 112.329 1.00 24.77 ?  357 TYR A N     1 
ATOM   2887  C  CA    . TYR A 1 357 ? 143.430 128.352 111.107 1.00 12.22 ?  357 TYR A CA    1 
ATOM   2888  C  C     . TYR A 1 357 ? 144.927 128.615 111.156 1.00 13.71 ?  357 TYR A C     1 
ATOM   2889  O  O     . TYR A 1 357 ? 145.481 128.919 112.213 1.00 26.45 ?  357 TYR A O     1 
ATOM   2890  C  CB    . TYR A 1 357 ? 142.674 129.672 110.945 1.00 13.47 ?  357 TYR A CB    1 
ATOM   2891  C  CG    . TYR A 1 357 ? 141.175 129.579 111.105 1.00 15.80 ?  357 TYR A CG    1 
ATOM   2892  C  CD1   . TYR A 1 357 ? 140.488 128.428 110.760 1.00 17.54 ?  357 TYR A CD1   1 
ATOM   2893  C  CD2   . TYR A 1 357 ? 140.445 130.652 111.594 1.00 18.09 ?  357 TYR A CD2   1 
ATOM   2894  C  CE1   . TYR A 1 357 ? 139.120 128.341 110.898 1.00 20.23 ?  357 TYR A CE1   1 
ATOM   2895  C  CE2   . TYR A 1 357 ? 139.078 130.575 111.738 1.00 15.86 ?  357 TYR A CE2   1 
ATOM   2896  C  CZ    . TYR A 1 357 ? 138.420 129.418 111.387 1.00 19.73 ?  357 TYR A CZ    1 
ATOM   2897  O  OH    . TYR A 1 357 ? 137.054 129.335 111.527 1.00 28.22 ?  357 TYR A OH    1 
ATOM   2898  N  N     . ILE A 1 358 ? 145.590 128.490 110.014 1.00 16.22 ?  358 ILE A N     1 
ATOM   2899  C  CA    . ILE A 1 358 ? 147.032 128.680 109.928 1.00 22.30 ?  358 ILE A CA    1 
ATOM   2900  C  C     . ILE A 1 358 ? 147.296 129.953 109.141 1.00 18.25 ?  358 ILE A C     1 
ATOM   2901  O  O     . ILE A 1 358 ? 146.890 130.066 107.979 1.00 20.96 ?  358 ILE A O     1 
ATOM   2902  C  CB    . ILE A 1 358 ? 147.733 127.477 109.280 1.00 22.40 ?  358 ILE A CB    1 
ATOM   2903  C  CG1   . ILE A 1 358 ? 147.408 126.187 110.036 1.00 19.24 ?  358 ILE A CG1   1 
ATOM   2904  C  CG2   . ILE A 1 358 ? 149.234 127.704 109.227 1.00 16.40 ?  358 ILE A CG2   1 
ATOM   2905  C  CD1   . ILE A 1 358 ? 147.644 126.270 111.521 1.00 19.28 ?  358 ILE A CD1   1 
ATOM   2906  N  N     . MET A 1 359 ? 147.973 130.907 109.770 1.00 15.72 ?  359 MET A N     1 
ATOM   2907  C  CA    . MET A 1 359 ? 148.431 132.118 109.106 1.00 9.17  ?  359 MET A CA    1 
ATOM   2908  C  C     . MET A 1 359 ? 149.950 132.095 109.052 1.00 11.86 ?  359 MET A C     1 
ATOM   2909  O  O     . MET A 1 359 ? 150.609 132.036 110.094 1.00 21.73 ?  359 MET A O     1 
ATOM   2910  C  CB    . MET A 1 359 ? 147.942 133.373 109.829 1.00 11.58 ?  359 MET A CB    1 
ATOM   2911  C  CG    . MET A 1 359 ? 148.239 134.651 109.068 1.00 12.28 ?  359 MET A CG    1 
ATOM   2912  S  SD    . MET A 1 359 ? 147.870 136.145 109.996 1.00 30.94 ?  359 MET A SD    1 
ATOM   2913  C  CE    . MET A 1 359 ? 149.426 137.013 109.872 1.00 9.99  ?  359 MET A CE    1 
ATOM   2914  N  N     . PHE A 1 360 ? 150.499 132.144 107.844 1.00 12.36 ?  360 PHE A N     1 
ATOM   2915  C  CA    . PHE A 1 360 ? 151.943 132.217 107.652 1.00 10.56 ?  360 PHE A CA    1 
ATOM   2916  C  C     . PHE A 1 360 ? 152.321 133.691 107.651 1.00 14.38 ?  360 PHE A C     1 
ATOM   2917  O  O     . PHE A 1 360 ? 152.192 134.377 106.636 1.00 20.45 ?  360 PHE A O     1 
ATOM   2918  C  CB    . PHE A 1 360 ? 152.347 131.507 106.367 1.00 14.32 ?  360 PHE A CB    1 
ATOM   2919  C  CG    . PHE A 1 360 ? 152.054 130.036 106.382 1.00 19.70 ?  360 PHE A CG    1 
ATOM   2920  C  CD1   . PHE A 1 360 ? 152.610 129.216 107.348 1.00 19.15 ?  360 PHE A CD1   1 
ATOM   2921  C  CD2   . PHE A 1 360 ? 151.203 129.477 105.446 1.00 14.52 ?  360 PHE A CD2   1 
ATOM   2922  C  CE1   . PHE A 1 360 ? 152.335 127.866 107.371 1.00 19.62 ?  360 PHE A CE1   1 
ATOM   2923  C  CE2   . PHE A 1 360 ? 150.925 128.129 105.465 1.00 15.20 ?  360 PHE A CE2   1 
ATOM   2924  C  CZ    . PHE A 1 360 ? 151.490 127.322 106.428 1.00 17.18 ?  360 PHE A CZ    1 
ATOM   2925  N  N     . GLN A 1 361 ? 152.796 134.172 108.802 1.00 17.83 ?  361 GLN A N     1 
ATOM   2926  C  CA    . GLN A 1 361 ? 152.920 135.608 109.031 1.00 10.93 ?  361 GLN A CA    1 
ATOM   2927  C  C     . GLN A 1 361 ? 153.900 136.255 108.061 1.00 17.63 ?  361 GLN A C     1 
ATOM   2928  O  O     . GLN A 1 361 ? 153.643 137.349 107.547 1.00 22.44 ?  361 GLN A O     1 
ATOM   2929  C  CB    . GLN A 1 361 ? 153.342 135.859 110.477 1.00 19.39 ?  361 GLN A CB    1 
ATOM   2930  C  CG    . GLN A 1 361 ? 153.913 137.235 110.745 1.00 22.88 ?  361 GLN A CG    1 
ATOM   2931  C  CD    . GLN A 1 361 ? 153.292 137.884 111.962 1.00 22.79 ?  361 GLN A CD    1 
ATOM   2932  O  OE1   . GLN A 1 361 ? 153.229 137.284 113.033 1.00 24.42 ?  361 GLN A OE1   1 
ATOM   2933  N  NE2   . GLN A 1 361 ? 152.823 139.115 111.803 1.00 23.32 ?  361 GLN A NE2   1 
ATOM   2934  N  N     . ASP A 1 362 ? 155.032 135.601 107.798 1.00 25.25 ?  362 ASP A N     1 
ATOM   2935  C  CA    . ASP A 1 362 ? 156.003 136.170 106.873 1.00 18.40 ?  362 ASP A CA    1 
ATOM   2936  C  C     . ASP A 1 362 ? 155.554 136.067 105.423 1.00 17.69 ?  362 ASP A C     1 
ATOM   2937  O  O     . ASP A 1 362 ? 156.035 136.836 104.585 1.00 28.33 ?  362 ASP A O     1 
ATOM   2938  C  CB    . ASP A 1 362 ? 157.362 135.498 107.051 1.00 24.85 ?  362 ASP A CB    1 
ATOM   2939  C  CG    . ASP A 1 362 ? 157.971 135.777 108.408 1.00 31.03 ?  362 ASP A CG    1 
ATOM   2940  O  OD1   . ASP A 1 362 ? 157.356 135.404 109.428 1.00 29.17 ?  362 ASP A OD1   1 
ATOM   2941  O  OD2   . ASP A 1 362 ? 159.062 136.381 108.454 1.00 33.69 -1 362 ASP A OD2   1 
ATOM   2942  N  N     . ASN A 1 363 ? 154.655 135.134 105.106 1.00 24.62 ?  363 ASN A N     1 
ATOM   2943  C  CA    . ASN A 1 363 ? 154.059 135.112 103.775 1.00 14.12 ?  363 ASN A CA    1 
ATOM   2944  C  C     . ASN A 1 363 ? 153.120 136.293 103.583 1.00 18.06 ?  363 ASN A C     1 
ATOM   2945  O  O     . ASN A 1 363 ? 153.022 136.848 102.483 1.00 28.52 ?  363 ASN A O     1 
ATOM   2946  C  CB    . ASN A 1 363 ? 153.318 133.795 103.552 1.00 12.26 ?  363 ASN A CB    1 
ATOM   2947  C  CG    . ASN A 1 363 ? 154.232 132.682 103.095 1.00 18.23 ?  363 ASN A CG    1 
ATOM   2948  O  OD1   . ASN A 1 363 ? 155.360 132.924 102.673 1.00 21.41 ?  363 ASN A OD1   1 
ATOM   2949  N  ND2   . ASN A 1 363 ? 153.749 131.450 103.177 1.00 20.23 ?  363 ASN A ND2   1 
ATOM   2950  N  N     . VAL A 1 364 ? 152.414 136.682 104.644 1.00 14.61 ?  364 VAL A N     1 
ATOM   2951  C  CA    . VAL A 1 364 ? 151.525 137.835 104.570 1.00 9.24  ?  364 VAL A CA    1 
ATOM   2952  C  C     . VAL A 1 364 ? 152.323 139.128 104.480 1.00 16.15 ?  364 VAL A C     1 
ATOM   2953  O  O     . VAL A 1 364 ? 151.990 140.026 103.698 1.00 19.34 ?  364 VAL A O     1 
ATOM   2954  C  CB    . VAL A 1 364 ? 150.574 137.846 105.779 1.00 1.23  ?  364 VAL A CB    1 
ATOM   2955  C  CG1   . VAL A 1 364 ? 149.571 138.971 105.648 1.00 9.60  ?  364 VAL A CG1   1 
ATOM   2956  C  CG2   . VAL A 1 364 ? 149.876 136.510 105.914 1.00 6.84  ?  364 VAL A CG2   1 
ATOM   2957  N  N     . ASN A 1 365 ? 153.391 139.243 105.268 1.00 22.21 ?  365 ASN A N     1 
ATOM   2958  C  CA    . ASN A 1 365 ? 154.051 140.524 105.470 1.00 11.29 ?  365 ASN A CA    1 
ATOM   2959  C  C     . ASN A 1 365 ? 155.179 140.800 104.489 1.00 14.01 ?  365 ASN A C     1 
ATOM   2960  O  O     . ASN A 1 365 ? 155.608 141.953 104.378 1.00 23.15 ?  365 ASN A O     1 
ATOM   2961  C  CB    . ASN A 1 365 ? 154.591 140.615 106.899 1.00 17.60 ?  365 ASN A CB    1 
ATOM   2962  C  CG    . ASN A 1 365 ? 153.509 140.937 107.903 1.00 16.59 ?  365 ASN A CG    1 
ATOM   2963  O  OD1   . ASN A 1 365 ? 152.781 141.915 107.750 1.00 22.15 ?  365 ASN A OD1   1 
ATOM   2964  N  ND2   . ASN A 1 365 ? 153.395 140.115 108.935 1.00 15.77 ?  365 ASN A ND2   1 
ATOM   2965  N  N     . LYS A 1 366 ? 155.674 139.787 103.777 1.00 19.65 ?  366 LYS A N     1 
ATOM   2966  C  CA    . LYS A 1 366 ? 156.685 140.047 102.761 1.00 22.10 ?  366 LYS A CA    1 
ATOM   2967  C  C     . LYS A 1 366 ? 156.096 140.736 101.539 1.00 24.85 ?  366 LYS A C     1 
ATOM   2968  O  O     . LYS A 1 366 ? 156.832 141.383 100.788 1.00 30.20 ?  366 LYS A O     1 
ATOM   2969  C  CB    . LYS A 1 366 ? 157.381 138.747 102.354 1.00 18.14 ?  366 LYS A CB    1 
ATOM   2970  C  CG    . LYS A 1 366 ? 156.518 137.793 101.549 1.00 27.92 ?  366 LYS A CG    1 
ATOM   2971  C  CD    . LYS A 1 366 ? 157.375 136.840 100.734 1.00 29.61 ?  366 LYS A CD    1 
ATOM   2972  C  CE    . LYS A 1 366 ? 157.919 135.711 101.594 1.00 24.39 ?  366 LYS A CE    1 
ATOM   2973  N  NZ    . LYS A 1 366 ? 159.123 135.084 100.982 1.00 31.12 1  366 LYS A NZ    1 
ATOM   2974  N  N     . VAL A 1 367 ? 154.785 140.614 101.332 1.00 24.91 ?  367 VAL A N     1 
ATOM   2975  C  CA    . VAL A 1 367 ? 154.079 141.298 100.260 1.00 13.81 ?  367 VAL A CA    1 
ATOM   2976  C  C     . VAL A 1 367 ? 153.094 142.330 100.782 1.00 21.55 ?  367 VAL A C     1 
ATOM   2977  O  O     . VAL A 1 367 ? 152.404 142.970 99.984  1.00 26.26 ?  367 VAL A O     1 
ATOM   2978  C  CB    . VAL A 1 367 ? 153.359 140.294 99.337  1.00 16.64 ?  367 VAL A CB    1 
ATOM   2979  C  CG1   . VAL A 1 367 ? 154.350 139.639 98.396  1.00 22.54 ?  367 VAL A CG1   1 
ATOM   2980  C  CG2   . VAL A 1 367 ? 152.647 139.246 100.164 1.00 13.91 ?  367 VAL A CG2   1 
ATOM   2981  N  N     . HIS A 1 368 ? 153.004 142.505 102.099 1.00 21.75 ?  368 HIS A N     1 
ATOM   2982  C  CA    . HIS A 1 368 ? 152.078 143.464 102.682 1.00 9.89  ?  368 HIS A CA    1 
ATOM   2983  C  C     . HIS A 1 368 ? 152.466 144.883 102.286 1.00 14.33 ?  368 HIS A C     1 
ATOM   2984  O  O     . HIS A 1 368 ? 153.632 145.274 102.390 1.00 24.79 ?  368 HIS A O     1 
ATOM   2985  C  CB    . HIS A 1 368 ? 152.067 143.317 104.200 1.00 8.77  ?  368 HIS A CB    1 
ATOM   2986  C  CG    . HIS A 1 368 ? 151.100 144.224 104.892 1.00 10.72 ?  368 HIS A CG    1 
ATOM   2987  N  ND1   . HIS A 1 368 ? 151.312 144.699 106.167 1.00 18.69 ?  368 HIS A ND1   1 
ATOM   2988  C  CD2   . HIS A 1 368 ? 149.914 144.738 104.491 1.00 6.90  ?  368 HIS A CD2   1 
ATOM   2989  C  CE1   . HIS A 1 368 ? 150.300 145.468 106.522 1.00 16.05 ?  368 HIS A CE1   1 
ATOM   2990  N  NE2   . HIS A 1 368 ? 149.438 145.509 105.523 1.00 10.79 ?  368 HIS A NE2   1 
ATOM   2991  N  N     . ALA A 1 369 ? 151.480 145.656 101.833 1.00 18.19 ?  369 ALA A N     1 
ATOM   2992  C  CA    . ALA A 1 369 ? 151.740 146.985 101.299 1.00 9.05  ?  369 ALA A CA    1 
ATOM   2993  C  C     . ALA A 1 369 ? 151.785 148.067 102.367 1.00 20.16 ?  369 ALA A C     1 
ATOM   2994  O  O     . ALA A 1 369 ? 152.251 149.175 102.083 1.00 24.96 ?  369 ALA A O     1 
ATOM   2995  C  CB    . ALA A 1 369 ? 150.680 147.343 100.258 1.00 14.58 ?  369 ALA A CB    1 
ATOM   2996  N  N     . ASN A 1 370 ? 151.324 147.781 103.581 1.00 19.06 ?  370 ASN A N     1 
ATOM   2997  C  CA    . ASN A 1 370 ? 151.195 148.787 104.629 1.00 9.80  ?  370 ASN A CA    1 
ATOM   2998  C  C     . ASN A 1 370 ? 151.905 148.339 105.894 1.00 8.58  ?  370 ASN A C     1 
ATOM   2999  O  O     . ASN A 1 370 ? 151.374 148.433 107.002 1.00 18.09 ?  370 ASN A O     1 
ATOM   3000  C  CB    . ASN A 1 370 ? 149.727 149.086 104.913 1.00 10.11 ?  370 ASN A CB    1 
ATOM   3001  C  CG    . ASN A 1 370 ? 148.989 149.586 103.693 1.00 12.97 ?  370 ASN A CG    1 
ATOM   3002  O  OD1   . ASN A 1 370 ? 149.372 150.586 103.091 1.00 28.26 ?  370 ASN A OD1   1 
ATOM   3003  N  ND2   . ASN A 1 370 ? 147.925 148.890 103.319 1.00 13.93 ?  370 ASN A ND2   1 
ATOM   3004  N  N     . ASN A 1 371 ? 153.131 147.837 105.745 1.00 17.89 ?  371 ASN A N     1 
ATOM   3005  C  CA    . ASN A 1 371 ? 153.916 147.457 106.913 1.00 11.60 ?  371 ASN A CA    1 
ATOM   3006  C  C     . ASN A 1 371 ? 154.358 148.666 107.725 1.00 19.41 ?  371 ASN A C     1 
ATOM   3007  O  O     . ASN A 1 371 ? 154.676 148.517 108.909 1.00 22.71 ?  371 ASN A O     1 
ATOM   3008  C  CB    . ASN A 1 371 ? 155.139 146.644 106.490 1.00 6.17  ?  371 ASN A CB    1 
ATOM   3009  C  CG    . ASN A 1 371 ? 154.825 145.178 106.299 1.00 15.84 ?  371 ASN A CG    1 
ATOM   3010  O  OD1   . ASN A 1 371 ? 153.864 144.658 106.861 1.00 23.36 ?  371 ASN A OD1   1 
ATOM   3011  N  ND2   . ASN A 1 371 ? 155.637 144.501 105.500 1.00 18.12 ?  371 ASN A ND2   1 
ATOM   3012  N  N     . HIS A 1 372 ? 154.393 149.851 107.112 1.00 20.00 ?  372 HIS A N     1 
ATOM   3013  C  CA    . HIS A 1 372 ? 154.713 151.064 107.858 1.00 17.08 ?  372 HIS A CA    1 
ATOM   3014  C  C     . HIS A 1 372 ? 153.660 151.349 108.920 1.00 20.55 ?  372 HIS A C     1 
ATOM   3015  O  O     . HIS A 1 372 ? 153.992 151.757 110.039 1.00 30.06 ?  372 HIS A O     1 
ATOM   3016  C  CB    . HIS A 1 372 ? 154.848 152.245 106.898 1.00 18.82 ?  372 HIS A CB    1 
ATOM   3017  C  CG    . HIS A 1 372 ? 153.560 152.646 106.252 1.00 19.92 ?  372 HIS A CG    1 
ATOM   3018  N  ND1   . HIS A 1 372 ? 152.848 151.801 105.428 1.00 19.60 ?  372 HIS A ND1   1 
ATOM   3019  C  CD2   . HIS A 1 372 ? 152.847 153.795 106.318 1.00 23.20 ?  372 HIS A CD2   1 
ATOM   3020  C  CE1   . HIS A 1 372 ? 151.757 152.414 105.010 1.00 18.35 ?  372 HIS A CE1   1 
ATOM   3021  N  NE2   . HIS A 1 372 ? 151.732 153.625 105.535 1.00 23.99 ?  372 HIS A NE2   1 
ATOM   3022  N  N     . ILE A 1 373 ? 152.383 151.156 108.586 1.00 14.86 ?  373 ILE A N     1 
ATOM   3023  C  CA    . ILE A 1 373 ? 151.328 151.299 109.581 1.00 16.32 ?  373 ILE A CA    1 
ATOM   3024  C  C     . ILE A 1 373 ? 151.472 150.231 110.656 1.00 19.30 ?  373 ILE A C     1 
ATOM   3025  O  O     . ILE A 1 373 ? 151.505 150.532 111.855 1.00 29.97 ?  373 ILE A O     1 
ATOM   3026  C  CB    . ILE A 1 373 ? 149.944 151.235 108.907 1.00 17.88 ?  373 ILE A CB    1 
ATOM   3027  C  CG1   . ILE A 1 373 ? 149.792 152.362 107.886 1.00 16.77 ?  373 ILE A CG1   1 
ATOM   3028  C  CG2   . ILE A 1 373 ? 148.837 151.300 109.947 1.00 17.56 ?  373 ILE A CG2   1 
ATOM   3029  C  CD1   . ILE A 1 373 ? 148.602 152.198 106.972 1.00 13.85 ?  373 ILE A CD1   1 
ATOM   3030  N  N     . SER A 1 374 ? 151.589 148.975 110.238 1.00 20.52 ?  374 SER A N     1 
ATOM   3031  C  CA    . SER A 1 374 ? 151.726 147.830 111.126 1.00 12.72 ?  374 SER A CA    1 
ATOM   3032  C  C     . SER A 1 374 ? 151.898 146.587 110.268 1.00 15.89 ?  374 SER A C     1 
ATOM   3033  O  O     . SER A 1 374 ? 151.546 146.576 109.086 1.00 16.80 ?  374 SER A O     1 
ATOM   3034  C  CB    . SER A 1 374 ? 150.514 147.668 112.045 1.00 17.29 ?  374 SER A CB    1 
ATOM   3035  O  OG    . SER A 1 374 ? 150.730 146.643 112.993 1.00 25.82 ?  374 SER A OG    1 
ATOM   3036  N  N     . LYS A 1 375 ? 152.444 145.543 110.876 1.00 22.63 ?  375 LYS A N     1 
ATOM   3037  C  CA    . LYS A 1 375 ? 152.452 144.235 110.245 1.00 15.46 ?  375 LYS A CA    1 
ATOM   3038  C  C     . LYS A 1 375 ? 151.132 143.524 110.509 1.00 14.23 ?  375 LYS A C     1 
ATOM   3039  O  O     . LYS A 1 375 ? 150.458 143.773 111.513 1.00 25.63 ?  375 LYS A O     1 
ATOM   3040  C  CB    . LYS A 1 375 ? 153.611 143.387 110.766 1.00 11.70 ?  375 LYS A CB    1 
ATOM   3041  C  CG    . LYS A 1 375 ? 154.962 144.057 110.667 1.00 19.34 ?  375 LYS A CG    1 
ATOM   3042  C  CD    . LYS A 1 375 ? 155.852 143.333 109.679 1.00 19.61 ?  375 LYS A CD    1 
ATOM   3043  C  CE    . LYS A 1 375 ? 157.124 144.108 109.402 1.00 20.30 ?  375 LYS A CE    1 
ATOM   3044  N  NZ    . LYS A 1 375 ? 157.850 143.559 108.226 1.00 25.16 1  375 LYS A NZ    1 
ATOM   3045  N  N     . VAL A 1 376 ? 150.758 142.639 109.590 1.00 11.48 ?  376 VAL A N     1 
ATOM   3046  C  CA    . VAL A 1 376 ? 149.570 141.824 109.801 1.00 17.46 ?  376 VAL A CA    1 
ATOM   3047  C  C     . VAL A 1 376 ? 149.892 140.772 110.852 1.00 14.05 ?  376 VAL A C     1 
ATOM   3048  O  O     . VAL A 1 376 ? 150.823 139.975 110.690 1.00 20.12 ?  376 VAL A O     1 
ATOM   3049  C  CB    . VAL A 1 376 ? 149.101 141.182 108.490 1.00 12.52 ?  376 VAL A CB    1 
ATOM   3050  C  CG1   . VAL A 1 376 ? 147.822 140.399 108.717 1.00 13.55 ?  376 VAL A CG1   1 
ATOM   3051  C  CG2   . VAL A 1 376 ? 148.898 142.242 107.426 1.00 3.43  ?  376 VAL A CG2   1 
ATOM   3052  N  N     . LYS A 1 377 ? 149.128 140.771 111.943 1.00 17.05 ?  377 LYS A N     1 
ATOM   3053  C  CA    . LYS A 1 377 ? 149.382 139.865 113.052 1.00 10.87 ?  377 LYS A CA    1 
ATOM   3054  C  C     . LYS A 1 377 ? 148.349 138.764 113.194 1.00 11.62 ?  377 LYS A C     1 
ATOM   3055  O  O     . LYS A 1 377 ? 148.610 137.794 113.909 1.00 27.28 ?  377 LYS A O     1 
ATOM   3056  C  CB    . LYS A 1 377 ? 149.451 140.639 114.376 1.00 13.24 ?  377 LYS A CB    1 
ATOM   3057  C  CG    . LYS A 1 377 ? 150.306 141.885 114.334 1.00 11.59 ?  377 LYS A CG    1 
ATOM   3058  C  CD    . LYS A 1 377 ? 149.838 142.873 115.379 1.00 22.02 ?  377 LYS A CD    1 
ATOM   3059  C  CE    . LYS A 1 377 ? 150.015 144.297 114.914 1.00 18.69 ?  377 LYS A CE    1 
ATOM   3060  N  NZ    . LYS A 1 377 ? 149.299 145.251 115.801 1.00 20.26 1  377 LYS A NZ    1 
ATOM   3061  N  N     . PHE A 1 378 ? 147.191 138.891 112.556 1.00 13.99 ?  378 PHE A N     1 
ATOM   3062  C  CA    . PHE A 1 378 ? 146.164 137.864 112.638 1.00 7.50  ?  378 PHE A CA    1 
ATOM   3063  C  C     . PHE A 1 378 ? 145.174 138.067 111.503 1.00 10.29 ?  378 PHE A C     1 
ATOM   3064  O  O     . PHE A 1 378 ? 145.145 139.119 110.860 1.00 18.96 ?  378 PHE A O     1 
ATOM   3065  C  CB    . PHE A 1 378 ? 145.457 137.866 114.002 1.00 6.96  ?  378 PHE A CB    1 
ATOM   3066  C  CG    . PHE A 1 378 ? 144.585 139.067 114.257 1.00 6.75  ?  378 PHE A CG    1 
ATOM   3067  C  CD1   . PHE A 1 378 ? 145.071 140.354 114.102 1.00 10.61 ?  378 PHE A CD1   1 
ATOM   3068  C  CD2   . PHE A 1 378 ? 143.281 138.901 114.687 1.00 4.93  ?  378 PHE A CD2   1 
ATOM   3069  C  CE1   . PHE A 1 378 ? 144.271 141.445 114.351 1.00 8.34  ?  378 PHE A CE1   1 
ATOM   3070  C  CE2   . PHE A 1 378 ? 142.478 139.990 114.939 1.00 10.30 ?  378 PHE A CE2   1 
ATOM   3071  C  CZ    . PHE A 1 378 ? 142.975 141.263 114.772 1.00 8.75  ?  378 PHE A CZ    1 
ATOM   3072  N  N     . SER A 1 379 ? 144.374 137.038 111.260 1.00 5.32  ?  379 SER A N     1 
ATOM   3073  C  CA    . SER A 1 379 ? 143.360 137.048 110.222 1.00 7.81  ?  379 SER A CA    1 
ATOM   3074  C  C     . SER A 1 379 ? 141.979 137.123 110.865 1.00 8.33  ?  379 SER A C     1 
ATOM   3075  O  O     . SER A 1 379 ? 141.843 137.280 112.082 1.00 16.72 ?  379 SER A O     1 
ATOM   3076  C  CB    . SER A 1 379 ? 143.509 135.819 109.323 1.00 13.39 ?  379 SER A CB    1 
ATOM   3077  O  OG    . SER A 1 379 ? 143.068 136.101 108.010 1.00 14.39 ?  379 SER A OG    1 
ATOM   3078  N  N     . ASN A 1 380 ? 140.946 137.027 110.037 1.00 8.33  ?  380 ASN A N     1 
ATOM   3079  C  CA    . ASN A 1 380 ? 139.573 137.136 110.492 1.00 7.79  ?  380 ASN A CA    1 
ATOM   3080  C  C     . ASN A 1 380 ? 138.997 135.749 110.771 1.00 16.69 ?  380 ASN A C     1 
ATOM   3081  O  O     . ASN A 1 380 ? 139.706 134.739 110.762 1.00 19.66 ?  380 ASN A O     1 
ATOM   3082  C  CB    . ASN A 1 380 ? 138.739 137.903 109.466 1.00 10.47 ?  380 ASN A CB    1 
ATOM   3083  C  CG    . ASN A 1 380 ? 138.635 137.184 108.143 1.00 7.14  ?  380 ASN A CG    1 
ATOM   3084  O  OD1   . ASN A 1 380 ? 139.609 136.620 107.651 1.00 18.25 ?  380 ASN A OD1   1 
ATOM   3085  N  ND2   . ASN A 1 380 ? 137.448 137.202 107.556 1.00 14.30 ?  380 ASN A ND2   1 
ATOM   3086  N  N     . LEU A 1 381 ? 137.691 135.701 111.036 1.00 17.42 ?  381 LEU A N     1 
ATOM   3087  C  CA    . LEU A 1 381 ? 137.026 134.428 111.287 1.00 10.98 ?  381 LEU A CA    1 
ATOM   3088  C  C     . LEU A 1 381 ? 137.019 133.544 110.047 1.00 10.10 ?  381 LEU A C     1 
ATOM   3089  O  O     . LEU A 1 381 ? 137.054 132.314 110.164 1.00 20.39 ?  381 LEU A O     1 
ATOM   3090  C  CB    . LEU A 1 381 ? 135.603 134.682 111.783 1.00 12.55 ?  381 LEU A CB    1 
ATOM   3091  C  CG    . LEU A 1 381 ? 134.646 133.499 111.930 1.00 14.65 ?  381 LEU A CG    1 
ATOM   3092  C  CD1   . LEU A 1 381 ? 135.035 132.623 113.105 1.00 16.28 ?  381 LEU A CD1   1 
ATOM   3093  C  CD2   . LEU A 1 381 ? 133.225 134.003 112.080 1.00 17.94 ?  381 LEU A CD2   1 
ATOM   3094  N  N     . CYS A 1 382 ? 136.975 134.141 108.861 1.00 18.94 ?  382 CYS A N     1 
ATOM   3095  C  CA    . CYS A 1 382 ? 137.039 133.393 107.614 1.00 13.00 ?  382 CYS A CA    1 
ATOM   3096  C  C     . CYS A 1 382 ? 138.462 133.230 107.098 1.00 7.71  ?  382 CYS A C     1 
ATOM   3097  O  O     . CYS A 1 382 ? 138.659 132.596 106.058 1.00 17.19 ?  382 CYS A O     1 
ATOM   3098  C  CB    . CYS A 1 382 ? 136.170 134.068 106.550 1.00 20.13 ?  382 CYS A CB    1 
ATOM   3099  S  SG    . CYS A 1 382 ? 134.458 134.341 107.056 1.00 26.50 ?  382 CYS A SG    1 
ATOM   3100  N  N     . SER A 1 383 ? 139.448 133.794 107.798 1.00 15.62 ?  383 SER A N     1 
ATOM   3101  C  CA    . SER A 1 383 ? 140.867 133.551 107.532 1.00 10.49 ?  383 SER A CA    1 
ATOM   3102  C  C     . SER A 1 383 ? 141.290 134.060 106.156 1.00 12.80 ?  383 SER A C     1 
ATOM   3103  O  O     . SER A 1 383 ? 142.104 133.441 105.470 1.00 26.33 ?  383 SER A O     1 
ATOM   3104  C  CB    . SER A 1 383 ? 141.207 132.067 107.692 1.00 16.56 ?  383 SER A CB    1 
ATOM   3105  O  OG    . SER A 1 383 ? 142.592 131.833 107.524 1.00 24.81 ?  383 SER A OG    1 
ATOM   3106  N  N     . GLU A 1 384 ? 140.738 135.201 105.742 1.00 14.02 ?  384 GLU A N     1 
ATOM   3107  C  CA    . GLU A 1 384 ? 141.167 135.812 104.489 1.00 5.78  ?  384 GLU A CA    1 
ATOM   3108  C  C     . GLU A 1 384 ? 141.422 137.310 104.578 1.00 14.42 ?  384 GLU A C     1 
ATOM   3109  O  O     . GLU A 1 384 ? 142.057 137.854 103.672 1.00 20.38 ?  384 GLU A O     1 
ATOM   3110  C  CB    . GLU A 1 384 ? 140.144 135.533 103.374 1.00 9.03  ?  384 GLU A CB    1 
ATOM   3111  C  CG    . GLU A 1 384 ? 139.263 136.701 102.959 1.00 10.86 ?  384 GLU A CG    1 
ATOM   3112  C  CD    . GLU A 1 384 ? 138.130 136.960 103.924 1.00 21.19 ?  384 GLU A CD    1 
ATOM   3113  O  OE1   . GLU A 1 384 ? 137.798 136.050 104.708 1.00 14.47 ?  384 GLU A OE1   1 
ATOM   3114  O  OE2   . GLU A 1 384 ? 137.558 138.066 103.883 1.00 27.61 -1 384 GLU A OE2   1 
ATOM   3115  N  N     . VAL A 1 385 ? 140.980 137.990 105.630 1.00 17.24 ?  385 VAL A N     1 
ATOM   3116  C  CA    . VAL A 1 385 ? 141.255 139.411 105.804 1.00 5.14  ?  385 VAL A CA    1 
ATOM   3117  C  C     . VAL A 1 385 ? 142.633 139.554 106.434 1.00 15.31 ?  385 VAL A C     1 
ATOM   3118  O  O     . VAL A 1 385 ? 142.880 139.042 107.530 1.00 23.18 ?  385 VAL A O     1 
ATOM   3119  C  CB    . VAL A 1 385 ? 140.182 140.086 106.668 1.00 7.09  ?  385 VAL A CB    1 
ATOM   3120  C  CG1   . VAL A 1 385 ? 140.575 141.513 106.949 1.00 8.27  ?  385 VAL A CG1   1 
ATOM   3121  C  CG2   . VAL A 1 385 ? 138.843 140.037 105.976 1.00 7.56  ?  385 VAL A CG2   1 
ATOM   3122  N  N     . LEU A 1 386 ? 143.533 140.251 105.740 1.00 16.57 ?  386 LEU A N     1 
ATOM   3123  C  CA    . LEU A 1 386 ? 144.925 140.407 106.162 1.00 2.61  ?  386 LEU A CA    1 
ATOM   3124  C  C     . LEU A 1 386 ? 145.301 141.878 106.023 1.00 5.27  ?  386 LEU A C     1 
ATOM   3125  O  O     . LEU A 1 386 ? 145.775 142.311 104.971 1.00 11.88 ?  386 LEU A O     1 
ATOM   3126  C  CB    . LEU A 1 386 ? 145.839 139.508 105.343 1.00 2.13  ?  386 LEU A CB    1 
ATOM   3127  C  CG    . LEU A 1 386 ? 145.640 138.014 105.594 1.00 6.65  ?  386 LEU A CG    1 
ATOM   3128  C  CD1   . LEU A 1 386 ? 146.512 137.210 104.671 1.00 10.46 ?  386 LEU A CD1   1 
ATOM   3129  C  CD2   . LEU A 1 386 ? 145.940 137.676 107.041 1.00 13.82 ?  386 LEU A CD2   1 
ATOM   3130  N  N     . GLN A 1 387 ? 145.094 142.638 107.094 1.00 14.61 ?  387 GLN A N     1 
ATOM   3131  C  CA    . GLN A 1 387 ? 145.315 144.074 107.095 1.00 10.55 ?  387 GLN A CA    1 
ATOM   3132  C  C     . GLN A 1 387 ? 146.103 144.477 108.333 1.00 12.82 ?  387 GLN A C     1 
ATOM   3133  O  O     . GLN A 1 387 ? 146.142 143.760 109.334 1.00 25.68 ?  387 GLN A O     1 
ATOM   3134  C  CB    . GLN A 1 387 ? 143.988 144.842 107.048 1.00 3.94  ?  387 GLN A CB    1 
ATOM   3135  C  CG    . GLN A 1 387 ? 143.088 144.444 105.899 1.00 7.66  ?  387 GLN A CG    1 
ATOM   3136  C  CD    . GLN A 1 387 ? 141.822 145.259 105.848 1.00 9.54  ?  387 GLN A CD    1 
ATOM   3137  O  OE1   . GLN A 1 387 ? 141.713 146.294 106.500 1.00 26.99 ?  387 GLN A OE1   1 
ATOM   3138  N  NE2   . GLN A 1 387 ? 140.852 144.798 105.072 1.00 13.40 ?  387 GLN A NE2   1 
ATOM   3139  N  N     . ALA A 1 388 ? 146.744 145.638 108.245 1.00 12.69 ?  388 ALA A N     1 
ATOM   3140  C  CA    . ALA A 1 388 ? 147.486 146.174 109.376 1.00 10.57 ?  388 ALA A CA    1 
ATOM   3141  C  C     . ALA A 1 388 ? 146.531 146.644 110.466 1.00 13.36 ?  388 ALA A C     1 
ATOM   3142  O  O     . ALA A 1 388 ? 145.493 147.248 110.189 1.00 25.27 ?  388 ALA A O     1 
ATOM   3143  C  CB    . ALA A 1 388 ? 148.376 147.331 108.926 1.00 11.56 ?  388 ALA A CB    1 
ATOM   3144  N  N     . SER A 1 389 ? 146.886 146.358 111.715 1.00 19.36 ?  389 SER A N     1 
ATOM   3145  C  CA    . SER A 1 389 ? 146.094 146.770 112.862 1.00 13.85 ?  389 SER A CA    1 
ATOM   3146  C  C     . SER A 1 389 ? 146.998 147.374 113.922 1.00 15.70 ?  389 SER A C     1 
ATOM   3147  O  O     . SER A 1 389 ? 148.156 146.978 114.076 1.00 23.18 ?  389 SER A O     1 
ATOM   3148  C  CB    . SER A 1 389 ? 145.311 145.596 113.466 1.00 14.60 ?  389 SER A CB    1 
ATOM   3149  O  OG    . SER A 1 389 ? 146.159 144.494 113.731 1.00 25.24 ?  389 SER A OG    1 
ATOM   3150  N  N     . GLN A 1 390 ? 146.455 148.340 114.655 1.00 17.82 ?  390 GLN A N     1 
ATOM   3151  C  CA    . GLN A 1 390 ? 147.129 148.946 115.794 1.00 14.43 ?  390 GLN A CA    1 
ATOM   3152  C  C     . GLN A 1 390 ? 146.255 148.758 117.023 1.00 14.63 ?  390 GLN A C     1 
ATOM   3153  O  O     . GLN A 1 390 ? 145.064 149.081 116.995 1.00 27.28 ?  390 GLN A O     1 
ATOM   3154  C  CB    . GLN A 1 390 ? 147.406 150.429 115.549 1.00 17.79 ?  390 GLN A CB    1 
ATOM   3155  C  CG    . GLN A 1 390 ? 148.413 150.688 114.446 1.00 17.56 ?  390 GLN A CG    1 
ATOM   3156  C  CD    . GLN A 1 390 ? 148.521 152.153 114.085 1.00 22.86 ?  390 GLN A CD    1 
ATOM   3157  O  OE1   . GLN A 1 390 ? 147.729 152.977 114.541 1.00 31.19 ?  390 GLN A OE1   1 
ATOM   3158  N  NE2   . GLN A 1 390 ? 149.508 152.487 113.264 1.00 21.59 ?  390 GLN A NE2   1 
ATOM   3159  N  N     . VAL A 1 391 ? 146.845 148.229 118.094 1.00 23.96 ?  391 VAL A N     1 
ATOM   3160  C  CA    . VAL A 1 391 ? 146.071 147.921 119.289 1.00 24.92 ?  391 VAL A CA    1 
ATOM   3161  C  C     . VAL A 1 391 ? 145.637 149.210 119.977 1.00 25.86 ?  391 VAL A C     1 
ATOM   3162  O  O     . VAL A 1 391 ? 146.333 150.234 119.946 1.00 26.45 ?  391 VAL A O     1 
ATOM   3163  C  CB    . VAL A 1 391 ? 146.877 147.015 120.240 1.00 15.46 ?  391 VAL A CB    1 
ATOM   3164  C  CG1   . VAL A 1 391 ? 147.927 147.811 120.996 1.00 21.40 ?  391 VAL A CG1   1 
ATOM   3165  C  CG2   . VAL A 1 391 ? 145.950 146.294 121.202 1.00 16.26 ?  391 VAL A CG2   1 
ATOM   3166  N  N     . SER A 1 392 ? 144.454 149.169 120.578 1.00 28.22 ?  392 SER A N     1 
ATOM   3167  C  CA    . SER A 1 392 ? 143.938 150.288 121.345 1.00 18.16 ?  392 SER A CA    1 
ATOM   3168  C  C     . SER A 1 392 ? 144.374 150.176 122.801 1.00 27.95 ?  392 SER A C     1 
ATOM   3169  O  O     . SER A 1 392 ? 144.738 149.103 123.287 1.00 36.07 ?  392 SER A O     1 
ATOM   3170  C  CB    . SER A 1 392 ? 142.413 150.350 121.258 1.00 24.73 ?  392 SER A CB    1 
ATOM   3171  O  OG    . SER A 1 392 ? 141.986 150.618 119.935 1.00 33.95 ?  392 SER A OG    1 
ATOM   3172  N  N     . SER A 1 393 ? 144.336 151.306 123.496 1.00 33.60 ?  393 SER A N     1 
ATOM   3173  C  CA    . SER A 1 393 ? 144.678 151.376 124.913 1.00 31.95 ?  393 SER A CA    1 
ATOM   3174  C  C     . SER A 1 393 ? 143.451 151.902 125.649 1.00 32.73 ?  393 SER A C     1 
ATOM   3175  O  O     . SER A 1 393 ? 143.322 153.106 125.885 1.00 34.99 ?  393 SER A O     1 
ATOM   3176  C  CB    . SER A 1 393 ? 145.900 152.257 125.144 1.00 31.84 ?  393 SER A CB    1 
ATOM   3177  O  OG    . SER A 1 393 ? 146.690 151.762 126.210 1.00 39.31 ?  393 SER A OG    1 
ATOM   3178  N  N     . TYR A 1 394 ? 142.550 150.994 126.008 1.00 34.05 ?  394 TYR A N     1 
ATOM   3179  C  CA    . TYR A 1 394 ? 141.355 151.360 126.756 1.00 31.62 ?  394 TYR A CA    1 
ATOM   3180  C  C     . TYR A 1 394 ? 141.723 151.514 128.226 1.00 35.26 ?  394 TYR A C     1 
ATOM   3181  O  O     . TYR A 1 394 ? 142.148 150.550 128.872 1.00 37.43 ?  394 TYR A O     1 
ATOM   3182  C  CB    . TYR A 1 394 ? 140.262 150.314 126.567 1.00 28.57 ?  394 TYR A CB    1 
ATOM   3183  C  CG    . TYR A 1 394 ? 139.785 150.194 125.138 1.00 30.05 ?  394 TYR A CG    1 
ATOM   3184  C  CD1   . TYR A 1 394 ? 139.014 151.193 124.558 1.00 31.16 ?  394 TYR A CD1   1 
ATOM   3185  C  CD2   . TYR A 1 394 ? 140.110 149.089 124.367 1.00 31.12 ?  394 TYR A CD2   1 
ATOM   3186  C  CE1   . TYR A 1 394 ? 138.579 151.091 123.254 1.00 33.30 ?  394 TYR A CE1   1 
ATOM   3187  C  CE2   . TYR A 1 394 ? 139.678 148.976 123.063 1.00 30.57 ?  394 TYR A CE2   1 
ATOM   3188  C  CZ    . TYR A 1 394 ? 138.914 149.980 122.511 1.00 37.78 ?  394 TYR A CZ    1 
ATOM   3189  O  OH    . TYR A 1 394 ? 138.483 149.871 121.209 1.00 39.81 ?  394 TYR A OH    1 
ATOM   3190  N  N     . THR A 1 395 ? 141.567 152.723 128.746 1.00 34.33 ?  395 THR A N     1 
ATOM   3191  C  CA    . THR A 1 395 ? 142.004 153.077 130.084 1.00 36.56 ?  395 THR A CA    1 
ATOM   3192  C  C     . THR A 1 395 ? 140.820 153.042 131.047 1.00 37.82 ?  395 THR A C     1 
ATOM   3193  O  O     . THR A 1 395 ? 139.730 152.564 130.714 1.00 34.94 ?  395 THR A O     1 
ATOM   3194  C  CB    . THR A 1 395 ? 142.679 154.449 130.054 1.00 35.93 ?  395 THR A CB    1 
ATOM   3195  O  OG1   . THR A 1 395 ? 141.761 155.421 129.540 1.00 37.71 ?  395 THR A OG1   1 
ATOM   3196  C  CG2   . THR A 1 395 ? 143.906 154.408 129.162 1.00 34.69 ?  395 THR A CG2   1 
ATOM   3197  N  N     . ASP A 1 396 ? 141.037 153.537 132.264 1.00 39.46 ?  396 ASP A N     1 
ATOM   3198  C  CA    . ASP A 1 396 ? 139.979 153.596 133.259 1.00 35.04 ?  396 ASP A CA    1 
ATOM   3199  C  C     . ASP A 1 396 ? 138.829 154.475 132.768 1.00 37.72 ?  396 ASP A C     1 
ATOM   3200  O  O     . ASP A 1 396 ? 138.928 155.181 131.763 1.00 43.75 ?  396 ASP A O     1 
ATOM   3201  C  CB    . ASP A 1 396 ? 140.521 154.123 134.586 1.00 37.84 ?  396 ASP A CB    1 
ATOM   3202  C  CG    . ASP A 1 396 ? 141.566 153.209 135.194 1.00 43.06 ?  396 ASP A CG    1 
ATOM   3203  O  OD1   . ASP A 1 396 ? 141.294 151.997 135.321 1.00 40.24 ?  396 ASP A OD1   1 
ATOM   3204  O  OD2   . ASP A 1 396 ? 142.656 153.701 135.550 1.00 44.39 -1 396 ASP A OD2   1 
ATOM   3205  N  N     . TYR A 1 397 ? 137.717 154.416 133.505 1.00 35.15 ?  397 TYR A N     1 
ATOM   3206  C  CA    . TYR A 1 397 ? 136.512 155.129 133.090 1.00 35.34 ?  397 TYR A CA    1 
ATOM   3207  C  C     . TYR A 1 397 ? 136.753 156.630 133.002 1.00 36.99 ?  397 TYR A C     1 
ATOM   3208  O  O     . TYR A 1 397 ? 136.298 157.284 132.056 1.00 41.13 ?  397 TYR A O     1 
ATOM   3209  C  CB    . TYR A 1 397 ? 135.368 154.827 134.057 1.00 30.96 ?  397 TYR A CB    1 
ATOM   3210  C  CG    . TYR A 1 397 ? 134.059 155.476 133.674 1.00 33.12 ?  397 TYR A CG    1 
ATOM   3211  C  CD1   . TYR A 1 397 ? 133.188 154.856 132.790 1.00 33.56 ?  397 TYR A CD1   1 
ATOM   3212  C  CD2   . TYR A 1 397 ? 133.698 156.713 134.191 1.00 34.28 ?  397 TYR A CD2   1 
ATOM   3213  C  CE1   . TYR A 1 397 ? 131.995 155.448 132.434 1.00 29.73 ?  397 TYR A CE1   1 
ATOM   3214  C  CE2   . TYR A 1 397 ? 132.508 157.312 133.840 1.00 33.91 ?  397 TYR A CE2   1 
ATOM   3215  C  CZ    . TYR A 1 397 ? 131.660 156.675 132.963 1.00 34.95 ?  397 TYR A CZ    1 
ATOM   3216  O  OH    . TYR A 1 397 ? 130.472 157.270 132.612 1.00 39.62 ?  397 TYR A OH    1 
ATOM   3217  N  N     . ASP A 1 398 ? 137.467 157.193 133.972 1.00 40.12 ?  398 ASP A N     1 
ATOM   3218  C  CA    . ASP A 1 398 ? 137.696 158.630 134.016 1.00 39.48 ?  398 ASP A CA    1 
ATOM   3219  C  C     . ASP A 1 398 ? 138.724 159.109 132.999 1.00 45.32 ?  398 ASP A C     1 
ATOM   3220  O  O     . ASP A 1 398 ? 138.770 160.309 132.713 1.00 46.74 ?  398 ASP A O     1 
ATOM   3221  C  CB    . ASP A 1 398 ? 138.139 159.043 135.421 1.00 43.35 ?  398 ASP A CB    1 
ATOM   3222  C  CG    . ASP A 1 398 ? 139.065 158.025 136.062 1.00 46.91 ?  398 ASP A CG    1 
ATOM   3223  O  OD1   . ASP A 1 398 ? 138.603 156.904 136.354 1.00 43.86 ?  398 ASP A OD1   1 
ATOM   3224  O  OD2   . ASP A 1 398 ? 140.254 158.346 136.272 1.00 45.84 -1 398 ASP A OD2   1 
ATOM   3225  N  N     . GLU A 1 399 ? 139.539 158.215 132.451 1.00 46.09 ?  399 GLU A N     1 
ATOM   3226  C  CA    . GLU A 1 399 ? 140.625 158.590 131.558 1.00 42.81 ?  399 GLU A CA    1 
ATOM   3227  C  C     . GLU A 1 399 ? 140.221 158.413 130.100 1.00 45.49 ?  399 GLU A C     1 
ATOM   3228  O  O     . GLU A 1 399 ? 139.319 157.642 129.763 1.00 45.00 ?  399 GLU A O     1 
ATOM   3229  C  CB    . GLU A 1 399 ? 141.876 157.761 131.853 1.00 42.35 ?  399 GLU A CB    1 
ATOM   3230  C  CG    . GLU A 1 399 ? 141.993 157.300 133.291 1.00 44.59 ?  399 GLU A CG    1 
ATOM   3231  C  CD    . GLU A 1 399 ? 143.375 156.778 133.622 1.00 50.14 ?  399 GLU A CD    1 
ATOM   3232  O  OE1   . GLU A 1 399 ? 143.694 155.639 133.218 1.00 46.87 ?  399 GLU A OE1   1 
ATOM   3233  O  OE2   . GLU A 1 399 ? 144.143 157.503 134.288 1.00 49.31 -1 399 GLU A OE2   1 
ATOM   3234  N  N     . GLU A 1 400 ? 140.909 159.150 129.232 1.00 43.20 ?  400 GLU A N     1 
ATOM   3235  C  CA    . GLU A 1 400 ? 140.684 159.037 127.799 1.00 40.44 ?  400 GLU A CA    1 
ATOM   3236  C  C     . GLU A 1 400 ? 141.349 157.780 127.252 1.00 41.95 ?  400 GLU A C     1 
ATOM   3237  O  O     . GLU A 1 400 ? 142.425 157.380 127.701 1.00 41.73 ?  400 GLU A O     1 
ATOM   3238  C  CB    . GLU A 1 400 ? 141.223 160.271 127.077 1.00 40.61 ?  400 GLU A CB    1 
ATOM   3239  C  CG    . GLU A 1 400 ? 140.341 161.500 127.201 1.00 44.10 ?  400 GLU A CG    1 
ATOM   3240  C  CD    . GLU A 1 400 ? 139.338 161.613 126.070 1.00 49.46 ?  400 GLU A CD    1 
ATOM   3241  O  OE1   . GLU A 1 400 ? 138.235 162.149 126.304 1.00 45.54 ?  400 GLU A OE1   1 
ATOM   3242  O  OE2   . GLU A 1 400 ? 139.651 161.166 124.948 1.00 49.57 -1 400 GLU A OE2   1 
ATOM   3243  N  N     . ASP A 1 401 ? 140.699 157.157 126.273 1.00 39.60 ?  401 ASP A N     1 
ATOM   3244  C  CA    . ASP A 1 401 ? 141.214 155.946 125.655 1.00 36.96 ?  401 ASP A CA    1 
ATOM   3245  C  C     . ASP A 1 401 ? 142.028 156.286 124.415 1.00 37.21 ?  401 ASP A C     1 
ATOM   3246  O  O     . ASP A 1 401 ? 141.688 157.206 123.666 1.00 39.03 ?  401 ASP A O     1 
ATOM   3247  C  CB    . ASP A 1 401 ? 140.072 155.003 125.277 1.00 35.70 ?  401 ASP A CB    1 
ATOM   3248  C  CG    . ASP A 1 401 ? 139.205 154.632 126.462 1.00 39.29 ?  401 ASP A CG    1 
ATOM   3249  O  OD1   . ASP A 1 401 ? 139.723 154.611 127.597 1.00 41.78 ?  401 ASP A OD1   1 
ATOM   3250  O  OD2   . ASP A 1 401 ? 138.006 154.356 126.256 1.00 40.69 -1 401 ASP A OD2   1 
ATOM   3251  N  N     . GLU A 1 402 ? 143.109 155.540 124.207 1.00 33.55 ?  402 GLU A N     1 
ATOM   3252  C  CA    . GLU A 1 402 ? 143.905 155.640 122.989 1.00 32.92 ?  402 GLU A CA    1 
ATOM   3253  C  C     . GLU A 1 402 ? 143.344 154.647 121.980 1.00 31.86 ?  402 GLU A C     1 
ATOM   3254  O  O     . GLU A 1 402 ? 143.551 153.437 122.108 1.00 39.81 ?  402 GLU A O     1 
ATOM   3255  C  CB    . GLU A 1 402 ? 145.379 155.364 123.276 1.00 36.93 ?  402 GLU A CB    1 
ATOM   3256  C  CG    . GLU A 1 402 ? 146.037 156.380 124.190 1.00 36.37 ?  402 GLU A CG    1 
ATOM   3257  C  CD    . GLU A 1 402 ? 146.912 155.733 125.245 1.00 43.09 ?  402 GLU A CD    1 
ATOM   3258  O  OE1   . GLU A 1 402 ? 148.099 155.471 124.957 1.00 43.53 ?  402 GLU A OE1   1 
ATOM   3259  O  OE2   . GLU A 1 402 ? 146.414 155.488 126.364 1.00 43.84 -1 402 GLU A OE2   1 
ATOM   3260  N  N     . ILE A 1 403 ? 142.634 155.155 120.982 1.00 29.35 ?  403 ILE A N     1 
ATOM   3261  C  CA    . ILE A 1 403 ? 141.948 154.315 120.007 1.00 30.38 ?  403 ILE A CA    1 
ATOM   3262  C  C     . ILE A 1 403 ? 142.926 153.924 118.908 1.00 29.83 ?  403 ILE A C     1 
ATOM   3263  O  O     . ILE A 1 403 ? 143.571 154.786 118.300 1.00 31.37 ?  403 ILE A O     1 
ATOM   3264  C  CB    . ILE A 1 403 ? 140.724 155.042 119.427 1.00 27.23 ?  403 ILE A CB    1 
ATOM   3265  C  CG1   . ILE A 1 403 ? 139.697 155.318 120.529 1.00 30.31 ?  403 ILE A CG1   1 
ATOM   3266  C  CG2   . ILE A 1 403 ? 140.107 154.232 118.302 1.00 22.57 ?  403 ILE A CG2   1 
ATOM   3267  C  CD1   . ILE A 1 403 ? 139.391 154.118 121.397 1.00 30.63 ?  403 ILE A CD1   1 
ATOM   3268  N  N     . GLY A 1 404 ? 143.035 152.622 118.654 1.00 24.83 ?  404 GLY A N     1 
ATOM   3269  C  CA    . GLY A 1 404 ? 143.894 152.120 117.601 1.00 15.92 ?  404 GLY A CA    1 
ATOM   3270  C  C     . GLY A 1 404 ? 143.160 151.888 116.298 1.00 22.98 ?  404 GLY A C     1 
ATOM   3271  O  O     . GLY A 1 404 ? 142.236 152.631 115.959 1.00 33.56 ?  404 GLY A O     1 
ATOM   3272  N  N     . LEU A 1 405 ? 143.562 150.859 115.554 1.00 21.63 ?  405 LEU A N     1 
ATOM   3273  C  CA    . LEU A 1 405 ? 142.954 150.526 114.270 1.00 8.88  ?  405 LEU A CA    1 
ATOM   3274  C  C     . LEU A 1 405 ? 142.526 149.065 114.298 1.00 15.28 ?  405 LEU A C     1 
ATOM   3275  O  O     . LEU A 1 405 ? 143.373 148.169 114.323 1.00 16.33 ?  405 LEU A O     1 
ATOM   3276  C  CB    . LEU A 1 405 ? 143.923 150.781 113.114 1.00 18.00 ?  405 LEU A CB    1 
ATOM   3277  C  CG    . LEU A 1 405 ? 144.402 152.214 112.887 1.00 17.66 ?  405 LEU A CG    1 
ATOM   3278  C  CD1   . LEU A 1 405 ? 145.508 152.237 111.849 1.00 18.80 ?  405 LEU A CD1   1 
ATOM   3279  C  CD2   . LEU A 1 405 ? 143.255 153.113 112.471 1.00 16.03 ?  405 LEU A CD2   1 
ATOM   3280  N  N     . ASP A 1 406 ? 141.219 148.828 114.290 1.00 23.95 ?  406 ASP A N     1 
ATOM   3281  C  CA    . ASP A 1 406 ? 140.665 147.483 114.231 1.00 12.97 ?  406 ASP A CA    1 
ATOM   3282  C  C     . ASP A 1 406 ? 140.113 147.221 112.838 1.00 17.53 ?  406 ASP A C     1 
ATOM   3283  O  O     . ASP A 1 406 ? 139.386 148.045 112.278 1.00 31.72 ?  406 ASP A O     1 
ATOM   3284  C  CB    . ASP A 1 406 ? 139.570 147.291 115.279 1.00 16.10 ?  406 ASP A CB    1 
ATOM   3285  C  CG    . ASP A 1 406 ? 140.126 146.938 116.647 1.00 30.19 ?  406 ASP A CG    1 
ATOM   3286  O  OD1   . ASP A 1 406 ? 141.344 146.688 116.754 1.00 30.73 ?  406 ASP A OD1   1 
ATOM   3287  O  OD2   . ASP A 1 406 ? 139.344 146.917 117.620 1.00 30.34 -1 406 ASP A OD2   1 
ATOM   3288  N  N     . ILE A 1 407 ? 140.442 146.061 112.293 1.00 23.30 ?  407 ILE A N     1 
ATOM   3289  C  CA    . ILE A 1 407 ? 140.217 145.789 110.880 1.00 17.70 ?  407 ILE A CA    1 
ATOM   3290  C  C     . ILE A 1 407 ? 138.750 145.467 110.626 1.00 18.01 ?  407 ILE A C     1 
ATOM   3291  O  O     . ILE A 1 407 ? 138.089 144.798 111.429 1.00 21.33 ?  407 ILE A O     1 
ATOM   3292  C  CB    . ILE A 1 407 ? 141.125 144.639 110.413 1.00 13.02 ?  407 ILE A CB    1 
ATOM   3293  C  CG1   . ILE A 1 407 ? 142.593 144.978 110.661 1.00 2.81  ?  407 ILE A CG1   1 
ATOM   3294  C  CG2   . ILE A 1 407 ? 140.899 144.342 108.958 1.00 16.48 ?  407 ILE A CG2   1 
ATOM   3295  C  CD1   . ILE A 1 407 ? 143.404 143.796 111.104 1.00 18.29 ?  407 ILE A CD1   1 
ATOM   3296  N  N     . SER A 1 408 ? 138.243 145.953 109.495 1.00 27.38 ?  408 SER A N     1 
ATOM   3297  C  CA    . SER A 1 408 ? 136.953 145.552 108.955 1.00 20.37 ?  408 SER A CA    1 
ATOM   3298  C  C     . SER A 1 408 ? 136.918 145.966 107.491 1.00 24.30 ?  408 SER A C     1 
ATOM   3299  O  O     . SER A 1 408 ? 137.320 147.082 107.151 1.00 36.21 ?  408 SER A O     1 
ATOM   3300  C  CB    . SER A 1 408 ? 135.789 146.189 109.722 1.00 21.57 ?  408 SER A CB    1 
ATOM   3301  O  OG    . SER A 1 408 ? 135.408 147.425 109.148 1.00 28.81 ?  408 SER A OG    1 
ATOM   3302  N  N     . CYS A 1 409 ? 136.454 145.067 106.630 1.00 20.11 ?  409 CYS A N     1 
ATOM   3303  C  CA    . CYS A 1 409 ? 136.336 145.363 105.211 1.00 26.27 ?  409 CYS A CA    1 
ATOM   3304  C  C     . CYS A 1 409 ? 135.005 144.849 104.683 1.00 26.33 ?  409 CYS A C     1 
ATOM   3305  O  O     . CYS A 1 409 ? 134.438 143.879 105.192 1.00 24.50 ?  409 CYS A O     1 
ATOM   3306  C  CB    . CYS A 1 409 ? 137.500 144.767 104.402 1.00 22.59 ?  409 CYS A CB    1 
ATOM   3307  S  SG    . CYS A 1 409 ? 137.457 142.978 104.180 1.00 39.49 ?  409 CYS A SG    1 
ATOM   3308  N  N     . ASN A 1 410 ? 134.509 145.526 103.652 1.00 22.83 ?  410 ASN A N     1 
ATOM   3309  C  CA    . ASN A 1 410 ? 133.272 145.141 102.995 1.00 18.43 ?  410 ASN A CA    1 
ATOM   3310  C  C     . ASN A 1 410 ? 133.584 144.132 101.903 1.00 20.75 ?  410 ASN A C     1 
ATOM   3311  O  O     . ASN A 1 410 ? 134.520 144.324 101.120 1.00 22.15 ?  410 ASN A O     1 
ATOM   3312  C  CB    . ASN A 1 410 ? 132.569 146.356 102.396 1.00 22.82 ?  410 ASN A CB    1 
ATOM   3313  C  CG    . ASN A 1 410 ? 133.213 147.653 102.804 1.00 30.14 ?  410 ASN A CG    1 
ATOM   3314  O  OD1   . ASN A 1 410 ? 133.707 147.794 103.923 1.00 31.24 ?  410 ASN A OD1   1 
ATOM   3315  N  ND2   . ASN A 1 410 ? 133.227 148.612 101.892 1.00 28.88 ?  410 ASN A ND2   1 
ATOM   3316  N  N     . LEU A 1 411 ? 132.796 143.069 101.848 1.00 17.79 ?  411 LEU A N     1 
ATOM   3317  C  CA    . LEU A 1 411 ? 133.044 141.965 100.938 1.00 12.06 ?  411 LEU A CA    1 
ATOM   3318  C  C     . LEU A 1 411 ? 132.187 142.100 99.688  1.00 13.10 ?  411 LEU A C     1 
ATOM   3319  O  O     . LEU A 1 411 ? 131.079 142.639 99.722  1.00 19.18 ?  411 LEU A O     1 
ATOM   3320  C  CB    . LEU A 1 411 ? 132.758 140.631 101.628 1.00 21.93 ?  411 LEU A CB    1 
ATOM   3321  C  CG    . LEU A 1 411 ? 133.511 140.345 102.925 1.00 14.94 ?  411 LEU A CG    1 
ATOM   3322  C  CD1   . LEU A 1 411 ? 133.500 138.865 103.207 1.00 20.54 ?  411 LEU A CD1   1 
ATOM   3323  C  CD2   . LEU A 1 411 ? 134.938 140.847 102.840 1.00 19.17 ?  411 LEU A CD2   1 
ATOM   3324  N  N     . GLY A 1 412 ? 132.722 141.605 98.578  1.00 21.24 ?  412 GLY A N     1 
ATOM   3325  C  CA    . GLY A 1 412 ? 132.004 141.557 97.322  1.00 10.26 ?  412 GLY A CA    1 
ATOM   3326  C  C     . GLY A 1 412 ? 132.725 140.648 96.354  1.00 11.55 ?  412 GLY A C     1 
ATOM   3327  O  O     . GLY A 1 412 ? 133.956 140.673 96.287  1.00 25.53 ?  412 GLY A O     1 
ATOM   3328  N  N     . SER A 1 413 ? 131.987 139.841 95.602  1.00 15.23 ?  413 SER A N     1 
ATOM   3329  C  CA    . SER A 1 413 ? 132.582 138.826 94.744  1.00 9.33  ?  413 SER A CA    1 
ATOM   3330  C  C     . SER A 1 413 ? 132.241 139.093 93.288  1.00 15.97 ?  413 SER A C     1 
ATOM   3331  O  O     . SER A 1 413 ? 131.081 139.350 92.954  1.00 24.07 ?  413 SER A O     1 
ATOM   3332  C  CB    . SER A 1 413 ? 132.108 137.430 95.141  1.00 10.90 ?  413 SER A CB    1 
ATOM   3333  O  OG    . SER A 1 413 ? 132.669 137.045 96.380  1.00 29.53 ?  413 SER A OG    1 
ATOM   3334  N  N     . LEU A 1 414 ? 133.254 139.031 92.431  1.00 20.43 ?  414 LEU A N     1 
ATOM   3335  C  CA    . LEU A 1 414 ? 133.027 138.941 90.999  1.00 13.30 ?  414 LEU A CA    1 
ATOM   3336  C  C     . LEU A 1 414 ? 132.668 137.510 90.632  1.00 21.18 ?  414 LEU A C     1 
ATOM   3337  O  O     . LEU A 1 414 ? 133.235 136.556 91.170  1.00 21.96 ?  414 LEU A O     1 
ATOM   3338  C  CB    . LEU A 1 414 ? 134.270 139.372 90.223  1.00 14.83 ?  414 LEU A CB    1 
ATOM   3339  C  CG    . LEU A 1 414 ? 134.990 140.649 90.647  1.00 19.22 ?  414 LEU A CG    1 
ATOM   3340  C  CD1   . LEU A 1 414 ? 136.290 140.774 89.879  1.00 24.86 ?  414 LEU A CD1   1 
ATOM   3341  C  CD2   . LEU A 1 414 ? 134.108 141.858 90.410  1.00 24.81 ?  414 LEU A CD2   1 
ATOM   3342  N  N     . ASN A 1 415 ? 131.721 137.358 89.716  1.00 28.22 ?  415 ASN A N     1 
ATOM   3343  C  CA    . ASN A 1 415 ? 131.415 136.055 89.142  1.00 25.19 ?  415 ASN A CA    1 
ATOM   3344  C  C     . ASN A 1 415 ? 132.308 135.871 87.924  1.00 27.36 ?  415 ASN A C     1 
ATOM   3345  O  O     . ASN A 1 415 ? 132.087 136.501 86.886  1.00 29.83 ?  415 ASN A O     1 
ATOM   3346  C  CB    . ASN A 1 415 ? 129.938 135.953 88.778  1.00 20.33 ?  415 ASN A CB    1 
ATOM   3347  C  CG    . ASN A 1 415 ? 129.472 134.523 88.618  1.00 23.73 ?  415 ASN A CG    1 
ATOM   3348  O  OD1   . ASN A 1 415 ? 130.090 133.732 87.911  1.00 32.26 ?  415 ASN A OD1   1 
ATOM   3349  N  ND2   . ASN A 1 415 ? 128.373 134.184 89.277  1.00 30.02 ?  415 ASN A ND2   1 
ATOM   3350  N  N     . ILE A 1 416 ? 133.319 135.011 88.056  1.00 19.85 ?  416 ILE A N     1 
ATOM   3351  C  CA    . ILE A 1 416 ? 134.327 134.872 87.009  1.00 22.02 ?  416 ILE A CA    1 
ATOM   3352  C  C     . ILE A 1 416 ? 133.689 134.411 85.706  1.00 28.81 ?  416 ILE A C     1 
ATOM   3353  O  O     . ILE A 1 416 ? 134.045 134.888 84.622  1.00 26.69 ?  416 ILE A O     1 
ATOM   3354  C  CB    . ILE A 1 416 ? 135.444 133.916 87.469  1.00 24.02 ?  416 ILE A CB    1 
ATOM   3355  C  CG1   . ILE A 1 416 ? 136.215 134.532 88.637  1.00 21.73 ?  416 ILE A CG1   1 
ATOM   3356  C  CG2   . ILE A 1 416 ? 136.388 133.603 86.327  1.00 15.94 ?  416 ILE A CG2   1 
ATOM   3357  C  CD1   . ILE A 1 416 ? 137.174 133.583 89.310  1.00 19.62 ?  416 ILE A CD1   1 
ATOM   3358  N  N     . LEU A 1 417 ? 132.726 133.492 85.788  1.00 23.98 ?  417 LEU A N     1 
ATOM   3359  C  CA    . LEU A 1 417 ? 132.077 132.990 84.580  1.00 27.03 ?  417 LEU A CA    1 
ATOM   3360  C  C     . LEU A 1 417 ? 131.327 134.099 83.851  1.00 28.59 ?  417 LEU A C     1 
ATOM   3361  O  O     . LEU A 1 417 ? 131.488 134.279 82.639  1.00 36.05 ?  417 LEU A O     1 
ATOM   3362  C  CB    . LEU A 1 417 ? 131.129 131.846 84.936  1.00 27.64 ?  417 LEU A CB    1 
ATOM   3363  C  CG    . LEU A 1 417 ? 130.601 131.007 83.774  1.00 25.66 ?  417 LEU A CG    1 
ATOM   3364  C  CD1   . LEU A 1 417 ? 130.636 129.543 84.140  1.00 26.86 ?  417 LEU A CD1   1 
ATOM   3365  C  CD2   . LEU A 1 417 ? 129.191 131.429 83.406  1.00 32.99 ?  417 LEU A CD2   1 
ATOM   3366  N  N     . ASN A 1 418 ? 130.504 134.857 84.577  1.00 30.17 ?  418 ASN A N     1 
ATOM   3367  C  CA    . ASN A 1 418 ? 129.697 135.892 83.942  1.00 30.26 ?  418 ASN A CA    1 
ATOM   3368  C  C     . ASN A 1 418 ? 130.527 137.107 83.557  1.00 29.72 ?  418 ASN A C     1 
ATOM   3369  O  O     . ASN A 1 418 ? 130.226 137.765 82.555  1.00 32.38 ?  418 ASN A O     1 
ATOM   3370  C  CB    . ASN A 1 418 ? 128.553 136.303 84.867  1.00 26.41 ?  418 ASN A CB    1 
ATOM   3371  C  CG    . ASN A 1 418 ? 127.531 135.203 85.049  1.00 31.04 ?  418 ASN A CG    1 
ATOM   3372  O  OD1   . ASN A 1 418 ? 127.230 134.462 84.115  1.00 36.97 ?  418 ASN A OD1   1 
ATOM   3373  N  ND2   . ASN A 1 418 ? 126.993 135.086 86.256  1.00 32.23 ?  418 ASN A ND2   1 
ATOM   3374  N  N     . VAL A 1 419 ? 131.560 137.424 84.337  1.00 29.60 ?  419 VAL A N     1 
ATOM   3375  C  CA    . VAL A 1 419 ? 132.461 138.513 83.972  1.00 28.99 ?  419 VAL A CA    1 
ATOM   3376  C  C     . VAL A 1 419 ? 133.225 138.168 82.701  1.00 31.93 ?  419 VAL A C     1 
ATOM   3377  O  O     . VAL A 1 419 ? 133.380 139.006 81.806  1.00 35.55 ?  419 VAL A O     1 
ATOM   3378  C  CB    . VAL A 1 419 ? 133.408 138.829 85.145  1.00 27.28 ?  419 VAL A CB    1 
ATOM   3379  C  CG1   . VAL A 1 419 ? 134.618 139.588 84.664  1.00 31.92 ?  419 VAL A CG1   1 
ATOM   3380  C  CG2   . VAL A 1 419 ? 132.680 139.620 86.210  1.00 27.21 ?  419 VAL A CG2   1 
ATOM   3381  N  N     . MET A 1 420 ? 133.704 136.926 82.595  1.00 37.60 ?  420 MET A N     1 
ATOM   3382  C  CA    . MET A 1 420 ? 134.443 136.506 81.410  1.00 31.13 ?  420 MET A CA    1 
ATOM   3383  C  C     . MET A 1 420 ? 133.535 136.372 80.197  1.00 29.91 ?  420 MET A C     1 
ATOM   3384  O  O     . MET A 1 420 ? 133.965 136.649 79.071  1.00 35.71 ?  420 MET A O     1 
ATOM   3385  C  CB    . MET A 1 420 ? 135.162 135.188 81.686  1.00 32.87 ?  420 MET A CB    1 
ATOM   3386  C  CG    . MET A 1 420 ? 136.445 135.342 82.481  1.00 30.68 ?  420 MET A CG    1 
ATOM   3387  S  SD    . MET A 1 420 ? 137.613 136.450 81.680  1.00 39.19 ?  420 MET A SD    1 
ATOM   3388  C  CE    . MET A 1 420 ? 138.357 135.343 80.488  1.00 30.33 ?  420 MET A CE    1 
ATOM   3389  N  N     . GLU A 1 421 ? 132.288 135.941 80.399  1.00 38.79 ?  421 GLU A N     1 
ATOM   3390  C  CA    . GLU A 1 421 ? 131.342 135.859 79.291  1.00 37.01 ?  421 GLU A CA    1 
ATOM   3391  C  C     . GLU A 1 421 ? 131.044 137.238 78.718  1.00 41.48 ?  421 GLU A C     1 
ATOM   3392  O  O     . GLU A 1 421 ? 130.957 137.407 77.496  1.00 43.64 ?  421 GLU A O     1 
ATOM   3393  C  CB    . GLU A 1 421 ? 130.052 135.184 79.754  1.00 35.64 ?  421 GLU A CB    1 
ATOM   3394  C  CG    . GLU A 1 421 ? 130.061 133.670 79.641  1.00 40.90 ?  421 GLU A CG    1 
ATOM   3395  C  CD    . GLU A 1 421 ? 128.758 133.048 80.104  1.00 46.28 ?  421 GLU A CD    1 
ATOM   3396  O  OE1   . GLU A 1 421 ? 127.960 133.758 80.752  1.00 45.01 ?  421 GLU A OE1   1 
ATOM   3397  O  OE2   . GLU A 1 421 ? 128.531 131.854 79.820  1.00 45.47 -1 421 GLU A OE2   1 
ATOM   3398  N  N     . HIS A 1 422 ? 130.885 138.236 79.585  1.00 37.78 ?  422 HIS A N     1 
ATOM   3399  C  CA    . HIS A 1 422 ? 130.577 139.593 79.158  1.00 34.71 ?  422 HIS A CA    1 
ATOM   3400  C  C     . HIS A 1 422 ? 131.812 140.382 78.748  1.00 39.06 ?  422 HIS A C     1 
ATOM   3401  O  O     . HIS A 1 422 ? 131.666 141.513 78.271  1.00 39.00 ?  422 HIS A O     1 
ATOM   3402  C  CB    . HIS A 1 422 ? 129.843 140.339 80.275  1.00 34.38 ?  422 HIS A CB    1 
ATOM   3403  C  CG    . HIS A 1 422 ? 128.493 139.777 80.590  1.00 36.59 ?  422 HIS A CG    1 
ATOM   3404  N  ND1   . HIS A 1 422 ? 128.303 138.781 81.524  1.00 36.17 ?  422 HIS A ND1   1 
ATOM   3405  C  CD2   . HIS A 1 422 ? 127.266 140.071 80.100  1.00 38.64 ?  422 HIS A CD2   1 
ATOM   3406  C  CE1   . HIS A 1 422 ? 127.018 138.484 81.593  1.00 39.68 ?  422 HIS A CE1   1 
ATOM   3407  N  NE2   . HIS A 1 422 ? 126.366 139.252 80.739  1.00 41.23 ?  422 HIS A NE2   1 
ATOM   3408  N  N     . LYS A 1 423 ? 133.007 139.816 78.914  1.00 42.93 ?  423 LYS A N     1 
ATOM   3409  C  CA    . LYS A 1 423 ? 134.264 140.501 78.613  1.00 43.56 ?  423 LYS A CA    1 
ATOM   3410  C  C     . LYS A 1 423 ? 134.322 141.856 79.313  1.00 43.41 ?  423 LYS A C     1 
ATOM   3411  O  O     . LYS A 1 423 ? 134.651 142.883 78.716  1.00 46.66 ?  423 LYS A O     1 
ATOM   3412  C  CB    . LYS A 1 423 ? 134.459 140.654 77.104  1.00 40.83 ?  423 LYS A CB    1 
ATOM   3413  C  CG    . LYS A 1 423 ? 134.255 139.373 76.318  1.00 42.34 ?  423 LYS A CG    1 
ATOM   3414  C  CD    . LYS A 1 423 ? 135.563 138.620 76.153  1.00 46.49 ?  423 LYS A CD    1 
ATOM   3415  C  CE    . LYS A 1 423 ? 135.323 137.157 75.819  1.00 46.50 ?  423 LYS A CE    1 
ATOM   3416  N  NZ    . LYS A 1 423 ? 135.198 136.318 77.042  1.00 44.64 1  423 LYS A NZ    1 
ATOM   3417  N  N     . SER A 1 424 ? 133.994 141.849 80.600  1.00 33.13 ?  424 SER A N     1 
ATOM   3418  C  CA    . SER A 1 424 ? 133.796 143.070 81.371  1.00 32.99 ?  424 SER A CA    1 
ATOM   3419  C  C     . SER A 1 424 ? 134.547 143.008 82.690  1.00 36.41 ?  424 SER A C     1 
ATOM   3420  O  O     . SER A 1 424 ? 133.997 143.291 83.754  1.00 39.49 ?  424 SER A O     1 
ATOM   3421  C  CB    . SER A 1 424 ? 132.312 143.313 81.620  1.00 35.65 ?  424 SER A CB    1 
ATOM   3422  O  OG    . SER A 1 424 ? 131.807 142.396 82.574  1.00 32.10 ?  424 SER A OG    1 
ATOM   3423  N  N     . ILE A 1 425 ? 135.825 142.628 82.645  1.00 34.09 ?  425 ILE A N     1 
ATOM   3424  C  CA    . ILE A 1 425 ? 136.629 142.633 83.864  1.00 28.18 ?  425 ILE A CA    1 
ATOM   3425  C  C     . ILE A 1 425 ? 136.791 144.056 84.382  1.00 31.11 ?  425 ILE A C     1 
ATOM   3426  O  O     . ILE A 1 425 ? 136.581 144.331 85.568  1.00 36.98 ?  425 ILE A O     1 
ATOM   3427  C  CB    . ILE A 1 425 ? 137.992 141.961 83.620  1.00 32.28 ?  425 ILE A CB    1 
ATOM   3428  C  CG1   . ILE A 1 425 ? 137.840 140.440 83.601  1.00 33.29 ?  425 ILE A CG1   1 
ATOM   3429  C  CG2   . ILE A 1 425 ? 138.993 142.374 84.686  1.00 28.28 ?  425 ILE A CG2   1 
ATOM   3430  C  CD1   . ILE A 1 425 ? 139.110 139.698 83.294  1.00 32.74 ?  425 ILE A CD1   1 
ATOM   3431  N  N     . GLU A 1 426 ? 137.138 144.987 83.492  1.00 28.74 ?  426 GLU A N     1 
ATOM   3432  C  CA    . GLU A 1 426 ? 137.409 146.359 83.911  1.00 27.28 ?  426 GLU A CA    1 
ATOM   3433  C  C     . GLU A 1 426 ? 136.172 147.017 84.508  1.00 30.36 ?  426 GLU A C     1 
ATOM   3434  O  O     . GLU A 1 426 ? 136.215 147.554 85.622  1.00 37.14 ?  426 GLU A O     1 
ATOM   3435  C  CB    . GLU A 1 426 ? 137.922 147.168 82.722  1.00 29.43 ?  426 GLU A CB    1 
ATOM   3436  C  CG    . GLU A 1 426 ? 137.863 148.669 82.923  1.00 33.41 ?  426 GLU A CG    1 
ATOM   3437  C  CD    . GLU A 1 426 ? 138.527 149.432 81.796  1.00 39.47 ?  426 GLU A CD    1 
ATOM   3438  O  OE1   . GLU A 1 426 ? 138.814 148.815 80.748  1.00 38.35 ?  426 GLU A OE1   1 
ATOM   3439  O  OE2   . GLU A 1 426 ? 138.761 150.647 81.959  1.00 38.54 -1 426 GLU A OE2   1 
ATOM   3440  N  N     . LYS A 1 427 ? 135.056 146.985 83.778  1.00 32.91 ?  427 LYS A N     1 
ATOM   3441  C  CA    . LYS A 1 427 ? 133.848 147.661 84.237  1.00 28.97 ?  427 LYS A CA    1 
ATOM   3442  C  C     . LYS A 1 427 ? 133.311 147.026 85.511  1.00 30.16 ?  427 LYS A C     1 
ATOM   3443  O  O     . LYS A 1 427 ? 132.908 147.735 86.440  1.00 36.77 ?  427 LYS A O     1 
ATOM   3444  C  CB    . LYS A 1 427 ? 132.758 147.680 83.152  1.00 34.40 ?  427 LYS A CB    1 
ATOM   3445  C  CG    . LYS A 1 427 ? 133.055 148.339 81.771  1.00 38.16 ?  427 LYS A CG    1 
ATOM   3446  C  CD    . LYS A 1 427 ? 134.365 148.003 81.047  1.00 38.84 ?  427 LYS A CD    1 
ATOM   3447  C  CE    . LYS A 1 427 ? 134.546 146.506 80.832  1.00 34.59 ?  427 LYS A CE    1 
ATOM   3448  N  NZ    . LYS A 1 427 ? 135.850 146.181 80.191  1.00 35.02 1  427 LYS A NZ    1 
ATOM   3449  N  N     . THR A 1 428 ? 133.299 145.693 85.577  1.00 29.14 ?  428 THR A N     1 
ATOM   3450  C  CA    . THR A 1 428 ? 132.819 145.026 86.781  1.00 22.10 ?  428 THR A CA    1 
ATOM   3451  C  C     . THR A 1 428 ? 133.698 145.350 87.978  1.00 28.69 ?  428 THR A C     1 
ATOM   3452  O  O     . THR A 1 428 ? 133.188 145.637 89.066  1.00 31.20 ?  428 THR A O     1 
ATOM   3453  C  CB    . THR A 1 428 ? 132.752 143.516 86.571  1.00 24.52 ?  428 THR A CB    1 
ATOM   3454  O  OG1   . THR A 1 428 ? 132.133 143.232 85.311  1.00 28.64 ?  428 THR A OG1   1 
ATOM   3455  C  CG2   . THR A 1 428 ? 131.945 142.871 87.679  1.00 25.65 ?  428 THR A CG2   1 
ATOM   3456  N  N     . VAL A 1 429 ? 135.020 145.320 87.799  1.00 28.73 ?  429 VAL A N     1 
ATOM   3457  C  CA    . VAL A 1 429 ? 135.921 145.596 88.914  1.00 22.63 ?  429 VAL A CA    1 
ATOM   3458  C  C     . VAL A 1 429 ? 135.747 147.029 89.397  1.00 23.97 ?  429 VAL A C     1 
ATOM   3459  O  O     . VAL A 1 429 ? 135.683 147.286 90.603  1.00 30.65 ?  429 VAL A O     1 
ATOM   3460  C  CB    . VAL A 1 429 ? 137.380 145.302 88.518  1.00 24.00 ?  429 VAL A CB    1 
ATOM   3461  C  CG1   . VAL A 1 429 ? 138.331 145.943 89.504  1.00 19.09 ?  429 VAL A CG1   1 
ATOM   3462  C  CG2   . VAL A 1 429 ? 137.624 143.808 88.469  1.00 23.11 ?  429 VAL A CG2   1 
ATOM   3463  N  N     . LYS A 1 430 ? 135.641 147.982 88.467  1.00 24.20 ?  430 LYS A N     1 
ATOM   3464  C  CA    . LYS A 1 430 ? 135.509 149.378 88.872  1.00 23.38 ?  430 LYS A CA    1 
ATOM   3465  C  C     . LYS A 1 430 ? 134.169 149.646 89.550  1.00 23.32 ?  430 LYS A C     1 
ATOM   3466  O  O     . LYS A 1 430 ? 134.113 150.345 90.569  1.00 31.57 ?  430 LYS A O     1 
ATOM   3467  C  CB    . LYS A 1 430 ? 135.708 150.291 87.663  1.00 24.45 ?  430 LYS A CB    1 
ATOM   3468  C  CG    . LYS A 1 430 ? 137.114 150.223 87.092  1.00 26.85 ?  430 LYS A CG    1 
ATOM   3469  C  CD    . LYS A 1 430 ? 137.436 151.425 86.230  1.00 29.76 ?  430 LYS A CD    1 
ATOM   3470  C  CE    . LYS A 1 430 ? 138.877 151.377 85.758  1.00 29.64 ?  430 LYS A CE    1 
ATOM   3471  N  NZ    . LYS A 1 430 ? 139.218 152.537 84.892  1.00 33.48 1  430 LYS A NZ    1 
ATOM   3472  N  N     . LEU A 1 431 ? 133.079 149.094 89.011  1.00 24.92 ?  431 LEU A N     1 
ATOM   3473  C  CA    . LEU A 1 431 ? 131.772 149.295 89.629  1.00 20.54 ?  431 LEU A CA    1 
ATOM   3474  C  C     . LEU A 1 431 ? 131.692 148.621 90.994  1.00 22.83 ?  431 LEU A C     1 
ATOM   3475  O  O     . LEU A 1 431 ? 131.104 149.173 91.931  1.00 28.68 ?  431 LEU A O     1 
ATOM   3476  C  CB    . LEU A 1 431 ? 130.674 148.773 88.706  1.00 27.17 ?  431 LEU A CB    1 
ATOM   3477  C  CG    . LEU A 1 431 ? 129.934 149.800 87.847  1.00 30.22 ?  431 LEU A CG    1 
ATOM   3478  C  CD1   . LEU A 1 431 ? 128.838 149.119 87.049  1.00 29.53 ?  431 LEU A CD1   1 
ATOM   3479  C  CD2   . LEU A 1 431 ? 129.362 150.911 88.707  1.00 31.29 ?  431 LEU A CD2   1 
ATOM   3480  N  N     . ALA A 1 432 ? 132.271 147.424 91.125  1.00 24.46 ?  432 ALA A N     1 
ATOM   3481  C  CA    . ALA A 1 432 ? 132.307 146.752 92.417  1.00 15.27 ?  432 ALA A CA    1 
ATOM   3482  C  C     . ALA A 1 432 ? 133.147 147.531 93.417  1.00 26.11 ?  432 ALA A C     1 
ATOM   3483  O  O     . ALA A 1 432 ? 132.805 147.601 94.601  1.00 28.99 ?  432 ALA A O     1 
ATOM   3484  C  CB    . ALA A 1 432 ? 132.851 145.335 92.251  1.00 21.06 ?  432 ALA A CB    1 
ATOM   3485  N  N     . THR A 1 433 ? 134.255 148.116 92.959  1.00 28.03 ?  433 THR A N     1 
ATOM   3486  C  CA    . THR A 1 433 ? 135.065 148.956 93.831  1.00 21.24 ?  433 THR A CA    1 
ATOM   3487  C  C     . THR A 1 433 ? 134.277 150.167 94.305  1.00 23.51 ?  433 THR A C     1 
ATOM   3488  O  O     . THR A 1 433 ? 134.344 150.538 95.481  1.00 34.90 ?  433 THR A O     1 
ATOM   3489  C  CB    . THR A 1 433 ? 136.336 149.393 93.103  1.00 27.47 ?  433 THR A CB    1 
ATOM   3490  O  OG1   . THR A 1 433 ? 137.089 148.236 92.718  1.00 29.32 ?  433 THR A OG1   1 
ATOM   3491  C  CG2   . THR A 1 433 ? 137.191 150.272 93.999  1.00 24.32 ?  433 THR A CG2   1 
ATOM   3492  N  N     . ASP A 1 434 ? 133.518 150.793 93.404  1.00 22.85 ?  434 ASP A N     1 
ATOM   3493  C  CA    . ASP A 1 434 ? 132.686 151.927 93.796  1.00 22.59 ?  434 ASP A CA    1 
ATOM   3494  C  C     . ASP A 1 434 ? 131.629 151.514 94.817  1.00 20.26 ?  434 ASP A C     1 
ATOM   3495  O  O     . ASP A 1 434 ? 131.395 152.222 95.803  1.00 24.84 ?  434 ASP A O     1 
ATOM   3496  C  CB    . ASP A 1 434 ? 132.025 152.543 92.565  1.00 24.86 ?  434 ASP A CB    1 
ATOM   3497  C  CG    . ASP A 1 434 ? 133.029 153.143 91.605  1.00 31.71 ?  434 ASP A CG    1 
ATOM   3498  O  OD1   . ASP A 1 434 ? 134.142 153.491 92.049  1.00 35.06 ?  434 ASP A OD1   1 
ATOM   3499  O  OD2   . ASP A 1 434 ? 132.703 153.269 90.406  1.00 33.12 -1 434 ASP A OD2   1 
ATOM   3500  N  N     . SER A 1 435 ? 130.977 150.371 94.592  1.00 22.09 ?  435 SER A N     1 
ATOM   3501  C  CA    . SER A 1 435 ? 129.951 149.906 95.522  1.00 20.46 ?  435 SER A CA    1 
ATOM   3502  C  C     . SER A 1 435 ? 130.542 149.586 96.890  1.00 23.29 ?  435 SER A C     1 
ATOM   3503  O  O     . SER A 1 435 ? 129.955 149.926 97.924  1.00 29.51 ?  435 SER A O     1 
ATOM   3504  C  CB    . SER A 1 435 ? 129.238 148.685 94.944  1.00 23.10 ?  435 SER A CB    1 
ATOM   3505  O  OG    . SER A 1 435 ? 130.048 147.529 95.037  1.00 20.02 ?  435 SER A OG    1 
ATOM   3506  N  N     . LEU A 1 436 ? 131.710 148.940 96.917  1.00 19.07 ?  436 LEU A N     1 
ATOM   3507  C  CA    . LEU A 1 436 ? 132.355 148.626 98.186  1.00 10.90 ?  436 LEU A CA    1 
ATOM   3508  C  C     . LEU A 1 436 ? 132.825 149.890 98.893  1.00 17.35 ?  436 LEU A C     1 
ATOM   3509  O  O     . LEU A 1 436 ? 132.762 149.979 100.123 1.00 21.46 ?  436 LEU A O     1 
ATOM   3510  C  CB    . LEU A 1 436 ? 133.518 147.665 97.952  1.00 22.54 ?  436 LEU A CB    1 
ATOM   3511  C  CG    . LEU A 1 436 ? 133.136 146.245 97.531  1.00 19.18 ?  436 LEU A CG    1 
ATOM   3512  C  CD1   . LEU A 1 436 ? 134.349 145.483 97.024  1.00 10.93 ?  436 LEU A CD1   1 
ATOM   3513  C  CD2   . LEU A 1 436 ? 132.478 145.504 98.677  1.00 20.99 ?  436 LEU A CD2   1 
ATOM   3514  N  N     . THR A 1 437 ? 133.294 150.881 98.132  1.00 23.18 ?  437 THR A N     1 
ATOM   3515  C  CA    . THR A 1 437 ? 133.648 152.168 98.718  1.00 21.46 ?  437 THR A CA    1 
ATOM   3516  C  C     . THR A 1 437 ? 132.435 152.835 99.348  1.00 24.16 ?  437 THR A C     1 
ATOM   3517  O  O     . THR A 1 437 ? 132.526 153.405 100.441 1.00 35.32 ?  437 THR A O     1 
ATOM   3518  C  CB    . THR A 1 437 ? 134.260 153.075 97.652  1.00 19.83 ?  437 THR A CB    1 
ATOM   3519  O  OG1   . THR A 1 437 ? 135.265 152.353 96.932  1.00 21.94 ?  437 THR A OG1   1 
ATOM   3520  C  CG2   . THR A 1 437 ? 134.880 154.304 98.286  1.00 22.56 ?  437 THR A CG2   1 
ATOM   3521  N  N     . HIS A 1 438 ? 131.288 152.780 98.669  1.00 21.99 ?  438 HIS A N     1 
ATOM   3522  C  CA    . HIS A 1 438 ? 130.071 153.352 99.234  1.00 23.39 ?  438 HIS A CA    1 
ATOM   3523  C  C     . HIS A 1 438 ? 129.657 152.622 100.506 1.00 23.90 ?  438 HIS A C     1 
ATOM   3524  O  O     . HIS A 1 438 ? 129.235 153.252 101.483 1.00 31.71 ?  438 HIS A O     1 
ATOM   3525  C  CB    . HIS A 1 438 ? 128.944 153.318 98.204  1.00 26.69 ?  438 HIS A CB    1 
ATOM   3526  C  CG    . HIS A 1 438 ? 127.633 153.802 98.734  1.00 27.28 ?  438 HIS A CG    1 
ATOM   3527  N  ND1   . HIS A 1 438 ? 127.315 155.140 98.822  1.00 27.32 ?  438 HIS A ND1   1 
ATOM   3528  C  CD2   . HIS A 1 438 ? 126.559 153.130 99.211  1.00 28.60 ?  438 HIS A CD2   1 
ATOM   3529  C  CE1   . HIS A 1 438 ? 126.102 155.271 99.328  1.00 31.76 ?  438 HIS A CE1   1 
ATOM   3530  N  NE2   . HIS A 1 438 ? 125.622 154.065 99.573  1.00 31.05 ?  438 HIS A NE2   1 
ATOM   3531  N  N     . VAL A 1 439 ? 129.767 151.292 100.511 1.00 25.03 ?  439 VAL A N     1 
ATOM   3532  C  CA    . VAL A 1 439 ? 129.423 150.529 101.709 1.00 20.09 ?  439 VAL A CA    1 
ATOM   3533  C  C     . VAL A 1 439 ? 130.356 150.892 102.858 1.00 27.11 ?  439 VAL A C     1 
ATOM   3534  O  O     . VAL A 1 439 ? 129.929 151.003 104.013 1.00 36.62 ?  439 VAL A O     1 
ATOM   3535  C  CB    . VAL A 1 439 ? 129.448 149.018 101.411 1.00 23.14 ?  439 VAL A CB    1 
ATOM   3536  C  CG1   . VAL A 1 439 ? 129.220 148.223 102.680 1.00 24.30 ?  439 VAL A CG1   1 
ATOM   3537  C  CG2   . VAL A 1 439 ? 128.394 148.668 100.383 1.00 25.36 ?  439 VAL A CG2   1 
ATOM   3538  N  N     . SER A 1 440 ? 131.642 151.083 102.561 1.00 25.44 ?  440 SER A N     1 
ATOM   3539  C  CA    . SER A 1 440 ? 132.586 151.516 103.586 1.00 20.24 ?  440 SER A CA    1 
ATOM   3540  C  C     . SER A 1 440 ? 132.227 152.897 104.117 1.00 26.38 ?  440 SER A C     1 
ATOM   3541  O  O     . SER A 1 440 ? 132.302 153.147 105.325 1.00 34.05 ?  440 SER A O     1 
ATOM   3542  C  CB    . SER A 1 440 ? 134.007 151.513 103.024 1.00 25.82 ?  440 SER A CB    1 
ATOM   3543  O  OG    . SER A 1 440 ? 134.969 151.576 104.062 1.00 30.51 ?  440 SER A OG    1 
ATOM   3544  N  N     . GLU A 1 441 ? 131.836 153.809 103.226 1.00 29.54 ?  441 GLU A N     1 
ATOM   3545  C  CA    . GLU A 1 441 ? 131.538 155.175 103.638 1.00 21.89 ?  441 GLU A CA    1 
ATOM   3546  C  C     . GLU A 1 441 ? 130.254 155.261 104.454 1.00 31.00 ?  441 GLU A C     1 
ATOM   3547  O  O     . GLU A 1 441 ? 130.147 156.109 105.345 1.00 40.06 ?  441 GLU A O     1 
ATOM   3548  C  CB    . GLU A 1 441 ? 131.447 156.081 102.413 1.00 22.46 ?  441 GLU A CB    1 
ATOM   3549  C  CG    . GLU A 1 441 ? 132.793 156.418 101.800 1.00 28.54 ?  441 GLU A CG    1 
ATOM   3550  C  CD    . GLU A 1 441 ? 132.664 157.206 100.515 1.00 38.58 ?  441 GLU A CD    1 
ATOM   3551  O  OE1   . GLU A 1 441 ? 132.260 156.617 99.489  1.00 38.78 ?  441 GLU A OE1   1 
ATOM   3552  O  OE2   . GLU A 1 441 ? 132.965 158.417 100.526 1.00 37.83 -1 441 GLU A OE2   1 
ATOM   3553  N  N     . THR A 1 442 ? 129.273 154.408 104.170 1.00 32.28 ?  442 THR A N     1 
ATOM   3554  C  CA    . THR A 1 442 ? 128.003 154.446 104.882 1.00 31.30 ?  442 THR A CA    1 
ATOM   3555  C  C     . THR A 1 442 ? 127.999 153.603 106.150 1.00 32.40 ?  442 THR A C     1 
ATOM   3556  O  O     . THR A 1 442 ? 126.987 153.577 106.855 1.00 38.71 ?  442 THR A O     1 
ATOM   3557  C  CB    . THR A 1 442 ? 126.860 153.991 103.968 1.00 30.83 ?  442 THR A CB    1 
ATOM   3558  O  OG1   . THR A 1 442 ? 127.068 152.628 103.577 1.00 30.72 ?  442 THR A OG1   1 
ATOM   3559  C  CG2   . THR A 1 442 ? 126.785 154.869 102.733 1.00 30.57 ?  442 THR A CG2   1 
ATOM   3560  N  N     . THR A 1 443 ? 129.095 152.916 106.457 1.00 31.71 ?  443 THR A N     1 
ATOM   3561  C  CA    . THR A 1 443 ? 129.192 152.127 107.676 1.00 34.28 ?  443 THR A CA    1 
ATOM   3562  C  C     . THR A 1 443 ? 129.718 152.999 108.808 1.00 37.40 ?  443 THR A C     1 
ATOM   3563  O  O     . THR A 1 443 ? 130.734 153.683 108.652 1.00 39.22 ?  443 THR A O     1 
ATOM   3564  C  CB    . THR A 1 443 ? 130.106 150.919 107.469 1.00 33.99 ?  443 THR A CB    1 
ATOM   3565  O  OG1   . THR A 1 443 ? 129.525 150.040 106.499 1.00 38.06 ?  443 THR A OG1   1 
ATOM   3566  C  CG2   . THR A 1 443 ? 130.295 150.167 108.774 1.00 30.56 ?  443 THR A CG2   1 
ATOM   3567  N  N     . ASP A 1 444 ? 129.020 152.978 109.942 1.00 42.90 ?  444 ASP A N     1 
ATOM   3568  C  CA    . ASP A 1 444 ? 129.419 153.750 111.119 1.00 42.22 ?  444 ASP A CA    1 
ATOM   3569  C  C     . ASP A 1 444 ? 129.100 152.920 112.358 1.00 41.14 ?  444 ASP A C     1 
ATOM   3570  O  O     . ASP A 1 444 ? 127.953 152.888 112.812 1.00 42.24 ?  444 ASP A O     1 
ATOM   3571  C  CB    . ASP A 1 444 ? 128.717 155.102 111.158 1.00 43.39 ?  444 ASP A CB    1 
ATOM   3572  C  CG    . ASP A 1 444 ? 129.590 156.194 111.740 1.00 46.17 ?  444 ASP A CG    1 
ATOM   3573  O  OD1   . ASP A 1 444 ? 129.985 156.072 112.918 1.00 45.39 ?  444 ASP A OD1   1 
ATOM   3574  O  OD2   . ASP A 1 444 ? 129.883 157.171 111.022 1.00 47.95 -1 444 ASP A OD2   1 
ATOM   3575  N  N     . ILE A 1 445 ? 130.115 152.256 112.899 1.00 38.07 ?  445 ILE A N     1 
ATOM   3576  C  CA    . ILE A 1 445 ? 129.967 151.438 114.097 1.00 40.95 ?  445 ILE A CA    1 
ATOM   3577  C  C     . ILE A 1 445 ? 130.211 152.341 115.301 1.00 44.55 ?  445 ILE A C     1 
ATOM   3578  O  O     . ILE A 1 445 ? 131.339 152.772 115.546 1.00 44.52 ?  445 ILE A O     1 
ATOM   3579  C  CB    . ILE A 1 445 ? 130.932 150.247 114.090 1.00 39.74 ?  445 ILE A CB    1 
ATOM   3580  C  CG1   . ILE A 1 445 ? 130.855 149.512 112.749 1.00 37.73 ?  445 ILE A CG1   1 
ATOM   3581  C  CG2   . ILE A 1 445 ? 130.628 149.310 115.246 1.00 39.98 ?  445 ILE A CG2   1 
ATOM   3582  C  CD1   . ILE A 1 445 ? 129.824 148.407 112.701 1.00 37.05 ?  445 ILE A CD1   1 
ATOM   3583  N  N     . ARG A 1 446 ? 129.152 152.625 116.059 1.00 47.24 ?  446 ARG A N     1 
ATOM   3584  C  CA    . ARG A 1 446 ? 129.211 153.582 117.154 1.00 50.94 ?  446 ARG A CA    1 
ATOM   3585  C  C     . ARG A 1 446 ? 129.432 152.915 118.508 1.00 49.67 ?  446 ARG A C     1 
ATOM   3586  O  O     . ARG A 1 446 ? 129.251 153.560 119.546 1.00 45.92 ?  446 ARG A O     1 
ATOM   3587  C  CB    . ARG A 1 446 ? 127.941 154.434 117.175 1.00 47.16 ?  446 ARG A CB    1 
ATOM   3588  C  CG    . ARG A 1 446 ? 126.651 153.637 117.096 1.00 46.72 ?  446 ARG A CG    1 
ATOM   3589  C  CD    . ARG A 1 446 ? 125.474 154.517 116.692 1.00 50.06 ?  446 ARG A CD    1 
ATOM   3590  N  NE    . ARG A 1 446 ? 125.673 155.141 115.387 1.00 52.22 ?  446 ARG A NE    1 
ATOM   3591  C  CZ    . ARG A 1 446 ? 126.063 156.395 115.202 1.00 52.70 ?  446 ARG A CZ    1 
ATOM   3592  N  NH1   . ARG A 1 446 ? 126.291 157.206 116.221 1.00 49.54 1  446 ARG A NH1   1 
ATOM   3593  N  NH2   . ARG A 1 446 ? 126.228 156.846 113.963 1.00 51.25 ?  446 ARG A NH2   1 
ATOM   3594  N  N     . ASN A 1 447 ? 129.819 151.640 118.517 1.00 39.92 ?  447 ASN A N     1 
ATOM   3595  C  CA    . ASN A 1 447 ? 130.181 150.956 119.749 1.00 34.85 ?  447 ASN A CA    1 
ATOM   3596  C  C     . ASN A 1 447 ? 131.517 150.236 119.655 1.00 35.19 ?  447 ASN A C     1 
ATOM   3597  O  O     . ASN A 1 447 ? 131.929 149.599 120.631 1.00 36.74 ?  447 ASN A O     1 
ATOM   3598  C  CB    . ASN A 1 447 ? 129.086 149.958 120.154 1.00 34.46 ?  447 ASN A CB    1 
ATOM   3599  C  CG    . ASN A 1 447 ? 128.338 150.394 121.394 1.00 33.05 ?  447 ASN A CG    1 
ATOM   3600  O  OD1   . ASN A 1 447 ? 128.942 150.703 122.420 1.00 37.76 ?  447 ASN A OD1   1 
ATOM   3601  N  ND2   . ASN A 1 447 ? 127.016 150.431 121.304 1.00 34.04 ?  447 ASN A ND2   1 
ATOM   3602  N  N     . ALA A 1 448 ? 132.201 150.314 118.515 1.00 38.72 ?  448 ALA A N     1 
ATOM   3603  C  CA    . ALA A 1 448 ? 133.550 149.783 118.335 1.00 33.62 ?  448 ALA A CA    1 
ATOM   3604  C  C     . ALA A 1 448 ? 134.414 150.935 117.847 1.00 33.26 ?  448 ALA A C     1 
ATOM   3605  O  O     . ALA A 1 448 ? 134.512 151.179 116.634 1.00 33.62 ?  448 ALA A O     1 
ATOM   3606  C  CB    . ALA A 1 448 ? 133.564 148.614 117.354 1.00 29.25 ?  448 ALA A CB    1 
ATOM   3607  N  N     . PRO A 1 449 ? 135.039 151.688 118.757 1.00 30.75 ?  449 PRO A N     1 
ATOM   3608  C  CA    . PRO A 1 449 ? 135.755 152.905 118.335 1.00 27.60 ?  449 PRO A CA    1 
ATOM   3609  C  C     . PRO A 1 449 ? 136.888 152.642 117.361 1.00 29.34 ?  449 PRO A C     1 
ATOM   3610  O  O     . PRO A 1 449 ? 137.082 153.419 116.417 1.00 29.06 ?  449 PRO A O     1 
ATOM   3611  C  CB    . PRO A 1 449 ? 136.276 153.483 119.659 1.00 27.90 ?  449 PRO A CB    1 
ATOM   3612  C  CG    . PRO A 1 449 ? 135.550 152.748 120.734 1.00 31.86 ?  449 PRO A CG    1 
ATOM   3613  C  CD    . PRO A 1 449 ? 135.200 151.417 120.193 1.00 30.43 ?  449 PRO A CD    1 
ATOM   3614  N  N     . ALA A 1 450 ? 137.642 151.559 117.557 1.00 31.60 ?  450 ALA A N     1 
ATOM   3615  C  CA    . ALA A 1 450 ? 138.767 151.279 116.676 1.00 23.57 ?  450 ALA A CA    1 
ATOM   3616  C  C     . ALA A 1 450 ? 138.300 150.795 115.312 1.00 25.16 ?  450 ALA A C     1 
ATOM   3617  O  O     . ALA A 1 450 ? 138.916 151.131 114.295 1.00 27.25 ?  450 ALA A O     1 
ATOM   3618  C  CB    . ALA A 1 450 ? 139.698 150.257 117.324 1.00 24.69 ?  450 ALA A CB    1 
ATOM   3619  N  N     . VAL A 1 451 ? 137.213 150.024 115.268 1.00 30.39 ?  451 VAL A N     1 
ATOM   3620  C  CA    . VAL A 1 451 ? 136.634 149.619 113.990 1.00 23.44 ?  451 VAL A CA    1 
ATOM   3621  C  C     . VAL A 1 451 ? 136.184 150.844 113.206 1.00 24.66 ?  451 VAL A C     1 
ATOM   3622  O  O     . VAL A 1 451 ? 136.451 150.970 112.006 1.00 30.89 ?  451 VAL A O     1 
ATOM   3623  C  CB    . VAL A 1 451 ? 135.473 148.633 114.217 1.00 25.62 ?  451 VAL A CB    1 
ATOM   3624  C  CG1   . VAL A 1 451 ? 134.610 148.522 112.973 1.00 26.43 ?  451 VAL A CG1   1 
ATOM   3625  C  CG2   . VAL A 1 451 ? 136.007 147.272 114.619 1.00 25.40 ?  451 VAL A CG2   1 
ATOM   3626  N  N     . ARG A 1 452 ? 135.506 151.774 113.881 1.00 24.67 ?  452 ARG A N     1 
ATOM   3627  C  CA    . ARG A 1 452 ? 135.056 152.999 113.228 1.00 25.38 ?  452 ARG A CA    1 
ATOM   3628  C  C     . ARG A 1 452 ? 136.236 153.824 112.728 1.00 26.48 ?  452 ARG A C     1 
ATOM   3629  O  O     . ARG A 1 452 ? 136.234 154.312 111.589 1.00 31.93 ?  452 ARG A O     1 
ATOM   3630  C  CB    . ARG A 1 452 ? 134.203 153.812 114.203 1.00 26.48 ?  452 ARG A CB    1 
ATOM   3631  C  CG    . ARG A 1 452 ? 133.125 154.662 113.561 1.00 29.65 ?  452 ARG A CG    1 
ATOM   3632  C  CD    . ARG A 1 452 ? 133.259 156.111 113.988 1.00 28.18 ?  452 ARG A CD    1 
ATOM   3633  N  NE    . ARG A 1 452 ? 132.873 156.316 115.378 1.00 37.09 ?  452 ARG A NE    1 
ATOM   3634  C  CZ    . ARG A 1 452 ? 131.670 156.708 115.774 1.00 39.49 ?  452 ARG A CZ    1 
ATOM   3635  N  NH1   . ARG A 1 452 ? 130.702 156.952 114.906 1.00 35.94 1  452 ARG A NH1   1 
ATOM   3636  N  NH2   . ARG A 1 452 ? 131.433 156.862 117.073 1.00 36.35 ?  452 ARG A NH2   1 
ATOM   3637  N  N     . ARG A 1 453 ? 137.261 153.986 113.568 1.00 27.41 ?  453 ARG A N     1 
ATOM   3638  C  CA    . ARG A 1 453 ? 138.412 154.796 113.181 1.00 24.98 ?  453 ARG A CA    1 
ATOM   3639  C  C     . ARG A 1 453 ? 139.149 154.179 112.000 1.00 30.87 ?  453 ARG A C     1 
ATOM   3640  O  O     . ARG A 1 453 ? 139.540 154.888 111.067 1.00 35.58 ?  453 ARG A O     1 
ATOM   3641  C  CB    . ARG A 1 453 ? 139.357 154.973 114.369 1.00 26.76 ?  453 ARG A CB    1 
ATOM   3642  C  CG    . ARG A 1 453 ? 140.442 156.007 114.139 1.00 30.43 ?  453 ARG A CG    1 
ATOM   3643  C  CD    . ARG A 1 453 ? 141.601 155.827 115.100 1.00 27.05 ?  453 ARG A CD    1 
ATOM   3644  N  NE    . ARG A 1 453 ? 142.837 156.378 114.560 1.00 29.09 ?  453 ARG A NE    1 
ATOM   3645  C  CZ    . ARG A 1 453 ? 144.047 155.903 114.820 1.00 30.96 ?  453 ARG A CZ    1 
ATOM   3646  N  NH1   . ARG A 1 453 ? 144.224 154.868 115.624 1.00 31.00 1  453 ARG A NH1   1 
ATOM   3647  N  NH2   . ARG A 1 453 ? 145.104 156.479 114.258 1.00 30.21 ?  453 ARG A NH2   1 
ATOM   3648  N  N     . ALA A 1 454 ? 139.341 152.858 112.019 1.00 26.81 ?  454 ALA A N     1 
ATOM   3649  C  CA    . ALA A 1 454 ? 140.039 152.203 110.923 1.00 20.64 ?  454 ALA A CA    1 
ATOM   3650  C  C     . ALA A 1 454 ? 139.202 152.184 109.653 1.00 19.20 ?  454 ALA A C     1 
ATOM   3651  O  O     . ALA A 1 454 ? 139.757 152.230 108.553 1.00 25.25 ?  454 ALA A O     1 
ATOM   3652  C  CB    . ALA A 1 454 ? 140.436 150.785 111.322 1.00 23.13 ?  454 ALA A CB    1 
ATOM   3653  N  N     . ASN A 1 455 ? 137.876 152.116 109.775 1.00 23.57 ?  455 ASN A N     1 
ATOM   3654  C  CA    . ASN A 1 455 ? 137.034 152.214 108.591 1.00 23.02 ?  455 ASN A CA    1 
ATOM   3655  C  C     . ASN A 1 455 ? 137.127 153.599 107.967 1.00 26.24 ?  455 ASN A C     1 
ATOM   3656  O  O     . ASN A 1 455 ? 137.148 153.733 106.738 1.00 32.44 ?  455 ASN A O     1 
ATOM   3657  C  CB    . ASN A 1 455 ? 135.587 151.878 108.945 1.00 21.33 ?  455 ASN A CB    1 
ATOM   3658  C  CG    . ASN A 1 455 ? 134.681 151.867 107.733 1.00 27.83 ?  455 ASN A CG    1 
ATOM   3659  O  OD1   . ASN A 1 455 ? 134.854 151.058 106.823 1.00 34.90 ?  455 ASN A OD1   1 
ATOM   3660  N  ND2   . ASN A 1 455 ? 133.708 152.768 107.712 1.00 26.61 ?  455 ASN A ND2   1 
ATOM   3661  N  N     . LYS A 1 456 ? 137.177 154.643 108.796 1.00 29.69 ?  456 LYS A N     1 
ATOM   3662  C  CA    . LYS A 1 456 ? 137.303 155.993 108.256 1.00 26.25 ?  456 LYS A CA    1 
ATOM   3663  C  C     . LYS A 1 456 ? 138.690 156.241 107.673 1.00 27.17 ?  456 LYS A C     1 
ATOM   3664  O  O     . LYS A 1 456 ? 138.827 156.943 106.665 1.00 31.74 ?  456 LYS A O     1 
ATOM   3665  C  CB    . LYS A 1 456 ? 136.982 157.027 109.333 1.00 26.62 ?  456 LYS A CB    1 
ATOM   3666  C  CG    . LYS A 1 456 ? 135.592 156.896 109.924 1.00 29.67 ?  456 LYS A CG    1 
ATOM   3667  C  CD    . LYS A 1 456 ? 135.216 158.125 110.728 1.00 34.00 ?  456 LYS A CD    1 
ATOM   3668  C  CE    . LYS A 1 456 ? 133.732 158.140 111.049 1.00 32.56 ?  456 LYS A CE    1 
ATOM   3669  N  NZ    . LYS A 1 456 ? 132.908 157.727 109.881 1.00 33.57 1  456 LYS A NZ    1 
ATOM   3670  N  N     . ALA A 1 457 ? 139.730 155.675 108.285 1.00 26.25 ?  457 ALA A N     1 
ATOM   3671  C  CA    . ALA A 1 457 ? 141.099 155.986 107.891 1.00 22.46 ?  457 ALA A CA    1 
ATOM   3672  C  C     . ALA A 1 457 ? 141.608 155.100 106.758 1.00 27.03 ?  457 ALA A C     1 
ATOM   3673  O  O     . ALA A 1 457 ? 142.091 155.604 105.742 1.00 31.58 ?  457 ALA A O     1 
ATOM   3674  C  CB    . ALA A 1 457 ? 142.026 155.869 109.104 1.00 22.61 ?  457 ALA A CB    1 
ATOM   3675  N  N     . MET A 1 458 ? 141.514 153.781 106.922 1.00 29.41 ?  458 MET A N     1 
ATOM   3676  C  CA    . MET A 1 458 ? 142.060 152.851 105.941 1.00 19.45 ?  458 MET A CA    1 
ATOM   3677  C  C     . MET A 1 458 ? 141.198 152.768 104.688 1.00 21.76 ?  458 MET A C     1 
ATOM   3678  O  O     . MET A 1 458 ? 141.729 152.626 103.582 1.00 29.94 ?  458 MET A O     1 
ATOM   3679  C  CB    . MET A 1 458 ? 142.212 151.465 106.566 1.00 22.04 ?  458 MET A CB    1 
ATOM   3680  C  CG    . MET A 1 458 ? 142.907 151.466 107.913 1.00 22.23 ?  458 MET A CG    1 
ATOM   3681  S  SD    . MET A 1 458 ? 144.627 151.981 107.789 1.00 33.05 ?  458 MET A SD    1 
ATOM   3682  C  CE    . MET A 1 458 ? 145.442 150.388 107.711 1.00 25.27 ?  458 MET A CE    1 
ATOM   3683  N  N     . LYS A 1 459 ? 139.876 152.847 104.844 1.00 17.12 ?  459 LYS A N     1 
ATOM   3684  C  CA    . LYS A 1 459 ? 138.937 152.709 103.729 1.00 21.91 ?  459 LYS A CA    1 
ATOM   3685  C  C     . LYS A 1 459 ? 139.157 151.395 102.981 1.00 17.93 ?  459 LYS A C     1 
ATOM   3686  O  O     . LYS A 1 459 ? 139.134 151.348 101.751 1.00 25.40 ?  459 LYS A O     1 
ATOM   3687  C  CB    . LYS A 1 459 ? 139.030 153.900 102.774 1.00 21.80 ?  459 LYS A CB    1 
ATOM   3688  C  CG    . LYS A 1 459 ? 138.970 155.250 103.462 1.00 24.86 ?  459 LYS A CG    1 
ATOM   3689  C  CD    . LYS A 1 459 ? 139.850 156.261 102.756 1.00 25.02 ?  459 LYS A CD    1 
ATOM   3690  C  CE    . LYS A 1 459 ? 139.807 157.607 103.450 1.00 28.55 ?  459 LYS A CE    1 
ATOM   3691  N  NZ    . LYS A 1 459 ? 140.793 158.554 102.864 1.00 31.75 1  459 LYS A NZ    1 
ATOM   3692  N  N     . SER A 1 460 ? 139.372 150.320 103.733 1.00 20.38 ?  460 SER A N     1 
ATOM   3693  C  CA    . SER A 1 460 ? 139.672 149.023 103.146 1.00 14.03 ?  460 SER A CA    1 
ATOM   3694  C  C     . SER A 1 460 ? 138.406 148.352 102.632 1.00 20.49 ?  460 SER A C     1 
ATOM   3695  O  O     . SER A 1 460 ? 137.349 148.416 103.264 1.00 29.78 ?  460 SER A O     1 
ATOM   3696  C  CB    . SER A 1 460 ? 140.355 148.118 104.169 1.00 8.71  ?  460 SER A CB    1 
ATOM   3697  O  OG    . SER A 1 460 ? 141.426 148.786 104.808 1.00 30.12 ?  460 SER A OG    1 
ATOM   3698  N  N     . ILE A 1 461 ? 138.525 147.703 101.476 1.00 13.07 ?  461 ILE A N     1 
ATOM   3699  C  CA    . ILE A 1 461 ? 137.444 146.925 100.892 1.00 14.90 ?  461 ILE A CA    1 
ATOM   3700  C  C     . ILE A 1 461 ? 137.993 145.555 100.528 1.00 15.17 ?  461 ILE A C     1 
ATOM   3701  O  O     . ILE A 1 461 ? 139.201 145.361 100.384 1.00 22.96 ?  461 ILE A O     1 
ATOM   3702  C  CB    . ILE A 1 461 ? 136.830 147.606 99.649  1.00 14.02 ?  461 ILE A CB    1 
ATOM   3703  C  CG1   . ILE A 1 461 ? 137.890 147.781 98.561  1.00 7.16  ?  461 ILE A CG1   1 
ATOM   3704  C  CG2   . ILE A 1 461 ? 136.216 148.945 100.023 1.00 14.31 ?  461 ILE A CG2   1 
ATOM   3705  C  CD1   . ILE A 1 461 ? 137.376 148.439 97.311  1.00 7.09  ?  461 ILE A CD1   1 
ATOM   3706  N  N     . GLY A 1 462 ? 137.087 144.592 100.403 1.00 16.88 ?  462 GLY A N     1 
ATOM   3707  C  CA    . GLY A 1 462 ? 137.480 143.289 99.911  1.00 8.05  ?  462 GLY A CA    1 
ATOM   3708  C  C     . GLY A 1 462 ? 136.692 142.875 98.689  1.00 5.76  ?  462 GLY A C     1 
ATOM   3709  O  O     . GLY A 1 462 ? 135.496 142.592 98.786  1.00 24.60 ?  462 GLY A O     1 
ATOM   3710  N  N     . LEU A 1 463 ? 137.352 142.821 97.538  1.00 13.49 ?  463 LEU A N     1 
ATOM   3711  C  CA    . LEU A 1 463 ? 136.720 142.407 96.293  1.00 11.99 ?  463 LEU A CA    1 
ATOM   3712  C  C     . LEU A 1 463 ? 137.227 141.015 95.944  1.00 15.77 ?  463 LEU A C     1 
ATOM   3713  O  O     . LEU A 1 463 ? 138.372 140.853 95.511  1.00 27.78 ?  463 LEU A O     1 
ATOM   3714  C  CB    . LEU A 1 463 ? 137.009 143.402 95.171  1.00 18.12 ?  463 LEU A CB    1 
ATOM   3715  C  CG    . LEU A 1 463 ? 136.419 143.061 93.800  1.00 17.19 ?  463 LEU A CG    1 
ATOM   3716  C  CD1   . LEU A 1 463 ? 134.934 142.766 93.911  1.00 7.19  ?  463 LEU A CD1   1 
ATOM   3717  C  CD2   . LEU A 1 463 ? 136.672 144.185 92.809  1.00 15.33 ?  463 LEU A CD2   1 
ATOM   3718  N  N     . GLY A 1 464 ? 136.375 140.011 96.140  1.00 17.43 ?  464 GLY A N     1 
ATOM   3719  C  CA    . GLY A 1 464 ? 136.713 138.639 95.845  1.00 11.70 ?  464 GLY A CA    1 
ATOM   3720  C  C     . GLY A 1 464 ? 136.159 138.179 94.510  1.00 11.76 ?  464 GLY A C     1 
ATOM   3721  O  O     . GLY A 1 464 ? 135.633 138.956 93.711  1.00 18.98 ?  464 GLY A O     1 
ATOM   3722  N  N     . ALA A 1 465 ? 136.293 136.880 94.272  1.00 14.71 ?  465 ALA A N     1 
ATOM   3723  C  CA    . ALA A 1 465 ? 135.758 136.255 93.078  1.00 11.19 ?  465 ALA A CA    1 
ATOM   3724  C  C     . ALA A 1 465 ? 135.238 134.873 93.436  1.00 16.81 ?  465 ALA A C     1 
ATOM   3725  O  O     . ALA A 1 465 ? 135.648 134.273 94.432  1.00 29.03 ?  465 ALA A O     1 
ATOM   3726  C  CB    . ALA A 1 465 ? 136.813 136.165 91.968  1.00 15.71 ?  465 ALA A CB    1 
ATOM   3727  N  N     . MET A 1 466 ? 134.313 134.378 92.618  1.00 22.27 ?  466 MET A N     1 
ATOM   3728  C  CA    . MET A 1 466 ? 133.810 133.020 92.744  1.00 21.62 ?  466 MET A CA    1 
ATOM   3729  C  C     . MET A 1 466 ? 133.631 132.443 91.347  1.00 19.91 ?  466 MET A C     1 
ATOM   3730  O  O     . MET A 1 466 ? 133.903 133.105 90.340  1.00 23.91 ?  466 MET A O     1 
ATOM   3731  C  CB    . MET A 1 466 ? 132.492 132.961 93.521  1.00 26.40 ?  466 MET A CB    1 
ATOM   3732  C  CG    . MET A 1 466 ? 131.444 133.953 93.066  1.00 27.60 ?  466 MET A CG    1 
ATOM   3733  S  SD    . MET A 1 466 ? 129.934 133.778 94.027  1.00 40.18 ?  466 MET A SD    1 
ATOM   3734  C  CE    . MET A 1 466 ? 129.340 135.457 94.017  1.00 26.82 ?  466 MET A CE    1 
ATOM   3735  N  N     . ASN A 1 467 ? 133.166 131.194 91.298  1.00 20.36 ?  467 ASN A N     1 
ATOM   3736  C  CA    . ASN A 1 467 ? 132.905 130.483 90.047  1.00 20.74 ?  467 ASN A CA    1 
ATOM   3737  C  C     . ASN A 1 467 ? 134.177 130.270 89.234  1.00 21.97 ?  467 ASN A C     1 
ATOM   3738  O  O     . ASN A 1 467 ? 134.129 130.169 88.008  1.00 27.77 ?  467 ASN A O     1 
ATOM   3739  C  CB    . ASN A 1 467 ? 131.849 131.200 89.201  1.00 21.02 ?  467 ASN A CB    1 
ATOM   3740  C  CG    . ASN A 1 467 ? 130.829 130.251 88.618  1.00 26.60 ?  467 ASN A CG    1 
ATOM   3741  O  OD1   . ASN A 1 467 ? 130.820 129.063 88.932  1.00 30.58 ?  467 ASN A OD1   1 
ATOM   3742  N  ND2   . ASN A 1 467 ? 129.954 130.773 87.773  1.00 28.87 ?  467 ASN A ND2   1 
ATOM   3743  N  N     . LEU A 1 468 ? 135.330 130.208 89.903  1.00 17.20 ?  468 LEU A N     1 
ATOM   3744  C  CA    . LEU A 1 468 ? 136.563 129.880 89.197  1.00 18.24 ?  468 LEU A CA    1 
ATOM   3745  C  C     . LEU A 1 468 ? 136.529 128.447 88.687  1.00 22.11 ?  468 LEU A C     1 
ATOM   3746  O  O     . LEU A 1 468 ? 136.778 128.190 87.502  1.00 24.19 ?  468 LEU A O     1 
ATOM   3747  C  CB    . LEU A 1 468 ? 137.769 130.096 90.111  1.00 22.48 ?  468 LEU A CB    1 
ATOM   3748  C  CG    . LEU A 1 468 ? 139.094 129.545 89.577  1.00 20.24 ?  468 LEU A CG    1 
ATOM   3749  C  CD1   . LEU A 1 468 ? 139.618 130.402 88.440  1.00 17.75 ?  468 LEU A CD1   1 
ATOM   3750  C  CD2   . LEU A 1 468 ? 140.125 129.426 90.680  1.00 14.67 ?  468 LEU A CD2   1 
ATOM   3751  N  N     . HIS A 1 469 ? 136.205 127.497 89.567  1.00 25.00 ?  469 HIS A N     1 
ATOM   3752  C  CA    . HIS A 1 469 ? 136.108 126.108 89.142  1.00 15.91 ?  469 HIS A CA    1 
ATOM   3753  C  C     . HIS A 1 469 ? 134.942 125.908 88.187  1.00 25.43 ?  469 HIS A C     1 
ATOM   3754  O  O     . HIS A 1 469 ? 135.042 125.122 87.241  1.00 35.75 ?  469 HIS A O     1 
ATOM   3755  C  CB    . HIS A 1 469 ? 135.973 125.184 90.350  1.00 20.66 ?  469 HIS A CB    1 
ATOM   3756  C  CG    . HIS A 1 469 ? 136.150 123.734 90.018  1.00 24.47 ?  469 HIS A CG    1 
ATOM   3757  N  ND1   . HIS A 1 469 ? 135.920 122.728 90.930  1.00 30.41 ?  469 HIS A ND1   1 
ATOM   3758  C  CD2   . HIS A 1 469 ? 136.543 123.123 88.876  1.00 25.57 ?  469 HIS A CD2   1 
ATOM   3759  C  CE1   . HIS A 1 469 ? 136.156 121.559 90.362  1.00 26.91 ?  469 HIS A CE1   1 
ATOM   3760  N  NE2   . HIS A 1 469 ? 136.536 121.771 89.115  1.00 23.55 ?  469 HIS A NE2   1 
ATOM   3761  N  N     . GLY A 1 470 ? 133.827 126.601 88.417  1.00 23.18 ?  470 GLY A N     1 
ATOM   3762  C  CA    . GLY A 1 470 ? 132.713 126.505 87.488  1.00 18.91 ?  470 GLY A CA    1 
ATOM   3763  C  C     . GLY A 1 470 ? 133.078 126.993 86.101  1.00 13.76 ?  470 GLY A C     1 
ATOM   3764  O  O     . GLY A 1 470 ? 132.763 126.349 85.097  1.00 30.84 ?  470 GLY A O     1 
ATOM   3765  N  N     . TYR A 1 471 ? 133.766 128.135 86.030  1.00 17.80 ?  471 TYR A N     1 
ATOM   3766  C  CA    . TYR A 1 471 ? 134.192 128.667 84.741  1.00 20.66 ?  471 TYR A CA    1 
ATOM   3767  C  C     . TYR A 1 471 ? 135.181 127.733 84.056  1.00 26.74 ?  471 TYR A C     1 
ATOM   3768  O  O     . TYR A 1 471 ? 135.093 127.508 82.845  1.00 30.29 ?  471 TYR A O     1 
ATOM   3769  C  CB    . TYR A 1 471 ? 134.808 130.054 84.921  1.00 21.83 ?  471 TYR A CB    1 
ATOM   3770  C  CG    . TYR A 1 471 ? 135.383 130.631 83.651  1.00 25.96 ?  471 TYR A CG    1 
ATOM   3771  C  CD1   . TYR A 1 471 ? 134.555 131.162 82.673  1.00 25.94 ?  471 TYR A CD1   1 
ATOM   3772  C  CD2   . TYR A 1 471 ? 136.751 130.633 83.423  1.00 20.53 ?  471 TYR A CD2   1 
ATOM   3773  C  CE1   . TYR A 1 471 ? 135.073 131.687 81.508  1.00 26.67 ?  471 TYR A CE1   1 
ATOM   3774  C  CE2   . TYR A 1 471 ? 137.279 131.153 82.260  1.00 20.47 ?  471 TYR A CE2   1 
ATOM   3775  C  CZ    . TYR A 1 471 ? 136.435 131.679 81.307  1.00 28.50 ?  471 TYR A CZ    1 
ATOM   3776  O  OH    . TYR A 1 471 ? 136.958 132.199 80.148  1.00 31.36 ?  471 TYR A OH    1 
ATOM   3777  N  N     . LEU A 1 472 ? 136.135 127.185 84.813  1.00 22.56 ?  472 LEU A N     1 
ATOM   3778  C  CA    . LEU A 1 472 ? 137.130 126.302 84.210  1.00 21.54 ?  472 LEU A CA    1 
ATOM   3779  C  C     . LEU A 1 472 ? 136.504 124.995 83.736  1.00 26.87 ?  472 LEU A C     1 
ATOM   3780  O  O     . LEU A 1 472 ? 136.821 124.511 82.643  1.00 31.87 ?  472 LEU A O     1 
ATOM   3781  C  CB    . LEU A 1 472 ? 138.258 126.028 85.204  1.00 27.45 ?  472 LEU A CB    1 
ATOM   3782  C  CG    . LEU A 1 472 ? 139.115 127.230 85.607  1.00 29.85 ?  472 LEU A CG    1 
ATOM   3783  C  CD1   . LEU A 1 472 ? 139.915 126.908 86.855  1.00 22.43 ?  472 LEU A CD1   1 
ATOM   3784  C  CD2   . LEU A 1 472 ? 140.028 127.657 84.471  1.00 22.59 ?  472 LEU A CD2   1 
ATOM   3785  N  N     . ALA A 1 473 ? 135.620 124.406 84.544  1.00 28.89 ?  473 ALA A N     1 
ATOM   3786  C  CA    . ALA A 1 473 ? 134.987 123.147 84.172  1.00 25.05 ?  473 ALA A CA    1 
ATOM   3787  C  C     . ALA A 1 473 ? 134.035 123.329 82.998  1.00 32.50 ?  473 ALA A C     1 
ATOM   3788  O  O     . ALA A 1 473 ? 133.910 122.437 82.152  1.00 40.07 ?  473 ALA A O     1 
ATOM   3789  C  CB    . ALA A 1 473 ? 134.253 122.560 85.376  1.00 26.38 ?  473 ALA A CB    1 
ATOM   3790  N  N     . GLN A 1 474 ? 133.355 124.473 82.929  1.00 28.34 ?  474 GLN A N     1 
ATOM   3791  C  CA    . GLN A 1 474 ? 132.482 124.749 81.798  1.00 25.63 ?  474 GLN A CA    1 
ATOM   3792  C  C     . GLN A 1 474 ? 133.249 125.192 80.560  1.00 24.52 ?  474 GLN A C     1 
ATOM   3793  O  O     . GLN A 1 474 ? 132.635 125.371 79.504  1.00 35.27 ?  474 GLN A O     1 
ATOM   3794  C  CB    . GLN A 1 474 ? 131.446 125.808 82.179  1.00 27.87 ?  474 GLN A CB    1 
ATOM   3795  C  CG    . GLN A 1 474 ? 130.321 125.264 83.040  1.00 31.27 ?  474 GLN A CG    1 
ATOM   3796  C  CD    . GLN A 1 474 ? 129.479 126.355 83.659  1.00 30.88 ?  474 GLN A CD    1 
ATOM   3797  O  OE1   . GLN A 1 474 ? 128.758 127.068 82.963  1.00 33.25 ?  474 GLN A OE1   1 
ATOM   3798  N  NE2   . GLN A 1 474 ? 129.563 126.491 84.976  1.00 31.70 ?  474 GLN A NE2   1 
ATOM   3799  N  N     . ASN A 1 475 ? 134.563 125.378 80.665  1.00 30.94 ?  475 ASN A N     1 
ATOM   3800  C  CA    . ASN A 1 475 ? 135.409 125.702 79.526  1.00 32.64 ?  475 ASN A CA    1 
ATOM   3801  C  C     . ASN A 1 475 ? 136.393 124.586 79.199  1.00 33.12 ?  475 ASN A C     1 
ATOM   3802  O  O     . ASN A 1 475 ? 137.343 124.813 78.444  1.00 36.54 ?  475 ASN A O     1 
ATOM   3803  C  CB    . ASN A 1 475 ? 136.162 127.009 79.781  1.00 34.58 ?  475 ASN A CB    1 
ATOM   3804  C  CG    . ASN A 1 475 ? 135.275 128.227 79.642  1.00 30.33 ?  475 ASN A CG    1 
ATOM   3805  O  OD1   . ASN A 1 475 ? 135.193 128.831 78.574  1.00 35.59 ?  475 ASN A OD1   1 
ATOM   3806  N  ND2   . ASN A 1 475 ? 134.597 128.589 80.723  1.00 25.96 ?  475 ASN A ND2   1 
ATOM   3807  N  N     . GLY A 1 476 ? 136.189 123.394 79.750  1.00 29.91 ?  476 GLY A N     1 
ATOM   3808  C  CA    . GLY A 1 476 ? 137.066 122.268 79.479  1.00 30.17 ?  476 GLY A CA    1 
ATOM   3809  C  C     . GLY A 1 476 ? 138.475 122.422 80.006  1.00 34.66 ?  476 GLY A C     1 
ATOM   3810  O  O     . GLY A 1 476 ? 139.433 122.044 79.318  1.00 36.43 ?  476 GLY A O     1 
ATOM   3811  N  N     . ILE A 1 477 ? 138.631 122.968 81.209  1.00 31.37 ?  477 ILE A N     1 
ATOM   3812  C  CA    . ILE A 1 477 ? 139.935 123.146 81.833  1.00 28.71 ?  477 ILE A CA    1 
ATOM   3813  C  C     . ILE A 1 477 ? 139.908 122.483 83.202  1.00 31.58 ?  477 ILE A C     1 
ATOM   3814  O  O     . ILE A 1 477 ? 139.021 122.763 84.015  1.00 35.25 ?  477 ILE A O     1 
ATOM   3815  C  CB    . ILE A 1 477 ? 140.311 124.635 81.963  1.00 28.00 ?  477 ILE A CB    1 
ATOM   3816  C  CG1   . ILE A 1 477 ? 140.271 125.320 80.597  1.00 30.91 ?  477 ILE A CG1   1 
ATOM   3817  C  CG2   . ILE A 1 477 ? 141.684 124.780 82.588  1.00 31.37 ?  477 ILE A CG2   1 
ATOM   3818  C  CD1   . ILE A 1 477 ? 140.156 126.823 80.674  1.00 32.68 ?  477 ILE A CD1   1 
ATOM   3819  N  N     . ALA A 1 478 ? 140.873 121.601 83.451  1.00 31.56 ?  478 ALA A N     1 
ATOM   3820  C  CA    . ALA A 1 478 ? 140.986 120.970 84.757  1.00 26.59 ?  478 ALA A CA    1 
ATOM   3821  C  C     . ALA A 1 478 ? 141.509 121.968 85.780  1.00 33.48 ?  478 ALA A C     1 
ATOM   3822  O  O     . ALA A 1 478 ? 142.354 122.810 85.471  1.00 35.57 ?  478 ALA A O     1 
ATOM   3823  C  CB    . ALA A 1 478 ? 141.910 119.756 84.684  1.00 28.38 ?  478 ALA A CB    1 
ATOM   3824  N  N     . TYR A 1 479 ? 141.001 121.866 87.011  1.00 31.35 ?  479 TYR A N     1 
ATOM   3825  C  CA    . TYR A 1 479 ? 141.408 122.794 88.061  1.00 22.61 ?  479 TYR A CA    1 
ATOM   3826  C  C     . TYR A 1 479 ? 142.899 122.679 88.353  1.00 30.04 ?  479 TYR A C     1 
ATOM   3827  O  O     . TYR A 1 479 ? 143.573 123.689 88.584  1.00 39.24 ?  479 TYR A O     1 
ATOM   3828  C  CB    . TYR A 1 479 ? 140.589 122.540 89.326  1.00 21.64 ?  479 TYR A CB    1 
ATOM   3829  C  CG    . TYR A 1 479 ? 140.748 123.596 90.396  1.00 27.42 ?  479 TYR A CG    1 
ATOM   3830  C  CD1   . TYR A 1 479 ? 139.922 124.710 90.423  1.00 23.50 ?  479 TYR A CD1   1 
ATOM   3831  C  CD2   . TYR A 1 479 ? 141.715 123.474 91.385  1.00 28.82 ?  479 TYR A CD2   1 
ATOM   3832  C  CE1   . TYR A 1 479 ? 140.057 125.674 91.397  1.00 24.74 ?  479 TYR A CE1   1 
ATOM   3833  C  CE2   . TYR A 1 479 ? 141.858 124.436 92.363  1.00 26.82 ?  479 TYR A CE2   1 
ATOM   3834  C  CZ    . TYR A 1 479 ? 141.027 125.533 92.364  1.00 30.44 ?  479 TYR A CZ    1 
ATOM   3835  O  OH    . TYR A 1 479 ? 141.163 126.495 93.337  1.00 31.19 ?  479 TYR A OH    1 
ATOM   3836  N  N     . GLU A 1 480 ? 143.430 121.457 88.351  1.00 34.75 ?  480 GLU A N     1 
ATOM   3837  C  CA    . GLU A 1 480 ? 144.843 121.236 88.618  1.00 30.47 ?  480 GLU A CA    1 
ATOM   3838  C  C     . GLU A 1 480 ? 145.731 121.511 87.414  1.00 32.31 ?  480 GLU A C     1 
ATOM   3839  O  O     . GLU A 1 480 ? 146.957 121.523 87.564  1.00 38.83 ?  480 GLU A O     1 
ATOM   3840  C  CB    . GLU A 1 480 ? 145.075 119.797 89.074  1.00 35.32 ?  480 GLU A CB    1 
ATOM   3841  C  CG    . GLU A 1 480 ? 144.299 119.384 90.300  1.00 33.17 ?  480 GLU A CG    1 
ATOM   3842  C  CD    . GLU A 1 480 ? 144.041 117.895 90.323  1.00 41.41 ?  480 GLU A CD    1 
ATOM   3843  O  OE1   . GLU A 1 480 ? 143.027 117.458 89.740  1.00 41.14 ?  480 GLU A OE1   1 
ATOM   3844  O  OE2   . GLU A 1 480 ? 144.852 117.158 90.919  1.00 42.62 -1 480 GLU A OE2   1 
ATOM   3845  N  N     . SER A 1 481 ? 145.154 121.722 86.237  1.00 33.54 ?  481 SER A N     1 
ATOM   3846  C  CA    . SER A 1 481 ? 145.951 121.872 85.034  1.00 32.41 ?  481 SER A CA    1 
ATOM   3847  C  C     . SER A 1 481 ? 146.736 123.184 85.060  1.00 34.48 ?  481 SER A C     1 
ATOM   3848  O  O     . SER A 1 481 ? 146.311 124.161 85.680  1.00 37.49 ?  481 SER A O     1 
ATOM   3849  C  CB    . SER A 1 481 ? 145.059 121.826 83.797  1.00 32.23 ?  481 SER A CB    1 
ATOM   3850  O  OG    . SER A 1 481 ? 144.465 123.087 83.551  1.00 36.70 ?  481 SER A OG    1 
ATOM   3851  N  N     . PRO A 1 482 ? 147.900 123.221 84.407  1.00 39.26 ?  482 PRO A N     1 
ATOM   3852  C  CA    . PRO A 1 482 ? 148.633 124.492 84.297  1.00 35.92 ?  482 PRO A CA    1 
ATOM   3853  C  C     . PRO A 1 482 ? 147.860 125.571 83.562  1.00 35.70 ?  482 PRO A C     1 
ATOM   3854  O  O     . PRO A 1 482 ? 148.080 126.761 83.821  1.00 39.30 ?  482 PRO A O     1 
ATOM   3855  C  CB    . PRO A 1 482 ? 149.908 124.095 83.539  1.00 35.33 ?  482 PRO A CB    1 
ATOM   3856  C  CG    . PRO A 1 482 ? 150.047 122.630 83.762  1.00 36.84 ?  482 PRO A CG    1 
ATOM   3857  C  CD    . PRO A 1 482 ? 148.653 122.096 83.830  1.00 40.09 ?  482 PRO A CD    1 
ATOM   3858  N  N     . GLU A 1 483 ? 146.967 125.193 82.645  1.00 37.21 ?  483 GLU A N     1 
ATOM   3859  C  CA    . GLU A 1 483 ? 146.156 126.183 81.943  1.00 36.11 ?  483 GLU A CA    1 
ATOM   3860  C  C     . GLU A 1 483 ? 145.214 126.903 82.899  1.00 33.32 ?  483 GLU A C     1 
ATOM   3861  O  O     . GLU A 1 483 ? 144.959 128.103 82.745  1.00 36.83 ?  483 GLU A O     1 
ATOM   3862  C  CB    . GLU A 1 483 ? 145.371 125.513 80.816  1.00 38.31 ?  483 GLU A CB    1 
ATOM   3863  C  CG    . GLU A 1 483 ? 146.234 125.034 79.664  1.00 40.47 ?  483 GLU A CG    1 
ATOM   3864  C  CD    . GLU A 1 483 ? 146.711 123.609 79.851  1.00 43.75 ?  483 GLU A CD    1 
ATOM   3865  O  OE1   . GLU A 1 483 ? 146.467 123.038 80.934  1.00 41.03 ?  483 GLU A OE1   1 
ATOM   3866  O  OE2   . GLU A 1 483 ? 147.336 123.059 78.921  1.00 43.14 -1 483 GLU A OE2   1 
ATOM   3867  N  N     . ALA A 1 484 ? 144.683 126.185 83.890  1.00 27.96 ?  484 ALA A N     1 
ATOM   3868  C  CA    . ALA A 1 484 ? 143.832 126.820 84.889  1.00 28.48 ?  484 ALA A CA    1 
ATOM   3869  C  C     . ALA A 1 484 ? 144.602 127.860 85.689  1.00 29.73 ?  484 ALA A C     1 
ATOM   3870  O  O     . ALA A 1 484 ? 144.100 128.961 85.940  1.00 31.79 ?  484 ALA A O     1 
ATOM   3871  C  CB    . ALA A 1 484 ? 143.238 125.766 85.819  1.00 27.81 ?  484 ALA A CB    1 
ATOM   3872  N  N     . ARG A 1 485 ? 145.828 127.527 86.100  1.00 30.89 ?  485 ARG A N     1 
ATOM   3873  C  CA    . ARG A 1 485 ? 146.648 128.489 86.824  1.00 24.15 ?  485 ARG A CA    1 
ATOM   3874  C  C     . ARG A 1 485 ? 147.050 129.659 85.939  1.00 25.15 ?  485 ARG A C     1 
ATOM   3875  O  O     . ARG A 1 485 ? 147.153 130.788 86.422  1.00 35.58 ?  485 ARG A O     1 
ATOM   3876  C  CB    . ARG A 1 485 ? 147.885 127.799 87.397  1.00 27.04 ?  485 ARG A CB    1 
ATOM   3877  C  CG    . ARG A 1 485 ? 147.581 126.894 88.573  1.00 26.39 ?  485 ARG A CG    1 
ATOM   3878  C  CD    . ARG A 1 485 ? 148.852 126.409 89.239  1.00 28.57 ?  485 ARG A CD    1 
ATOM   3879  N  NE    . ARG A 1 485 ? 149.681 125.629 88.330  1.00 31.77 ?  485 ARG A NE    1 
ATOM   3880  C  CZ    . ARG A 1 485 ? 149.509 124.339 88.079  1.00 32.64 ?  485 ARG A CZ    1 
ATOM   3881  N  NH1   . ARG A 1 485 ? 148.539 123.646 88.653  1.00 30.58 1  485 ARG A NH1   1 
ATOM   3882  N  NH2   . ARG A 1 485 ? 150.333 123.728 87.233  1.00 29.50 ?  485 ARG A NH2   1 
ATOM   3883  N  N     . ASP A 1 486 ? 147.273 129.412 84.648  1.00 30.78 ?  486 ASP A N     1 
ATOM   3884  C  CA    . ASP A 1 486 ? 147.553 130.499 83.714  1.00 29.20 ?  486 ASP A CA    1 
ATOM   3885  C  C     . ASP A 1 486 ? 146.368 131.454 83.613  1.00 29.58 ?  486 ASP A C     1 
ATOM   3886  O  O     . ASP A 1 486 ? 146.534 132.684 83.648  1.00 36.63 ?  486 ASP A O     1 
ATOM   3887  C  CB    . ASP A 1 486 ? 147.900 129.913 82.346  1.00 33.34 ?  486 ASP A CB    1 
ATOM   3888  C  CG    . ASP A 1 486 ? 148.364 130.959 81.364  1.00 40.71 ?  486 ASP A CG    1 
ATOM   3889  O  OD1   . ASP A 1 486 ? 149.302 131.713 81.690  1.00 42.51 ?  486 ASP A OD1   1 
ATOM   3890  O  OD2   . ASP A 1 486 ? 147.791 131.019 80.257  1.00 39.27 -1 486 ASP A OD2   1 
ATOM   3891  N  N     . PHE A 1 487 ? 145.159 130.901 83.499  1.00 30.32 ?  487 PHE A N     1 
ATOM   3892  C  CA    . PHE A 1 487 ? 143.972 131.744 83.462  1.00 25.86 ?  487 PHE A CA    1 
ATOM   3893  C  C     . PHE A 1 487 ? 143.813 132.523 84.756  1.00 25.25 ?  487 PHE A C     1 
ATOM   3894  O  O     . PHE A 1 487 ? 143.476 133.708 84.732  1.00 31.24 ?  487 PHE A O     1 
ATOM   3895  C  CB    . PHE A 1 487 ? 142.711 130.925 83.206  1.00 26.95 ?  487 PHE A CB    1 
ATOM   3896  C  CG    . PHE A 1 487 ? 141.455 131.653 83.589  1.00 29.75 ?  487 PHE A CG    1 
ATOM   3897  C  CD1   . PHE A 1 487 ? 140.960 132.666 82.787  1.00 26.34 ?  487 PHE A CD1   1 
ATOM   3898  C  CD2   . PHE A 1 487 ? 140.791 131.357 84.769  1.00 26.22 ?  487 PHE A CD2   1 
ATOM   3899  C  CE1   . PHE A 1 487 ? 139.823 133.356 83.140  1.00 26.84 ?  487 PHE A CE1   1 
ATOM   3900  C  CE2   . PHE A 1 487 ? 139.652 132.046 85.126  1.00 25.28 ?  487 PHE A CE2   1 
ATOM   3901  C  CZ    . PHE A 1 487 ? 139.169 133.047 84.309  1.00 28.34 ?  487 PHE A CZ    1 
ATOM   3902  N  N     . ALA A 1 488 ? 144.011 131.862 85.898  1.00 25.81 ?  488 ALA A N     1 
ATOM   3903  C  CA    . ALA A 1 488 ? 143.881 132.551 87.175  1.00 20.51 ?  488 ALA A CA    1 
ATOM   3904  C  C     . ALA A 1 488 ? 144.898 133.676 87.290  1.00 27.80 ?  488 ALA A C     1 
ATOM   3905  O  O     . ALA A 1 488 ? 144.570 134.777 87.745  1.00 34.78 ?  488 ALA A O     1 
ATOM   3906  C  CB    . ALA A 1 488 ? 144.038 131.559 88.325  1.00 18.44 ?  488 ALA A CB    1 
ATOM   3907  N  N     . ASN A 1 489 ? 146.135 133.424 86.857  1.00 28.19 ?  489 ASN A N     1 
ATOM   3908  C  CA    . ASN A 1 489 ? 147.164 134.454 86.865  1.00 20.94 ?  489 ASN A CA    1 
ATOM   3909  C  C     . ASN A 1 489 ? 146.726 135.669 86.061  1.00 20.93 ?  489 ASN A C     1 
ATOM   3910  O  O     . ASN A 1 489 ? 146.722 136.794 86.570  1.00 30.25 ?  489 ASN A O     1 
ATOM   3911  C  CB    . ASN A 1 489 ? 148.467 133.879 86.310  1.00 22.28 ?  489 ASN A CB    1 
ATOM   3912  C  CG    . ASN A 1 489 ? 149.683 134.670 86.730  1.00 30.45 ?  489 ASN A CG    1 
ATOM   3913  O  OD1   . ASN A 1 489 ? 149.826 135.041 87.893  1.00 36.75 ?  489 ASN A OD1   1 
ATOM   3914  N  ND2   . ASN A 1 489 ? 150.577 134.923 85.783  1.00 28.71 ?  489 ASN A ND2   1 
ATOM   3915  N  N     . THR A 1 490 ? 146.322 135.454 84.806  1.00 26.43 ?  490 THR A N     1 
ATOM   3916  C  CA    . THR A 1 490 ? 145.937 136.585 83.964  1.00 24.41 ?  490 THR A CA    1 
ATOM   3917  C  C     . THR A 1 490 ? 144.703 137.294 84.510  1.00 26.18 ?  490 THR A C     1 
ATOM   3918  O  O     . THR A 1 490 ? 144.667 138.529 84.588  1.00 27.97 ?  490 THR A O     1 
ATOM   3919  C  CB    . THR A 1 490 ? 145.693 136.117 82.531  1.00 26.36 ?  490 THR A CB    1 
ATOM   3920  O  OG1   . THR A 1 490 ? 146.838 135.394 82.066  1.00 31.50 ?  490 THR A OG1   1 
ATOM   3921  C  CG2   . THR A 1 490 ? 145.448 137.308 81.619  1.00 25.93 ?  490 THR A CG2   1 
ATOM   3922  N  N     . PHE A 1 491 ? 143.687 136.527 84.910  1.00 21.58 ?  491 PHE A N     1 
ATOM   3923  C  CA    . PHE A 1 491 ? 142.431 137.106 85.367  1.00 18.72 ?  491 PHE A CA    1 
ATOM   3924  C  C     . PHE A 1 491 ? 142.635 137.949 86.616  1.00 25.92 ?  491 PHE A C     1 
ATOM   3925  O  O     . PHE A 1 491 ? 142.152 139.082 86.699  1.00 28.50 ?  491 PHE A O     1 
ATOM   3926  C  CB    . PHE A 1 491 ? 141.415 135.994 85.632  1.00 24.90 ?  491 PHE A CB    1 
ATOM   3927  C  CG    . PHE A 1 491 ? 140.109 136.483 86.185  1.00 22.44 ?  491 PHE A CG    1 
ATOM   3928  C  CD1   . PHE A 1 491 ? 139.107 136.919 85.339  1.00 18.33 ?  491 PHE A CD1   1 
ATOM   3929  C  CD2   . PHE A 1 491 ? 139.883 136.509 87.551  1.00 18.60 ?  491 PHE A CD2   1 
ATOM   3930  C  CE1   . PHE A 1 491 ? 137.908 137.373 85.840  1.00 15.30 ?  491 PHE A CE1   1 
ATOM   3931  C  CE2   . PHE A 1 491 ? 138.688 136.965 88.057  1.00 18.33 ?  491 PHE A CE2   1 
ATOM   3932  C  CZ    . PHE A 1 491 ? 137.698 137.397 87.200  1.00 19.82 ?  491 PHE A CZ    1 
ATOM   3933  N  N     . PHE A 1 492 ? 143.354 137.413 87.601  1.00 20.75 ?  492 PHE A N     1 
ATOM   3934  C  CA    . PHE A 1 492 ? 143.522 138.146 88.843  1.00 13.53 ?  492 PHE A CA    1 
ATOM   3935  C  C     . PHE A 1 492 ? 144.562 139.249 88.733  1.00 12.28 ?  492 PHE A C     1 
ATOM   3936  O  O     . PHE A 1 492 ? 144.458 140.239 89.461  1.00 22.08 ?  492 PHE A O     1 
ATOM   3937  C  CB    . PHE A 1 492 ? 143.851 137.175 89.974  1.00 20.06 ?  492 PHE A CB    1 
ATOM   3938  C  CG    . PHE A 1 492 ? 142.666 136.378 90.427  1.00 16.34 ?  492 PHE A CG    1 
ATOM   3939  C  CD1   . PHE A 1 492 ? 141.708 136.947 91.248  1.00 15.80 ?  492 PHE A CD1   1 
ATOM   3940  C  CD2   . PHE A 1 492 ? 142.484 135.076 89.998  1.00 21.73 ?  492 PHE A CD2   1 
ATOM   3941  C  CE1   . PHE A 1 492 ? 140.608 136.222 91.653  1.00 14.75 ?  492 PHE A CE1   1 
ATOM   3942  C  CE2   . PHE A 1 492 ? 141.384 134.347 90.399  1.00 16.11 ?  492 PHE A CE2   1 
ATOM   3943  C  CZ    . PHE A 1 492 ? 140.447 134.920 91.228  1.00 15.69 ?  492 PHE A CZ    1 
ATOM   3944  N  N     . MET A 1 493 ? 145.525 139.143 87.813  1.00 13.10 ?  493 MET A N     1 
ATOM   3945  C  CA    . MET A 1 493 ? 146.363 140.298 87.521  1.00 22.63 ?  493 MET A CA    1 
ATOM   3946  C  C     . MET A 1 493 ? 145.525 141.426 86.938  1.00 18.41 ?  493 MET A C     1 
ATOM   3947  O  O     . MET A 1 493 ? 145.709 142.593 87.294  1.00 28.96 ?  493 MET A O     1 
ATOM   3948  C  CB    . MET A 1 493 ? 147.499 139.907 86.573  1.00 25.38 ?  493 MET A CB    1 
ATOM   3949  C  CG    . MET A 1 493 ? 148.233 141.071 85.891  1.00 20.10 ?  493 MET A CG    1 
ATOM   3950  S  SD    . MET A 1 493 ? 147.439 141.795 84.440  1.00 34.53 ?  493 MET A SD    1 
ATOM   3951  C  CE    . MET A 1 493 ? 147.450 140.399 83.324  1.00 28.29 ?  493 MET A CE    1 
ATOM   3952  N  N     . MET A 1 494 ? 144.593 141.094 86.040  1.00 22.19 ?  494 MET A N     1 
ATOM   3953  C  CA    . MET A 1 494 ? 143.735 142.122 85.460  1.00 17.81 ?  494 MET A CA    1 
ATOM   3954  C  C     . MET A 1 494 ? 142.819 142.730 86.516  1.00 19.45 ?  494 MET A C     1 
ATOM   3955  O  O     . MET A 1 494 ? 142.593 143.947 86.530  1.00 32.12 ?  494 MET A O     1 
ATOM   3956  C  CB    . MET A 1 494 ? 142.919 141.531 84.311  1.00 24.00 ?  494 MET A CB    1 
ATOM   3957  C  CG    . MET A 1 494 ? 143.639 141.582 82.980  1.00 23.09 ?  494 MET A CG    1 
ATOM   3958  S  SD    . MET A 1 494 ? 142.880 140.622 81.662  1.00 41.86 ?  494 MET A SD    1 
ATOM   3959  C  CE    . MET A 1 494 ? 141.391 141.571 81.383  1.00 27.84 ?  494 MET A CE    1 
ATOM   3960  N  N     . VAL A 1 495 ? 142.283 141.891 87.404  1.00 22.31 ?  495 VAL A N     1 
ATOM   3961  C  CA    . VAL A 1 495 ? 141.444 142.382 88.491  1.00 13.04 ?  495 VAL A CA    1 
ATOM   3962  C  C     . VAL A 1 495 ? 142.236 143.319 89.392  1.00 19.56 ?  495 VAL A C     1 
ATOM   3963  O  O     . VAL A 1 495 ? 141.747 144.381 89.788  1.00 26.90 ?  495 VAL A O     1 
ATOM   3964  C  CB    . VAL A 1 495 ? 140.849 141.202 89.281  1.00 15.82 ?  495 VAL A CB    1 
ATOM   3965  C  CG1   . VAL A 1 495 ? 140.248 141.682 90.592  1.00 11.99 ?  495 VAL A CG1   1 
ATOM   3966  C  CG2   . VAL A 1 495 ? 139.808 140.481 88.449  1.00 18.51 ?  495 VAL A CG2   1 
ATOM   3967  N  N     . ASN A 1 496 ? 143.473 142.942 89.730  1.00 23.48 ?  496 ASN A N     1 
ATOM   3968  C  CA    . ASN A 1 496 ? 144.321 143.812 90.536  1.00 15.17 ?  496 ASN A CA    1 
ATOM   3969  C  C     . ASN A 1 496 ? 144.607 145.123 89.819  1.00 17.85 ?  496 ASN A C     1 
ATOM   3970  O  O     . ASN A 1 496 ? 144.561 146.196 90.430  1.00 23.80 ?  496 ASN A O     1 
ATOM   3971  C  CB    . ASN A 1 496 ? 145.626 143.094 90.880  1.00 19.22 ?  496 ASN A CB    1 
ATOM   3972  C  CG    . ASN A 1 496 ? 146.347 143.724 92.051  1.00 18.58 ?  496 ASN A CG    1 
ATOM   3973  O  OD1   . ASN A 1 496 ? 145.720 144.212 92.988  1.00 25.12 ?  496 ASN A OD1   1 
ATOM   3974  N  ND2   . ASN A 1 496 ? 147.671 143.715 92.004  1.00 18.92 ?  496 ASN A ND2   1 
ATOM   3975  N  N     . PHE A 1 497 ? 144.899 145.056 88.518  1.00 21.05 ?  497 PHE A N     1 
ATOM   3976  C  CA    . PHE A 1 497 ? 145.176 146.259 87.744  1.00 15.64 ?  497 PHE A CA    1 
ATOM   3977  C  C     . PHE A 1 497 ? 143.998 147.219 87.788  1.00 24.19 ?  497 PHE A C     1 
ATOM   3978  O  O     . PHE A 1 497 ? 144.160 148.411 88.071  1.00 28.93 ?  497 PHE A O     1 
ATOM   3979  C  CB    . PHE A 1 497 ? 145.500 145.883 86.298  1.00 17.27 ?  497 PHE A CB    1 
ATOM   3980  C  CG    . PHE A 1 497 ? 145.804 147.060 85.415  1.00 19.90 ?  497 PHE A CG    1 
ATOM   3981  C  CD1   . PHE A 1 497 ? 147.094 147.547 85.310  1.00 23.61 ?  497 PHE A CD1   1 
ATOM   3982  C  CD2   . PHE A 1 497 ? 144.800 147.676 84.688  1.00 21.10 ?  497 PHE A CD2   1 
ATOM   3983  C  CE1   . PHE A 1 497 ? 147.375 148.627 84.499  1.00 24.21 ?  497 PHE A CE1   1 
ATOM   3984  C  CE2   . PHE A 1 497 ? 145.077 148.756 83.878  1.00 22.95 ?  497 PHE A CE2   1 
ATOM   3985  C  CZ    . PHE A 1 497 ? 146.365 149.232 83.783  1.00 24.69 ?  497 PHE A CZ    1 
ATOM   3986  N  N     . TYR A 1 498 ? 142.796 146.709 87.531  1.00 26.98 ?  498 TYR A N     1 
ATOM   3987  C  CA    . TYR A 1 498 ? 141.641 147.592 87.468  1.00 18.45 ?  498 TYR A CA    1 
ATOM   3988  C  C     . TYR A 1 498 ? 141.181 148.041 88.849  1.00 22.85 ?  498 TYR A C     1 
ATOM   3989  O  O     . TYR A 1 498 ? 140.660 149.149 88.983  1.00 25.76 ?  498 TYR A O     1 
ATOM   3990  C  CB    . TYR A 1 498 ? 140.514 146.917 86.690  1.00 19.95 ?  498 TYR A CB    1 
ATOM   3991  C  CG    . TYR A 1 498 ? 140.825 146.842 85.215  1.00 24.72 ?  498 TYR A CG    1 
ATOM   3992  C  CD1   . TYR A 1 498 ? 141.049 147.996 84.481  1.00 24.50 ?  498 TYR A CD1   1 
ATOM   3993  C  CD2   . TYR A 1 498 ? 140.920 145.622 84.564  1.00 26.25 ?  498 TYR A CD2   1 
ATOM   3994  C  CE1   . TYR A 1 498 ? 141.346 147.940 83.137  1.00 25.80 ?  498 TYR A CE1   1 
ATOM   3995  C  CE2   . TYR A 1 498 ? 141.215 145.555 83.220  1.00 24.86 ?  498 TYR A CE2   1 
ATOM   3996  C  CZ    . TYR A 1 498 ? 141.427 146.717 82.511  1.00 30.37 ?  498 TYR A CZ    1 
ATOM   3997  O  OH    . TYR A 1 498 ? 141.722 146.661 81.169  1.00 32.57 ?  498 TYR A OH    1 
ATOM   3998  N  N     . SER A 1 499 ? 141.401 147.234 89.889  1.00 23.88 ?  499 SER A N     1 
ATOM   3999  C  CA    . SER A 1 499 ? 141.096 147.689 91.240  1.00 15.88 ?  499 SER A CA    1 
ATOM   4000  C  C     . SER A 1 499 ? 142.048 148.795 91.675  1.00 19.19 ?  499 SER A C     1 
ATOM   4001  O  O     . SER A 1 499 ? 141.625 149.776 92.296  1.00 30.15 ?  499 SER A O     1 
ATOM   4002  C  CB    . SER A 1 499 ? 141.144 146.518 92.220  1.00 15.23 ?  499 SER A CB    1 
ATOM   4003  O  OG    . SER A 1 499 ? 142.472 146.084 92.444  1.00 23.12 ?  499 SER A OG    1 
ATOM   4004  N  N     . ILE A 1 500 ? 143.337 148.664 91.348  1.00 17.80 ?  500 ILE A N     1 
ATOM   4005  C  CA    . ILE A 1 500 ? 144.292 149.726 91.650  1.00 19.65 ?  500 ILE A CA    1 
ATOM   4006  C  C     . ILE A 1 500 ? 143.952 150.982 90.860  1.00 18.17 ?  500 ILE A C     1 
ATOM   4007  O  O     . ILE A 1 500 ? 144.021 152.100 91.382  1.00 28.08 ?  500 ILE A O     1 
ATOM   4008  C  CB    . ILE A 1 500 ? 145.730 149.250 91.370  1.00 22.99 ?  500 ILE A CB    1 
ATOM   4009  C  CG1   . ILE A 1 500 ? 146.142 148.173 92.368  1.00 19.08 ?  500 ILE A CG1   1 
ATOM   4010  C  CG2   . ILE A 1 500 ? 146.702 150.407 91.444  1.00 20.01 ?  500 ILE A CG2   1 
ATOM   4011  C  CD1   . ILE A 1 500 ? 147.336 147.381 91.928  1.00 19.14 ?  500 ILE A CD1   1 
ATOM   4012  N  N     . GLN A 1 501 ? 143.573 150.817 89.590  1.00 24.23 ?  501 GLN A N     1 
ATOM   4013  C  CA    . GLN A 1 501 ? 143.187 151.963 88.775  1.00 22.16 ?  501 GLN A CA    1 
ATOM   4014  C  C     . GLN A 1 501 ? 141.964 152.666 89.346  1.00 28.31 ?  501 GLN A C     1 
ATOM   4015  O  O     . GLN A 1 501 ? 141.926 153.898 89.417  1.00 35.38 ?  501 GLN A O     1 
ATOM   4016  C  CB    . GLN A 1 501 ? 142.925 151.515 87.339  1.00 24.46 ?  501 GLN A CB    1 
ATOM   4017  C  CG    . GLN A 1 501 ? 143.357 152.518 86.292  1.00 25.08 ?  501 GLN A CG    1 
ATOM   4018  C  CD    . GLN A 1 501 ? 143.073 152.045 84.885  1.00 29.25 ?  501 GLN A CD    1 
ATOM   4019  O  OE1   . GLN A 1 501 ? 141.923 151.803 84.519  1.00 28.56 ?  501 GLN A OE1   1 
ATOM   4020  N  NE2   . GLN A 1 501 ? 144.122 151.906 84.086  1.00 33.56 ?  501 GLN A NE2   1 
ATOM   4021  N  N     . ARG A 1 502 ? 140.953 151.900 89.763  1.00 29.65 ?  502 ARG A N     1 
ATOM   4022  C  CA    . ARG A 1 502 ? 139.761 152.507 90.342  1.00 20.32 ?  502 ARG A CA    1 
ATOM   4023  C  C     . ARG A 1 502 ? 140.072 153.186 91.669  1.00 18.03 ?  502 ARG A C     1 
ATOM   4024  O  O     . ARG A 1 502 ? 139.538 154.259 91.958  1.00 30.49 ?  502 ARG A O     1 
ATOM   4025  C  CB    . ARG A 1 502 ? 138.667 151.455 90.519  1.00 24.31 ?  502 ARG A CB    1 
ATOM   4026  C  CG    . ARG A 1 502 ? 137.295 152.043 90.785  1.00 26.79 ?  502 ARG A CG    1 
ATOM   4027  C  CD    . ARG A 1 502 ? 136.947 153.121 89.777  1.00 27.43 ?  502 ARG A CD    1 
ATOM   4028  N  NE    . ARG A 1 502 ? 135.819 153.929 90.222  1.00 25.88 ?  502 ARG A NE    1 
ATOM   4029  C  CZ    . ARG A 1 502 ? 135.710 155.235 90.027  1.00 28.77 ?  502 ARG A CZ    1 
ATOM   4030  N  NH1   . ARG A 1 502 ? 136.645 155.918 89.387  1.00 32.34 1  502 ARG A NH1   1 
ATOM   4031  N  NH2   . ARG A 1 502 ? 134.639 155.873 90.487  1.00 30.22 ?  502 ARG A NH2   1 
ATOM   4032  N  N     . SER A 1 503 ? 140.929 152.577 92.492  1.00 18.39 ?  503 SER A N     1 
ATOM   4033  C  CA    . SER A 1 503 ? 141.309 153.203 93.753  1.00 23.96 ?  503 SER A CA    1 
ATOM   4034  C  C     . SER A 1 503 ? 142.042 154.517 93.514  1.00 24.98 ?  503 SER A C     1 
ATOM   4035  O  O     . SER A 1 503 ? 141.783 155.516 94.195  1.00 27.44 ?  503 SER A O     1 
ATOM   4036  C  CB    . SER A 1 503 ? 142.173 152.241 94.570  1.00 18.45 ?  503 SER A CB    1 
ATOM   4037  O  OG    . SER A 1 503 ? 142.123 152.554 95.948  1.00 22.93 ?  503 SER A OG    1 
ATOM   4038  N  N     . ALA A 1 504 ? 142.949 154.538 92.536  1.00 27.15 ?  504 ALA A N     1 
ATOM   4039  C  CA    . ALA A 1 504 ? 143.664 155.767 92.208  1.00 25.35 ?  504 ALA A CA    1 
ATOM   4040  C  C     . ALA A 1 504 ? 142.722 156.826 91.649  1.00 30.07 ?  504 ALA A C     1 
ATOM   4041  O  O     . ALA A 1 504 ? 142.858 158.012 91.964  1.00 37.59 ?  504 ALA A O     1 
ATOM   4042  C  CB    . ALA A 1 504 ? 144.789 155.467 91.221  1.00 27.51 ?  504 ALA A CB    1 
ATOM   4043  N  N     . GLU A 1 505 ? 141.760 156.419 90.819  1.00 28.85 ?  505 GLU A N     1 
ATOM   4044  C  CA    . GLU A 1 505 ? 140.791 157.368 90.282  1.00 28.97 ?  505 GLU A CA    1 
ATOM   4045  C  C     . GLU A 1 505 ? 139.902 157.937 91.381  1.00 30.69 ?  505 GLU A C     1 
ATOM   4046  O  O     . GLU A 1 505 ? 139.577 159.128 91.368  1.00 35.21 ?  505 GLU A O     1 
ATOM   4047  C  CB    . GLU A 1 505 ? 139.947 156.699 89.200  1.00 29.45 ?  505 GLU A CB    1 
ATOM   4048  C  CG    . GLU A 1 505 ? 140.696 156.438 87.906  1.00 32.55 ?  505 GLU A CG    1 
ATOM   4049  C  CD    . GLU A 1 505 ? 140.097 155.300 87.105  1.00 35.89 ?  505 GLU A CD    1 
ATOM   4050  O  OE1   . GLU A 1 505 ? 139.059 154.753 87.528  1.00 36.53 ?  505 GLU A OE1   1 
ATOM   4051  O  OE2   . GLU A 1 505 ? 140.667 154.953 86.049  1.00 39.44 -1 505 GLU A OE2   1 
ATOM   4052  N  N     . ILE A 1 506 ? 139.493 157.099 92.336  1.00 28.29 ?  506 ILE A N     1 
ATOM   4053  C  CA    . ILE A 1 506 ? 138.696 157.581 93.459  1.00 25.45 ?  506 ILE A CA    1 
ATOM   4054  C  C     . ILE A 1 506 ? 139.506 158.549 94.311  1.00 28.32 ?  506 ILE A C     1 
ATOM   4055  O  O     . ILE A 1 506 ? 138.994 159.579 94.759  1.00 37.79 ?  506 ILE A O     1 
ATOM   4056  C  CB    . ILE A 1 506 ? 138.171 156.394 94.287  1.00 25.65 ?  506 ILE A CB    1 
ATOM   4057  C  CG1   . ILE A 1 506 ? 137.129 155.608 93.492  1.00 28.37 ?  506 ILE A CG1   1 
ATOM   4058  C  CG2   . ILE A 1 506 ? 137.570 156.873 95.594  1.00 27.04 ?  506 ILE A CG2   1 
ATOM   4059  C  CD1   . ILE A 1 506 ? 136.816 154.253 94.079  1.00 22.37 ?  506 ILE A CD1   1 
ATOM   4060  N  N     . ALA A 1 507 ? 140.783 158.236 94.545  1.00 30.87 ?  507 ALA A N     1 
ATOM   4061  C  CA    . ALA A 1 507 ? 141.639 159.151 95.294  1.00 28.95 ?  507 ALA A CA    1 
ATOM   4062  C  C     . ALA A 1 507 ? 141.800 160.479 94.564  1.00 30.76 ?  507 ALA A C     1 
ATOM   4063  O  O     . ALA A 1 507 ? 141.798 161.545 95.190  1.00 33.56 ?  507 ALA A O     1 
ATOM   4064  C  CB    . ALA A 1 507 ? 143.002 158.506 95.545  1.00 25.37 ?  507 ALA A CB    1 
ATOM   4065  N  N     . LYS A 1 508 ? 141.949 160.435 93.239  1.00 36.54 ?  508 LYS A N     1 
ATOM   4066  C  CA    . LYS A 1 508 ? 142.062 161.663 92.457  1.00 33.53 ?  508 LYS A CA    1 
ATOM   4067  C  C     . LYS A 1 508 ? 140.776 162.481 92.512  1.00 38.04 ?  508 LYS A C     1 
ATOM   4068  O  O     . LYS A 1 508 ? 140.822 163.709 92.650  1.00 44.21 ?  508 LYS A O     1 
ATOM   4069  C  CB    . LYS A 1 508 ? 142.416 161.327 91.010  1.00 36.70 ?  508 LYS A CB    1 
ATOM   4070  C  CG    . LYS A 1 508 ? 142.346 162.511 90.063  1.00 40.47 ?  508 LYS A CG    1 
ATOM   4071  C  CD    . LYS A 1 508 ? 142.347 162.059 88.614  1.00 38.88 ?  508 LYS A CD    1 
ATOM   4072  C  CE    . LYS A 1 508 ? 142.537 163.234 87.672  1.00 39.18 ?  508 LYS A CE    1 
ATOM   4073  N  NZ    . LYS A 1 508 ? 143.359 162.867 86.488  1.00 42.23 1  508 LYS A NZ    1 
ATOM   4074  N  N     . GLU A 1 509 ? 139.624 161.820 92.403  1.00 36.02 ?  509 GLU A N     1 
ATOM   4075  C  CA    . GLU A 1 509 ? 138.351 162.534 92.397  1.00 36.32 ?  509 GLU A CA    1 
ATOM   4076  C  C     . GLU A 1 509 ? 138.056 163.145 93.760  1.00 39.00 ?  509 GLU A C     1 
ATOM   4077  O  O     . GLU A 1 509 ? 137.701 164.325 93.861  1.00 43.38 ?  509 GLU A O     1 
ATOM   4078  C  CB    . GLU A 1 509 ? 137.225 161.590 91.974  1.00 36.42 ?  509 GLU A CB    1 
ATOM   4079  C  CG    . GLU A 1 509 ? 137.213 161.261 90.491  1.00 42.34 ?  509 GLU A CG    1 
ATOM   4080  C  CD    . GLU A 1 509 ? 136.479 159.969 90.187  1.00 44.67 ?  509 GLU A CD    1 
ATOM   4081  O  OE1   . GLU A 1 509 ? 135.862 159.403 91.113  1.00 42.56 ?  509 GLU A OE1   1 
ATOM   4082  O  OE2   . GLU A 1 509 ? 136.517 159.522 89.022  1.00 42.61 -1 509 GLU A OE2   1 
ATOM   4083  N  N     . LYS A 1 510 ? 138.197 162.356 94.824  1.00 35.73 ?  510 LYS A N     1 
ATOM   4084  C  CA    . LYS A 1 510 ? 137.934 162.836 96.173  1.00 31.94 ?  510 LYS A CA    1 
ATOM   4085  C  C     . LYS A 1 510 ? 139.095 163.629 96.755  1.00 34.00 ?  510 LYS A C     1 
ATOM   4086  O  O     . LYS A 1 510 ? 138.938 164.225 97.826  1.00 39.30 ?  510 LYS A O     1 
ATOM   4087  C  CB    . LYS A 1 510 ? 137.602 161.658 97.088  1.00 30.48 ?  510 LYS A CB    1 
ATOM   4088  C  CG    . LYS A 1 510 ? 136.520 160.750 96.535  1.00 33.39 ?  510 LYS A CG    1 
ATOM   4089  C  CD    . LYS A 1 510 ? 135.950 159.834 97.599  1.00 33.07 ?  510 LYS A CD    1 
ATOM   4090  C  CE    . LYS A 1 510 ? 134.850 158.962 97.020  1.00 35.82 ?  510 LYS A CE    1 
ATOM   4091  N  NZ    . LYS A 1 510 ? 133.823 158.606 98.031  1.00 34.70 1  510 LYS A NZ    1 
ATOM   4092  N  N     . GLY A 1 511 ? 140.245 163.649 96.086  1.00 37.13 ?  511 GLY A N     1 
ATOM   4093  C  CA    . GLY A 1 511 ? 141.381 164.408 96.561  1.00 37.04 ?  511 GLY A CA    1 
ATOM   4094  C  C     . GLY A 1 511 ? 142.010 163.898 97.834  1.00 40.69 ?  511 GLY A C     1 
ATOM   4095  O  O     . GLY A 1 511 ? 142.848 164.593 98.415  1.00 42.75 ?  511 GLY A O     1 
ATOM   4096  N  N     . GLU A 1 512 ? 141.636 162.705 98.291  1.00 34.12 ?  512 GLU A N     1 
ATOM   4097  C  CA    . GLU A 1 512 ? 142.168 162.144 99.521  1.00 29.43 ?  512 GLU A CA    1 
ATOM   4098  C  C     . GLU A 1 512 ? 142.554 160.688 99.307  1.00 29.65 ?  512 GLU A C     1 
ATOM   4099  O  O     . GLU A 1 512 ? 141.922 159.965 98.533  1.00 33.10 ?  512 GLU A O     1 
ATOM   4100  C  CB    . GLU A 1 512 ? 141.158 162.253 100.672 1.00 31.02 ?  512 GLU A CB    1 
ATOM   4101  C  CG    . GLU A 1 512 ? 139.838 161.550 100.417 1.00 31.59 ?  512 GLU A CG    1 
ATOM   4102  C  CD    . GLU A 1 512 ? 139.176 161.083 101.696 1.00 35.46 ?  512 GLU A CD    1 
ATOM   4103  O  OE1   . GLU A 1 512 ? 139.905 160.787 102.664 1.00 35.24 ?  512 GLU A OE1   1 
ATOM   4104  O  OE2   . GLU A 1 512 ? 137.930 161.011 101.733 1.00 34.76 -1 512 GLU A OE2   1 
ATOM   4105  N  N     . THR A 1 513 ? 143.606 160.273 99.998  1.00 29.89 ?  513 THR A N     1 
ATOM   4106  C  CA    . THR A 1 513 ? 144.073 158.896 100.022 1.00 25.22 ?  513 THR A CA    1 
ATOM   4107  C  C     . THR A 1 513 ? 143.776 158.293 101.391 1.00 27.22 ?  513 THR A C     1 
ATOM   4108  O  O     . THR A 1 513 ? 143.281 158.967 102.298 1.00 36.88 ?  513 THR A O     1 
ATOM   4109  C  CB    . THR A 1 513 ? 145.568 158.830 99.702  1.00 24.19 ?  513 THR A CB    1 
ATOM   4110  O  OG1   . THR A 1 513 ? 146.297 159.599 100.664 1.00 28.55 ?  513 THR A OG1   1 
ATOM   4111  C  CG2   . THR A 1 513 ? 145.840 159.382 98.316  1.00 23.90 ?  513 THR A CG2   1 
ATOM   4112  N  N     . PHE A 1 514 ? 144.079 157.007 101.541 1.00 23.27 ?  514 PHE A N     1 
ATOM   4113  C  CA    . PHE A 1 514 ? 143.915 156.393 102.847 1.00 25.13 ?  514 PHE A CA    1 
ATOM   4114  C  C     . PHE A 1 514 ? 145.021 156.862 103.788 1.00 25.64 ?  514 PHE A C     1 
ATOM   4115  O  O     . PHE A 1 514 ? 146.099 157.283 103.361 1.00 28.15 ?  514 PHE A O     1 
ATOM   4116  C  CB    . PHE A 1 514 ? 143.888 154.865 102.739 1.00 18.28 ?  514 PHE A CB    1 
ATOM   4117  C  CG    . PHE A 1 514 ? 145.194 154.246 102.327 1.00 19.11 ?  514 PHE A CG    1 
ATOM   4118  C  CD1   . PHE A 1 514 ? 145.495 154.060 100.991 1.00 17.86 ?  514 PHE A CD1   1 
ATOM   4119  C  CD2   . PHE A 1 514 ? 146.105 153.817 103.277 1.00 22.51 ?  514 PHE A CD2   1 
ATOM   4120  C  CE1   . PHE A 1 514 ? 146.685 153.477 100.611 1.00 18.86 ?  514 PHE A CE1   1 
ATOM   4121  C  CE2   . PHE A 1 514 ? 147.295 153.234 102.902 1.00 17.63 ?  514 PHE A CE2   1 
ATOM   4122  C  CZ    . PHE A 1 514 ? 147.585 153.066 101.568 1.00 18.53 ?  514 PHE A CZ    1 
ATOM   4123  N  N     . ASP A 1 515 ? 144.729 156.806 105.084 1.00 29.13 ?  515 ASP A N     1 
ATOM   4124  C  CA    . ASP A 1 515 ? 145.650 157.336 106.081 1.00 27.15 ?  515 ASP A CA    1 
ATOM   4125  C  C     . ASP A 1 515 ? 146.988 156.613 106.023 1.00 29.36 ?  515 ASP A C     1 
ATOM   4126  O  O     . ASP A 1 515 ? 147.048 155.384 105.917 1.00 35.37 ?  515 ASP A O     1 
ATOM   4127  C  CB    . ASP A 1 515 ? 145.045 157.215 107.478 1.00 30.15 ?  515 ASP A CB    1 
ATOM   4128  C  CG    . ASP A 1 515 ? 144.098 158.352 107.802 1.00 38.05 ?  515 ASP A CG    1 
ATOM   4129  O  OD1   . ASP A 1 515 ? 143.573 158.979 106.858 1.00 36.62 ?  515 ASP A OD1   1 
ATOM   4130  O  OD2   . ASP A 1 515 ? 143.878 158.617 109.002 1.00 38.93 -1 515 ASP A OD2   1 
ATOM   4131  N  N     . GLN A 1 516 ? 148.067 157.393 106.099 1.00 27.50 ?  516 GLN A N     1 
ATOM   4132  C  CA    . GLN A 1 516 ? 149.434 156.881 106.002 1.00 28.05 ?  516 GLN A CA    1 
ATOM   4133  C  C     . GLN A 1 516 ? 149.668 156.165 104.674 1.00 25.00 ?  516 GLN A C     1 
ATOM   4134  O  O     . GLN A 1 516 ? 150.335 155.132 104.614 1.00 33.02 ?  516 GLN A O     1 
ATOM   4135  C  CB    . GLN A 1 516 ? 149.773 155.963 107.180 1.00 25.48 ?  516 GLN A CB    1 
ATOM   4136  C  CG    . GLN A 1 516 ? 149.601 156.606 108.543 1.00 27.14 ?  516 GLN A CG    1 
ATOM   4137  C  CD    . GLN A 1 516 ? 149.927 155.655 109.674 1.00 29.50 ?  516 GLN A CD    1 
ATOM   4138  O  OE1   . GLN A 1 516 ? 151.091 155.336 109.914 1.00 29.48 ?  516 GLN A OE1   1 
ATOM   4139  N  NE2   . GLN A 1 516 ? 148.900 155.198 110.377 1.00 28.58 ?  516 GLN A NE2   1 
ATOM   4140  N  N     . TYR A 1 517 ? 149.105 156.714 103.597 1.00 23.76 ?  517 TYR A N     1 
ATOM   4141  C  CA    . TYR A 1 517 ? 149.366 156.152 102.277 1.00 23.56 ?  517 TYR A CA    1 
ATOM   4142  C  C     . TYR A 1 517 ? 150.803 156.394 101.837 1.00 27.07 ?  517 TYR A C     1 
ATOM   4143  O  O     . TYR A 1 517 ? 151.394 155.540 101.167 1.00 34.91 ?  517 TYR A O     1 
ATOM   4144  C  CB    . TYR A 1 517 ? 148.404 156.733 101.239 1.00 24.34 ?  517 TYR A CB    1 
ATOM   4145  C  CG    . TYR A 1 517 ? 148.973 156.719 99.837  1.00 26.69 ?  517 TYR A CG    1 
ATOM   4146  C  CD1   . TYR A 1 517 ? 148.972 155.555 99.079  1.00 21.22 ?  517 TYR A CD1   1 
ATOM   4147  C  CD2   . TYR A 1 517 ? 149.529 157.863 99.279  1.00 25.97 ?  517 TYR A CD2   1 
ATOM   4148  C  CE1   . TYR A 1 517 ? 149.499 155.532 97.808  1.00 27.38 ?  517 TYR A CE1   1 
ATOM   4149  C  CE2   . TYR A 1 517 ? 150.061 157.847 98.010  1.00 25.76 ?  517 TYR A CE2   1 
ATOM   4150  C  CZ    . TYR A 1 517 ? 150.044 156.680 97.279  1.00 26.31 ?  517 TYR A CZ    1 
ATOM   4151  O  OH    . TYR A 1 517 ? 150.570 156.664 96.009  1.00 34.34 ?  517 TYR A OH    1 
ATOM   4152  N  N     . GLU A 1 518 ? 151.378 157.542 102.199 1.00 30.87 ?  518 GLU A N     1 
ATOM   4153  C  CA    . GLU A 1 518 ? 152.693 157.918 101.689 1.00 33.64 ?  518 GLU A CA    1 
ATOM   4154  C  C     . GLU A 1 518 ? 153.787 156.950 102.119 1.00 35.51 ?  518 GLU A C     1 
ATOM   4155  O  O     . GLU A 1 518 ? 154.815 156.855 101.439 1.00 38.35 ?  518 GLU A O     1 
ATOM   4156  C  CB    . GLU A 1 518 ? 153.043 159.337 102.139 1.00 34.11 ?  518 GLU A CB    1 
ATOM   4157  C  CG    . GLU A 1 518 ? 152.218 160.425 101.469 1.00 36.55 ?  518 GLU A CG    1 
ATOM   4158  C  CD    . GLU A 1 518 ? 152.456 160.515 99.971  1.00 43.50 ?  518 GLU A CD    1 
ATOM   4159  O  OE1   . GLU A 1 518 ? 153.532 160.084 99.505  1.00 39.21 ?  518 GLU A OE1   1 
ATOM   4160  O  OE2   . GLU A 1 518 ? 151.565 161.022 99.259  1.00 40.04 -1 518 GLU A OE2   1 
ATOM   4161  N  N     . GLY A 1 519 ? 153.598 156.236 103.227 1.00 24.41 ?  519 GLY A N     1 
ATOM   4162  C  CA    . GLY A 1 519 ? 154.540 155.216 103.634 1.00 20.56 ?  519 GLY A CA    1 
ATOM   4163  C  C     . GLY A 1 519 ? 154.323 153.853 103.026 1.00 21.97 ?  519 GLY A C     1 
ATOM   4164  O  O     . GLY A 1 519 ? 155.150 152.959 103.224 1.00 31.43 ?  519 GLY A O     1 
ATOM   4165  N  N     . SER A 1 520 ? 153.233 153.668 102.287 1.00 22.12 ?  520 SER A N     1 
ATOM   4166  C  CA    . SER A 1 520 ? 152.899 152.379 101.703 1.00 24.05 ?  520 SER A CA    1 
ATOM   4167  C  C     . SER A 1 520 ? 153.786 152.084 100.496 1.00 22.41 ?  520 SER A C     1 
ATOM   4168  O  O     . SER A 1 520 ? 154.473 152.958 99.963  1.00 27.98 ?  520 SER A O     1 
ATOM   4169  C  CB    . SER A 1 520 ? 151.427 152.343 101.301 1.00 20.05 ?  520 SER A CB    1 
ATOM   4170  O  OG    . SER A 1 520 ? 151.141 153.348 100.345 1.00 20.38 ?  520 SER A OG    1 
ATOM   4171  N  N     . THR A 1 521 ? 153.761 150.823 100.061 1.00 20.89 ?  521 THR A N     1 
ATOM   4172  C  CA    . THR A 1 521 ? 154.537 150.429 98.893  1.00 19.04 ?  521 THR A CA    1 
ATOM   4173  C  C     . THR A 1 521 ? 153.930 150.949 97.598  1.00 25.45 ?  521 THR A C     1 
ATOM   4174  O  O     . THR A 1 521 ? 154.634 151.019 96.585  1.00 28.88 ?  521 THR A O     1 
ATOM   4175  C  CB    . THR A 1 521 ? 154.663 148.908 98.825  1.00 28.33 ?  521 THR A CB    1 
ATOM   4176  O  OG1   . THR A 1 521 ? 153.359 148.320 98.866  1.00 29.39 ?  521 THR A OG1   1 
ATOM   4177  C  CG2   . THR A 1 521 ? 155.476 148.393 99.999  1.00 20.51 ?  521 THR A CG2   1 
ATOM   4178  N  N     . TYR A 1 522 ? 152.643 151.301 97.603  1.00 28.74 ?  522 TYR A N     1 
ATOM   4179  C  CA    . TYR A 1 522 ? 152.064 151.975 96.447  1.00 21.52 ?  522 TYR A CA    1 
ATOM   4180  C  C     . TYR A 1 522 ? 152.713 153.335 96.230  1.00 25.88 ?  522 TYR A C     1 
ATOM   4181  O  O     . TYR A 1 522 ? 153.023 153.711 95.093  1.00 29.89 ?  522 TYR A O     1 
ATOM   4182  C  CB    . TYR A 1 522 ? 150.554 152.136 96.621  1.00 18.60 ?  522 TYR A CB    1 
ATOM   4183  C  CG    . TYR A 1 522 ? 149.804 150.860 96.926  1.00 21.92 ?  522 TYR A CG    1 
ATOM   4184  C  CD1   . TYR A 1 522 ? 149.598 149.901 95.945  1.00 21.23 ?  522 TYR A CD1   1 
ATOM   4185  C  CD2   . TYR A 1 522 ? 149.275 150.631 98.188  1.00 23.68 ?  522 TYR A CD2   1 
ATOM   4186  C  CE1   . TYR A 1 522 ? 148.903 148.741 96.217  1.00 20.05 ?  522 TYR A CE1   1 
ATOM   4187  C  CE2   . TYR A 1 522 ? 148.576 149.476 98.468  1.00 22.90 ?  522 TYR A CE2   1 
ATOM   4188  C  CZ    . TYR A 1 522 ? 148.395 148.534 97.479  1.00 23.08 ?  522 TYR A CZ    1 
ATOM   4189  O  OH    . TYR A 1 522 ? 147.701 147.381 97.756  1.00 27.20 ?  522 TYR A OH    1 
ATOM   4190  N  N     . ALA A 1 523 ? 152.920 154.090 97.311  1.00 28.81 ?  523 ALA A N     1 
ATOM   4191  C  CA    . ALA A 1 523 ? 153.526 155.410 97.194  1.00 26.99 ?  523 ALA A CA    1 
ATOM   4192  C  C     . ALA A 1 523 ? 154.990 155.317 96.785  1.00 28.38 ?  523 ALA A C     1 
ATOM   4193  O  O     . ALA A 1 523 ? 155.460 156.101 95.954  1.00 32.27 ?  523 ALA A O     1 
ATOM   4194  C  CB    . ALA A 1 523 ? 153.382 156.170 98.510  1.00 23.69 ?  523 ALA A CB    1 
ATOM   4195  N  N     . THR A 1 524 ? 155.726 154.364 97.361  1.00 29.12 ?  524 THR A N     1 
ATOM   4196  C  CA    . THR A 1 524 ? 157.130 154.196 97.009  1.00 28.63 ?  524 THR A CA    1 
ATOM   4197  C  C     . THR A 1 524 ? 157.312 153.539 95.649  1.00 31.29 ?  524 THR A C     1 
ATOM   4198  O  O     . THR A 1 524 ? 158.405 153.619 95.079  1.00 36.00 ?  524 THR A O     1 
ATOM   4199  C  CB    . THR A 1 524 ? 157.845 153.370 98.079  1.00 30.58 ?  524 THR A CB    1 
ATOM   4200  O  OG1   . THR A 1 524 ? 157.422 152.005 97.996  1.00 32.71 ?  524 THR A OG1   1 
ATOM   4201  C  CG2   . THR A 1 524 ? 157.532 153.909 99.465  1.00 27.59 ?  524 THR A CG2   1 
ATOM   4202  N  N     . GLY A 1 525 ? 156.273 152.898 95.117  1.00 25.73 ?  525 GLY A N     1 
ATOM   4203  C  CA    . GLY A 1 525 ? 156.358 152.223 93.840  1.00 27.99 ?  525 GLY A CA    1 
ATOM   4204  C  C     . GLY A 1 525 ? 156.926 150.823 93.889  1.00 32.06 ?  525 GLY A C     1 
ATOM   4205  O  O     . GLY A 1 525 ? 157.009 150.172 92.841  1.00 31.32 ?  525 GLY A O     1 
ATOM   4206  N  N     . GLU A 1 526 ? 157.322 150.339 95.067  1.00 32.87 ?  526 GLU A N     1 
ATOM   4207  C  CA    . GLU A 1 526 ? 157.854 148.988 95.188  1.00 33.19 ?  526 GLU A CA    1 
ATOM   4208  C  C     . GLU A 1 526 ? 156.786 147.929 94.948  1.00 36.82 ?  526 GLU A C     1 
ATOM   4209  O  O     . GLU A 1 526 ? 157.113 146.821 94.507  1.00 40.66 ?  526 GLU A O     1 
ATOM   4210  C  CB    . GLU A 1 526 ? 158.501 148.817 96.567  1.00 33.10 ?  526 GLU A CB    1 
ATOM   4211  C  CG    . GLU A 1 526 ? 158.596 147.391 97.078  1.00 33.56 ?  526 GLU A CG    1 
ATOM   4212  C  CD    . GLU A 1 526 ? 158.659 147.320 98.590  1.00 40.85 ?  526 GLU A CD    1 
ATOM   4213  O  OE1   . GLU A 1 526 ? 158.640 148.386 99.237  1.00 44.68 ?  526 GLU A OE1   1 
ATOM   4214  O  OE2   . GLU A 1 526 ? 158.728 146.196 99.130  1.00 39.17 -1 526 GLU A OE2   1 
ATOM   4215  N  N     . TYR A 1 527 ? 155.516 148.258 95.200  1.00 34.23 ?  527 TYR A N     1 
ATOM   4216  C  CA    . TYR A 1 527 ? 154.434 147.306 94.972  1.00 25.64 ?  527 TYR A CA    1 
ATOM   4217  C  C     . TYR A 1 527 ? 154.359 146.869 93.515  1.00 26.99 ?  527 TYR A C     1 
ATOM   4218  O  O     . TYR A 1 527 ? 154.006 145.720 93.230  1.00 29.87 ?  527 TYR A O     1 
ATOM   4219  C  CB    . TYR A 1 527 ? 153.102 147.920 95.410  1.00 22.95 ?  527 TYR A CB    1 
ATOM   4220  C  CG    . TYR A 1 527 ? 151.902 147.028 95.186  1.00 27.51 ?  527 TYR A CG    1 
ATOM   4221  C  CD1   . TYR A 1 527 ? 151.489 146.132 96.163  1.00 24.78 ?  527 TYR A CD1   1 
ATOM   4222  C  CD2   . TYR A 1 527 ? 151.178 147.086 94.003  1.00 28.27 ?  527 TYR A CD2   1 
ATOM   4223  C  CE1   . TYR A 1 527 ? 150.394 145.316 95.962  1.00 26.06 ?  527 TYR A CE1   1 
ATOM   4224  C  CE2   . TYR A 1 527 ? 150.086 146.274 93.796  1.00 24.90 ?  527 TYR A CE2   1 
ATOM   4225  C  CZ    . TYR A 1 527 ? 149.697 145.392 94.778  1.00 18.91 ?  527 TYR A CZ    1 
ATOM   4226  O  OH    . TYR A 1 527 ? 148.606 144.583 94.575  1.00 30.61 ?  527 TYR A OH    1 
ATOM   4227  N  N     . PHE A 1 528 ? 154.685 147.763 92.585  1.00 29.56 ?  528 PHE A N     1 
ATOM   4228  C  CA    . PHE A 1 528 ? 154.509 147.520 91.162  1.00 28.24 ?  528 PHE A CA    1 
ATOM   4229  C  C     . PHE A 1 528 ? 155.727 146.883 90.503  1.00 34.05 ?  528 PHE A C     1 
ATOM   4230  O  O     . PHE A 1 528 ? 155.781 146.823 89.273  1.00 41.91 ?  528 PHE A O     1 
ATOM   4231  C  CB    . PHE A 1 528 ? 154.175 148.829 90.443  1.00 29.14 ?  528 PHE A CB    1 
ATOM   4232  C  CG    . PHE A 1 528 ? 152.954 149.522 90.972  1.00 31.18 ?  528 PHE A CG    1 
ATOM   4233  C  CD1   . PHE A 1 528 ? 153.053 150.439 92.004  1.00 29.96 ?  528 PHE A CD1   1 
ATOM   4234  C  CD2   . PHE A 1 528 ? 151.707 149.264 90.432  1.00 29.03 ?  528 PHE A CD2   1 
ATOM   4235  C  CE1   . PHE A 1 528 ? 151.932 151.081 92.488  1.00 32.17 ?  528 PHE A CE1   1 
ATOM   4236  C  CE2   . PHE A 1 528 ? 150.582 149.903 90.913  1.00 29.46 ?  528 PHE A CE2   1 
ATOM   4237  C  CZ    . PHE A 1 528 ? 150.695 150.812 91.942  1.00 28.16 ?  528 PHE A CZ    1 
ATOM   4238  N  N     . ASP A 1 529 ? 156.701 146.411 91.287  1.00 34.97 ?  529 ASP A N     1 
ATOM   4239  C  CA    . ASP A 1 529 ? 157.945 145.911 90.709  1.00 32.88 ?  529 ASP A CA    1 
ATOM   4240  C  C     . ASP A 1 529 ? 157.699 144.710 89.803  1.00 34.45 ?  529 ASP A C     1 
ATOM   4241  O  O     . ASP A 1 529 ? 158.116 144.698 88.638  1.00 41.56 ?  529 ASP A O     1 
ATOM   4242  C  CB    . ASP A 1 529 ? 158.925 145.544 91.824  1.00 35.83 ?  529 ASP A CB    1 
ATOM   4243  C  CG    . ASP A 1 529 ? 159.609 146.755 92.421  1.00 42.01 ?  529 ASP A CG    1 
ATOM   4244  O  OD1   . ASP A 1 529 ? 159.481 147.857 91.848  1.00 41.20 ?  529 ASP A OD1   1 
ATOM   4245  O  OD2   . ASP A 1 529 ? 160.277 146.606 93.465  1.00 42.29 -1 529 ASP A OD2   1 
ATOM   4246  N  N     . LYS A 1 530 ? 157.009 143.690 90.320  1.00 37.67 ?  530 LYS A N     1 
ATOM   4247  C  CA    . LYS A 1 530 ? 156.742 142.498 89.525  1.00 38.51 ?  530 LYS A CA    1 
ATOM   4248  C  C     . LYS A 1 530 ? 155.767 142.772 88.391  1.00 36.82 ?  530 LYS A C     1 
ATOM   4249  O  O     . LYS A 1 530 ? 155.707 141.989 87.438  1.00 40.77 ?  530 LYS A O     1 
ATOM   4250  C  CB    . LYS A 1 530 ? 156.202 141.378 90.415  1.00 38.22 ?  530 LYS A CB    1 
ATOM   4251  C  CG    . LYS A 1 530 ? 154.688 141.331 90.512  1.00 32.22 ?  530 LYS A CG    1 
ATOM   4252  C  CD    . LYS A 1 530 ? 154.238 140.353 91.578  1.00 34.28 ?  530 LYS A CD    1 
ATOM   4253  C  CE    . LYS A 1 530 ? 152.730 140.222 91.599  1.00 34.98 ?  530 LYS A CE    1 
ATOM   4254  N  NZ    . LYS A 1 530 ? 152.203 140.344 92.981  1.00 38.69 1  530 LYS A NZ    1 
ATOM   4255  N  N     . TYR A 1 531 ? 155.009 143.858 88.470  1.00 32.53 ?  531 TYR A N     1 
ATOM   4256  C  CA    . TYR A 1 531 ? 154.063 144.199 87.420  1.00 28.43 ?  531 TYR A CA    1 
ATOM   4257  C  C     . TYR A 1 531 ? 154.702 144.999 86.297  1.00 29.37 ?  531 TYR A C     1 
ATOM   4258  O  O     . TYR A 1 531 ? 154.300 144.855 85.137  1.00 35.21 ?  531 TYR A O     1 
ATOM   4259  C  CB    . TYR A 1 531 ? 152.891 144.974 88.016  1.00 25.66 ?  531 TYR A CB    1 
ATOM   4260  C  CG    . TYR A 1 531 ? 151.949 144.106 88.810  1.00 29.92 ?  531 TYR A CG    1 
ATOM   4261  C  CD1   . TYR A 1 531 ? 151.395 142.964 88.251  1.00 29.59 ?  531 TYR A CD1   1 
ATOM   4262  C  CD2   . TYR A 1 531 ? 151.617 144.423 90.119  1.00 27.27 ?  531 TYR A CD2   1 
ATOM   4263  C  CE1   . TYR A 1 531 ? 150.534 142.165 88.968  1.00 32.41 ?  531 TYR A CE1   1 
ATOM   4264  C  CE2   . TYR A 1 531 ? 150.756 143.628 90.844  1.00 25.93 ?  531 TYR A CE2   1 
ATOM   4265  C  CZ    . TYR A 1 531 ? 150.217 142.502 90.264  1.00 28.95 ?  531 TYR A CZ    1 
ATOM   4266  O  OH    . TYR A 1 531 ? 149.358 141.705 90.981  1.00 30.57 ?  531 TYR A OH    1 
ATOM   4267  N  N     . VAL A 1 532 ? 155.692 145.837 86.613  1.00 36.10 ?  532 VAL A N     1 
ATOM   4268  C  CA    . VAL A 1 532 ? 156.442 146.543 85.581  1.00 35.37 ?  532 VAL A CA    1 
ATOM   4269  C  C     . VAL A 1 532 ? 157.594 145.714 85.035  1.00 37.91 ?  532 VAL A C     1 
ATOM   4270  O  O     . VAL A 1 532 ? 158.156 146.069 83.986  1.00 42.70 ?  532 VAL A O     1 
ATOM   4271  C  CB    . VAL A 1 532 ? 156.987 147.888 86.106  1.00 36.98 ?  532 VAL A CB    1 
ATOM   4272  C  CG1   . VAL A 1 532 ? 155.852 148.750 86.635  1.00 33.66 ?  532 VAL A CG1   1 
ATOM   4273  C  CG2   . VAL A 1 532 ? 158.041 147.660 87.176  1.00 36.45 ?  532 VAL A CG2   1 
ATOM   4274  N  N     . SER A 1 533 ? 157.966 144.622 85.703  1.00 37.93 ?  533 SER A N     1 
ATOM   4275  C  CA    . SER A 1 533 ? 159.045 143.762 85.232  1.00 36.60 ?  533 SER A CA    1 
ATOM   4276  C  C     . SER A 1 533 ? 158.550 142.498 84.543  1.00 41.39 ?  533 SER A C     1 
ATOM   4277  O  O     . SER A 1 533 ? 159.129 142.084 83.534  1.00 43.93 ?  533 SER A O     1 
ATOM   4278  C  CB    . SER A 1 533 ? 159.957 143.375 86.399  1.00 41.09 ?  533 SER A CB    1 
ATOM   4279  O  OG    . SER A 1 533 ? 159.444 142.257 87.101  1.00 42.74 ?  533 SER A OG    1 
ATOM   4280  N  N     . THR A 1 534 ? 157.496 141.873 85.059  1.00 42.79 ?  534 THR A N     1 
ATOM   4281  C  CA    . THR A 1 534 ? 157.009 140.596 84.558  1.00 38.26 ?  534 THR A CA    1 
ATOM   4282  C  C     . THR A 1 534 ? 155.693 140.787 83.816  1.00 37.89 ?  534 THR A C     1 
ATOM   4283  O  O     . THR A 1 534 ? 154.798 141.493 84.291  1.00 42.30 ?  534 THR A O     1 
ATOM   4284  C  CB    . THR A 1 534 ? 156.820 139.596 85.705  1.00 36.43 ?  534 THR A CB    1 
ATOM   4285  O  OG1   . THR A 1 534 ? 158.093 139.278 86.280  1.00 42.70 ?  534 THR A OG1   1 
ATOM   4286  C  CG2   . THR A 1 534 ? 156.162 138.317 85.209  1.00 39.87 ?  534 THR A CG2   1 
ATOM   4287  N  N     . ASP A 1 535 ? 155.586 140.161 82.647  1.00 40.76 ?  535 ASP A N     1 
ATOM   4288  C  CA    . ASP A 1 535 ? 154.352 140.157 81.877  1.00 41.03 ?  535 ASP A CA    1 
ATOM   4289  C  C     . ASP A 1 535 ? 153.476 138.996 82.331  1.00 44.13 ?  535 ASP A C     1 
ATOM   4290  O  O     . ASP A 1 535 ? 153.964 137.876 82.509  1.00 45.35 ?  535 ASP A O     1 
ATOM   4291  C  CB    . ASP A 1 535 ? 154.648 140.046 80.382  1.00 41.69 ?  535 ASP A CB    1 
ATOM   4292  C  CG    . ASP A 1 535 ? 153.446 139.588 79.581  1.00 47.77 ?  535 ASP A CG    1 
ATOM   4293  O  OD1   . ASP A 1 535 ? 152.569 140.429 79.288  1.00 48.39 ?  535 ASP A OD1   1 
ATOM   4294  O  OD2   . ASP A 1 535 ? 153.376 138.386 79.247  1.00 46.71 -1 535 ASP A OD2   1 
ATOM   4295  N  N     . PHE A 1 536 ? 152.185 139.268 82.520  1.00 33.07 ?  536 PHE A N     1 
ATOM   4296  C  CA    . PHE A 1 536 ? 151.242 138.267 83.001  1.00 31.59 ?  536 PHE A CA    1 
ATOM   4297  C  C     . PHE A 1 536 ? 150.222 137.876 81.939  1.00 38.43 ?  536 PHE A C     1 
ATOM   4298  O  O     . PHE A 1 536 ? 149.133 137.402 82.273  1.00 40.84 ?  536 PHE A O     1 
ATOM   4299  C  CB    . PHE A 1 536 ? 150.540 138.767 84.263  1.00 32.63 ?  536 PHE A CB    1 
ATOM   4300  C  CG    . PHE A 1 536 ? 151.457 138.922 85.442  1.00 33.32 ?  536 PHE A CG    1 
ATOM   4301  C  CD1   . PHE A 1 536 ? 152.162 140.095 85.639  1.00 32.41 ?  536 PHE A CD1   1 
ATOM   4302  C  CD2   . PHE A 1 536 ? 151.618 137.890 86.349  1.00 29.13 ?  536 PHE A CD2   1 
ATOM   4303  C  CE1   . PHE A 1 536 ? 153.007 140.235 86.721  1.00 33.49 ?  536 PHE A CE1   1 
ATOM   4304  C  CE2   . PHE A 1 536 ? 152.462 138.026 87.431  1.00 28.57 ?  536 PHE A CE2   1 
ATOM   4305  C  CZ    . PHE A 1 536 ? 153.156 139.200 87.618  1.00 31.83 ?  536 PHE A CZ    1 
ATOM   4306  N  N     . SER A 1 537 ? 150.552 138.075 80.666  1.00 39.75 ?  537 SER A N     1 
ATOM   4307  C  CA    . SER A 1 537 ? 149.709 137.599 79.585  1.00 37.63 ?  537 SER A CA    1 
ATOM   4308  C  C     . SER A 1 537 ? 149.671 136.070 79.595  1.00 38.56 ?  537 SER A C     1 
ATOM   4309  O  O     . SER A 1 537 ? 150.642 135.424 80.000  1.00 43.02 ?  537 SER A O     1 
ATOM   4310  C  CB    . SER A 1 537 ? 150.238 138.107 78.246  1.00 38.04 ?  537 SER A CB    1 
ATOM   4311  O  OG    . SER A 1 537 ? 149.359 137.799 77.179  1.00 45.62 ?  537 SER A OG    1 
ATOM   4312  N  N     . PRO A 1 538 ? 148.557 135.468 79.177  1.00 39.69 ?  538 PRO A N     1 
ATOM   4313  C  CA    . PRO A 1 538 ? 148.461 134.004 79.204  1.00 38.42 ?  538 PRO A CA    1 
ATOM   4314  C  C     . PRO A 1 538 ? 149.540 133.350 78.353  1.00 41.89 ?  538 PRO A C     1 
ATOM   4315  O  O     . PRO A 1 538 ? 149.858 133.810 77.254  1.00 40.90 ?  538 PRO A O     1 
ATOM   4316  C  CB    . PRO A 1 538 ? 147.062 133.728 78.642  1.00 37.81 ?  538 PRO A CB    1 
ATOM   4317  C  CG    . PRO A 1 538 ? 146.308 134.989 78.860  1.00 39.79 ?  538 PRO A CG    1 
ATOM   4318  C  CD    . PRO A 1 538 ? 147.305 136.092 78.718  1.00 37.05 ?  538 PRO A CD    1 
ATOM   4319  N  N     . LYS A 1 539 ? 150.104 132.262 78.878  1.00 42.14 ?  539 LYS A N     1 
ATOM   4320  C  CA    . LYS A 1 539 ? 151.147 131.517 78.189  1.00 41.99 ?  539 LYS A CA    1 
ATOM   4321  C  C     . LYS A 1 539 ? 150.602 130.419 77.286  1.00 44.20 ?  539 LYS A C     1 
ATOM   4322  O  O     . LYS A 1 539 ? 151.372 129.831 76.521  1.00 48.33 ?  539 LYS A O     1 
ATOM   4323  C  CB    . LYS A 1 539 ? 152.115 130.900 79.204  1.00 44.26 ?  539 LYS A CB    1 
ATOM   4324  C  CG    . LYS A 1 539 ? 152.385 131.772 80.417  1.00 46.33 ?  539 LYS A CG    1 
ATOM   4325  C  CD    . LYS A 1 539 ? 153.679 132.555 80.260  1.00 45.75 ?  539 LYS A CD    1 
ATOM   4326  C  CE    . LYS A 1 539 ? 153.744 133.710 81.246  1.00 46.33 ?  539 LYS A CE    1 
ATOM   4327  N  NZ    . LYS A 1 539 ? 152.897 134.857 80.818  1.00 44.50 1  539 LYS A NZ    1 
ATOM   4328  N  N     . TYR A 1 540 ? 149.306 130.132 77.355  1.00 43.85 ?  540 TYR A N     1 
ATOM   4329  C  CA    . TYR A 1 540 ? 148.684 129.092 76.552  1.00 43.78 ?  540 TYR A CA    1 
ATOM   4330  C  C     . TYR A 1 540 ? 147.703 129.709 75.567  1.00 46.70 ?  540 TYR A C     1 
ATOM   4331  O  O     . TYR A 1 540 ? 146.979 130.653 75.904  1.00 45.29 ?  540 TYR A O     1 
ATOM   4332  C  CB    . TYR A 1 540 ? 147.968 128.066 77.436  1.00 41.74 ?  540 TYR A CB    1 
ATOM   4333  C  CG    . TYR A 1 540 ? 148.882 127.388 78.428  1.00 45.65 ?  540 TYR A CG    1 
ATOM   4334  C  CD1   . TYR A 1 540 ? 149.127 127.946 79.674  1.00 45.44 ?  540 TYR A CD1   1 
ATOM   4335  C  CD2   . TYR A 1 540 ? 149.513 126.193 78.111  1.00 45.66 ?  540 TYR A CD2   1 
ATOM   4336  C  CE1   . TYR A 1 540 ? 149.967 127.331 80.579  1.00 46.54 ?  540 TYR A CE1   1 
ATOM   4337  C  CE2   . TYR A 1 540 ? 150.354 125.570 79.009  1.00 41.75 ?  540 TYR A CE2   1 
ATOM   4338  C  CZ    . TYR A 1 540 ? 150.578 126.143 80.241  1.00 45.77 ?  540 TYR A CZ    1 
ATOM   4339  O  OH    . TYR A 1 540 ? 151.418 125.525 81.136  1.00 45.71 ?  540 TYR A OH    1 
ATOM   4340  N  N     . GLU A 1 541 ? 147.692 129.177 74.343  1.00 49.36 ?  541 GLU A N     1 
ATOM   4341  C  CA    . GLU A 1 541 ? 146.793 129.697 73.319  1.00 47.22 ?  541 GLU A CA    1 
ATOM   4342  C  C     . GLU A 1 541 ? 145.334 129.460 73.683  1.00 49.17 ?  541 GLU A C     1 
ATOM   4343  O  O     . GLU A 1 541 ? 144.468 130.263 73.319  1.00 47.50 ?  541 GLU A O     1 
ATOM   4344  C  CB    . GLU A 1 541 ? 147.125 129.076 71.959  1.00 48.57 ?  541 GLU A CB    1 
ATOM   4345  C  CG    . GLU A 1 541 ? 146.620 127.651 71.750  1.00 52.66 ?  541 GLU A CG    1 
ATOM   4346  C  CD    . GLU A 1 541 ? 147.370 126.627 72.583  1.00 57.43 ?  541 GLU A CD    1 
ATOM   4347  O  OE1   . GLU A 1 541 ? 148.494 126.929 73.038  1.00 55.11 ?  541 GLU A OE1   1 
ATOM   4348  O  OE2   . GLU A 1 541 ? 146.835 125.516 72.782  1.00 52.48 -1 541 GLU A OE2   1 
ATOM   4349  N  N     . LYS A 1 542 ? 145.040 128.370 74.397  1.00 47.03 ?  542 LYS A N     1 
ATOM   4350  C  CA    . LYS A 1 542 ? 143.672 128.126 74.841  1.00 44.20 ?  542 LYS A CA    1 
ATOM   4351  C  C     . LYS A 1 542 ? 143.207 129.207 75.806  1.00 43.71 ?  542 LYS A C     1 
ATOM   4352  O  O     . LYS A 1 542 ? 142.073 129.691 75.712  1.00 46.35 ?  542 LYS A O     1 
ATOM   4353  C  CB    . LYS A 1 542 ? 143.573 126.748 75.492  1.00 42.74 ?  542 LYS A CB    1 
ATOM   4354  C  CG    . LYS A 1 542 ? 142.150 126.271 75.722  1.00 44.00 ?  542 LYS A CG    1 
ATOM   4355  C  CD    . LYS A 1 542 ? 142.093 125.230 76.828  1.00 44.81 ?  542 LYS A CD    1 
ATOM   4356  C  CE    . LYS A 1 542 ? 140.788 124.455 76.789  1.00 46.45 ?  542 LYS A CE    1 
ATOM   4357  N  NZ    . LYS A 1 542 ? 139.616 125.353 76.600  1.00 47.24 1  542 LYS A NZ    1 
ATOM   4358  N  N     . ILE A 1 543 ? 144.069 129.594 76.746  1.00 40.29 ?  543 ILE A N     1 
ATOM   4359  C  CA    . ILE A 1 543 ? 143.717 130.636 77.704  1.00 38.16 ?  543 ILE A CA    1 
ATOM   4360  C  C     . ILE A 1 543 ? 143.677 131.999 77.024  1.00 39.04 ?  543 ILE A C     1 
ATOM   4361  O  O     . ILE A 1 543 ? 142.833 132.844 77.348  1.00 41.31 ?  543 ILE A O     1 
ATOM   4362  C  CB    . ILE A 1 543 ? 144.697 130.619 78.889  1.00 38.43 ?  543 ILE A CB    1 
ATOM   4363  C  CG1   . ILE A 1 543 ? 144.726 129.233 79.536  1.00 38.67 ?  543 ILE A CG1   1 
ATOM   4364  C  CG2   . ILE A 1 543 ? 144.315 131.671 79.909  1.00 39.41 ?  543 ILE A CG2   1 
ATOM   4365  C  CD1   . ILE A 1 543 ? 143.356 128.669 79.841  1.00 37.81 ?  543 ILE A CD1   1 
ATOM   4366  N  N     . ALA A 1 544 ? 144.589 132.239 76.079  1.00 41.27 ?  544 ALA A N     1 
ATOM   4367  C  CA    . ALA A 1 544 ? 144.640 133.534 75.409  1.00 43.83 ?  544 ALA A CA    1 
ATOM   4368  C  C     . ALA A 1 544 ? 143.370 133.813 74.616  1.00 43.06 ?  544 ALA A C     1 
ATOM   4369  O  O     . ALA A 1 544 ? 142.984 134.977 74.458  1.00 43.78 ?  544 ALA A O     1 
ATOM   4370  C  CB    . ALA A 1 544 ? 145.862 133.602 74.493  1.00 44.54 ?  544 ALA A CB    1 
ATOM   4371  N  N     . ASN A 1 545 ? 142.712 132.770 74.105  1.00 44.96 ?  545 ASN A N     1 
ATOM   4372  C  CA    . ASN A 1 545 ? 141.447 132.977 73.407  1.00 46.63 ?  545 ASN A CA    1 
ATOM   4373  C  C     . ASN A 1 545 ? 140.314 133.284 74.376  1.00 46.37 ?  545 ASN A C     1 
ATOM   4374  O  O     . ASN A 1 545 ? 139.328 133.920 73.989  1.00 45.67 ?  545 ASN A O     1 
ATOM   4375  C  CB    . ASN A 1 545 ? 141.103 131.755 72.556  1.00 46.98 ?  545 ASN A CB    1 
ATOM   4376  C  CG    . ASN A 1 545 ? 142.243 131.334 71.652  1.00 50.71 ?  545 ASN A CG    1 
ATOM   4377  O  OD1   . ASN A 1 545 ? 143.125 132.132 71.334  1.00 50.89 ?  545 ASN A OD1   1 
ATOM   4378  N  ND2   . ASN A 1 545 ? 142.231 130.075 71.231  1.00 49.17 ?  545 ASN A ND2   1 
ATOM   4379  N  N     . LEU A 1 546 ? 140.430 132.837 75.629  1.00 44.44 ?  546 LEU A N     1 
ATOM   4380  C  CA    . LEU A 1 546 ? 139.412 133.160 76.623  1.00 42.41 ?  546 LEU A CA    1 
ATOM   4381  C  C     . LEU A 1 546 ? 139.358 134.655 76.900  1.00 42.24 ?  546 LEU A C     1 
ATOM   4382  O  O     . LEU A 1 546 ? 138.299 135.185 77.255  1.00 45.24 ?  546 LEU A O     1 
ATOM   4383  C  CB    . LEU A 1 546 ? 139.677 132.391 77.917  1.00 40.80 ?  546 LEU A CB    1 
ATOM   4384  C  CG    . LEU A 1 546 ? 139.533 130.870 77.868  1.00 39.12 ?  546 LEU A CG    1 
ATOM   4385  C  CD1   . LEU A 1 546 ? 139.910 130.263 79.206  1.00 39.65 ?  546 LEU A CD1   1 
ATOM   4386  C  CD2   . LEU A 1 546 ? 138.120 130.473 77.480  1.00 40.10 ?  546 LEU A CD2   1 
ATOM   4387  N  N     . PHE A 1 547 ? 140.482 135.350 76.739  1.00 40.24 ?  547 PHE A N     1 
ATOM   4388  C  CA    . PHE A 1 547 ? 140.560 136.786 76.962  1.00 40.24 ?  547 PHE A CA    1 
ATOM   4389  C  C     . PHE A 1 547 ? 140.459 137.584 75.669  1.00 40.78 ?  547 PHE A C     1 
ATOM   4390  O  O     . PHE A 1 547 ? 140.681 138.798 75.684  1.00 42.05 ?  547 PHE A O     1 
ATOM   4391  C  CB    . PHE A 1 547 ? 141.859 137.133 77.691  1.00 36.73 ?  547 PHE A CB    1 
ATOM   4392  C  CG    . PHE A 1 547 ? 141.886 136.696 79.126  1.00 38.42 ?  547 PHE A CG    1 
ATOM   4393  C  CD1   . PHE A 1 547 ? 141.353 137.498 80.119  1.00 37.60 ?  547 PHE A CD1   1 
ATOM   4394  C  CD2   . PHE A 1 547 ? 142.446 135.481 79.482  1.00 37.01 ?  547 PHE A CD2   1 
ATOM   4395  C  CE1   . PHE A 1 547 ? 141.379 137.098 81.440  1.00 33.39 ?  547 PHE A CE1   1 
ATOM   4396  C  CE2   . PHE A 1 547 ? 142.474 135.077 80.801  1.00 35.07 ?  547 PHE A CE2   1 
ATOM   4397  C  CZ    . PHE A 1 547 ? 141.940 135.886 81.780  1.00 34.33 ?  547 PHE A CZ    1 
ATOM   4398  N  N     . GLU A 1 548 ? 140.137 136.930 74.555  1.00 50.24 ?  548 GLU A N     1 
ATOM   4399  C  CA    . GLU A 1 548 ? 140.005 137.628 73.284  1.00 52.22 ?  548 GLU A CA    1 
ATOM   4400  C  C     . GLU A 1 548 ? 138.850 138.619 73.343  1.00 51.05 ?  548 GLU A C     1 
ATOM   4401  O  O     . GLU A 1 548 ? 137.771 138.312 73.855  1.00 51.91 ?  548 GLU A O     1 
ATOM   4402  C  CB    . GLU A 1 548 ? 139.798 136.621 72.149  1.00 48.82 ?  548 GLU A CB    1 
ATOM   4403  C  CG    . GLU A 1 548 ? 139.120 137.176 70.901  1.00 51.53 ?  548 GLU A CG    1 
ATOM   4404  C  CD    . GLU A 1 548 ? 137.610 137.019 70.931  1.00 52.72 ?  548 GLU A CD    1 
ATOM   4405  O  OE1   . GLU A 1 548 ? 136.908 137.911 70.411  1.00 51.34 ?  548 GLU A OE1   1 
ATOM   4406  O  OE2   . GLU A 1 548 ? 137.128 136.000 71.470  1.00 53.80 -1 548 GLU A OE2   1 
ATOM   4407  N  N     . GLY A 1 549 ? 139.081 139.815 72.807  1.00 45.32 ?  549 GLY A N     1 
ATOM   4408  C  CA    . GLY A 1 549 ? 138.121 140.891 72.908  1.00 46.85 ?  549 GLY A CA    1 
ATOM   4409  C  C     . GLY A 1 549 ? 138.205 141.695 74.185  1.00 47.31 ?  549 GLY A C     1 
ATOM   4410  O  O     . GLY A 1 549 ? 137.378 142.593 74.388  1.00 46.90 ?  549 GLY A O     1 
ATOM   4411  N  N     . MET A 1 550 ? 139.173 141.403 75.050  1.00 47.64 ?  550 MET A N     1 
ATOM   4412  C  CA    . MET A 1 550 ? 139.355 142.106 76.310  1.00 44.25 ?  550 MET A CA    1 
ATOM   4413  C  C     . MET A 1 550 ? 140.831 142.434 76.468  1.00 44.66 ?  550 MET A C     1 
ATOM   4414  O  O     . MET A 1 550 ? 141.677 141.537 76.409  1.00 48.18 ?  550 MET A O     1 
ATOM   4415  C  CB    . MET A 1 550 ? 138.857 141.258 77.483  1.00 43.54 ?  550 MET A CB    1 
ATOM   4416  C  CG    . MET A 1 550 ? 138.282 142.056 78.635  1.00 48.40 ?  550 MET A CG    1 
ATOM   4417  S  SD    . MET A 1 550 ? 138.036 141.060 80.116  1.00 55.01 ?  550 MET A SD    1 
ATOM   4418  C  CE    . MET A 1 550 ? 138.069 139.402 79.442  1.00 44.39 ?  550 MET A CE    1 
ATOM   4419  N  N     . HIS A 1 551 ? 141.139 143.713 76.664  1.00 40.57 ?  551 HIS A N     1 
ATOM   4420  C  CA    . HIS A 1 551 ? 142.529 144.145 76.711  1.00 40.38 ?  551 HIS A CA    1 
ATOM   4421  C  C     . HIS A 1 551 ? 143.205 143.658 77.987  1.00 41.17 ?  551 HIS A C     1 
ATOM   4422  O  O     . HIS A 1 551 ? 142.684 143.840 79.091  1.00 42.19 ?  551 HIS A O     1 
ATOM   4423  C  CB    . HIS A 1 551 ? 142.619 145.667 76.618  1.00 39.62 ?  551 HIS A CB    1 
ATOM   4424  C  CG    . HIS A 1 551 ? 143.982 146.208 76.920  1.00 43.71 ?  551 HIS A CG    1 
ATOM   4425  N  ND1   . HIS A 1 551 ? 145.007 146.198 75.998  1.00 46.46 ?  551 HIS A ND1   1 
ATOM   4426  C  CD2   . HIS A 1 551 ? 144.489 146.771 78.041  1.00 43.40 ?  551 HIS A CD2   1 
ATOM   4427  C  CE1   . HIS A 1 551 ? 146.086 146.732 76.539  1.00 44.87 ?  551 HIS A CE1   1 
ATOM   4428  N  NE2   . HIS A 1 551 ? 145.800 147.089 77.777  1.00 43.03 ?  551 HIS A NE2   1 
ATOM   4429  N  N     . ILE A 1 552 ? 144.370 143.043 77.830  1.00 37.11 ?  552 ILE A N     1 
ATOM   4430  C  CA    . ILE A 1 552 ? 145.177 142.562 78.947  1.00 36.65 ?  552 ILE A CA    1 
ATOM   4431  C  C     . ILE A 1 552 ? 146.283 143.582 79.197  1.00 39.13 ?  552 ILE A C     1 
ATOM   4432  O  O     . ILE A 1 552 ? 147.100 143.819 78.295  1.00 41.15 ?  552 ILE A O     1 
ATOM   4433  C  CB    . ILE A 1 552 ? 145.765 141.173 78.661  1.00 36.39 ?  552 ILE A CB    1 
ATOM   4434  C  CG1   . ILE A 1 552 ? 144.644 140.166 78.402  1.00 35.61 ?  552 ILE A CG1   1 
ATOM   4435  C  CG2   . ILE A 1 552 ? 146.637 140.717 79.813  1.00 35.93 ?  552 ILE A CG2   1 
ATOM   4436  C  CD1   . ILE A 1 552 ? 145.125 138.864 77.813  1.00 39.04 ?  552 ILE A CD1   1 
ATOM   4437  N  N     . PRO A 1 553 ? 146.338 144.209 80.371  1.00 41.21 ?  553 PRO A N     1 
ATOM   4438  C  CA    . PRO A 1 553 ? 147.400 145.188 80.634  1.00 37.58 ?  553 PRO A CA    1 
ATOM   4439  C  C     . PRO A 1 553 ? 148.781 144.561 80.532  1.00 37.53 ?  553 PRO A C     1 
ATOM   4440  O  O     . PRO A 1 553 ? 149.029 143.462 81.034  1.00 35.05 ?  553 PRO A O     1 
ATOM   4441  C  CB    . PRO A 1 553 ? 147.101 145.659 82.062  1.00 34.42 ?  553 PRO A CB    1 
ATOM   4442  C  CG    . PRO A 1 553 ? 145.663 145.349 82.273  1.00 32.51 ?  553 PRO A CG    1 
ATOM   4443  C  CD    . PRO A 1 553 ? 145.387 144.113 81.487  1.00 33.93 ?  553 PRO A CD    1 
ATOM   4444  N  N     . THR A 1 554 ? 149.681 145.280 79.878  1.00 42.64 ?  554 THR A N     1 
ATOM   4445  C  CA    . THR A 1 554 ? 151.047 144.843 79.666  1.00 40.12 ?  554 THR A CA    1 
ATOM   4446  C  C     . THR A 1 554 ? 151.955 145.479 80.714  1.00 36.10 ?  554 THR A C     1 
ATOM   4447  O  O     . THR A 1 554 ? 151.492 146.076 81.690  1.00 38.78 ?  554 THR A O     1 
ATOM   4448  C  CB    . THR A 1 554 ? 151.488 145.191 78.243  1.00 38.52 ?  554 THR A CB    1 
ATOM   4449  O  OG1   . THR A 1 554 ? 151.430 146.611 78.059  1.00 43.66 ?  554 THR A OG1   1 
ATOM   4450  C  CG2   . THR A 1 554 ? 150.578 144.519 77.228  1.00 40.83 ?  554 THR A CG2   1 
ATOM   4451  N  N     . THR A 1 555 ? 153.267 145.343 80.522  1.00 38.32 ?  555 THR A N     1 
ATOM   4452  C  CA    . THR A 1 555 ? 154.207 146.020 81.407  1.00 35.88 ?  555 THR A CA    1 
ATOM   4453  C  C     . THR A 1 555 ? 154.121 147.533 81.244  1.00 38.84 ?  555 THR A C     1 
ATOM   4454  O  O     . THR A 1 555 ? 154.266 148.274 82.220  1.00 42.01 ?  555 THR A O     1 
ATOM   4455  C  CB    . THR A 1 555 ? 155.629 145.533 81.143  1.00 39.23 ?  555 THR A CB    1 
ATOM   4456  O  OG1   . THR A 1 555 ? 155.802 145.293 79.741  1.00 47.13 ?  555 THR A OG1   1 
ATOM   4457  C  CG2   . THR A 1 555 ? 155.899 144.246 81.908  1.00 38.19 ?  555 THR A CG2   1 
ATOM   4458  N  N     . GLU A 1 556 ? 153.891 148.008 80.018  1.00 39.45 ?  556 GLU A N     1 
ATOM   4459  C  CA    . GLU A 1 556 ? 153.736 149.443 79.794  1.00 41.11 ?  556 GLU A CA    1 
ATOM   4460  C  C     . GLU A 1 556 ? 152.491 149.980 80.490  1.00 41.76 ?  556 GLU A C     1 
ATOM   4461  O  O     . GLU A 1 556 ? 152.518 151.067 81.082  1.00 44.03 ?  556 GLU A O     1 
ATOM   4462  C  CB    . GLU A 1 556 ? 153.681 149.734 78.294  1.00 41.87 ?  556 GLU A CB    1 
ATOM   4463  C  CG    . GLU A 1 556 ? 154.903 149.283 77.485  1.00 45.29 ?  556 GLU A CG    1 
ATOM   4464  C  CD    . GLU A 1 556 ? 156.230 149.399 78.229  1.00 49.26 ?  556 GLU A CD    1 
ATOM   4465  O  OE1   . GLU A 1 556 ? 157.087 148.507 78.053  1.00 49.26 ?  556 GLU A OE1   1 
ATOM   4466  O  OE2   . GLU A 1 556 ? 156.448 150.404 78.939  1.00 43.00 -1 556 GLU A OE2   1 
ATOM   4467  N  N     . ASP A 1 557 ? 151.387 149.233 80.422  1.00 42.48 ?  557 ASP A N     1 
ATOM   4468  C  CA    . ASP A 1 557 ? 150.174 149.647 81.117  1.00 39.88 ?  557 ASP A CA    1 
ATOM   4469  C  C     . ASP A 1 557 ? 150.399 149.694 82.622  1.00 37.08 ?  557 ASP A C     1 
ATOM   4470  O  O     . ASP A 1 557 ? 149.916 150.606 83.301  1.00 37.78 ?  557 ASP A O     1 
ATOM   4471  C  CB    . ASP A 1 557 ? 149.026 148.698 80.776  1.00 37.18 ?  557 ASP A CB    1 
ATOM   4472  C  CG    . ASP A 1 557 ? 148.237 149.155 79.571  1.00 43.58 ?  557 ASP A CG    1 
ATOM   4473  O  OD1   . ASP A 1 557 ? 147.891 150.352 79.504  1.00 45.62 ?  557 ASP A OD1   1 
ATOM   4474  O  OD2   . ASP A 1 557 ? 147.963 148.315 78.687  1.00 43.98 -1 557 ASP A OD2   1 
ATOM   4475  N  N     . TRP A 1 558 ? 151.137 148.722 83.157  1.00 30.18 ?  558 TRP A N     1 
ATOM   4476  C  CA    . TRP A 1 558 ? 151.429 148.726 84.585  1.00 27.84 ?  558 TRP A CA    1 
ATOM   4477  C  C     . TRP A 1 558 ? 152.363 149.867 84.969  1.00 34.90 ?  558 TRP A C     1 
ATOM   4478  O  O     . TRP A 1 558 ? 152.230 150.421 86.062  1.00 35.93 ?  558 TRP A O     1 
ATOM   4479  C  CB    . TRP A 1 558 ? 152.020 147.383 85.003  1.00 30.23 ?  558 TRP A CB    1 
ATOM   4480  C  CG    . TRP A 1 558 ? 150.988 146.380 85.411  1.00 29.42 ?  558 TRP A CG    1 
ATOM   4481  C  CD1   . TRP A 1 558 ? 150.572 145.293 84.701  1.00 28.16 ?  558 TRP A CD1   1 
ATOM   4482  C  CD2   . TRP A 1 558 ? 150.234 146.374 86.630  1.00 28.54 ?  558 TRP A CD2   1 
ATOM   4483  N  NE1   . TRP A 1 558 ? 149.612 144.607 85.402  1.00 30.68 ?  558 TRP A NE1   1 
ATOM   4484  C  CE2   . TRP A 1 558 ? 149.387 145.250 86.591  1.00 29.91 ?  558 TRP A CE2   1 
ATOM   4485  C  CE3   . TRP A 1 558 ? 150.198 147.205 87.753  1.00 32.95 ?  558 TRP A CE3   1 
ATOM   4486  C  CZ2   . TRP A 1 558 ? 148.515 144.938 87.629  1.00 24.29 ?  558 TRP A CZ2   1 
ATOM   4487  C  CZ3   . TRP A 1 558 ? 149.330 146.894 88.780  1.00 27.71 ?  558 TRP A CZ3   1 
ATOM   4488  C  CH2   . TRP A 1 558 ? 148.501 145.772 88.713  1.00 19.86 ?  558 TRP A CH2   1 
ATOM   4489  N  N     . LYS A 1 559 ? 153.306 150.234 84.098  1.00 40.62 ?  559 LYS A N     1 
ATOM   4490  C  CA    . LYS A 1 559 ? 154.140 151.404 84.363  1.00 35.82 ?  559 LYS A CA    1 
ATOM   4491  C  C     . LYS A 1 559 ? 153.306 152.679 84.386  1.00 36.87 ?  559 LYS A C     1 
ATOM   4492  O  O     . LYS A 1 559 ? 153.500 153.545 85.249  1.00 40.72 ?  559 LYS A O     1 
ATOM   4493  C  CB    . LYS A 1 559 ? 155.248 151.513 83.316  1.00 38.77 ?  559 LYS A CB    1 
ATOM   4494  C  CG    . LYS A 1 559 ? 156.300 150.425 83.394  1.00 38.52 ?  559 LYS A CG    1 
ATOM   4495  C  CD    . LYS A 1 559 ? 157.137 150.383 82.128  1.00 41.10 ?  559 LYS A CD    1 
ATOM   4496  C  CE    . LYS A 1 559 ? 158.247 149.351 82.227  1.00 40.35 ?  559 LYS A CE    1 
ATOM   4497  N  NZ    . LYS A 1 559 ? 159.007 149.466 83.502  1.00 43.81 1  559 LYS A NZ    1 
ATOM   4498  N  N     . LYS A 1 560 ? 152.374 152.809 83.439  1.00 36.29 ?  560 LYS A N     1 
ATOM   4499  C  CA    . LYS A 1 560 ? 151.487 153.968 83.435  1.00 33.56 ?  560 LYS A CA    1 
ATOM   4500  C  C     . LYS A 1 560 ? 150.628 154.007 84.692  1.00 36.41 ?  560 LYS A C     1 
ATOM   4501  O  O     . LYS A 1 560 ? 150.429 155.074 85.284  1.00 42.03 ?  560 LYS A O     1 
ATOM   4502  C  CB    . LYS A 1 560 ? 150.608 153.953 82.183  1.00 34.44 ?  560 LYS A CB    1 
ATOM   4503  C  CG    . LYS A 1 560 ? 151.365 154.206 80.891  1.00 38.39 ?  560 LYS A CG    1 
ATOM   4504  C  CD    . LYS A 1 560 ? 150.430 154.197 79.695  1.00 39.77 ?  560 LYS A CD    1 
ATOM   4505  C  CE    . LYS A 1 560 ? 151.123 153.655 78.456  1.00 40.30 ?  560 LYS A CE    1 
ATOM   4506  N  NZ    . LYS A 1 560 ? 150.832 152.211 78.241  1.00 40.83 1  560 LYS A NZ    1 
ATOM   4507  N  N     . LEU A 1 561 ? 150.114 152.851 85.118  1.00 33.41 ?  561 LEU A N     1 
ATOM   4508  C  CA    . LEU A 1 561 ? 149.326 152.796 86.346  1.00 29.59 ?  561 LEU A CA    1 
ATOM   4509  C  C     . LEU A 1 561 ? 150.174 153.131 87.566  1.00 32.43 ?  561 LEU A C     1 
ATOM   4510  O  O     . LEU A 1 561 ? 149.694 153.776 88.502  1.00 36.45 ?  561 LEU A O     1 
ATOM   4511  C  CB    . LEU A 1 561 ? 148.685 151.417 86.503  1.00 31.12 ?  561 LEU A CB    1 
ATOM   4512  C  CG    . LEU A 1 561 ? 147.887 151.230 87.794  1.00 31.43 ?  561 LEU A CG    1 
ATOM   4513  C  CD1   . LEU A 1 561 ? 146.745 152.228 87.857  1.00 27.55 ?  561 LEU A CD1   1 
ATOM   4514  C  CD2   . LEU A 1 561 ? 147.368 149.814 87.922  1.00 28.89 ?  561 LEU A CD2   1 
ATOM   4515  N  N     . LYS A 1 562 ? 151.429 152.682 87.584  1.00 34.56 ?  562 LYS A N     1 
ATOM   4516  C  CA    . LYS A 1 562 ? 152.324 153.014 88.687  1.00 33.38 ?  562 LYS A CA    1 
ATOM   4517  C  C     . LYS A 1 562 ? 152.569 154.513 88.762  1.00 34.22 ?  562 LYS A C     1 
ATOM   4518  O  O     . LYS A 1 562 ? 152.552 155.098 89.851  1.00 38.77 ?  562 LYS A O     1 
ATOM   4519  C  CB    . LYS A 1 562 ? 153.644 152.257 88.528  1.00 35.62 ?  562 LYS A CB    1 
ATOM   4520  C  CG    . LYS A 1 562 ? 154.747 152.710 89.462  1.00 31.08 ?  562 LYS A CG    1 
ATOM   4521  C  CD    . LYS A 1 562 ? 156.057 152.021 89.131  1.00 28.64 ?  562 LYS A CD    1 
ATOM   4522  C  CE    . LYS A 1 562 ? 157.181 152.506 90.028  1.00 34.47 ?  562 LYS A CE    1 
ATOM   4523  N  NZ    . LYS A 1 562 ? 158.290 151.516 90.101  1.00 41.45 1  562 LYS A NZ    1 
ATOM   4524  N  N     . ALA A 1 563 ? 152.790 155.155 87.612  1.00 32.24 ?  563 ALA A N     1 
ATOM   4525  C  CA    . ALA A 1 563 ? 152.939 156.608 87.596  1.00 33.14 ?  563 ALA A CA    1 
ATOM   4526  C  C     . ALA A 1 563 ? 151.660 157.298 88.058  1.00 36.18 ?  563 ALA A C     1 
ATOM   4527  O  O     . ALA A 1 563 ? 151.708 158.271 88.822  1.00 42.44 ?  563 ALA A O     1 
ATOM   4528  C  CB    . ALA A 1 563 ? 153.332 157.078 86.198  1.00 35.79 ?  563 ALA A CB    1 
ATOM   4529  N  N     . PHE A 1 564 ? 150.506 156.800 87.608  1.00 34.18 ?  564 PHE A N     1 
ATOM   4530  C  CA    . PHE A 1 564 ? 149.226 157.373 88.012  1.00 31.53 ?  564 PHE A CA    1 
ATOM   4531  C  C     . PHE A 1 564 ? 149.027 157.272 89.520  1.00 35.60 ?  564 PHE A C     1 
ATOM   4532  O  O     . PHE A 1 564 ? 148.551 158.217 90.157  1.00 38.50 ?  564 PHE A O     1 
ATOM   4533  C  CB    . PHE A 1 564 ? 148.094 156.666 87.266  1.00 32.91 ?  564 PHE A CB    1 
ATOM   4534  C  CG    . PHE A 1 564 ? 146.778 157.384 87.323  1.00 33.21 ?  564 PHE A CG    1 
ATOM   4535  C  CD1   . PHE A 1 564 ? 146.447 158.327 86.367  1.00 35.68 ?  564 PHE A CD1   1 
ATOM   4536  C  CD2   . PHE A 1 564 ? 145.866 157.102 88.325  1.00 34.31 ?  564 PHE A CD2   1 
ATOM   4537  C  CE1   . PHE A 1 564 ? 145.232 158.983 86.415  1.00 39.13 ?  564 PHE A CE1   1 
ATOM   4538  C  CE2   . PHE A 1 564 ? 144.652 157.755 88.378  1.00 35.63 ?  564 PHE A CE2   1 
ATOM   4539  C  CZ    . PHE A 1 564 ? 144.333 158.696 87.422  1.00 38.90 ?  564 PHE A CZ    1 
ATOM   4540  N  N     . VAL A 1 565 ? 149.382 156.128 90.105  1.00 35.82 ?  565 VAL A N     1 
ATOM   4541  C  CA    . VAL A 1 565 ? 149.244 155.942 91.545  1.00 29.96 ?  565 VAL A CA    1 
ATOM   4542  C  C     . VAL A 1 565 ? 150.225 156.830 92.297  1.00 33.54 ?  565 VAL A C     1 
ATOM   4543  O  O     . VAL A 1 565 ? 149.880 157.428 93.324  1.00 36.12 ?  565 VAL A O     1 
ATOM   4544  C  CB    . VAL A 1 565 ? 149.430 154.455 91.903  1.00 29.53 ?  565 VAL A CB    1 
ATOM   4545  C  CG1   . VAL A 1 565 ? 149.662 154.282 93.394  1.00 28.69 ?  565 VAL A CG1   1 
ATOM   4546  C  CG2   . VAL A 1 565 ? 148.224 153.660 91.457  1.00 33.70 ?  565 VAL A CG2   1 
ATOM   4547  N  N     . ALA A 1 566 ? 151.458 156.938 91.802  1.00 36.68 ?  566 ALA A N     1 
ATOM   4548  C  CA    . ALA A 1 566 ? 152.445 157.786 92.459  1.00 36.24 ?  566 ALA A CA    1 
ATOM   4549  C  C     . ALA A 1 566 ? 152.044 159.252 92.416  1.00 38.26 ?  566 ALA A C     1 
ATOM   4550  O  O     . ALA A 1 566 ? 152.384 160.014 93.327  1.00 42.85 ?  566 ALA A O     1 
ATOM   4551  C  CB    . ALA A 1 566 ? 153.816 157.591 91.814  1.00 36.68 ?  566 ALA A CB    1 
ATOM   4552  N  N     . GLU A 1 567 ? 151.324 159.666 91.375  1.00 40.84 ?  567 GLU A N     1 
ATOM   4553  C  CA    . GLU A 1 567 ? 150.941 161.063 91.235  1.00 40.06 ?  567 GLU A CA    1 
ATOM   4554  C  C     . GLU A 1 567 ? 149.582 161.389 91.845  1.00 39.80 ?  567 GLU A C     1 
ATOM   4555  O  O     . GLU A 1 567 ? 149.329 162.559 92.154  1.00 43.67 ?  567 GLU A O     1 
ATOM   4556  C  CB    . GLU A 1 567 ? 150.966 161.455 89.751  1.00 42.38 ?  567 GLU A CB    1 
ATOM   4557  C  CG    . GLU A 1 567 ? 150.938 162.947 89.480  1.00 43.90 ?  567 GLU A CG    1 
ATOM   4558  C  CD    . GLU A 1 567 ? 149.630 163.393 88.870  1.00 47.55 ?  567 GLU A CD    1 
ATOM   4559  O  OE1   . GLU A 1 567 ? 148.989 162.568 88.188  1.00 46.07 ?  567 GLU A OE1   1 
ATOM   4560  O  OE2   . GLU A 1 567 ? 149.243 164.564 89.068  1.00 47.17 -1 567 GLU A OE2   1 
ATOM   4561  N  N     . HIS A 1 568 ? 148.709 160.397 92.040  1.00 39.70 ?  568 HIS A N     1 
ATOM   4562  C  CA    . HIS A 1 568 ? 147.397 160.623 92.632  1.00 38.76 ?  568 HIS A CA    1 
ATOM   4563  C  C     . HIS A 1 568 ? 147.135 159.864 93.924  1.00 35.94 ?  568 HIS A C     1 
ATOM   4564  O  O     . HIS A 1 568 ? 146.227 160.253 94.666  1.00 40.11 ?  568 HIS A O     1 
ATOM   4565  C  CB    . HIS A 1 568 ? 146.283 160.263 91.636  1.00 37.02 ?  568 HIS A CB    1 
ATOM   4566  C  CG    . HIS A 1 568 ? 146.158 161.220 90.494  1.00 38.46 ?  568 HIS A CG    1 
ATOM   4567  N  ND1   . HIS A 1 568 ? 145.470 160.917 89.340  1.00 42.97 ?  568 HIS A ND1   1 
ATOM   4568  C  CD2   . HIS A 1 568 ? 146.638 162.473 90.327  1.00 38.74 ?  568 HIS A CD2   1 
ATOM   4569  C  CE1   . HIS A 1 568 ? 145.537 161.941 88.508  1.00 42.21 ?  568 HIS A CE1   1 
ATOM   4570  N  NE2   . HIS A 1 568 ? 146.235 162.902 89.086  1.00 41.84 ?  568 HIS A NE2   1 
ATOM   4571  N  N     . GLY A 1 569 ? 147.882 158.805 94.216  1.00 29.47 ?  569 GLY A N     1 
ATOM   4572  C  CA    . GLY A 1 569 ? 147.655 158.050 95.432  1.00 29.61 ?  569 GLY A CA    1 
ATOM   4573  C  C     . GLY A 1 569 ? 146.580 156.993 95.280  1.00 28.19 ?  569 GLY A C     1 
ATOM   4574  O  O     . GLY A 1 569 ? 145.974 156.809 94.226  1.00 33.66 ?  569 GLY A O     1 
ATOM   4575  N  N     . MET A 1 570 ? 146.344 156.278 96.378  1.00 24.21 ?  570 MET A N     1 
ATOM   4576  C  CA    . MET A 1 570 ? 145.359 155.209 96.436  1.00 22.67 ?  570 MET A CA    1 
ATOM   4577  C  C     . MET A 1 570 ? 144.344 155.506 97.528  1.00 24.38 ?  570 MET A C     1 
ATOM   4578  O  O     . MET A 1 570 ? 144.706 155.955 98.618  1.00 31.69 ?  570 MET A O     1 
ATOM   4579  C  CB    . MET A 1 570 ? 146.025 153.855 96.701  1.00 26.83 ?  570 MET A CB    1 
ATOM   4580  C  CG    . MET A 1 570 ? 146.926 153.377 95.581  1.00 24.76 ?  570 MET A CG    1 
ATOM   4581  S  SD    . MET A 1 570 ? 146.105 152.199 94.503  1.00 38.07 ?  570 MET A SD    1 
ATOM   4582  C  CE    . MET A 1 570 ? 146.022 150.781 95.585  1.00 24.88 ?  570 MET A CE    1 
ATOM   4583  N  N     . TYR A 1 571 ? 143.071 155.248 97.231  1.00 15.53 ?  571 TYR A N     1 
ATOM   4584  C  CA    . TYR A 1 571 ? 142.017 155.528 98.198  1.00 9.58  ?  571 TYR A CA    1 
ATOM   4585  C  C     . TYR A 1 571 ? 141.853 154.407 99.216  1.00 18.52 ?  571 TYR A C     1 
ATOM   4586  O  O     . TYR A 1 571 ? 141.515 154.676 100.374 1.00 20.21 ?  571 TYR A O     1 
ATOM   4587  C  CB    . TYR A 1 571 ? 140.693 155.768 97.474  1.00 20.46 ?  571 TYR A CB    1 
ATOM   4588  C  CG    . TYR A 1 571 ? 139.621 156.359 98.354  1.00 24.83 ?  571 TYR A CG    1 
ATOM   4589  C  CD1   . TYR A 1 571 ? 139.645 157.701 98.699  1.00 23.83 ?  571 TYR A CD1   1 
ATOM   4590  C  CD2   . TYR A 1 571 ? 138.586 155.575 98.842  1.00 19.14 ?  571 TYR A CD2   1 
ATOM   4591  C  CE1   . TYR A 1 571 ? 138.670 158.246 99.503  1.00 26.06 ?  571 TYR A CE1   1 
ATOM   4592  C  CE2   . TYR A 1 571 ? 137.608 156.112 99.647  1.00 20.62 ?  571 TYR A CE2   1 
ATOM   4593  C  CZ    . TYR A 1 571 ? 137.652 157.448 99.974  1.00 28.45 ?  571 TYR A CZ    1 
ATOM   4594  O  OH    . TYR A 1 571 ? 136.677 157.989 100.776 1.00 27.40 ?  571 TYR A OH    1 
ATOM   4595  N  N     . HIS A 1 572 ? 142.079 153.162 98.815  1.00 23.11 ?  572 HIS A N     1 
ATOM   4596  C  CA    . HIS A 1 572 ? 141.898 152.007 99.682  1.00 14.41 ?  572 HIS A CA    1 
ATOM   4597  C  C     . HIS A 1 572 ? 143.252 151.422 100.046 1.00 13.07 ?  572 HIS A C     1 
ATOM   4598  O  O     . HIS A 1 572 ? 144.082 151.173 99.167  1.00 26.25 ?  572 HIS A O     1 
ATOM   4599  C  CB    . HIS A 1 572 ? 141.034 150.940 99.006  1.00 14.72 ?  572 HIS A CB    1 
ATOM   4600  C  CG    . HIS A 1 572 ? 139.832 151.489 98.304  1.00 9.11  ?  572 HIS A CG    1 
ATOM   4601  N  ND1   . HIS A 1 572 ? 139.836 151.812 96.966  1.00 18.58 ?  572 HIS A ND1   1 
ATOM   4602  C  CD2   . HIS A 1 572 ? 138.587 151.767 98.755  1.00 15.19 ?  572 HIS A CD2   1 
ATOM   4603  C  CE1   . HIS A 1 572 ? 138.646 152.269 96.622  1.00 19.44 ?  572 HIS A CE1   1 
ATOM   4604  N  NE2   . HIS A 1 572 ? 137.869 152.250 97.689  1.00 24.26 ?  572 HIS A NE2   1 
ATOM   4605  N  N     . SER A 1 573 ? 143.472 151.209 101.345 1.00 8.03  ?  573 SER A N     1 
ATOM   4606  C  CA    . SER A 1 573 ? 144.684 150.525 101.781 1.00 8.56  ?  573 SER A CA    1 
ATOM   4607  C  C     . SER A 1 573 ? 144.703 149.087 101.285 1.00 15.34 ?  573 SER A C     1 
ATOM   4608  O  O     . SER A 1 573 ? 145.750 148.576 100.872 1.00 24.43 ?  573 SER A O     1 
ATOM   4609  C  CB    . SER A 1 573 ? 144.796 150.575 103.304 1.00 12.75 ?  573 SER A CB    1 
ATOM   4610  O  OG    . SER A 1 573 ? 143.569 150.220 103.911 1.00 21.38 ?  573 SER A OG    1 
ATOM   4611  N  N     . TYR A 1 574 ? 143.551 148.422 101.317 1.00 16.85 ?  574 TYR A N     1 
ATOM   4612  C  CA    . TYR A 1 574 ? 143.399 147.062 100.829 1.00 5.31  ?  574 TYR A CA    1 
ATOM   4613  C  C     . TYR A 1 574 ? 142.172 147.005 99.934  1.00 9.09  ?  574 TYR A C     1 
ATOM   4614  O  O     . TYR A 1 574 ? 141.175 147.684 100.195 1.00 13.59 ?  574 TYR A O     1 
ATOM   4615  C  CB    . TYR A 1 574 ? 143.267 146.073 101.989 1.00 12.98 ?  574 TYR A CB    1 
ATOM   4616  C  CG    . TYR A 1 574 ? 144.387 146.193 102.994 1.00 7.77  ?  574 TYR A CG    1 
ATOM   4617  C  CD1   . TYR A 1 574 ? 144.317 147.116 104.027 1.00 6.39  ?  574 TYR A CD1   1 
ATOM   4618  C  CD2   . TYR A 1 574 ? 145.517 145.397 102.903 1.00 10.01 ?  574 TYR A CD2   1 
ATOM   4619  C  CE1   . TYR A 1 574 ? 145.335 147.242 104.940 1.00 9.56  ?  574 TYR A CE1   1 
ATOM   4620  C  CE2   . TYR A 1 574 ? 146.541 145.514 103.817 1.00 17.92 ?  574 TYR A CE2   1 
ATOM   4621  C  CZ    . TYR A 1 574 ? 146.443 146.440 104.833 1.00 8.20  ?  574 TYR A CZ    1 
ATOM   4622  O  OH    . TYR A 1 574 ? 147.455 146.566 105.751 1.00 14.62 ?  574 TYR A OH    1 
ATOM   4623  N  N     . ARG A 1 575 ? 142.251 146.215 98.879  1.00 16.15 ?  575 ARG A N     1 
ATOM   4624  C  CA    . ARG A 1 575 ? 141.163 146.193 97.909  1.00 7.89  ?  575 ARG A CA    1 
ATOM   4625  C  C     . ARG A 1 575 ? 140.596 144.806 97.659  1.00 12.24 ?  575 ARG A C     1 
ATOM   4626  O  O     . ARG A 1 575 ? 139.382 144.665 97.507  1.00 20.45 ?  575 ARG A O     1 
ATOM   4627  C  CB    . ARG A 1 575 ? 141.635 146.793 96.580  1.00 15.51 ?  575 ARG A CB    1 
ATOM   4628  C  CG    . ARG A 1 575 ? 142.124 148.223 96.674  1.00 6.14  ?  575 ARG A CG    1 
ATOM   4629  C  CD    . ARG A 1 575 ? 143.133 148.509 95.582  1.00 12.48 ?  575 ARG A CD    1 
ATOM   4630  N  NE    . ARG A 1 575 ? 144.411 147.859 95.848  1.00 22.24 ?  575 ARG A NE    1 
ATOM   4631  C  CZ    . ARG A 1 575 ? 144.853 146.784 95.213  1.00 14.81 ?  575 ARG A CZ    1 
ATOM   4632  N  NH1   . ARG A 1 575 ? 144.146 146.206 94.258  1.00 16.91 1  575 ARG A NH1   1 
ATOM   4633  N  NH2   . ARG A 1 575 ? 146.034 146.273 95.547  1.00 10.77 ?  575 ARG A NH2   1 
ATOM   4634  N  N     . LEU A 1 576 ? 141.439 143.780 97.610  1.00 20.61 ?  576 LEU A N     1 
ATOM   4635  C  CA    . LEU A 1 576 ? 141.036 142.455 97.163  1.00 8.99  ?  576 LEU A CA    1 
ATOM   4636  C  C     . LEU A 1 576 ? 141.216 141.446 98.285  1.00 6.92  ?  576 LEU A C     1 
ATOM   4637  O  O     . LEU A 1 576 ? 142.302 141.342 98.862  1.00 16.05 ?  576 LEU A O     1 
ATOM   4638  C  CB    . LEU A 1 576 ? 141.849 142.024 95.940  1.00 4.75  ?  576 LEU A CB    1 
ATOM   4639  C  CG    . LEU A 1 576 ? 141.878 142.996 94.761  1.00 10.05 ?  576 LEU A CG    1 
ATOM   4640  C  CD1   . LEU A 1 576 ? 142.832 142.506 93.689  1.00 12.27 ?  576 LEU A CD1   1 
ATOM   4641  C  CD2   . LEU A 1 576 ? 140.487 143.186 94.191  1.00 10.86 ?  576 LEU A CD2   1 
ATOM   4642  N  N     . CYS A 1 577 ? 140.151 140.712 98.588  1.00 5.06  ?  577 CYS A N     1 
ATOM   4643  C  CA    . CYS A 1 577 ? 140.220 139.562 99.478  1.00 3.41  ?  577 CYS A CA    1 
ATOM   4644  C  C     . CYS A 1 577 ? 139.177 138.560 99.012  1.00 17.51 ?  577 CYS A C     1 
ATOM   4645  O  O     . CYS A 1 577 ? 138.043 138.941 98.713  1.00 21.24 ?  577 CYS A O     1 
ATOM   4646  C  CB    . CYS A 1 577 ? 139.994 139.962 100.944 1.00 3.50  ?  577 CYS A CB    1 
ATOM   4647  S  SG    . CYS A 1 577 ? 138.280 140.155 101.484 1.00 32.82 ?  577 CYS A SG    1 
ATOM   4648  N  N     . ILE A 1 578 ? 139.566 137.294 98.925  1.00 15.25 ?  578 ILE A N     1 
ATOM   4649  C  CA    . ILE A 1 578 ? 138.703 136.244 98.398  1.00 10.66 ?  578 ILE A CA    1 
ATOM   4650  C  C     . ILE A 1 578 ? 138.102 135.504 99.587  1.00 4.01  ?  578 ILE A C     1 
ATOM   4651  O  O     . ILE A 1 578 ? 138.752 134.665 100.213 1.00 14.86 ?  578 ILE A O     1 
ATOM   4652  C  CB    . ILE A 1 578 ? 139.459 135.308 97.454  1.00 10.51 ?  578 ILE A CB    1 
ATOM   4653  C  CG1   . ILE A 1 578 ? 140.050 136.108 96.294  1.00 0.00  ?  578 ILE A CG1   1 
ATOM   4654  C  CG2   . ILE A 1 578 ? 138.533 134.238 96.917  1.00 13.45 ?  578 ILE A CG2   1 
ATOM   4655  C  CD1   . ILE A 1 578 ? 140.699 135.264 95.241  1.00 6.95  ?  578 ILE A CD1   1 
ATOM   4656  N  N     . ALA A 1 579 ? 136.849 135.824 99.892  1.00 17.63 ?  579 ALA A N     1 
ATOM   4657  C  CA    . ALA A 1 579 ? 136.113 135.237 100.998 1.00 12.12 ?  579 ALA A CA    1 
ATOM   4658  C  C     . ALA A 1 579 ? 135.504 133.901 100.585 1.00 21.37 ?  579 ALA A C     1 
ATOM   4659  O  O     . ALA A 1 579 ? 135.476 133.556 99.404  1.00 27.27 ?  579 ALA A O     1 
ATOM   4660  C  CB    . ALA A 1 579 ? 135.036 136.214 101.461 1.00 9.65  ?  579 ALA A CB    1 
ATOM   4661  N  N     . PRO A 1 580 ? 135.033 133.103 101.551 1.00 26.58 ?  580 PRO A N     1 
ATOM   4662  C  CA    . PRO A 1 580 ? 134.387 131.828 101.189 1.00 22.98 ?  580 PRO A CA    1 
ATOM   4663  C  C     . PRO A 1 580 ? 133.153 131.973 100.310 1.00 25.85 ?  580 PRO A C     1 
ATOM   4664  O  O     . PRO A 1 580 ? 132.910 131.095 99.473  1.00 33.51 ?  580 PRO A O     1 
ATOM   4665  C  CB    . PRO A 1 580 ? 134.038 131.209 102.552 1.00 23.37 ?  580 PRO A CB    1 
ATOM   4666  C  CG    . PRO A 1 580 ? 134.266 132.282 103.565 1.00 24.80 ?  580 PRO A CG    1 
ATOM   4667  C  CD    . PRO A 1 580 ? 135.294 133.185 102.996 1.00 21.17 ?  580 PRO A CD    1 
ATOM   4668  N  N     . THR A 1 581 ? 132.375 133.046 100.464 1.00 22.49 ?  581 THR A N     1 
ATOM   4669  C  CA    . THR A 1 581 ? 131.149 133.276 99.690  1.00 33.36 ?  581 THR A CA    1 
ATOM   4670  C  C     . THR A 1 581 ? 130.212 132.067 99.766  1.00 31.70 ?  581 THR A C     1 
ATOM   4671  O  O     . THR A 1 581 ? 129.924 131.396 98.776  1.00 32.03 ?  581 THR A O     1 
ATOM   4672  C  CB    . THR A 1 581 ? 131.455 133.625 98.228  1.00 32.67 ?  581 THR A CB    1 
ATOM   4673  O  OG1   . THR A 1 581 ? 131.548 132.422 97.454  1.00 26.83 ?  581 THR A OG1   1 
ATOM   4674  C  CG2   . THR A 1 581 ? 132.745 134.416 98.108  1.00 30.85 ?  581 THR A CG2   1 
ATOM   4675  N  N     . GLY A 1 582 ? 129.743 131.811 100.984 1.00 35.50 ?  582 GLY A N     1 
ATOM   4676  C  CA    . GLY A 1 582 ? 129.001 130.598 101.270 1.00 32.59 ?  582 GLY A CA    1 
ATOM   4677  C  C     . GLY A 1 582 ? 127.653 130.455 100.591 1.00 35.28 ?  582 GLY A C     1 
ATOM   4678  O  O     . GLY A 1 582 ? 127.482 129.580 99.737  1.00 37.33 ?  582 GLY A O     1 
ATOM   4679  N  N     . SER A 1 583 ? 126.688 131.303 100.947 1.00 37.73 ?  583 SER A N     1 
ATOM   4680  C  CA    . SER A 1 583 ? 125.318 131.115 100.487 1.00 38.50 ?  583 SER A CA    1 
ATOM   4681  C  C     . SER A 1 583 ? 124.974 131.917 99.240  1.00 36.64 ?  583 SER A C     1 
ATOM   4682  O  O     . SER A 1 583 ? 124.027 131.556 98.534  1.00 38.67 ?  583 SER A O     1 
ATOM   4683  C  CB    . SER A 1 583 ? 124.332 131.479 101.602 1.00 42.09 ?  583 SER A CB    1 
ATOM   4684  O  OG    . SER A 1 583 ? 123.072 130.869 101.386 1.00 39.94 ?  583 SER A OG    1 
ATOM   4685  N  N     . ILE A 1 584 ? 125.710 132.993 98.951  1.00 33.14 ?  584 ILE A N     1 
ATOM   4686  C  CA    . ILE A 1 584 ? 125.443 133.756 97.738  1.00 31.28 ?  584 ILE A CA    1 
ATOM   4687  C  C     . ILE A 1 584 ? 125.881 133.002 96.492  1.00 33.16 ?  584 ILE A C     1 
ATOM   4688  O  O     . ILE A 1 584 ? 125.514 133.388 95.377  1.00 40.10 ?  584 ILE A O     1 
ATOM   4689  C  CB    . ILE A 1 584 ? 126.125 135.136 97.800  1.00 34.85 ?  584 ILE A CB    1 
ATOM   4690  C  CG1   . ILE A 1 584 ? 127.607 134.986 98.148  1.00 34.66 ?  584 ILE A CG1   1 
ATOM   4691  C  CG2   . ILE A 1 584 ? 125.416 136.039 98.795  1.00 33.01 ?  584 ILE A CG2   1 
ATOM   4692  C  CD1   . ILE A 1 584 ? 128.382 136.284 98.096  1.00 33.24 ?  584 ILE A CD1   1 
ATOM   4693  N  N     . SER A 1 585 ? 126.666 131.934 96.650  1.00 32.18 ?  585 SER A N     1 
ATOM   4694  C  CA    . SER A 1 585 ? 127.079 131.141 95.499  1.00 29.46 ?  585 SER A CA    1 
ATOM   4695  C  C     . SER A 1 585 ? 125.904 130.399 94.878  1.00 31.36 ?  585 SER A C     1 
ATOM   4696  O  O     . SER A 1 585 ? 125.870 130.208 93.658  1.00 33.66 ?  585 SER A O     1 
ATOM   4697  C  CB    . SER A 1 585 ? 128.177 130.161 95.907  1.00 29.82 ?  585 SER A CB    1 
ATOM   4698  O  OG    . SER A 1 585 ? 127.780 129.389 97.027  1.00 35.57 ?  585 SER A OG    1 
ATOM   4699  N  N     . TYR A 1 586 ? 124.942 129.965 95.695  1.00 31.83 ?  586 TYR A N     1 
ATOM   4700  C  CA    . TYR A 1 586 ? 123.737 129.347 95.154  1.00 33.16 ?  586 TYR A CA    1 
ATOM   4701  C  C     . TYR A 1 586 ? 122.931 130.348 94.339  1.00 32.37 ?  586 TYR A C     1 
ATOM   4702  O  O     . TYR A 1 586 ? 122.516 130.055 93.213  1.00 39.34 ?  586 TYR A O     1 
ATOM   4703  C  CB    . TYR A 1 586 ? 122.882 128.778 96.284  1.00 33.29 ?  586 TYR A CB    1 
ATOM   4704  C  CG    . TYR A 1 586 ? 123.540 127.680 97.080  1.00 34.35 ?  586 TYR A CG    1 
ATOM   4705  C  CD1   . TYR A 1 586 ? 123.518 126.367 96.636  1.00 35.32 ?  586 TYR A CD1   1 
ATOM   4706  C  CD2   . TYR A 1 586 ? 124.174 127.954 98.283  1.00 31.34 ?  586 TYR A CD2   1 
ATOM   4707  C  CE1   . TYR A 1 586 ? 124.114 125.360 97.363  1.00 36.39 ?  586 TYR A CE1   1 
ATOM   4708  C  CE2   . TYR A 1 586 ? 124.773 126.954 99.017  1.00 33.62 ?  586 TYR A CE2   1 
ATOM   4709  C  CZ    . TYR A 1 586 ? 124.741 125.658 98.552  1.00 37.41 ?  586 TYR A CZ    1 
ATOM   4710  O  OH    . TYR A 1 586 ? 125.337 124.657 99.282  1.00 40.64 ?  586 TYR A OH    1 
ATOM   4711  N  N     . VAL A 1 587 ? 122.713 131.543 94.894  1.00 29.24 ?  587 VAL A N     1 
ATOM   4712  C  CA    . VAL A 1 587 ? 121.910 132.561 94.223  1.00 27.25 ?  587 VAL A CA    1 
ATOM   4713  C  C     . VAL A 1 587 ? 122.532 132.934 92.885  1.00 30.87 ?  587 VAL A C     1 
ATOM   4714  O  O     . VAL A 1 587 ? 121.831 133.087 91.877  1.00 33.39 ?  587 VAL A O     1 
ATOM   4715  C  CB    . VAL A 1 587 ? 121.747 133.790 95.137  1.00 29.69 ?  587 VAL A CB    1 
ATOM   4716  C  CG1   . VAL A 1 587 ? 121.093 134.935 94.386  1.00 30.93 ?  587 VAL A CG1   1 
ATOM   4717  C  CG2   . VAL A 1 587 ? 120.945 133.425 96.372  1.00 31.47 ?  587 VAL A CG2   1 
ATOM   4718  N  N     . GLN A 1 588 ? 123.852 133.080 92.851  1.00 32.92 ?  588 GLN A N     1 
ATOM   4719  C  CA    . GLN A 1 588 ? 124.559 133.419 91.626  1.00 29.21 ?  588 GLN A CA    1 
ATOM   4720  C  C     . GLN A 1 588 ? 124.793 132.215 90.727  1.00 28.76 ?  588 GLN A C     1 
ATOM   4721  O  O     . GLN A 1 588 ? 125.338 132.383 89.632  1.00 31.83 ?  588 GLN A O     1 
ATOM   4722  C  CB    . GLN A 1 588 ? 125.900 134.074 91.959  1.00 26.58 ?  588 GLN A CB    1 
ATOM   4723  C  CG    . GLN A 1 588 ? 125.785 135.490 92.481  1.00 24.83 ?  588 GLN A CG    1 
ATOM   4724  C  CD    . GLN A 1 588 ? 125.958 136.522 91.391  1.00 27.77 ?  588 GLN A CD    1 
ATOM   4725  O  OE1   . GLN A 1 588 ? 126.799 136.371 90.508  1.00 29.67 ?  588 GLN A OE1   1 
ATOM   4726  N  NE2   . GLN A 1 588 ? 125.166 137.584 91.448  1.00 29.68 ?  588 GLN A NE2   1 
ATOM   4727  N  N     . SER A 1 589 ? 124.392 131.021 91.162  1.00 32.59 ?  589 SER A N     1 
ATOM   4728  C  CA    . SER A 1 589 ? 124.632 129.779 90.434  1.00 29.72 ?  589 SER A CA    1 
ATOM   4729  C  C     . SER A 1 589 ? 126.116 129.643 90.100  1.00 32.19 ?  589 SER A C     1 
ATOM   4730  O  O     . SER A 1 589 ? 126.526 129.557 88.941  1.00 30.48 ?  589 SER A O     1 
ATOM   4731  C  CB    . SER A 1 589 ? 123.763 129.700 89.178  1.00 30.42 ?  589 SER A CB    1 
ATOM   4732  O  OG    . SER A 1 589 ? 123.466 128.353 88.853  1.00 40.48 ?  589 SER A OG    1 
ATOM   4733  N  N     . SER A 1 590 ? 126.922 129.637 91.156  1.00 33.30 ?  590 SER A N     1 
ATOM   4734  C  CA    . SER A 1 590 ? 128.368 129.671 91.029  1.00 26.43 ?  590 SER A CA    1 
ATOM   4735  C  C     . SER A 1 590 ? 128.990 128.741 92.058  1.00 27.25 ?  590 SER A C     1 
ATOM   4736  O  O     . SER A 1 590 ? 128.405 128.474 93.109  1.00 31.48 ?  590 SER A O     1 
ATOM   4737  C  CB    . SER A 1 590 ? 128.906 131.094 91.214  1.00 23.21 ?  590 SER A CB    1 
ATOM   4738  O  OG    . SER A 1 590 ? 129.334 131.306 92.545  1.00 32.45 ?  590 SER A OG    1 
ATOM   4739  N  N     . THR A 1 591 ? 130.180 128.242 91.739  1.00 27.43 ?  591 THR A N     1 
ATOM   4740  C  CA    . THR A 1 591 ? 130.948 127.484 92.714  1.00 22.38 ?  591 THR A CA    1 
ATOM   4741  C  C     . THR A 1 591 ? 131.496 128.420 93.784  1.00 27.07 ?  591 THR A C     1 
ATOM   4742  O  O     . THR A 1 591 ? 131.772 129.596 93.532  1.00 25.19 ?  591 THR A O     1 
ATOM   4743  C  CB    . THR A 1 591 ? 132.087 126.724 92.035  1.00 25.20 ?  591 THR A CB    1 
ATOM   4744  O  OG1   . THR A 1 591 ? 133.065 127.650 91.552  1.00 33.06 ?  591 THR A OG1   1 
ATOM   4745  C  CG2   . THR A 1 591 ? 131.556 125.910 90.871  1.00 25.62 ?  591 THR A CG2   1 
ATOM   4746  N  N     . ALA A 1 592 ? 131.648 127.889 94.993  1.00 26.79 ?  592 ALA A N     1 
ATOM   4747  C  CA    . ALA A 1 592 ? 132.003 128.715 96.138  1.00 24.60 ?  592 ALA A CA    1 
ATOM   4748  C  C     . ALA A 1 592 ? 133.450 129.178 96.033  1.00 28.69 ?  592 ALA A C     1 
ATOM   4749  O  O     . ALA A 1 592 ? 134.373 128.355 96.013  1.00 31.31 ?  592 ALA A O     1 
ATOM   4750  C  CB    . ALA A 1 592 ? 131.783 127.942 97.434  1.00 28.80 ?  592 ALA A CB    1 
ATOM   4751  N  N     . SER A 1 593 ? 133.641 130.492 95.963  1.00 27.10 ?  593 SER A N     1 
ATOM   4752  C  CA    . SER A 1 593 ? 134.959 131.136 96.010  1.00 11.59 ?  593 SER A CA    1 
ATOM   4753  C  C     . SER A 1 593 ? 135.807 130.622 94.842  1.00 13.13 ?  593 SER A C     1 
ATOM   4754  O  O     . SER A 1 593 ? 135.274 130.198 93.809  1.00 27.44 ?  593 SER A O     1 
ATOM   4755  C  CB    . SER A 1 593 ? 135.571 130.919 97.382  1.00 28.10 ?  593 SER A CB    1 
ATOM   4756  O  OG    . SER A 1 593 ? 136.771 131.652 97.537  1.00 29.10 ?  593 SER A OG    1 
ATOM   4757  N  N     . VAL A 1 594 ? 137.131 130.667 94.992  1.00 23.32 ?  594 VAL A N     1 
ATOM   4758  C  CA    . VAL A 1 594 ? 138.046 130.119 93.998  1.00 19.82 ?  594 VAL A CA    1 
ATOM   4759  C  C     . VAL A 1 594 ? 138.469 128.699 94.330  1.00 14.86 ?  594 VAL A C     1 
ATOM   4760  O  O     . VAL A 1 594 ? 139.312 128.129 93.626  1.00 17.59 ?  594 VAL A O     1 
ATOM   4761  C  CB    . VAL A 1 594 ? 139.282 131.027 93.834  1.00 18.67 ?  594 VAL A CB    1 
ATOM   4762  C  CG1   . VAL A 1 594 ? 138.885 132.345 93.193  1.00 11.94 ?  594 VAL A CG1   1 
ATOM   4763  C  CG2   . VAL A 1 594 ? 139.947 131.268 95.176  1.00 18.42 ?  594 VAL A CG2   1 
ATOM   4764  N  N     . MET A 1 595 ? 137.908 128.112 95.383  1.00 22.05 ?  595 MET A N     1 
ATOM   4765  C  CA    . MET A 1 595 ? 138.214 126.740 95.743  1.00 20.53 ?  595 MET A CA    1 
ATOM   4766  C  C     . MET A 1 595 ? 137.493 125.765 94.815  1.00 23.58 ?  595 MET A C     1 
ATOM   4767  O  O     . MET A 1 595 ? 136.453 126.095 94.239  1.00 25.01 ?  595 MET A O     1 
ATOM   4768  C  CB    . MET A 1 595 ? 137.815 126.474 97.194  1.00 22.89 ?  595 MET A CB    1 
ATOM   4769  C  CG    . MET A 1 595 ? 138.982 126.306 98.169  1.00 21.47 ?  595 MET A CG    1 
ATOM   4770  S  SD    . MET A 1 595 ? 140.427 127.345 97.866  1.00 30.92 ?  595 MET A SD    1 
ATOM   4771  C  CE    . MET A 1 595 ? 139.737 128.991 97.993  1.00 31.89 ?  595 MET A CE    1 
ATOM   4772  N  N     . PRO A 1 596 ? 138.034 124.562 94.643  1.00 30.79 ?  596 PRO A N     1 
ATOM   4773  C  CA    . PRO A 1 596 ? 137.345 123.551 93.837  1.00 20.09 ?  596 PRO A CA    1 
ATOM   4774  C  C     . PRO A 1 596 ? 136.103 123.023 94.538  1.00 25.96 ?  596 PRO A C     1 
ATOM   4775  O  O     . PRO A 1 596 ? 135.946 123.121 95.756  1.00 30.13 ?  596 PRO A O     1 
ATOM   4776  C  CB    . PRO A 1 596 ? 138.397 122.452 93.668  1.00 23.39 ?  596 PRO A CB    1 
ATOM   4777  C  CG    . PRO A 1 596 ? 139.303 122.622 94.836  1.00 29.22 ?  596 PRO A CG    1 
ATOM   4778  C  CD    . PRO A 1 596 ? 139.344 124.089 95.123  1.00 28.42 ?  596 PRO A CD    1 
ATOM   4779  N  N     . ILE A 1 597 ? 135.206 122.452 93.731  1.00 27.79 ?  597 ILE A N     1 
ATOM   4780  C  CA    . ILE A 1 597 ? 133.943 121.946 94.249  1.00 30.69 ?  597 ILE A CA    1 
ATOM   4781  C  C     . ILE A 1 597 ? 134.184 120.719 95.119  1.00 31.57 ?  597 ILE A C     1 
ATOM   4782  O  O     . ILE A 1 597 ? 135.124 119.943 94.902  1.00 31.34 ?  597 ILE A O     1 
ATOM   4783  C  CB    . ILE A 1 597 ? 132.975 121.624 93.096  1.00 31.28 ?  597 ILE A CB    1 
ATOM   4784  C  CG1   . ILE A 1 597 ? 133.476 120.417 92.299  1.00 27.57 ?  597 ILE A CG1   1 
ATOM   4785  C  CG2   . ILE A 1 597 ? 132.812 122.824 92.194  1.00 29.49 ?  597 ILE A CG2   1 
ATOM   4786  C  CD1   . ILE A 1 597 ? 132.380 119.571 91.714  1.00 28.63 ?  597 ILE A CD1   1 
ATOM   4787  N  N     . MET A 1 598 ? 133.321 120.538 96.116  1.00 40.39 ?  598 MET A N     1 
ATOM   4788  C  CA    . MET A 1 598 ? 133.395 119.378 96.993  1.00 41.34 ?  598 MET A CA    1 
ATOM   4789  C  C     . MET A 1 598 ? 132.597 118.198 96.454  1.00 40.72 ?  598 MET A C     1 
ATOM   4790  O  O     . MET A 1 598 ? 133.079 117.061 96.481  1.00 44.88 ?  598 MET A O     1 
ATOM   4791  C  CB    . MET A 1 598 ? 132.901 119.746 98.393  1.00 42.03 ?  598 MET A CB    1 
ATOM   4792  C  CG    . MET A 1 598 ? 133.390 121.096 98.884  1.00 39.71 ?  598 MET A CG    1 
ATOM   4793  S  SD    . MET A 1 598 ? 133.277 121.283 100.672 1.00 57.19 ?  598 MET A SD    1 
ATOM   4794  C  CE    . MET A 1 598 ? 131.997 120.093 101.064 1.00 44.70 ?  598 MET A CE    1 
ATOM   4795  N  N     . GLU A 1 599 ? 131.382 118.446 95.968  1.00 41.01 ?  599 GLU A N     1 
ATOM   4796  C  CA    . GLU A 1 599 ? 130.532 117.418 95.387  1.00 39.32 ?  599 GLU A CA    1 
ATOM   4797  C  C     . GLU A 1 599 ? 130.042 117.884 94.026  1.00 38.14 ?  599 GLU A C     1 
ATOM   4798  O  O     . GLU A 1 599 ? 129.727 119.062 93.845  1.00 42.33 ?  599 GLU A O     1 
ATOM   4799  C  CB    . GLU A 1 599 ? 129.329 117.104 96.287  1.00 42.81 ?  599 GLU A CB    1 
ATOM   4800  C  CG    . GLU A 1 599 ? 129.618 117.187 97.775  1.00 44.35 ?  599 GLU A CG    1 
ATOM   4801  C  CD    . GLU A 1 599 ? 128.358 117.139 98.619  1.00 48.19 ?  599 GLU A CD    1 
ATOM   4802  O  OE1   . GLU A 1 599 ? 127.752 116.054 98.724  1.00 47.76 ?  599 GLU A OE1   1 
ATOM   4803  O  OE2   . GLU A 1 599 ? 127.978 118.188 99.180  1.00 45.85 -1 599 GLU A OE2   1 
ATOM   4804  N  N     . ARG A 1 600 ? 129.986 116.957 93.067  1.00 41.41 ?  600 ARG A N     1 
ATOM   4805  C  CA    . ARG A 1 600 ? 129.431 117.287 91.759  1.00 36.75 ?  600 ARG A CA    1 
ATOM   4806  C  C     . ARG A 1 600 ? 127.940 117.583 91.862  1.00 37.88 ?  600 ARG A C     1 
ATOM   4807  O  O     . ARG A 1 600 ? 127.457 118.592 91.338  1.00 41.00 ?  600 ARG A O     1 
ATOM   4808  C  CB    . ARG A 1 600 ? 129.685 116.149 90.774  1.00 36.61 ?  600 ARG A CB    1 
ATOM   4809  C  CG    . ARG A 1 600 ? 131.077 116.142 90.183  1.00 36.23 ?  600 ARG A CG    1 
ATOM   4810  C  CD    . ARG A 1 600 ? 131.168 115.167 89.032  1.00 36.48 ?  600 ARG A CD    1 
ATOM   4811  N  NE    . ARG A 1 600 ? 132.540 114.956 88.588  1.00 35.63 ?  600 ARG A NE    1 
ATOM   4812  C  CZ    . ARG A 1 600 ? 133.389 114.114 89.160  1.00 38.66 ?  600 ARG A CZ    1 
ATOM   4813  N  NH1   . ARG A 1 600 ? 133.045 113.400 90.218  1.00 37.64 1  600 ARG A NH1   1 
ATOM   4814  N  NH2   . ARG A 1 600 ? 134.613 113.987 88.657  1.00 39.46 ?  600 ARG A NH2   1 
ATOM   4815  N  N     . ILE A 1 601 ? 127.198 116.707 92.530  1.00 45.37 ?  601 ILE A N     1 
ATOM   4816  C  CA    . ILE A 1 601 ? 125.793 116.927 92.847  1.00 43.26 ?  601 ILE A CA    1 
ATOM   4817  C  C     . ILE A 1 601 ? 125.684 116.981 94.362  1.00 42.50 ?  601 ILE A C     1 
ATOM   4818  O  O     . ILE A 1 601 ? 126.031 116.013 95.049  1.00 46.73 ?  601 ILE A O     1 
ATOM   4819  C  CB    . ILE A 1 601 ? 124.888 115.832 92.263  1.00 42.87 ?  601 ILE A CB    1 
ATOM   4820  C  CG1   . ILE A 1 601 ? 125.215 115.606 90.786  1.00 43.32 ?  601 ILE A CG1   1 
ATOM   4821  C  CG2   . ILE A 1 601 ? 123.426 116.212 92.429  1.00 42.85 ?  601 ILE A CG2   1 
ATOM   4822  C  CD1   . ILE A 1 601 ? 124.397 114.521 90.137  1.00 43.38 ?  601 ILE A CD1   1 
ATOM   4823  N  N     . GLU A 1 602 ? 125.205 118.104 94.879  1.00 49.62 ?  602 GLU A N     1 
ATOM   4824  C  CA    . GLU A 1 602 ? 125.191 118.365 96.310  1.00 49.44 ?  602 GLU A CA    1 
ATOM   4825  C  C     . GLU A 1 602 ? 123.813 118.030 96.866  1.00 51.45 ?  602 GLU A C     1 
ATOM   4826  O  O     . GLU A 1 602 ? 122.808 118.611 96.443  1.00 53.93 ?  602 GLU A O     1 
ATOM   4827  C  CB    . GLU A 1 602 ? 125.559 119.821 96.590  1.00 49.41 ?  602 GLU A CB    1 
ATOM   4828  C  CG    . GLU A 1 602 ? 125.108 120.339 97.937  1.00 50.26 ?  602 GLU A CG    1 
ATOM   4829  C  CD    . GLU A 1 602 ? 125.322 121.831 98.077  1.00 54.59 ?  602 GLU A CD    1 
ATOM   4830  O  OE1   . GLU A 1 602 ? 126.290 122.351 97.483  1.00 52.32 ?  602 GLU A OE1   1 
ATOM   4831  O  OE2   . GLU A 1 602 ? 124.525 122.484 98.782  1.00 56.03 -1 602 GLU A OE2   1 
ATOM   4832  N  N     . GLU A 1 603 ? 123.770 117.090 97.805  1.00 56.98 ?  603 GLU A N     1 
ATOM   4833  C  CA    . GLU A 1 603 ? 122.528 116.636 98.414  1.00 57.36 ?  603 GLU A CA    1 
ATOM   4834  C  C     . GLU A 1 603 ? 122.349 117.314 99.765  1.00 58.62 ?  603 GLU A C     1 
ATOM   4835  O  O     . GLU A 1 603 ? 123.240 117.255 100.618 1.00 58.60 ?  603 GLU A O     1 
ATOM   4836  C  CB    . GLU A 1 603 ? 122.530 115.116 98.580  1.00 59.38 ?  603 GLU A CB    1 
ATOM   4837  C  CG    . GLU A 1 603 ? 121.262 114.552 99.194  1.00 60.68 ?  603 GLU A CG    1 
ATOM   4838  C  CD    . GLU A 1 603 ? 121.414 113.102 99.615  1.00 61.55 ?  603 GLU A CD    1 
ATOM   4839  O  OE1   . GLU A 1 603 ? 121.442 112.222 98.729  1.00 60.08 ?  603 GLU A OE1   1 
ATOM   4840  O  OE2   . GLU A 1 603 ? 121.506 112.841 100.833 1.00 59.52 -1 603 GLU A OE2   1 
ATOM   4841  N  N     . ARG A 1 604 ? 121.199 117.955 99.955  1.00 61.77 ?  604 ARG A N     1 
ATOM   4842  C  CA    . ARG A 1 604 ? 120.890 118.663 101.187 1.00 61.85 ?  604 ARG A CA    1 
ATOM   4843  C  C     . ARG A 1 604 ? 119.487 118.305 101.646 1.00 62.69 ?  604 ARG A C     1 
ATOM   4844  O  O     . ARG A 1 604 ? 118.630 117.924 100.845 1.00 64.24 ?  604 ARG A O     1 
ATOM   4845  C  CB    . ARG A 1 604 ? 120.997 120.184 101.009 1.00 59.98 ?  604 ARG A CB    1 
ATOM   4846  C  CG    . ARG A 1 604 ? 122.377 120.684 100.620 1.00 61.07 ?  604 ARG A CG    1 
ATOM   4847  C  CD    . ARG A 1 604 ? 123.356 120.557 101.773 1.00 62.30 ?  604 ARG A CD    1 
ATOM   4848  N  NE    . ARG A 1 604 ? 124.372 119.542 101.518 1.00 63.37 ?  604 ARG A NE    1 
ATOM   4849  C  CZ    . ARG A 1 604 ? 125.652 119.806 101.294 1.00 62.57 ?  604 ARG A CZ    1 
ATOM   4850  N  NH1   . ARG A 1 604 ? 126.111 121.046 101.290 1.00 61.28 1  604 ARG A NH1   1 
ATOM   4851  N  NH2   . ARG A 1 604 ? 126.491 118.801 101.067 1.00 60.05 ?  604 ARG A NH2   1 
ATOM   4852  N  N     . THR A 1 605 ? 119.260 118.430 102.951 1.00 68.82 ?  605 THR A N     1 
ATOM   4853  C  CA    . THR A 1 605 ? 117.947 118.222 103.549 1.00 70.06 ?  605 THR A CA    1 
ATOM   4854  C  C     . THR A 1 605 ? 117.515 119.516 104.223 1.00 69.42 ?  605 THR A C     1 
ATOM   4855  O  O     . THR A 1 605 ? 118.173 119.980 105.160 1.00 69.58 ?  605 THR A O     1 
ATOM   4856  C  CB    . THR A 1 605 ? 117.971 117.072 104.559 1.00 70.54 ?  605 THR A CB    1 
ATOM   4857  O  OG1   . THR A 1 605 ? 118.891 116.066 104.119 1.00 71.33 ?  605 THR A OG1   1 
ATOM   4858  C  CG2   . THR A 1 605 ? 116.588 116.458 104.694 1.00 69.20 ?  605 THR A CG2   1 
ATOM   4859  N  N     . TYR A 1 606 ? 116.416 120.093 103.749 1.00 68.76 ?  606 TYR A N     1 
ATOM   4860  C  CA    . TYR A 1 606 ? 115.857 121.319 104.308 1.00 71.10 ?  606 TYR A CA    1 
ATOM   4861  C  C     . TYR A 1 606 ? 114.536 120.964 104.977 1.00 72.93 ?  606 TYR A C     1 
ATOM   4862  O  O     . TYR A 1 606 ? 113.566 120.607 104.298 1.00 70.59 ?  606 TYR A O     1 
ATOM   4863  C  CB    . TYR A 1 606 ? 115.672 122.380 103.226 1.00 69.38 ?  606 TYR A CB    1 
ATOM   4864  C  CG    . TYR A 1 606 ? 116.974 122.879 102.645 1.00 70.30 ?  606 TYR A CG    1 
ATOM   4865  C  CD1   . TYR A 1 606 ? 117.734 123.835 103.308 1.00 68.23 ?  606 TYR A CD1   1 
ATOM   4866  C  CD2   . TYR A 1 606 ? 117.450 122.389 101.438 1.00 69.45 ?  606 TYR A CD2   1 
ATOM   4867  C  CE1   . TYR A 1 606 ? 118.928 124.289 102.781 1.00 68.83 ?  606 TYR A CE1   1 
ATOM   4868  C  CE2   . TYR A 1 606 ? 118.640 122.837 100.903 1.00 67.17 ?  606 TYR A CE2   1 
ATOM   4869  C  CZ    . TYR A 1 606 ? 119.375 123.785 101.578 1.00 70.11 ?  606 TYR A CZ    1 
ATOM   4870  O  OH    . TYR A 1 606 ? 120.562 124.232 101.046 1.00 70.97 ?  606 TYR A OH    1 
ATOM   4871  N  N     . GLY A 1 607 ? 114.497 121.068 106.299 1.00 80.04 ?  607 GLY A N     1 
ATOM   4872  C  CA    . GLY A 1 607 ? 113.334 120.602 107.034 1.00 78.48 ?  607 GLY A CA    1 
ATOM   4873  C  C     . GLY A 1 607 ? 113.181 119.104 106.860 1.00 78.34 ?  607 GLY A C     1 
ATOM   4874  O  O     . GLY A 1 607 ? 114.116 118.329 107.097 1.00 78.36 ?  607 GLY A O     1 
ATOM   4875  N  N     . ASN A 1 608 ? 111.992 118.677 106.436 1.00 79.97 ?  608 ASN A N     1 
ATOM   4876  C  CA    . ASN A 1 608 ? 111.718 117.276 106.145 1.00 81.03 ?  608 ASN A CA    1 
ATOM   4877  C  C     . ASN A 1 608 ? 111.732 116.988 104.648 1.00 80.88 ?  608 ASN A C     1 
ATOM   4878  O  O     . ASN A 1 608 ? 111.110 116.023 104.192 1.00 80.73 ?  608 ASN A O     1 
ATOM   4879  C  CB    . ASN A 1 608 ? 110.380 116.858 106.757 1.00 80.47 ?  608 ASN A CB    1 
ATOM   4880  C  CG    . ASN A 1 608 ? 110.357 117.010 108.267 1.00 81.27 ?  608 ASN A CG    1 
ATOM   4881  O  OD1   . ASN A 1 608 ? 111.400 117.149 108.906 1.00 80.58 ?  608 ASN A OD1   1 
ATOM   4882  N  ND2   . ASN A 1 608 ? 109.162 116.981 108.845 1.00 80.54 ?  608 ASN A ND2   1 
ATOM   4883  N  N     . SER A 1 609 ? 112.436 117.810 103.875 1.00 77.90 ?  609 SER A N     1 
ATOM   4884  C  CA    . SER A 1 609 ? 112.509 117.676 102.427 1.00 77.94 ?  609 SER A CA    1 
ATOM   4885  C  C     . SER A 1 609 ? 113.960 117.511 101.999 1.00 77.93 ?  609 SER A C     1 
ATOM   4886  O  O     . SER A 1 609 ? 114.845 118.221 102.486 1.00 78.15 ?  609 SER A O     1 
ATOM   4887  C  CB    . SER A 1 609 ? 111.896 118.893 101.731 1.00 76.58 ?  609 SER A CB    1 
ATOM   4888  O  OG    . SER A 1 609 ? 112.608 120.076 102.052 1.00 77.68 ?  609 SER A OG    1 
ATOM   4889  N  N     . LYS A 1 610 ? 114.196 116.578 101.082 1.00 66.97 ?  610 LYS A N     1 
ATOM   4890  C  CA    . LYS A 1 610 ? 115.525 116.303 100.555 1.00 66.32 ?  610 LYS A CA    1 
ATOM   4891  C  C     . LYS A 1 610 ? 115.603 116.787 99.115  1.00 66.53 ?  610 LYS A C     1 
ATOM   4892  O  O     . LYS A 1 610 ? 114.748 116.444 98.292  1.00 67.67 ?  610 LYS A O     1 
ATOM   4893  C  CB    . LYS A 1 610 ? 115.847 114.810 100.635 1.00 66.92 ?  610 LYS A CB    1 
ATOM   4894  C  CG    . LYS A 1 610 ? 116.860 114.332 99.608  1.00 66.39 ?  610 LYS A CG    1 
ATOM   4895  C  CD    . LYS A 1 610 ? 117.548 113.056 100.064 1.00 66.95 ?  610 LYS A CD    1 
ATOM   4896  C  CE    . LYS A 1 610 ? 118.060 113.176 101.491 1.00 66.22 ?  610 LYS A CE    1 
ATOM   4897  N  NZ    . LYS A 1 610 ? 119.013 114.308 101.644 1.00 66.39 1  610 LYS A NZ    1 
ATOM   4898  N  N     . THR A 1 611 ? 116.626 117.583 98.814  1.00 64.78 ?  611 THR A N     1 
ATOM   4899  C  CA    . THR A 1 611 ? 116.797 118.164 97.491  1.00 63.63 ?  611 THR A CA    1 
ATOM   4900  C  C     . THR A 1 611 ? 118.262 118.088 97.092  1.00 62.02 ?  611 THR A C     1 
ATOM   4901  O  O     . THR A 1 611 ? 119.153 118.072 97.943  1.00 61.18 ?  611 THR A O     1 
ATOM   4902  C  CB    . THR A 1 611 ? 116.314 119.618 97.449  1.00 64.51 ?  611 THR A CB    1 
ATOM   4903  O  OG1   . THR A 1 611 ? 116.706 120.215 96.207  1.00 68.33 ?  611 THR A OG1   1 
ATOM   4904  C  CG2   . THR A 1 611 ? 116.908 120.405 98.602  1.00 61.51 ?  611 THR A CG2   1 
ATOM   4905  N  N     . TYR A 1 612 ? 118.503 118.043 95.784  1.00 55.17 ?  612 TYR A N     1 
ATOM   4906  C  CA    . TYR A 1 612 ? 119.839 117.861 95.240  1.00 53.75 ?  612 TYR A CA    1 
ATOM   4907  C  C     . TYR A 1 612 ? 120.219 119.056 94.380  1.00 55.99 ?  612 TYR A C     1 
ATOM   4908  O  O     . TYR A 1 612 ? 119.396 119.577 93.621  1.00 55.12 ?  612 TYR A O     1 
ATOM   4909  C  CB    . TYR A 1 612 ? 119.950 116.572 94.410  1.00 56.44 ?  612 TYR A CB    1 
ATOM   4910  C  CG    . TYR A 1 612 ? 119.502 115.310 95.120  1.00 58.31 ?  612 TYR A CG    1 
ATOM   4911  C  CD1   . TYR A 1 612 ? 118.168 115.102 95.452  1.00 57.73 ?  612 TYR A CD1   1 
ATOM   4912  C  CD2   . TYR A 1 612 ? 120.422 114.337 95.482  1.00 57.67 ?  612 TYR A CD2   1 
ATOM   4913  C  CE1   . TYR A 1 612 ? 117.763 113.955 96.102  1.00 58.44 ?  612 TYR A CE1   1 
ATOM   4914  C  CE2   . TYR A 1 612 ? 120.026 113.186 96.134  1.00 58.52 ?  612 TYR A CE2   1 
ATOM   4915  C  CZ    . TYR A 1 612 ? 118.696 113.002 96.442  1.00 60.23 ?  612 TYR A CZ    1 
ATOM   4916  O  OH    . TYR A 1 612 ? 118.298 111.856 97.093  1.00 60.85 ?  612 TYR A OH    1 
ATOM   4917  N  N     . TYR A 1 613 ? 121.472 119.485 94.503  1.00 51.49 ?  613 TYR A N     1 
ATOM   4918  C  CA    . TYR A 1 613 ? 121.995 120.631 93.761  1.00 42.49 ?  613 TYR A CA    1 
ATOM   4919  C  C     . TYR A 1 613 ? 123.178 120.216 92.902  1.00 41.14 ?  613 TYR A C     1 
ATOM   4920  O  O     . TYR A 1 613 ? 124.304 120.085 93.414  1.00 44.64 ?  613 TYR A O     1 
ATOM   4921  C  CB    . TYR A 1 613 ? 122.403 121.753 94.714  1.00 41.40 ?  613 TYR A CB    1 
ATOM   4922  C  CG    . TYR A 1 613 ? 122.973 122.964 94.014  1.00 41.89 ?  613 TYR A CG    1 
ATOM   4923  C  CD1   . TYR A 1 613 ? 122.322 123.535 92.931  1.00 42.79 ?  613 TYR A CD1   1 
ATOM   4924  C  CD2   . TYR A 1 613 ? 124.164 123.536 94.437  1.00 42.04 ?  613 TYR A CD2   1 
ATOM   4925  C  CE1   . TYR A 1 613 ? 122.836 124.642 92.291  1.00 43.12 ?  613 TYR A CE1   1 
ATOM   4926  C  CE2   . TYR A 1 613 ? 124.689 124.643 93.802  1.00 43.78 ?  613 TYR A CE2   1 
ATOM   4927  C  CZ    . TYR A 1 613 ? 124.020 125.193 92.731  1.00 46.61 ?  613 TYR A CZ    1 
ATOM   4928  O  OH    . TYR A 1 613 ? 124.537 126.296 92.095  1.00 46.20 ?  613 TYR A OH    1 
ATOM   4929  N  N     . PRO A 1 614 ? 122.984 119.994 91.607  1.00 40.55 ?  614 PRO A N     1 
ATOM   4930  C  CA    . PRO A 1 614 ? 124.134 119.801 90.720  1.00 40.16 ?  614 PRO A CA    1 
ATOM   4931  C  C     . PRO A 1 614 ? 124.957 121.074 90.631  1.00 40.09 ?  614 PRO A C     1 
ATOM   4932  O  O     . PRO A 1 614 ? 124.443 122.186 90.778  1.00 43.40 ?  614 PRO A O     1 
ATOM   4933  C  CB    . PRO A 1 614 ? 123.498 119.453 89.368  1.00 37.04 ?  614 PRO A CB    1 
ATOM   4934  C  CG    . PRO A 1 614 ? 122.056 119.170 89.660  1.00 43.01 ?  614 PRO A CG    1 
ATOM   4935  C  CD    . PRO A 1 614 ? 121.709 119.958 90.875  1.00 42.07 ?  614 PRO A CD    1 
ATOM   4936  N  N     . MET A 1 615 ? 126.254 120.902 90.397  1.00 37.48 ?  615 MET A N     1 
ATOM   4937  C  CA    . MET A 1 615 ? 127.126 122.052 90.252  1.00 37.01 ?  615 MET A CA    1 
ATOM   4938  C  C     . MET A 1 615 ? 126.712 122.866 89.028  1.00 41.63 ?  615 MET A C     1 
ATOM   4939  O  O     . MET A 1 615 ? 126.215 122.310 88.044  1.00 38.54 ?  615 MET A O     1 
ATOM   4940  C  CB    . MET A 1 615 ? 128.582 121.609 90.131  1.00 33.82 ?  615 MET A CB    1 
ATOM   4941  C  CG    . MET A 1 615 ? 129.270 121.428 91.472  1.00 36.13 ?  615 MET A CG    1 
ATOM   4942  S  SD    . MET A 1 615 ? 128.810 122.701 92.662  1.00 52.76 ?  615 MET A SD    1 
ATOM   4943  C  CE    . MET A 1 615 ? 127.921 121.734 93.878  1.00 35.65 ?  615 MET A CE    1 
ATOM   4944  N  N     . PRO A 1 616 ? 126.872 124.186 89.076  1.00 40.49 ?  616 PRO A N     1 
ATOM   4945  C  CA    . PRO A 1 616 ? 126.404 125.029 87.968  1.00 35.85 ?  616 PRO A CA    1 
ATOM   4946  C  C     . PRO A 1 616 ? 127.054 124.639 86.650  1.00 36.86 ?  616 PRO A C     1 
ATOM   4947  O  O     . PRO A 1 616 ? 128.280 124.587 86.532  1.00 38.67 ?  616 PRO A O     1 
ATOM   4948  C  CB    . PRO A 1 616 ? 126.814 126.438 88.404  1.00 36.67 ?  616 PRO A CB    1 
ATOM   4949  C  CG    . PRO A 1 616 ? 126.892 126.357 89.890  1.00 38.59 ?  616 PRO A CG    1 
ATOM   4950  C  CD    . PRO A 1 616 ? 127.391 124.985 90.198  1.00 35.46 ?  616 PRO A CD    1 
ATOM   4951  N  N     . GLY A 1 617 ? 126.217 124.368 85.653  1.00 36.72 ?  617 GLY A N     1 
ATOM   4952  C  CA    . GLY A 1 617 ? 126.698 123.954 84.354  1.00 31.13 ?  617 GLY A CA    1 
ATOM   4953  C  C     . GLY A 1 617 ? 127.113 122.506 84.252  1.00 38.40 ?  617 GLY A C     1 
ATOM   4954  O  O     . GLY A 1 617 ? 127.671 122.112 83.223  1.00 40.80 ?  617 GLY A O     1 
ATOM   4955  N  N     . LEU A 1 618 ? 126.867 121.703 85.285  1.00 39.29 ?  618 LEU A N     1 
ATOM   4956  C  CA    . LEU A 1 618 ? 127.256 120.300 85.248  1.00 34.62 ?  618 LEU A CA    1 
ATOM   4957  C  C     . LEU A 1 618 ? 126.446 119.548 84.200  1.00 39.88 ?  618 LEU A C     1 
ATOM   4958  O  O     . LEU A 1 618 ? 125.233 119.733 84.074  1.00 40.59 ?  618 LEU A O     1 
ATOM   4959  C  CB    . LEU A 1 618 ? 127.067 119.654 86.620  1.00 34.82 ?  618 LEU A CB    1 
ATOM   4960  C  CG    . LEU A 1 618 ? 127.439 118.176 86.754  1.00 37.41 ?  618 LEU A CG    1 
ATOM   4961  C  CD1   . LEU A 1 618 ? 128.909 117.947 86.442  1.00 34.92 ?  618 LEU A CD1   1 
ATOM   4962  C  CD2   . LEU A 1 618 ? 127.098 117.657 88.142  1.00 35.44 ?  618 LEU A CD2   1 
ATOM   4963  N  N     . ALA A 1 619 ? 127.131 118.697 83.447  1.00 43.40 ?  619 ALA A N     1 
ATOM   4964  C  CA    . ALA A 1 619 ? 126.516 117.894 82.399  1.00 43.12 ?  619 ALA A CA    1 
ATOM   4965  C  C     . ALA A 1 619 ? 127.389 116.664 82.188  1.00 44.84 ?  619 ALA A C     1 
ATOM   4966  O  O     . ALA A 1 619 ? 128.278 116.370 82.993  1.00 50.01 ?  619 ALA A O     1 
ATOM   4967  C  CB    . ALA A 1 619 ? 126.340 118.709 81.114  1.00 41.78 ?  619 ALA A CB    1 
ATOM   4968  N  N     . SER A 1 620 ? 127.134 115.938 81.101  1.00 50.05 ?  620 SER A N     1 
ATOM   4969  C  CA    . SER A 1 620 ? 127.976 114.798 80.767  1.00 50.39 ?  620 SER A CA    1 
ATOM   4970  C  C     . SER A 1 620 ? 129.197 115.213 79.957  1.00 50.52 ?  620 SER A C     1 
ATOM   4971  O  O     . SER A 1 620 ? 130.206 114.501 79.955  1.00 54.16 ?  620 SER A O     1 
ATOM   4972  C  CB    . SER A 1 620 ? 127.166 113.751 80.000  1.00 53.17 ?  620 SER A CB    1 
ATOM   4973  O  OG    . SER A 1 620 ? 126.027 113.351 80.740  1.00 55.31 ?  620 SER A OG    1 
ATOM   4974  N  N     . ASN A 1 621 ? 129.126 116.356 79.272  1.00 48.00 ?  621 ASN A N     1 
ATOM   4975  C  CA    . ASN A 1 621 ? 130.259 116.809 78.472  1.00 48.37 ?  621 ASN A CA    1 
ATOM   4976  C  C     . ASN A 1 621 ? 131.356 117.418 79.337  1.00 51.61 ?  621 ASN A C     1 
ATOM   4977  O  O     . ASN A 1 621 ? 132.502 117.533 78.888  1.00 51.96 ?  621 ASN A O     1 
ATOM   4978  C  CB    . ASN A 1 621 ? 129.789 117.816 77.422  1.00 49.02 ?  621 ASN A CB    1 
ATOM   4979  C  CG    . ASN A 1 621 ? 129.709 119.229 77.962  1.00 51.03 ?  621 ASN A CG    1 
ATOM   4980  O  OD1   . ASN A 1 621 ? 128.831 119.551 78.762  1.00 50.38 ?  621 ASN A OD1   1 
ATOM   4981  N  ND2   . ASN A 1 621 ? 130.626 120.082 77.524  1.00 47.50 ?  621 ASN A ND2   1 
ATOM   4982  N  N     . ASN A 1 622 ? 131.032 117.813 80.568  1.00 44.03 ?  622 ASN A N     1 
ATOM   4983  C  CA    . ASN A 1 622 ? 132.007 118.378 81.493  1.00 40.24 ?  622 ASN A CA    1 
ATOM   4984  C  C     . ASN A 1 622 ? 131.914 117.730 82.871  1.00 42.76 ?  622 ASN A C     1 
ATOM   4985  O  O     . ASN A 1 622 ? 132.209 118.364 83.885  1.00 48.61 ?  622 ASN A O     1 
ATOM   4986  C  CB    . ASN A 1 622 ? 131.847 119.897 81.593  1.00 42.91 ?  622 ASN A CB    1 
ATOM   4987  C  CG    . ASN A 1 622 ? 130.446 120.322 82.007  1.00 42.30 ?  622 ASN A CG    1 
ATOM   4988  O  OD1   . ASN A 1 622 ? 129.762 119.629 82.756  1.00 43.38 ?  622 ASN A OD1   1 
ATOM   4989  N  ND2   . ASN A 1 622 ? 130.018 121.479 81.518  1.00 41.97 ?  622 ASN A ND2   1 
ATOM   4990  N  N     . TRP A 1 623 ? 131.492 116.464 82.917  1.00 37.70 ?  623 TRP A N     1 
ATOM   4991  C  CA    . TRP A 1 623 ? 131.365 115.773 84.196  1.00 38.13 ?  623 TRP A CA    1 
ATOM   4992  C  C     . TRP A 1 623 ? 132.719 115.598 84.872  1.00 38.97 ?  623 TRP A C     1 
ATOM   4993  O  O     . TRP A 1 623 ? 132.850 115.816 86.082  1.00 36.89 ?  623 TRP A O     1 
ATOM   4994  C  CB    . TRP A 1 623 ? 130.693 114.417 83.989  1.00 41.13 ?  623 TRP A CB    1 
ATOM   4995  C  CG    . TRP A 1 623 ? 130.618 113.581 85.229  1.00 37.94 ?  623 TRP A CG    1 
ATOM   4996  C  CD1   . TRP A 1 623 ? 131.535 112.667 85.656  1.00 37.18 ?  623 TRP A CD1   1 
ATOM   4997  C  CD2   . TRP A 1 623 ? 129.566 113.577 86.199  1.00 36.34 ?  623 TRP A CD2   1 
ATOM   4998  N  NE1   . TRP A 1 623 ? 131.122 112.096 86.834  1.00 37.99 ?  623 TRP A NE1   1 
ATOM   4999  C  CE2   . TRP A 1 623 ? 129.914 112.636 87.187  1.00 38.89 ?  623 TRP A CE2   1 
ATOM   5000  C  CE3   . TRP A 1 623 ? 128.364 114.276 86.328  1.00 37.48 ?  623 TRP A CE3   1 
ATOM   5001  C  CZ2   . TRP A 1 623 ? 129.105 112.380 88.291  1.00 37.40 ?  623 TRP A CZ2   1 
ATOM   5002  C  CZ3   . TRP A 1 623 ? 127.561 114.019 87.423  1.00 38.40 ?  623 TRP A CZ3   1 
ATOM   5003  C  CH2   . TRP A 1 623 ? 127.936 113.080 88.390  1.00 37.73 ?  623 TRP A CH2   1 
ATOM   5004  N  N     . PHE A 1 624 ? 133.738 115.204 84.111  1.00 43.16 ?  624 PHE A N     1 
ATOM   5005  C  CA    . PHE A 1 624 ? 135.046 114.929 84.690  1.00 41.82 ?  624 PHE A CA    1 
ATOM   5006  C  C     . PHE A 1 624 ? 135.904 116.174 84.849  1.00 42.59 ?  624 PHE A C     1 
ATOM   5007  O  O     . PHE A 1 624 ? 136.914 116.125 85.560  1.00 50.03 ?  624 PHE A O     1 
ATOM   5008  C  CB    . PHE A 1 624 ? 135.782 113.888 83.845  1.00 41.56 ?  624 PHE A CB    1 
ATOM   5009  C  CG    . PHE A 1 624 ? 135.136 112.532 83.873  1.00 45.32 ?  624 PHE A CG    1 
ATOM   5010  C  CD1   . PHE A 1 624 ? 135.163 111.765 85.025  1.00 42.10 ?  624 PHE A CD1   1 
ATOM   5011  C  CD2   . PHE A 1 624 ? 134.483 112.035 82.757  1.00 44.92 ?  624 PHE A CD2   1 
ATOM   5012  C  CE1   . PHE A 1 624 ? 134.563 110.524 85.061  1.00 41.33 ?  624 PHE A CE1   1 
ATOM   5013  C  CE2   . PHE A 1 624 ? 133.881 110.794 82.788  1.00 42.77 ?  624 PHE A CE2   1 
ATOM   5014  C  CZ    . PHE A 1 624 ? 133.921 110.037 83.940  1.00 45.45 ?  624 PHE A CZ    1 
ATOM   5015  N  N     . PHE A 1 625 ? 135.532 117.285 84.213  1.00 34.98 ?  625 PHE A N     1 
ATOM   5016  C  CA    . PHE A 1 625 ? 136.175 118.556 84.518  1.00 32.84 ?  625 PHE A CA    1 
ATOM   5017  C  C     . PHE A 1 625 ? 135.700 119.124 85.845  1.00 32.46 ?  625 PHE A C     1 
ATOM   5018  O  O     . PHE A 1 625 ? 136.391 119.964 86.431  1.00 36.35 ?  625 PHE A O     1 
ATOM   5019  C  CB    . PHE A 1 625 ? 135.931 119.562 83.396  1.00 31.54 ?  625 PHE A CB    1 
ATOM   5020  C  CG    . PHE A 1 625 ? 136.685 119.257 82.138  1.00 30.72 ?  625 PHE A CG    1 
ATOM   5021  C  CD1   . PHE A 1 625 ? 138.066 119.302 82.118  1.00 33.14 ?  625 PHE A CD1   1 
ATOM   5022  C  CD2   . PHE A 1 625 ? 136.013 118.931 80.972  1.00 34.06 ?  625 PHE A CD2   1 
ATOM   5023  C  CE1   . PHE A 1 625 ? 138.765 119.026 80.962  1.00 36.70 ?  625 PHE A CE1   1 
ATOM   5024  C  CE2   . PHE A 1 625 ? 136.708 118.655 79.813  1.00 32.14 ?  625 PHE A CE2   1 
ATOM   5025  C  CZ    . PHE A 1 625 ? 138.085 118.701 79.809  1.00 36.32 ?  625 PHE A CZ    1 
ATOM   5026  N  N     . TYR A 1 626 ? 134.541 118.687 86.330  1.00 29.43 ?  626 TYR A N     1 
ATOM   5027  C  CA    . TYR A 1 626 ? 134.059 119.055 87.659  1.00 31.49 ?  626 TYR A CA    1 
ATOM   5028  C  C     . TYR A 1 626 ? 134.589 118.094 88.716  1.00 27.64 ?  626 TYR A C     1 
ATOM   5029  O  O     . TYR A 1 626 ? 133.840 117.534 89.513  1.00 30.79 ?  626 TYR A O     1 
ATOM   5030  C  CB    . TYR A 1 626 ? 132.536 119.092 87.667  1.00 32.51 ?  626 TYR A CB    1 
ATOM   5031  C  CG    . TYR A 1 626 ? 131.961 120.452 87.364  1.00 28.67 ?  626 TYR A CG    1 
ATOM   5032  C  CD1   . TYR A 1 626 ? 132.083 121.494 88.270  1.00 32.63 ?  626 TYR A CD1   1 
ATOM   5033  C  CD2   . TYR A 1 626 ? 131.299 120.695 86.170  1.00 30.61 ?  626 TYR A CD2   1 
ATOM   5034  C  CE1   . TYR A 1 626 ? 131.561 122.739 87.997  1.00 29.49 ?  626 TYR A CE1   1 
ATOM   5035  C  CE2   . TYR A 1 626 ? 130.773 121.935 85.887  1.00 28.96 ?  626 TYR A CE2   1 
ATOM   5036  C  CZ    . TYR A 1 626 ? 130.907 122.953 86.805  1.00 27.83 ?  626 TYR A CZ    1 
ATOM   5037  O  OH    . TYR A 1 626 ? 130.387 124.193 86.532  1.00 34.46 ?  626 TYR A OH    1 
ATOM   5038  N  N     . LYS A 1 627 ? 135.904 117.908 88.721  1.00 31.50 ?  627 LYS A N     1 
ATOM   5039  C  CA    . LYS A 1 627 ? 136.536 117.000 89.666  1.00 31.57 ?  627 LYS A CA    1 
ATOM   5040  C  C     . LYS A 1 627 ? 136.336 117.498 91.090  1.00 31.68 ?  627 LYS A C     1 
ATOM   5041  O  O     . LYS A 1 627 ? 136.519 118.684 91.378  1.00 35.85 ?  627 LYS A O     1 
ATOM   5042  C  CB    . LYS A 1 627 ? 138.024 116.873 89.344  1.00 34.95 ?  627 LYS A CB    1 
ATOM   5043  C  CG    . LYS A 1 627 ? 138.765 115.843 90.167  1.00 34.41 ?  627 LYS A CG    1 
ATOM   5044  C  CD    . LYS A 1 627 ? 140.164 115.629 89.622  1.00 32.48 ?  627 LYS A CD    1 
ATOM   5045  C  CE    . LYS A 1 627 ? 140.933 114.621 90.451  1.00 38.41 ?  627 LYS A CE    1 
ATOM   5046  N  NZ    . LYS A 1 627 ? 142.356 114.537 90.024  1.00 39.70 1  627 LYS A NZ    1 
ATOM   5047  N  N     . GLU A 1 628 ? 135.950 116.590 91.980  1.00 35.59 ?  628 GLU A N     1 
ATOM   5048  C  CA    . GLU A 1 628 ? 135.721 116.966 93.367  1.00 36.22 ?  628 GLU A CA    1 
ATOM   5049  C  C     . GLU A 1 628 ? 137.033 117.337 94.047  1.00 39.79 ?  628 GLU A C     1 
ATOM   5050  O  O     . GLU A 1 628 ? 138.104 116.831 93.704  1.00 42.87 ?  628 GLU A O     1 
ATOM   5051  C  CB    . GLU A 1 628 ? 135.033 115.829 94.121  1.00 37.35 ?  628 GLU A CB    1 
ATOM   5052  C  CG    . GLU A 1 628 ? 133.646 115.498 93.596  1.00 39.53 ?  628 GLU A CG    1 
ATOM   5053  C  CD    . GLU A 1 628 ? 132.919 114.491 94.465  1.00 47.64 ?  628 GLU A CD    1 
ATOM   5054  O  OE1   . GLU A 1 628 ? 133.393 114.219 95.587  1.00 43.85 ?  628 GLU A OE1   1 
ATOM   5055  O  OE2   . GLU A 1 628 ? 131.869 113.976 94.026  1.00 44.12 -1 628 GLU A OE2   1 
ATOM   5056  N  N     . ALA A 1 629 ? 136.936 118.243 95.023  1.00 38.57 ?  629 ALA A N     1 
ATOM   5057  C  CA    . ALA A 1 629 ? 138.129 118.753 95.690  1.00 34.48 ?  629 ALA A CA    1 
ATOM   5058  C  C     . ALA A 1 629 ? 138.865 117.662 96.455  1.00 37.29 ?  629 ALA A C     1 
ATOM   5059  O  O     . ALA A 1 629 ? 140.083 117.752 96.642  1.00 44.58 ?  629 ALA A O     1 
ATOM   5060  C  CB    . ALA A 1 629 ? 137.751 119.893 96.631  1.00 35.14 ?  629 ALA A CB    1 
ATOM   5061  N  N     . TYR A 1 630 ? 138.151 116.637 96.917  1.00 42.65 ?  630 TYR A N     1 
ATOM   5062  C  CA    . TYR A 1 630 ? 138.799 115.584 97.689  1.00 41.94 ?  630 TYR A CA    1 
ATOM   5063  C  C     . TYR A 1 630 ? 139.619 114.654 96.804  1.00 44.19 ?  630 TYR A C     1 
ATOM   5064  O  O     . TYR A 1 630 ? 140.591 114.054 97.276  1.00 44.91 ?  630 TYR A O     1 
ATOM   5065  C  CB    . TYR A 1 630 ? 137.755 114.793 98.470  1.00 39.33 ?  630 TYR A CB    1 
ATOM   5066  C  CG    . TYR A 1 630 ? 136.969 115.632 99.448  1.00 40.78 ?  630 TYR A CG    1 
ATOM   5067  C  CD1   . TYR A 1 630 ? 137.523 116.018 100.660 1.00 38.92 ?  630 TYR A CD1   1 
ATOM   5068  C  CD2   . TYR A 1 630 ? 135.674 116.036 99.160  1.00 40.39 ?  630 TYR A CD2   1 
ATOM   5069  C  CE1   . TYR A 1 630 ? 136.809 116.782 101.557 1.00 39.65 ?  630 TYR A CE1   1 
ATOM   5070  C  CE2   . TYR A 1 630 ? 134.953 116.801 100.052 1.00 40.55 ?  630 TYR A CE2   1 
ATOM   5071  C  CZ    . TYR A 1 630 ? 135.526 117.171 101.250 1.00 44.72 ?  630 TYR A CZ    1 
ATOM   5072  O  OH    . TYR A 1 630 ? 134.813 117.933 102.144 1.00 48.31 ?  630 TYR A OH    1 
ATOM   5073  N  N     . ASP A 1 631 ? 139.253 114.524 95.531  1.00 40.74 ?  631 ASP A N     1 
ATOM   5074  C  CA    . ASP A 1 631 ? 139.942 113.608 94.632  1.00 39.43 ?  631 ASP A CA    1 
ATOM   5075  C  C     . ASP A 1 631 ? 141.185 114.208 93.990  1.00 43.72 ?  631 ASP A C     1 
ATOM   5076  O  O     . ASP A 1 631 ? 141.929 113.477 93.329  1.00 46.48 ?  631 ASP A O     1 
ATOM   5077  C  CB    . ASP A 1 631 ? 138.988 113.132 93.533  1.00 42.42 ?  631 ASP A CB    1 
ATOM   5078  C  CG    . ASP A 1 631 ? 137.658 112.658 94.079  1.00 49.41 ?  631 ASP A CG    1 
ATOM   5079  O  OD1   . ASP A 1 631 ? 137.648 111.994 95.136  1.00 48.62 ?  631 ASP A OD1   1 
ATOM   5080  O  OD2   . ASP A 1 631 ? 136.620 112.947 93.448  1.00 51.07 -1 631 ASP A OD2   1 
ATOM   5081  N  N     . MET A 1 632 ? 141.434 115.502 94.162  1.00 39.69 ?  632 MET A N     1 
ATOM   5082  C  CA    . MET A 1 632 ? 142.556 116.155 93.506  1.00 37.62 ?  632 MET A CA    1 
ATOM   5083  C  C     . MET A 1 632 ? 143.727 116.337 94.464  1.00 36.03 ?  632 MET A C     1 
ATOM   5084  O  O     . MET A 1 632 ? 143.582 116.283 95.687  1.00 38.98 ?  632 MET A O     1 
ATOM   5085  C  CB    . MET A 1 632 ? 142.144 117.510 92.928  1.00 37.51 ?  632 MET A CB    1 
ATOM   5086  C  CG    . MET A 1 632 ? 141.180 118.307 93.767  1.00 39.98 ?  632 MET A CG    1 
ATOM   5087  S  SD    . MET A 1 632 ? 140.854 119.919 93.035  1.00 47.46 ?  632 MET A SD    1 
ATOM   5088  C  CE    . MET A 1 632 ? 139.724 119.477 91.721  1.00 33.77 ?  632 MET A CE    1 
ATOM   5089  N  N     . ASP A 1 633 ? 144.901 116.555 93.878  1.00 34.02 ?  633 ASP A N     1 
ATOM   5090  C  CA    . ASP A 1 633 ? 146.117 116.772 94.650  1.00 30.19 ?  633 ASP A CA    1 
ATOM   5091  C  C     . ASP A 1 633 ? 146.065 118.136 95.326  1.00 28.33 ?  633 ASP A C     1 
ATOM   5092  O  O     . ASP A 1 633 ? 145.874 119.159 94.661  1.00 30.74 ?  633 ASP A O     1 
ATOM   5093  C  CB    . ASP A 1 633 ? 147.336 116.671 93.736  1.00 26.25 ?  633 ASP A CB    1 
ATOM   5094  C  CG    . ASP A 1 633 ? 148.637 116.563 94.504  1.00 38.00 ?  633 ASP A CG    1 
ATOM   5095  O  OD1   . ASP A 1 633 ? 148.597 116.468 95.749  1.00 39.38 ?  633 ASP A OD1   1 
ATOM   5096  O  OD2   . ASP A 1 633 ? 149.706 116.578 93.859  1.00 36.15 -1 633 ASP A OD2   1 
ATOM   5097  N  N     . MET A 1 634 ? 146.235 118.153 96.649  1.00 26.57 ?  634 MET A N     1 
ATOM   5098  C  CA    . MET A 1 634 ? 146.258 119.417 97.372  1.00 23.16 ?  634 MET A CA    1 
ATOM   5099  C  C     . MET A 1 634 ? 147.482 120.256 97.033  1.00 25.24 ?  634 MET A C     1 
ATOM   5100  O  O     . MET A 1 634 ? 147.461 121.469 97.250  1.00 26.06 ?  634 MET A O     1 
ATOM   5101  C  CB    . MET A 1 634 ? 146.195 119.172 98.879  1.00 23.97 ?  634 MET A CB    1 
ATOM   5102  C  CG    . MET A 1 634 ? 144.784 119.004 99.412  1.00 29.04 ?  634 MET A CG    1 
ATOM   5103  S  SD    . MET A 1 634 ? 143.714 120.382 98.957  1.00 38.84 ?  634 MET A SD    1 
ATOM   5104  C  CE    . MET A 1 634 ? 142.505 119.543 97.937  1.00 28.17 ?  634 MET A CE    1 
ATOM   5105  N  N     . PHE A 1 635 ? 148.544 119.642 96.505  1.00 24.58 ?  635 PHE A N     1 
ATOM   5106  C  CA    . PHE A 1 635 ? 149.690 120.424 96.054  1.00 21.50 ?  635 PHE A CA    1 
ATOM   5107  C  C     . PHE A 1 635 ? 149.324 121.292 94.855  1.00 21.21 ?  635 PHE A C     1 
ATOM   5108  O  O     . PHE A 1 635 ? 149.735 122.454 94.774  1.00 26.87 ?  635 PHE A O     1 
ATOM   5109  C  CB    . PHE A 1 635 ? 150.859 119.499 95.719  1.00 20.93 ?  635 PHE A CB    1 
ATOM   5110  C  CG    . PHE A 1 635 ? 151.742 119.191 96.895  1.00 27.72 ?  635 PHE A CG    1 
ATOM   5111  C  CD1   . PHE A 1 635 ? 151.199 118.983 98.151  1.00 22.95 ?  635 PHE A CD1   1 
ATOM   5112  C  CD2   . PHE A 1 635 ? 153.115 119.115 96.745  1.00 23.97 ?  635 PHE A CD2   1 
ATOM   5113  C  CE1   . PHE A 1 635 ? 152.008 118.704 99.233  1.00 23.47 ?  635 PHE A CE1   1 
ATOM   5114  C  CE2   . PHE A 1 635 ? 153.928 118.836 97.825  1.00 26.52 ?  635 PHE A CE2   1 
ATOM   5115  C  CZ    . PHE A 1 635 ? 153.372 118.629 99.069  1.00 24.17 ?  635 PHE A CZ    1 
ATOM   5116  N  N     . LYS A 1 636 ? 148.533 120.754 93.926  1.00 26.05 ?  636 LYS A N     1 
ATOM   5117  C  CA    . LYS A 1 636 ? 148.112 121.544 92.774  1.00 24.89 ?  636 LYS A CA    1 
ATOM   5118  C  C     . LYS A 1 636 ? 147.099 122.614 93.165  1.00 23.61 ?  636 LYS A C     1 
ATOM   5119  O  O     . LYS A 1 636 ? 147.101 123.710 92.592  1.00 31.09 ?  636 LYS A O     1 
ATOM   5120  C  CB    . LYS A 1 636 ? 147.546 120.626 91.693  1.00 27.32 ?  636 LYS A CB    1 
ATOM   5121  C  CG    . LYS A 1 636 ? 148.552 119.606 91.183  1.00 27.16 ?  636 LYS A CG    1 
ATOM   5122  C  CD    . LYS A 1 636 ? 148.587 119.559 89.669  1.00 30.50 ?  636 LYS A CD    1 
ATOM   5123  C  CE    . LYS A 1 636 ? 148.463 118.135 89.157  1.00 32.33 ?  636 LYS A CE    1 
ATOM   5124  N  NZ    . LYS A 1 636 ? 148.595 118.068 87.676  1.00 32.76 1  636 LYS A NZ    1 
ATOM   5125  N  N     . VAL A 1 637 ? 146.243 122.329 94.148  1.00 20.12 ?  637 VAL A N     1 
ATOM   5126  C  CA    . VAL A 1 637 ? 145.339 123.355 94.660  1.00 17.76 ?  637 VAL A CA    1 
ATOM   5127  C  C     . VAL A 1 637 ? 146.130 124.457 95.355  1.00 23.34 ?  637 VAL A C     1 
ATOM   5128  O  O     . VAL A 1 637 ? 145.801 125.644 95.240  1.00 26.50 ?  637 VAL A O     1 
ATOM   5129  C  CB    . VAL A 1 637 ? 144.292 122.725 95.595  1.00 21.56 ?  637 VAL A CB    1 
ATOM   5130  C  CG1   . VAL A 1 637 ? 143.288 123.770 96.053  1.00 23.10 ?  637 VAL A CG1   1 
ATOM   5131  C  CG2   . VAL A 1 637 ? 143.585 121.577 94.897  1.00 24.87 ?  637 VAL A CG2   1 
ATOM   5132  N  N     . VAL A 1 638 ? 147.185 124.085 96.085  1.00 26.37 ?  638 VAL A N     1 
ATOM   5133  C  CA    . VAL A 1 638 ? 148.066 125.078 96.689  1.00 21.65 ?  638 VAL A CA    1 
ATOM   5134  C  C     . VAL A 1 638 ? 148.728 125.920 95.609  1.00 18.06 ?  638 VAL A C     1 
ATOM   5135  O  O     . VAL A 1 638 ? 148.855 127.141 95.743  1.00 31.86 ?  638 VAL A O     1 
ATOM   5136  C  CB    . VAL A 1 638 ? 149.114 124.393 97.588  1.00 21.89 ?  638 VAL A CB    1 
ATOM   5137  C  CG1   . VAL A 1 638 ? 150.310 125.305 97.801  1.00 15.98 ?  638 VAL A CG1   1 
ATOM   5138  C  CG2   . VAL A 1 638 ? 148.504 124.000 98.918  1.00 22.01 ?  638 VAL A CG2   1 
ATOM   5139  N  N     . ASP A 1 639 ? 149.164 125.279 94.524  1.00 13.54 ?  639 ASP A N     1 
ATOM   5140  C  CA    . ASP A 1 639 ? 149.753 126.013 93.410  1.00 16.83 ?  639 ASP A CA    1 
ATOM   5141  C  C     . ASP A 1 639 ? 148.764 127.015 92.828  1.00 24.01 ?  639 ASP A C     1 
ATOM   5142  O  O     . ASP A 1 639 ? 149.125 128.161 92.541  1.00 29.17 ?  639 ASP A O     1 
ATOM   5143  C  CB    . ASP A 1 639 ? 150.219 125.036 92.331  1.00 15.86 ?  639 ASP A CB    1 
ATOM   5144  C  CG    . ASP A 1 639 ? 151.498 124.322 92.704  1.00 29.95 ?  639 ASP A CG    1 
ATOM   5145  O  OD1   . ASP A 1 639 ? 152.380 124.958 93.319  1.00 34.26 ?  639 ASP A OD1   1 
ATOM   5146  O  OD2   . ASP A 1 639 ? 151.624 123.120 92.387  1.00 34.71 -1 639 ASP A OD2   1 
ATOM   5147  N  N     . MET A 1 640 ? 147.508 126.602 92.660  1.00 23.60 ?  640 MET A N     1 
ATOM   5148  C  CA    . MET A 1 640 ? 146.493 127.502 92.119  1.00 21.42 ?  640 MET A CA    1 
ATOM   5149  C  C     . MET A 1 640 ? 146.237 128.679 93.055  1.00 22.11 ?  640 MET A C     1 
ATOM   5150  O  O     . MET A 1 640 ? 146.175 129.835 92.619  1.00 25.58 ?  640 MET A O     1 
ATOM   5151  C  CB    . MET A 1 640 ? 145.202 126.726 91.861  1.00 24.83 ?  640 MET A CB    1 
ATOM   5152  C  CG    . MET A 1 640 ? 143.978 127.598 91.661  1.00 24.53 ?  640 MET A CG    1 
ATOM   5153  S  SD    . MET A 1 640 ? 143.987 128.453 90.078  1.00 27.79 ?  640 MET A SD    1 
ATOM   5154  C  CE    . MET A 1 640 ? 142.998 127.339 89.094  1.00 26.13 ?  640 MET A CE    1 
ATOM   5155  N  N     . ILE A 1 641 ? 146.095 128.403 94.353  1.00 21.70 ?  641 ILE A N     1 
ATOM   5156  C  CA    . ILE A 1 641 ? 145.801 129.466 95.308  1.00 16.23 ?  641 ILE A CA    1 
ATOM   5157  C  C     . ILE A 1 641 ? 146.981 130.422 95.425  1.00 18.08 ?  641 ILE A C     1 
ATOM   5158  O  O     . ILE A 1 641 ? 146.801 131.635 95.579  1.00 25.78 ?  641 ILE A O     1 
ATOM   5159  C  CB    . ILE A 1 641 ? 145.403 128.869 96.670  1.00 24.77 ?  641 ILE A CB    1 
ATOM   5160  C  CG1   . ILE A 1 641 ? 144.169 127.979 96.522  1.00 23.13 ?  641 ILE A CG1   1 
ATOM   5161  C  CG2   . ILE A 1 641 ? 145.116 129.968 97.679  1.00 16.45 ?  641 ILE A CG2   1 
ATOM   5162  C  CD1   . ILE A 1 641 ? 143.041 128.620 95.750  1.00 19.77 ?  641 ILE A CD1   1 
ATOM   5163  N  N     . ALA A 1 642 ? 148.206 129.897 95.346  1.00 13.80 ?  642 ALA A N     1 
ATOM   5164  C  CA    . ALA A 1 642 ? 149.385 130.751 95.380  1.00 14.95 ?  642 ALA A CA    1 
ATOM   5165  C  C     . ALA A 1 642 ? 149.512 131.581 94.111  1.00 15.06 ?  642 ALA A C     1 
ATOM   5166  O  O     . ALA A 1 642 ? 149.996 132.716 94.161  1.00 24.85 ?  642 ALA A O     1 
ATOM   5167  C  CB    . ALA A 1 642 ? 150.637 129.904 95.591  1.00 16.20 ?  642 ALA A CB    1 
ATOM   5168  N  N     . THR A 1 643 ? 149.099 131.030 92.968  1.00 17.82 ?  643 THR A N     1 
ATOM   5169  C  CA    . THR A 1 643 ? 149.050 131.823 91.746  1.00 20.13 ?  643 THR A CA    1 
ATOM   5170  C  C     . THR A 1 643 ? 148.052 132.965 91.879  1.00 18.40 ?  643 THR A C     1 
ATOM   5171  O  O     . THR A 1 643 ? 148.334 134.098 91.475  1.00 22.42 ?  643 THR A O     1 
ATOM   5172  C  CB    . THR A 1 643 ? 148.696 130.931 90.558  1.00 22.01 ?  643 THR A CB    1 
ATOM   5173  O  OG1   . THR A 1 643 ? 149.743 129.975 90.350  1.00 28.71 ?  643 THR A OG1   1 
ATOM   5174  C  CG2   . THR A 1 643 ? 148.524 131.760 89.301  1.00 17.65 ?  643 THR A CG2   1 
ATOM   5175  N  N     . ILE A 1 644 ? 146.881 132.688 92.453  1.00 16.05 ?  644 ILE A N     1 
ATOM   5176  C  CA    . ILE A 1 644 ? 145.903 133.748 92.671  1.00 14.62 ?  644 ILE A CA    1 
ATOM   5177  C  C     . ILE A 1 644 ? 146.385 134.712 93.749  1.00 17.27 ?  644 ILE A C     1 
ATOM   5178  O  O     . ILE A 1 644 ? 146.193 135.929 93.641  1.00 22.60 ?  644 ILE A O     1 
ATOM   5179  C  CB    . ILE A 1 644 ? 144.530 133.148 93.020  1.00 15.77 ?  644 ILE A CB    1 
ATOM   5180  C  CG1   . ILE A 1 644 ? 144.031 132.252 91.887  1.00 14.71 ?  644 ILE A CG1   1 
ATOM   5181  C  CG2   . ILE A 1 644 ? 143.525 134.248 93.292  1.00 7.74  ?  644 ILE A CG2   1 
ATOM   5182  C  CD1   . ILE A 1 644 ? 142.891 131.349 92.290  1.00 22.09 ?  644 ILE A CD1   1 
ATOM   5183  N  N     . GLN A 1 645 ? 147.024 134.187 94.800  1.00 11.57 ?  645 GLN A N     1 
ATOM   5184  C  CA    . GLN A 1 645 ? 147.390 135.012 95.948  1.00 11.89 ?  645 GLN A CA    1 
ATOM   5185  C  C     . GLN A 1 645 ? 148.383 136.107 95.580  1.00 18.71 ?  645 GLN A C     1 
ATOM   5186  O  O     . GLN A 1 645 ? 148.404 137.163 96.223  1.00 23.96 ?  645 GLN A O     1 
ATOM   5187  C  CB    . GLN A 1 645 ? 147.962 134.133 97.061  1.00 8.94  ?  645 GLN A CB    1 
ATOM   5188  C  CG    . GLN A 1 645 ? 148.303 134.875 98.343  1.00 10.21 ?  645 GLN A CG    1 
ATOM   5189  C  CD    . GLN A 1 645 ? 147.083 135.466 99.016  1.00 12.21 ?  645 GLN A CD    1 
ATOM   5190  O  OE1   . GLN A 1 645 ? 146.397 134.792 99.781  1.00 18.33 ?  645 GLN A OE1   1 
ATOM   5191  N  NE2   . GLN A 1 645 ? 146.809 136.733 98.737  1.00 4.73  ?  645 GLN A NE2   1 
ATOM   5192  N  N     . GLN A 1 646 ? 149.204 135.888 94.555  1.00 20.94 ?  646 GLN A N     1 
ATOM   5193  C  CA    . GLN A 1 646 ? 150.199 136.887 94.188  1.00 14.79 ?  646 GLN A CA    1 
ATOM   5194  C  C     . GLN A 1 646 ? 149.583 138.160 93.624  1.00 15.69 ?  646 GLN A C     1 
ATOM   5195  O  O     . GLN A 1 646 ? 150.278 139.178 93.543  1.00 20.87 ?  646 GLN A O     1 
ATOM   5196  C  CB    . GLN A 1 646 ? 151.191 136.293 93.189  1.00 20.94 ?  646 GLN A CB    1 
ATOM   5197  C  CG    . GLN A 1 646 ? 150.717 136.285 91.754  1.00 22.21 ?  646 GLN A CG    1 
ATOM   5198  C  CD    . GLN A 1 646 ? 151.671 135.548 90.837  1.00 30.10 ?  646 GLN A CD    1 
ATOM   5199  O  OE1   . GLN A 1 646 ? 151.310 134.544 90.225  1.00 25.03 ?  646 GLN A OE1   1 
ATOM   5200  N  NE2   . GLN A 1 646 ? 152.898 136.044 90.740  1.00 26.74 ?  646 GLN A NE2   1 
ATOM   5201  N  N     . HIS A 1 647 ? 148.306 138.137 93.249  1.00 21.92 ?  647 HIS A N     1 
ATOM   5202  C  CA    . HIS A 1 647 ? 147.604 139.322 92.782  1.00 14.76 ?  647 HIS A CA    1 
ATOM   5203  C  C     . HIS A 1 647 ? 146.585 139.840 93.786  1.00 15.27 ?  647 HIS A C     1 
ATOM   5204  O  O     . HIS A 1 647 ? 145.893 140.820 93.498  1.00 25.12 ?  647 HIS A O     1 
ATOM   5205  C  CB    . HIS A 1 647 ? 146.910 139.031 91.448  1.00 11.36 ?  647 HIS A CB    1 
ATOM   5206  C  CG    . HIS A 1 647 ? 147.816 138.447 90.414  1.00 16.48 ?  647 HIS A CG    1 
ATOM   5207  N  ND1   . HIS A 1 647 ? 148.924 139.112 89.935  1.00 19.03 ?  647 HIS A ND1   1 
ATOM   5208  C  CD2   . HIS A 1 647 ? 147.783 137.258 89.767  1.00 17.59 ?  647 HIS A CD2   1 
ATOM   5209  C  CE1   . HIS A 1 647 ? 149.534 138.359 89.038  1.00 20.83 ?  647 HIS A CE1   1 
ATOM   5210  N  NE2   . HIS A 1 647 ? 148.861 137.229 88.916  1.00 20.71 ?  647 HIS A NE2   1 
ATOM   5211  N  N     . ILE A 1 648 ? 146.474 139.209 94.951  1.00 13.52 ?  648 ILE A N     1 
ATOM   5212  C  CA    . ILE A 1 648 ? 145.513 139.586 95.979  1.00 12.03 ?  648 ILE A CA    1 
ATOM   5213  C  C     . ILE A 1 648 ? 146.291 140.197 97.135  1.00 12.20 ?  648 ILE A C     1 
ATOM   5214  O  O     . ILE A 1 648 ? 147.211 139.569 97.672  1.00 25.66 ?  648 ILE A O     1 
ATOM   5215  C  CB    . ILE A 1 648 ? 144.683 138.377 96.440  1.00 10.19 ?  648 ILE A CB    1 
ATOM   5216  C  CG1   . ILE A 1 648 ? 143.967 137.729 95.252  1.00 11.20 ?  648 ILE A CG1   1 
ATOM   5217  C  CG2   . ILE A 1 648 ? 143.673 138.785 97.496  1.00 5.66  ?  648 ILE A CG2   1 
ATOM   5218  C  CD1   . ILE A 1 648 ? 142.832 138.553 94.695  1.00 5.31  ?  648 ILE A CD1   1 
ATOM   5219  N  N     . ASP A 1 649 ? 145.931 141.426 97.515  1.00 7.57  ?  649 ASP A N     1 
ATOM   5220  C  CA    . ASP A 1 649 ? 146.673 142.105 98.574  1.00 8.07  ?  649 ASP A CA    1 
ATOM   5221  C  C     . ASP A 1 649 ? 146.365 141.515 99.942  1.00 9.20  ?  649 ASP A C     1 
ATOM   5222  O  O     . ASP A 1 649 ? 147.254 141.436 100.796 1.00 27.02 ?  649 ASP A O     1 
ATOM   5223  C  CB    . ASP A 1 649 ? 146.373 143.603 98.560  1.00 18.44 ?  649 ASP A CB    1 
ATOM   5224  C  CG    . ASP A 1 649 ? 144.903 143.902 98.377  1.00 19.25 ?  649 ASP A CG    1 
ATOM   5225  O  OD1   . ASP A 1 649 ? 144.427 143.847 97.228  1.00 24.05 ?  649 ASP A OD1   1 
ATOM   5226  O  OD2   . ASP A 1 649 ? 144.225 144.201 99.380  1.00 20.27 -1 649 ASP A OD2   1 
ATOM   5227  N  N     . GLN A 1 650 ? 145.123 141.116 100.173 1.00 13.71 ?  650 GLN A N     1 
ATOM   5228  C  CA    . GLN A 1 650 ? 144.739 140.403 101.380 1.00 4.37  ?  650 GLN A CA    1 
ATOM   5229  C  C     . GLN A 1 650 ? 144.842 138.901 101.107 1.00 10.77 ?  650 GLN A C     1 
ATOM   5230  O  O     . GLN A 1 650 ? 145.452 138.479 100.122 1.00 20.19 ?  650 GLN A O     1 
ATOM   5231  C  CB    . GLN A 1 650 ? 143.349 140.854 101.827 1.00 6.40  ?  650 GLN A CB    1 
ATOM   5232  C  CG    . GLN A 1 650 ? 143.249 142.348 102.076 1.00 9.80  ?  650 GLN A CG    1 
ATOM   5233  C  CD    . GLN A 1 650 ? 141.908 142.753 102.640 1.00 13.56 ?  650 GLN A CD    1 
ATOM   5234  O  OE1   . GLN A 1 650 ? 141.595 142.458 103.790 1.00 15.64 ?  650 GLN A OE1   1 
ATOM   5235  N  NE2   . GLN A 1 650 ? 141.107 143.436 101.833 1.00 3.67  ?  650 GLN A NE2   1 
ATOM   5236  N  N     . GLY A 1 651 ? 144.283 138.073 101.986 1.00 9.85  ?  651 GLY A N     1 
ATOM   5237  C  CA    . GLY A 1 651 ? 144.388 136.638 101.861 1.00 5.75  ?  651 GLY A CA    1 
ATOM   5238  C  C     . GLY A 1 651 ? 143.218 136.008 101.122 1.00 5.51  ?  651 GLY A C     1 
ATOM   5239  O  O     . GLY A 1 651 ? 142.289 136.664 100.661 1.00 10.85 ?  651 GLY A O     1 
ATOM   5240  N  N     . ILE A 1 652 ? 143.295 134.685 101.015 1.00 13.76 ?  652 ILE A N     1 
ATOM   5241  C  CA    . ILE A 1 652 ? 142.279 133.863 100.372 1.00 2.10  ?  652 ILE A CA    1 
ATOM   5242  C  C     . ILE A 1 652 ? 141.876 132.775 101.353 1.00 12.29 ?  652 ILE A C     1 
ATOM   5243  O  O     . ILE A 1 652 ? 142.740 132.094 101.914 1.00 26.74 ?  652 ILE A O     1 
ATOM   5244  C  CB    . ILE A 1 652 ? 142.797 133.241 99.060  1.00 6.19  ?  652 ILE A CB    1 
ATOM   5245  C  CG1   . ILE A 1 652 ? 143.345 134.323 98.128  1.00 4.30  ?  652 ILE A CG1   1 
ATOM   5246  C  CG2   . ILE A 1 652 ? 141.705 132.441 98.378  1.00 11.90 ?  652 ILE A CG2   1 
ATOM   5247  C  CD1   . ILE A 1 652 ? 143.936 133.779 96.859  1.00 5.06  ?  652 ILE A CD1   1 
ATOM   5248  N  N     . SER A 1 653 ? 140.575 132.613 101.566 1.00 10.56 ?  653 SER A N     1 
ATOM   5249  C  CA    . SER A 1 653 ? 140.074 131.577 102.465 1.00 12.86 ?  653 SER A CA    1 
ATOM   5250  C  C     . SER A 1 653 ? 140.335 130.221 101.828 1.00 18.04 ?  653 SER A C     1 
ATOM   5251  O  O     . SER A 1 653 ? 139.578 129.766 100.971 1.00 20.45 ?  653 SER A O     1 
ATOM   5252  C  CB    . SER A 1 653 ? 138.590 131.780 102.741 1.00 13.46 ?  653 SER A CB    1 
ATOM   5253  O  OG    . SER A 1 653 ? 138.390 132.481 103.950 1.00 20.71 ?  653 SER A OG    1 
ATOM   5254  N  N     . PHE A 1 654 ? 141.403 129.561 102.262 1.00 22.22 ?  654 PHE A N     1 
ATOM   5255  C  CA    . PHE A 1 654 ? 141.915 128.358 101.615 1.00 10.48 ?  654 PHE A CA    1 
ATOM   5256  C  C     . PHE A 1 654 ? 141.554 127.146 102.464 1.00 13.54 ?  654 PHE A C     1 
ATOM   5257  O  O     . PHE A 1 654 ? 142.178 126.897 103.502 1.00 21.98 ?  654 PHE A O     1 
ATOM   5258  C  CB    . PHE A 1 654 ? 143.425 128.469 101.419 1.00 15.97 ?  654 PHE A CB    1 
ATOM   5259  C  CG    . PHE A 1 654 ? 144.026 127.345 100.630 1.00 16.96 ?  654 PHE A CG    1 
ATOM   5260  C  CD1   . PHE A 1 654 ? 143.236 126.518 99.852  1.00 18.84 ?  654 PHE A CD1   1 
ATOM   5261  C  CD2   . PHE A 1 654 ? 145.389 127.123 100.662 1.00 21.85 ?  654 PHE A CD2   1 
ATOM   5262  C  CE1   . PHE A 1 654 ? 143.794 125.490 99.130  1.00 18.09 ?  654 PHE A CE1   1 
ATOM   5263  C  CE2   . PHE A 1 654 ? 145.950 126.098 99.938  1.00 21.06 ?  654 PHE A CE2   1 
ATOM   5264  C  CZ    . PHE A 1 654 ? 145.152 125.280 99.171  1.00 19.78 ?  654 PHE A CZ    1 
ATOM   5265  N  N     . THR A 1 655 ? 140.563 126.385 102.012 1.00 22.24 ?  655 THR A N     1 
ATOM   5266  C  CA    . THR A 1 655 ? 140.158 125.156 102.678 1.00 23.33 ?  655 THR A CA    1 
ATOM   5267  C  C     . THR A 1 655 ? 140.961 123.984 102.129 1.00 26.54 ?  655 THR A C     1 
ATOM   5268  O  O     . THR A 1 655 ? 141.127 123.852 100.912 1.00 26.35 ?  655 THR A O     1 
ATOM   5269  C  CB    . THR A 1 655 ? 138.661 124.909 102.485 1.00 23.96 ?  655 THR A CB    1 
ATOM   5270  O  OG1   . THR A 1 655 ? 137.919 125.968 103.099 1.00 31.72 ?  655 THR A OG1   1 
ATOM   5271  C  CG2   . THR A 1 655 ? 138.253 123.587 103.111 1.00 26.42 ?  655 THR A CG2   1 
ATOM   5272  N  N     . LEU A 1 656 ? 141.463 123.142 103.027 1.00 29.51 ?  656 LEU A N     1 
ATOM   5273  C  CA    . LEU A 1 656 ? 142.161 121.925 102.640 1.00 29.05 ?  656 LEU A CA    1 
ATOM   5274  C  C     . LEU A 1 656 ? 141.186 120.758 102.642 1.00 28.32 ?  656 LEU A C     1 
ATOM   5275  O  O     . LEU A 1 656 ? 140.521 120.495 103.649 1.00 28.78 ?  656 LEU A O     1 
ATOM   5276  C  CB    . LEU A 1 656 ? 143.327 121.639 103.586 1.00 29.85 ?  656 LEU A CB    1 
ATOM   5277  C  CG    . LEU A 1 656 ? 144.492 122.624 103.537 1.00 32.35 ?  656 LEU A CG    1 
ATOM   5278  C  CD1   . LEU A 1 656 ? 145.662 122.097 104.346 1.00 29.79 ?  656 LEU A CD1   1 
ATOM   5279  C  CD2   . LEU A 1 656 ? 144.907 122.906 102.103 1.00 27.79 ?  656 LEU A CD2   1 
ATOM   5280  N  N     . PHE A 1 657 ? 141.109 120.060 101.517 1.00 27.28 ?  657 PHE A N     1 
ATOM   5281  C  CA    . PHE A 1 657 ? 140.179 118.953 101.336 1.00 27.17 ?  657 PHE A CA    1 
ATOM   5282  C  C     . PHE A 1 657 ? 140.965 117.652 101.426 1.00 34.16 ?  657 PHE A C     1 
ATOM   5283  O  O     . PHE A 1 657 ? 141.719 117.308 100.511 1.00 37.77 ?  657 PHE A O     1 
ATOM   5284  C  CB    . PHE A 1 657 ? 139.450 119.085 100.003 1.00 28.61 ?  657 PHE A CB    1 
ATOM   5285  C  CG    . PHE A 1 657 ? 138.772 120.410 99.822  1.00 33.56 ?  657 PHE A CG    1 
ATOM   5286  C  CD1   . PHE A 1 657 ? 137.487 120.614 100.291 1.00 30.41 ?  657 PHE A CD1   1 
ATOM   5287  C  CD2   . PHE A 1 657 ? 139.426 121.460 99.197  1.00 34.59 ?  657 PHE A CD2   1 
ATOM   5288  C  CE1   . PHE A 1 657 ? 136.862 121.832 100.130 1.00 33.52 ?  657 PHE A CE1   1 
ATOM   5289  C  CE2   . PHE A 1 657 ? 138.805 122.680 99.032  1.00 30.81 ?  657 PHE A CE2   1 
ATOM   5290  C  CZ    . PHE A 1 657 ? 137.522 122.867 99.502  1.00 32.22 ?  657 PHE A CZ    1 
ATOM   5291  N  N     . LEU A 1 658 ? 140.781 116.932 102.528 1.00 42.10 ?  658 LEU A N     1 
ATOM   5292  C  CA    . LEU A 1 658 ? 141.600 115.779 102.867 1.00 40.48 ?  658 LEU A CA    1 
ATOM   5293  C  C     . LEU A 1 658 ? 140.783 114.498 102.788 1.00 44.65 ?  658 LEU A C     1 
ATOM   5294  O  O     . LEU A 1 658 ? 139.607 114.475 103.160 1.00 48.50 ?  658 LEU A O     1 
ATOM   5295  C  CB    . LEU A 1 658 ? 142.181 115.929 104.275 1.00 38.92 ?  658 LEU A CB    1 
ATOM   5296  C  CG    . LEU A 1 658 ? 142.588 117.340 104.697 1.00 38.09 ?  658 LEU A CG    1 
ATOM   5297  C  CD1   . LEU A 1 658 ? 142.754 117.403 106.202 1.00 37.57 ?  658 LEU A CD1   1 
ATOM   5298  C  CD2   . LEU A 1 658 ? 143.866 117.761 103.996 1.00 39.85 ?  658 LEU A CD2   1 
ATOM   5299  N  N     . LYS A 1 659 ? 141.410 113.437 102.292 1.00 48.81 ?  659 LYS A N     1 
ATOM   5300  C  CA    . LYS A 1 659 ? 140.809 112.116 102.361 1.00 49.27 ?  659 LYS A CA    1 
ATOM   5301  C  C     . LYS A 1 659 ? 141.077 111.488 103.727 1.00 49.70 ?  659 LYS A C     1 
ATOM   5302  O  O     . LYS A 1 659 ? 141.947 111.925 104.482 1.00 53.26 ?  659 LYS A O     1 
ATOM   5303  C  CB    . LYS A 1 659 ? 141.350 111.214 101.252 1.00 50.47 ?  659 LYS A CB    1 
ATOM   5304  C  CG    . LYS A 1 659 ? 140.841 111.563 99.867  1.00 50.24 ?  659 LYS A CG    1 
ATOM   5305  C  CD    . LYS A 1 659 ? 141.238 110.503 98.854  1.00 50.40 ?  659 LYS A CD    1 
ATOM   5306  C  CE    . LYS A 1 659 ? 140.649 110.801 97.485  1.00 49.54 ?  659 LYS A CE    1 
ATOM   5307  N  NZ    . LYS A 1 659 ? 140.668 109.606 96.599  1.00 49.60 1  659 LYS A NZ    1 
ATOM   5308  N  N     . ASP A 1 660 ? 140.300 110.452 104.043 1.00 56.54 ?  660 ASP A N     1 
ATOM   5309  C  CA    . ASP A 1 660 ? 140.515 109.720 105.285 1.00 56.20 ?  660 ASP A CA    1 
ATOM   5310  C  C     . ASP A 1 660 ? 141.829 108.952 105.284 1.00 56.75 ?  660 ASP A C     1 
ATOM   5311  O  O     . ASP A 1 660 ? 142.393 108.711 106.357 1.00 56.19 ?  660 ASP A O     1 
ATOM   5312  C  CB    . ASP A 1 660 ? 139.353 108.759 105.537 1.00 57.79 ?  660 ASP A CB    1 
ATOM   5313  C  CG    . ASP A 1 660 ? 138.365 109.291 106.554 1.00 58.39 ?  660 ASP A CG    1 
ATOM   5314  O  OD1   . ASP A 1 660 ? 137.331 108.630 106.785 1.00 57.17 ?  660 ASP A OD1   1 
ATOM   5315  O  OD2   . ASP A 1 660 ? 138.625 110.367 107.129 1.00 56.44 -1 660 ASP A OD2   1 
ATOM   5316  N  N     . THR A 1 661 ? 142.327 108.568 104.107 1.00 54.72 ?  661 THR A N     1 
ATOM   5317  C  CA    . THR A 1 661 ? 143.523 107.735 104.036 1.00 54.28 ?  661 THR A CA    1 
ATOM   5318  C  C     . THR A 1 661 ? 144.779 108.488 104.459 1.00 54.79 ?  661 THR A C     1 
ATOM   5319  O  O     . THR A 1 661 ? 145.680 107.890 105.059 1.00 57.02 ?  661 THR A O     1 
ATOM   5320  C  CB    . THR A 1 661 ? 143.696 107.188 102.620 1.00 55.29 ?  661 THR A CB    1 
ATOM   5321  O  OG1   . THR A 1 661 ? 143.282 108.178 101.670 1.00 55.34 ?  661 THR A OG1   1 
ATOM   5322  C  CG2   . THR A 1 661 ? 142.860 105.932 102.431 1.00 54.88 ?  661 THR A CG2   1 
ATOM   5323  N  N     . MET A 1 662 ? 144.866 109.780 104.160 1.00 53.00 ?  662 MET A N     1 
ATOM   5324  C  CA    . MET A 1 662 ? 146.088 110.528 104.421 1.00 52.79 ?  662 MET A CA    1 
ATOM   5325  C  C     . MET A 1 662 ? 146.263 110.779 105.914 1.00 51.88 ?  662 MET A C     1 
ATOM   5326  O  O     . MET A 1 662 ? 145.293 111.004 106.643 1.00 52.12 ?  662 MET A O     1 
ATOM   5327  C  CB    . MET A 1 662 ? 146.088 111.852 103.655 1.00 51.51 ?  662 MET A CB    1 
ATOM   5328  C  CG    . MET A 1 662 ? 144.963 112.802 104.006 1.00 52.69 ?  662 MET A CG    1 
ATOM   5329  S  SD    . MET A 1 662 ? 145.021 114.313 103.021 1.00 60.26 ?  662 MET A SD    1 
ATOM   5330  C  CE    . MET A 1 662 ? 145.883 113.747 101.557 1.00 49.12 ?  662 MET A CE    1 
ATOM   5331  N  N     . THR A 1 663 ? 147.514 110.733 106.362 1.00 44.50 ?  663 THR A N     1 
ATOM   5332  C  CA    . THR A 1 663 ? 147.848 110.834 107.774 1.00 43.95 ?  663 THR A CA    1 
ATOM   5333  C  C     . THR A 1 663 ? 148.044 112.299 108.160 1.00 45.06 ?  663 THR A C     1 
ATOM   5334  O  O     . THR A 1 663 ? 147.784 113.213 107.374 1.00 48.51 ?  663 THR A O     1 
ATOM   5335  C  CB    . THR A 1 663 ? 149.096 110.007 108.076 1.00 43.10 ?  663 THR A CB    1 
ATOM   5336  O  OG1   . THR A 1 663 ? 150.246 110.667 107.533 1.00 41.26 ?  663 THR A OG1   1 
ATOM   5337  C  CG2   . THR A 1 663 ? 148.979 108.628 107.450 1.00 44.67 ?  663 THR A CG2   1 
ATOM   5338  N  N     . THR A 1 664 ? 148.504 112.537 109.391 1.00 39.46 ?  664 THR A N     1 
ATOM   5339  C  CA    . THR A 1 664 ? 148.845 113.898 109.790 1.00 41.82 ?  664 THR A CA    1 
ATOM   5340  C  C     . THR A 1 664 ? 150.104 114.382 109.085 1.00 40.57 ?  664 THR A C     1 
ATOM   5341  O  O     . THR A 1 664 ? 150.294 115.592 108.922 1.00 42.64 ?  664 THR A O     1 
ATOM   5342  C  CB    . THR A 1 664 ? 149.024 113.987 111.305 1.00 41.38 ?  664 THR A CB    1 
ATOM   5343  O  OG1   . THR A 1 664 ? 150.111 113.147 111.712 1.00 40.03 ?  664 THR A OG1   1 
ATOM   5344  C  CG2   . THR A 1 664 ? 147.755 113.556 112.022 1.00 39.88 ?  664 THR A CG2   1 
ATOM   5345  N  N     . ARG A 1 665 ? 150.972 113.457 108.669 1.00 39.85 ?  665 ARG A N     1 
ATOM   5346  C  CA    . ARG A 1 665 ? 152.159 113.846 107.916 1.00 38.49 ?  665 ARG A CA    1 
ATOM   5347  C  C     . ARG A 1 665 ? 151.783 114.460 106.576 1.00 41.53 ?  665 ARG A C     1 
ATOM   5348  O  O     . ARG A 1 665 ? 152.423 115.412 106.124 1.00 42.68 ?  665 ARG A O     1 
ATOM   5349  C  CB    . ARG A 1 665 ? 153.075 112.643 107.707 1.00 39.32 ?  665 ARG A CB    1 
ATOM   5350  C  CG    . ARG A 1 665 ? 154.344 112.973 106.944 1.00 37.71 ?  665 ARG A CG    1 
ATOM   5351  C  CD    . ARG A 1 665 ? 155.294 111.795 106.903 1.00 39.18 ?  665 ARG A CD    1 
ATOM   5352  N  NE    . ARG A 1 665 ? 156.348 111.977 105.914 1.00 41.76 ?  665 ARG A NE    1 
ATOM   5353  C  CZ    . ARG A 1 665 ? 156.181 111.852 104.604 1.00 45.20 ?  665 ARG A CZ    1 
ATOM   5354  N  NH1   . ARG A 1 665 ? 155.007 111.534 104.085 1.00 43.53 1  665 ARG A NH1   1 
ATOM   5355  N  NH2   . ARG A 1 665 ? 157.218 112.050 103.796 1.00 42.18 ?  665 ARG A NH2   1 
ATOM   5356  N  N     . ASP A 1 666 ? 150.753 113.924 105.919 1.00 38.83 ?  666 ASP A N     1 
ATOM   5357  C  CA    . ASP A 1 666 ? 150.316 114.496 104.650 1.00 35.10 ?  666 ASP A CA    1 
ATOM   5358  C  C     . ASP A 1 666 ? 149.746 115.896 104.840 1.00 37.66 ?  666 ASP A C     1 
ATOM   5359  O  O     . ASP A 1 666 ? 150.004 116.794 104.031 1.00 40.48 ?  666 ASP A O     1 
ATOM   5360  C  CB    . ASP A 1 666 ? 149.291 113.578 103.988 1.00 40.83 ?  666 ASP A CB    1 
ATOM   5361  C  CG    . ASP A 1 666 ? 149.877 112.232 103.612 1.00 45.35 ?  666 ASP A CG    1 
ATOM   5362  O  OD1   . ASP A 1 666 ? 150.972 112.205 103.013 1.00 45.48 ?  666 ASP A OD1   1 
ATOM   5363  O  OD2   . ASP A 1 666 ? 149.243 111.199 103.915 1.00 45.22 -1 666 ASP A OD2   1 
ATOM   5364  N  N     . LEU A 1 667 ? 148.968 116.103 105.904 1.00 36.21 ?  667 LEU A N     1 
ATOM   5365  C  CA    . LEU A 1 667 ? 148.452 117.435 106.197 1.00 31.15 ?  667 LEU A CA    1 
ATOM   5366  C  C     . LEU A 1 667 ? 149.592 118.403 106.494 1.00 29.82 ?  667 LEU A C     1 
ATOM   5367  O  O     . LEU A 1 667 ? 149.582 119.551 106.034 1.00 34.82 ?  667 LEU A O     1 
ATOM   5368  C  CB    . LEU A 1 667 ? 147.472 117.357 107.370 1.00 34.82 ?  667 LEU A CB    1 
ATOM   5369  C  CG    . LEU A 1 667 ? 146.795 118.602 107.955 1.00 36.50 ?  667 LEU A CG    1 
ATOM   5370  C  CD1   . LEU A 1 667 ? 146.536 119.666 106.900 1.00 35.38 ?  667 LEU A CD1   1 
ATOM   5371  C  CD2   . LEU A 1 667 ? 145.501 118.213 108.646 1.00 32.66 ?  667 LEU A CD2   1 
ATOM   5372  N  N     . ASN A 1 668 ? 150.592 117.949 107.250 1.00 32.07 ?  668 ASN A N     1 
ATOM   5373  C  CA    . ASN A 1 668 ? 151.750 118.791 107.536 1.00 26.94 ?  668 ASN A CA    1 
ATOM   5374  C  C     . ASN A 1 668 ? 152.526 119.113 106.265 1.00 26.92 ?  668 ASN A C     1 
ATOM   5375  O  O     . ASN A 1 668 ? 153.017 120.232 106.100 1.00 33.03 ?  668 ASN A O     1 
ATOM   5376  C  CB    . ASN A 1 668 ? 152.652 118.106 108.560 1.00 27.90 ?  668 ASN A CB    1 
ATOM   5377  C  CG    . ASN A 1 668 ? 152.362 118.549 109.977 1.00 30.77 ?  668 ASN A CG    1 
ATOM   5378  O  OD1   . ASN A 1 668 ? 151.812 119.624 110.203 1.00 31.97 ?  668 ASN A OD1   1 
ATOM   5379  N  ND2   . ASN A 1 668 ? 152.724 117.714 110.942 1.00 37.76 ?  668 ASN A ND2   1 
ATOM   5380  N  N     . ARG A 1 669 ? 152.655 118.140 105.363 1.00 30.35 ?  669 ARG A N     1 
ATOM   5381  C  CA    . ARG A 1 669 ? 153.328 118.384 104.092 1.00 31.14 ?  669 ARG A CA    1 
ATOM   5382  C  C     . ARG A 1 669 ? 152.571 119.406 103.258 1.00 27.39 ?  669 ARG A C     1 
ATOM   5383  O  O     . ARG A 1 669 ? 153.181 120.269 102.620 1.00 31.90 ?  669 ARG A O     1 
ATOM   5384  C  CB    . ARG A 1 669 ? 153.486 117.077 103.318 1.00 29.28 ?  669 ARG A CB    1 
ATOM   5385  C  CG    . ARG A 1 669 ? 154.628 116.203 103.791 1.00 31.02 ?  669 ARG A CG    1 
ATOM   5386  C  CD    . ARG A 1 669 ? 155.108 115.296 102.675 1.00 34.56 ?  669 ARG A CD    1 
ATOM   5387  N  NE    . ARG A 1 669 ? 155.980 115.993 101.739 1.00 33.91 ?  669 ARG A NE    1 
ATOM   5388  C  CZ    . ARG A 1 669 ? 155.875 115.917 100.419 1.00 33.75 ?  669 ARG A CZ    1 
ATOM   5389  N  NH1   . ARG A 1 669 ? 154.938 115.183 99.842  1.00 34.67 1  669 ARG A NH1   1 
ATOM   5390  N  NH2   . ARG A 1 669 ? 156.730 116.596 99.659  1.00 33.28 ?  669 ARG A NH2   1 
ATOM   5391  N  N     . ILE A 1 670 ? 151.240 119.318 103.242 1.00 23.06 ?  670 ILE A N     1 
ATOM   5392  C  CA    . ILE A 1 670 ? 150.444 120.309 102.522 1.00 27.95 ?  670 ILE A CA    1 
ATOM   5393  C  C     . ILE A 1 670 ? 150.640 121.691 103.131 1.00 30.84 ?  670 ILE A C     1 
ATOM   5394  O  O     . ILE A 1 670 ? 150.792 122.685 102.413 1.00 29.03 ?  670 ILE A O     1 
ATOM   5395  C  CB    . ILE A 1 670 ? 148.959 119.902 102.504 1.00 28.07 ?  670 ILE A CB    1 
ATOM   5396  C  CG1   . ILE A 1 670 ? 148.769 118.602 101.723 1.00 30.56 ?  670 ILE A CG1   1 
ATOM   5397  C  CG2   . ILE A 1 670 ? 148.113 121.001 101.885 1.00 27.64 ?  670 ILE A CG2   1 
ATOM   5398  C  CD1   . ILE A 1 670 ? 147.503 117.861 102.075 1.00 29.61 ?  670 ILE A CD1   1 
ATOM   5399  N  N     . ASP A 1 671 ? 150.649 121.776 104.465 1.00 28.70 ?  671 ASP A N     1 
ATOM   5400  C  CA    . ASP A 1 671 ? 150.858 123.062 105.127 1.00 22.91 ?  671 ASP A CA    1 
ATOM   5401  C  C     . ASP A 1 671 ? 152.236 123.635 104.811 1.00 23.48 ?  671 ASP A C     1 
ATOM   5402  O  O     . ASP A 1 671 ? 152.376 124.837 104.556 1.00 25.79 ?  671 ASP A O     1 
ATOM   5403  C  CB    . ASP A 1 671 ? 150.678 122.910 106.638 1.00 26.10 ?  671 ASP A CB    1 
ATOM   5404  C  CG    . ASP A 1 671 ? 149.284 122.452 107.018 1.00 37.56 ?  671 ASP A CG    1 
ATOM   5405  O  OD1   . ASP A 1 671 ? 148.333 122.746 106.265 1.00 36.26 ?  671 ASP A OD1   1 
ATOM   5406  O  OD2   . ASP A 1 671 ? 149.139 121.795 108.071 1.00 37.09 -1 671 ASP A OD2   1 
ATOM   5407  N  N     . LEU A 1 672 ? 153.266 122.788 104.816 1.00 25.36 ?  672 LEU A N     1 
ATOM   5408  C  CA    . LEU A 1 672 ? 154.619 123.258 104.539 1.00 19.20 ?  672 LEU A CA    1 
ATOM   5409  C  C     . LEU A 1 672 ? 154.797 123.643 103.078 1.00 19.80 ?  672 LEU A C     1 
ATOM   5410  O  O     . LEU A 1 672 ? 155.549 124.573 102.773 1.00 25.70 ?  672 LEU A O     1 
ATOM   5411  C  CB    . LEU A 1 672 ? 155.634 122.188 104.935 1.00 22.76 ?  672 LEU A CB    1 
ATOM   5412  C  CG    . LEU A 1 672 ? 155.760 121.929 106.437 1.00 23.94 ?  672 LEU A CG    1 
ATOM   5413  C  CD1   . LEU A 1 672 ? 156.464 120.608 106.700 1.00 19.57 ?  672 LEU A CD1   1 
ATOM   5414  C  CD2   . LEU A 1 672 ? 156.483 123.078 107.119 1.00 21.82 ?  672 LEU A CD2   1 
ATOM   5415  N  N     . TYR A 1 673 ? 154.122 122.946 102.163 1.00 21.30 ?  673 TYR A N     1 
ATOM   5416  C  CA    . TYR A 1 673 ? 154.173 123.329 100.758 1.00 18.93 ?  673 TYR A CA    1 
ATOM   5417  C  C     . TYR A 1 673 ? 153.419 124.630 100.519 1.00 21.16 ?  673 TYR A C     1 
ATOM   5418  O  O     . TYR A 1 673 ? 153.827 125.449 99.689  1.00 24.42 ?  673 TYR A O     1 
ATOM   5419  C  CB    . TYR A 1 673 ? 153.606 122.206 99.890  1.00 14.92 ?  673 TYR A CB    1 
ATOM   5420  C  CG    . TYR A 1 673 ? 153.678 122.483 98.409  1.00 19.19 ?  673 TYR A CG    1 
ATOM   5421  C  CD1   . TYR A 1 673 ? 154.900 122.624 97.770  1.00 18.76 ?  673 TYR A CD1   1 
ATOM   5422  C  CD2   . TYR A 1 673 ? 152.524 122.596 97.648  1.00 18.36 ?  673 TYR A CD2   1 
ATOM   5423  C  CE1   . TYR A 1 673 ? 154.971 122.874 96.418  1.00 23.48 ?  673 TYR A CE1   1 
ATOM   5424  C  CE2   . TYR A 1 673 ? 152.586 122.845 96.296  1.00 21.21 ?  673 TYR A CE2   1 
ATOM   5425  C  CZ    . TYR A 1 673 ? 153.811 122.982 95.686  1.00 25.20 ?  673 TYR A CZ    1 
ATOM   5426  O  OH    . TYR A 1 673 ? 153.880 123.231 94.336  1.00 24.69 ?  673 TYR A OH    1 
ATOM   5427  N  N     . ALA A 1 674 ? 152.309 124.832 101.232 1.00 23.17 ?  674 ALA A N     1 
ATOM   5428  C  CA    . ALA A 1 674 ? 151.603 126.104 101.161 1.00 16.78 ?  674 ALA A CA    1 
ATOM   5429  C  C     . ALA A 1 674 ? 152.473 127.241 101.677 1.00 17.23 ?  674 ALA A C     1 
ATOM   5430  O  O     . ALA A 1 674 ? 152.527 128.316 101.069 1.00 25.24 ?  674 ALA A O     1 
ATOM   5431  C  CB    . ALA A 1 674 ? 150.298 126.017 101.951 1.00 12.27 ?  674 ALA A CB    1 
ATOM   5432  N  N     . HIS A 1 675 ? 153.173 127.018 102.789 1.00 15.67 ?  675 HIS A N     1 
ATOM   5433  C  CA    . HIS A 1 675 ? 154.095 128.030 103.295 1.00 19.64 ?  675 HIS A CA    1 
ATOM   5434  C  C     . HIS A 1 675 ? 155.222 128.292 102.303 1.00 19.45 ?  675 HIS A C     1 
ATOM   5435  O  O     . HIS A 1 675 ? 155.634 129.442 102.110 1.00 24.55 ?  675 HIS A O     1 
ATOM   5436  C  CB    . HIS A 1 675 ? 154.660 127.596 104.646 1.00 18.08 ?  675 HIS A CB    1 
ATOM   5437  C  CG    . HIS A 1 675 ? 155.767 128.470 105.142 1.00 20.55 ?  675 HIS A CG    1 
ATOM   5438  N  ND1   . HIS A 1 675 ? 157.096 128.136 105.007 1.00 28.37 ?  675 HIS A ND1   1 
ATOM   5439  C  CD2   . HIS A 1 675 ? 155.742 129.669 105.768 1.00 18.60 ?  675 HIS A CD2   1 
ATOM   5440  C  CE1   . HIS A 1 675 ? 157.843 129.092 105.531 1.00 23.86 ?  675 HIS A CE1   1 
ATOM   5441  N  NE2   . HIS A 1 675 ? 157.046 130.033 106.000 1.00 24.59 ?  675 HIS A NE2   1 
ATOM   5442  N  N     . HIS A 1 676 ? 155.736 127.236 101.671 1.00 22.03 ?  676 HIS A N     1 
ATOM   5443  C  CA    . HIS A 1 676 ? 156.807 127.395 100.693 1.00 19.91 ?  676 HIS A CA    1 
ATOM   5444  C  C     . HIS A 1 676 ? 156.335 128.164 99.466  1.00 25.51 ?  676 HIS A C     1 
ATOM   5445  O  O     . HIS A 1 676 ? 157.087 128.962 98.897  1.00 25.79 ?  676 HIS A O     1 
ATOM   5446  C  CB    . HIS A 1 676 ? 157.345 126.023 100.288 1.00 23.94 ?  676 HIS A CB    1 
ATOM   5447  C  CG    . HIS A 1 676 ? 158.260 126.056 99.103  1.00 24.67 ?  676 HIS A CG    1 
ATOM   5448  N  ND1   . HIS A 1 676 ? 159.558 126.510 99.178  1.00 22.61 ?  676 HIS A ND1   1 
ATOM   5449  C  CD2   . HIS A 1 676 ? 158.061 125.692 97.816  1.00 25.58 ?  676 HIS A CD2   1 
ATOM   5450  C  CE1   . HIS A 1 676 ? 160.121 126.423 97.986  1.00 29.10 ?  676 HIS A CE1   1 
ATOM   5451  N  NE2   . HIS A 1 676 ? 159.234 125.931 97.142  1.00 27.74 ?  676 HIS A NE2   1 
ATOM   5452  N  N     . ARG A 1 677 ? 155.094 127.940 99.046  1.00 23.74 ?  677 ARG A N     1 
ATOM   5453  C  CA    . ARG A 1 677 ? 154.572 128.526 97.820  1.00 19.41 ?  677 ARG A CA    1 
ATOM   5454  C  C     . ARG A 1 677 ? 154.002 129.923 98.018  1.00 20.49 ?  677 ARG A C     1 
ATOM   5455  O  O     . ARG A 1 677 ? 153.475 130.500 97.061  1.00 27.52 ?  677 ARG A O     1 
ATOM   5456  C  CB    . ARG A 1 677 ? 153.502 127.614 97.215  1.00 22.31 ?  677 ARG A CB    1 
ATOM   5457  C  CG    . ARG A 1 677 ? 154.063 126.479 96.375  1.00 22.58 ?  677 ARG A CG    1 
ATOM   5458  C  CD    . ARG A 1 677 ? 154.623 126.989 95.059  1.00 18.82 ?  677 ARG A CD    1 
ATOM   5459  N  NE    . ARG A 1 677 ? 153.591 127.105 94.035  1.00 26.67 ?  677 ARG A NE    1 
ATOM   5460  C  CZ    . ARG A 1 677 ? 153.245 128.241 93.444  1.00 31.68 ?  677 ARG A CZ    1 
ATOM   5461  N  NH1   . ARG A 1 677 ? 153.833 129.387 93.749  1.00 29.78 1  677 ARG A NH1   1 
ATOM   5462  N  NH2   . ARG A 1 677 ? 152.286 128.228 92.523  1.00 25.25 ?  677 ARG A NH2   1 
ATOM   5463  N  N     . GLY A 1 678 ? 154.094 130.480 99.220  1.00 18.80 ?  678 GLY A N     1 
ATOM   5464  C  CA    . GLY A 1 678 ? 153.610 131.821 99.467  1.00 11.84 ?  678 GLY A CA    1 
ATOM   5465  C  C     . GLY A 1 678 ? 152.166 131.924 99.892  1.00 17.48 ?  678 GLY A C     1 
ATOM   5466  O  O     . GLY A 1 678 ? 151.587 133.012 99.801  1.00 21.36 ?  678 GLY A O     1 
ATOM   5467  N  N     . ILE A 1 679 ? 151.559 130.828 100.346 1.00 18.57 ?  679 ILE A N     1 
ATOM   5468  C  CA    . ILE A 1 679 ? 150.191 130.883 100.843 1.00 11.37 ?  679 ILE A CA    1 
ATOM   5469  C  C     . ILE A 1 679 ? 150.163 131.683 102.135 1.00 13.32 ?  679 ILE A C     1 
ATOM   5470  O  O     . ILE A 1 679 ? 150.970 131.454 103.045 1.00 29.23 ?  679 ILE A O     1 
ATOM   5471  C  CB    . ILE A 1 679 ? 149.631 129.468 101.046 1.00 16.02 ?  679 ILE A CB    1 
ATOM   5472  C  CG1   . ILE A 1 679 ? 149.451 128.769 99.698  1.00 13.20 ?  679 ILE A CG1   1 
ATOM   5473  C  CG2   . ILE A 1 679 ? 148.324 129.505 101.817 1.00 14.77 ?  679 ILE A CG2   1 
ATOM   5474  C  CD1   . ILE A 1 679 ? 148.531 129.490 98.765  1.00 13.30 ?  679 ILE A CD1   1 
ATOM   5475  N  N     . LYS A 1 680 ? 149.236 132.636 102.218 1.00 9.75  ?  680 LYS A N     1 
ATOM   5476  C  CA    . LYS A 1 680 ? 149.181 133.517 103.377 1.00 6.25  ?  680 LYS A CA    1 
ATOM   5477  C  C     . LYS A 1 680 ? 148.433 132.872 104.538 1.00 5.30  ?  680 LYS A C     1 
ATOM   5478  O  O     . LYS A 1 680 ? 148.896 132.913 105.681 1.00 17.26 ?  680 LYS A O     1 
ATOM   5479  C  CB    . LYS A 1 680 ? 148.532 134.844 102.987 1.00 8.74  ?  680 LYS A CB    1 
ATOM   5480  C  CG    . LYS A 1 680 ? 149.349 135.677 102.020 1.00 0.00  ?  680 LYS A CG    1 
ATOM   5481  C  CD    . LYS A 1 680 ? 148.712 137.035 101.812 1.00 5.72  ?  680 LYS A CD    1 
ATOM   5482  C  CE    . LYS A 1 680 ? 149.398 137.806 100.710 1.00 9.99  ?  680 LYS A CE    1 
ATOM   5483  N  NZ    . LYS A 1 680 ? 148.806 139.155 100.540 1.00 15.99 1  680 LYS A NZ    1 
ATOM   5484  N  N     . THR A 1 681 ? 147.277 132.272 104.264 1.00 10.68 ?  681 THR A N     1 
ATOM   5485  C  CA    . THR A 1 681 ? 146.457 131.659 105.297 1.00 8.05  ?  681 THR A CA    1 
ATOM   5486  C  C     . THR A 1 681 ? 145.895 130.341 104.790 1.00 14.02 ?  681 THR A C     1 
ATOM   5487  O  O     . THR A 1 681 ? 145.694 130.154 103.588 1.00 25.07 ?  681 THR A O     1 
ATOM   5488  C  CB    . THR A 1 681 ? 145.297 132.574 105.731 1.00 14.36 ?  681 THR A CB    1 
ATOM   5489  O  OG1   . THR A 1 681 ? 144.622 133.082 104.573 1.00 21.48 ?  681 THR A OG1   1 
ATOM   5490  C  CG2   . THR A 1 681 ? 145.803 133.737 106.567 1.00 11.98 ?  681 THR A CG2   1 
ATOM   5491  N  N     . ILE A 1 682 ? 145.639 129.428 105.723 1.00 10.50 ?  682 ILE A N     1 
ATOM   5492  C  CA    . ILE A 1 682 ? 144.939 128.179 105.450 1.00 11.42 ?  682 ILE A CA    1 
ATOM   5493  C  C     . ILE A 1 682 ? 143.688 128.151 106.314 1.00 14.42 ?  682 ILE A C     1 
ATOM   5494  O  O     . ILE A 1 682 ? 143.773 128.277 107.541 1.00 15.39 ?  682 ILE A O     1 
ATOM   5495  C  CB    . ILE A 1 682 ? 145.822 126.949 105.723 1.00 16.27 ?  682 ILE A CB    1 
ATOM   5496  C  CG1   . ILE A 1 682 ? 147.180 127.099 105.038 1.00 17.97 ?  682 ILE A CG1   1 
ATOM   5497  C  CG2   . ILE A 1 682 ? 145.132 125.697 105.245 1.00 19.16 ?  682 ILE A CG2   1 
ATOM   5498  C  CD1   . ILE A 1 682 ? 148.087 125.908 105.221 1.00 19.40 ?  682 ILE A CD1   1 
ATOM   5499  N  N     . TYR A 1 683 ? 142.528 127.991 105.677 1.00 16.60 ?  683 TYR A N     1 
ATOM   5500  C  CA    . TYR A 1 683 ? 141.261 128.156 106.390 1.00 11.86 ?  683 TYR A CA    1 
ATOM   5501  C  C     . TYR A 1 683 ? 140.849 126.888 107.133 1.00 23.72 ?  683 TYR A C     1 
ATOM   5502  O  O     . TYR A 1 683 ? 140.823 126.856 108.365 1.00 33.70 ?  683 TYR A O     1 
ATOM   5503  C  CB    . TYR A 1 683 ? 140.168 128.582 105.404 1.00 18.22 ?  683 TYR A CB    1 
ATOM   5504  C  CG    . TYR A 1 683 ? 138.853 128.945 106.049 1.00 15.29 ?  683 TYR A CG    1 
ATOM   5505  C  CD1   . TYR A 1 683 ? 138.800 129.392 107.361 1.00 15.83 ?  683 TYR A CD1   1 
ATOM   5506  C  CD2   . TYR A 1 683 ? 137.663 128.852 105.340 1.00 13.23 ?  683 TYR A CD2   1 
ATOM   5507  C  CE1   . TYR A 1 683 ? 137.605 129.725 107.951 1.00 19.36 ?  683 TYR A CE1   1 
ATOM   5508  C  CE2   . TYR A 1 683 ? 136.460 129.188 105.924 1.00 18.00 ?  683 TYR A CE2   1 
ATOM   5509  C  CZ    . TYR A 1 683 ? 136.438 129.624 107.230 1.00 20.89 ?  683 TYR A CZ    1 
ATOM   5510  O  OH    . TYR A 1 683 ? 135.243 129.960 107.821 1.00 28.35 ?  683 TYR A OH    1 
ATOM   5511  N  N     . TYR A 1 684 ? 140.552 125.825 106.402 1.00 31.22 ?  684 TYR A N     1 
ATOM   5512  C  CA    . TYR A 1 684 ? 139.935 124.653 106.998 1.00 24.27 ?  684 TYR A CA    1 
ATOM   5513  C  C     . TYR A 1 684 ? 140.601 123.392 106.484 1.00 33.98 ?  684 TYR A C     1 
ATOM   5514  O  O     . TYR A 1 684 ? 141.085 123.341 105.350 1.00 35.72 ?  684 TYR A O     1 
ATOM   5515  C  CB    . TYR A 1 684 ? 138.433 124.595 106.700 1.00 27.98 ?  684 TYR A CB    1 
ATOM   5516  C  CG    . TYR A 1 684 ? 137.570 125.186 107.788 1.00 25.86 ?  684 TYR A CG    1 
ATOM   5517  C  CD1   . TYR A 1 684 ? 137.840 124.938 109.125 1.00 28.64 ?  684 TYR A CD1   1 
ATOM   5518  C  CD2   . TYR A 1 684 ? 136.484 125.990 107.478 1.00 27.48 ?  684 TYR A CD2   1 
ATOM   5519  C  CE1   . TYR A 1 684 ? 137.055 125.475 110.123 1.00 32.74 ?  684 TYR A CE1   1 
ATOM   5520  C  CE2   . TYR A 1 684 ? 135.694 126.534 108.467 1.00 26.81 ?  684 TYR A CE2   1 
ATOM   5521  C  CZ    . TYR A 1 684 ? 135.983 126.274 109.788 1.00 33.03 ?  684 TYR A CZ    1 
ATOM   5522  O  OH    . TYR A 1 684 ? 135.197 126.812 110.779 1.00 36.74 ?  684 TYR A OH    1 
ATOM   5523  N  N     . ALA A 1 685 ? 140.624 122.378 107.337 1.00 33.01 ?  685 ALA A N     1 
ATOM   5524  C  CA    . ALA A 1 685 ? 141.064 121.038 106.973 1.00 30.94 ?  685 ALA A CA    1 
ATOM   5525  C  C     . ALA A 1 685 ? 139.810 120.169 106.936 1.00 33.77 ?  685 ALA A C     1 
ATOM   5526  O  O     . ALA A 1 685 ? 139.466 119.506 107.914 1.00 41.20 ?  685 ALA A O     1 
ATOM   5527  C  CB    . ALA A 1 685 ? 142.097 120.511 107.957 1.00 31.56 ?  685 ALA A CB    1 
ATOM   5528  N  N     . ARG A 1 686 ? 139.126 120.185 105.796 1.00 34.12 ?  686 ARG A N     1 
ATOM   5529  C  CA    . ARG A 1 686 ? 137.903 119.418 105.615 1.00 35.47 ?  686 ARG A CA    1 
ATOM   5530  C  C     . ARG A 1 686 ? 138.247 118.004 105.170 1.00 39.33 ?  686 ARG A C     1 
ATOM   5531  O  O     . ARG A 1 686 ? 138.981 117.814 104.195 1.00 41.11 ?  686 ARG A O     1 
ATOM   5532  C  CB    . ARG A 1 686 ? 136.990 120.086 104.587 1.00 38.70 ?  686 ARG A CB    1 
ATOM   5533  C  CG    . ARG A 1 686 ? 136.192 121.252 105.132 1.00 41.76 ?  686 ARG A CG    1 
ATOM   5534  C  CD    . ARG A 1 686 ? 134.912 121.441 104.343 1.00 42.10 ?  686 ARG A CD    1 
ATOM   5535  N  NE    . ARG A 1 686 ? 134.183 120.188 104.193 1.00 43.83 ?  686 ARG A NE    1 
ATOM   5536  C  CZ    . ARG A 1 686 ? 132.890 120.039 104.444 1.00 44.76 ?  686 ARG A CZ    1 
ATOM   5537  N  NH1   . ARG A 1 686 ? 132.146 121.053 104.852 1.00 42.57 1  686 ARG A NH1   1 
ATOM   5538  N  NH2   . ARG A 1 686 ? 132.331 118.844 104.283 1.00 43.63 ?  686 ARG A NH2   1 
ATOM   5539  N  N     . THR A 1 687 ? 137.715 117.019 105.883 1.00 44.90 ?  687 THR A N     1 
ATOM   5540  C  CA    . THR A 1 687 ? 137.997 115.618 105.616 1.00 47.74 ?  687 THR A CA    1 
ATOM   5541  C  C     . THR A 1 687 ? 136.725 114.909 105.173 1.00 46.02 ?  687 THR A C     1 
ATOM   5542  O  O     . THR A 1 687 ? 135.649 115.135 105.735 1.00 49.65 ?  687 THR A O     1 
ATOM   5543  C  CB    . THR A 1 687 ? 138.580 114.934 106.857 1.00 47.73 ?  687 THR A CB    1 
ATOM   5544  O  OG1   . THR A 1 687 ? 139.796 115.589 107.237 1.00 47.03 ?  687 THR A OG1   1 
ATOM   5545  C  CG2   . THR A 1 687 ? 138.882 113.480 106.569 1.00 47.44 ?  687 THR A CG2   1 
ATOM   5546  N  N     . LYS A 1 688 ? 136.850 114.061 104.157 1.00 44.89 ?  688 LYS A N     1 
ATOM   5547  C  CA    . LYS A 1 688 ? 135.717 113.293 103.656 1.00 50.69 ?  688 LYS A CA    1 
ATOM   5548  C  C     . LYS A 1 688 ? 135.783 111.850 104.145 1.00 54.40 ?  688 LYS A C     1 
ATOM   5549  O  O     . LYS A 1 688 ? 136.847 111.360 104.519 1.00 56.78 ?  688 LYS A O     1 
ATOM   5550  C  CB    . LYS A 1 688 ? 135.673 113.330 102.128 1.00 49.89 ?  688 LYS A CB    1 
ATOM   5551  C  CG    . LYS A 1 688 ? 136.582 112.315 101.457 1.00 49.17 ?  688 LYS A CG    1 
ATOM   5552  C  CD    . LYS A 1 688 ? 136.110 111.984 100.050 1.00 51.52 ?  688 LYS A CD    1 
ATOM   5553  C  CE    . LYS A 1 688 ? 134.596 111.877 99.973  1.00 51.01 ?  688 LYS A CE    1 
ATOM   5554  N  NZ    . LYS A 1 688 ? 134.143 111.487 98.609  1.00 50.48 ?  688 LYS A NZ    1 
ATOM   5555  N  N     . VAL B 1 6   ? 155.061 117.118 164.594 1.00 58.06 ?  6   VAL B N     1 
ATOM   5556  C  CA    . VAL B 1 6   ? 153.958 117.853 165.201 1.00 60.47 ?  6   VAL B CA    1 
ATOM   5557  C  C     . VAL B 1 6   ? 154.492 118.967 166.093 1.00 60.85 ?  6   VAL B C     1 
ATOM   5558  O  O     . VAL B 1 6   ? 155.268 118.713 167.015 1.00 56.42 ?  6   VAL B O     1 
ATOM   5559  C  CB    . VAL B 1 6   ? 153.033 116.914 165.992 1.00 59.34 ?  6   VAL B CB    1 
ATOM   5560  C  CG1   . VAL B 1 6   ? 151.827 117.676 166.512 1.00 55.45 ?  6   VAL B CG1   1 
ATOM   5561  C  CG2   . VAL B 1 6   ? 152.596 115.746 165.125 1.00 59.30 ?  6   VAL B CG2   1 
ATOM   5562  N  N     . PRO B 1 7   ? 154.083 120.203 165.809 1.00 59.15 ?  7   PRO B N     1 
ATOM   5563  C  CA    . PRO B 1 7   ? 154.555 121.339 166.610 1.00 53.13 ?  7   PRO B CA    1 
ATOM   5564  C  C     . PRO B 1 7   ? 154.118 121.228 168.062 1.00 55.56 ?  7   PRO B C     1 
ATOM   5565  O  O     . PRO B 1 7   ? 153.091 120.628 168.384 1.00 60.63 ?  7   PRO B O     1 
ATOM   5566  C  CB    . PRO B 1 7   ? 153.911 122.551 165.931 1.00 52.80 ?  7   PRO B CB    1 
ATOM   5567  C  CG    . PRO B 1 7   ? 153.529 122.106 164.574 1.00 56.23 ?  7   PRO B CG    1 
ATOM   5568  C  CD    . PRO B 1 7   ? 153.390 120.618 164.578 1.00 56.88 ?  7   PRO B CD    1 
ATOM   5569  N  N     . LYS B 1 8   ? 154.929 121.812 168.948 1.00 55.11 ?  8   LYS B N     1 
ATOM   5570  C  CA    . LYS B 1 8   ? 154.631 121.764 170.376 1.00 54.87 ?  8   LYS B CA    1 
ATOM   5571  C  C     . LYS B 1 8   ? 153.318 122.464 170.694 1.00 57.26 ?  8   LYS B C     1 
ATOM   5572  O  O     . LYS B 1 8   ? 152.514 121.962 171.490 1.00 59.71 ?  8   LYS B O     1 
ATOM   5573  C  CB    . LYS B 1 8   ? 155.776 122.390 171.171 1.00 55.07 ?  8   LYS B CB    1 
ATOM   5574  C  CG    . LYS B 1 8   ? 155.795 121.998 172.639 1.00 55.73 ?  8   LYS B CG    1 
ATOM   5575  C  CD    . LYS B 1 8   ? 156.302 123.137 173.508 1.00 56.79 ?  8   LYS B CD    1 
ATOM   5576  C  CE    . LYS B 1 8   ? 155.660 123.107 174.885 1.00 58.05 ?  8   LYS B CE    1 
ATOM   5577  N  NZ    . LYS B 1 8   ? 156.502 123.788 175.906 1.00 56.65 1  8   LYS B NZ    1 
ATOM   5578  N  N     . TRP B 1 9   ? 153.079 123.627 170.083 1.00 58.22 ?  9   TRP B N     1 
ATOM   5579  C  CA    . TRP B 1 9   ? 151.821 124.327 170.312 1.00 51.60 ?  9   TRP B CA    1 
ATOM   5580  C  C     . TRP B 1 9   ? 150.639 123.550 169.751 1.00 51.94 ?  9   TRP B C     1 
ATOM   5581  O  O     . TRP B 1 9   ? 149.545 123.598 170.319 1.00 58.14 ?  9   TRP B O     1 
ATOM   5582  C  CB    . TRP B 1 9   ? 151.869 125.728 169.705 1.00 50.43 ?  9   TRP B CB    1 
ATOM   5583  C  CG    . TRP B 1 9   ? 152.219 125.763 168.250 1.00 48.99 ?  9   TRP B CG    1 
ATOM   5584  C  CD1   . TRP B 1 9   ? 151.351 125.722 167.201 1.00 48.05 ?  9   TRP B CD1   1 
ATOM   5585  C  CD2   . TRP B 1 9   ? 153.529 125.876 167.684 1.00 48.63 ?  9   TRP B CD2   1 
ATOM   5586  N  NE1   . TRP B 1 9   ? 152.039 125.790 166.015 1.00 47.61 ?  9   TRP B NE1   1 
ATOM   5587  C  CE2   . TRP B 1 9   ? 153.378 125.887 166.285 1.00 50.20 ?  9   TRP B CE2   1 
ATOM   5588  C  CE3   . TRP B 1 9   ? 154.814 125.962 168.225 1.00 45.96 ?  9   TRP B CE3   1 
ATOM   5589  C  CZ2   . TRP B 1 9   ? 154.463 125.979 165.418 1.00 49.91 ?  9   TRP B CZ2   1 
ATOM   5590  C  CZ3   . TRP B 1 9   ? 155.889 126.055 167.363 1.00 51.15 ?  9   TRP B CZ3   1 
ATOM   5591  C  CH2   . TRP B 1 9   ? 155.707 126.062 165.977 1.00 51.69 ?  9   TRP B CH2   1 
ATOM   5592  N  N     . ILE B 1 10  ? 150.835 122.835 168.642 1.00 52.13 ?  10  ILE B N     1 
ATOM   5593  C  CA    . ILE B 1 10  ? 149.758 122.016 168.097 1.00 53.51 ?  10  ILE B CA    1 
ATOM   5594  C  C     . ILE B 1 10  ? 149.439 120.863 169.039 1.00 54.08 ?  10  ILE B C     1 
ATOM   5595  O  O     . ILE B 1 10  ? 148.269 120.521 169.251 1.00 56.39 ?  10  ILE B O     1 
ATOM   5596  C  CB    . ILE B 1 10  ? 150.126 121.523 166.686 1.00 54.76 ?  10  ILE B CB    1 
ATOM   5597  C  CG1   . ILE B 1 10  ? 149.947 122.648 165.664 1.00 53.72 ?  10  ILE B CG1   1 
ATOM   5598  C  CG2   . ILE B 1 10  ? 149.274 120.330 166.295 1.00 55.30 ?  10  ILE B CG2   1 
ATOM   5599  C  CD1   . ILE B 1 10  ? 148.736 123.520 165.909 1.00 54.18 ?  10  ILE B CD1   1 
ATOM   5600  N  N     . GLN B 1 11  ? 150.469 120.249 169.627 1.00 57.56 ?  11  GLN B N     1 
ATOM   5601  C  CA    . GLN B 1 11  ? 150.235 119.205 170.618 1.00 57.04 ?  11  GLN B CA    1 
ATOM   5602  C  C     . GLN B 1 11  ? 149.498 119.754 171.832 1.00 59.28 ?  11  GLN B C     1 
ATOM   5603  O  O     . GLN B 1 11  ? 148.538 119.140 172.311 1.00 60.20 ?  11  GLN B O     1 
ATOM   5604  C  CB    . GLN B 1 11  ? 151.559 118.572 171.047 1.00 56.99 ?  11  GLN B CB    1 
ATOM   5605  C  CG    . GLN B 1 11  ? 152.034 117.441 170.155 1.00 60.82 ?  11  GLN B CG    1 
ATOM   5606  C  CD    . GLN B 1 11  ? 153.545 117.330 170.122 1.00 62.31 ?  11  GLN B CD    1 
ATOM   5607  O  OE1   . GLN B 1 11  ? 154.139 117.091 169.071 1.00 61.39 ?  11  GLN B OE1   1 
ATOM   5608  N  NE2   . GLN B 1 11  ? 154.177 117.507 171.276 1.00 60.14 ?  11  GLN B NE2   1 
ATOM   5609  N  N     . LEU B 1 12  ? 149.926 120.914 172.335 1.00 58.79 ?  12  LEU B N     1 
ATOM   5610  C  CA    . LEU B 1 12  ? 149.277 121.500 173.505 1.00 54.13 ?  12  LEU B CA    1 
ATOM   5611  C  C     . LEU B 1 12  ? 147.825 121.856 173.213 1.00 57.99 ?  12  LEU B C     1 
ATOM   5612  O  O     . LEU B 1 12  ? 146.946 121.659 174.060 1.00 60.10 ?  12  LEU B O     1 
ATOM   5613  C  CB    . LEU B 1 12  ? 150.046 122.735 173.969 1.00 55.26 ?  12  LEU B CB    1 
ATOM   5614  C  CG    . LEU B 1 12  ? 151.171 122.492 174.975 1.00 58.07 ?  12  LEU B CG    1 
ATOM   5615  C  CD1   . LEU B 1 12  ? 152.022 123.739 175.127 1.00 58.53 ?  12  LEU B CD1   1 
ATOM   5616  C  CD2   . LEU B 1 12  ? 150.605 122.059 176.313 1.00 56.30 ?  12  LEU B CD2   1 
ATOM   5617  N  N     . ASN B 1 13  ? 147.556 122.391 172.021 1.00 53.89 ?  13  ASN B N     1 
ATOM   5618  C  CA    . ASN B 1 13  ? 146.186 122.710 171.640 1.00 52.68 ?  13  ASN B CA    1 
ATOM   5619  C  C     . ASN B 1 13  ? 145.348 121.445 171.497 1.00 56.13 ?  13  ASN B C     1 
ATOM   5620  O  O     . ASN B 1 13  ? 144.133 121.469 171.723 1.00 62.41 ?  13  ASN B O     1 
ATOM   5621  C  CB    . ASN B 1 13  ? 146.186 123.515 170.341 1.00 53.91 ?  13  ASN B CB    1 
ATOM   5622  C  CG    . ASN B 1 13  ? 144.802 123.675 169.752 1.00 53.99 ?  13  ASN B CG    1 
ATOM   5623  O  OD1   . ASN B 1 13  ? 144.389 122.901 168.890 1.00 55.79 ?  13  ASN B OD1   1 
ATOM   5624  N  ND2   . ASN B 1 13  ? 144.075 124.685 170.214 1.00 54.99 ?  13  ASN B ND2   1 
ATOM   5625  N  N     . ASN B 1 14  ? 145.980 120.331 171.125 1.00 59.08 ?  14  ASN B N     1 
ATOM   5626  C  CA    . ASN B 1 14  ? 145.255 119.075 170.981 1.00 55.76 ?  14  ASN B CA    1 
ATOM   5627  C  C     . ASN B 1 14  ? 144.932 118.429 172.322 1.00 58.53 ?  14  ASN B C     1 
ATOM   5628  O  O     . ASN B 1 14  ? 144.082 117.536 172.372 1.00 63.28 ?  14  ASN B O     1 
ATOM   5629  C  CB    . ASN B 1 14  ? 146.056 118.104 170.116 1.00 59.59 ?  14  ASN B CB    1 
ATOM   5630  C  CG    . ASN B 1 14  ? 145.928 118.402 168.636 1.00 59.07 ?  14  ASN B CG    1 
ATOM   5631  O  OD1   . ASN B 1 14  ? 145.621 119.525 168.242 1.00 59.30 ?  14  ASN B OD1   1 
ATOM   5632  N  ND2   . ASN B 1 14  ? 146.163 117.392 167.808 1.00 58.70 ?  14  ASN B ND2   1 
ATOM   5633  N  N     . GLU B 1 15  ? 145.581 118.859 173.406 1.00 59.48 ?  15  GLU B N     1 
ATOM   5634  C  CA    . GLU B 1 15  ? 145.291 118.308 174.724 1.00 59.95 ?  15  GLU B CA    1 
ATOM   5635  C  C     . GLU B 1 15  ? 144.005 118.856 175.327 1.00 61.82 ?  15  GLU B C     1 
ATOM   5636  O  O     . GLU B 1 15  ? 143.614 118.412 176.411 1.00 64.87 ?  15  GLU B O     1 
ATOM   5637  C  CB    . GLU B 1 15  ? 146.451 118.571 175.689 1.00 60.50 ?  15  GLU B CB    1 
ATOM   5638  C  CG    . GLU B 1 15  ? 147.816 118.203 175.145 1.00 62.55 ?  15  GLU B CG    1 
ATOM   5639  C  CD    . GLU B 1 15  ? 148.898 118.259 176.204 1.00 66.42 ?  15  GLU B CD    1 
ATOM   5640  O  OE1   . GLU B 1 15  ? 148.557 118.233 177.404 1.00 64.42 ?  15  GLU B OE1   1 
ATOM   5641  O  OE2   . GLU B 1 15  ? 150.090 118.331 175.836 1.00 66.45 -1 15  GLU B OE2   1 
ATOM   5642  N  N     . ILE B 1 16  ? 143.353 119.814 174.667 1.00 60.94 ?  16  ILE B N     1 
ATOM   5643  C  CA    . ILE B 1 16  ? 142.058 120.289 175.141 1.00 60.27 ?  16  ILE B CA    1 
ATOM   5644  C  C     . ILE B 1 16  ? 141.034 119.163 175.099 1.00 60.83 ?  16  ILE B C     1 
ATOM   5645  O  O     . ILE B 1 16  ? 140.254 118.975 176.040 1.00 61.27 ?  16  ILE B O     1 
ATOM   5646  C  CB    . ILE B 1 16  ? 141.599 121.506 174.318 1.00 61.94 ?  16  ILE B CB    1 
ATOM   5647  C  CG1   . ILE B 1 16  ? 142.682 122.586 174.318 1.00 60.80 ?  16  ILE B CG1   1 
ATOM   5648  C  CG2   . ILE B 1 16  ? 140.289 122.054 174.861 1.00 60.34 ?  16  ILE B CG2   1 
ATOM   5649  C  CD1   . ILE B 1 16  ? 142.185 123.950 173.907 1.00 58.23 ?  16  ILE B CD1   1 
ATOM   5650  N  N     . MET B 1 17  ? 141.024 118.393 174.008 1.00 62.13 ?  17  MET B N     1 
ATOM   5651  C  CA    . MET B 1 17  ? 140.071 117.298 173.877 1.00 63.00 ?  17  MET B CA    1 
ATOM   5652  C  C     . MET B 1 17  ? 140.386 116.134 174.805 1.00 63.88 ?  17  MET B C     1 
ATOM   5653  O  O     . MET B 1 17  ? 139.488 115.340 175.104 1.00 65.86 ?  17  MET B O     1 
ATOM   5654  C  CB    . MET B 1 17  ? 140.027 116.805 172.431 1.00 63.13 ?  17  MET B CB    1 
ATOM   5655  C  CG    . MET B 1 17  ? 139.803 117.867 171.347 1.00 63.32 ?  17  MET B CG    1 
ATOM   5656  S  SD    . MET B 1 17  ? 138.213 118.737 171.242 1.00 70.70 ?  17  MET B SD    1 
ATOM   5657  C  CE    . MET B 1 17  ? 138.210 119.800 172.681 1.00 62.37 ?  17  MET B CE    1 
ATOM   5658  N  N     . ILE B 1 18  ? 141.632 116.005 175.257 1.00 63.36 ?  18  ILE B N     1 
ATOM   5659  C  CA    . ILE B 1 18  ? 141.967 114.972 176.232 1.00 63.14 ?  18  ILE B CA    1 
ATOM   5660  C  C     . ILE B 1 18  ? 141.278 115.346 177.540 1.00 63.69 ?  18  ILE B C     1 
ATOM   5661  O  O     . ILE B 1 18  ? 141.642 116.332 178.189 1.00 64.62 ?  18  ILE B O     1 
ATOM   5662  C  CB    . ILE B 1 18  ? 143.483 114.823 176.411 1.00 63.13 ?  18  ILE B CB    1 
ATOM   5663  C  CG1   . ILE B 1 18  ? 144.086 113.985 175.280 1.00 62.85 ?  18  ILE B CG1   1 
ATOM   5664  C  CG2   . ILE B 1 18  ? 143.803 114.155 177.740 1.00 63.54 ?  18  ILE B CG2   1 
ATOM   5665  C  CD1   . ILE B 1 18  ? 144.217 114.704 173.955 1.00 62.27 ?  18  ILE B CD1   1 
ATOM   5666  N  N     . GLN B 1 19  ? 140.263 114.575 177.917 1.00 68.67 ?  19  GLN B N     1 
ATOM   5667  C  CA    . GLN B 1 19  ? 139.435 114.909 179.068 1.00 69.55 ?  19  GLN B CA    1 
ATOM   5668  C  C     . GLN B 1 19  ? 140.126 114.454 180.346 1.00 70.48 ?  19  GLN B C     1 
ATOM   5669  O  O     . GLN B 1 19  ? 140.358 113.257 180.544 1.00 71.79 ?  19  GLN B O     1 
ATOM   5670  C  CB    . GLN B 1 19  ? 138.058 114.265 178.933 1.00 70.06 ?  19  GLN B CB    1 
ATOM   5671  C  CG    . GLN B 1 19  ? 137.085 115.070 178.088 1.00 69.09 ?  19  GLN B CG    1 
ATOM   5672  C  CD    . GLN B 1 19  ? 135.682 115.073 178.657 1.00 72.31 ?  19  GLN B CD    1 
ATOM   5673  O  OE1   . GLN B 1 19  ? 135.461 114.671 179.798 1.00 72.66 ?  19  GLN B OE1   1 
ATOM   5674  N  NE2   . GLN B 1 19  ? 134.722 115.531 177.860 1.00 69.92 ?  19  GLN B NE2   1 
ATOM   5675  N  N     . LYS B 1 20  ? 140.456 115.409 181.209 1.00 74.71 ?  20  LYS B N     1 
ATOM   5676  C  CA    . LYS B 1 20  ? 141.070 115.135 182.501 1.00 74.45 ?  20  LYS B CA    1 
ATOM   5677  C  C     . LYS B 1 20  ? 140.052 115.436 183.591 1.00 77.20 ?  20  LYS B C     1 
ATOM   5678  O  O     . LYS B 1 20  ? 139.501 116.542 183.641 1.00 74.44 ?  20  LYS B O     1 
ATOM   5679  C  CB    . LYS B 1 20  ? 142.336 115.969 182.693 1.00 71.73 ?  20  LYS B CB    1 
ATOM   5680  C  CG    . LYS B 1 20  ? 143.043 115.729 184.016 1.00 74.91 ?  20  LYS B CG    1 
ATOM   5681  C  CD    . LYS B 1 20  ? 143.838 116.950 184.454 1.00 75.30 ?  20  LYS B CD    1 
ATOM   5682  C  CE    . LYS B 1 20  ? 142.943 118.165 184.622 1.00 76.62 ?  20  LYS B CE    1 
ATOM   5683  N  NZ    . LYS B 1 20  ? 141.692 117.840 185.361 1.00 78.76 1  20  LYS B NZ    1 
ATOM   5684  N  N     . ASP B 1 21  ? 139.802 114.450 184.456 1.00 82.99 ?  21  ASP B N     1 
ATOM   5685  C  CA    . ASP B 1 21  ? 138.832 114.571 185.545 1.00 82.58 ?  21  ASP B CA    1 
ATOM   5686  C  C     . ASP B 1 21  ? 137.438 114.902 185.014 1.00 82.92 ?  21  ASP B C     1 
ATOM   5687  O  O     . ASP B 1 21  ? 136.682 115.661 185.624 1.00 82.22 ?  21  ASP B O     1 
ATOM   5688  C  CB    . ASP B 1 21  ? 139.286 115.608 186.578 1.00 82.38 ?  21  ASP B CB    1 
ATOM   5689  C  CG    . ASP B 1 21  ? 138.573 115.459 187.909 1.00 84.51 ?  21  ASP B CG    1 
ATOM   5690  O  OD1   . ASP B 1 21  ? 138.353 114.308 188.341 1.00 82.89 ?  21  ASP B OD1   1 
ATOM   5691  O  OD2   . ASP B 1 21  ? 138.232 116.493 188.521 1.00 84.64 -1 21  ASP B OD2   1 
ATOM   5692  N  N     . GLY B 1 22  ? 137.095 114.328 183.862 1.00 75.34 ?  22  GLY B N     1 
ATOM   5693  C  CA    . GLY B 1 22  ? 135.777 114.510 183.289 1.00 74.48 ?  22  GLY B CA    1 
ATOM   5694  C  C     . GLY B 1 22  ? 135.522 115.858 182.657 1.00 76.15 ?  22  GLY B C     1 
ATOM   5695  O  O     . GLY B 1 22  ? 134.368 116.161 182.333 1.00 75.95 ?  22  GLY B O     1 
ATOM   5696  N  N     . LYS B 1 23  ? 136.554 116.678 182.472 1.00 72.59 ?  23  LYS B N     1 
ATOM   5697  C  CA    . LYS B 1 23  ? 136.404 118.004 181.896 1.00 69.37 ?  23  LYS B CA    1 
ATOM   5698  C  C     . LYS B 1 23  ? 137.484 118.240 180.851 1.00 70.04 ?  23  LYS B C     1 
ATOM   5699  O  O     . LYS B 1 23  ? 138.590 117.700 180.944 1.00 69.80 ?  23  LYS B O     1 
ATOM   5700  C  CB    . LYS B 1 23  ? 136.485 119.098 182.968 1.00 68.27 ?  23  LYS B CB    1 
ATOM   5701  C  CG    . LYS B 1 23  ? 135.361 119.068 183.986 1.00 68.38 ?  23  LYS B CG    1 
ATOM   5702  C  CD    . LYS B 1 23  ? 135.491 120.222 184.962 1.00 68.60 ?  23  LYS B CD    1 
ATOM   5703  C  CE    . LYS B 1 23  ? 134.458 120.137 186.070 1.00 69.97 ?  23  LYS B CE    1 
ATOM   5704  N  NZ    . LYS B 1 23  ? 134.677 121.186 187.102 1.00 68.39 1  23  LYS B NZ    1 
ATOM   5705  N  N     . PHE B 1 24  ? 137.150 119.053 179.851 1.00 65.61 ?  24  PHE B N     1 
ATOM   5706  C  CA    . PHE B 1 24  ? 138.141 119.464 178.869 1.00 62.62 ?  24  PHE B CA    1 
ATOM   5707  C  C     . PHE B 1 24  ? 139.210 120.323 179.533 1.00 61.66 ?  24  PHE B C     1 
ATOM   5708  O  O     . PHE B 1 24  ? 138.940 121.080 180.468 1.00 61.85 ?  24  PHE B O     1 
ATOM   5709  C  CB    . PHE B 1 24  ? 137.485 120.247 177.731 1.00 61.12 ?  24  PHE B CB    1 
ATOM   5710  C  CG    . PHE B 1 24  ? 136.516 119.443 176.916 1.00 61.30 ?  24  PHE B CG    1 
ATOM   5711  C  CD1   . PHE B 1 24  ? 136.941 118.752 175.796 1.00 64.24 ?  24  PHE B CD1   1 
ATOM   5712  C  CD2   . PHE B 1 24  ? 135.176 119.395 177.258 1.00 61.65 ?  24  PHE B CD2   1 
ATOM   5713  C  CE1   . PHE B 1 24  ? 136.050 118.017 175.040 1.00 64.73 ?  24  PHE B CE1   1 
ATOM   5714  C  CE2   . PHE B 1 24  ? 134.281 118.661 176.504 1.00 62.37 ?  24  PHE B CE2   1 
ATOM   5715  C  CZ    . PHE B 1 24  ? 134.719 117.971 175.394 1.00 61.31 ?  24  PHE B CZ    1 
ATOM   5716  N  N     . GLN B 1 25  ? 140.442 120.198 179.041 1.00 62.73 ?  25  GLN B N     1 
ATOM   5717  C  CA    . GLN B 1 25  ? 141.558 120.992 179.556 1.00 63.64 ?  25  GLN B CA    1 
ATOM   5718  C  C     . GLN B 1 25  ? 141.596 122.310 178.790 1.00 64.69 ?  25  GLN B C     1 
ATOM   5719  O  O     . GLN B 1 25  ? 142.396 122.521 177.876 1.00 64.40 ?  25  GLN B O     1 
ATOM   5720  C  CB    . GLN B 1 25  ? 142.867 120.221 179.439 1.00 64.71 ?  25  GLN B CB    1 
ATOM   5721  C  CG    . GLN B 1 25  ? 142.955 119.016 180.361 1.00 62.14 ?  25  GLN B CG    1 
ATOM   5722  C  CD    . GLN B 1 25  ? 144.154 118.143 180.063 1.00 63.89 ?  25  GLN B CD    1 
ATOM   5723  O  OE1   . GLN B 1 25  ? 145.242 118.361 180.594 1.00 63.37 ?  25  GLN B OE1   1 
ATOM   5724  N  NE2   . GLN B 1 25  ? 143.962 117.148 179.206 1.00 64.37 ?  25  GLN B NE2   1 
ATOM   5725  N  N     . PHE B 1 26  ? 140.696 123.215 179.182 1.00 59.58 ?  26  PHE B N     1 
ATOM   5726  C  CA    . PHE B 1 26  ? 140.600 124.507 178.514 1.00 56.88 ?  26  PHE B CA    1 
ATOM   5727  C  C     . PHE B 1 26  ? 141.833 125.365 178.762 1.00 59.74 ?  26  PHE B C     1 
ATOM   5728  O  O     . PHE B 1 26  ? 142.169 126.216 177.932 1.00 60.98 ?  26  PHE B O     1 
ATOM   5729  C  CB    . PHE B 1 26  ? 139.341 125.242 178.974 1.00 52.78 ?  26  PHE B CB    1 
ATOM   5730  C  CG    . PHE B 1 26  ? 138.069 124.655 178.437 1.00 55.55 ?  26  PHE B CG    1 
ATOM   5731  C  CD1   . PHE B 1 26  ? 137.913 124.433 177.079 1.00 55.27 ?  26  PHE B CD1   1 
ATOM   5732  C  CD2   . PHE B 1 26  ? 137.029 124.324 179.289 1.00 54.50 ?  26  PHE B CD2   1 
ATOM   5733  C  CE1   . PHE B 1 26  ? 136.745 123.892 176.583 1.00 56.32 ?  26  PHE B CE1   1 
ATOM   5734  C  CE2   . PHE B 1 26  ? 135.858 123.784 178.796 1.00 52.70 ?  26  PHE B CE2   1 
ATOM   5735  C  CZ    . PHE B 1 26  ? 135.716 123.568 177.442 1.00 52.96 ?  26  PHE B CZ    1 
ATOM   5736  N  N     . ASP B 1 27  ? 142.514 125.158 179.890 1.00 63.05 ?  27  ASP B N     1 
ATOM   5737  C  CA    . ASP B 1 27  ? 143.712 125.925 180.209 1.00 58.55 ?  27  ASP B CA    1 
ATOM   5738  C  C     . ASP B 1 27  ? 144.893 125.578 179.314 1.00 60.78 ?  27  ASP B C     1 
ATOM   5739  O  O     . ASP B 1 27  ? 145.892 126.305 179.332 1.00 62.31 ?  27  ASP B O     1 
ATOM   5740  C  CB    . ASP B 1 27  ? 144.094 125.706 181.673 1.00 60.43 ?  27  ASP B CB    1 
ATOM   5741  C  CG    . ASP B 1 27  ? 142.902 125.791 182.605 1.00 65.03 ?  27  ASP B CG    1 
ATOM   5742  O  OD1   . ASP B 1 27  ? 141.863 125.169 182.299 1.00 65.00 ?  27  ASP B OD1   1 
ATOM   5743  O  OD2   . ASP B 1 27  ? 143.002 126.479 183.642 1.00 65.17 -1 27  ASP B OD2   1 
ATOM   5744  N  N     . LYS B 1 28  ? 144.810 124.495 178.540 1.00 60.48 ?  28  LYS B N     1 
ATOM   5745  C  CA    . LYS B 1 28  ? 145.899 124.134 177.641 1.00 61.30 ?  28  LYS B CA    1 
ATOM   5746  C  C     . LYS B 1 28  ? 146.037 125.104 176.478 1.00 61.69 ?  28  LYS B C     1 
ATOM   5747  O  O     . LYS B 1 28  ? 147.112 125.175 175.873 1.00 62.22 ?  28  LYS B O     1 
ATOM   5748  C  CB    . LYS B 1 28  ? 145.695 122.715 177.109 1.00 61.12 ?  28  LYS B CB    1 
ATOM   5749  C  CG    . LYS B 1 28  ? 145.996 121.625 178.121 1.00 61.20 ?  28  LYS B CG    1 
ATOM   5750  C  CD    . LYS B 1 28  ? 147.490 121.451 178.310 1.00 61.63 ?  28  LYS B CD    1 
ATOM   5751  C  CE    . LYS B 1 28  ? 147.797 120.632 179.549 1.00 61.66 ?  28  LYS B CE    1 
ATOM   5752  N  NZ    . LYS B 1 28  ? 149.245 120.306 179.646 1.00 59.46 1  28  LYS B NZ    1 
ATOM   5753  N  N     . ASP B 1 29  ? 144.981 125.852 176.151 1.00 58.24 ?  29  ASP B N     1 
ATOM   5754  C  CA    . ASP B 1 29  ? 145.062 126.782 175.032 1.00 55.40 ?  29  ASP B CA    1 
ATOM   5755  C  C     . ASP B 1 29  ? 145.926 127.991 175.369 1.00 55.16 ?  29  ASP B C     1 
ATOM   5756  O  O     . ASP B 1 29  ? 146.568 128.557 174.478 1.00 57.74 ?  29  ASP B O     1 
ATOM   5757  C  CB    . ASP B 1 29  ? 143.660 127.219 174.611 1.00 55.23 ?  29  ASP B CB    1 
ATOM   5758  C  CG    . ASP B 1 29  ? 143.465 127.173 173.109 1.00 58.52 ?  29  ASP B CG    1 
ATOM   5759  O  OD1   . ASP B 1 29  ? 142.597 127.908 172.597 1.00 55.50 ?  29  ASP B OD1   1 
ATOM   5760  O  OD2   . ASP B 1 29  ? 144.181 126.400 172.439 1.00 58.35 -1 29  ASP B OD2   1 
ATOM   5761  N  N     . LYS B 1 30  ? 145.949 128.406 176.638 1.00 55.30 ?  30  LYS B N     1 
ATOM   5762  C  CA    . LYS B 1 30  ? 146.906 129.427 177.057 1.00 56.62 ?  30  LYS B CA    1 
ATOM   5763  C  C     . LYS B 1 30  ? 148.334 128.916 176.930 1.00 56.50 ?  30  LYS B C     1 
ATOM   5764  O  O     . LYS B 1 30  ? 149.219 129.633 176.446 1.00 57.10 ?  30  LYS B O     1 
ATOM   5765  C  CB    . LYS B 1 30  ? 146.618 129.862 178.493 1.00 54.70 ?  30  LYS B CB    1 
ATOM   5766  C  CG    . LYS B 1 30  ? 145.294 130.581 178.672 1.00 56.61 ?  30  LYS B CG    1 
ATOM   5767  C  CD    . LYS B 1 30  ? 145.502 132.039 179.053 1.00 58.11 ?  30  LYS B CD    1 
ATOM   5768  C  CE    . LYS B 1 30  ? 146.587 132.189 180.110 1.00 58.82 ?  30  LYS B CE    1 
ATOM   5769  N  NZ    . LYS B 1 30  ? 146.592 133.549 180.717 1.00 58.06 1  30  LYS B NZ    1 
ATOM   5770  N  N     . GLU B 1 31  ? 148.575 127.674 177.352 1.00 57.78 ?  31  GLU B N     1 
ATOM   5771  C  CA    . GLU B 1 31  ? 149.875 127.058 177.122 1.00 54.53 ?  31  GLU B CA    1 
ATOM   5772  C  C     . GLU B 1 31  ? 150.145 126.908 175.632 1.00 55.31 ?  31  GLU B C     1 
ATOM   5773  O  O     . GLU B 1 31  ? 151.276 127.104 175.176 1.00 57.92 ?  31  GLU B O     1 
ATOM   5774  C  CB    . GLU B 1 31  ? 149.949 125.703 177.823 1.00 55.06 ?  31  GLU B CB    1 
ATOM   5775  C  CG    . GLU B 1 31  ? 149.951 125.786 179.339 1.00 56.40 ?  31  GLU B CG    1 
ATOM   5776  C  CD    . GLU B 1 31  ? 150.080 124.427 179.996 1.00 63.70 ?  31  GLU B CD    1 
ATOM   5777  O  OE1   . GLU B 1 31  ? 150.076 123.412 179.269 1.00 65.30 ?  31  GLU B OE1   1 
ATOM   5778  O  OE2   . GLU B 1 31  ? 150.186 124.372 181.239 1.00 60.64 -1 31  GLU B OE2   1 
ATOM   5779  N  N     . ALA B 1 32  ? 149.114 126.564 174.857 1.00 52.44 ?  32  ALA B N     1 
ATOM   5780  C  CA    . ALA B 1 32  ? 149.291 126.410 173.418 1.00 49.90 ?  32  ALA B CA    1 
ATOM   5781  C  C     . ALA B 1 32  ? 149.701 127.723 172.763 1.00 51.55 ?  32  ALA B C     1 
ATOM   5782  O  O     . ALA B 1 32  ? 150.627 127.749 171.949 1.00 52.12 ?  32  ALA B O     1 
ATOM   5783  C  CB    . ALA B 1 32  ? 148.008 125.874 172.783 1.00 49.16 ?  32  ALA B CB    1 
ATOM   5784  N  N     . VAL B 1 33  ? 149.032 128.825 173.111 1.00 54.60 ?  33  VAL B N     1 
ATOM   5785  C  CA    . VAL B 1 33  ? 149.371 130.107 172.497 1.00 50.88 ?  33  VAL B CA    1 
ATOM   5786  C  C     . VAL B 1 33  ? 150.728 130.600 172.990 1.00 53.80 ?  33  VAL B C     1 
ATOM   5787  O  O     . VAL B 1 33  ? 151.504 131.185 172.223 1.00 55.05 ?  33  VAL B O     1 
ATOM   5788  C  CB    . VAL B 1 33  ? 148.255 131.143 172.737 1.00 45.90 ?  33  VAL B CB    1 
ATOM   5789  C  CG1   . VAL B 1 33  ? 148.115 131.489 174.206 1.00 47.37 ?  33  VAL B CG1   1 
ATOM   5790  C  CG2   . VAL B 1 33  ? 148.512 132.397 171.913 1.00 49.25 ?  33  VAL B CG2   1 
ATOM   5791  N  N     . HIS B 1 34  ? 151.042 130.371 174.269 1.00 51.44 ?  34  HIS B N     1 
ATOM   5792  C  CA    . HIS B 1 34  ? 152.353 130.760 174.780 1.00 47.49 ?  34  HIS B CA    1 
ATOM   5793  C  C     . HIS B 1 34  ? 153.465 130.014 174.055 1.00 48.88 ?  34  HIS B C     1 
ATOM   5794  O  O     . HIS B 1 34  ? 154.476 130.609 173.661 1.00 52.29 ?  34  HIS B O     1 
ATOM   5795  C  CB    . HIS B 1 34  ? 152.428 130.504 176.284 1.00 52.36 ?  34  HIS B CB    1 
ATOM   5796  C  CG    . HIS B 1 34  ? 153.738 130.892 176.896 1.00 53.70 ?  34  HIS B CG    1 
ATOM   5797  N  ND1   . HIS B 1 34  ? 154.790 130.011 177.022 1.00 52.99 ?  34  HIS B ND1   1 
ATOM   5798  C  CD2   . HIS B 1 34  ? 154.166 132.067 177.416 1.00 53.10 ?  34  HIS B CD2   1 
ATOM   5799  C  CE1   . HIS B 1 34  ? 155.810 130.626 177.594 1.00 51.59 ?  34  HIS B CE1   1 
ATOM   5800  N  NE2   . HIS B 1 34  ? 155.457 131.874 177.844 1.00 53.65 ?  34  HIS B NE2   1 
ATOM   5801  N  N     . SER B 1 35  ? 153.294 128.703 173.869 1.00 54.75 ?  35  SER B N     1 
ATOM   5802  C  CA    . SER B 1 35  ? 154.281 127.921 173.137 1.00 52.29 ?  35  SER B CA    1 
ATOM   5803  C  C     . SER B 1 35  ? 154.363 128.365 171.684 1.00 52.81 ?  35  SER B C     1 
ATOM   5804  O  O     . SER B 1 35  ? 155.461 128.497 171.133 1.00 55.62 ?  35  SER B O     1 
ATOM   5805  C  CB    . SER B 1 35  ? 153.943 126.433 173.225 1.00 52.45 ?  35  SER B CB    1 
ATOM   5806  O  OG    . SER B 1 35  ? 154.867 125.660 172.481 1.00 56.52 ?  35  SER B OG    1 
ATOM   5807  N  N     . TYR B 1 36  ? 153.211 128.609 171.053 1.00 49.85 ?  36  TYR B N     1 
ATOM   5808  C  CA    . TYR B 1 36  ? 153.198 129.089 169.676 1.00 50.26 ?  36  TYR B CA    1 
ATOM   5809  C  C     . TYR B 1 36  ? 154.029 130.351 169.535 1.00 47.90 ?  36  TYR B C     1 
ATOM   5810  O  O     . TYR B 1 36  ? 154.936 130.420 168.698 1.00 49.13 ?  36  TYR B O     1 
ATOM   5811  C  CB    . TYR B 1 36  ? 151.759 129.346 169.229 1.00 45.19 ?  36  TYR B CB    1 
ATOM   5812  C  CG    . TYR B 1 36  ? 151.636 129.900 167.829 1.00 43.48 ?  36  TYR B CG    1 
ATOM   5813  C  CD1   . TYR B 1 36  ? 152.299 129.306 166.765 1.00 44.00 ?  36  TYR B CD1   1 
ATOM   5814  C  CD2   . TYR B 1 36  ? 150.858 131.021 167.572 1.00 45.84 ?  36  TYR B CD2   1 
ATOM   5815  C  CE1   . TYR B 1 36  ? 152.187 129.807 165.485 1.00 46.30 ?  36  TYR B CE1   1 
ATOM   5816  C  CE2   . TYR B 1 36  ? 150.741 131.530 166.295 1.00 44.51 ?  36  TYR B CE2   1 
ATOM   5817  C  CZ    . TYR B 1 36  ? 151.409 130.920 165.256 1.00 46.87 ?  36  TYR B CZ    1 
ATOM   5818  O  OH    . TYR B 1 36  ? 151.298 131.423 163.981 1.00 47.50 ?  36  TYR B OH    1 
ATOM   5819  N  N     . PHE B 1 37  ? 153.760 131.348 170.378 1.00 51.88 ?  37  PHE B N     1 
ATOM   5820  C  CA    . PHE B 1 37  ? 154.544 132.575 170.338 1.00 50.44 ?  37  PHE B CA    1 
ATOM   5821  C  C     . PHE B 1 37  ? 156.021 132.281 170.561 1.00 51.90 ?  37  PHE B C     1 
ATOM   5822  O  O     . PHE B 1 37  ? 156.833 132.443 169.644 1.00 55.87 ?  37  PHE B O     1 
ATOM   5823  C  CB    . PHE B 1 37  ? 154.021 133.574 171.367 1.00 52.29 ?  37  PHE B CB    1 
ATOM   5824  C  CG    . PHE B 1 37  ? 153.107 134.603 170.781 1.00 53.14 ?  37  PHE B CG    1 
ATOM   5825  C  CD1   . PHE B 1 37  ? 153.620 135.757 170.218 1.00 51.94 ?  37  PHE B CD1   1 
ATOM   5826  C  CD2   . PHE B 1 37  ? 151.739 134.410 170.771 1.00 52.91 ?  37  PHE B CD2   1 
ATOM   5827  C  CE1   . PHE B 1 37  ? 152.786 136.704 169.670 1.00 53.84 ?  37  PHE B CE1   1 
ATOM   5828  C  CE2   . PHE B 1 37  ? 150.902 135.354 170.225 1.00 51.40 ?  37  PHE B CE2   1 
ATOM   5829  C  CZ    . PHE B 1 37  ? 151.425 136.500 169.672 1.00 51.87 ?  37  PHE B CZ    1 
ATOM   5830  N  N     . VAL B 1 38  ? 156.361 131.755 171.742 1.00 55.94 ?  38  VAL B N     1 
ATOM   5831  C  CA    . VAL B 1 38  ? 157.751 131.640 172.172 1.00 56.74 ?  38  VAL B CA    1 
ATOM   5832  C  C     . VAL B 1 38  ? 158.575 130.782 171.216 1.00 55.35 ?  38  VAL B C     1 
ATOM   5833  O  O     . VAL B 1 38  ? 159.786 130.993 171.074 1.00 57.62 ?  38  VAL B O     1 
ATOM   5834  C  CB    . VAL B 1 38  ? 157.785 131.104 173.621 1.00 54.50 ?  38  VAL B CB    1 
ATOM   5835  C  CG1   . VAL B 1 38  ? 159.061 130.330 173.908 1.00 56.35 ?  38  VAL B CG1   1 
ATOM   5836  C  CG2   . VAL B 1 38  ? 157.621 132.249 174.608 1.00 52.68 ?  38  VAL B CG2   1 
ATOM   5837  N  N     . ASP B 1 39  ? 157.947 129.836 170.517 1.00 53.36 ?  39  ASP B N     1 
ATOM   5838  C  CA    . ASP B 1 39  ? 158.688 128.923 169.659 1.00 52.42 ?  39  ASP B CA    1 
ATOM   5839  C  C     . ASP B 1 39  ? 158.663 129.295 168.184 1.00 57.74 ?  39  ASP B C     1 
ATOM   5840  O  O     . ASP B 1 39  ? 159.598 128.937 167.461 1.00 61.98 ?  39  ASP B O     1 
ATOM   5841  C  CB    . ASP B 1 39  ? 158.149 127.497 169.818 1.00 55.14 ?  39  ASP B CB    1 
ATOM   5842  C  CG    . ASP B 1 39  ? 158.317 126.965 171.225 1.00 60.48 ?  39  ASP B CG    1 
ATOM   5843  O  OD1   . ASP B 1 39  ? 158.905 127.676 172.065 1.00 59.89 ?  39  ASP B OD1   1 
ATOM   5844  O  OD2   . ASP B 1 39  ? 157.861 125.834 171.494 1.00 62.77 -1 39  ASP B OD2   1 
ATOM   5845  N  N     . TYR B 1 40  ? 157.634 129.993 167.704 1.00 58.16 ?  40  TYR B N     1 
ATOM   5846  C  CA    . TYR B 1 40  ? 157.531 130.304 166.285 1.00 55.81 ?  40  TYR B CA    1 
ATOM   5847  C  C     . TYR B 1 40  ? 157.501 131.796 166.007 1.00 59.41 ?  40  TYR B C     1 
ATOM   5848  O  O     . TYR B 1 40  ? 158.227 132.272 165.126 1.00 62.58 ?  40  TYR B O     1 
ATOM   5849  C  CB    . TYR B 1 40  ? 156.275 129.636 165.703 1.00 52.29 ?  40  TYR B CB    1 
ATOM   5850  C  CG    . TYR B 1 40  ? 156.171 129.712 164.199 1.00 56.35 ?  40  TYR B CG    1 
ATOM   5851  C  CD1   . TYR B 1 40  ? 156.916 128.868 163.389 1.00 56.20 ?  40  TYR B CD1   1 
ATOM   5852  C  CD2   . TYR B 1 40  ? 155.320 130.624 163.589 1.00 58.17 ?  40  TYR B CD2   1 
ATOM   5853  C  CE1   . TYR B 1 40  ? 156.822 128.934 162.013 1.00 57.45 ?  40  TYR B CE1   1 
ATOM   5854  C  CE2   . TYR B 1 40  ? 155.219 130.697 162.215 1.00 57.38 ?  40  TYR B CE2   1 
ATOM   5855  C  CZ    . TYR B 1 40  ? 155.972 129.849 161.431 1.00 59.93 ?  40  TYR B CZ    1 
ATOM   5856  O  OH    . TYR B 1 40  ? 155.874 129.919 160.061 1.00 61.60 ?  40  TYR B OH    1 
ATOM   5857  N  N     . ILE B 1 41  ? 156.680 132.555 166.735 1.00 54.61 ?  41  ILE B N     1 
ATOM   5858  C  CA    . ILE B 1 41  ? 156.450 133.950 166.371 1.00 54.22 ?  41  ILE B CA    1 
ATOM   5859  C  C     . ILE B 1 41  ? 157.667 134.796 166.717 1.00 53.52 ?  41  ILE B C     1 
ATOM   5860  O  O     . ILE B 1 41  ? 158.156 135.573 165.892 1.00 56.05 ?  41  ILE B O     1 
ATOM   5861  C  CB    . ILE B 1 41  ? 155.176 134.481 167.051 1.00 52.78 ?  41  ILE B CB    1 
ATOM   5862  C  CG1   . ILE B 1 41  ? 153.954 133.684 166.596 1.00 50.99 ?  41  ILE B CG1   1 
ATOM   5863  C  CG2   . ILE B 1 41  ? 154.988 135.958 166.747 1.00 51.98 ?  41  ILE B CG2   1 
ATOM   5864  C  CD1   . ILE B 1 41  ? 153.802 133.605 165.096 1.00 49.66 ?  41  ILE B CD1   1 
ATOM   5865  N  N     . ASN B 1 42  ? 158.178 134.649 167.941 1.00 52.27 ?  42  ASN B N     1 
ATOM   5866  C  CA    . ASN B 1 42  ? 159.357 135.411 168.339 1.00 54.55 ?  42  ASN B CA    1 
ATOM   5867  C  C     . ASN B 1 42  ? 160.581 135.014 167.525 1.00 56.60 ?  42  ASN B C     1 
ATOM   5868  O  O     . ASN B 1 42  ? 161.500 135.823 167.358 1.00 58.07 ?  42  ASN B O     1 
ATOM   5869  C  CB    . ASN B 1 42  ? 159.622 135.225 169.832 1.00 55.05 ?  42  ASN B CB    1 
ATOM   5870  C  CG    . ASN B 1 42  ? 158.484 135.739 170.693 1.00 56.64 ?  42  ASN B CG    1 
ATOM   5871  O  OD1   . ASN B 1 42  ? 157.465 136.200 170.181 1.00 59.11 ?  42  ASN B OD1   1 
ATOM   5872  N  ND2   . ASN B 1 42  ? 158.656 135.667 172.006 1.00 58.92 ?  42  ASN B ND2   1 
ATOM   5873  N  N     . GLN B 1 43  ? 160.612 133.783 167.015 1.00 59.89 ?  43  GLN B N     1 
ATOM   5874  C  CA    . GLN B 1 43  ? 161.708 133.362 166.150 1.00 57.85 ?  43  GLN B CA    1 
ATOM   5875  C  C     . GLN B 1 43  ? 161.576 133.948 164.749 1.00 58.98 ?  43  GLN B C     1 
ATOM   5876  O  O     . GLN B 1 43  ? 162.579 134.324 164.134 1.00 61.60 ?  43  GLN B O     1 
ATOM   5877  C  CB    . GLN B 1 43  ? 161.766 131.835 166.080 1.00 57.38 ?  43  GLN B CB    1 
ATOM   5878  C  CG    . GLN B 1 43  ? 162.672 131.193 167.120 1.00 60.30 ?  43  GLN B CG    1 
ATOM   5879  C  CD    . GLN B 1 43  ? 162.180 131.409 168.536 1.00 62.50 ?  43  GLN B CD    1 
ATOM   5880  O  OE1   . GLN B 1 43  ? 161.007 131.707 168.757 1.00 62.16 ?  43  GLN B OE1   1 
ATOM   5881  N  NE2   . GLN B 1 43  ? 163.075 131.263 169.504 1.00 60.18 ?  43  GLN B NE2   1 
ATOM   5882  N  N     . ASN B 1 44  ? 160.351 134.035 164.232 1.00 54.48 ?  44  ASN B N     1 
ATOM   5883  C  CA    . ASN B 1 44  ? 160.110 134.469 162.863 1.00 56.91 ?  44  ASN B CA    1 
ATOM   5884  C  C     . ASN B 1 44  ? 159.710 135.935 162.765 1.00 57.23 ?  44  ASN B C     1 
ATOM   5885  O  O     . ASN B 1 44  ? 159.334 136.390 161.680 1.00 55.75 ?  44  ASN B O     1 
ATOM   5886  C  CB    . ASN B 1 44  ? 159.038 133.590 162.213 1.00 54.58 ?  44  ASN B CB    1 
ATOM   5887  C  CG    . ASN B 1 44  ? 159.489 132.153 162.033 1.00 58.80 ?  44  ASN B CG    1 
ATOM   5888  O  OD1   . ASN B 1 44  ? 159.611 131.666 160.909 1.00 62.13 ?  44  ASN B OD1   1 
ATOM   5889  N  ND2   . ASN B 1 44  ? 159.727 131.460 163.142 1.00 57.89 ?  44  ASN B ND2   1 
ATOM   5890  N  N     . THR B 1 45  ? 159.783 136.682 163.861 1.00 57.35 ?  45  THR B N     1 
ATOM   5891  C  CA    . THR B 1 45  ? 159.481 138.107 163.847 1.00 58.16 ?  45  THR B CA    1 
ATOM   5892  C  C     . THR B 1 45  ? 160.764 138.888 163.595 1.00 57.10 ?  45  THR B C     1 
ATOM   5893  O  O     . THR B 1 45  ? 161.707 138.812 164.389 1.00 58.92 ?  45  THR B O     1 
ATOM   5894  C  CB    . THR B 1 45  ? 158.844 138.548 165.164 1.00 56.69 ?  45  THR B CB    1 
ATOM   5895  O  OG1   . THR B 1 45  ? 157.569 137.912 165.319 1.00 60.69 ?  45  THR B OG1   1 
ATOM   5896  C  CG2   . THR B 1 45  ? 158.660 140.057 165.188 1.00 54.98 ?  45  THR B CG2   1 
ATOM   5897  N  N     . VAL B 1 46  ? 160.801 139.631 162.489 1.00 56.57 ?  46  VAL B N     1 
ATOM   5898  C  CA    . VAL B 1 46  ? 161.941 140.494 162.213 1.00 56.20 ?  46  VAL B CA    1 
ATOM   5899  C  C     . VAL B 1 46  ? 161.994 141.593 163.264 1.00 57.03 ?  46  VAL B C     1 
ATOM   5900  O  O     . VAL B 1 46  ? 161.008 142.305 163.490 1.00 58.62 ?  46  VAL B O     1 
ATOM   5901  C  CB    . VAL B 1 46  ? 161.848 141.085 160.800 1.00 54.12 ?  46  VAL B CB    1 
ATOM   5902  C  CG1   . VAL B 1 46  ? 163.064 141.947 160.506 1.00 54.46 ?  46  VAL B CG1   1 
ATOM   5903  C  CG2   . VAL B 1 46  ? 161.717 139.985 159.774 1.00 54.07 ?  46  VAL B CG2   1 
ATOM   5904  N  N     . PHE B 1 47  ? 163.143 141.733 163.912 1.00 61.45 ?  47  PHE B N     1 
ATOM   5905  C  CA    . PHE B 1 47  ? 163.335 142.738 164.943 1.00 63.31 ?  47  PHE B CA    1 
ATOM   5906  C  C     . PHE B 1 47  ? 164.330 143.783 164.465 1.00 64.07 ?  47  PHE B C     1 
ATOM   5907  O  O     . PHE B 1 47  ? 165.304 143.462 163.777 1.00 63.48 ?  47  PHE B O     1 
ATOM   5908  C  CB    . PHE B 1 47  ? 163.823 142.110 166.249 1.00 62.59 ?  47  PHE B CB    1 
ATOM   5909  C  CG    . PHE B 1 47  ? 163.749 143.036 167.428 1.00 64.31 ?  47  PHE B CG    1 
ATOM   5910  C  CD1   . PHE B 1 47  ? 162.533 143.328 168.019 1.00 62.63 ?  47  PHE B CD1   1 
ATOM   5911  C  CD2   . PHE B 1 47  ? 164.896 143.618 167.941 1.00 63.97 ?  47  PHE B CD2   1 
ATOM   5912  C  CE1   . PHE B 1 47  ? 162.460 144.182 169.103 1.00 64.84 ?  47  PHE B CE1   1 
ATOM   5913  C  CE2   . PHE B 1 47  ? 164.830 144.473 169.025 1.00 63.35 ?  47  PHE B CE2   1 
ATOM   5914  C  CZ    . PHE B 1 47  ? 163.610 144.756 169.606 1.00 64.46 ?  47  PHE B CZ    1 
ATOM   5915  N  N     . PHE B 1 48  ? 164.074 145.033 164.832 1.00 61.83 ?  48  PHE B N     1 
ATOM   5916  C  CA    . PHE B 1 48  ? 164.918 146.157 164.474 1.00 57.75 ?  48  PHE B CA    1 
ATOM   5917  C  C     . PHE B 1 48  ? 165.400 146.838 165.746 1.00 60.79 ?  48  PHE B C     1 
ATOM   5918  O  O     . PHE B 1 48  ? 164.750 146.759 166.793 1.00 61.58 ?  48  PHE B O     1 
ATOM   5919  C  CB    . PHE B 1 48  ? 164.172 147.163 163.586 1.00 58.73 ?  48  PHE B CB    1 
ATOM   5920  C  CG    . PHE B 1 48  ? 163.630 146.572 162.313 1.00 57.73 ?  48  PHE B CG    1 
ATOM   5921  C  CD1   . PHE B 1 48  ? 162.491 145.784 162.322 1.00 57.85 ?  48  PHE B CD1   1 
ATOM   5922  C  CD2   . PHE B 1 48  ? 164.255 146.816 161.103 1.00 60.31 ?  48  PHE B CD2   1 
ATOM   5923  C  CE1   . PHE B 1 48  ? 161.992 145.249 161.152 1.00 59.31 ?  48  PHE B CE1   1 
ATOM   5924  C  CE2   . PHE B 1 48  ? 163.759 146.284 159.930 1.00 60.19 ?  48  PHE B CE2   1 
ATOM   5925  C  CZ    . PHE B 1 48  ? 162.627 145.499 159.955 1.00 57.88 ?  48  PHE B CZ    1 
ATOM   5926  N  N     . HIS B 1 49  ? 166.555 147.501 165.650 1.00 65.61 ?  49  HIS B N     1 
ATOM   5927  C  CA    . HIS B 1 49  ? 167.138 148.136 166.827 1.00 65.59 ?  49  HIS B CA    1 
ATOM   5928  C  C     . HIS B 1 49  ? 166.220 149.216 167.385 1.00 67.22 ?  49  HIS B C     1 
ATOM   5929  O  O     . HIS B 1 49  ? 166.086 149.359 168.605 1.00 67.83 ?  49  HIS B O     1 
ATOM   5930  C  CB    . HIS B 1 49  ? 168.509 148.719 166.483 1.00 66.47 ?  49  HIS B CB    1 
ATOM   5931  C  CG    . HIS B 1 49  ? 169.393 148.923 167.673 1.00 70.11 ?  49  HIS B CG    1 
ATOM   5932  N  ND1   . HIS B 1 49  ? 169.124 149.859 168.650 1.00 69.32 ?  49  HIS B ND1   1 
ATOM   5933  C  CD2   . HIS B 1 49  ? 170.542 148.311 168.047 1.00 69.08 ?  49  HIS B CD2   1 
ATOM   5934  C  CE1   . HIS B 1 49  ? 170.068 149.815 169.572 1.00 68.02 ?  49  HIS B CE1   1 
ATOM   5935  N  NE2   . HIS B 1 49  ? 170.941 148.884 169.229 1.00 68.93 ?  49  HIS B NE2   1 
ATOM   5936  N  N     . ASN B 1 50  ? 165.579 149.983 166.508 1.00 65.61 ?  50  ASN B N     1 
ATOM   5937  C  CA    . ASN B 1 50  ? 164.652 151.025 166.920 1.00 63.02 ?  50  ASN B CA    1 
ATOM   5938  C  C     . ASN B 1 50  ? 163.446 151.012 165.995 1.00 61.96 ?  50  ASN B C     1 
ATOM   5939  O  O     . ASN B 1 50  ? 163.469 150.412 164.918 1.00 61.45 ?  50  ASN B O     1 
ATOM   5940  C  CB    . ASN B 1 50  ? 165.319 152.407 166.913 1.00 61.90 ?  50  ASN B CB    1 
ATOM   5941  C  CG    . ASN B 1 50  ? 166.109 152.664 165.647 1.00 63.89 ?  50  ASN B CG    1 
ATOM   5942  O  OD1   . ASN B 1 50  ? 165.538 152.894 164.582 1.00 64.93 ?  50  ASN B OD1   1 
ATOM   5943  N  ND2   . ASN B 1 50  ? 167.430 152.625 165.757 1.00 64.38 ?  50  ASN B ND2   1 
ATOM   5944  N  N     . LEU B 1 51  ? 162.377 151.678 166.439 1.00 58.68 ?  51  LEU B N     1 
ATOM   5945  C  CA    . LEU B 1 51  ? 161.179 151.784 165.615 1.00 58.75 ?  51  LEU B CA    1 
ATOM   5946  C  C     . LEU B 1 51  ? 161.442 152.581 164.344 1.00 60.56 ?  51  LEU B C     1 
ATOM   5947  O  O     . LEU B 1 51  ? 160.813 152.325 163.311 1.00 62.00 ?  51  LEU B O     1 
ATOM   5948  C  CB    . LEU B 1 51  ? 160.045 152.420 166.419 1.00 58.13 ?  51  LEU B CB    1 
ATOM   5949  C  CG    . LEU B 1 51  ? 158.735 152.706 165.683 1.00 57.06 ?  51  LEU B CG    1 
ATOM   5950  C  CD1   . LEU B 1 51  ? 158.153 151.433 165.089 1.00 54.72 ?  51  LEU B CD1   1 
ATOM   5951  C  CD2   . LEU B 1 51  ? 157.740 153.374 166.611 1.00 57.42 ?  51  LEU B CD2   1 
ATOM   5952  N  N     . LYS B 1 52  ? 162.363 153.547 164.399 1.00 59.05 ?  52  LYS B N     1 
ATOM   5953  C  CA    . LYS B 1 52  ? 162.689 154.331 163.212 1.00 57.11 ?  52  LYS B CA    1 
ATOM   5954  C  C     . LYS B 1 52  ? 163.254 153.449 162.106 1.00 60.44 ?  52  LYS B C     1 
ATOM   5955  O  O     . LYS B 1 52  ? 162.881 153.593 160.935 1.00 61.28 ?  52  LYS B O     1 
ATOM   5956  C  CB    . LYS B 1 52  ? 163.681 155.435 163.572 1.00 56.54 ?  52  LYS B CB    1 
ATOM   5957  C  CG    . LYS B 1 52  ? 163.584 156.673 162.700 1.00 60.79 ?  52  LYS B CG    1 
ATOM   5958  C  CD    . LYS B 1 52  ? 164.709 157.648 163.009 1.00 63.71 ?  52  LYS B CD    1 
ATOM   5959  C  CE    . LYS B 1 52  ? 164.403 158.473 164.248 1.00 60.86 ?  52  LYS B CE    1 
ATOM   5960  N  NZ    . LYS B 1 52  ? 165.567 158.546 165.172 1.00 61.13 1  52  LYS B NZ    1 
ATOM   5961  N  N     . GLU B 1 53  ? 164.155 152.530 162.459 1.00 62.10 ?  53  GLU B N     1 
ATOM   5962  C  CA    . GLU B 1 53  ? 164.722 151.629 161.461 1.00 60.79 ?  53  GLU B CA    1 
ATOM   5963  C  C     . GLU B 1 53  ? 163.651 150.730 160.859 1.00 61.00 ?  53  GLU B C     1 
ATOM   5964  O  O     . GLU B 1 53  ? 163.634 150.499 159.644 1.00 61.80 ?  53  GLU B O     1 
ATOM   5965  C  CB    . GLU B 1 53  ? 165.838 150.791 162.085 1.00 60.31 ?  53  GLU B CB    1 
ATOM   5966  C  CG    . GLU B 1 53  ? 166.789 150.176 161.074 1.00 62.43 ?  53  GLU B CG    1 
ATOM   5967  C  CD    . GLU B 1 53  ? 167.121 148.731 161.389 1.00 65.53 ?  53  GLU B CD    1 
ATOM   5968  O  OE1   . GLU B 1 53  ? 167.306 148.409 162.581 1.00 66.13 ?  53  GLU B OE1   1 
ATOM   5969  O  OE2   . GLU B 1 53  ? 167.197 147.919 160.444 1.00 64.07 -1 53  GLU B OE2   1 
ATOM   5970  N  N     . LYS B 1 54  ? 162.744 150.216 161.694 1.00 58.53 ?  54  LYS B N     1 
ATOM   5971  C  CA    . LYS B 1 54  ? 161.666 149.368 161.195 1.00 58.25 ?  54  LYS B CA    1 
ATOM   5972  C  C     . LYS B 1 54  ? 160.765 150.138 160.239 1.00 54.87 ?  54  LYS B C     1 
ATOM   5973  O  O     . LYS B 1 54  ? 160.408 149.642 159.163 1.00 56.61 ?  54  LYS B O     1 
ATOM   5974  C  CB    . LYS B 1 54  ? 160.855 148.812 162.363 1.00 56.86 ?  54  LYS B CB    1 
ATOM   5975  C  CG    . LYS B 1 54  ? 159.555 148.148 161.948 1.00 56.41 ?  54  LYS B CG    1 
ATOM   5976  C  CD    . LYS B 1 54  ? 158.918 147.406 163.105 1.00 57.38 ?  54  LYS B CD    1 
ATOM   5977  C  CE    . LYS B 1 54  ? 157.622 146.739 162.680 1.00 59.39 ?  54  LYS B CE    1 
ATOM   5978  N  NZ    . LYS B 1 54  ? 157.247 145.627 163.595 1.00 59.58 1  54  LYS B NZ    1 
ATOM   5979  N  N     . LEU B 1 55  ? 160.392 151.361 160.615 1.00 55.55 ?  55  LEU B N     1 
ATOM   5980  C  CA    . LEU B 1 55  ? 159.524 152.165 159.762 1.00 56.17 ?  55  LEU B CA    1 
ATOM   5981  C  C     . LEU B 1 55  ? 160.206 152.500 158.445 1.00 59.21 ?  55  LEU B C     1 
ATOM   5982  O  O     . LEU B 1 55  ? 159.575 152.445 157.383 1.00 63.12 ?  55  LEU B O     1 
ATOM   5983  C  CB    . LEU B 1 55  ? 159.105 153.439 160.492 1.00 57.73 ?  55  LEU B CB    1 
ATOM   5984  C  CG    . LEU B 1 55  ? 158.075 153.254 161.607 1.00 57.81 ?  55  LEU B CG    1 
ATOM   5985  C  CD1   . LEU B 1 55  ? 157.868 154.557 162.352 1.00 58.16 ?  55  LEU B CD1   1 
ATOM   5986  C  CD2   . LEU B 1 55  ? 156.760 152.737 161.044 1.00 57.18 ?  55  LEU B CD2   1 
ATOM   5987  N  N     . ASP B 1 56  ? 161.495 152.852 158.494 1.00 60.82 ?  56  ASP B N     1 
ATOM   5988  C  CA    . ASP B 1 56  ? 162.231 153.157 157.272 1.00 60.69 ?  56  ASP B CA    1 
ATOM   5989  C  C     . ASP B 1 56  ? 162.325 151.937 156.366 1.00 59.63 ?  56  ASP B C     1 
ATOM   5990  O  O     . ASP B 1 56  ? 162.139 152.042 155.147 1.00 62.40 ?  56  ASP B O     1 
ATOM   5991  C  CB    . ASP B 1 56  ? 163.625 153.678 157.618 1.00 62.18 ?  56  ASP B CB    1 
ATOM   5992  C  CG    . ASP B 1 56  ? 163.662 155.184 157.773 1.00 64.79 ?  56  ASP B CG    1 
ATOM   5993  O  OD1   . ASP B 1 56  ? 164.597 155.693 158.425 1.00 65.13 ?  56  ASP B OD1   1 
ATOM   5994  O  OD2   . ASP B 1 56  ? 162.756 155.860 157.241 1.00 63.28 -1 56  ASP B OD2   1 
ATOM   5995  N  N     . TYR B 1 57  ? 162.605 150.766 156.946 1.00 55.20 ?  57  TYR B N     1 
ATOM   5996  C  CA    . TYR B 1 57  ? 162.646 149.539 156.161 1.00 56.47 ?  57  TYR B CA    1 
ATOM   5997  C  C     . TYR B 1 57  ? 161.297 149.254 155.519 1.00 57.12 ?  57  TYR B C     1 
ATOM   5998  O  O     . TYR B 1 57  ? 161.230 148.829 154.362 1.00 58.36 ?  57  TYR B O     1 
ATOM   5999  C  CB    . TYR B 1 57  ? 163.078 148.367 157.043 1.00 57.82 ?  57  TYR B CB    1 
ATOM   6000  C  CG    . TYR B 1 57  ? 162.979 147.013 156.371 1.00 57.26 ?  57  TYR B CG    1 
ATOM   6001  C  CD1   . TYR B 1 57  ? 164.011 146.534 155.577 1.00 57.59 ?  57  TYR B CD1   1 
ATOM   6002  C  CD2   . TYR B 1 57  ? 161.857 146.212 156.540 1.00 58.80 ?  57  TYR B CD2   1 
ATOM   6003  C  CE1   . TYR B 1 57  ? 163.925 145.299 154.963 1.00 57.28 ?  57  TYR B CE1   1 
ATOM   6004  C  CE2   . TYR B 1 57  ? 161.763 144.979 155.931 1.00 59.93 ?  57  TYR B CE2   1 
ATOM   6005  C  CZ    . TYR B 1 57  ? 162.800 144.526 155.144 1.00 60.41 ?  57  TYR B CZ    1 
ATOM   6006  O  OH    . TYR B 1 57  ? 162.707 143.295 154.537 1.00 60.67 ?  57  TYR B OH    1 
ATOM   6007  N  N     . LEU B 1 58  ? 160.210 149.482 156.255 1.00 55.53 ?  58  LEU B N     1 
ATOM   6008  C  CA    . LEU B 1 58  ? 158.892 149.158 155.724 1.00 55.09 ?  58  LEU B CA    1 
ATOM   6009  C  C     . LEU B 1 58  ? 158.476 150.124 154.620 1.00 52.51 ?  58  LEU B C     1 
ATOM   6010  O  O     . LEU B 1 58  ? 157.888 149.703 153.618 1.00 54.87 ?  58  LEU B O     1 
ATOM   6011  C  CB    . LEU B 1 58  ? 157.865 149.134 156.856 1.00 53.67 ?  58  LEU B CB    1 
ATOM   6012  C  CG    . LEU B 1 58  ? 158.045 147.938 157.798 1.00 53.10 ?  58  LEU B CG    1 
ATOM   6013  C  CD1   . LEU B 1 58  ? 157.240 148.100 159.073 1.00 53.31 ?  58  LEU B CD1   1 
ATOM   6014  C  CD2   . LEU B 1 58  ? 157.681 146.643 157.093 1.00 51.72 ?  58  LEU B CD2   1 
ATOM   6015  N  N     . VAL B 1 59  ? 158.764 151.420 154.773 1.00 55.94 ?  59  VAL B N     1 
ATOM   6016  C  CA    . VAL B 1 59  ? 158.368 152.359 153.725 1.00 59.41 ?  59  VAL B CA    1 
ATOM   6017  C  C     . VAL B 1 59  ? 159.248 152.192 152.492 1.00 61.68 ?  59  VAL B C     1 
ATOM   6018  O  O     . VAL B 1 59  ? 158.757 152.218 151.357 1.00 58.99 ?  59  VAL B O     1 
ATOM   6019  C  CB    . VAL B 1 59  ? 158.385 153.816 154.230 1.00 58.77 ?  59  VAL B CB    1 
ATOM   6020  C  CG1   . VAL B 1 59  ? 157.162 154.103 155.095 1.00 57.57 ?  59  VAL B CG1   1 
ATOM   6021  C  CG2   . VAL B 1 59  ? 159.687 154.161 154.929 1.00 59.07 ?  59  VAL B CG2   1 
ATOM   6022  N  N     . GLU B 1 60  ? 160.559 152.016 152.688 1.00 62.25 ?  60  GLU B N     1 
ATOM   6023  C  CA    . GLU B 1 60  ? 161.473 151.979 151.551 1.00 60.57 ?  60  GLU B CA    1 
ATOM   6024  C  C     . GLU B 1 60  ? 161.404 150.662 150.788 1.00 61.73 ?  60  GLU B C     1 
ATOM   6025  O  O     . GLU B 1 60  ? 161.712 150.632 149.592 1.00 64.04 ?  60  GLU B O     1 
ATOM   6026  C  CB    . GLU B 1 60  ? 162.905 152.258 152.018 1.00 60.61 ?  60  GLU B CB    1 
ATOM   6027  C  CG    . GLU B 1 60  ? 163.684 151.038 152.470 1.00 61.74 ?  60  GLU B CG    1 
ATOM   6028  C  CD    . GLU B 1 60  ? 164.913 151.401 153.281 1.00 64.83 ?  60  GLU B CD    1 
ATOM   6029  O  OE1   . GLU B 1 60  ? 165.164 152.610 153.474 1.00 64.26 ?  60  GLU B OE1   1 
ATOM   6030  O  OE2   . GLU B 1 60  ? 165.626 150.479 153.729 1.00 61.61 -1 60  GLU B OE2   1 
ATOM   6031  N  N     . ASN B 1 61  ? 161.006 149.571 151.443 1.00 57.46 ?  61  ASN B N     1 
ATOM   6032  C  CA    . ASN B 1 61  ? 160.873 148.278 150.786 1.00 57.98 ?  61  ASN B CA    1 
ATOM   6033  C  C     . ASN B 1 61  ? 159.468 148.033 150.249 1.00 57.86 ?  61  ASN B C     1 
ATOM   6034  O  O     . ASN B 1 61  ? 159.090 146.875 150.038 1.00 59.49 ?  61  ASN B O     1 
ATOM   6035  C  CB    . ASN B 1 61  ? 161.273 147.150 151.739 1.00 59.20 ?  61  ASN B CB    1 
ATOM   6036  C  CG    . ASN B 1 61  ? 162.773 146.978 151.838 1.00 61.20 ?  61  ASN B CG    1 
ATOM   6037  O  OD1   . ASN B 1 61  ? 163.360 146.136 151.160 1.00 60.39 ?  61  ASN B OD1   1 
ATOM   6038  N  ND2   . ASN B 1 61  ? 163.404 147.779 152.687 1.00 60.53 ?  61  ASN B ND2   1 
ATOM   6039  N  N     . GLN B 1 62  ? 158.691 149.097 150.036 1.00 56.47 ?  62  GLN B N     1 
ATOM   6040  C  CA    . GLN B 1 62  ? 157.365 149.011 149.421 1.00 58.76 ?  62  GLN B CA    1 
ATOM   6041  C  C     . GLN B 1 62  ? 156.410 148.149 150.244 1.00 57.86 ?  62  GLN B C     1 
ATOM   6042  O  O     . GLN B 1 62  ? 155.648 147.346 149.704 1.00 59.50 ?  62  GLN B O     1 
ATOM   6043  C  CB    . GLN B 1 62  ? 157.457 148.497 147.982 1.00 58.26 ?  62  GLN B CB    1 
ATOM   6044  C  CG    . GLN B 1 62  ? 158.376 149.314 147.087 1.00 58.23 ?  62  GLN B CG    1 
ATOM   6045  C  CD    . GLN B 1 62  ? 157.987 150.778 147.036 1.00 61.67 ?  62  GLN B CD    1 
ATOM   6046  O  OE1   . GLN B 1 62  ? 158.551 151.609 147.747 1.00 60.56 ?  62  GLN B OE1   1 
ATOM   6047  N  NE2   . GLN B 1 62  ? 157.016 151.101 146.191 1.00 59.67 ?  62  GLN B NE2   1 
ATOM   6048  N  N     . TYR B 1 63  ? 156.449 148.318 151.564 1.00 56.30 ?  63  TYR B N     1 
ATOM   6049  C  CA    . TYR B 1 63  ? 155.505 147.658 152.458 1.00 55.71 ?  63  TYR B CA    1 
ATOM   6050  C  C     . TYR B 1 63  ? 154.433 148.602 152.980 1.00 54.98 ?  63  TYR B C     1 
ATOM   6051  O  O     . TYR B 1 63  ? 153.264 148.215 153.069 1.00 55.89 ?  63  TYR B O     1 
ATOM   6052  C  CB    . TYR B 1 63  ? 156.239 147.026 153.644 1.00 52.99 ?  63  TYR B CB    1 
ATOM   6053  C  CG    . TYR B 1 63  ? 157.001 145.769 153.300 1.00 55.76 ?  63  TYR B CG    1 
ATOM   6054  C  CD1   . TYR B 1 63  ? 156.357 144.678 152.731 1.00 53.23 ?  63  TYR B CD1   1 
ATOM   6055  C  CD2   . TYR B 1 63  ? 158.363 145.670 153.548 1.00 55.99 ?  63  TYR B CD2   1 
ATOM   6056  C  CE1   . TYR B 1 63  ? 157.049 143.528 152.418 1.00 54.08 ?  63  TYR B CE1   1 
ATOM   6057  C  CE2   . TYR B 1 63  ? 159.062 144.523 153.238 1.00 55.25 ?  63  TYR B CE2   1 
ATOM   6058  C  CZ    . TYR B 1 63  ? 158.401 143.455 152.674 1.00 58.33 ?  63  TYR B CZ    1 
ATOM   6059  O  OH    . TYR B 1 63  ? 159.097 142.311 152.363 1.00 61.61 ?  63  TYR B OH    1 
ATOM   6060  N  N     . TYR B 1 64  ? 154.804 149.830 153.323 1.00 51.12 ?  64  TYR B N     1 
ATOM   6061  C  CA    . TYR B 1 64  ? 153.881 150.834 153.828 1.00 49.36 ?  64  TYR B CA    1 
ATOM   6062  C  C     . TYR B 1 64  ? 153.714 151.954 152.811 1.00 51.84 ?  64  TYR B C     1 
ATOM   6063  O  O     . TYR B 1 64  ? 154.377 151.994 151.771 1.00 56.22 ?  64  TYR B O     1 
ATOM   6064  C  CB    . TYR B 1 64  ? 154.377 151.412 155.157 1.00 51.22 ?  64  TYR B CB    1 
ATOM   6065  C  CG    . TYR B 1 64  ? 154.150 150.518 156.349 1.00 49.14 ?  64  TYR B CG    1 
ATOM   6066  C  CD1   . TYR B 1 64  ? 153.444 149.330 156.229 1.00 47.95 ?  64  TYR B CD1   1 
ATOM   6067  C  CD2   . TYR B 1 64  ? 154.642 150.865 157.597 1.00 50.77 ?  64  TYR B CD2   1 
ATOM   6068  C  CE1   . TYR B 1 64  ? 153.238 148.512 157.320 1.00 45.37 ?  64  TYR B CE1   1 
ATOM   6069  C  CE2   . TYR B 1 64  ? 154.440 150.057 158.690 1.00 50.87 ?  64  TYR B CE2   1 
ATOM   6070  C  CZ    . TYR B 1 64  ? 153.738 148.881 158.547 1.00 50.19 ?  64  TYR B CZ    1 
ATOM   6071  O  OH    . TYR B 1 64  ? 153.539 148.075 159.641 1.00 55.95 ?  64  TYR B OH    1 
ATOM   6072  N  N     . GLU B 1 65  ? 152.814 152.875 153.132 1.00 56.36 ?  65  GLU B N     1 
ATOM   6073  C  CA    . GLU B 1 65  ? 152.617 154.088 152.353 1.00 57.07 ?  65  GLU B CA    1 
ATOM   6074  C  C     . GLU B 1 65  ? 153.254 155.258 153.089 1.00 58.36 ?  65  GLU B C     1 
ATOM   6075  O  O     . GLU B 1 65  ? 152.966 155.486 154.268 1.00 59.05 ?  65  GLU B O     1 
ATOM   6076  C  CB    . GLU B 1 65  ? 151.129 154.358 152.118 1.00 54.02 ?  65  GLU B CB    1 
ATOM   6077  C  CG    . GLU B 1 65  ? 150.435 153.322 151.253 1.00 52.75 ?  65  GLU B CG    1 
ATOM   6078  C  CD    . GLU B 1 65  ? 148.929 153.500 151.230 1.00 59.36 ?  65  GLU B CD    1 
ATOM   6079  O  OE1   . GLU B 1 65  ? 148.331 153.660 152.313 1.00 59.54 ?  65  GLU B OE1   1 
ATOM   6080  O  OE2   . GLU B 1 65  ? 148.343 153.480 150.126 1.00 56.85 -1 65  GLU B OE2   1 
ATOM   6081  N  N     . GLU B 1 66  ? 154.125 155.990 152.395 1.00 58.13 ?  66  GLU B N     1 
ATOM   6082  C  CA    . GLU B 1 66  ? 154.778 157.137 153.012 1.00 59.42 ?  66  GLU B CA    1 
ATOM   6083  C  C     . GLU B 1 66  ? 153.823 158.305 153.213 1.00 60.55 ?  66  GLU B C     1 
ATOM   6084  O  O     . GLU B 1 66  ? 154.104 159.184 154.036 1.00 58.82 ?  66  GLU B O     1 
ATOM   6085  C  CB    . GLU B 1 66  ? 155.974 157.576 152.161 1.00 61.14 ?  66  GLU B CB    1 
ATOM   6086  C  CG    . GLU B 1 66  ? 156.960 158.524 152.849 1.00 61.57 ?  66  GLU B CG    1 
ATOM   6087  C  CD    . GLU B 1 66  ? 157.326 158.102 154.263 1.00 65.09 ?  66  GLU B CD    1 
ATOM   6088  O  OE1   . GLU B 1 66  ? 156.565 158.410 155.204 1.00 63.13 ?  66  GLU B OE1   1 
ATOM   6089  O  OE2   . GLU B 1 66  ? 158.383 157.459 154.434 1.00 62.81 -1 66  GLU B OE2   1 
ATOM   6090  N  N     . GLU B 1 67  ? 152.700 158.332 152.491 1.00 58.11 ?  67  GLU B N     1 
ATOM   6091  C  CA    . GLU B 1 67  ? 151.799 159.478 152.553 1.00 55.39 ?  67  GLU B CA    1 
ATOM   6092  C  C     . GLU B 1 67  ? 151.176 159.628 153.936 1.00 59.38 ?  67  GLU B C     1 
ATOM   6093  O  O     . GLU B 1 67  ? 151.202 160.717 154.522 1.00 60.34 ?  67  GLU B O     1 
ATOM   6094  C  CB    . GLU B 1 67  ? 150.712 159.345 151.487 1.00 57.45 ?  67  GLU B CB    1 
ATOM   6095  C  CG    . GLU B 1 67  ? 151.244 159.255 150.068 1.00 58.19 ?  67  GLU B CG    1 
ATOM   6096  C  CD    . GLU B 1 67  ? 151.348 157.825 149.575 1.00 61.21 ?  67  GLU B CD    1 
ATOM   6097  O  OE1   . GLU B 1 67  ? 150.294 157.202 149.329 1.00 62.20 ?  67  GLU B OE1   1 
ATOM   6098  O  OE2   . GLU B 1 67  ? 152.483 157.325 149.433 1.00 62.48 -1 67  GLU B OE2   1 
ATOM   6099  N  N     . PHE B 1 68  ? 150.610 158.548 154.475 1.00 53.85 ?  68  PHE B N     1 
ATOM   6100  C  CA    . PHE B 1 68  ? 149.929 158.646 155.761 1.00 49.12 ?  68  PHE B CA    1 
ATOM   6101  C  C     . PHE B 1 68  ? 150.907 158.732 156.925 1.00 50.48 ?  68  PHE B C     1 
ATOM   6102  O  O     . PHE B 1 68  ? 150.594 159.357 157.944 1.00 54.75 ?  68  PHE B O     1 
ATOM   6103  C  CB    . PHE B 1 68  ? 148.965 157.467 155.944 1.00 49.06 ?  68  PHE B CB    1 
ATOM   6104  C  CG    . PHE B 1 68  ? 149.589 156.245 156.558 1.00 45.75 ?  68  PHE B CG    1 
ATOM   6105  C  CD1   . PHE B 1 68  ? 150.252 155.321 155.771 1.00 48.64 ?  68  PHE B CD1   1 
ATOM   6106  C  CD2   . PHE B 1 68  ? 149.485 156.002 157.919 1.00 45.10 ?  68  PHE B CD2   1 
ATOM   6107  C  CE1   . PHE B 1 68  ? 150.821 154.194 156.330 1.00 48.69 ?  68  PHE B CE1   1 
ATOM   6108  C  CE2   . PHE B 1 68  ? 150.052 154.876 158.482 1.00 47.79 ?  68  PHE B CE2   1 
ATOM   6109  C  CZ    . PHE B 1 68  ? 150.716 153.970 157.685 1.00 48.99 ?  68  PHE B CZ    1 
ATOM   6110  N  N     . LEU B 1 69  ? 152.086 158.120 156.801 1.00 48.84 ?  69  LEU B N     1 
ATOM   6111  C  CA    . LEU B 1 69  ? 153.073 158.202 157.871 1.00 50.00 ?  69  LEU B CA    1 
ATOM   6112  C  C     . LEU B 1 69  ? 153.748 159.566 157.924 1.00 53.07 ?  69  LEU B C     1 
ATOM   6113  O  O     . LEU B 1 69  ? 154.192 159.990 158.996 1.00 50.57 ?  69  LEU B O     1 
ATOM   6114  C  CB    . LEU B 1 69  ? 154.122 157.103 157.710 1.00 50.19 ?  69  LEU B CB    1 
ATOM   6115  C  CG    . LEU B 1 69  ? 153.719 155.729 158.248 1.00 49.96 ?  69  LEU B CG    1 
ATOM   6116  C  CD1   . LEU B 1 69  ? 154.746 154.676 157.867 1.00 50.10 ?  69  LEU B CD1   1 
ATOM   6117  C  CD2   . LEU B 1 69  ? 153.529 155.781 159.754 1.00 50.65 ?  69  LEU B CD2   1 
ATOM   6118  N  N     . SER B 1 70  ? 153.834 160.263 156.789 1.00 57.68 ?  70  SER B N     1 
ATOM   6119  C  CA    . SER B 1 70  ? 154.431 161.593 156.773 1.00 54.92 ?  70  SER B CA    1 
ATOM   6120  C  C     . SER B 1 70  ? 153.573 162.621 157.495 1.00 51.98 ?  70  SER B C     1 
ATOM   6121  O  O     . SER B 1 70  ? 154.061 163.715 157.797 1.00 53.93 ?  70  SER B O     1 
ATOM   6122  C  CB    . SER B 1 70  ? 154.676 162.047 155.335 1.00 53.34 ?  70  SER B CB    1 
ATOM   6123  O  OG    . SER B 1 70  ? 153.495 161.940 154.562 1.00 54.26 ?  70  SER B OG    1 
ATOM   6124  N  N     . LEU B 1 71  ? 152.309 162.299 157.772 1.00 46.56 ?  71  LEU B N     1 
ATOM   6125  C  CA    . LEU B 1 71  ? 151.419 163.224 158.461 1.00 46.13 ?  71  LEU B CA    1 
ATOM   6126  C  C     . LEU B 1 71  ? 151.780 163.407 159.927 1.00 47.72 ?  71  LEU B C     1 
ATOM   6127  O  O     . LEU B 1 71  ? 151.250 164.321 160.567 1.00 50.28 ?  71  LEU B O     1 
ATOM   6128  C  CB    . LEU B 1 71  ? 149.974 162.739 158.341 1.00 46.23 ?  71  LEU B CB    1 
ATOM   6129  C  CG    . LEU B 1 71  ? 149.314 162.936 156.976 1.00 50.87 ?  71  LEU B CG    1 
ATOM   6130  C  CD1   . LEU B 1 71  ? 147.805 162.865 157.099 1.00 48.61 ?  71  LEU B CD1   1 
ATOM   6131  C  CD2   . LEU B 1 71  ? 149.740 164.257 156.358 1.00 49.17 ?  71  LEU B CD2   1 
ATOM   6132  N  N     . TYR B 1 72  ? 152.659 162.570 160.470 1.00 45.28 ?  72  TYR B N     1 
ATOM   6133  C  CA    . TYR B 1 72  ? 153.078 162.651 161.860 1.00 44.42 ?  72  TYR B CA    1 
ATOM   6134  C  C     . TYR B 1 72  ? 154.585 162.833 161.936 1.00 48.54 ?  72  TYR B C     1 
ATOM   6135  O  O     . TYR B 1 72  ? 155.326 162.294 161.108 1.00 50.77 ?  72  TYR B O     1 
ATOM   6136  C  CB    . TYR B 1 72  ? 152.696 161.387 162.642 1.00 46.60 ?  72  TYR B CB    1 
ATOM   6137  C  CG    . TYR B 1 72  ? 151.275 160.915 162.452 1.00 44.13 ?  72  TYR B CG    1 
ATOM   6138  C  CD1   . TYR B 1 72  ? 150.936 160.083 161.396 1.00 40.51 ?  72  TYR B CD1   1 
ATOM   6139  C  CD2   . TYR B 1 72  ? 150.277 161.282 163.344 1.00 45.33 ?  72  TYR B CD2   1 
ATOM   6140  C  CE1   . TYR B 1 72  ? 149.644 159.647 161.221 1.00 40.64 ?  72  TYR B CE1   1 
ATOM   6141  C  CE2   . TYR B 1 72  ? 148.981 160.846 163.179 1.00 41.64 ?  72  TYR B CE2   1 
ATOM   6142  C  CZ    . TYR B 1 72  ? 148.670 160.028 162.115 1.00 42.12 ?  72  TYR B CZ    1 
ATOM   6143  O  OH    . TYR B 1 72  ? 147.380 159.591 161.943 1.00 47.11 ?  72  TYR B OH    1 
ATOM   6144  N  N     . SER B 1 73  ? 155.032 163.593 162.929 1.00 54.10 ?  73  SER B N     1 
ATOM   6145  C  CA    . SER B 1 73  ? 156.431 163.531 163.317 1.00 54.69 ?  73  SER B CA    1 
ATOM   6146  C  C     . SER B 1 73  ? 156.726 162.155 163.901 1.00 54.99 ?  73  SER B C     1 
ATOM   6147  O  O     . SER B 1 73  ? 155.840 161.488 164.443 1.00 58.63 ?  73  SER B O     1 
ATOM   6148  C  CB    . SER B 1 73  ? 156.758 164.623 164.334 1.00 53.07 ?  73  SER B CB    1 
ATOM   6149  O  OG    . SER B 1 73  ? 156.156 164.348 165.586 1.00 51.89 ?  73  SER B OG    1 
ATOM   6150  N  N     . PHE B 1 74  ? 157.981 161.719 163.775 1.00 56.10 ?  74  PHE B N     1 
ATOM   6151  C  CA    . PHE B 1 74  ? 158.321 160.380 164.246 1.00 55.84 ?  74  PHE B CA    1 
ATOM   6152  C  C     . PHE B 1 74  ? 158.086 160.230 165.744 1.00 55.08 ?  74  PHE B C     1 
ATOM   6153  O  O     . PHE B 1 74  ? 157.845 159.118 166.222 1.00 60.39 ?  74  PHE B O     1 
ATOM   6154  C  CB    . PHE B 1 74  ? 159.769 160.032 163.916 1.00 56.32 ?  74  PHE B CB    1 
ATOM   6155  C  CG    . PHE B 1 74  ? 160.216 158.732 164.519 1.00 57.06 ?  74  PHE B CG    1 
ATOM   6156  C  CD1   . PHE B 1 74  ? 159.706 157.533 164.053 1.00 56.22 ?  74  PHE B CD1   1 
ATOM   6157  C  CD2   . PHE B 1 74  ? 161.112 158.710 165.572 1.00 57.99 ?  74  PHE B CD2   1 
ATOM   6158  C  CE1   . PHE B 1 74  ? 160.098 156.335 164.611 1.00 58.61 ?  74  PHE B CE1   1 
ATOM   6159  C  CE2   . PHE B 1 74  ? 161.509 157.515 166.135 1.00 57.74 ?  74  PHE B CE2   1 
ATOM   6160  C  CZ    . PHE B 1 74  ? 161.000 156.326 165.655 1.00 59.91 ?  74  PHE B CZ    1 
ATOM   6161  N  N     . GLU B 1 75  ? 158.150 161.329 166.499 1.00 54.53 ?  75  GLU B N     1 
ATOM   6162  C  CA    . GLU B 1 75  ? 157.854 161.251 167.925 1.00 58.15 ?  75  GLU B CA    1 
ATOM   6163  C  C     . GLU B 1 75  ? 156.409 160.828 168.161 1.00 60.11 ?  75  GLU B C     1 
ATOM   6164  O  O     . GLU B 1 75  ? 156.127 160.018 169.051 1.00 60.42 ?  75  GLU B O     1 
ATOM   6165  C  CB    . GLU B 1 75  ? 158.139 162.595 168.595 1.00 56.36 ?  75  GLU B CB    1 
ATOM   6166  C  CG    . GLU B 1 75  ? 159.611 162.964 168.628 1.00 56.59 ?  75  GLU B CG    1 
ATOM   6167  C  CD    . GLU B 1 75  ? 160.479 161.844 169.169 1.00 63.42 ?  75  GLU B CD    1 
ATOM   6168  O  OE1   . GLU B 1 75  ? 160.272 161.437 170.332 1.00 63.49 ?  75  GLU B OE1   1 
ATOM   6169  O  OE2   . GLU B 1 75  ? 161.367 161.368 168.430 1.00 62.13 -1 75  GLU B OE2   1 
ATOM   6170  N  N     . ASP B 1 76  ? 155.480 161.363 167.367 1.00 55.72 ?  76  ASP B N     1 
ATOM   6171  C  CA    . ASP B 1 76  ? 154.076 160.992 167.512 1.00 54.37 ?  76  ASP B CA    1 
ATOM   6172  C  C     . ASP B 1 76  ? 153.853 159.522 167.174 1.00 55.43 ?  76  ASP B C     1 
ATOM   6173  O  O     . ASP B 1 76  ? 153.104 158.825 167.867 1.00 58.92 ?  76  ASP B O     1 
ATOM   6174  C  CB    . ASP B 1 76  ? 153.209 161.885 166.627 1.00 55.73 ?  76  ASP B CB    1 
ATOM   6175  C  CG    . ASP B 1 76  ? 153.266 163.340 167.039 1.00 58.99 ?  76  ASP B CG    1 
ATOM   6176  O  OD1   . ASP B 1 76  ? 153.295 163.614 168.257 1.00 59.14 ?  76  ASP B OD1   1 
ATOM   6177  O  OD2   . ASP B 1 76  ? 153.276 164.213 166.146 1.00 58.03 -1 76  ASP B OD2   1 
ATOM   6178  N  N     . ILE B 1 77  ? 154.493 159.035 166.109 1.00 48.13 ?  77  ILE B N     1 
ATOM   6179  C  CA    . ILE B 1 77  ? 154.372 157.624 165.748 1.00 49.21 ?  77  ILE B CA    1 
ATOM   6180  C  C     . ILE B 1 77  ? 154.964 156.744 166.841 1.00 50.79 ?  77  ILE B C     1 
ATOM   6181  O  O     . ILE B 1 77  ? 154.420 155.682 167.172 1.00 54.21 ?  77  ILE B O     1 
ATOM   6182  C  CB    . ILE B 1 77  ? 155.039 157.364 164.386 1.00 49.26 ?  77  ILE B CB    1 
ATOM   6183  C  CG1   . ILE B 1 77  ? 154.364 158.196 163.297 1.00 49.08 ?  77  ILE B CG1   1 
ATOM   6184  C  CG2   . ILE B 1 77  ? 154.974 155.888 164.034 1.00 49.31 ?  77  ILE B CG2   1 
ATOM   6185  C  CD1   . ILE B 1 77  ? 155.150 158.264 162.014 1.00 50.74 ?  77  ILE B CD1   1 
ATOM   6186  N  N     . LYS B 1 78  ? 156.092 157.169 167.411 1.00 52.56 ?  78  LYS B N     1 
ATOM   6187  C  CA    . LYS B 1 78  ? 156.705 156.418 168.499 1.00 51.80 ?  78  LYS B CA    1 
ATOM   6188  C  C     . LYS B 1 78  ? 155.786 156.360 169.710 1.00 52.98 ?  78  LYS B C     1 
ATOM   6189  O  O     . LYS B 1 78  ? 155.667 155.316 170.356 1.00 56.49 ?  78  LYS B O     1 
ATOM   6190  C  CB    . LYS B 1 78  ? 158.051 157.040 168.869 1.00 55.18 ?  78  LYS B CB    1 
ATOM   6191  C  CG    . LYS B 1 78  ? 158.817 156.276 169.933 1.00 54.95 ?  78  LYS B CG    1 
ATOM   6192  C  CD    . LYS B 1 78  ? 160.248 156.020 169.497 1.00 55.76 ?  78  LYS B CD    1 
ATOM   6193  C  CE    . LYS B 1 78  ? 161.240 156.572 170.504 1.00 57.25 ?  78  LYS B CE    1 
ATOM   6194  N  NZ    . LYS B 1 78  ? 162.646 156.425 170.037 1.00 55.90 1  78  LYS B NZ    1 
ATOM   6195  N  N     . GLU B 1 79  ? 155.121 157.472 170.032 1.00 53.27 ?  79  GLU B N     1 
ATOM   6196  C  CA    . GLU B 1 79  ? 154.185 157.463 171.153 1.00 52.11 ?  79  GLU B CA    1 
ATOM   6197  C  C     . GLU B 1 79  ? 152.959 156.607 170.860 1.00 51.11 ?  79  GLU B C     1 
ATOM   6198  O  O     . GLU B 1 79  ? 152.422 155.967 171.770 1.00 52.30 ?  79  GLU B O     1 
ATOM   6199  C  CB    . GLU B 1 79  ? 153.770 158.891 171.509 1.00 52.64 ?  79  GLU B CB    1 
ATOM   6200  C  CG    . GLU B 1 79  ? 154.911 159.805 171.960 1.00 56.29 ?  79  GLU B CG    1 
ATOM   6201  C  CD    . GLU B 1 79  ? 156.000 159.093 172.757 1.00 58.47 ?  79  GLU B CD    1 
ATOM   6202  O  OE1   . GLU B 1 79  ? 157.190 159.402 172.532 1.00 56.16 ?  79  GLU B OE1   1 
ATOM   6203  O  OE2   . GLU B 1 79  ? 155.677 158.269 173.641 1.00 57.13 -1 79  GLU B OE2   1 
ATOM   6204  N  N     . VAL B 1 80  ? 152.507 156.575 169.606 1.00 48.64 ?  80  VAL B N     1 
ATOM   6205  C  CA    . VAL B 1 80  ? 151.396 155.699 169.241 1.00 45.07 ?  80  VAL B CA    1 
ATOM   6206  C  C     . VAL B 1 80  ? 151.787 154.235 169.423 1.00 48.97 ?  80  VAL B C     1 
ATOM   6207  O  O     . VAL B 1 80  ? 151.029 153.434 169.989 1.00 51.77 ?  80  VAL B O     1 
ATOM   6208  C  CB    . VAL B 1 80  ? 150.943 155.998 167.799 1.00 44.98 ?  80  VAL B CB    1 
ATOM   6209  C  CG1   . VAL B 1 80  ? 150.060 154.890 167.268 1.00 46.55 ?  80  VAL B CG1   1 
ATOM   6210  C  CG2   . VAL B 1 80  ? 150.214 157.330 167.743 1.00 45.90 ?  80  VAL B CG2   1 
ATOM   6211  N  N     . PHE B 1 81  ? 152.985 153.867 168.962 1.00 47.44 ?  81  PHE B N     1 
ATOM   6212  C  CA    . PHE B 1 81  ? 153.468 152.504 169.160 1.00 44.10 ?  81  PHE B CA    1 
ATOM   6213  C  C     . PHE B 1 81  ? 153.659 152.197 170.642 1.00 45.61 ?  81  PHE B C     1 
ATOM   6214  O  O     . PHE B 1 81  ? 153.422 151.067 171.085 1.00 51.04 ?  81  PHE B O     1 
ATOM   6215  C  CB    . PHE B 1 81  ? 154.772 152.291 168.392 1.00 43.36 ?  81  PHE B CB    1 
ATOM   6216  C  CG    . PHE B 1 81  ? 154.573 151.838 166.975 1.00 43.48 ?  81  PHE B CG    1 
ATOM   6217  C  CD1   . PHE B 1 81  ? 154.218 152.739 165.986 1.00 44.24 ?  81  PHE B CD1   1 
ATOM   6218  C  CD2   . PHE B 1 81  ? 154.746 150.509 166.631 1.00 43.71 ?  81  PHE B CD2   1 
ATOM   6219  C  CE1   . PHE B 1 81  ? 154.036 152.322 164.683 1.00 44.16 ?  81  PHE B CE1   1 
ATOM   6220  C  CE2   . PHE B 1 81  ? 154.564 150.087 165.329 1.00 45.21 ?  81  PHE B CE2   1 
ATOM   6221  C  CZ    . PHE B 1 81  ? 154.209 150.996 164.354 1.00 43.39 ?  81  PHE B CZ    1 
ATOM   6222  N  N     . LYS B 1 82  ? 154.091 153.189 171.421 1.00 47.11 ?  82  LYS B N     1 
ATOM   6223  C  CA    . LYS B 1 82  ? 154.188 153.024 172.868 1.00 51.39 ?  82  LYS B CA    1 
ATOM   6224  C  C     . LYS B 1 82  ? 152.825 152.717 173.469 1.00 51.71 ?  82  LYS B C     1 
ATOM   6225  O  O     . LYS B 1 82  ? 152.692 151.842 174.332 1.00 51.17 ?  82  LYS B O     1 
ATOM   6226  C  CB    . LYS B 1 82  ? 154.769 154.289 173.498 1.00 53.58 ?  82  LYS B CB    1 
ATOM   6227  C  CG    . LYS B 1 82  ? 156.114 154.119 174.177 1.00 53.04 ?  82  LYS B CG    1 
ATOM   6228  C  CD    . LYS B 1 82  ? 157.249 154.049 173.176 1.00 54.24 ?  82  LYS B CD    1 
ATOM   6229  C  CE    . LYS B 1 82  ? 158.585 154.243 173.873 1.00 55.14 ?  82  LYS B CE    1 
ATOM   6230  N  NZ    . LYS B 1 82  ? 159.643 153.351 173.332 1.00 56.03 1  82  LYS B NZ    1 
ATOM   6231  N  N     . THR B 1 83  ? 151.797 153.441 173.024 1.00 47.16 ?  83  THR B N     1 
ATOM   6232  C  CA    . THR B 1 83  ? 150.445 153.201 173.513 1.00 45.62 ?  83  THR B CA    1 
ATOM   6233  C  C     . THR B 1 83  ? 149.972 151.799 173.156 1.00 47.50 ?  83  THR B C     1 
ATOM   6234  O  O     . THR B 1 83  ? 149.310 151.134 173.962 1.00 51.83 ?  83  THR B O     1 
ATOM   6235  C  CB    . THR B 1 83  ? 149.489 154.252 172.949 1.00 45.08 ?  83  THR B CB    1 
ATOM   6236  O  OG1   . THR B 1 83  ? 150.019 155.559 173.199 1.00 51.98 ?  83  THR B OG1   1 
ATOM   6237  C  CG2   . THR B 1 83  ? 148.126 154.138 173.603 1.00 47.96 ?  83  THR B CG2   1 
ATOM   6238  N  N     . ALA B 1 84  ? 150.297 151.332 171.948 1.00 41.73 ?  84  ALA B N     1 
ATOM   6239  C  CA    . ALA B 1 84  ? 149.913 149.976 171.567 1.00 38.19 ?  84  ALA B CA    1 
ATOM   6240  C  C     . ALA B 1 84  ? 150.605 148.932 172.436 1.00 41.93 ?  84  ALA B C     1 
ATOM   6241  O  O     . ALA B 1 84  ? 149.972 147.962 172.869 1.00 50.02 ?  84  ALA B O     1 
ATOM   6242  C  CB    . ALA B 1 84  ? 150.227 149.733 170.095 1.00 41.37 ?  84  ALA B CB    1 
ATOM   6243  N  N     . TYR B 1 85  ? 151.900 149.108 172.699 1.00 48.73 ?  85  TYR B N     1 
ATOM   6244  C  CA    . TYR B 1 85  ? 152.639 148.139 173.498 1.00 44.08 ?  85  TYR B CA    1 
ATOM   6245  C  C     . TYR B 1 85  ? 152.465 148.349 174.995 1.00 45.71 ?  85  TYR B C     1 
ATOM   6246  O  O     . TYR B 1 85  ? 152.835 147.466 175.775 1.00 48.79 ?  85  TYR B O     1 
ATOM   6247  C  CB    . TYR B 1 85  ? 154.127 148.183 173.140 1.00 45.03 ?  85  TYR B CB    1 
ATOM   6248  C  CG    . TYR B 1 85  ? 154.461 147.515 171.827 1.00 45.73 ?  85  TYR B CG    1 
ATOM   6249  C  CD1   . TYR B 1 85  ? 154.394 148.215 170.631 1.00 45.47 ?  85  TYR B CD1   1 
ATOM   6250  C  CD2   . TYR B 1 85  ? 154.846 146.183 171.784 1.00 45.37 ?  85  TYR B CD2   1 
ATOM   6251  C  CE1   . TYR B 1 85  ? 154.700 147.609 169.431 1.00 45.26 ?  85  TYR B CE1   1 
ATOM   6252  C  CE2   . TYR B 1 85  ? 155.153 145.568 170.588 1.00 45.88 ?  85  TYR B CE2   1 
ATOM   6253  C  CZ    . TYR B 1 85  ? 155.078 146.286 169.416 1.00 47.44 ?  85  TYR B CZ    1 
ATOM   6254  O  OH    . TYR B 1 85  ? 155.384 145.677 168.223 1.00 49.52 ?  85  TYR B OH    1 
ATOM   6255  N  N     . ALA B 1 86  ? 151.916 149.491 175.416 1.00 48.77 ?  86  ALA B N     1 
ATOM   6256  C  CA    . ALA B 1 86  ? 151.679 149.715 176.837 1.00 49.11 ?  86  ALA B CA    1 
ATOM   6257  C  C     . ALA B 1 86  ? 150.603 148.795 177.394 1.00 51.18 ?  86  ALA B C     1 
ATOM   6258  O  O     . ALA B 1 86  ? 150.594 148.533 178.601 1.00 50.07 ?  86  ALA B O     1 
ATOM   6259  C  CB    . ALA B 1 86  ? 151.290 151.172 177.090 1.00 45.01 ?  86  ALA B CB    1 
ATOM   6260  N  N     . LYS B 1 87  ? 149.698 148.304 176.548 1.00 43.59 ?  87  LYS B N     1 
ATOM   6261  C  CA    . LYS B 1 87  ? 148.640 147.415 177.006 1.00 43.37 ?  87  LYS B CA    1 
ATOM   6262  C  C     . LYS B 1 87  ? 149.140 146.009 177.305 1.00 46.64 ?  87  LYS B C     1 
ATOM   6263  O  O     . LYS B 1 87  ? 148.482 145.285 178.060 1.00 46.53 ?  87  LYS B O     1 
ATOM   6264  C  CB    . LYS B 1 87  ? 147.522 147.347 175.964 1.00 46.41 ?  87  LYS B CB    1 
ATOM   6265  C  CG    . LYS B 1 87  ? 146.144 147.100 176.551 1.00 47.31 ?  87  LYS B CG    1 
ATOM   6266  C  CD    . LYS B 1 87  ? 145.483 145.891 175.914 1.00 43.91 ?  87  LYS B CD    1 
ATOM   6267  C  CE    . LYS B 1 87  ? 144.245 145.471 176.686 1.00 43.53 ?  87  LYS B CE    1 
ATOM   6268  N  NZ    . LYS B 1 87  ? 143.549 144.323 176.040 1.00 41.20 1  87  LYS B NZ    1 
ATOM   6269  N  N     . LYS B 1 88  ? 150.284 145.616 176.742 1.00 51.97 ?  88  LYS B N     1 
ATOM   6270  C  CA    . LYS B 1 88  ? 150.821 144.264 176.889 1.00 47.74 ?  88  LYS B CA    1 
ATOM   6271  C  C     . LYS B 1 88  ? 149.771 143.223 176.508 1.00 46.69 ?  88  LYS B C     1 
ATOM   6272  O  O     . LYS B 1 88  ? 149.495 142.278 177.248 1.00 49.88 ?  88  LYS B O     1 
ATOM   6273  C  CB    . LYS B 1 88  ? 151.344 144.027 178.307 1.00 48.98 ?  88  LYS B CB    1 
ATOM   6274  C  CG    . LYS B 1 88  ? 152.174 145.171 178.863 1.00 47.10 ?  88  LYS B CG    1 
ATOM   6275  C  CD    . LYS B 1 88  ? 153.525 144.685 179.357 1.00 50.61 ?  88  LYS B CD    1 
ATOM   6276  C  CE    . LYS B 1 88  ? 153.387 143.886 180.641 1.00 52.66 ?  88  LYS B CE    1 
ATOM   6277  N  NZ    . LYS B 1 88  ? 154.599 143.064 180.918 1.00 51.45 1  88  LYS B NZ    1 
ATOM   6278  N  N     . PHE B 1 89  ? 149.172 143.418 175.334 1.00 45.43 ?  89  PHE B N     1 
ATOM   6279  C  CA    . PHE B 1 89  ? 148.082 142.557 174.898 1.00 40.04 ?  89  PHE B CA    1 
ATOM   6280  C  C     . PHE B 1 89  ? 148.571 141.130 174.693 1.00 42.32 ?  89  PHE B C     1 
ATOM   6281  O  O     . PHE B 1 89  ? 149.615 140.898 174.081 1.00 43.62 ?  89  PHE B O     1 
ATOM   6282  C  CB    . PHE B 1 89  ? 147.468 143.091 173.604 1.00 39.99 ?  89  PHE B CB    1 
ATOM   6283  C  CG    . PHE B 1 89  ? 146.454 142.167 172.994 1.00 38.98 ?  89  PHE B CG    1 
ATOM   6284  C  CD1   . PHE B 1 89  ? 145.159 142.129 173.476 1.00 37.21 ?  89  PHE B CD1   1 
ATOM   6285  C  CD2   . PHE B 1 89  ? 146.798 141.330 171.948 1.00 39.03 ?  89  PHE B CD2   1 
ATOM   6286  C  CE1   . PHE B 1 89  ? 144.226 141.280 172.925 1.00 39.04 ?  89  PHE B CE1   1 
ATOM   6287  C  CE2   . PHE B 1 89  ? 145.868 140.477 171.393 1.00 35.00 ?  89  PHE B CE2   1 
ATOM   6288  C  CZ    . PHE B 1 89  ? 144.581 140.452 171.881 1.00 38.35 ?  89  PHE B CZ    1 
ATOM   6289  N  N     . ARG B 1 90  ? 147.802 140.174 175.203 1.00 43.49 ?  90  ARG B N     1 
ATOM   6290  C  CA    . ARG B 1 90  ? 148.097 138.758 175.053 1.00 43.41 ?  90  ARG B CA    1 
ATOM   6291  C  C     . ARG B 1 90  ? 146.922 138.077 174.369 1.00 43.90 ?  90  ARG B C     1 
ATOM   6292  O  O     . ARG B 1 90  ? 145.771 138.271 174.771 1.00 47.64 ?  90  ARG B O     1 
ATOM   6293  C  CB    . ARG B 1 90  ? 148.373 138.103 176.408 1.00 46.45 ?  90  ARG B CB    1 
ATOM   6294  C  CG    . ARG B 1 90  ? 149.545 138.704 177.157 1.00 46.45 ?  90  ARG B CG    1 
ATOM   6295  C  CD    . ARG B 1 90  ? 150.849 138.043 176.754 1.00 48.43 ?  90  ARG B CD    1 
ATOM   6296  N  NE    . ARG B 1 90  ? 151.623 138.882 175.848 1.00 51.01 ?  90  ARG B NE    1 
ATOM   6297  C  CZ    . ARG B 1 90  ? 152.351 139.923 176.227 1.00 49.77 ?  90  ARG B CZ    1 
ATOM   6298  N  NH1   . ARG B 1 90  ? 152.446 140.275 177.499 1.00 47.15 1  90  ARG B NH1   1 
ATOM   6299  N  NH2   . ARG B 1 90  ? 153.001 140.630 175.307 1.00 51.52 ?  90  ARG B NH2   1 
ATOM   6300  N  N     . PHE B 1 91  ? 147.214 137.296 173.342 1.00 36.62 ?  91  PHE B N     1 
ATOM   6301  C  CA    . PHE B 1 91  ? 146.180 136.491 172.712 1.00 39.12 ?  91  PHE B CA    1 
ATOM   6302  C  C     . PHE B 1 91  ? 145.734 135.405 173.684 1.00 44.74 ?  91  PHE B C     1 
ATOM   6303  O  O     . PHE B 1 91  ? 146.570 134.641 174.178 1.00 45.97 ?  91  PHE B O     1 
ATOM   6304  C  CB    . PHE B 1 91  ? 146.698 135.869 171.420 1.00 39.16 ?  91  PHE B CB    1 
ATOM   6305  C  CG    . PHE B 1 91  ? 146.790 136.837 170.275 1.00 40.47 ?  91  PHE B CG    1 
ATOM   6306  C  CD1   . PHE B 1 91  ? 145.650 137.264 169.617 1.00 43.58 ?  91  PHE B CD1   1 
ATOM   6307  C  CD2   . PHE B 1 91  ? 148.017 137.319 169.857 1.00 42.01 ?  91  PHE B CD2   1 
ATOM   6308  C  CE1   . PHE B 1 91  ? 145.733 138.150 168.563 1.00 40.28 ?  91  PHE B CE1   1 
ATOM   6309  C  CE2   . PHE B 1 91  ? 148.105 138.205 168.804 1.00 40.89 ?  91  PHE B CE2   1 
ATOM   6310  C  CZ    . PHE B 1 91  ? 146.961 138.621 168.156 1.00 36.90 ?  91  PHE B CZ    1 
ATOM   6311  N  N     . PRO B 1 92  ? 144.438 135.304 173.990 1.00 44.11 ?  92  PRO B N     1 
ATOM   6312  C  CA    . PRO B 1 92  ? 144.008 134.320 174.993 1.00 40.42 ?  92  PRO B CA    1 
ATOM   6313  C  C     . PRO B 1 92  ? 144.070 132.889 174.496 1.00 39.94 ?  92  PRO B C     1 
ATOM   6314  O  O     . PRO B 1 92  ? 144.274 131.973 175.303 1.00 43.37 ?  92  PRO B O     1 
ATOM   6315  C  CB    . PRO B 1 92  ? 142.569 134.750 175.303 1.00 40.58 ?  92  PRO B CB    1 
ATOM   6316  C  CG    . PRO B 1 92  ? 142.104 135.381 174.039 1.00 40.82 ?  92  PRO B CG    1 
ATOM   6317  C  CD    . PRO B 1 92  ? 143.303 136.055 173.427 1.00 42.53 ?  92  PRO B CD    1 
ATOM   6318  N  N     . SER B 1 93  ? 143.907 132.667 173.198 1.00 38.53 ?  93  SER B N     1 
ATOM   6319  C  CA    . SER B 1 93  ? 143.857 131.332 172.630 1.00 40.38 ?  93  SER B CA    1 
ATOM   6320  C  C     . SER B 1 93  ? 144.870 131.224 171.502 1.00 42.60 ?  93  SER B C     1 
ATOM   6321  O  O     . SER B 1 93  ? 145.307 132.227 170.933 1.00 47.55 ?  93  SER B O     1 
ATOM   6322  C  CB    . SER B 1 93  ? 142.451 131.001 172.114 1.00 44.04 ?  93  SER B CB    1 
ATOM   6323  O  OG    . SER B 1 93  ? 142.362 131.202 170.716 1.00 50.00 ?  93  SER B OG    1 
ATOM   6324  N  N     . PHE B 1 94  ? 145.253 129.985 171.190 1.00 41.90 ?  94  PHE B N     1 
ATOM   6325  C  CA    . PHE B 1 94  ? 146.190 129.766 170.095 1.00 40.14 ?  94  PHE B CA    1 
ATOM   6326  C  C     . PHE B 1 94  ? 145.588 130.174 168.758 1.00 42.76 ?  94  PHE B C     1 
ATOM   6327  O  O     . PHE B 1 94  ? 146.294 130.692 167.888 1.00 47.43 ?  94  PHE B O     1 
ATOM   6328  C  CB    . PHE B 1 94  ? 146.633 128.305 170.052 1.00 40.16 ?  94  PHE B CB    1 
ATOM   6329  C  CG    . PHE B 1 94  ? 147.214 127.897 168.732 1.00 41.76 ?  94  PHE B CG    1 
ATOM   6330  C  CD1   . PHE B 1 94  ? 148.446 128.379 168.328 1.00 42.32 ?  94  PHE B CD1   1 
ATOM   6331  C  CD2   . PHE B 1 94  ? 146.523 127.052 167.883 1.00 43.73 ?  94  PHE B CD2   1 
ATOM   6332  C  CE1   . PHE B 1 94  ? 148.978 128.020 167.110 1.00 42.88 ?  94  PHE B CE1   1 
ATOM   6333  C  CE2   . PHE B 1 94  ? 147.056 126.689 166.664 1.00 41.04 ?  94  PHE B CE2   1 
ATOM   6334  C  CZ    . PHE B 1 94  ? 148.283 127.173 166.278 1.00 40.39 ?  94  PHE B CZ    1 
ATOM   6335  N  N     . MET B 1 95  ? 144.288 129.938 168.572 1.00 38.81 ?  95  MET B N     1 
ATOM   6336  C  CA    . MET B 1 95  ? 143.666 130.222 167.284 1.00 34.84 ?  95  MET B CA    1 
ATOM   6337  C  C     . MET B 1 95  ? 143.632 131.713 166.980 1.00 41.06 ?  95  MET B C     1 
ATOM   6338  O  O     . MET B 1 95  ? 143.753 132.099 165.815 1.00 43.38 ?  95  MET B O     1 
ATOM   6339  C  CB    . MET B 1 95  ? 142.257 129.633 167.232 1.00 41.10 ?  95  MET B CB    1 
ATOM   6340  C  CG    . MET B 1 95  ? 141.543 129.759 165.882 1.00 45.93 ?  95  MET B CG    1 
ATOM   6341  S  SD    . MET B 1 95  ? 142.277 129.062 164.376 1.00 55.90 ?  95  MET B SD    1 
ATOM   6342  C  CE    . MET B 1 95  ? 143.358 127.769 164.981 1.00 43.07 ?  95  MET B CE    1 
ATOM   6343  N  N     . SER B 1 96  ? 143.483 132.561 167.998 1.00 36.73 ?  96  SER B N     1 
ATOM   6344  C  CA    . SER B 1 96  ? 143.512 134.003 167.764 1.00 33.30 ?  96  SER B CA    1 
ATOM   6345  C  C     . SER B 1 96  ? 144.842 134.434 167.159 1.00 36.80 ?  96  SER B C     1 
ATOM   6346  O  O     . SER B 1 96  ? 144.885 135.081 166.102 1.00 32.79 ?  96  SER B O     1 
ATOM   6347  C  CB    . SER B 1 96  ? 143.259 134.743 169.076 1.00 36.01 ?  96  SER B CB    1 
ATOM   6348  O  OG    . SER B 1 96  ? 142.285 134.077 169.856 1.00 42.95 ?  96  SER B OG    1 
ATOM   6349  N  N     . ALA B 1 97  ? 145.944 134.065 167.815 1.00 36.06 ?  97  ALA B N     1 
ATOM   6350  C  CA    . ALA B 1 97  ? 147.269 134.426 167.327 1.00 32.56 ?  97  ALA B CA    1 
ATOM   6351  C  C     . ALA B 1 97  ? 147.562 133.772 165.985 1.00 34.38 ?  97  ALA B C     1 
ATOM   6352  O  O     . ALA B 1 97  ? 148.152 134.400 165.101 1.00 40.22 ?  97  ALA B O     1 
ATOM   6353  C  CB    . ALA B 1 97  ? 148.327 134.034 168.354 1.00 38.51 ?  97  ALA B CB    1 
ATOM   6354  N  N     . PHE B 1 98  ? 147.170 132.509 165.822 1.00 37.04 ?  98  PHE B N     1 
ATOM   6355  C  CA    . PHE B 1 98  ? 147.404 131.816 164.561 1.00 34.05 ?  98  PHE B CA    1 
ATOM   6356  C  C     . PHE B 1 98  ? 146.679 132.509 163.416 1.00 36.17 ?  98  PHE B C     1 
ATOM   6357  O  O     . PHE B 1 98  ? 147.261 132.750 162.354 1.00 48.45 ?  98  PHE B O     1 
ATOM   6358  C  CB    . PHE B 1 98  ? 146.964 130.357 164.674 1.00 39.75 ?  98  PHE B CB    1 
ATOM   6359  C  CG    . PHE B 1 98  ? 147.067 129.594 163.386 1.00 39.93 ?  98  PHE B CG    1 
ATOM   6360  C  CD1   . PHE B 1 98  ? 148.278 129.067 162.974 1.00 39.71 ?  98  PHE B CD1   1 
ATOM   6361  C  CD2   . PHE B 1 98  ? 145.952 129.403 162.587 1.00 41.60 ?  98  PHE B CD2   1 
ATOM   6362  C  CE1   . PHE B 1 98  ? 148.375 128.366 161.790 1.00 39.50 ?  98  PHE B CE1   1 
ATOM   6363  C  CE2   . PHE B 1 98  ? 146.046 128.705 161.401 1.00 44.69 ?  98  PHE B CE2   1 
ATOM   6364  C  CZ    . PHE B 1 98  ? 147.258 128.185 161.003 1.00 43.40 ?  98  PHE B CZ    1 
ATOM   6365  N  N     . LYS B 1 99  ? 145.405 132.850 163.621 1.00 41.42 ?  99  LYS B N     1 
ATOM   6366  C  CA    . LYS B 1 99  ? 144.639 133.515 162.577 1.00 39.05 ?  99  LYS B CA    1 
ATOM   6367  C  C     . LYS B 1 99  ? 145.223 134.880 162.253 1.00 37.72 ?  99  LYS B C     1 
ATOM   6368  O  O     . LYS B 1 99  ? 145.343 135.245 161.079 1.00 42.56 ?  99  LYS B O     1 
ATOM   6369  C  CB    . LYS B 1 99  ? 143.176 133.639 162.998 1.00 37.97 ?  99  LYS B CB    1 
ATOM   6370  C  CG    . LYS B 1 99  ? 142.367 132.370 162.800 1.00 42.93 ?  99  LYS B CG    1 
ATOM   6371  C  CD    . LYS B 1 99  ? 142.471 131.862 161.375 1.00 42.94 ?  99  LYS B CD    1 
ATOM   6372  C  CE    . LYS B 1 99  ? 141.241 131.065 160.985 1.00 42.46 ?  99  LYS B CE    1 
ATOM   6373  N  NZ    . LYS B 1 99  ? 140.746 131.442 159.634 1.00 47.99 1  99  LYS B NZ    1 
ATOM   6374  N  N     . PHE B 1 100 ? 145.615 135.646 163.275 1.00 36.96 ?  100 PHE B N     1 
ATOM   6375  C  CA    . PHE B 1 100 ? 146.194 136.955 162.995 1.00 34.43 ?  100 PHE B CA    1 
ATOM   6376  C  C     . PHE B 1 100 ? 147.499 136.827 162.219 1.00 37.14 ?  100 PHE B C     1 
ATOM   6377  O  O     . PHE B 1 100 ? 147.677 137.461 161.175 1.00 41.84 ?  100 PHE B O     1 
ATOM   6378  C  CB    . PHE B 1 100 ? 146.431 137.747 164.278 1.00 34.19 ?  100 PHE B CB    1 
ATOM   6379  C  CG    . PHE B 1 100 ? 147.124 139.053 164.034 1.00 37.70 ?  100 PHE B CG    1 
ATOM   6380  C  CD1   . PHE B 1 100 ? 146.449 140.105 163.437 1.00 37.53 ?  100 PHE B CD1   1 
ATOM   6381  C  CD2   . PHE B 1 100 ? 148.459 139.216 164.349 1.00 34.09 ?  100 PHE B CD2   1 
ATOM   6382  C  CE1   . PHE B 1 100 ? 147.087 141.301 163.187 1.00 37.84 ?  100 PHE B CE1   1 
ATOM   6383  C  CE2   . PHE B 1 100 ? 149.100 140.408 164.100 1.00 35.09 ?  100 PHE B CE2   1 
ATOM   6384  C  CZ    . PHE B 1 100 ? 148.414 141.453 163.521 1.00 37.50 ?  100 PHE B CZ    1 
ATOM   6385  N  N     . TYR B 1 101 ? 148.418 135.996 162.703 1.00 40.14 ?  101 TYR B N     1 
ATOM   6386  C  CA    . TYR B 1 101 ? 149.730 135.893 162.084 1.00 36.34 ?  101 TYR B CA    1 
ATOM   6387  C  C     . TYR B 1 101 ? 149.721 135.070 160.804 1.00 35.53 ?  101 TYR B C     1 
ATOM   6388  O  O     . TYR B 1 101 ? 150.759 134.979 160.143 1.00 44.77 ?  101 TYR B O     1 
ATOM   6389  C  CB    . TYR B 1 101 ? 150.733 135.317 163.085 1.00 35.64 ?  101 TYR B CB    1 
ATOM   6390  C  CG    . TYR B 1 101 ? 151.137 136.323 164.136 1.00 33.35 ?  101 TYR B CG    1 
ATOM   6391  C  CD1   . TYR B 1 101 ? 151.966 137.390 163.821 1.00 34.17 ?  101 TYR B CD1   1 
ATOM   6392  C  CD2   . TYR B 1 101 ? 150.666 136.223 165.436 1.00 37.40 ?  101 TYR B CD2   1 
ATOM   6393  C  CE1   . TYR B 1 101 ? 152.326 138.318 164.774 1.00 36.52 ?  101 TYR B CE1   1 
ATOM   6394  C  CE2   . TYR B 1 101 ? 151.020 137.146 166.394 1.00 39.90 ?  101 TYR B CE2   1 
ATOM   6395  C  CZ    . TYR B 1 101 ? 151.850 138.191 166.059 1.00 40.02 ?  101 TYR B CZ    1 
ATOM   6396  O  OH    . TYR B 1 101 ? 152.203 139.111 167.017 1.00 39.82 ?  101 TYR B OH    1 
ATOM   6397  N  N     . ASN B 1 102 ? 148.589 134.467 160.442 1.00 38.82 ?  102 ASN B N     1 
ATOM   6398  C  CA    . ASN B 1 102 ? 148.473 133.797 159.157 1.00 41.96 ?  102 ASN B CA    1 
ATOM   6399  C  C     . ASN B 1 102 ? 147.641 134.569 158.142 1.00 43.72 ?  102 ASN B C     1 
ATOM   6400  O  O     . ASN B 1 102 ? 147.762 134.300 156.942 1.00 48.13 ?  102 ASN B O     1 
ATOM   6401  C  CB    . ASN B 1 102 ? 147.863 132.402 159.341 1.00 40.56 ?  102 ASN B CB    1 
ATOM   6402  C  CG    . ASN B 1 102 ? 148.910 131.340 159.612 1.00 44.81 ?  102 ASN B CG    1 
ATOM   6403  O  OD1   . ASN B 1 102 ? 149.778 131.511 160.469 1.00 48.40 ?  102 ASN B OD1   1 
ATOM   6404  N  ND2   . ASN B 1 102 ? 148.834 130.236 158.880 1.00 43.12 ?  102 ASN B ND2   1 
ATOM   6405  N  N     . ASP B 1 103 ? 146.805 135.511 158.578 1.00 42.99 ?  103 ASP B N     1 
ATOM   6406  C  CA    . ASP B 1 103 ? 145.933 136.223 157.652 1.00 42.91 ?  103 ASP B CA    1 
ATOM   6407  C  C     . ASP B 1 103 ? 146.199 137.718 157.576 1.00 42.58 ?  103 ASP B C     1 
ATOM   6408  O  O     . ASP B 1 103 ? 146.083 138.299 156.496 1.00 46.97 ?  103 ASP B O     1 
ATOM   6409  C  CB    . ASP B 1 103 ? 144.462 135.998 158.040 1.00 45.28 ?  103 ASP B CB    1 
ATOM   6410  C  CG    . ASP B 1 103 ? 144.034 134.551 157.897 1.00 50.09 ?  103 ASP B CG    1 
ATOM   6411  O  OD1   . ASP B 1 103 ? 144.844 133.729 157.423 1.00 50.18 ?  103 ASP B OD1   1 
ATOM   6412  O  OD2   . ASP B 1 103 ? 142.884 134.233 158.265 1.00 53.52 -1 103 ASP B OD2   1 
ATOM   6413  N  N     . TYR B 1 104 ? 146.551 138.361 158.687 1.00 36.66 ?  104 TYR B N     1 
ATOM   6414  C  CA    . TYR B 1 104 ? 146.615 139.813 158.751 1.00 41.43 ?  104 TYR B CA    1 
ATOM   6415  C  C     . TYR B 1 104 ? 148.000 140.368 159.039 1.00 39.97 ?  104 TYR B C     1 
ATOM   6416  O  O     . TYR B 1 104 ? 148.271 141.513 158.674 1.00 45.56 ?  104 TYR B O     1 
ATOM   6417  C  CB    . TYR B 1 104 ? 145.645 140.340 159.820 1.00 37.76 ?  104 TYR B CB    1 
ATOM   6418  C  CG    . TYR B 1 104 ? 144.227 139.862 159.627 1.00 41.00 ?  104 TYR B CG    1 
ATOM   6419  C  CD1   . TYR B 1 104 ? 143.358 140.539 158.784 1.00 40.31 ?  104 TYR B CD1   1 
ATOM   6420  C  CD2   . TYR B 1 104 ? 143.760 138.731 160.280 1.00 35.66 ?  104 TYR B CD2   1 
ATOM   6421  C  CE1   . TYR B 1 104 ? 142.064 140.105 158.600 1.00 39.93 ?  104 TYR B CE1   1 
ATOM   6422  C  CE2   . TYR B 1 104 ? 142.467 138.288 160.101 1.00 36.77 ?  104 TYR B CE2   1 
ATOM   6423  C  CZ    . TYR B 1 104 ? 141.623 138.980 159.260 1.00 41.95 ?  104 TYR B CZ    1 
ATOM   6424  O  OH    . TYR B 1 104 ? 140.332 138.546 159.076 1.00 41.50 ?  104 TYR B OH    1 
ATOM   6425  N  N     . ALA B 1 105 ? 148.875 139.604 159.687 1.00 42.71 ?  105 ALA B N     1 
ATOM   6426  C  CA    . ALA B 1 105 ? 150.209 140.102 159.992 1.00 42.57 ?  105 ALA B CA    1 
ATOM   6427  C  C     . ALA B 1 105 ? 151.014 140.291 158.715 1.00 45.88 ?  105 ALA B C     1 
ATOM   6428  O  O     . ALA B 1 105 ? 150.978 139.454 157.808 1.00 44.64 ?  105 ALA B O     1 
ATOM   6429  C  CB    . ALA B 1 105 ? 150.935 139.143 160.931 1.00 38.01 ?  105 ALA B CB    1 
ATOM   6430  N  N     . LEU B 1 106 ? 151.740 141.403 158.645 1.00 47.08 ?  106 LEU B N     1 
ATOM   6431  C  CA    . LEU B 1 106 ? 152.555 141.689 157.473 1.00 44.38 ?  106 LEU B CA    1 
ATOM   6432  C  C     . LEU B 1 106 ? 153.755 140.754 157.428 1.00 47.36 ?  106 LEU B C     1 
ATOM   6433  O  O     . LEU B 1 106 ? 154.484 140.611 158.413 1.00 47.74 ?  106 LEU B O     1 
ATOM   6434  C  CB    . LEU B 1 106 ? 153.016 143.145 157.488 1.00 48.24 ?  106 LEU B CB    1 
ATOM   6435  C  CG    . LEU B 1 106 ? 153.767 143.641 156.251 1.00 44.94 ?  106 LEU B CG    1 
ATOM   6436  C  CD1   . LEU B 1 106 ? 152.847 143.676 155.044 1.00 44.16 ?  106 LEU B CD1   1 
ATOM   6437  C  CD2   . LEU B 1 106 ? 154.370 145.011 156.506 1.00 44.60 ?  106 LEU B CD2   1 
ATOM   6438  N  N     . LYS B 1 107 ? 153.959 140.121 156.279 1.00 55.35 ?  107 LYS B N     1 
ATOM   6439  C  CA    . LYS B 1 107 ? 155.061 139.200 156.067 1.00 55.18 ?  107 LYS B CA    1 
ATOM   6440  C  C     . LYS B 1 107 ? 155.974 139.735 154.974 1.00 56.71 ?  107 LYS B C     1 
ATOM   6441  O  O     . LYS B 1 107 ? 155.614 140.645 154.222 1.00 55.21 ?  107 LYS B O     1 
ATOM   6442  C  CB    . LYS B 1 107 ? 154.557 137.804 155.687 1.00 54.68 ?  107 LYS B CB    1 
ATOM   6443  C  CG    . LYS B 1 107 ? 154.146 136.950 156.869 1.00 52.82 ?  107 LYS B CG    1 
ATOM   6444  C  CD    . LYS B 1 107 ? 153.339 135.749 156.420 1.00 55.63 ?  107 LYS B CD    1 
ATOM   6445  C  CE    . LYS B 1 107 ? 152.599 135.126 157.586 1.00 57.28 ?  107 LYS B CE    1 
ATOM   6446  N  NZ    . LYS B 1 107 ? 152.180 136.151 158.582 1.00 56.18 1  107 LYS B NZ    1 
ATOM   6447  N  N     . THR B 1 108 ? 157.172 139.161 154.900 1.00 60.92 ?  108 THR B N     1 
ATOM   6448  C  CA    . THR B 1 108 ? 158.116 139.529 153.860 1.00 60.71 ?  108 THR B CA    1 
ATOM   6449  C  C     . THR B 1 108 ? 157.552 139.170 152.486 1.00 62.10 ?  108 THR B C     1 
ATOM   6450  O  O     . THR B 1 108 ? 156.575 138.430 152.356 1.00 62.89 ?  108 THR B O     1 
ATOM   6451  C  CB    . THR B 1 108 ? 159.458 138.832 154.082 1.00 59.88 ?  108 THR B CB    1 
ATOM   6452  O  OG1   . THR B 1 108 ? 159.238 137.433 154.300 1.00 62.05 ?  108 THR B OG1   1 
ATOM   6453  C  CG2   . THR B 1 108 ? 160.175 139.416 155.285 1.00 57.02 ?  108 THR B CG2   1 
ATOM   6454  N  N     . ASN B 1 109 ? 158.189 139.714 151.444 1.00 63.27 ?  109 ASN B N     1 
ATOM   6455  C  CA    . ASN B 1 109 ? 157.716 139.472 150.084 1.00 63.09 ?  109 ASN B CA    1 
ATOM   6456  C  C     . ASN B 1 109 ? 157.756 137.993 149.722 1.00 66.07 ?  109 ASN B C     1 
ATOM   6457  O  O     . ASN B 1 109 ? 156.978 137.543 148.873 1.00 65.99 ?  109 ASN B O     1 
ATOM   6458  C  CB    . ASN B 1 109 ? 158.542 140.285 149.087 1.00 61.80 ?  109 ASN B CB    1 
ATOM   6459  C  CG    . ASN B 1 109 ? 158.520 141.769 149.389 1.00 64.04 ?  109 ASN B CG    1 
ATOM   6460  O  OD1   . ASN B 1 109 ? 157.476 142.415 149.304 1.00 66.19 ?  109 ASN B OD1   1 
ATOM   6461  N  ND2   . ASN B 1 109 ? 159.676 142.317 149.742 1.00 63.88 ?  109 ASN B ND2   1 
ATOM   6462  N  N     . ASP B 1 110 ? 158.645 137.223 150.346 1.00 66.04 ?  110 ASP B N     1 
ATOM   6463  C  CA    . ASP B 1 110 ? 158.683 135.780 150.162 1.00 67.63 ?  110 ASP B CA    1 
ATOM   6464  C  C     . ASP B 1 110 ? 157.843 135.036 151.193 1.00 66.77 ?  110 ASP B C     1 
ATOM   6465  O  O     . ASP B 1 110 ? 157.859 133.801 151.211 1.00 67.18 ?  110 ASP B O     1 
ATOM   6466  C  CB    . ASP B 1 110 ? 160.130 135.274 150.197 1.00 68.15 ?  110 ASP B CB    1 
ATOM   6467  C  CG    . ASP B 1 110 ? 160.803 135.517 151.530 1.00 69.90 ?  110 ASP B CG    1 
ATOM   6468  O  OD1   . ASP B 1 110 ? 160.398 136.457 152.239 1.00 69.54 ?  110 ASP B OD1   1 
ATOM   6469  O  OD2   . ASP B 1 110 ? 161.742 134.766 151.869 1.00 69.81 -1 110 ASP B OD2   1 
ATOM   6470  N  N     . LYS B 1 111 ? 157.110 135.764 152.041 1.00 64.62 ?  111 LYS B N     1 
ATOM   6471  C  CA    . LYS B 1 111 ? 156.225 135.174 153.049 1.00 64.06 ?  111 LYS B CA    1 
ATOM   6472  C  C     . LYS B 1 111 ? 156.979 134.211 153.963 1.00 66.24 ?  111 LYS B C     1 
ATOM   6473  O  O     . LYS B 1 111 ? 156.486 133.134 154.304 1.00 67.00 ?  111 LYS B O     1 
ATOM   6474  C  CB    . LYS B 1 111 ? 155.027 134.478 152.397 1.00 64.89 ?  111 LYS B CB    1 
ATOM   6475  C  CG    . LYS B 1 111 ? 154.354 135.281 151.293 1.00 64.51 ?  111 LYS B CG    1 
ATOM   6476  C  CD    . LYS B 1 111 ? 153.957 136.672 151.766 1.00 66.11 ?  111 LYS B CD    1 
ATOM   6477  C  CE    . LYS B 1 111 ? 152.770 136.619 152.715 1.00 67.79 ?  111 LYS B CE    1 
ATOM   6478  N  NZ    . LYS B 1 111 ? 151.564 136.030 152.071 1.00 68.04 1  111 LYS B NZ    1 
ATOM   6479  N  N     . LYS B 1 112 ? 158.185 134.604 154.364 1.00 65.24 ?  112 LYS B N     1 
ATOM   6480  C  CA    . LYS B 1 112 ? 159.038 133.786 155.219 1.00 64.41 ?  112 LYS B CA    1 
ATOM   6481  C  C     . LYS B 1 112 ? 159.118 134.292 156.650 1.00 64.17 ?  112 LYS B C     1 
ATOM   6482  O  O     . LYS B 1 112 ? 159.043 133.492 157.585 1.00 65.83 ?  112 LYS B O     1 
ATOM   6483  C  CB    . LYS B 1 112 ? 160.451 133.707 154.626 1.00 63.97 ?  112 LYS B CB    1 
ATOM   6484  C  CG    . LYS B 1 112 ? 161.555 133.420 155.633 1.00 67.04 ?  112 LYS B CG    1 
ATOM   6485  C  CD    . LYS B 1 112 ? 161.581 131.951 156.029 1.00 65.11 ?  112 LYS B CD    1 
ATOM   6486  C  CE    . LYS B 1 112 ? 162.169 131.765 157.419 1.00 65.22 ?  112 LYS B CE    1 
ATOM   6487  N  NZ    . LYS B 1 112 ? 161.304 132.365 158.472 1.00 64.88 1  112 LYS B NZ    1 
ATOM   6488  N  N     . LYS B 1 113 ? 159.255 135.596 156.846 1.00 60.20 ?  113 LYS B N     1 
ATOM   6489  C  CA    . LYS B 1 113 ? 159.381 136.198 158.165 1.00 59.08 ?  113 LYS B CA    1 
ATOM   6490  C  C     . LYS B 1 113 ? 158.177 137.094 158.441 1.00 59.43 ?  113 LYS B C     1 
ATOM   6491  O  O     . LYS B 1 113 ? 157.316 137.301 157.583 1.00 57.53 ?  113 LYS B O     1 
ATOM   6492  C  CB    . LYS B 1 113 ? 160.692 136.981 158.273 1.00 57.33 ?  113 LYS B CB    1 
ATOM   6493  C  CG    . LYS B 1 113 ? 161.921 136.116 158.493 1.00 57.95 ?  113 LYS B CG    1 
ATOM   6494  C  CD    . LYS B 1 113 ? 161.987 135.602 159.919 1.00 59.48 ?  113 LYS B CD    1 
ATOM   6495  C  CE    . LYS B 1 113 ? 163.404 135.214 160.301 1.00 57.00 ?  113 LYS B CE    1 
ATOM   6496  N  NZ    . LYS B 1 113 ? 163.542 133.744 160.484 1.00 58.77 1  113 LYS B NZ    1 
ATOM   6497  N  N     . ILE B 1 114 ? 158.125 137.631 159.657 1.00 52.83 ?  114 ILE B N     1 
ATOM   6498  C  CA    . ILE B 1 114 ? 157.007 138.446 160.123 1.00 49.84 ?  114 ILE B CA    1 
ATOM   6499  C  C     . ILE B 1 114 ? 157.527 139.843 160.430 1.00 51.40 ?  114 ILE B C     1 
ATOM   6500  O  O     . ILE B 1 114 ? 158.447 140.003 161.242 1.00 54.24 ?  114 ILE B O     1 
ATOM   6501  C  CB    . ILE B 1 114 ? 156.333 137.829 161.359 1.00 51.19 ?  114 ILE B CB    1 
ATOM   6502  C  CG1   . ILE B 1 114 ? 155.517 136.596 160.969 1.00 49.80 ?  114 ILE B CG1   1 
ATOM   6503  C  CG2   . ILE B 1 114 ? 155.452 138.849 162.056 1.00 51.04 ?  114 ILE B CG2   1 
ATOM   6504  C  CD1   . ILE B 1 114 ? 155.139 135.726 162.144 1.00 46.81 ?  114 ILE B CD1   1 
ATOM   6505  N  N     . LEU B 1 115 ? 156.940 140.851 159.785 1.00 48.43 ?  115 LEU B N     1 
ATOM   6506  C  CA    . LEU B 1 115 ? 157.301 142.238 160.057 1.00 47.70 ?  115 LEU B CA    1 
ATOM   6507  C  C     . LEU B 1 115 ? 156.426 142.868 161.131 1.00 50.04 ?  115 LEU B C     1 
ATOM   6508  O  O     . LEU B 1 115 ? 156.915 143.670 161.934 1.00 51.35 ?  115 LEU B O     1 
ATOM   6509  C  CB    . LEU B 1 115 ? 157.208 143.081 158.782 1.00 49.26 ?  115 LEU B CB    1 
ATOM   6510  C  CG    . LEU B 1 115 ? 158.301 142.964 157.721 1.00 47.40 ?  115 LEU B CG    1 
ATOM   6511  C  CD1   . LEU B 1 115 ? 159.676 142.849 158.358 1.00 49.77 ?  115 LEU B CD1   1 
ATOM   6512  C  CD2   . LEU B 1 115 ? 158.026 141.799 156.800 1.00 48.91 ?  115 LEU B CD2   1 
ATOM   6513  N  N     . GLU B 1 116 ? 155.142 142.526 161.163 1.00 46.96 ?  116 GLU B N     1 
ATOM   6514  C  CA    . GLU B 1 116 ? 154.168 143.199 162.010 1.00 46.21 ?  116 GLU B CA    1 
ATOM   6515  C  C     . GLU B 1 116 ? 153.694 142.273 163.118 1.00 44.69 ?  116 GLU B C     1 
ATOM   6516  O  O     . GLU B 1 116 ? 153.285 141.137 162.855 1.00 49.18 ?  116 GLU B O     1 
ATOM   6517  C  CB    . GLU B 1 116 ? 152.967 143.671 161.189 1.00 43.45 ?  116 GLU B CB    1 
ATOM   6518  C  CG    . GLU B 1 116 ? 153.013 145.132 160.801 1.00 44.40 ?  116 GLU B CG    1 
ATOM   6519  C  CD    . GLU B 1 116 ? 151.837 145.535 159.936 1.00 47.71 ?  116 GLU B CD    1 
ATOM   6520  O  OE1   . GLU B 1 116 ? 151.044 144.648 159.560 1.00 49.39 ?  116 GLU B OE1   1 
ATOM   6521  O  OE2   . GLU B 1 116 ? 151.704 146.738 159.634 1.00 50.22 -1 116 GLU B OE2   1 
ATOM   6522  N  N     . ARG B 1 117 ? 153.744 142.764 164.351 1.00 39.36 ?  117 ARG B N     1 
ATOM   6523  C  CA    . ARG B 1 117 ? 153.042 142.133 165.452 1.00 41.72 ?  117 ARG B CA    1 
ATOM   6524  C  C     . ARG B 1 117 ? 151.607 142.654 165.479 1.00 41.09 ?  117 ARG B C     1 
ATOM   6525  O  O     . ARG B 1 117 ? 151.196 143.453 164.634 1.00 39.45 ?  117 ARG B O     1 
ATOM   6526  C  CB    . ARG B 1 117 ? 153.758 142.405 166.774 1.00 42.00 ?  117 ARG B CB    1 
ATOM   6527  C  CG    . ARG B 1 117 ? 155.177 141.872 166.836 1.00 40.80 ?  117 ARG B CG    1 
ATOM   6528  C  CD    . ARG B 1 117 ? 155.239 140.402 166.450 1.00 46.77 ?  117 ARG B CD    1 
ATOM   6529  N  NE    . ARG B 1 117 ? 155.079 139.522 167.602 1.00 44.38 ?  117 ARG B NE    1 
ATOM   6530  C  CZ    . ARG B 1 117 ? 155.982 139.361 168.561 1.00 45.70 ?  117 ARG B CZ    1 
ATOM   6531  N  NH1   . ARG B 1 117 ? 157.144 139.992 168.532 1.00 43.54 1  117 ARG B NH1   1 
ATOM   6532  N  NH2   . ARG B 1 117 ? 155.714 138.540 169.573 1.00 47.75 ?  117 ARG B NH2   1 
ATOM   6533  N  N     . TYR B 1 118 ? 150.826 142.193 166.454 1.00 41.03 ?  118 TYR B N     1 
ATOM   6534  C  CA    . TYR B 1 118 ? 149.476 142.722 166.610 1.00 35.12 ?  118 TYR B CA    1 
ATOM   6535  C  C     . TYR B 1 118 ? 149.512 144.209 166.935 1.00 38.01 ?  118 TYR B C     1 
ATOM   6536  O  O     . TYR B 1 118 ? 148.732 144.996 166.384 1.00 40.88 ?  118 TYR B O     1 
ATOM   6537  C  CB    . TYR B 1 118 ? 148.730 141.945 167.692 1.00 36.39 ?  118 TYR B CB    1 
ATOM   6538  C  CG    . TYR B 1 118 ? 147.240 142.188 167.701 1.00 38.14 ?  118 TYR B CG    1 
ATOM   6539  C  CD1   . TYR B 1 118 ? 146.479 141.990 166.558 1.00 33.51 ?  118 TYR B CD1   1 
ATOM   6540  C  CD2   . TYR B 1 118 ? 146.595 142.616 168.850 1.00 36.95 ?  118 TYR B CD2   1 
ATOM   6541  C  CE1   . TYR B 1 118 ? 145.120 142.210 166.561 1.00 33.42 ?  118 TYR B CE1   1 
ATOM   6542  C  CE2   . TYR B 1 118 ? 145.234 142.835 168.864 1.00 33.77 ?  118 TYR B CE2   1 
ATOM   6543  C  CZ    . TYR B 1 118 ? 144.502 142.631 167.715 1.00 35.25 ?  118 TYR B CZ    1 
ATOM   6544  O  OH    . TYR B 1 118 ? 143.145 142.852 167.722 1.00 45.00 ?  118 TYR B OH    1 
ATOM   6545  N  N     . GLU B 1 119 ? 150.428 144.610 167.817 1.00 44.44 ?  119 GLU B N     1 
ATOM   6546  C  CA    . GLU B 1 119 ? 150.542 146.016 168.185 1.00 38.64 ?  119 GLU B CA    1 
ATOM   6547  C  C     . GLU B 1 119 ? 150.976 146.871 167.002 1.00 38.45 ?  119 GLU B C     1 
ATOM   6548  O  O     . GLU B 1 119 ? 150.490 147.991 166.837 1.00 49.14 ?  119 GLU B O     1 
ATOM   6549  C  CB    . GLU B 1 119 ? 151.514 146.171 169.353 1.00 38.99 ?  119 GLU B CB    1 
ATOM   6550  C  CG    . GLU B 1 119 ? 151.019 145.557 170.650 1.00 39.79 ?  119 GLU B CG    1 
ATOM   6551  C  CD    . GLU B 1 119 ? 151.518 144.140 170.854 1.00 45.71 ?  119 GLU B CD    1 
ATOM   6552  O  OE1   . GLU B 1 119 ? 151.768 143.444 169.847 1.00 45.33 ?  119 GLU B OE1   1 
ATOM   6553  O  OE2   . GLU B 1 119 ? 151.657 143.719 172.021 1.00 46.42 -1 119 GLU B OE2   1 
ATOM   6554  N  N     . ASP B 1 120 ? 151.894 146.371 166.171 1.00 40.96 ?  120 ASP B N     1 
ATOM   6555  C  CA    . ASP B 1 120 ? 152.329 147.143 165.009 1.00 39.84 ?  120 ASP B CA    1 
ATOM   6556  C  C     . ASP B 1 120 ? 151.190 147.333 164.016 1.00 39.51 ?  120 ASP B C     1 
ATOM   6557  O  O     . ASP B 1 120 ? 150.988 148.433 163.489 1.00 44.82 ?  120 ASP B O     1 
ATOM   6558  C  CB    . ASP B 1 120 ? 153.520 146.465 164.333 1.00 45.29 ?  120 ASP B CB    1 
ATOM   6559  C  CG    . ASP B 1 120 ? 154.556 145.984 165.321 1.00 47.85 ?  120 ASP B CG    1 
ATOM   6560  O  OD1   . ASP B 1 120 ? 155.012 144.832 165.187 1.00 51.60 ?  120 ASP B OD1   1 
ATOM   6561  O  OD2   . ASP B 1 120 ? 154.908 146.757 166.236 1.00 46.55 -1 120 ASP B OD2   1 
ATOM   6562  N  N     . ARG B 1 121 ? 150.439 146.264 163.742 1.00 34.52 ?  121 ARG B N     1 
ATOM   6563  C  CA    . ARG B 1 121 ? 149.297 146.367 162.840 1.00 31.09 ?  121 ARG B CA    1 
ATOM   6564  C  C     . ARG B 1 121 ? 148.260 147.342 163.380 1.00 35.79 ?  121 ARG B C     1 
ATOM   6565  O  O     . ARG B 1 121 ? 147.728 148.174 162.633 1.00 45.87 ?  121 ARG B O     1 
ATOM   6566  C  CB    . ARG B 1 121 ? 148.682 144.984 162.624 1.00 35.38 ?  121 ARG B CB    1 
ATOM   6567  C  CG    . ARG B 1 121 ? 147.416 144.971 161.787 1.00 32.93 ?  121 ARG B CG    1 
ATOM   6568  C  CD    . ARG B 1 121 ? 147.727 144.856 160.310 1.00 32.41 ?  121 ARG B CD    1 
ATOM   6569  N  NE    . ARG B 1 121 ? 147.482 146.112 159.614 1.00 43.28 ?  121 ARG B NE    1 
ATOM   6570  C  CZ    . ARG B 1 121 ? 148.241 146.587 158.637 1.00 39.89 ?  121 ARG B CZ    1 
ATOM   6571  N  NH1   . ARG B 1 121 ? 149.306 145.932 158.209 1.00 42.44 1  121 ARG B NH1   1 
ATOM   6572  N  NH2   . ARG B 1 121 ? 147.923 147.750 158.078 1.00 32.92 ?  121 ARG B NH2   1 
ATOM   6573  N  N     . ILE B 1 122 ? 147.973 147.268 164.680 1.00 35.39 ?  122 ILE B N     1 
ATOM   6574  C  CA    . ILE B 1 122 ? 146.987 148.164 165.273 1.00 29.58 ?  122 ILE B CA    1 
ATOM   6575  C  C     . ILE B 1 122 ? 147.476 149.608 165.236 1.00 30.42 ?  122 ILE B C     1 
ATOM   6576  O  O     . ILE B 1 122 ? 146.703 150.528 164.954 1.00 37.63 ?  122 ILE B O     1 
ATOM   6577  C  CB    . ILE B 1 122 ? 146.642 147.700 166.698 1.00 35.40 ?  122 ILE B CB    1 
ATOM   6578  C  CG1   . ILE B 1 122 ? 145.624 146.562 166.630 1.00 32.27 ?  122 ILE B CG1   1 
ATOM   6579  C  CG2   . ILE B 1 122 ? 146.107 148.850 167.538 1.00 31.89 ?  122 ILE B CG2   1 
ATOM   6580  C  CD1   . ILE B 1 122 ? 145.037 146.192 167.953 1.00 32.92 ?  122 ILE B CD1   1 
ATOM   6581  N  N     . SER B 1 123 ? 148.764 149.831 165.506 1.00 33.76 ?  123 SER B N     1 
ATOM   6582  C  CA    . SER B 1 123 ? 149.312 151.182 165.451 1.00 32.60 ?  123 SER B CA    1 
ATOM   6583  C  C     . SER B 1 123 ? 149.238 151.754 164.045 1.00 36.18 ?  123 SER B C     1 
ATOM   6584  O  O     . SER B 1 123 ? 148.894 152.925 163.861 1.00 36.84 ?  123 SER B O     1 
ATOM   6585  C  CB    . SER B 1 123 ? 150.758 151.186 165.941 1.00 32.05 ?  123 SER B CB    1 
ATOM   6586  O  OG    . SER B 1 123 ? 150.859 150.639 167.237 1.00 37.98 ?  123 SER B OG    1 
ATOM   6587  N  N     . ILE B 1 124 ? 149.564 150.944 163.037 1.00 36.71 ?  124 ILE B N     1 
ATOM   6588  C  CA    . ILE B 1 124 ? 149.506 151.426 161.661 1.00 34.76 ?  124 ILE B CA    1 
ATOM   6589  C  C     . ILE B 1 124 ? 148.070 151.737 161.262 1.00 39.62 ?  124 ILE B C     1 
ATOM   6590  O  O     . ILE B 1 124 ? 147.796 152.766 160.629 1.00 39.84 ?  124 ILE B O     1 
ATOM   6591  C  CB    . ILE B 1 124 ? 150.161 150.407 160.713 1.00 39.41 ?  124 ILE B CB    1 
ATOM   6592  C  CG1   . ILE B 1 124 ? 151.683 150.490 160.837 1.00 41.25 ?  124 ILE B CG1   1 
ATOM   6593  C  CG2   . ILE B 1 124 ? 149.730 150.648 159.277 1.00 36.46 ?  124 ILE B CG2   1 
ATOM   6594  C  CD1   . ILE B 1 124 ? 152.231 151.893 160.682 1.00 36.63 ?  124 ILE B CD1   1 
ATOM   6595  N  N     . VAL B 1 125 ? 147.127 150.870 161.642 1.00 32.40 ?  125 VAL B N     1 
ATOM   6596  C  CA    . VAL B 1 125 ? 145.724 151.115 161.322 1.00 30.50 ?  125 VAL B CA    1 
ATOM   6597  C  C     . VAL B 1 125 ? 145.233 152.386 162.007 1.00 25.65 ?  125 VAL B C     1 
ATOM   6598  O  O     . VAL B 1 125 ? 144.510 153.191 161.408 1.00 35.98 ?  125 VAL B O     1 
ATOM   6599  C  CB    . VAL B 1 125 ? 144.870 149.890 161.700 1.00 37.24 ?  125 VAL B CB    1 
ATOM   6600  C  CG1   . VAL B 1 125 ? 143.395 150.226 161.643 1.00 32.65 ?  125 VAL B CG1   1 
ATOM   6601  C  CG2   . VAL B 1 125 ? 145.177 148.729 160.770 1.00 27.59 ?  125 VAL B CG2   1 
ATOM   6602  N  N     . ALA B 1 126 ? 145.626 152.594 163.264 1.00 24.10 ?  126 ALA B N     1 
ATOM   6603  C  CA    . ALA B 1 126 ? 145.210 153.791 163.990 1.00 26.21 ?  126 ALA B CA    1 
ATOM   6604  C  C     . ALA B 1 126 ? 145.817 155.053 163.393 1.00 31.08 ?  126 ALA B C     1 
ATOM   6605  O  O     . ALA B 1 126 ? 145.145 156.087 163.299 1.00 34.62 ?  126 ALA B O     1 
ATOM   6606  C  CB    . ALA B 1 126 ? 145.593 153.664 165.461 1.00 29.96 ?  126 ALA B CB    1 
ATOM   6607  N  N     . LEU B 1 127 ? 147.091 154.995 163.001 1.00 36.91 ?  127 LEU B N     1 
ATOM   6608  C  CA    . LEU B 1 127 ? 147.734 156.154 162.393 1.00 26.42 ?  127 LEU B CA    1 
ATOM   6609  C  C     . LEU B 1 127 ? 147.110 156.479 161.045 1.00 26.74 ?  127 LEU B C     1 
ATOM   6610  O  O     . LEU B 1 127 ? 147.021 157.650 160.660 1.00 33.01 ?  127 LEU B O     1 
ATOM   6611  C  CB    . LEU B 1 127 ? 149.235 155.907 162.245 1.00 28.93 ?  127 LEU B CB    1 
ATOM   6612  C  CG    . LEU B 1 127 ? 150.074 155.947 163.523 1.00 32.83 ?  127 LEU B CG    1 
ATOM   6613  C  CD1   . LEU B 1 127 ? 151.403 155.249 163.311 1.00 38.52 ?  127 LEU B CD1   1 
ATOM   6614  C  CD2   . LEU B 1 127 ? 150.290 157.375 163.984 1.00 33.35 ?  127 LEU B CD2   1 
ATOM   6615  N  N     . PHE B 1 128 ? 146.680 155.454 160.307 1.00 32.50 ?  128 PHE B N     1 
ATOM   6616  C  CA    . PHE B 1 128 ? 145.962 155.696 159.061 1.00 33.27 ?  128 PHE B CA    1 
ATOM   6617  C  C     . PHE B 1 128 ? 144.582 156.289 159.330 1.00 30.13 ?  128 PHE B C     1 
ATOM   6618  O  O     . PHE B 1 128 ? 144.123 157.166 158.591 1.00 40.74 ?  128 PHE B O     1 
ATOM   6619  C  CB    . PHE B 1 128 ? 145.870 154.395 158.258 1.00 29.67 ?  128 PHE B CB    1 
ATOM   6620  C  CG    . PHE B 1 128 ? 144.866 154.427 157.139 1.00 35.44 ?  128 PHE B CG    1 
ATOM   6621  C  CD1   . PHE B 1 128 ? 143.535 154.107 157.361 1.00 33.75 ?  128 PHE B CD1   1 
ATOM   6622  C  CD2   . PHE B 1 128 ? 145.257 154.782 155.861 1.00 37.02 ?  128 PHE B CD2   1 
ATOM   6623  C  CE1   . PHE B 1 128 ? 142.620 154.144 156.332 1.00 34.62 ?  128 PHE B CE1   1 
ATOM   6624  C  CE2   . PHE B 1 128 ? 144.345 154.818 154.828 1.00 36.99 ?  128 PHE B CE2   1 
ATOM   6625  C  CZ    . PHE B 1 128 ? 143.027 154.500 155.064 1.00 34.68 ?  128 PHE B CZ    1 
ATOM   6626  N  N     . PHE B 1 129 ? 143.905 155.815 160.379 1.00 27.70 ?  129 PHE B N     1 
ATOM   6627  C  CA    . PHE B 1 129 ? 142.582 156.331 160.715 1.00 21.42 ?  129 PHE B CA    1 
ATOM   6628  C  C     . PHE B 1 129 ? 142.636 157.797 161.124 1.00 30.37 ?  129 PHE B C     1 
ATOM   6629  O  O     . PHE B 1 129 ? 141.787 158.594 160.710 1.00 33.81 ?  129 PHE B O     1 
ATOM   6630  C  CB    . PHE B 1 129 ? 141.963 155.507 161.843 1.00 24.55 ?  129 PHE B CB    1 
ATOM   6631  C  CG    . PHE B 1 129 ? 141.352 154.217 161.395 1.00 26.58 ?  129 PHE B CG    1 
ATOM   6632  C  CD1   . PHE B 1 129 ? 141.098 153.978 160.057 1.00 26.21 ?  129 PHE B CD1   1 
ATOM   6633  C  CD2   . PHE B 1 129 ? 141.020 153.244 162.321 1.00 28.07 ?  129 PHE B CD2   1 
ATOM   6634  C  CE1   . PHE B 1 129 ? 140.532 152.789 159.653 1.00 25.06 ?  129 PHE B CE1   1 
ATOM   6635  C  CE2   . PHE B 1 129 ? 140.450 152.054 161.921 1.00 30.63 ?  129 PHE B CE2   1 
ATOM   6636  C  CZ    . PHE B 1 129 ? 140.207 151.826 160.586 1.00 30.17 ?  129 PHE B CZ    1 
ATOM   6637  N  N     . ALA B 1 130 ? 143.620 158.168 161.946 1.00 35.74 ?  130 ALA B N     1 
ATOM   6638  C  CA    . ALA B 1 130 ? 143.638 159.510 162.518 1.00 35.44 ?  130 ALA B CA    1 
ATOM   6639  C  C     . ALA B 1 130 ? 143.944 160.576 161.474 1.00 42.14 ?  130 ALA B C     1 
ATOM   6640  O  O     . ALA B 1 130 ? 143.472 161.712 161.601 1.00 47.31 ?  130 ALA B O     1 
ATOM   6641  C  CB    . ALA B 1 130 ? 144.649 159.578 163.655 1.00 33.44 ?  130 ALA B CB    1 
ATOM   6642  N  N     . ASN B 1 131 ? 144.731 160.236 160.453 1.00 41.73 ?  131 ASN B N     1 
ATOM   6643  C  CA    . ASN B 1 131 ? 145.036 161.145 159.346 1.00 41.38 ?  131 ASN B CA    1 
ATOM   6644  C  C     . ASN B 1 131 ? 145.713 162.425 159.840 1.00 42.82 ?  131 ASN B C     1 
ATOM   6645  O  O     . ASN B 1 131 ? 145.361 163.536 159.440 1.00 46.71 ?  131 ASN B O     1 
ATOM   6646  C  CB    . ASN B 1 131 ? 143.772 161.466 158.542 1.00 40.39 ?  131 ASN B CB    1 
ATOM   6647  C  CG    . ASN B 1 131 ? 144.075 161.875 157.117 1.00 46.02 ?  131 ASN B CG    1 
ATOM   6648  O  OD1   . ASN B 1 131 ? 144.939 161.294 156.461 1.00 45.99 ?  131 ASN B OD1   1 
ATOM   6649  N  ND2   . ASN B 1 131 ? 143.360 162.879 156.626 1.00 44.13 ?  131 ASN B ND2   1 
ATOM   6650  N  N     . GLY B 1 132 ? 146.698 162.261 160.720 1.00 42.48 ?  132 GLY B N     1 
ATOM   6651  C  CA    . GLY B 1 132 ? 147.517 163.365 161.180 1.00 39.49 ?  132 GLY B CA    1 
ATOM   6652  C  C     . GLY B 1 132 ? 147.293 163.790 162.615 1.00 44.84 ?  132 GLY B C     1 
ATOM   6653  O  O     . GLY B 1 132 ? 148.040 164.645 163.107 1.00 50.55 ?  132 GLY B O     1 
ATOM   6654  N  N     . ASP B 1 133 ? 146.303 163.233 163.305 1.00 46.99 ?  133 ASP B N     1 
ATOM   6655  C  CA    . ASP B 1 133 ? 146.005 163.601 164.684 1.00 47.34 ?  133 ASP B CA    1 
ATOM   6656  C  C     . ASP B 1 133 ? 146.623 162.569 165.621 1.00 48.68 ?  133 ASP B C     1 
ATOM   6657  O  O     . ASP B 1 133 ? 146.290 161.382 165.552 1.00 48.93 ?  133 ASP B O     1 
ATOM   6658  C  CB    . ASP B 1 133 ? 144.496 163.697 164.904 1.00 47.18 ?  133 ASP B CB    1 
ATOM   6659  C  CG    . ASP B 1 133 ? 144.135 164.441 166.176 1.00 52.90 ?  133 ASP B CG    1 
ATOM   6660  O  OD1   . ASP B 1 133 ? 145.034 164.683 167.007 1.00 54.28 ?  133 ASP B OD1   1 
ATOM   6661  O  OD2   . ASP B 1 133 ? 142.944 164.776 166.348 1.00 50.36 -1 133 ASP B OD2   1 
ATOM   6662  N  N     . THR B 1 134 ? 147.520 163.022 166.498 1.00 49.26 ?  134 THR B N     1 
ATOM   6663  C  CA    . THR B 1 134 ? 148.209 162.094 167.390 1.00 45.20 ?  134 THR B CA    1 
ATOM   6664  C  C     . THR B 1 134 ? 147.291 161.604 168.503 1.00 47.30 ?  134 THR B C     1 
ATOM   6665  O  O     . THR B 1 134 ? 147.292 160.414 168.837 1.00 50.75 ?  134 THR B O     1 
ATOM   6666  C  CB    . THR B 1 134 ? 149.452 162.759 167.975 1.00 53.73 ?  134 THR B CB    1 
ATOM   6667  O  OG1   . THR B 1 134 ? 150.283 163.226 166.907 1.00 55.93 ?  134 THR B OG1   1 
ATOM   6668  C  CG2   . THR B 1 134 ? 150.234 161.769 168.822 1.00 50.56 ?  134 THR B CG2   1 
ATOM   6669  N  N     . GLU B 1 135 ? 146.502 162.506 169.094 1.00 46.01 ?  135 GLU B N     1 
ATOM   6670  C  CA    . GLU B 1 135 ? 145.568 162.096 170.135 1.00 45.42 ?  135 GLU B CA    1 
ATOM   6671  C  C     . GLU B 1 135 ? 144.496 161.168 169.579 1.00 50.14 ?  135 GLU B C     1 
ATOM   6672  O  O     . GLU B 1 135 ? 144.115 160.189 170.229 1.00 51.83 ?  135 GLU B O     1 
ATOM   6673  C  CB    . GLU B 1 135 ? 144.935 163.323 170.787 1.00 47.74 ?  135 GLU B CB    1 
ATOM   6674  C  CG    . GLU B 1 135 ? 145.944 164.322 171.326 1.00 48.68 ?  135 GLU B CG    1 
ATOM   6675  C  CD    . GLU B 1 135 ? 147.090 163.655 172.057 1.00 55.32 ?  135 GLU B CD    1 
ATOM   6676  O  OE1   . GLU B 1 135 ? 146.836 162.983 173.079 1.00 54.01 ?  135 GLU B OE1   1 
ATOM   6677  O  OE2   . GLU B 1 135 ? 148.247 163.801 171.610 1.00 55.95 -1 135 GLU B OE2   1 
ATOM   6678  N  N     . LYS B 1 136 ? 144.000 161.462 168.375 1.00 40.63 ?  136 LYS B N     1 
ATOM   6679  C  CA    . LYS B 1 136 ? 143.036 160.574 167.735 1.00 38.65 ?  136 LYS B CA    1 
ATOM   6680  C  C     . LYS B 1 136 ? 143.653 159.212 167.442 1.00 39.71 ?  136 LYS B C     1 
ATOM   6681  O  O     . LYS B 1 136 ? 142.998 158.177 167.605 1.00 46.00 ?  136 LYS B O     1 
ATOM   6682  C  CB    . LYS B 1 136 ? 142.509 161.217 166.453 1.00 46.29 ?  136 LYS B CB    1 
ATOM   6683  C  CG    . LYS B 1 136 ? 141.236 160.603 165.911 1.00 41.83 ?  136 LYS B CG    1 
ATOM   6684  C  CD    . LYS B 1 136 ? 140.012 161.156 166.613 1.00 43.62 ?  136 LYS B CD    1 
ATOM   6685  C  CE    . LYS B 1 136 ? 138.740 160.785 165.872 1.00 46.52 ?  136 LYS B CE    1 
ATOM   6686  N  NZ    . LYS B 1 136 ? 137.565 161.541 166.382 1.00 49.13 1  136 LYS B NZ    1 
ATOM   6687  N  N     . ALA B 1 137 ? 144.914 159.193 167.000 1.00 34.81 ?  137 ALA B N     1 
ATOM   6688  C  CA    . ALA B 1 137 ? 145.592 157.925 166.752 1.00 31.55 ?  137 ALA B CA    1 
ATOM   6689  C  C     . ALA B 1 137 ? 145.745 157.123 168.037 1.00 35.22 ?  137 ALA B C     1 
ATOM   6690  O  O     . ALA B 1 137 ? 145.566 155.901 168.040 1.00 38.48 ?  137 ALA B O     1 
ATOM   6691  C  CB    . ALA B 1 137 ? 146.955 158.170 166.108 1.00 31.27 ?  137 ALA B CB    1 
ATOM   6692  N  N     . LYS B 1 138 ? 146.080 157.794 169.141 1.00 39.95 ?  138 LYS B N     1 
ATOM   6693  C  CA    . LYS B 1 138 ? 146.180 157.104 170.423 1.00 38.43 ?  138 LYS B CA    1 
ATOM   6694  C  C     . LYS B 1 138 ? 144.822 156.579 170.872 1.00 38.29 ?  138 LYS B C     1 
ATOM   6695  O  O     . LYS B 1 138 ? 144.729 155.493 171.455 1.00 41.57 ?  138 LYS B O     1 
ATOM   6696  C  CB    . LYS B 1 138 ? 146.773 158.038 171.477 1.00 46.55 ?  138 LYS B CB    1 
ATOM   6697  C  CG    . LYS B 1 138 ? 148.256 157.823 171.722 1.00 45.57 ?  138 LYS B CG    1 
ATOM   6698  C  CD    . LYS B 1 138 ? 149.022 159.133 171.707 1.00 42.75 ?  138 LYS B CD    1 
ATOM   6699  C  CE    . LYS B 1 138 ? 148.483 160.102 172.741 1.00 41.41 ?  138 LYS B CE    1 
ATOM   6700  N  NZ    . LYS B 1 138 ? 149.307 161.340 172.816 1.00 45.27 1  138 LYS B NZ    1 
ATOM   6701  N  N     . GLU B 1 139 ? 143.756 157.340 170.617 1.00 42.21 ?  139 GLU B N     1 
ATOM   6702  C  CA    . GLU B 1 139 ? 142.413 156.867 170.940 1.00 37.82 ?  139 GLU B CA    1 
ATOM   6703  C  C     . GLU B 1 139 ? 142.056 155.625 170.134 1.00 34.72 ?  139 GLU B C     1 
ATOM   6704  O  O     . GLU B 1 139 ? 141.478 154.674 170.671 1.00 43.86 ?  139 GLU B O     1 
ATOM   6705  C  CB    . GLU B 1 139 ? 141.394 157.979 170.698 1.00 36.39 ?  139 GLU B CB    1 
ATOM   6706  C  CG    . GLU B 1 139 ? 140.925 158.668 171.963 1.00 41.29 ?  139 GLU B CG    1 
ATOM   6707  C  CD    . GLU B 1 139 ? 140.685 160.150 171.766 1.00 49.30 ?  139 GLU B CD    1 
ATOM   6708  O  OE1   . GLU B 1 139 ? 140.128 160.529 170.713 1.00 46.90 ?  139 GLU B OE1   1 
ATOM   6709  O  OE2   . GLU B 1 139 ? 141.050 160.937 172.663 1.00 47.07 -1 139 GLU B OE2   1 
ATOM   6710  N  N     . TYR B 1 140 ? 142.388 155.618 168.842 1.00 27.13 ?  140 TYR B N     1 
ATOM   6711  C  CA    . TYR B 1 140 ? 142.145 154.433 168.022 1.00 28.57 ?  140 TYR B CA    1 
ATOM   6712  C  C     . TYR B 1 140 ? 142.973 153.250 168.507 1.00 32.48 ?  140 TYR B C     1 
ATOM   6713  O  O     . TYR B 1 140 ? 142.500 152.106 168.506 1.00 35.20 ?  140 TYR B O     1 
ATOM   6714  C  CB    . TYR B 1 140 ? 142.456 154.728 166.557 1.00 31.21 ?  140 TYR B CB    1 
ATOM   6715  C  CG    . TYR B 1 140 ? 141.429 155.567 165.838 1.00 33.68 ?  140 TYR B CG    1 
ATOM   6716  C  CD1   . TYR B 1 140 ? 140.095 155.188 165.792 1.00 36.18 ?  140 TYR B CD1   1 
ATOM   6717  C  CD2   . TYR B 1 140 ? 141.801 156.731 165.184 1.00 34.26 ?  140 TYR B CD2   1 
ATOM   6718  C  CE1   . TYR B 1 140 ? 139.162 155.954 165.125 1.00 34.00 ?  140 TYR B CE1   1 
ATOM   6719  C  CE2   . TYR B 1 140 ? 140.878 157.499 164.519 1.00 32.61 ?  140 TYR B CE2   1 
ATOM   6720  C  CZ    . TYR B 1 140 ? 139.561 157.110 164.492 1.00 30.34 ?  140 TYR B CZ    1 
ATOM   6721  O  OH    . TYR B 1 140 ? 138.648 157.887 163.822 1.00 37.65 ?  140 TYR B OH    1 
ATOM   6722  N  N     . VAL B 1 141 ? 144.221 153.504 168.909 1.00 36.80 ?  141 VAL B N     1 
ATOM   6723  C  CA    . VAL B 1 141 ? 145.069 152.446 169.449 1.00 34.60 ?  141 VAL B CA    1 
ATOM   6724  C  C     . VAL B 1 141 ? 144.447 151.854 170.704 1.00 31.82 ?  141 VAL B C     1 
ATOM   6725  O  O     . VAL B 1 141 ? 144.407 150.634 170.876 1.00 38.24 ?  141 VAL B O     1 
ATOM   6726  C  CB    . VAL B 1 141 ? 146.486 152.980 169.727 1.00 36.80 ?  141 VAL B CB    1 
ATOM   6727  C  CG1   . VAL B 1 141 ? 147.191 152.098 170.730 1.00 35.04 ?  141 VAL B CG1   1 
ATOM   6728  C  CG2   . VAL B 1 141 ? 147.286 153.026 168.453 1.00 35.06 ?  141 VAL B CG2   1 
ATOM   6729  N  N     . ASN B 1 142 ? 143.959 152.709 171.602 1.00 33.90 ?  142 ASN B N     1 
ATOM   6730  C  CA    . ASN B 1 142 ? 143.319 152.209 172.814 1.00 33.04 ?  142 ASN B CA    1 
ATOM   6731  C  C     . ASN B 1 142 ? 142.047 151.440 172.484 1.00 34.96 ?  142 ASN B C     1 
ATOM   6732  O  O     . ASN B 1 142 ? 141.745 150.427 173.122 1.00 41.23 ?  142 ASN B O     1 
ATOM   6733  C  CB    . ASN B 1 142 ? 143.020 153.365 173.765 1.00 30.82 ?  142 ASN B CB    1 
ATOM   6734  C  CG    . ASN B 1 142 ? 144.255 153.849 174.493 1.00 36.66 ?  142 ASN B CG    1 
ATOM   6735  O  OD1   . ASN B 1 142 ? 145.021 153.054 175.036 1.00 37.28 ?  142 ASN B OD1   1 
ATOM   6736  N  ND2   . ASN B 1 142 ? 144.459 155.161 174.506 1.00 38.79 ?  142 ASN B ND2   1 
ATOM   6737  N  N     . LEU B 1 143 ? 141.290 151.909 171.491 1.00 34.18 ?  143 LEU B N     1 
ATOM   6738  C  CA    . LEU B 1 143 ? 140.053 151.235 171.115 1.00 28.75 ?  143 LEU B CA    1 
ATOM   6739  C  C     . LEU B 1 143 ? 140.319 149.848 170.543 1.00 32.78 ?  143 LEU B C     1 
ATOM   6740  O  O     . LEU B 1 143 ? 139.587 148.899 170.840 1.00 36.15 ?  143 LEU B O     1 
ATOM   6741  C  CB    . LEU B 1 143 ? 139.281 152.089 170.112 1.00 28.80 ?  143 LEU B CB    1 
ATOM   6742  C  CG    . LEU B 1 143 ? 137.777 151.845 170.056 1.00 34.07 ?  143 LEU B CG    1 
ATOM   6743  C  CD1   . LEU B 1 143 ? 137.118 152.400 171.304 1.00 32.88 ?  143 LEU B CD1   1 
ATOM   6744  C  CD2   . LEU B 1 143 ? 137.192 152.474 168.810 1.00 33.46 ?  143 LEU B CD2   1 
ATOM   6745  N  N     . MET B 1 144 ? 141.356 149.710 169.718 1.00 34.58 ?  144 MET B N     1 
ATOM   6746  C  CA    . MET B 1 144 ? 141.614 148.442 169.045 1.00 24.95 ?  144 MET B CA    1 
ATOM   6747  C  C     . MET B 1 144 ? 142.453 147.476 169.871 1.00 25.64 ?  144 MET B C     1 
ATOM   6748  O  O     . MET B 1 144 ? 142.235 146.263 169.793 1.00 34.30 ?  144 MET B O     1 
ATOM   6749  C  CB    . MET B 1 144 ? 142.290 148.693 167.696 1.00 27.95 ?  144 MET B CB    1 
ATOM   6750  C  CG    . MET B 1 144 ? 141.405 149.425 166.701 1.00 28.00 ?  144 MET B CG    1 
ATOM   6751  S  SD    . MET B 1 144 ? 142.094 149.453 165.039 1.00 45.60 ?  144 MET B SD    1 
ATOM   6752  C  CE    . MET B 1 144 ? 143.494 150.535 165.288 1.00 26.96 ?  144 MET B CE    1 
ATOM   6753  N  N     . ILE B 1 145 ? 143.417 147.974 170.650 1.00 28.38 ?  145 ILE B N     1 
ATOM   6754  C  CA    . ILE B 1 145 ? 144.206 147.090 171.502 1.00 29.34 ?  145 ILE B CA    1 
ATOM   6755  C  C     . ILE B 1 145 ? 143.364 146.574 172.660 1.00 35.80 ?  145 ILE B C     1 
ATOM   6756  O  O     . ILE B 1 145 ? 143.575 145.453 173.138 1.00 39.90 ?  145 ILE B O     1 
ATOM   6757  C  CB    . ILE B 1 145 ? 145.489 147.802 171.979 1.00 31.03 ?  145 ILE B CB    1 
ATOM   6758  C  CG1   . ILE B 1 145 ? 146.616 146.789 172.189 1.00 32.44 ?  145 ILE B CG1   1 
ATOM   6759  C  CG2   . ILE B 1 145 ? 145.249 148.601 173.254 1.00 33.30 ?  145 ILE B CG2   1 
ATOM   6760  C  CD1   . ILE B 1 145 ? 147.131 146.171 170.912 1.00 35.50 ?  145 ILE B CD1   1 
ATOM   6761  N  N     . ASN B 1 146 ? 142.395 147.366 173.128 1.00 33.84 ?  146 ASN B N     1 
ATOM   6762  C  CA    . ASN B 1 146 ? 141.389 146.854 174.046 1.00 27.26 ?  146 ASN B CA    1 
ATOM   6763  C  C     . ASN B 1 146 ? 140.393 145.949 173.341 1.00 29.59 ?  146 ASN B C     1 
ATOM   6764  O  O     . ASN B 1 146 ? 139.576 145.312 174.014 1.00 38.22 ?  146 ASN B O     1 
ATOM   6765  C  CB    . ASN B 1 146 ? 140.649 148.003 174.727 1.00 27.33 ?  146 ASN B CB    1 
ATOM   6766  C  CG    . ASN B 1 146 ? 141.517 148.750 175.715 1.00 33.18 ?  146 ASN B CG    1 
ATOM   6767  O  OD1   . ASN B 1 146 ? 142.540 148.241 176.168 1.00 41.26 ?  146 ASN B OD1   1 
ATOM   6768  N  ND2   . ASN B 1 146 ? 141.112 149.967 176.055 1.00 34.54 ?  146 ASN B ND2   1 
ATOM   6769  N  N     . GLN B 1 147 ? 140.447 145.894 172.010 1.00 33.55 ?  147 GLN B N     1 
ATOM   6770  C  CA    . GLN B 1 147 ? 139.597 145.022 171.205 1.00 24.10 ?  147 GLN B CA    1 
ATOM   6771  C  C     . GLN B 1 147 ? 138.122 145.341 171.412 1.00 23.97 ?  147 GLN B C     1 
ATOM   6772  O  O     . GLN B 1 147 ? 137.276 144.449 171.441 1.00 38.00 ?  147 GLN B O     1 
ATOM   6773  C  CB    . GLN B 1 147 ? 139.892 143.549 171.492 1.00 23.94 ?  147 GLN B CB    1 
ATOM   6774  C  CG    . GLN B 1 147 ? 141.259 143.105 171.011 1.00 24.48 ?  147 GLN B CG    1 
ATOM   6775  C  CD    . GLN B 1 147 ? 141.380 141.604 170.910 1.00 31.06 ?  147 GLN B CD    1 
ATOM   6776  O  OE1   . GLN B 1 147 ? 140.951 140.875 171.803 1.00 41.78 ?  147 GLN B OE1   1 
ATOM   6777  N  NE2   . GLN B 1 147 ? 141.969 141.131 169.821 1.00 31.16 ?  147 GLN B NE2   1 
ATOM   6778  N  N     . GLU B 1 148 ? 137.814 146.628 171.571 1.00 25.67 ?  148 GLU B N     1 
ATOM   6779  C  CA    . GLU B 1 148 ? 136.423 147.062 171.604 1.00 23.25 ?  148 GLU B CA    1 
ATOM   6780  C  C     . GLU B 1 148 ? 135.852 147.231 170.206 1.00 29.08 ?  148 GLU B C     1 
ATOM   6781  O  O     . GLU B 1 148 ? 134.659 146.991 169.993 1.00 35.96 ?  148 GLU B O     1 
ATOM   6782  C  CB    . GLU B 1 148 ? 136.295 148.376 172.371 1.00 18.14 ?  148 GLU B CB    1 
ATOM   6783  C  CG    . GLU B 1 148 ? 136.694 148.296 173.827 1.00 21.97 ?  148 GLU B CG    1 
ATOM   6784  C  CD    . GLU B 1 148 ? 137.034 149.655 174.402 1.00 35.44 ?  148 GLU B CD    1 
ATOM   6785  O  OE1   . GLU B 1 148 ? 138.147 150.151 174.139 1.00 35.25 ?  148 GLU B OE1   1 
ATOM   6786  O  OE2   . GLU B 1 148 ? 136.185 150.231 175.113 1.00 42.82 -1 148 GLU B OE2   1 
ATOM   6787  N  N     . TYR B 1 149 ? 136.681 147.642 169.251 1.00 26.98 ?  149 TYR B N     1 
ATOM   6788  C  CA    . TYR B 1 149 ? 136.267 147.831 167.869 1.00 19.69 ?  149 TYR B CA    1 
ATOM   6789  C  C     . TYR B 1 149 ? 137.252 147.122 166.956 1.00 24.35 ?  149 TYR B C     1 
ATOM   6790  O  O     . TYR B 1 149 ? 138.467 147.271 167.112 1.00 32.74 ?  149 TYR B O     1 
ATOM   6791  C  CB    . TYR B 1 149 ? 136.193 149.315 167.508 1.00 22.94 ?  149 TYR B CB    1 
ATOM   6792  C  CG    . TYR B 1 149 ? 136.034 149.572 166.029 1.00 24.46 ?  149 TYR B CG    1 
ATOM   6793  C  CD1   . TYR B 1 149 ? 134.906 149.139 165.348 1.00 19.89 ?  149 TYR B CD1   1 
ATOM   6794  C  CD2   . TYR B 1 149 ? 137.016 150.244 165.313 1.00 17.39 ?  149 TYR B CD2   1 
ATOM   6795  C  CE1   . TYR B 1 149 ? 134.758 149.370 163.997 1.00 19.99 ?  149 TYR B CE1   1 
ATOM   6796  C  CE2   . TYR B 1 149 ? 136.876 150.478 163.963 1.00 24.90 ?  149 TYR B CE2   1 
ATOM   6797  C  CZ    . TYR B 1 149 ? 135.744 150.041 163.310 1.00 20.08 ?  149 TYR B CZ    1 
ATOM   6798  O  OH    . TYR B 1 149 ? 135.600 150.271 161.963 1.00 16.11 ?  149 TYR B OH    1 
ATOM   6799  N  N     . GLN B 1 150 ? 136.725 146.356 166.012 1.00 19.57 ?  150 GLN B N     1 
ATOM   6800  C  CA    . GLN B 1 150 ? 137.543 145.662 165.021 1.00 12.37 ?  150 GLN B CA    1 
ATOM   6801  C  C     . GLN B 1 150 ? 137.195 146.168 163.632 1.00 20.86 ?  150 GLN B C     1 
ATOM   6802  O  O     . GLN B 1 150 ? 136.065 145.940 163.160 1.00 32.26 ?  150 GLN B O     1 
ATOM   6803  C  CB    . GLN B 1 150 ? 137.331 144.151 165.109 1.00 19.69 ?  150 GLN B CB    1 
ATOM   6804  C  CG    . GLN B 1 150 ? 138.001 143.343 164.010 1.00 20.88 ?  150 GLN B CG    1 
ATOM   6805  C  CD    . GLN B 1 150 ? 139.492 143.585 163.927 1.00 20.38 ?  150 GLN B CD    1 
ATOM   6806  O  OE1   . GLN B 1 150 ? 140.241 143.240 164.837 1.00 27.08 ?  150 GLN B OE1   1 
ATOM   6807  N  NE2   . GLN B 1 150 ? 139.932 144.177 162.825 1.00 15.99 ?  150 GLN B NE2   1 
ATOM   6808  N  N     . PRO B 1 151 ? 138.101 146.861 162.948 1.00 27.09 ?  151 PRO B N     1 
ATOM   6809  C  CA    . PRO B 1 151 ? 137.863 147.181 161.538 1.00 14.54 ?  151 PRO B CA    1 
ATOM   6810  C  C     . PRO B 1 151 ? 137.748 145.905 160.720 1.00 20.56 ?  151 PRO B C     1 
ATOM   6811  O  O     . PRO B 1 151 ? 138.310 144.865 161.071 1.00 29.40 ?  151 PRO B O     1 
ATOM   6812  C  CB    . PRO B 1 151 ? 139.097 147.997 161.140 1.00 18.53 ?  151 PRO B CB    1 
ATOM   6813  C  CG    . PRO B 1 151 ? 139.677 148.474 162.427 1.00 20.87 ?  151 PRO B CG    1 
ATOM   6814  C  CD    . PRO B 1 151 ? 139.367 147.423 163.439 1.00 17.91 ?  151 PRO B CD    1 
ATOM   6815  N  N     . SER B 1 152 ? 136.994 145.989 159.629 1.00 24.85 ?  152 SER B N     1 
ATOM   6816  C  CA    . SER B 1 152 ? 136.744 144.816 158.806 1.00 18.45 ?  152 SER B CA    1 
ATOM   6817  C  C     . SER B 1 152 ? 138.049 144.246 158.260 1.00 24.70 ?  152 SER B C     1 
ATOM   6818  O  O     . SER B 1 152 ? 139.100 144.892 158.280 1.00 25.54 ?  152 SER B O     1 
ATOM   6819  C  CB    . SER B 1 152 ? 135.803 145.162 157.654 1.00 21.43 ?  152 SER B CB    1 
ATOM   6820  O  OG    . SER B 1 152 ? 136.411 146.074 156.758 1.00 26.76 ?  152 SER B OG    1 
ATOM   6821  N  N     . THR B 1 153 ? 137.968 143.009 157.776 1.00 32.55 ?  153 THR B N     1 
ATOM   6822  C  CA    . THR B 1 153 ? 139.136 142.351 157.195 1.00 20.41 ?  153 THR B CA    1 
ATOM   6823  C  C     . THR B 1 153 ? 139.821 143.183 156.115 1.00 31.50 ?  153 THR B C     1 
ATOM   6824  O  O     . THR B 1 153 ? 141.058 143.290 156.160 1.00 34.82 ?  153 THR B O     1 
ATOM   6825  C  CB    . THR B 1 153 ? 138.730 140.972 156.649 1.00 27.31 ?  153 THR B CB    1 
ATOM   6826  O  OG1   . THR B 1 153 ? 138.476 140.080 157.740 1.00 33.85 ?  153 THR B OG1   1 
ATOM   6827  C  CG2   . THR B 1 153 ? 139.828 140.391 155.776 1.00 30.48 ?  153 THR B CG2   1 
ATOM   6828  N  N     . PRO B 1 154 ? 139.121 143.798 155.153 1.00 33.93 ?  154 PRO B N     1 
ATOM   6829  C  CA    . PRO B 1 154 ? 139.835 144.671 154.203 1.00 21.38 ?  154 PRO B CA    1 
ATOM   6830  C  C     . PRO B 1 154 ? 140.542 145.834 154.875 1.00 22.56 ?  154 PRO B C     1 
ATOM   6831  O  O     . PRO B 1 154 ? 141.725 146.077 154.606 1.00 31.19 ?  154 PRO B O     1 
ATOM   6832  C  CB    . PRO B 1 154 ? 138.718 145.144 153.263 1.00 24.01 ?  154 PRO B CB    1 
ATOM   6833  C  CG    . PRO B 1 154 ? 137.659 144.135 153.399 1.00 22.70 ?  154 PRO B CG    1 
ATOM   6834  C  CD    . PRO B 1 154 ? 137.692 143.694 154.811 1.00 25.54 ?  154 PRO B CD    1 
ATOM   6835  N  N     . THR B 1 155 ? 139.850 146.559 155.754 1.00 25.99 ?  155 THR B N     1 
ATOM   6836  C  CA    . THR B 1 155 ? 140.458 147.710 156.412 1.00 22.14 ?  155 THR B CA    1 
ATOM   6837  C  C     . THR B 1 155 ? 141.614 147.286 157.309 1.00 25.99 ?  155 THR B C     1 
ATOM   6838  O  O     . THR B 1 155 ? 142.711 147.846 157.234 1.00 25.30 ?  155 THR B O     1 
ATOM   6839  C  CB    . THR B 1 155 ? 139.406 148.470 157.220 1.00 23.99 ?  155 THR B CB    1 
ATOM   6840  O  OG1   . THR B 1 155 ? 138.268 148.737 156.394 1.00 26.39 ?  155 THR B OG1   1 
ATOM   6841  C  CG2   . THR B 1 155 ? 139.976 149.779 157.724 1.00 20.80 ?  155 THR B CG2   1 
ATOM   6842  N  N     . PHE B 1 156 ? 141.386 146.288 158.164 1.00 30.04 ?  156 PHE B N     1 
ATOM   6843  C  CA    . PHE B 1 156 ? 142.425 145.857 159.093 1.00 21.34 ?  156 PHE B CA    1 
ATOM   6844  C  C     . PHE B 1 156 ? 143.638 145.306 158.354 1.00 29.13 ?  156 PHE B C     1 
ATOM   6845  O  O     . PHE B 1 156 ? 144.781 145.566 158.741 1.00 32.96 ?  156 PHE B O     1 
ATOM   6846  C  CB    . PHE B 1 156 ? 141.864 144.814 160.059 1.00 26.41 ?  156 PHE B CB    1 
ATOM   6847  C  CG    . PHE B 1 156 ? 142.678 144.642 161.306 1.00 30.29 ?  156 PHE B CG    1 
ATOM   6848  C  CD1   . PHE B 1 156 ? 142.939 145.722 162.131 1.00 28.22 ?  156 PHE B CD1   1 
ATOM   6849  C  CD2   . PHE B 1 156 ? 143.182 143.401 161.655 1.00 23.06 ?  156 PHE B CD2   1 
ATOM   6850  C  CE1   . PHE B 1 156 ? 143.689 145.569 163.278 1.00 30.39 ?  156 PHE B CE1   1 
ATOM   6851  C  CE2   . PHE B 1 156 ? 143.931 143.243 162.802 1.00 25.10 ?  156 PHE B CE2   1 
ATOM   6852  C  CZ    . PHE B 1 156 ? 144.185 144.328 163.614 1.00 30.21 ?  156 PHE B CZ    1 
ATOM   6853  N  N     . LEU B 1 157 ? 143.406 144.541 157.288 1.00 32.80 ?  157 LEU B N     1 
ATOM   6854  C  CA    . LEU B 1 157 ? 144.505 143.912 156.567 1.00 27.12 ?  157 LEU B CA    1 
ATOM   6855  C  C     . LEU B 1 157 ? 145.279 144.917 155.722 1.00 33.90 ?  157 LEU B C     1 
ATOM   6856  O  O     . LEU B 1 157 ? 146.511 144.851 155.646 1.00 41.74 ?  157 LEU B O     1 
ATOM   6857  C  CB    . LEU B 1 157 ? 143.964 142.781 155.694 1.00 32.38 ?  157 LEU B CB    1 
ATOM   6858  C  CG    . LEU B 1 157 ? 144.922 142.154 154.683 1.00 33.14 ?  157 LEU B CG    1 
ATOM   6859  C  CD1   . LEU B 1 157 ? 145.993 141.353 155.395 1.00 33.58 ?  157 LEU B CD1   1 
ATOM   6860  C  CD2   . LEU B 1 157 ? 144.160 141.282 153.702 1.00 30.09 ?  157 LEU B CD2   1 
ATOM   6861  N  N     . ASN B 1 158 ? 144.583 145.859 155.085 1.00 35.49 ?  158 ASN B N     1 
ATOM   6862  C  CA    . ASN B 1 158 ? 145.189 146.649 154.023 1.00 28.83 ?  158 ASN B CA    1 
ATOM   6863  C  C     . ASN B 1 158 ? 145.549 148.073 154.422 1.00 32.73 ?  158 ASN B C     1 
ATOM   6864  O  O     . ASN B 1 158 ? 146.327 148.710 153.705 1.00 39.64 ?  158 ASN B O     1 
ATOM   6865  C  CB    . ASN B 1 158 ? 144.250 146.699 152.811 1.00 33.04 ?  158 ASN B CB    1 
ATOM   6866  C  CG    . ASN B 1 158 ? 144.093 145.352 152.142 1.00 38.50 ?  158 ASN B CG    1 
ATOM   6867  O  OD1   . ASN B 1 158 ? 145.067 144.628 151.945 1.00 39.97 ?  158 ASN B OD1   1 
ATOM   6868  N  ND2   . ASN B 1 158 ? 142.861 145.007 151.791 1.00 36.86 ?  158 ASN B ND2   1 
ATOM   6869  N  N     . ALA B 1 159 ? 145.021 148.590 155.530 1.00 32.24 ?  159 ALA B N     1 
ATOM   6870  C  CA    . ALA B 1 159 ? 145.264 149.985 155.880 1.00 32.52 ?  159 ALA B CA    1 
ATOM   6871  C  C     . ALA B 1 159 ? 146.751 150.242 156.081 1.00 38.45 ?  159 ALA B C     1 
ATOM   6872  O  O     . ALA B 1 159 ? 147.426 149.523 156.823 1.00 44.26 ?  159 ALA B O     1 
ATOM   6873  C  CB    . ALA B 1 159 ? 144.491 150.362 157.142 1.00 33.14 ?  159 ALA B CB    1 
ATOM   6874  N  N     . GLY B 1 160 ? 147.258 151.277 155.418 1.00 43.15 ?  160 GLY B N     1 
ATOM   6875  C  CA    . GLY B 1 160 ? 148.658 151.626 155.527 1.00 38.96 ?  160 GLY B CA    1 
ATOM   6876  C  C     . GLY B 1 160 ? 149.617 150.721 154.793 1.00 41.97 ?  160 GLY B C     1 
ATOM   6877  O  O     . GLY B 1 160 ? 150.797 150.675 155.148 1.00 50.62 ?  160 GLY B O     1 
ATOM   6878  N  N     . ARG B 1 161 ? 149.153 149.997 153.779 1.00 44.25 ?  161 ARG B N     1 
ATOM   6879  C  CA    . ARG B 1 161 ? 149.996 149.102 153.001 1.00 44.56 ?  161 ARG B CA    1 
ATOM   6880  C  C     . ARG B 1 161 ? 150.100 149.598 151.565 1.00 48.02 ?  161 ARG B C     1 
ATOM   6881  O  O     . ARG B 1 161 ? 149.097 149.987 150.959 1.00 49.36 ?  161 ARG B O     1 
ATOM   6882  C  CB    . ARG B 1 161 ? 149.451 147.672 153.020 1.00 41.42 ?  161 ARG B CB    1 
ATOM   6883  C  CG    . ARG B 1 161 ? 149.577 146.981 154.365 1.00 41.80 ?  161 ARG B CG    1 
ATOM   6884  C  CD    . ARG B 1 161 ? 149.579 145.473 154.204 1.00 42.34 ?  161 ARG B CD    1 
ATOM   6885  N  NE    . ARG B 1 161 ? 149.577 144.791 155.491 1.00 44.00 ?  161 ARG B NE    1 
ATOM   6886  C  CZ    . ARG B 1 161 ? 149.286 143.509 155.659 1.00 46.38 ?  161 ARG B CZ    1 
ATOM   6887  N  NH1   . ARG B 1 161 ? 148.980 142.730 154.635 1.00 49.01 1  161 ARG B NH1   1 
ATOM   6888  N  NH2   . ARG B 1 161 ? 149.302 142.995 156.885 1.00 45.53 ?  161 ARG B NH2   1 
ATOM   6889  N  N     . LYS B 1 162 ? 151.322 149.586 151.029 1.00 57.73 ?  162 LYS B N     1 
ATOM   6890  C  CA    . LYS B 1 162 ? 151.540 150.053 149.664 1.00 57.20 ?  162 LYS B CA    1 
ATOM   6891  C  C     . LYS B 1 162 ? 150.907 149.108 148.649 1.00 58.40 ?  162 LYS B C     1 
ATOM   6892  O  O     . LYS B 1 162 ? 150.186 149.545 147.744 1.00 60.39 ?  162 LYS B O     1 
ATOM   6893  C  CB    . LYS B 1 162 ? 153.038 150.204 149.398 1.00 57.41 ?  162 LYS B CB    1 
ATOM   6894  C  CG    . LYS B 1 162 ? 153.396 150.413 147.939 1.00 59.42 ?  162 LYS B CG    1 
ATOM   6895  C  CD    . LYS B 1 162 ? 153.280 151.875 147.549 1.00 58.54 ?  162 LYS B CD    1 
ATOM   6896  C  CE    . LYS B 1 162 ? 154.319 152.719 148.268 1.00 57.34 ?  162 LYS B CE    1 
ATOM   6897  N  NZ    . LYS B 1 162 ? 153.952 154.161 148.280 1.00 58.40 1  162 LYS B NZ    1 
ATOM   6898  N  N     . ARG B 1 163 ? 151.163 147.808 148.785 1.00 57.99 ?  163 ARG B N     1 
ATOM   6899  C  CA    . ARG B 1 163 ? 150.588 146.806 147.887 1.00 60.65 ?  163 ARG B CA    1 
ATOM   6900  C  C     . ARG B 1 163 ? 149.317 146.217 148.499 1.00 62.84 ?  163 ARG B C     1 
ATOM   6901  O  O     . ARG B 1 163 ? 149.245 145.047 148.872 1.00 61.14 ?  163 ARG B O     1 
ATOM   6902  C  CB    . ARG B 1 163 ? 151.613 145.721 147.578 1.00 61.32 ?  163 ARG B CB    1 
ATOM   6903  C  CG    . ARG B 1 163 ? 152.664 146.132 146.561 1.00 62.25 ?  163 ARG B CG    1 
ATOM   6904  C  CD    . ARG B 1 163 ? 153.857 145.197 146.603 1.00 61.92 ?  163 ARG B CD    1 
ATOM   6905  N  NE    . ARG B 1 163 ? 154.747 145.497 147.717 1.00 64.82 ?  163 ARG B NE    1 
ATOM   6906  C  CZ    . ARG B 1 163 ? 155.538 144.609 148.302 1.00 66.36 ?  163 ARG B CZ    1 
ATOM   6907  N  NH1   . ARG B 1 163 ? 155.576 143.347 147.905 1.00 63.10 1  163 ARG B NH1   1 
ATOM   6908  N  NH2   . ARG B 1 163 ? 156.313 144.996 149.312 1.00 62.68 ?  163 ARG B NH2   1 
ATOM   6909  N  N     . ARG B 1 164 ? 148.302 147.067 148.594 1.00 56.69 ?  164 ARG B N     1 
ATOM   6910  C  CA    . ARG B 1 164 ? 147.054 146.733 149.259 1.00 53.92 ?  164 ARG B CA    1 
ATOM   6911  C  C     . ARG B 1 164 ? 145.908 146.686 148.260 1.00 53.28 ?  164 ARG B C     1 
ATOM   6912  O  O     . ARG B 1 164 ? 145.944 147.335 147.211 1.00 52.80 ?  164 ARG B O     1 
ATOM   6913  C  CB    . ARG B 1 164 ? 146.729 147.752 150.357 1.00 52.22 ?  164 ARG B CB    1 
ATOM   6914  C  CG    . ARG B 1 164 ? 146.194 149.078 149.831 1.00 51.00 ?  164 ARG B CG    1 
ATOM   6915  C  CD    . ARG B 1 164 ? 145.675 149.957 150.956 1.00 53.16 ?  164 ARG B CD    1 
ATOM   6916  N  NE    . ARG B 1 164 ? 145.362 151.311 150.514 1.00 53.94 ?  164 ARG B NE    1 
ATOM   6917  C  CZ    . ARG B 1 164 ? 144.262 151.649 149.854 1.00 56.41 ?  164 ARG B CZ    1 
ATOM   6918  N  NH1   . ARG B 1 164 ? 143.341 150.753 149.538 1.00 51.21 1  164 ARG B NH1   1 
ATOM   6919  N  NH2   . ARG B 1 164 ? 144.081 152.919 149.506 1.00 56.21 ?  164 ARG B NH2   1 
ATOM   6920  N  N     . GLY B 1 165 ? 144.893 145.894 148.593 1.00 50.68 ?  165 GLY B N     1 
ATOM   6921  C  CA    . GLY B 1 165 ? 143.621 145.976 147.916 1.00 47.35 ?  165 GLY B CA    1 
ATOM   6922  C  C     . GLY B 1 165 ? 142.795 147.122 148.461 1.00 51.38 ?  165 GLY B C     1 
ATOM   6923  O  O     . GLY B 1 165 ? 143.231 147.903 149.306 1.00 52.32 ?  165 GLY B O     1 
ATOM   6924  N  N     . GLU B 1 166 ? 141.570 147.223 147.960 1.00 48.09 ?  166 GLU B N     1 
ATOM   6925  C  CA    . GLU B 1 166 ? 140.669 148.256 148.443 1.00 42.72 ?  166 GLU B CA    1 
ATOM   6926  C  C     . GLU B 1 166 ? 140.254 147.969 149.883 1.00 42.86 ?  166 GLU B C     1 
ATOM   6927  O  O     . GLU B 1 166 ? 140.227 146.819 150.329 1.00 39.32 ?  166 GLU B O     1 
ATOM   6928  C  CB    . GLU B 1 166 ? 139.436 148.354 147.546 1.00 41.35 ?  166 GLU B CB    1 
ATOM   6929  C  CG    . GLU B 1 166 ? 138.989 149.779 147.260 1.00 45.08 ?  166 GLU B CG    1 
ATOM   6930  C  CD    . GLU B 1 166 ? 140.020 150.574 146.477 1.00 49.94 ?  166 GLU B CD    1 
ATOM   6931  O  OE1   . GLU B 1 166 ? 140.827 149.959 145.750 1.00 49.58 ?  166 GLU B OE1   1 
ATOM   6932  O  OE2   . GLU B 1 166 ? 140.024 151.818 146.591 1.00 48.28 -1 166 GLU B OE2   1 
ATOM   6933  N  N     . LEU B 1 167 ? 139.937 149.035 150.615 1.00 38.04 ?  167 LEU B N     1 
ATOM   6934  C  CA    . LEU B 1 167 ? 139.455 148.896 151.982 1.00 32.21 ?  167 LEU B CA    1 
ATOM   6935  C  C     . LEU B 1 167 ? 137.984 148.514 152.047 1.00 35.31 ?  167 LEU B C     1 
ATOM   6936  O  O     . LEU B 1 167 ? 137.484 148.216 153.136 1.00 38.65 ?  167 LEU B O     1 
ATOM   6937  C  CB    . LEU B 1 167 ? 139.689 150.197 152.756 1.00 33.90 ?  167 LEU B CB    1 
ATOM   6938  C  CG    . LEU B 1 167 ? 140.939 150.281 153.635 1.00 34.71 ?  167 LEU B CG    1 
ATOM   6939  C  CD1   . LEU B 1 167 ? 142.152 149.700 152.931 1.00 31.87 ?  167 LEU B CD1   1 
ATOM   6940  C  CD2   . LEU B 1 167 ? 141.199 151.718 154.037 1.00 32.27 ?  167 LEU B CD2   1 
ATOM   6941  N  N     . VAL B 1 168 ? 137.289 148.515 150.914 1.00 36.93 ?  168 VAL B N     1 
ATOM   6942  C  CA    . VAL B 1 168 ? 135.899 148.090 150.820 1.00 28.61 ?  168 VAL B CA    1 
ATOM   6943  C  C     . VAL B 1 168 ? 135.860 146.785 150.039 1.00 33.31 ?  168 VAL B C     1 
ATOM   6944  O  O     . VAL B 1 168 ? 136.563 146.634 149.034 1.00 39.76 ?  168 VAL B O     1 
ATOM   6945  C  CB    . VAL B 1 168 ? 135.026 149.166 150.142 1.00 27.73 ?  168 VAL B CB    1 
ATOM   6946  C  CG1   . VAL B 1 168 ? 133.569 148.736 150.109 1.00 34.50 ?  168 VAL B CG1   1 
ATOM   6947  C  CG2   . VAL B 1 168 ? 135.176 150.495 150.856 1.00 31.65 ?  168 VAL B CG2   1 
ATOM   6948  N  N     . SER B 1 169 ? 135.048 145.837 150.507 1.00 29.47 ?  169 SER B N     1 
ATOM   6949  C  CA    . SER B 1 169 ? 134.924 144.552 149.838 1.00 29.73 ?  169 SER B CA    1 
ATOM   6950  C  C     . SER B 1 169 ? 133.496 144.170 149.481 1.00 31.28 ?  169 SER B C     1 
ATOM   6951  O  O     . SER B 1 169 ? 133.293 143.107 148.888 1.00 40.22 ?  169 SER B O     1 
ATOM   6952  C  CB    . SER B 1 169 ? 135.539 143.435 150.693 1.00 36.48 ?  169 SER B CB    1 
ATOM   6953  O  OG    . SER B 1 169 ? 136.929 143.315 150.443 1.00 43.76 ?  169 SER B OG    1 
ATOM   6954  N  N     . CYS B 1 170 ? 132.505 144.987 149.824 1.00 25.02 ?  170 CYS B N     1 
ATOM   6955  C  CA    . CYS B 1 170 ? 131.122 144.728 149.449 1.00 23.57 ?  170 CYS B CA    1 
ATOM   6956  C  C     . CYS B 1 170 ? 130.664 145.819 148.496 1.00 23.82 ?  170 CYS B C     1 
ATOM   6957  O  O     . CYS B 1 170 ? 130.727 147.007 148.829 1.00 31.72 ?  170 CYS B O     1 
ATOM   6958  C  CB    . CYS B 1 170 ? 130.212 144.648 150.678 1.00 34.88 ?  170 CYS B CB    1 
ATOM   6959  S  SG    . CYS B 1 170 ? 130.263 146.070 151.790 1.00 46.19 ?  170 CYS B SG    1 
ATOM   6960  N  N     . PHE B 1 171 ? 130.217 145.416 147.311 1.00 25.86 ?  171 PHE B N     1 
ATOM   6961  C  CA    . PHE B 1 171 ? 129.711 146.331 146.301 1.00 11.61 ?  171 PHE B CA    1 
ATOM   6962  C  C     . PHE B 1 171 ? 128.388 145.803 145.773 1.00 16.26 ?  171 PHE B C     1 
ATOM   6963  O  O     . PHE B 1 171 ? 128.195 144.590 145.660 1.00 24.49 ?  171 PHE B O     1 
ATOM   6964  C  CB    . PHE B 1 171 ? 130.709 146.505 145.151 1.00 17.72 ?  171 PHE B CB    1 
ATOM   6965  C  CG    . PHE B 1 171 ? 132.088 146.872 145.604 1.00 17.83 ?  171 PHE B CG    1 
ATOM   6966  C  CD1   . PHE B 1 171 ? 132.400 148.181 145.915 1.00 19.98 ?  171 PHE B CD1   1 
ATOM   6967  C  CD2   . PHE B 1 171 ? 133.072 145.908 145.718 1.00 19.73 ?  171 PHE B CD2   1 
ATOM   6968  C  CE1   . PHE B 1 171 ? 133.664 148.521 146.338 1.00 13.29 ?  171 PHE B CE1   1 
ATOM   6969  C  CE2   . PHE B 1 171 ? 134.339 146.245 146.139 1.00 17.80 ?  171 PHE B CE2   1 
ATOM   6970  C  CZ    . PHE B 1 171 ? 134.635 147.554 146.448 1.00 10.83 ?  171 PHE B CZ    1 
ATOM   6971  N  N     . LEU B 1 172 ? 127.479 146.721 145.459 1.00 14.93 ?  172 LEU B N     1 
ATOM   6972  C  CA    . LEU B 1 172 ? 126.155 146.380 144.956 1.00 7.54  ?  172 LEU B CA    1 
ATOM   6973  C  C     . LEU B 1 172 ? 125.916 147.168 143.681 1.00 13.54 ?  172 LEU B C     1 
ATOM   6974  O  O     . LEU B 1 172 ? 125.863 148.401 143.715 1.00 21.70 ?  172 LEU B O     1 
ATOM   6975  C  CB    . LEU B 1 172 ? 125.067 146.688 145.988 1.00 8.45  ?  172 LEU B CB    1 
ATOM   6976  C  CG    . LEU B 1 172 ? 125.009 145.867 147.274 1.00 2.85  ?  172 LEU B CG    1 
ATOM   6977  C  CD1   . LEU B 1 172 ? 126.043 146.341 148.279 1.00 11.18 ?  172 LEU B CD1   1 
ATOM   6978  C  CD2   . LEU B 1 172 ? 123.622 145.958 147.863 1.00 16.09 ?  172 LEU B CD2   1 
ATOM   6979  N  N     . LEU B 1 173 ? 125.758 146.463 142.567 1.00 20.16 ?  173 LEU B N     1 
ATOM   6980  C  CA    . LEU B 1 173 ? 125.601 147.081 141.260 1.00 8.80  ?  173 LEU B CA    1 
ATOM   6981  C  C     . LEU B 1 173 ? 124.193 146.858 140.730 1.00 18.02 ?  173 LEU B C     1 
ATOM   6982  O  O     . LEU B 1 173 ? 123.652 145.752 140.816 1.00 29.94 ?  173 LEU B O     1 
ATOM   6983  C  CB    . LEU B 1 173 ? 126.612 146.519 140.260 1.00 13.72 ?  173 LEU B CB    1 
ATOM   6984  C  CG    . LEU B 1 173 ? 128.079 146.455 140.677 1.00 19.57 ?  173 LEU B CG    1 
ATOM   6985  C  CD1   . LEU B 1 173 ? 128.909 145.968 139.505 1.00 22.40 ?  173 LEU B CD1   1 
ATOM   6986  C  CD2   . LEU B 1 173 ? 128.566 147.808 141.158 1.00 25.38 ?  173 LEU B CD2   1 
ATOM   6987  N  N     . GLU B 1 174 ? 123.604 147.918 140.189 1.00 26.42 ?  174 GLU B N     1 
ATOM   6988  C  CA    . GLU B 1 174 ? 122.380 147.809 139.413 1.00 22.09 ?  174 GLU B CA    1 
ATOM   6989  C  C     . GLU B 1 174 ? 122.736 147.582 137.951 1.00 20.40 ?  174 GLU B C     1 
ATOM   6990  O  O     . GLU B 1 174 ? 123.623 148.245 137.408 1.00 31.33 ?  174 GLU B O     1 
ATOM   6991  C  CB    . GLU B 1 174 ? 121.534 149.076 139.549 1.00 26.22 ?  174 GLU B CB    1 
ATOM   6992  C  CG    . GLU B 1 174 ? 120.969 149.320 140.931 1.00 22.93 ?  174 GLU B CG    1 
ATOM   6993  C  CD    . GLU B 1 174 ? 119.488 149.027 141.006 1.00 27.60 ?  174 GLU B CD    1 
ATOM   6994  O  OE1   . GLU B 1 174 ? 118.931 148.521 140.010 1.00 31.09 ?  174 GLU B OE1   1 
ATOM   6995  O  OE2   . GLU B 1 174 ? 118.878 149.307 142.057 1.00 26.84 -1 174 GLU B OE2   1 
ATOM   6996  N  N     . VAL B 1 175 ? 122.044 146.642 137.317 1.00 17.81 ?  175 VAL B N     1 
ATOM   6997  C  CA    . VAL B 1 175 ? 122.260 146.320 135.913 1.00 17.01 ?  175 VAL B CA    1 
ATOM   6998  C  C     . VAL B 1 175 ? 121.019 146.738 135.139 1.00 21.62 ?  175 VAL B C     1 
ATOM   6999  O  O     . VAL B 1 175 ? 119.911 146.270 135.429 1.00 24.85 ?  175 VAL B O     1 
ATOM   7000  C  CB    . VAL B 1 175 ? 122.564 144.827 135.711 1.00 18.44 ?  175 VAL B CB    1 
ATOM   7001  C  CG1   . VAL B 1 175 ? 123.062 144.574 134.298 1.00 7.81  ?  175 VAL B CG1   1 
ATOM   7002  C  CG2   . VAL B 1 175 ? 123.580 144.349 136.737 1.00 18.22 ?  175 VAL B CG2   1 
ATOM   7003  N  N     . ASN B 1 176 ? 121.202 147.615 134.161 1.00 17.07 ?  176 ASN B N     1 
ATOM   7004  C  CA    . ASN B 1 176 ? 120.106 148.079 133.327 1.00 18.01 ?  176 ASN B CA    1 
ATOM   7005  C  C     . ASN B 1 176 ? 119.865 147.114 132.172 1.00 22.69 ?  176 ASN B C     1 
ATOM   7006  O  O     . ASN B 1 176 ? 120.738 146.333 131.787 1.00 27.73 ?  176 ASN B O     1 
ATOM   7007  C  CB    . ASN B 1 176 ? 120.391 149.482 132.794 1.00 19.42 ?  176 ASN B CB    1 
ATOM   7008  C  CG    . ASN B 1 176 ? 119.160 150.354 132.757 1.00 17.10 ?  176 ASN B CG    1 
ATOM   7009  O  OD1   . ASN B 1 176 ? 118.035 149.860 132.753 1.00 26.13 ?  176 ASN B OD1   1 
ATOM   7010  N  ND2   . ASN B 1 176 ? 119.366 151.663 132.732 1.00 18.44 ?  176 ASN B ND2   1 
ATOM   7011  N  N     . ASP B 1 177 ? 118.657 147.182 131.614 1.00 27.31 ?  177 ASP B N     1 
ATOM   7012  C  CA    . ASP B 1 177 ? 118.221 146.254 130.572 1.00 23.71 ?  177 ASP B CA    1 
ATOM   7013  C  C     . ASP B 1 177 ? 118.739 146.737 129.220 1.00 24.80 ?  177 ASP B C     1 
ATOM   7014  O  O     . ASP B 1 177 ? 118.020 147.329 128.412 1.00 31.45 ?  177 ASP B O     1 
ATOM   7015  C  CB    . ASP B 1 177 ? 116.705 146.122 130.585 1.00 20.34 ?  177 ASP B CB    1 
ATOM   7016  C  CG    . ASP B 1 177 ? 116.217 144.951 129.771 1.00 26.79 ?  177 ASP B CG    1 
ATOM   7017  O  OD1   . ASP B 1 177 ? 116.911 143.913 129.747 1.00 34.35 ?  177 ASP B OD1   1 
ATOM   7018  O  OD2   . ASP B 1 177 ? 115.136 145.065 129.160 1.00 33.24 -1 177 ASP B OD2   1 
ATOM   7019  N  N     . SER B 1 178 ? 120.018 146.465 128.974 1.00 19.77 ?  178 SER B N     1 
ATOM   7020  C  CA    . SER B 1 178 ? 120.669 146.833 127.724 1.00 17.17 ?  178 SER B CA    1 
ATOM   7021  C  C     . SER B 1 178 ? 121.994 146.093 127.638 1.00 21.75 ?  178 SER B C     1 
ATOM   7022  O  O     . SER B 1 178 ? 122.590 145.737 128.658 1.00 34.49 ?  178 SER B O     1 
ATOM   7023  C  CB    . SER B 1 178 ? 120.887 148.346 127.623 1.00 14.65 ?  178 SER B CB    1 
ATOM   7024  O  OG    . SER B 1 178 ? 122.126 148.722 128.188 1.00 27.93 ?  178 SER B OG    1 
ATOM   7025  N  N     . LEU B 1 179 ? 122.446 145.859 126.403 1.00 32.35 ?  179 LEU B N     1 
ATOM   7026  C  CA    . LEU B 1 179 ? 123.726 145.189 126.203 1.00 19.98 ?  179 LEU B CA    1 
ATOM   7027  C  C     . LEU B 1 179 ? 124.884 146.063 126.663 1.00 17.04 ?  179 LEU B C     1 
ATOM   7028  O  O     . LEU B 1 179 ? 125.871 145.559 127.208 1.00 26.29 ?  179 LEU B O     1 
ATOM   7029  C  CB    . LEU B 1 179 ? 123.898 144.801 124.735 1.00 23.05 ?  179 LEU B CB    1 
ATOM   7030  C  CG    . LEU B 1 179 ? 125.127 143.945 124.420 1.00 23.10 ?  179 LEU B CG    1 
ATOM   7031  C  CD1   . LEU B 1 179 ? 124.977 142.556 125.018 1.00 20.90 ?  179 LEU B CD1   1 
ATOM   7032  C  CD2   . LEU B 1 179 ? 125.359 143.864 122.922 1.00 21.71 ?  179 LEU B CD2   1 
ATOM   7033  N  N     . ASN B 1 180 ? 124.785 147.376 126.444 1.00 19.32 ?  180 ASN B N     1 
ATOM   7034  C  CA    . ASN B 1 180 ? 125.807 148.293 126.936 1.00 14.81 ?  180 ASN B CA    1 
ATOM   7035  C  C     . ASN B 1 180 ? 125.931 148.202 128.450 1.00 22.05 ?  180 ASN B C     1 
ATOM   7036  O  O     . ASN B 1 180 ? 127.037 148.093 128.995 1.00 30.45 ?  180 ASN B O     1 
ATOM   7037  C  CB    . ASN B 1 180 ? 125.470 149.724 126.515 1.00 23.77 ?  180 ASN B CB    1 
ATOM   7038  C  CG    . ASN B 1 180 ? 125.901 150.036 125.099 1.00 29.53 ?  180 ASN B CG    1 
ATOM   7039  O  OD1   . ASN B 1 180 ? 126.752 149.356 124.532 1.00 34.41 ?  180 ASN B OD1   1 
ATOM   7040  N  ND2   . ASN B 1 180 ? 125.311 151.073 124.518 1.00 27.63 ?  180 ASN B ND2   1 
ATOM   7041  N  N     . ASP B 1 181 ? 124.794 148.220 129.145 1.00 24.53 ?  181 ASP B N     1 
ATOM   7042  C  CA    . ASP B 1 181 ? 124.805 148.161 130.600 1.00 15.71 ?  181 ASP B CA    1 
ATOM   7043  C  C     . ASP B 1 181 ? 125.245 146.795 131.107 1.00 20.15 ?  181 ASP B C     1 
ATOM   7044  O  O     . ASP B 1 181 ? 125.916 146.712 132.136 1.00 30.36 ?  181 ASP B O     1 
ATOM   7045  C  CB    . ASP B 1 181 ? 123.426 148.521 131.141 1.00 27.99 ?  181 ASP B CB    1 
ATOM   7046  C  CG    . ASP B 1 181 ? 123.078 149.980 130.916 1.00 31.71 ?  181 ASP B CG    1 
ATOM   7047  O  OD1   . ASP B 1 181 ? 123.668 150.845 131.595 1.00 32.18 ?  181 ASP B OD1   1 
ATOM   7048  O  OD2   . ASP B 1 181 ? 122.213 150.264 130.061 1.00 26.06 -1 181 ASP B OD2   1 
ATOM   7049  N  N     . ILE B 1 182 ? 124.892 145.718 130.404 1.00 21.62 ?  182 ILE B N     1 
ATOM   7050  C  CA    . ILE B 1 182 ? 125.329 144.388 130.816 1.00 21.44 ?  182 ILE B CA    1 
ATOM   7051  C  C     . ILE B 1 182 ? 126.839 144.241 130.655 1.00 19.32 ?  182 ILE B C     1 
ATOM   7052  O  O     . ILE B 1 182 ? 127.523 143.697 131.532 1.00 22.73 ?  182 ILE B O     1 
ATOM   7053  C  CB    . ILE B 1 182 ? 124.559 143.311 130.029 1.00 19.85 ?  182 ILE B CB    1 
ATOM   7054  C  CG1   . ILE B 1 182 ? 123.145 143.164 130.591 1.00 20.49 ?  182 ILE B CG1   1 
ATOM   7055  C  CG2   . ILE B 1 182 ? 125.288 141.980 130.072 1.00 22.79 ?  182 ILE B CG2   1 
ATOM   7056  C  CD1   . ILE B 1 182 ? 122.206 142.423 129.684 1.00 23.22 ?  182 ILE B CD1   1 
ATOM   7057  N  N     . SER B 1 183 ? 127.383 144.725 129.537 1.00 26.18 ?  183 SER B N     1 
ATOM   7058  C  CA    . SER B 1 183 ? 128.829 144.683 129.344 1.00 16.94 ?  183 SER B CA    1 
ATOM   7059  C  C     . SER B 1 183 ? 129.546 145.538 130.380 1.00 19.44 ?  183 SER B C     1 
ATOM   7060  O  O     . SER B 1 183 ? 130.589 145.138 130.913 1.00 27.79 ?  183 SER B O     1 
ATOM   7061  C  CB    . SER B 1 183 ? 129.181 145.144 127.932 1.00 17.25 ?  183 SER B CB    1 
ATOM   7062  O  OG    . SER B 1 183 ? 128.609 146.407 127.653 1.00 33.98 ?  183 SER B OG    1 
ATOM   7063  N  N     . ARG B 1 184 ? 129.001 146.719 130.682 1.00 25.39 ?  184 ARG B N     1 
ATOM   7064  C  CA    . ARG B 1 184 ? 129.598 147.556 131.715 1.00 17.87 ?  184 ARG B CA    1 
ATOM   7065  C  C     . ARG B 1 184 ? 129.519 146.888 133.081 1.00 26.39 ?  184 ARG B C     1 
ATOM   7066  O  O     . ARG B 1 184 ? 130.440 147.014 133.892 1.00 31.50 ?  184 ARG B O     1 
ATOM   7067  C  CB    . ARG B 1 184 ? 128.917 148.922 131.744 1.00 16.95 ?  184 ARG B CB    1 
ATOM   7068  C  CG    . ARG B 1 184 ? 129.591 149.915 132.669 1.00 27.61 ?  184 ARG B CG    1 
ATOM   7069  C  CD    . ARG B 1 184 ? 131.086 149.966 132.438 1.00 26.09 ?  184 ARG B CD    1 
ATOM   7070  N  NE    . ARG B 1 184 ? 131.437 150.931 131.405 1.00 34.37 ?  184 ARG B NE    1 
ATOM   7071  C  CZ    . ARG B 1 184 ? 132.598 150.955 130.767 1.00 34.93 ?  184 ARG B CZ    1 
ATOM   7072  N  NH1   . ARG B 1 184 ? 133.549 150.073 131.027 1.00 25.59 1  184 ARG B NH1   1 
ATOM   7073  N  NH2   . ARG B 1 184 ? 132.812 151.891 129.845 1.00 32.42 ?  184 ARG B NH2   1 
ATOM   7074  N  N     . ALA B 1 185 ? 128.421 146.183 133.361 1.00 31.15 ?  185 ALA B N     1 
ATOM   7075  C  CA    . ALA B 1 185 ? 128.300 145.459 134.619 1.00 8.29  ?  185 ALA B CA    1 
ATOM   7076  C  C     . ALA B 1 185 ? 129.343 144.360 134.721 1.00 12.71 ?  185 ALA B C     1 
ATOM   7077  O  O     . ALA B 1 185 ? 129.944 144.164 135.781 1.00 22.32 ?  185 ALA B O     1 
ATOM   7078  C  CB    . ALA B 1 185 ? 126.894 144.877 134.759 1.00 9.14  ?  185 ALA B CB    1 
ATOM   7079  N  N     . ILE B 1 186 ? 129.575 143.631 133.628 1.00 22.82 ?  186 ILE B N     1 
ATOM   7080  C  CA    . ILE B 1 186 ? 130.614 142.602 133.630 1.00 23.20 ?  186 ILE B CA    1 
ATOM   7081  C  C     . ILE B 1 186 ? 131.982 143.232 133.864 1.00 17.77 ?  186 ILE B C     1 
ATOM   7082  O  O     . ILE B 1 186 ? 132.789 142.731 134.661 1.00 26.42 ?  186 ILE B O     1 
ATOM   7083  C  CB    . ILE B 1 186 ? 130.574 141.801 132.314 1.00 27.87 ?  186 ILE B CB    1 
ATOM   7084  C  CG1   . ILE B 1 186 ? 129.429 140.790 132.340 1.00 21.95 ?  186 ILE B CG1   1 
ATOM   7085  C  CG2   . ILE B 1 186 ? 131.897 141.091 132.067 1.00 23.79 ?  186 ILE B CG2   1 
ATOM   7086  C  CD1   . ILE B 1 186 ? 128.763 140.600 131.002 1.00 27.46 ?  186 ILE B CD1   1 
ATOM   7087  N  N     . ASP B 1 187 ? 132.257 144.348 133.187 1.00 23.35 ?  187 ASP B N     1 
ATOM   7088  C  CA    . ASP B 1 187 ? 133.535 145.031 133.356 1.00 18.17 ?  187 ASP B CA    1 
ATOM   7089  C  C     . ASP B 1 187 ? 133.731 145.491 134.796 1.00 28.09 ?  187 ASP B C     1 
ATOM   7090  O  O     . ASP B 1 187 ? 134.791 145.270 135.390 1.00 34.35 ?  187 ASP B O     1 
ATOM   7091  C  CB    . ASP B 1 187 ? 133.619 146.219 132.398 1.00 17.20 ?  187 ASP B CB    1 
ATOM   7092  C  CG    . ASP B 1 187 ? 134.665 147.232 132.814 1.00 35.28 ?  187 ASP B CG    1 
ATOM   7093  O  OD1   . ASP B 1 187 ? 135.839 146.846 132.987 1.00 34.32 ?  187 ASP B OD1   1 
ATOM   7094  O  OD2   . ASP B 1 187 ? 134.311 148.419 132.974 1.00 41.83 -1 187 ASP B OD2   1 
ATOM   7095  N  N     . ILE B 1 188 ? 132.714 146.131 135.373 1.00 23.60 ?  188 ILE B N     1 
ATOM   7096  C  CA    . ILE B 1 188 ? 132.828 146.654 136.729 1.00 22.56 ?  188 ILE B CA    1 
ATOM   7097  C  C     . ILE B 1 188 ? 132.930 145.518 137.736 1.00 25.27 ?  188 ILE B C     1 
ATOM   7098  O  O     . ILE B 1 188 ? 133.655 145.617 138.731 1.00 27.77 ?  188 ILE B O     1 
ATOM   7099  C  CB    . ILE B 1 188 ? 131.646 147.590 137.042 1.00 26.73 ?  188 ILE B CB    1 
ATOM   7100  C  CG1   . ILE B 1 188 ? 131.696 148.830 136.153 1.00 25.52 ?  188 ILE B CG1   1 
ATOM   7101  C  CG2   . ILE B 1 188 ? 131.671 148.024 138.489 1.00 26.77 ?  188 ILE B CG2   1 
ATOM   7102  C  CD1   . ILE B 1 188 ? 130.488 149.720 136.302 1.00 21.59 ?  188 ILE B CD1   1 
ATOM   7103  N  N     . SER B 1 189 ? 132.208 144.421 137.500 1.00 19.85 ?  189 SER B N     1 
ATOM   7104  C  CA    . SER B 1 189 ? 132.319 143.261 138.374 1.00 13.40 ?  189 SER B CA    1 
ATOM   7105  C  C     . SER B 1 189 ? 133.730 142.698 138.358 1.00 20.94 ?  189 SER B C     1 
ATOM   7106  O  O     . SER B 1 189 ? 134.284 142.369 139.411 1.00 25.83 ?  189 SER B O     1 
ATOM   7107  C  CB    . SER B 1 189 ? 131.310 142.193 137.957 1.00 20.14 ?  189 SER B CB    1 
ATOM   7108  O  OG    . SER B 1 189 ? 129.994 142.713 137.958 1.00 29.91 ?  189 SER B OG    1 
ATOM   7109  N  N     . MET B 1 190 ? 134.336 142.588 137.172 1.00 30.19 ?  190 MET B N     1 
ATOM   7110  C  CA    . MET B 1 190 ? 135.711 142.104 137.103 1.00 22.37 ?  190 MET B CA    1 
ATOM   7111  C  C     . MET B 1 190 ? 136.679 143.080 137.761 1.00 16.93 ?  190 MET B C     1 
ATOM   7112  O  O     . MET B 1 190 ? 137.626 142.660 138.433 1.00 21.26 ?  190 MET B O     1 
ATOM   7113  C  CB    . MET B 1 190 ? 136.113 141.839 135.653 1.00 21.58 ?  190 MET B CB    1 
ATOM   7114  C  CG    . MET B 1 190 ? 135.349 140.701 135.012 1.00 27.32 ?  190 MET B CG    1 
ATOM   7115  S  SD    . MET B 1 190 ? 136.208 139.950 133.620 1.00 35.79 ?  190 MET B SD    1 
ATOM   7116  C  CE    . MET B 1 190 ? 136.133 141.280 132.428 1.00 25.79 ?  190 MET B CE    1 
ATOM   7117  N  N     . GLN B 1 191 ? 136.457 144.384 137.587 1.00 21.42 ?  191 GLN B N     1 
ATOM   7118  C  CA    . GLN B 1 191 ? 137.344 145.370 138.199 1.00 23.07 ?  191 GLN B CA    1 
ATOM   7119  C  C     . GLN B 1 191 ? 137.254 145.337 139.720 1.00 25.57 ?  191 GLN B C     1 
ATOM   7120  O  O     . GLN B 1 191 ? 138.271 145.476 140.409 1.00 32.40 ?  191 GLN B O     1 
ATOM   7121  C  CB    . GLN B 1 191 ? 137.025 146.771 137.676 1.00 24.32 ?  191 GLN B CB    1 
ATOM   7122  C  CG    . GLN B 1 191 ? 137.243 146.948 136.184 1.00 23.68 ?  191 GLN B CG    1 
ATOM   7123  C  CD    . GLN B 1 191 ? 138.707 147.009 135.802 1.00 27.63 ?  191 GLN B CD    1 
ATOM   7124  O  OE1   . GLN B 1 191 ? 139.588 147.054 136.660 1.00 30.80 ?  191 GLN B OE1   1 
ATOM   7125  N  NE2   . GLN B 1 191 ? 138.975 147.009 134.504 1.00 28.81 ?  191 GLN B NE2   1 
ATOM   7126  N  N     . LEU B 1 192 ? 136.048 145.168 140.263 1.00 24.98 ?  192 LEU B N     1 
ATOM   7127  C  CA    . LEU B 1 192 ? 135.882 145.148 141.711 1.00 16.38 ?  192 LEU B CA    1 
ATOM   7128  C  C     . LEU B 1 192 ? 136.343 143.826 142.312 1.00 23.84 ?  192 LEU B C     1 
ATOM   7129  O  O     . LEU B 1 192 ? 136.912 143.807 143.407 1.00 36.16 ?  192 LEU B O     1 
ATOM   7130  C  CB    . LEU B 1 192 ? 134.426 145.427 142.077 1.00 18.21 ?  192 LEU B CB    1 
ATOM   7131  C  CG    . LEU B 1 192 ? 133.909 146.826 141.735 1.00 19.83 ?  192 LEU B CG    1 
ATOM   7132  C  CD1   . LEU B 1 192 ? 132.402 146.888 141.883 1.00 19.10 ?  192 LEU B CD1   1 
ATOM   7133  C  CD2   . LEU B 1 192 ? 134.582 147.877 142.600 1.00 17.33 ?  192 LEU B CD2   1 
ATOM   7134  N  N     . SER B 1 193 ? 136.103 142.712 141.616 1.00 27.70 ?  193 SER B N     1 
ATOM   7135  C  CA    . SER B 1 193 ? 136.636 141.432 142.064 1.00 20.19 ?  193 SER B CA    1 
ATOM   7136  C  C     . SER B 1 193 ? 138.156 141.419 142.001 1.00 28.24 ?  193 SER B C     1 
ATOM   7137  O  O     . SER B 1 193 ? 138.805 140.759 142.817 1.00 36.87 ?  193 SER B O     1 
ATOM   7138  C  CB    . SER B 1 193 ? 136.053 140.301 141.219 1.00 25.64 ?  193 SER B CB    1 
ATOM   7139  O  OG    . SER B 1 193 ? 136.410 139.036 141.745 1.00 42.27 ?  193 SER B OG    1 
ATOM   7140  N  N     . LYS B 1 194 ? 138.735 142.142 141.041 1.00 34.56 ?  194 LYS B N     1 
ATOM   7141  C  CA    . LYS B 1 194 ? 140.184 142.298 140.991 1.00 32.01 ?  194 LYS B CA    1 
ATOM   7142  C  C     . LYS B 1 194 ? 140.704 142.977 142.251 1.00 35.73 ?  194 LYS B C     1 
ATOM   7143  O  O     . LYS B 1 194 ? 141.743 142.586 142.794 1.00 43.69 ?  194 LYS B O     1 
ATOM   7144  C  CB    . LYS B 1 194 ? 140.569 143.093 139.743 1.00 27.19 ?  194 LYS B CB    1 
ATOM   7145  C  CG    . LYS B 1 194 ? 141.954 143.698 139.781 1.00 36.44 ?  194 LYS B CG    1 
ATOM   7146  C  CD    . LYS B 1 194 ? 142.136 144.718 138.671 1.00 38.23 ?  194 LYS B CD    1 
ATOM   7147  C  CE    . LYS B 1 194 ? 143.609 145.004 138.423 1.00 36.81 ?  194 LYS B CE    1 
ATOM   7148  N  NZ    . LYS B 1 194 ? 143.800 146.006 137.339 1.00 37.91 1  194 LYS B NZ    1 
ATOM   7149  N  N     . LEU B 1 195 ? 139.983 143.988 142.739 1.00 34.15 ?  195 LEU B N     1 
ATOM   7150  C  CA    . LEU B 1 195 ? 140.339 144.650 143.988 1.00 35.73 ?  195 LEU B CA    1 
ATOM   7151  C  C     . LEU B 1 195 ? 140.118 143.766 145.207 1.00 35.64 ?  195 LEU B C     1 
ATOM   7152  O  O     . LEU B 1 195 ? 140.541 144.140 146.305 1.00 42.62 ?  195 LEU B O     1 
ATOM   7153  C  CB    . LEU B 1 195 ? 139.538 145.943 144.141 1.00 38.37 ?  195 LEU B CB    1 
ATOM   7154  C  CG    . LEU B 1 195 ? 139.723 146.979 143.034 1.00 37.71 ?  195 LEU B CG    1 
ATOM   7155  C  CD1   . LEU B 1 195 ? 138.886 148.218 143.315 1.00 32.38 ?  195 LEU B CD1   1 
ATOM   7156  C  CD2   . LEU B 1 195 ? 141.189 147.336 142.874 1.00 34.65 ?  195 LEU B CD2   1 
ATOM   7157  N  N     . GLY B 1 196 ? 139.467 142.620 145.046 1.00 31.06 ?  196 GLY B N     1 
ATOM   7158  C  CA    . GLY B 1 196 ? 139.219 141.712 146.143 1.00 30.00 ?  196 GLY B CA    1 
ATOM   7159  C  C     . GLY B 1 196 ? 137.862 141.834 146.793 1.00 36.77 ?  196 GLY B C     1 
ATOM   7160  O  O     . GLY B 1 196 ? 137.644 141.223 147.844 1.00 39.00 ?  196 GLY B O     1 
ATOM   7161  N  N     . GLY B 1 197 ? 136.944 142.593 146.206 1.00 30.42 ?  197 GLY B N     1 
ATOM   7162  C  CA    . GLY B 1 197 ? 135.644 142.840 146.802 1.00 25.49 ?  197 GLY B CA    1 
ATOM   7163  C  C     . GLY B 1 197 ? 134.562 141.942 146.225 1.00 27.37 ?  197 GLY B C     1 
ATOM   7164  O  O     . GLY B 1 197 ? 134.560 141.640 145.032 1.00 31.59 ?  197 GLY B O     1 
ATOM   7165  N  N     . GLY B 1 198 ? 133.645 141.522 147.092 1.00 25.08 ?  198 GLY B N     1 
ATOM   7166  C  CA    . GLY B 1 198 ? 132.473 140.806 146.628 1.00 14.95 ?  198 GLY B CA    1 
ATOM   7167  C  C     . GLY B 1 198 ? 131.488 141.755 145.970 1.00 14.13 ?  198 GLY B C     1 
ATOM   7168  O  O     . GLY B 1 198 ? 131.245 142.863 146.448 1.00 24.21 ?  198 GLY B O     1 
ATOM   7169  N  N     . VAL B 1 199 ? 130.919 141.313 144.854 1.00 22.61 ?  199 VAL B N     1 
ATOM   7170  C  CA    . VAL B 1 199 ? 130.066 142.148 144.017 1.00 17.88 ?  199 VAL B CA    1 
ATOM   7171  C  C     . VAL B 1 199 ? 128.681 141.526 143.958 1.00 8.99  ?  199 VAL B C     1 
ATOM   7172  O  O     . VAL B 1 199 ? 128.540 140.336 143.655 1.00 18.81 ?  199 VAL B O     1 
ATOM   7173  C  CB    . VAL B 1 199 ? 130.650 142.315 142.603 1.00 12.95 ?  199 VAL B CB    1 
ATOM   7174  C  CG1   . VAL B 1 199 ? 129.850 143.337 141.819 1.00 18.72 ?  199 VAL B CG1   1 
ATOM   7175  C  CG2   . VAL B 1 199 ? 132.111 142.713 142.678 1.00 17.15 ?  199 VAL B CG2   1 
ATOM   7176  N  N     . SER B 1 200 ? 127.663 142.328 144.250 1.00 18.60 ?  200 SER B N     1 
ATOM   7177  C  CA    . SER B 1 200 ? 126.273 141.914 144.148 1.00 7.07  ?  200 SER B CA    1 
ATOM   7178  C  C     . SER B 1 200 ? 125.621 142.663 142.998 1.00 13.22 ?  200 SER B C     1 
ATOM   7179  O  O     . SER B 1 200 ? 125.781 143.881 142.875 1.00 22.94 ?  200 SER B O     1 
ATOM   7180  C  CB    . SER B 1 200 ? 125.523 142.179 145.452 1.00 13.11 ?  200 SER B CB    1 
ATOM   7181  O  OG    . SER B 1 200 ? 124.366 141.370 145.542 1.00 22.00 ?  200 SER B OG    1 
ATOM   7182  N  N     . LEU B 1 201 ? 124.894 141.937 142.156 1.00 20.67 ?  201 LEU B N     1 
ATOM   7183  C  CA    . LEU B 1 201 ? 124.279 142.501 140.965 1.00 7.80  ?  201 LEU B CA    1 
ATOM   7184  C  C     . LEU B 1 201 ? 122.773 142.304 141.022 1.00 10.12 ?  201 LEU B C     1 
ATOM   7185  O  O     . LEU B 1 201 ? 122.297 141.208 141.335 1.00 14.11 ?  201 LEU B O     1 
ATOM   7186  C  CB    . LEU B 1 201 ? 124.855 141.859 139.701 1.00 20.30 ?  201 LEU B CB    1 
ATOM   7187  C  CG    . LEU B 1 201 ? 126.362 142.050 139.529 1.00 18.96 ?  201 LEU B CG    1 
ATOM   7188  C  CD1   . LEU B 1 201 ? 127.103 140.747 139.780 1.00 22.23 ?  201 LEU B CD1   1 
ATOM   7189  C  CD2   . LEU B 1 201 ? 126.678 142.595 138.150 1.00 16.03 ?  201 LEU B CD2   1 
ATOM   7190  N  N     . ASN B 1 202 ? 122.032 143.369 140.734 1.00 15.66 ?  202 ASN B N     1 
ATOM   7191  C  CA    . ASN B 1 202 ? 120.579 143.312 140.641 1.00 7.09  ?  202 ASN B CA    1 
ATOM   7192  C  C     . ASN B 1 202 ? 120.206 142.990 139.200 1.00 22.09 ?  202 ASN B C     1 
ATOM   7193  O  O     . ASN B 1 202 ? 120.459 143.789 138.293 1.00 34.99 ?  202 ASN B O     1 
ATOM   7194  C  CB    . ASN B 1 202 ? 119.958 144.630 141.090 1.00 9.23  ?  202 ASN B CB    1 
ATOM   7195  C  CG    . ASN B 1 202 ? 118.487 144.498 141.420 1.00 13.69 ?  202 ASN B CG    1 
ATOM   7196  O  OD1   . ASN B 1 202 ? 118.002 143.410 141.725 1.00 23.02 ?  202 ASN B OD1   1 
ATOM   7197  N  ND2   . ASN B 1 202 ? 117.769 145.611 141.362 1.00 13.77 ?  202 ASN B ND2   1 
ATOM   7198  N  N     . LEU B 1 203 ? 119.606 141.823 138.987 1.00 13.13 ?  203 LEU B N     1 
ATOM   7199  C  CA    . LEU B 1 203 ? 119.226 141.371 137.657 1.00 10.38 ?  203 LEU B CA    1 
ATOM   7200  C  C     . LEU B 1 203 ? 117.738 141.535 137.383 1.00 11.78 ?  203 LEU B C     1 
ATOM   7201  O  O     . LEU B 1 203 ? 117.244 141.017 136.379 1.00 20.55 ?  203 LEU B O     1 
ATOM   7202  C  CB    . LEU B 1 203 ? 119.637 139.909 137.465 1.00 19.25 ?  203 LEU B CB    1 
ATOM   7203  C  CG    . LEU B 1 203 ? 121.122 139.579 137.626 1.00 19.16 ?  203 LEU B CG    1 
ATOM   7204  C  CD1   . LEU B 1 203 ? 121.434 138.227 137.013 1.00 15.97 ?  203 LEU B CD1   1 
ATOM   7205  C  CD2   . LEU B 1 203 ? 121.995 140.659 137.009 1.00 18.43 ?  203 LEU B CD2   1 
ATOM   7206  N  N     . SER B 1 204 ? 117.015 142.247 138.250 1.00 16.09 ?  204 SER B N     1 
ATOM   7207  C  CA    . SER B 1 204 ? 115.565 142.333 138.112 1.00 17.71 ?  204 SER B CA    1 
ATOM   7208  C  C     . SER B 1 204 ? 115.151 143.220 136.945 1.00 20.50 ?  204 SER B C     1 
ATOM   7209  O  O     . SER B 1 204 ? 114.070 143.030 136.381 1.00 27.93 ?  204 SER B O     1 
ATOM   7210  C  CB    . SER B 1 204 ? 114.947 142.844 139.411 1.00 12.46 ?  204 SER B CB    1 
ATOM   7211  O  OG    . SER B 1 204 ? 115.199 141.946 140.473 1.00 24.39 ?  204 SER B OG    1 
ATOM   7212  N  N     . LYS B 1 205 ? 115.982 144.193 136.576 1.00 17.96 ?  205 LYS B N     1 
ATOM   7213  C  CA    . LYS B 1 205 ? 115.659 145.059 135.451 1.00 16.97 ?  205 LYS B CA    1 
ATOM   7214  C  C     . LYS B 1 205 ? 115.857 144.374 134.108 1.00 21.08 ?  205 LYS B C     1 
ATOM   7215  O  O     . LYS B 1 205 ? 115.220 144.773 133.128 1.00 30.01 ?  205 LYS B O     1 
ATOM   7216  C  CB    . LYS B 1 205 ? 116.496 146.335 135.505 1.00 17.17 ?  205 LYS B CB    1 
ATOM   7217  C  CG    . LYS B 1 205 ? 116.119 147.256 136.641 1.00 13.29 ?  205 LYS B CG    1 
ATOM   7218  C  CD    . LYS B 1 205 ? 116.921 148.535 136.594 1.00 19.85 ?  205 LYS B CD    1 
ATOM   7219  C  CE    . LYS B 1 205 ? 116.382 149.550 137.578 1.00 24.37 ?  205 LYS B CE    1 
ATOM   7220  N  NZ    . LYS B 1 205 ? 116.565 149.117 138.987 1.00 17.22 1  205 LYS B NZ    1 
ATOM   7221  N  N     . LEU B 1 206 ? 116.722 143.366 134.040 1.00 17.26 ?  206 LEU B N     1 
ATOM   7222  C  CA    . LEU B 1 206 ? 116.927 142.636 132.799 1.00 11.29 ?  206 LEU B CA    1 
ATOM   7223  C  C     . LEU B 1 206 ? 115.646 141.926 132.385 1.00 19.76 ?  206 LEU B C     1 
ATOM   7224  O  O     . LEU B 1 206 ? 114.993 141.270 133.201 1.00 25.80 ?  206 LEU B O     1 
ATOM   7225  C  CB    . LEU B 1 206 ? 118.058 141.624 132.963 1.00 19.80 ?  206 LEU B CB    1 
ATOM   7226  C  CG    . LEU B 1 206 ? 119.382 142.178 133.478 1.00 22.20 ?  206 LEU B CG    1 
ATOM   7227  C  CD1   . LEU B 1 206 ? 120.369 141.051 133.695 1.00 17.52 ?  206 LEU B CD1   1 
ATOM   7228  C  CD2   . LEU B 1 206 ? 119.937 143.205 132.513 1.00 26.19 ?  206 LEU B CD2   1 
ATOM   7229  N  N     . ARG B 1 207 ? 115.290 142.056 131.111 1.00 26.99 ?  207 ARG B N     1 
ATOM   7230  C  CA    . ARG B 1 207 ? 114.076 141.426 130.620 1.00 22.95 ?  207 ARG B CA    1 
ATOM   7231  C  C     . ARG B 1 207 ? 114.242 139.911 130.565 1.00 26.41 ?  207 ARG B C     1 
ATOM   7232  O  O     . ARG B 1 207 ? 115.346 139.385 130.398 1.00 30.49 ?  207 ARG B O     1 
ATOM   7233  C  CB    . ARG B 1 207 ? 113.698 141.977 129.245 1.00 23.26 ?  207 ARG B CB    1 
ATOM   7234  C  CG    . ARG B 1 207 ? 114.698 141.721 128.140 1.00 24.90 ?  207 ARG B CG    1 
ATOM   7235  C  CD    . ARG B 1 207 ? 114.328 142.517 126.900 1.00 22.50 ?  207 ARG B CD    1 
ATOM   7236  N  NE    . ARG B 1 207 ? 114.659 143.928 127.047 1.00 27.64 ?  207 ARG B NE    1 
ATOM   7237  C  CZ    . ARG B 1 207 ? 114.824 144.771 126.037 1.00 21.97 ?  207 ARG B CZ    1 
ATOM   7238  N  NH1   . ARG B 1 207 ? 114.660 144.388 124.783 1.00 28.60 1  207 ARG B NH1   1 
ATOM   7239  N  NH2   . ARG B 1 207 ? 115.164 146.031 126.293 1.00 18.36 ?  207 ARG B NH2   1 
ATOM   7240  N  N     . ALA B 1 208 ? 113.123 139.211 130.717 1.00 30.71 ?  208 ALA B N     1 
ATOM   7241  C  CA    . ALA B 1 208 ? 113.137 137.770 130.879 1.00 29.17 ?  208 ALA B CA    1 
ATOM   7242  C  C     . ALA B 1 208 ? 113.484 137.068 129.567 1.00 33.52 ?  208 ALA B C     1 
ATOM   7243  O  O     . ALA B 1 208 ? 113.649 137.688 128.513 1.00 35.30 ?  208 ALA B O     1 
ATOM   7244  C  CB    . ALA B 1 208 ? 111.785 137.282 131.390 1.00 26.41 ?  208 ALA B CB    1 
ATOM   7245  N  N     . LYS B 1 209 ? 113.602 135.747 129.655 1.00 26.37 ?  209 LYS B N     1 
ATOM   7246  C  CA    . LYS B 1 209 ? 113.856 134.928 128.481 1.00 22.11 ?  209 LYS B CA    1 
ATOM   7247  C  C     . LYS B 1 209 ? 112.643 134.930 127.560 1.00 33.53 ?  209 LYS B C     1 
ATOM   7248  O  O     . LYS B 1 209 ? 111.497 134.871 128.014 1.00 35.56 ?  209 LYS B O     1 
ATOM   7249  C  CB    . LYS B 1 209 ? 114.198 133.499 128.899 1.00 27.44 ?  209 LYS B CB    1 
ATOM   7250  C  CG    . LYS B 1 209 ? 115.018 132.725 127.882 1.00 33.01 ?  209 LYS B CG    1 
ATOM   7251  C  CD    . LYS B 1 209 ? 114.512 131.299 127.731 1.00 31.98 ?  209 LYS B CD    1 
ATOM   7252  C  CE    . LYS B 1 209 ? 114.003 130.744 129.051 1.00 36.48 ?  209 LYS B CE    1 
ATOM   7253  N  NZ    . LYS B 1 209 ? 113.346 129.419 128.884 1.00 35.63 1  209 LYS B NZ    1 
ATOM   7254  N  N     . GLY B 1 210 ? 112.902 134.990 126.257 1.00 36.34 ?  210 GLY B N     1 
ATOM   7255  C  CA    . GLY B 1 210 ? 111.823 135.052 125.294 1.00 32.08 ?  210 GLY B CA    1 
ATOM   7256  C  C     . GLY B 1 210 ? 111.170 136.407 125.163 1.00 36.40 ?  210 GLY B C     1 
ATOM   7257  O  O     . GLY B 1 210 ? 109.966 136.482 124.898 1.00 38.93 ?  210 GLY B O     1 
ATOM   7258  N  N     . GLU B 1 211 ? 111.923 137.483 125.353 1.00 39.33 ?  211 GLU B N     1 
ATOM   7259  C  CA    . GLU B 1 211 ? 111.429 138.836 125.158 1.00 33.16 ?  211 GLU B CA    1 
ATOM   7260  C  C     . GLU B 1 211 ? 111.997 139.416 123.870 1.00 36.67 ?  211 GLU B C     1 
ATOM   7261  O  O     . GLU B 1 211 ? 112.980 138.922 123.312 1.00 39.90 ?  211 GLU B O     1 
ATOM   7262  C  CB    . GLU B 1 211 ? 111.783 139.727 126.354 1.00 34.62 ?  211 GLU B CB    1 
ATOM   7263  C  CG    . GLU B 1 211 ? 110.964 139.434 127.594 1.00 35.76 ?  211 GLU B CG    1 
ATOM   7264  C  CD    . GLU B 1 211 ? 110.355 140.680 128.198 1.00 41.33 ?  211 GLU B CD    1 
ATOM   7265  O  OE1   . GLU B 1 211 ? 109.544 141.337 127.514 1.00 43.31 ?  211 GLU B OE1   1 
ATOM   7266  O  OE2   . GLU B 1 211 ? 110.676 141.000 129.361 1.00 41.92 -1 211 GLU B OE2   1 
ATOM   7267  N  N     . ALA B 1 212 ? 111.358 140.480 123.397 1.00 37.07 ?  212 ALA B N     1 
ATOM   7268  C  CA    . ALA B 1 212 ? 111.712 141.091 122.126 1.00 33.37 ?  212 ALA B CA    1 
ATOM   7269  C  C     . ALA B 1 212 ? 112.900 142.030 122.284 1.00 38.75 ?  212 ALA B C     1 
ATOM   7270  O  O     . ALA B 1 212 ? 113.014 142.747 123.282 1.00 40.21 ?  212 ALA B O     1 
ATOM   7271  C  CB    . ALA B 1 212 ? 110.521 141.854 121.546 1.00 37.58 ?  212 ALA B CB    1 
ATOM   7272  N  N     . ILE B 1 213 ? 113.783 142.019 121.290 1.00 35.60 ?  213 ILE B N     1 
ATOM   7273  C  CA    . ILE B 1 213 ? 114.896 142.958 121.201 1.00 35.47 ?  213 ILE B CA    1 
ATOM   7274  C  C     . ILE B 1 213 ? 114.669 143.780 119.939 1.00 35.53 ?  213 ILE B C     1 
ATOM   7275  O  O     . ILE B 1 213 ? 114.945 143.311 118.829 1.00 42.01 ?  213 ILE B O     1 
ATOM   7276  C  CB    . ILE B 1 213 ? 116.257 142.255 121.174 1.00 37.16 ?  213 ILE B CB    1 
ATOM   7277  C  CG1   . ILE B 1 213 ? 116.404 141.316 122.370 1.00 36.22 ?  213 ILE B CG1   1 
ATOM   7278  C  CG2   . ILE B 1 213 ? 117.383 143.276 121.164 1.00 33.09 ?  213 ILE B CG2   1 
ATOM   7279  C  CD1   . ILE B 1 213 ? 117.610 140.411 122.288 1.00 31.45 ?  213 ILE B CD1   1 
ATOM   7280  N  N     . LYS B 1 214 ? 114.160 145.005 120.111 1.00 40.21 ?  214 LYS B N     1 
ATOM   7281  C  CA    . LYS B 1 214 ? 113.873 145.958 119.037 1.00 39.89 ?  214 LYS B CA    1 
ATOM   7282  C  C     . LYS B 1 214 ? 113.197 145.296 117.839 1.00 45.59 ?  214 LYS B C     1 
ATOM   7283  O  O     . LYS B 1 214 ? 113.784 145.208 116.755 1.00 45.66 ?  214 LYS B O     1 
ATOM   7284  C  CB    . LYS B 1 214 ? 115.132 146.734 118.606 1.00 39.26 ?  214 LYS B CB    1 
ATOM   7285  C  CG    . LYS B 1 214 ? 116.390 145.940 118.283 1.00 41.69 ?  214 LYS B CG    1 
ATOM   7286  C  CD    . LYS B 1 214 ? 117.386 146.798 117.526 1.00 40.17 ?  214 LYS B CD    1 
ATOM   7287  C  CE    . LYS B 1 214 ? 118.749 146.138 117.459 1.00 42.26 ?  214 LYS B CE    1 
ATOM   7288  N  NZ    . LYS B 1 214 ? 119.845 147.146 117.469 1.00 44.06 1  214 LYS B NZ    1 
ATOM   7289  N  N     . ASP B 1 215 ? 111.971 144.813 118.044 1.00 52.33 ?  215 ASP B N     1 
ATOM   7290  C  CA    . ASP B 1 215 ? 111.049 144.229 117.075 1.00 53.60 ?  215 ASP B CA    1 
ATOM   7291  C  C     . ASP B 1 215 ? 111.377 142.776 116.744 1.00 54.25 ?  215 ASP B C     1 
ATOM   7292  O  O     . ASP B 1 215 ? 110.657 142.170 115.950 1.00 56.29 ?  215 ASP B O     1 
ATOM   7293  C  CB    . ASP B 1 215 ? 110.962 145.025 115.756 1.00 52.06 ?  215 ASP B CB    1 
ATOM   7294  C  CG    . ASP B 1 215 ? 110.244 146.347 115.922 1.00 59.18 ?  215 ASP B CG    1 
ATOM   7295  O  OD1   . ASP B 1 215 ? 109.015 146.335 116.143 1.00 56.38 ?  215 ASP B OD1   1 
ATOM   7296  O  OD2   . ASP B 1 215 ? 110.909 147.401 115.828 1.00 56.99 -1 215 ASP B OD2   1 
ATOM   7297  N  N     . VAL B 1 216 ? 112.425 142.192 117.314 1.00 48.01 ?  216 VAL B N     1 
ATOM   7298  C  CA    . VAL B 1 216 ? 112.697 140.771 117.127 1.00 43.71 ?  216 VAL B CA    1 
ATOM   7299  C  C     . VAL B 1 216 ? 112.242 140.032 118.380 1.00 48.49 ?  216 VAL B C     1 
ATOM   7300  O  O     . VAL B 1 216 ? 112.957 139.996 119.386 1.00 51.75 ?  216 VAL B O     1 
ATOM   7301  C  CB    . VAL B 1 216 ? 114.185 140.522 116.841 1.00 45.75 ?  216 VAL B CB    1 
ATOM   7302  C  CG1   . VAL B 1 216 ? 114.461 139.033 116.718 1.00 45.61 ?  216 VAL B CG1   1 
ATOM   7303  C  CG2   . VAL B 1 216 ? 114.605 141.255 115.579 1.00 43.69 ?  216 VAL B CG2   1 
ATOM   7304  N  N     . GLU B 1 217 ? 111.054 139.440 118.317 1.00 49.70 ?  217 GLU B N     1 
ATOM   7305  C  CA    . GLU B 1 217 ? 110.436 138.804 119.470 1.00 50.06 ?  217 GLU B CA    1 
ATOM   7306  C  C     . GLU B 1 217 ? 111.162 137.519 119.841 1.00 45.18 ?  217 GLU B C     1 
ATOM   7307  O  O     . GLU B 1 217 ? 111.817 136.887 119.012 1.00 45.39 ?  217 GLU B O     1 
ATOM   7308  C  CB    . GLU B 1 217 ? 108.963 138.503 119.190 1.00 46.34 ?  217 GLU B CB    1 
ATOM   7309  C  CG    . GLU B 1 217 ? 108.312 139.457 118.209 1.00 49.31 ?  217 GLU B CG    1 
ATOM   7310  C  CD    . GLU B 1 217 ? 107.926 140.772 118.854 1.00 52.31 ?  217 GLU B CD    1 
ATOM   7311  O  OE1   . GLU B 1 217 ? 107.340 140.745 119.956 1.00 50.98 ?  217 GLU B OE1   1 
ATOM   7312  O  OE2   . GLU B 1 217 ? 108.209 141.832 118.258 1.00 54.93 -1 217 GLU B OE2   1 
ATOM   7313  N  N     . ASN B 1 218 ? 111.037 137.143 121.115 1.00 42.09 ?  218 ASN B N     1 
ATOM   7314  C  CA    . ASN B 1 218 ? 111.569 135.879 121.631 1.00 43.42 ?  218 ASN B CA    1 
ATOM   7315  C  C     . ASN B 1 218 ? 113.066 135.743 121.363 1.00 46.69 ?  218 ASN B C     1 
ATOM   7316  O  O     . ASN B 1 218 ? 113.554 134.684 120.965 1.00 48.20 ?  218 ASN B O     1 
ATOM   7317  C  CB    . ASN B 1 218 ? 110.800 134.692 121.047 1.00 42.39 ?  218 ASN B CB    1 
ATOM   7318  C  CG    . ASN B 1 218 ? 110.801 133.490 121.963 1.00 46.35 ?  218 ASN B CG    1 
ATOM   7319  O  OD1   . ASN B 1 218 ? 109.939 133.358 122.832 1.00 49.47 ?  218 ASN B OD1   1 
ATOM   7320  N  ND2   . ASN B 1 218 ? 111.770 132.604 121.776 1.00 47.74 ?  218 ASN B ND2   1 
ATOM   7321  N  N     . ALA B 1 219 ? 113.809 136.828 121.592 1.00 35.88 ?  219 ALA B N     1 
ATOM   7322  C  CA    . ALA B 1 219 ? 115.231 136.865 121.281 1.00 33.97 ?  219 ALA B CA    1 
ATOM   7323  C  C     . ALA B 1 219 ? 116.137 136.967 122.500 1.00 37.71 ?  219 ALA B C     1 
ATOM   7324  O  O     . ALA B 1 219 ? 117.350 136.791 122.357 1.00 37.78 ?  219 ALA B O     1 
ATOM   7325  C  CB    . ALA B 1 219 ? 115.540 138.040 120.343 1.00 34.85 ?  219 ALA B CB    1 
ATOM   7326  N  N     . THR B 1 220 ? 115.590 137.244 123.678 1.00 34.96 ?  220 THR B N     1 
ATOM   7327  C  CA    . THR B 1 220 ? 116.396 137.464 124.871 1.00 33.11 ?  220 THR B CA    1 
ATOM   7328  C  C     . THR B 1 220 ? 116.627 136.146 125.600 1.00 35.08 ?  220 THR B C     1 
ATOM   7329  O  O     . THR B 1 220 ? 115.693 135.362 125.791 1.00 33.67 ?  220 THR B O     1 
ATOM   7330  C  CB    . THR B 1 220 ? 115.712 138.471 125.797 1.00 28.35 ?  220 THR B CB    1 
ATOM   7331  O  OG1   . THR B 1 220 ? 115.493 139.697 125.092 1.00 34.03 ?  220 THR B OG1   1 
ATOM   7332  C  CG2   . THR B 1 220 ? 116.571 138.750 127.016 1.00 33.35 ?  220 THR B CG2   1 
ATOM   7333  N  N     . LYS B 1 221 ? 117.878 135.904 125.997 1.00 35.88 ?  221 LYS B N     1 
ATOM   7334  C  CA    . LYS B 1 221 ? 118.215 134.726 126.785 1.00 32.46 ?  221 LYS B CA    1 
ATOM   7335  C  C     . LYS B 1 221 ? 117.802 134.851 128.242 1.00 36.33 ?  221 LYS B C     1 
ATOM   7336  O  O     . LYS B 1 221 ? 117.880 133.862 128.979 1.00 40.45 ?  221 LYS B O     1 
ATOM   7337  C  CB    . LYS B 1 221 ? 119.718 134.447 126.716 1.00 33.12 ?  221 LYS B CB    1 
ATOM   7338  C  CG    . LYS B 1 221 ? 120.401 134.991 125.482 1.00 31.06 ?  221 LYS B CG    1 
ATOM   7339  C  CD    . LYS B 1 221 ? 121.761 134.348 125.296 1.00 36.10 ?  221 LYS B CD    1 
ATOM   7340  C  CE    . LYS B 1 221 ? 121.634 132.905 124.850 1.00 37.98 ?  221 LYS B CE    1 
ATOM   7341  N  NZ    . LYS B 1 221 ? 120.885 132.792 123.574 1.00 37.38 1  221 LYS B NZ    1 
ATOM   7342  N  N     . GLY B 1 222 ? 117.378 136.030 128.675 1.00 34.14 ?  222 GLY B N     1 
ATOM   7343  C  CA    . GLY B 1 222 ? 116.935 136.221 130.036 1.00 32.70 ?  222 GLY B CA    1 
ATOM   7344  C  C     . GLY B 1 222 ? 118.077 136.534 130.981 1.00 31.75 ?  222 GLY B C     1 
ATOM   7345  O  O     . GLY B 1 222 ? 119.189 136.888 130.585 1.00 34.90 ?  222 GLY B O     1 
ATOM   7346  N  N     . VAL B 1 223 ? 117.777 136.401 132.276 1.00 26.93 ?  223 VAL B N     1 
ATOM   7347  C  CA    . VAL B 1 223 ? 118.777 136.678 133.303 1.00 30.96 ?  223 VAL B CA    1 
ATOM   7348  C  C     . VAL B 1 223 ? 119.805 135.569 133.435 1.00 22.59 ?  223 VAL B C     1 
ATOM   7349  O  O     . VAL B 1 223 ? 120.857 135.791 134.039 1.00 25.89 ?  223 VAL B O     1 
ATOM   7350  C  CB    . VAL B 1 223 ? 118.122 136.924 134.675 1.00 27.74 ?  223 VAL B CB    1 
ATOM   7351  C  CG1   . VAL B 1 223 ? 116.991 137.927 134.547 1.00 21.69 ?  223 VAL B CG1   1 
ATOM   7352  C  CG2   . VAL B 1 223 ? 117.624 135.620 135.278 1.00 26.44 ?  223 VAL B CG2   1 
ATOM   7353  N  N     . VAL B 1 224 ? 119.544 134.385 132.876 1.00 26.79 ?  224 VAL B N     1 
ATOM   7354  C  CA    . VAL B 1 224 ? 120.476 133.275 133.043 1.00 26.01 ?  224 VAL B CA    1 
ATOM   7355  C  C     . VAL B 1 224 ? 121.687 133.418 132.123 1.00 31.64 ?  224 VAL B C     1 
ATOM   7356  O  O     . VAL B 1 224 ? 122.795 133.013 132.487 1.00 37.19 ?  224 VAL B O     1 
ATOM   7357  C  CB    . VAL B 1 224 ? 119.752 131.938 132.825 1.00 32.12 ?  224 VAL B CB    1 
ATOM   7358  C  CG1   . VAL B 1 224 ? 120.681 130.775 133.122 1.00 28.23 ?  224 VAL B CG1   1 
ATOM   7359  C  CG2   . VAL B 1 224 ? 118.519 131.867 133.703 1.00 32.42 ?  224 VAL B CG2   1 
ATOM   7360  N  N     . GLY B 1 225 ? 121.515 133.991 130.930 1.00 20.31 ?  225 GLY B N     1 
ATOM   7361  C  CA    . GLY B 1 225 ? 122.673 134.286 130.101 1.00 17.94 ?  225 GLY B CA    1 
ATOM   7362  C  C     . GLY B 1 225 ? 123.598 135.298 130.748 1.00 20.10 ?  225 GLY B C     1 
ATOM   7363  O  O     . GLY B 1 225 ? 124.823 135.132 130.748 1.00 30.82 ?  225 GLY B O     1 
ATOM   7364  N  N     . VAL B 1 226 ? 123.022 136.355 131.324 1.00 18.63 ?  226 VAL B N     1 
ATOM   7365  C  CA    . VAL B 1 226 ? 123.810 137.318 132.083 1.00 21.71 ?  226 VAL B CA    1 
ATOM   7366  C  C     . VAL B 1 226 ? 124.428 136.654 133.303 1.00 18.90 ?  226 VAL B C     1 
ATOM   7367  O  O     . VAL B 1 226 ? 125.542 136.995 133.707 1.00 23.94 ?  226 VAL B O     1 
ATOM   7368  C  CB    . VAL B 1 226 ? 122.940 138.530 132.473 1.00 21.28 ?  226 VAL B CB    1 
ATOM   7369  C  CG1   . VAL B 1 226 ? 123.775 139.580 133.183 1.00 29.21 ?  226 VAL B CG1   1 
ATOM   7370  C  CG2   . VAL B 1 226 ? 122.278 139.114 131.241 1.00 23.54 ?  226 VAL B CG2   1 
ATOM   7371  N  N     . MET B 1 227 ? 123.718 135.702 133.910 1.00 22.86 ?  227 MET B N     1 
ATOM   7372  C  CA    . MET B 1 227 ? 124.265 134.965 135.043 1.00 23.74 ?  227 MET B CA    1 
ATOM   7373  C  C     . MET B 1 227 ? 125.504 134.176 134.645 1.00 25.47 ?  227 MET B C     1 
ATOM   7374  O  O     . MET B 1 227 ? 126.495 134.157 135.378 1.00 28.53 ?  227 MET B O     1 
ATOM   7375  C  CB    . MET B 1 227 ? 123.199 134.031 135.611 1.00 17.04 ?  227 MET B CB    1 
ATOM   7376  C  CG    . MET B 1 227 ? 122.266 134.675 136.610 1.00 18.35 ?  227 MET B CG    1 
ATOM   7377  S  SD    . MET B 1 227 ? 121.253 133.440 137.429 1.00 33.72 ?  227 MET B SD    1 
ATOM   7378  C  CE    . MET B 1 227 ? 122.350 132.962 138.749 1.00 30.40 ?  227 MET B CE    1 
ATOM   7379  N  N     . LYS B 1 228 ? 125.459 133.508 133.491 1.00 23.81 ?  228 LYS B N     1 
ATOM   7380  C  CA    . LYS B 1 228 ? 126.629 132.784 133.000 1.00 19.93 ?  228 LYS B CA    1 
ATOM   7381  C  C     . LYS B 1 228 ? 127.777 133.737 132.693 1.00 20.40 ?  228 LYS B C     1 
ATOM   7382  O  O     . LYS B 1 228 ? 128.940 133.449 133.012 1.00 26.34 ?  228 LYS B O     1 
ATOM   7383  C  CB    . LYS B 1 228 ? 126.267 131.979 131.755 1.00 22.60 ?  228 LYS B CB    1 
ATOM   7384  C  CG    . LYS B 1 228 ? 125.177 130.953 131.967 1.00 24.65 ?  228 LYS B CG    1 
ATOM   7385  C  CD    . LYS B 1 228 ? 125.182 129.930 130.850 1.00 33.66 ?  228 LYS B CD    1 
ATOM   7386  C  CE    . LYS B 1 228 ? 124.215 130.312 129.741 1.00 38.31 ?  228 LYS B CE    1 
ATOM   7387  N  NZ    . LYS B 1 228 ? 122.808 129.970 130.089 1.00 36.29 1  228 LYS B NZ    1 
ATOM   7388  N  N     . LEU B 1 229 ? 127.468 134.873 132.063 1.00 22.70 ?  229 LEU B N     1 
ATOM   7389  C  CA    . LEU B 1 229 ? 128.498 135.867 131.782 1.00 20.74 ?  229 LEU B CA    1 
ATOM   7390  C  C     . LEU B 1 229 ? 129.160 136.343 133.067 1.00 24.12 ?  229 LEU B C     1 
ATOM   7391  O  O     . LEU B 1 229 ? 130.389 136.441 133.149 1.00 29.02 ?  229 LEU B O     1 
ATOM   7392  C  CB    . LEU B 1 229 ? 127.896 137.054 131.032 1.00 23.24 ?  229 LEU B CB    1 
ATOM   7393  C  CG    . LEU B 1 229 ? 127.632 136.934 129.535 1.00 19.83 ?  229 LEU B CG    1 
ATOM   7394  C  CD1   . LEU B 1 229 ? 126.701 138.047 129.102 1.00 24.18 ?  229 LEU B CD1   1 
ATOM   7395  C  CD2   . LEU B 1 229 ? 128.931 136.988 128.758 1.00 19.50 ?  229 LEU B CD2   1 
ATOM   7396  N  N     . LEU B 1 230 ? 128.355 136.635 134.089 1.00 27.00 ?  230 LEU B N     1 
ATOM   7397  C  CA    . LEU B 1 230 ? 128.890 137.120 135.356 1.00 18.28 ?  230 LEU B CA    1 
ATOM   7398  C  C     . LEU B 1 230 ? 129.669 136.034 136.083 1.00 13.47 ?  230 LEU B C     1 
ATOM   7399  O  O     . LEU B 1 230 ? 130.683 136.318 136.724 1.00 32.34 ?  230 LEU B O     1 
ATOM   7400  C  CB    . LEU B 1 230 ? 127.758 137.647 136.235 1.00 19.19 ?  230 LEU B CB    1 
ATOM   7401  C  CG    . LEU B 1 230 ? 127.073 138.923 135.751 1.00 23.66 ?  230 LEU B CG    1 
ATOM   7402  C  CD1   . LEU B 1 230 ? 125.845 139.215 136.595 1.00 28.79 ?  230 LEU B CD1   1 
ATOM   7403  C  CD2   . LEU B 1 230 ? 128.039 140.096 135.773 1.00 24.41 ?  230 LEU B CD2   1 
ATOM   7404  N  N     . ASP B 1 231 ? 129.207 134.786 136.006 1.00 22.77 ?  231 ASP B N     1 
ATOM   7405  C  CA    . ASP B 1 231 ? 129.930 133.691 136.640 1.00 25.27 ?  231 ASP B CA    1 
ATOM   7406  C  C     . ASP B 1 231 ? 131.309 133.518 136.021 1.00 29.78 ?  231 ASP B C     1 
ATOM   7407  O  O     . ASP B 1 231 ? 132.305 133.362 136.737 1.00 33.95 ?  231 ASP B O     1 
ATOM   7408  C  CB    . ASP B 1 231 ? 129.124 132.398 136.532 1.00 24.32 ?  231 ASP B CB    1 
ATOM   7409  C  CG    . ASP B 1 231 ? 129.721 131.268 137.342 1.00 40.21 ?  231 ASP B CG    1 
ATOM   7410  O  OD1   . ASP B 1 231 ? 129.572 131.282 138.581 1.00 44.23 ?  231 ASP B OD1   1 
ATOM   7411  O  OD2   . ASP B 1 231 ? 130.342 130.365 136.743 1.00 39.45 -1 231 ASP B OD2   1 
ATOM   7412  N  N     . ASN B 1 232 ? 131.393 133.567 134.691 1.00 30.21 ?  232 ASN B N     1 
ATOM   7413  C  CA    . ASN B 1 232 ? 132.698 133.478 134.043 1.00 28.77 ?  232 ASN B CA    1 
ATOM   7414  C  C     . ASN B 1 232 ? 133.547 134.716 134.314 1.00 23.15 ?  232 ASN B C     1 
ATOM   7415  O  O     . ASN B 1 232 ? 134.773 134.617 134.435 1.00 31.63 ?  232 ASN B O     1 
ATOM   7416  C  CB    . ASN B 1 232 ? 132.524 133.241 132.548 1.00 26.34 ?  232 ASN B CB    1 
ATOM   7417  C  CG    . ASN B 1 232 ? 132.523 131.771 132.202 1.00 31.22 ?  232 ASN B CG    1 
ATOM   7418  O  OD1   . ASN B 1 232 ? 133.354 131.009 132.693 1.00 36.86 ?  232 ASN B OD1   1 
ATOM   7419  N  ND2   . ASN B 1 232 ? 131.564 131.355 131.400 1.00 35.04 ?  232 ASN B ND2   1 
ATOM   7420  N  N     . ALA B 1 233 ? 132.918 135.887 134.415 1.00 18.47 ?  233 ALA B N     1 
ATOM   7421  C  CA    . ALA B 1 233 ? 133.661 137.098 134.741 1.00 15.26 ?  233 ALA B CA    1 
ATOM   7422  C  C     . ALA B 1 233 ? 134.273 137.012 136.134 1.00 26.94 ?  233 ALA B C     1 
ATOM   7423  O  O     . ALA B 1 233 ? 135.414 137.436 136.348 1.00 30.67 ?  233 ALA B O     1 
ATOM   7424  C  CB    . ALA B 1 233 ? 132.746 138.315 134.627 1.00 20.26 ?  233 ALA B CB    1 
ATOM   7425  N  N     . PHE B 1 234 ? 133.522 136.473 137.098 1.00 30.52 ?  234 PHE B N     1 
ATOM   7426  C  CA    . PHE B 1 234 ? 134.042 136.318 138.451 1.00 24.01 ?  234 PHE B CA    1 
ATOM   7427  C  C     . PHE B 1 234 ? 135.081 135.208 138.528 1.00 24.34 ?  234 PHE B C     1 
ATOM   7428  O  O     . PHE B 1 234 ? 136.026 135.301 139.319 1.00 29.06 ?  234 PHE B O     1 
ATOM   7429  C  CB    . PHE B 1 234 ? 132.900 136.046 139.428 1.00 21.79 ?  234 PHE B CB    1 
ATOM   7430  C  CG    . PHE B 1 234 ? 132.123 137.272 139.801 1.00 21.25 ?  234 PHE B CG    1 
ATOM   7431  C  CD1   . PHE B 1 234 ? 132.755 138.360 140.374 1.00 24.86 ?  234 PHE B CD1   1 
ATOM   7432  C  CD2   . PHE B 1 234 ? 130.761 137.338 139.579 1.00 23.68 ?  234 PHE B CD2   1 
ATOM   7433  C  CE1   . PHE B 1 234 ? 132.040 139.489 140.713 1.00 24.28 ?  234 PHE B CE1   1 
ATOM   7434  C  CE2   . PHE B 1 234 ? 130.045 138.464 139.913 1.00 23.92 ?  234 PHE B CE2   1 
ATOM   7435  C  CZ    . PHE B 1 234 ? 130.684 139.538 140.484 1.00 24.77 ?  234 PHE B CZ    1 
ATOM   7436  N  N     . ARG B 1 235 ? 134.918 134.149 137.731 1.00 31.14 ?  235 ARG B N     1 
ATOM   7437  C  CA    . ARG B 1 235 ? 135.937 133.107 137.673 1.00 25.16 ?  235 ARG B CA    1 
ATOM   7438  C  C     . ARG B 1 235 ? 137.241 133.639 137.094 1.00 31.81 ?  235 ARG B C     1 
ATOM   7439  O  O     . ARG B 1 235 ? 138.326 133.262 137.549 1.00 40.91 ?  235 ARG B O     1 
ATOM   7440  C  CB    . ARG B 1 235 ? 135.430 131.917 136.860 1.00 28.01 ?  235 ARG B CB    1 
ATOM   7441  C  CG    . ARG B 1 235 ? 134.738 130.861 137.701 1.00 38.67 ?  235 ARG B CG    1 
ATOM   7442  C  CD    . ARG B 1 235 ? 134.508 129.571 136.934 1.00 33.71 ?  235 ARG B CD    1 
ATOM   7443  N  NE    . ARG B 1 235 ? 133.150 129.483 136.413 1.00 37.92 ?  235 ARG B NE    1 
ATOM   7444  C  CZ    . ARG B 1 235 ? 132.849 129.369 135.126 1.00 40.90 ?  235 ARG B CZ    1 
ATOM   7445  N  NH1   . ARG B 1 235 ? 133.791 129.308 134.200 1.00 42.51 1  235 ARG B NH1   1 
ATOM   7446  N  NH2   . ARG B 1 235 ? 131.572 129.316 134.762 1.00 36.14 ?  235 ARG B NH2   1 
ATOM   7447  N  N     . TYR B 1 236 ? 137.159 134.504 136.082 1.00 22.81 ?  236 TYR B N     1 
ATOM   7448  C  CA    . TYR B 1 236 ? 138.373 135.065 135.501 1.00 24.99 ?  236 TYR B CA    1 
ATOM   7449  C  C     . TYR B 1 236 ? 139.039 136.044 136.460 1.00 24.34 ?  236 TYR B C     1 
ATOM   7450  O  O     . TYR B 1 236 ? 140.251 135.978 136.687 1.00 26.55 ?  236 TYR B O     1 
ATOM   7451  C  CB    . TYR B 1 236 ? 138.057 135.752 134.175 1.00 24.45 ?  236 TYR B CB    1 
ATOM   7452  C  CG    . TYR B 1 236 ? 139.282 136.300 133.490 1.00 22.08 ?  236 TYR B CG    1 
ATOM   7453  C  CD1   . TYR B 1 236 ? 140.189 135.447 132.881 1.00 18.62 ?  236 TYR B CD1   1 
ATOM   7454  C  CD2   . TYR B 1 236 ? 139.543 137.662 133.464 1.00 18.79 ?  236 TYR B CD2   1 
ATOM   7455  C  CE1   . TYR B 1 236 ? 141.311 135.931 132.259 1.00 23.08 ?  236 TYR B CE1   1 
ATOM   7456  C  CE2   . TYR B 1 236 ? 140.666 138.156 132.842 1.00 13.61 ?  236 TYR B CE2   1 
ATOM   7457  C  CZ    . TYR B 1 236 ? 141.546 137.285 132.242 1.00 20.82 ?  236 TYR B CZ    1 
ATOM   7458  O  OH    . TYR B 1 236 ? 142.668 137.759 131.616 1.00 30.55 ?  236 TYR B OH    1 
ATOM   7459  N  N     . ALA B 1 237 ? 138.260 136.964 137.031 1.00 29.80 ?  237 ALA B N     1 
ATOM   7460  C  CA    . ALA B 1 237 ? 138.782 137.952 137.974 1.00 29.51 ?  237 ALA B CA    1 
ATOM   7461  C  C     . ALA B 1 237 ? 138.861 137.314 139.361 1.00 36.56 ?  237 ALA B C     1 
ATOM   7462  O  O     . ALA B 1 237 ? 138.096 137.617 140.278 1.00 36.35 ?  237 ALA B O     1 
ATOM   7463  C  CB    . ALA B 1 237 ? 137.918 139.204 137.974 1.00 30.47 ?  237 ALA B CB    1 
ATOM   7464  N  N     . ASP B 1 238 ? 139.826 136.403 139.498 1.00 51.59 ?  238 ASP B N     1 
ATOM   7465  C  CA    . ASP B 1 238 ? 139.970 135.583 140.693 1.00 51.32 ?  238 ASP B CA    1 
ATOM   7466  C  C     . ASP B 1 238 ? 140.969 136.161 141.686 1.00 55.56 ?  238 ASP B C     1 
ATOM   7467  O  O     . ASP B 1 238 ? 141.640 135.398 142.395 1.00 57.66 ?  238 ASP B O     1 
ATOM   7468  C  CB    . ASP B 1 238 ? 140.370 134.160 140.303 1.00 49.85 ?  238 ASP B CB    1 
ATOM   7469  C  CG    . ASP B 1 238 ? 139.260 133.160 140.538 1.00 54.08 ?  238 ASP B CG    1 
ATOM   7470  O  OD1   . ASP B 1 238 ? 139.282 132.086 139.903 1.00 53.16 ?  238 ASP B OD1   1 
ATOM   7471  O  OD2   . ASP B 1 238 ? 138.352 133.458 141.341 1.00 53.25 -1 238 ASP B OD2   1 
ATOM   7472  N  N     . GLN B 1 239 ? 141.095 137.489 141.741 1.00 64.45 ?  239 GLN B N     1 
ATOM   7473  C  CA    . GLN B 1 239 ? 141.976 138.169 142.692 1.00 65.28 ?  239 GLN B CA    1 
ATOM   7474  C  C     . GLN B 1 239 ? 143.422 137.696 142.547 1.00 67.16 ?  239 GLN B C     1 
ATOM   7475  O  O     . GLN B 1 239 ? 144.064 137.280 143.515 1.00 64.76 ?  239 GLN B O     1 
ATOM   7476  C  CB    . GLN B 1 239 ? 141.480 137.982 144.128 1.00 64.30 ?  239 GLN B CB    1 
ATOM   7477  C  CG    . GLN B 1 239 ? 140.020 138.342 144.329 1.00 63.46 ?  239 GLN B CG    1 
ATOM   7478  C  CD    . GLN B 1 239 ? 139.510 137.962 145.701 1.00 66.62 ?  239 GLN B CD    1 
ATOM   7479  O  OE1   . GLN B 1 239 ? 138.331 137.657 145.875 1.00 64.72 ?  239 GLN B OE1   1 
ATOM   7480  N  NE2   . GLN B 1 239 ? 140.398 137.979 146.688 1.00 66.44 ?  239 GLN B NE2   1 
ATOM   7481  N  N     . MET B 1 240 ? 143.929 137.757 141.314 1.00 68.36 ?  240 MET B N     1 
ATOM   7482  C  CA    . MET B 1 240 ? 145.301 137.361 140.994 1.00 67.11 ?  240 MET B CA    1 
ATOM   7483  C  C     . MET B 1 240 ? 145.592 135.921 141.407 1.00 67.96 ?  240 MET B C     1 
ATOM   7484  O  O     . MET B 1 240 ? 146.704 135.598 141.831 1.00 68.29 ?  240 MET B O     1 
ATOM   7485  C  CB    . MET B 1 240 ? 146.319 138.312 141.632 1.00 67.19 ?  240 MET B CB    1 
ATOM   7486  C  CG    . MET B 1 240 ? 146.331 139.710 141.042 1.00 68.64 ?  240 MET B CG    1 
ATOM   7487  S  SD    . MET B 1 240 ? 144.693 140.346 140.646 1.00 76.69 ?  240 MET B SD    1 
ATOM   7488  C  CE    . MET B 1 240 ? 145.067 142.084 140.446 1.00 66.55 ?  240 MET B CE    1 
ATOM   7489  N  N     . GLY B 1 241 ? 144.596 135.046 141.292 1.00 70.46 ?  241 GLY B N     1 
ATOM   7490  C  CA    . GLY B 1 241 ? 144.778 133.657 141.660 1.00 69.56 ?  241 GLY B CA    1 
ATOM   7491  C  C     . GLY B 1 241 ? 144.969 133.402 143.136 1.00 72.28 ?  241 GLY B C     1 
ATOM   7492  O  O     . GLY B 1 241 ? 145.451 132.327 143.506 1.00 72.91 ?  241 GLY B O     1 
ATOM   7493  N  N     . GLN B 1 242 ? 144.610 134.355 143.995 1.00 73.68 ?  242 GLN B N     1 
ATOM   7494  C  CA    . GLN B 1 242 ? 144.785 134.202 145.435 1.00 73.00 ?  242 GLN B CA    1 
ATOM   7495  C  C     . GLN B 1 242 ? 143.531 133.633 146.093 1.00 73.64 ?  242 GLN B C     1 
ATOM   7496  O  O     . GLN B 1 242 ? 143.575 132.572 146.725 1.00 71.98 ?  242 GLN B O     1 
ATOM   7497  C  CB    . GLN B 1 242 ? 145.156 135.549 146.066 1.00 71.35 ?  242 GLN B CB    1 
ATOM   7498  C  CG    . GLN B 1 242 ? 146.511 136.090 145.636 1.00 73.43 ?  242 GLN B CG    1 
ATOM   7499  C  CD    . GLN B 1 242 ? 147.039 137.156 146.577 1.00 75.32 ?  242 GLN B CD    1 
ATOM   7500  O  OE1   . GLN B 1 242 ? 146.483 137.384 147.651 1.00 75.18 ?  242 GLN B OE1   1 
ATOM   7501  N  NE2   . GLN B 1 242 ? 148.121 137.815 146.178 1.00 72.12 ?  242 GLN B NE2   1 
ATOM   7502  N  N     . ARG B 1 243 ? 142.406 134.329 145.948 1.00 68.25 ?  243 ARG B N     1 
ATOM   7503  C  CA    . ARG B 1 243 ? 141.136 133.920 146.526 1.00 66.93 ?  243 ARG B CA    1 
ATOM   7504  C  C     . ARG B 1 243 ? 140.076 133.917 145.437 1.00 66.24 ?  243 ARG B C     1 
ATOM   7505  O  O     . ARG B 1 243 ? 140.036 134.821 144.598 1.00 65.42 ?  243 ARG B O     1 
ATOM   7506  C  CB    . ARG B 1 243 ? 140.730 134.853 147.675 1.00 66.32 ?  243 ARG B CB    1 
ATOM   7507  C  CG    . ARG B 1 243 ? 139.391 134.536 148.318 1.00 66.93 ?  243 ARG B CG    1 
ATOM   7508  C  CD    . ARG B 1 243 ? 138.871 135.735 149.098 1.00 67.50 ?  243 ARG B CD    1 
ATOM   7509  N  NE    . ARG B 1 243 ? 138.105 136.650 148.261 1.00 69.40 ?  243 ARG B NE    1 
ATOM   7510  C  CZ    . ARG B 1 243 ? 136.925 137.160 148.590 1.00 69.52 ?  243 ARG B CZ    1 
ATOM   7511  N  NH1   . ARG B 1 243 ? 136.344 136.868 149.742 1.00 66.61 1  243 ARG B NH1   1 
ATOM   7512  N  NH2   . ARG B 1 243 ? 136.315 137.984 147.744 1.00 64.05 ?  243 ARG B NH2   1 
ATOM   7513  N  N     . GLN B 1 244 ? 139.224 132.894 145.453 1.00 64.22 ?  244 GLN B N     1 
ATOM   7514  C  CA    . GLN B 1 244 ? 138.238 132.718 144.395 1.00 63.23 ?  244 GLN B CA    1 
ATOM   7515  C  C     . GLN B 1 244 ? 137.286 133.906 144.332 1.00 63.95 ?  244 GLN B C     1 
ATOM   7516  O  O     . GLN B 1 244 ? 136.791 134.378 145.360 1.00 61.87 ?  244 GLN B O     1 
ATOM   7517  C  CB    . GLN B 1 244 ? 137.456 131.423 144.615 1.00 61.27 ?  244 GLN B CB    1 
ATOM   7518  C  CG    . GLN B 1 244 ? 138.321 130.172 144.609 1.00 62.33 ?  244 GLN B CG    1 
ATOM   7519  C  CD    . GLN B 1 244 ? 137.501 128.897 144.656 1.00 62.46 ?  244 GLN B CD    1 
ATOM   7520  O  OE1   . GLN B 1 244 ? 136.494 128.817 145.359 1.00 60.44 ?  244 GLN B OE1   1 
ATOM   7521  N  NE2   . GLN B 1 244 ? 137.930 127.890 143.904 1.00 60.00 ?  244 GLN B NE2   1 
ATOM   7522  N  N     . GLY B 1 245 ? 137.039 134.391 143.116 1.00 49.21 ?  245 GLY B N     1 
ATOM   7523  C  CA    . GLY B 1 245 ? 136.139 135.508 142.904 1.00 44.50 ?  245 GLY B CA    1 
ATOM   7524  C  C     . GLY B 1 245 ? 134.710 135.189 143.287 1.00 44.34 ?  245 GLY B C     1 
ATOM   7525  O  O     . GLY B 1 245 ? 134.115 134.242 142.764 1.00 41.39 ?  245 GLY B O     1 
ATOM   7526  N  N     . SER B 1 246 ? 134.145 135.976 144.197 1.00 39.46 ?  246 SER B N     1 
ATOM   7527  C  CA    . SER B 1 246 ? 132.815 135.734 144.734 1.00 33.42 ?  246 SER B CA    1 
ATOM   7528  C  C     . SER B 1 246 ? 131.877 136.852 144.303 1.00 30.07 ?  246 SER B C     1 
ATOM   7529  O  O     . SER B 1 246 ? 132.190 138.034 144.473 1.00 23.53 ?  246 SER B O     1 
ATOM   7530  C  CB    . SER B 1 246 ? 132.852 135.633 146.260 1.00 31.88 ?  246 SER B CB    1 
ATOM   7531  O  OG    . SER B 1 246 ? 133.487 136.764 146.831 1.00 38.37 ?  246 SER B OG    1 
ATOM   7532  N  N     . GLY B 1 247 ? 130.731 136.470 143.745 1.00 26.03 ?  247 GLY B N     1 
ATOM   7533  C  CA    . GLY B 1 247 ? 129.732 137.433 143.345 1.00 10.12 ?  247 GLY B CA    1 
ATOM   7534  C  C     . GLY B 1 247 ? 128.346 136.916 143.665 1.00 12.49 ?  247 GLY B C     1 
ATOM   7535  O  O     . GLY B 1 247 ? 128.136 135.722 143.879 1.00 22.70 ?  247 GLY B O     1 
ATOM   7536  N  N     . ALA B 1 248 ? 127.397 137.845 143.698 1.00 17.14 ?  248 ALA B N     1 
ATOM   7537  C  CA    . ALA B 1 248 ? 126.012 137.524 143.996 1.00 17.75 ?  248 ALA B CA    1 
ATOM   7538  C  C     . ALA B 1 248 ? 125.106 138.155 142.952 1.00 16.83 ?  248 ALA B C     1 
ATOM   7539  O  O     . ALA B 1 248 ? 125.389 139.235 142.428 1.00 23.25 ?  248 ALA B O     1 
ATOM   7540  C  CB    . ALA B 1 248 ? 125.606 138.003 145.396 1.00 4.65  ?  248 ALA B CB    1 
ATOM   7541  N  N     . ALA B 1 249 ? 124.015 137.461 142.648 1.00 16.18 ?  249 ALA B N     1 
ATOM   7542  C  CA    . ALA B 1 249 ? 122.993 137.952 141.737 1.00 14.30 ?  249 ALA B CA    1 
ATOM   7543  C  C     . ALA B 1 249 ? 121.657 137.949 142.462 1.00 16.37 ?  249 ALA B C     1 
ATOM   7544  O  O     . ALA B 1 249 ? 121.314 136.973 143.134 1.00 24.63 ?  249 ALA B O     1 
ATOM   7545  C  CB    . ALA B 1 249 ? 122.918 137.097 140.472 1.00 11.62 ?  249 ALA B CB    1 
ATOM   7546  N  N     . TYR B 1 250 ? 120.912 139.039 142.332 1.00 17.18 ?  250 TYR B N     1 
ATOM   7547  C  CA    . TYR B 1 250 ? 119.620 139.174 142.982 1.00 5.89  ?  250 TYR B CA    1 
ATOM   7548  C  C     . TYR B 1 250 ? 118.533 139.328 141.933 1.00 7.44  ?  250 TYR B C     1 
ATOM   7549  O  O     . TYR B 1 250 ? 118.697 140.063 140.955 1.00 21.34 ?  250 TYR B O     1 
ATOM   7550  C  CB    . TYR B 1 250 ? 119.600 140.368 143.938 1.00 12.37 ?  250 TYR B CB    1 
ATOM   7551  C  CG    . TYR B 1 250 ? 120.122 140.047 145.317 1.00 15.54 ?  250 TYR B CG    1 
ATOM   7552  C  CD1   . TYR B 1 250 ? 121.478 139.865 145.541 1.00 8.40  ?  250 TYR B CD1   1 
ATOM   7553  C  CD2   . TYR B 1 250 ? 119.257 139.915 146.394 1.00 12.52 ?  250 TYR B CD2   1 
ATOM   7554  C  CE1   . TYR B 1 250 ? 121.959 139.565 146.796 1.00 1.20  ?  250 TYR B CE1   1 
ATOM   7555  C  CE2   . TYR B 1 250 ? 119.730 139.615 147.655 1.00 7.97  ?  250 TYR B CE2   1 
ATOM   7556  C  CZ    . TYR B 1 250 ? 121.083 139.443 147.848 1.00 11.67 ?  250 TYR B CZ    1 
ATOM   7557  O  OH    . TYR B 1 250 ? 121.562 139.149 149.102 1.00 21.15 ?  250 TYR B OH    1 
ATOM   7558  N  N     . LEU B 1 251 ? 117.425 138.624 142.140 1.00 14.84 ?  251 LEU B N     1 
ATOM   7559  C  CA    . LEU B 1 251 ? 116.276 138.711 141.256 1.00 15.67 ?  251 LEU B CA    1 
ATOM   7560  C  C     . LEU B 1 251 ? 115.012 138.819 142.090 1.00 10.15 ?  251 LEU B C     1 
ATOM   7561  O  O     . LEU B 1 251 ? 114.876 138.142 143.112 1.00 19.07 ?  251 LEU B O     1 
ATOM   7562  C  CB    . LEU B 1 251 ? 116.184 137.494 140.329 1.00 14.63 ?  251 LEU B CB    1 
ATOM   7563  C  CG    . LEU B 1 251 ? 115.323 137.679 139.082 1.00 14.48 ?  251 LEU B CG    1 
ATOM   7564  C  CD1   . LEU B 1 251 ? 115.996 138.610 138.097 1.00 6.94  ?  251 LEU B CD1   1 
ATOM   7565  C  CD2   . LEU B 1 251 ? 115.021 136.342 138.440 1.00 10.11 ?  251 LEU B CD2   1 
ATOM   7566  N  N     . ASN B 1 252 ? 114.095 139.675 141.652 1.00 12.31 ?  252 ASN B N     1 
ATOM   7567  C  CA    . ASN B 1 252 ? 112.795 139.766 142.299 1.00 10.56 ?  252 ASN B CA    1 
ATOM   7568  C  C     . ASN B 1 252 ? 112.008 138.482 142.080 1.00 17.18 ?  252 ASN B C     1 
ATOM   7569  O  O     . ASN B 1 252 ? 112.090 137.855 141.021 1.00 27.97 ?  252 ASN B O     1 
ATOM   7570  C  CB    . ASN B 1 252 ? 112.016 140.963 141.759 1.00 13.51 ?  252 ASN B CB    1 
ATOM   7571  C  CG    . ASN B 1 252 ? 111.037 141.521 142.769 1.00 20.90 ?  252 ASN B CG    1 
ATOM   7572  O  OD1   . ASN B 1 252 ? 110.005 140.914 143.051 1.00 31.96 ?  252 ASN B OD1   1 
ATOM   7573  N  ND2   . ASN B 1 252 ? 111.358 142.682 143.323 1.00 16.81 ?  252 ASN B ND2   1 
ATOM   7574  N  N     . ILE B 1 253 ? 111.240 138.084 143.097 1.00 12.04 ?  253 ILE B N     1 
ATOM   7575  C  CA    . ILE B 1 253 ? 110.450 136.865 142.988 1.00 17.59 ?  253 ILE B CA    1 
ATOM   7576  C  C     . ILE B 1 253 ? 109.338 137.000 141.955 1.00 23.32 ?  253 ILE B C     1 
ATOM   7577  O  O     . ILE B 1 253 ? 108.839 135.988 141.451 1.00 24.82 ?  253 ILE B O     1 
ATOM   7578  C  CB    . ILE B 1 253 ? 109.884 136.472 144.366 1.00 20.99 ?  253 ILE B CB    1 
ATOM   7579  C  CG1   . ILE B 1 253 ? 109.537 134.982 144.394 1.00 16.36 ?  253 ILE B CG1   1 
ATOM   7580  C  CG2   . ILE B 1 253 ? 108.681 137.330 144.724 1.00 14.57 ?  253 ILE B CG2   1 
ATOM   7581  C  CD1   . ILE B 1 253 ? 109.720 134.339 145.740 1.00 18.96 ?  253 ILE B CD1   1 
ATOM   7582  N  N     . PHE B 1 254 ? 108.940 138.224 141.614 1.00 30.33 ?  254 PHE B N     1 
ATOM   7583  C  CA    . PHE B 1 254 ? 107.933 138.455 140.589 1.00 18.12 ?  254 PHE B CA    1 
ATOM   7584  C  C     . PHE B 1 254 ? 108.533 138.578 139.196 1.00 20.80 ?  254 PHE B C     1 
ATOM   7585  O  O     . PHE B 1 254 ? 107.791 138.776 138.229 1.00 27.34 ?  254 PHE B O     1 
ATOM   7586  C  CB    . PHE B 1 254 ? 107.117 139.706 140.924 1.00 21.69 ?  254 PHE B CB    1 
ATOM   7587  C  CG    . PHE B 1 254 ? 106.067 139.477 141.974 1.00 26.47 ?  254 PHE B CG    1 
ATOM   7588  C  CD1   . PHE B 1 254 ? 104.998 138.636 141.725 1.00 25.87 ?  254 PHE B CD1   1 
ATOM   7589  C  CD2   . PHE B 1 254 ? 106.155 140.092 143.209 1.00 25.47 ?  254 PHE B CD2   1 
ATOM   7590  C  CE1   . PHE B 1 254 ? 104.032 138.420 142.685 1.00 29.44 ?  254 PHE B CE1   1 
ATOM   7591  C  CE2   . PHE B 1 254 ? 105.191 139.878 144.174 1.00 26.38 ?  254 PHE B CE2   1 
ATOM   7592  C  CZ    . PHE B 1 254 ? 104.129 139.041 143.910 1.00 25.35 ?  254 PHE B CZ    1 
ATOM   7593  N  N     . HIS B 1 255 ? 109.852 138.473 139.075 1.00 27.15 ?  255 HIS B N     1 
ATOM   7594  C  CA    . HIS B 1 255 ? 110.485 138.395 137.769 1.00 20.76 ?  255 HIS B CA    1 
ATOM   7595  C  C     . HIS B 1 255 ? 110.105 137.090 137.086 1.00 23.58 ?  255 HIS B C     1 
ATOM   7596  O  O     . HIS B 1 255 ? 109.974 136.046 137.730 1.00 30.47 ?  255 HIS B O     1 
ATOM   7597  C  CB    . HIS B 1 255 ? 112.002 138.499 137.909 1.00 17.98 ?  255 HIS B CB    1 
ATOM   7598  C  CG    . HIS B 1 255 ? 112.710 138.858 136.639 1.00 22.26 ?  255 HIS B CG    1 
ATOM   7599  N  ND1   . HIS B 1 255 ? 112.914 137.955 135.619 1.00 14.82 ?  255 HIS B ND1   1 
ATOM   7600  C  CD2   . HIS B 1 255 ? 113.275 140.019 136.232 1.00 20.06 ?  255 HIS B CD2   1 
ATOM   7601  C  CE1   . HIS B 1 255 ? 113.567 138.547 134.635 1.00 12.90 ?  255 HIS B CE1   1 
ATOM   7602  N  NE2   . HIS B 1 255 ? 113.800 139.798 134.982 1.00 12.09 ?  255 HIS B NE2   1 
ATOM   7603  N  N     . ARG B 1 256 ? 109.928 137.159 135.768 1.00 26.39 ?  256 ARG B N     1 
ATOM   7604  C  CA    . ARG B 1 256 ? 109.495 135.991 135.012 1.00 22.29 ?  256 ARG B CA    1 
ATOM   7605  C  C     . ARG B 1 256 ? 110.524 134.869 135.078 1.00 24.96 ?  256 ARG B C     1 
ATOM   7606  O  O     . ARG B 1 256 ? 110.165 133.688 135.126 1.00 32.64 ?  256 ARG B O     1 
ATOM   7607  C  CB    . ARG B 1 256 ? 109.223 136.394 133.567 1.00 26.13 ?  256 ARG B CB    1 
ATOM   7608  C  CG    . ARG B 1 256 ? 108.059 135.683 132.939 1.00 35.87 ?  256 ARG B CG    1 
ATOM   7609  C  CD    . ARG B 1 256 ? 108.449 134.310 132.451 1.00 31.95 ?  256 ARG B CD    1 
ATOM   7610  N  NE    . ARG B 1 256 ? 109.822 134.243 131.968 1.00 30.96 ?  256 ARG B NE    1 
ATOM   7611  C  CZ    . ARG B 1 256 ? 110.398 133.134 131.527 1.00 33.29 ?  256 ARG B CZ    1 
ATOM   7612  N  NH1   . ARG B 1 256 ? 109.750 131.980 131.505 1.00 30.55 1  256 ARG B NH1   1 
ATOM   7613  N  NH2   . ARG B 1 256 ? 111.656 133.182 131.102 1.00 34.33 ?  256 ARG B NH2   1 
ATOM   7614  N  N     . ASP B 1 257 ? 111.806 135.218 135.088 1.00 26.22 ?  257 ASP B N     1 
ATOM   7615  C  CA    . ASP B 1 257 ? 112.887 134.244 135.099 1.00 21.49 ?  257 ASP B CA    1 
ATOM   7616  C  C     . ASP B 1 257 ? 113.206 133.712 136.487 1.00 22.72 ?  257 ASP B C     1 
ATOM   7617  O  O     . ASP B 1 257 ? 114.302 133.179 136.679 1.00 27.09 ?  257 ASP B O     1 
ATOM   7618  C  CB    . ASP B 1 257 ? 114.148 134.853 134.487 1.00 25.70 ?  257 ASP B CB    1 
ATOM   7619  C  CG    . ASP B 1 257 ? 114.130 134.833 132.979 1.00 32.76 ?  257 ASP B CG    1 
ATOM   7620  O  OD1   . ASP B 1 257 ? 113.254 134.159 132.400 1.00 31.80 ?  257 ASP B OD1   1 
ATOM   7621  O  OD2   . ASP B 1 257 ? 114.991 135.496 132.372 1.00 36.44 -1 257 ASP B OD2   1 
ATOM   7622  N  N     . ILE B 1 258 ? 112.293 133.839 137.452 1.00 26.47 ?  258 ILE B N     1 
ATOM   7623  C  CA    . ILE B 1 258 ? 112.610 133.449 138.823 1.00 23.00 ?  258 ILE B CA    1 
ATOM   7624  C  C     . ILE B 1 258 ? 112.860 131.949 138.916 1.00 22.75 ?  258 ILE B C     1 
ATOM   7625  O  O     . ILE B 1 258 ? 113.751 131.503 139.646 1.00 34.15 ?  258 ILE B O     1 
ATOM   7626  C  CB    . ILE B 1 258 ? 111.500 133.915 139.785 1.00 27.55 ?  258 ILE B CB    1 
ATOM   7627  C  CG1   . ILE B 1 258 ? 111.880 133.601 141.235 1.00 24.90 ?  258 ILE B CG1   1 
ATOM   7628  C  CG2   . ILE B 1 258 ? 110.155 133.304 139.416 1.00 19.92 ?  258 ILE B CG2   1 
ATOM   7629  C  CD1   . ILE B 1 258 ? 113.169 134.255 141.678 1.00 17.22 ?  258 ILE B CD1   1 
ATOM   7630  N  N     . ASN B 1 259 ? 112.097 131.145 138.172 1.00 31.64 ?  259 ASN B N     1 
ATOM   7631  C  CA    . ASN B 1 259 ? 112.295 129.700 138.222 1.00 28.34 ?  259 ASN B CA    1 
ATOM   7632  C  C     . ASN B 1 259 ? 113.600 129.298 137.544 1.00 28.53 ?  259 ASN B C     1 
ATOM   7633  O  O     . ASN B 1 259 ? 114.326 128.437 138.048 1.00 30.84 ?  259 ASN B O     1 
ATOM   7634  C  CB    . ASN B 1 259 ? 111.106 128.982 137.587 1.00 29.00 ?  259 ASN B CB    1 
ATOM   7635  C  CG    . ASN B 1 259 ? 109.918 128.894 138.520 1.00 33.29 ?  259 ASN B CG    1 
ATOM   7636  O  OD1   . ASN B 1 259 ? 110.013 128.337 139.613 1.00 34.36 ?  259 ASN B OD1   1 
ATOM   7637  N  ND2   . ASN B 1 259 ? 108.789 129.446 138.096 1.00 34.97 ?  259 ASN B ND2   1 
ATOM   7638  N  N     . ASP B 1 260 ? 113.915 129.917 136.404 1.00 31.47 ?  260 ASP B N     1 
ATOM   7639  C  CA    . ASP B 1 260 ? 115.220 129.708 135.785 1.00 24.64 ?  260 ASP B CA    1 
ATOM   7640  C  C     . ASP B 1 260 ? 116.337 130.198 136.696 1.00 28.75 ?  260 ASP B C     1 
ATOM   7641  O  O     . ASP B 1 260 ? 117.402 129.575 136.779 1.00 33.75 ?  260 ASP B O     1 
ATOM   7642  C  CB    . ASP B 1 260 ? 115.278 130.421 134.436 1.00 27.87 ?  260 ASP B CB    1 
ATOM   7643  C  CG    . ASP B 1 260 ? 114.199 129.955 133.483 1.00 40.56 ?  260 ASP B CG    1 
ATOM   7644  O  OD1   . ASP B 1 260 ? 114.062 130.559 132.398 1.00 37.76 ?  260 ASP B OD1   1 
ATOM   7645  O  OD2   . ASP B 1 260 ? 113.486 128.985 133.818 1.00 42.90 -1 260 ASP B OD2   1 
ATOM   7646  N  N     . PHE B 1 261 ? 116.112 131.324 137.375 1.00 33.42 ?  261 PHE B N     1 
ATOM   7647  C  CA    . PHE B 1 261 ? 117.085 131.853 138.325 1.00 20.73 ?  261 PHE B CA    1 
ATOM   7648  C  C     . PHE B 1 261 ? 117.380 130.846 139.430 1.00 23.47 ?  261 PHE B C     1 
ATOM   7649  O  O     . PHE B 1 261 ? 118.537 130.657 139.819 1.00 26.79 ?  261 PHE B O     1 
ATOM   7650  C  CB    . PHE B 1 261 ? 116.548 133.160 138.908 1.00 14.21 ?  261 PHE B CB    1 
ATOM   7651  C  CG    . PHE B 1 261 ? 117.513 133.888 139.793 1.00 27.64 ?  261 PHE B CG    1 
ATOM   7652  C  CD1   . PHE B 1 261 ? 118.558 134.611 139.250 1.00 22.13 ?  261 PHE B CD1   1 
ATOM   7653  C  CD2   . PHE B 1 261 ? 117.351 133.884 141.167 1.00 21.15 ?  261 PHE B CD2   1 
ATOM   7654  C  CE1   . PHE B 1 261 ? 119.437 135.293 140.059 1.00 14.29 ?  261 PHE B CE1   1 
ATOM   7655  C  CE2   . PHE B 1 261 ? 118.228 134.567 141.980 1.00 12.58 ?  261 PHE B CE2   1 
ATOM   7656  C  CZ    . PHE B 1 261 ? 119.271 135.271 141.424 1.00 17.93 ?  261 PHE B CZ    1 
ATOM   7657  N  N     . LEU B 1 262 ? 116.340 130.189 139.947 1.00 31.41 ?  262 LEU B N     1 
ATOM   7658  C  CA    . LEU B 1 262 ? 116.527 129.217 141.017 1.00 25.47 ?  262 LEU B CA    1 
ATOM   7659  C  C     . LEU B 1 262 ? 117.115 127.908 140.508 1.00 30.04 ?  262 LEU B C     1 
ATOM   7660  O  O     . LEU B 1 262 ? 117.847 127.236 141.242 1.00 32.42 ?  262 LEU B O     1 
ATOM   7661  C  CB    . LEU B 1 262 ? 115.199 128.959 141.722 1.00 32.20 ?  262 LEU B CB    1 
ATOM   7662  C  CG    . LEU B 1 262 ? 114.529 130.180 142.345 1.00 22.35 ?  262 LEU B CG    1 
ATOM   7663  C  CD1   . LEU B 1 262 ? 113.176 129.808 142.920 1.00 29.16 ?  262 LEU B CD1   1 
ATOM   7664  C  CD2   . LEU B 1 262 ? 115.427 130.783 143.403 1.00 22.81 ?  262 LEU B CD2   1 
ATOM   7665  N  N     . ASP B 1 263 ? 116.812 127.528 139.266 1.00 42.45 ?  263 ASP B N     1 
ATOM   7666  C  CA    . ASP B 1 263 ? 117.307 126.269 138.721 1.00 31.66 ?  263 ASP B CA    1 
ATOM   7667  C  C     . ASP B 1 263 ? 118.815 126.262 138.521 1.00 34.41 ?  263 ASP B C     1 
ATOM   7668  O  O     . ASP B 1 263 ? 119.387 125.187 138.316 1.00 47.73 ?  263 ASP B O     1 
ATOM   7669  C  CB    . ASP B 1 263 ? 116.616 125.958 137.393 1.00 37.05 ?  263 ASP B CB    1 
ATOM   7670  C  CG    . ASP B 1 263 ? 115.151 125.619 137.565 1.00 46.24 ?  263 ASP B CG    1 
ATOM   7671  O  OD1   . ASP B 1 263 ? 114.721 125.399 138.715 1.00 42.48 ?  263 ASP B OD1   1 
ATOM   7672  O  OD2   . ASP B 1 263 ? 114.428 125.574 136.547 1.00 47.80 -1 263 ASP B OD2   1 
ATOM   7673  N  N     . THR B 1 264 ? 119.470 127.422 138.566 1.00 38.94 ?  264 THR B N     1 
ATOM   7674  C  CA    . THR B 1 264 ? 120.920 127.473 138.443 1.00 37.20 ?  264 THR B CA    1 
ATOM   7675  C  C     . THR B 1 264 ? 121.637 126.893 139.655 1.00 40.49 ?  264 THR B C     1 
ATOM   7676  O  O     . THR B 1 264 ? 122.843 126.644 139.576 1.00 41.51 ?  264 THR B O     1 
ATOM   7677  C  CB    . THR B 1 264 ? 121.380 128.916 138.219 1.00 34.86 ?  264 THR B CB    1 
ATOM   7678  O  OG1   . THR B 1 264 ? 120.981 129.727 139.331 1.00 37.84 ?  264 THR B OG1   1 
ATOM   7679  C  CG2   . THR B 1 264 ? 120.769 129.478 136.949 1.00 35.27 ?  264 THR B CG2   1 
ATOM   7680  N  N     . LYS B 1 265 ? 120.931 126.668 140.762 1.00 34.45 ?  265 LYS B N     1 
ATOM   7681  C  CA    . LYS B 1 265 ? 121.532 126.147 141.981 1.00 36.43 ?  265 LYS B CA    1 
ATOM   7682  C  C     . LYS B 1 265 ? 121.147 124.705 142.277 1.00 41.95 ?  265 LYS B C     1 
ATOM   7683  O  O     . LYS B 1 265 ? 121.575 124.166 143.303 1.00 44.94 ?  265 LYS B O     1 
ATOM   7684  C  CB    . LYS B 1 265 ? 121.158 127.034 143.172 1.00 35.53 ?  265 LYS B CB    1 
ATOM   7685  C  CG    . LYS B 1 265 ? 121.925 128.335 143.225 1.00 38.41 ?  265 LYS B CG    1 
ATOM   7686  C  CD    . LYS B 1 265 ? 123.412 128.088 143.095 1.00 42.43 ?  265 LYS B CD    1 
ATOM   7687  C  CE    . LYS B 1 265 ? 124.174 129.388 143.021 1.00 39.18 ?  265 LYS B CE    1 
ATOM   7688  N  NZ    . LYS B 1 265 ? 125.602 129.164 142.678 1.00 43.31 1  265 LYS B NZ    1 
ATOM   7689  N  N     . LYS B 1 266 ? 120.354 124.069 141.422 1.00 46.48 ?  266 LYS B N     1 
ATOM   7690  C  CA    . LYS B 1 266 ? 120.012 122.671 141.630 1.00 48.96 ?  266 LYS B CA    1 
ATOM   7691  C  C     . LYS B 1 266 ? 121.229 121.783 141.397 1.00 55.08 ?  266 LYS B C     1 
ATOM   7692  O  O     . LYS B 1 266 ? 122.095 122.081 140.570 1.00 56.31 ?  266 LYS B O     1 
ATOM   7693  C  CB    . LYS B 1 266 ? 118.870 122.254 140.706 1.00 48.89 ?  266 LYS B CB    1 
ATOM   7694  C  CG    . LYS B 1 266 ? 117.504 122.737 141.155 1.00 50.80 ?  266 LYS B CG    1 
ATOM   7695  C  CD    . LYS B 1 266 ? 116.431 122.364 140.146 1.00 51.90 ?  266 LYS B CD    1 
ATOM   7696  C  CE    . LYS B 1 266 ? 115.042 122.681 140.675 1.00 50.94 ?  266 LYS B CE    1 
ATOM   7697  N  NZ    . LYS B 1 266 ? 114.002 122.543 139.617 1.00 50.51 1  266 LYS B NZ    1 
ATOM   7698  N  N     . ILE B 1 267 ? 121.294 120.683 142.149 1.00 58.24 ?  267 ILE B N     1 
ATOM   7699  C  CA    . ILE B 1 267 ? 122.410 119.754 142.003 1.00 60.88 ?  267 ILE B CA    1 
ATOM   7700  C  C     . ILE B 1 267 ? 122.369 119.073 140.642 1.00 62.41 ?  267 ILE B C     1 
ATOM   7701  O  O     . ILE B 1 267 ? 123.413 118.693 140.097 1.00 61.60 ?  267 ILE B O     1 
ATOM   7702  C  CB    . ILE B 1 267 ? 122.412 118.722 143.146 1.00 62.07 ?  267 ILE B CB    1 
ATOM   7703  C  CG1   . ILE B 1 267 ? 122.666 119.402 144.494 1.00 61.89 ?  267 ILE B CG1   1 
ATOM   7704  C  CG2   . ILE B 1 267 ? 123.456 117.648 142.893 1.00 58.67 ?  267 ILE B CG2   1 
ATOM   7705  C  CD1   . ILE B 1 267 ? 121.412 119.640 145.311 1.00 60.76 ?  267 ILE B CD1   1 
ATOM   7706  N  N     . SER B 1 268 ? 121.178 118.907 140.072 1.00 63.05 ?  268 SER B N     1 
ATOM   7707  C  CA    . SER B 1 268 ? 121.002 118.284 138.769 1.00 64.65 ?  268 SER B CA    1 
ATOM   7708  C  C     . SER B 1 268 ? 121.031 119.288 137.624 1.00 65.97 ?  268 SER B C     1 
ATOM   7709  O  O     . SER B 1 268 ? 120.659 118.936 136.500 1.00 65.58 ?  268 SER B O     1 
ATOM   7710  C  CB    . SER B 1 268 ? 119.685 117.504 138.736 1.00 66.48 ?  268 SER B CB    1 
ATOM   7711  O  OG    . SER B 1 268 ? 118.598 118.334 139.106 1.00 61.93 ?  268 SER B OG    1 
ATOM   7712  N  N     . ALA B 1 269 ? 121.452 120.524 137.884 1.00 70.03 ?  269 ALA B N     1 
ATOM   7713  C  CA    . ALA B 1 269 ? 121.411 121.560 136.862 1.00 70.26 ?  269 ALA B CA    1 
ATOM   7714  C  C     . ALA B 1 269 ? 122.362 121.239 135.716 1.00 71.13 ?  269 ALA B C     1 
ATOM   7715  O  O     . ALA B 1 269 ? 123.472 120.739 135.926 1.00 68.97 ?  269 ALA B O     1 
ATOM   7716  C  CB    . ALA B 1 269 ? 121.762 122.918 137.470 1.00 66.54 ?  269 ALA B CB    1 
ATOM   7717  N  N     . ASP B 1 270 ? 121.915 121.527 134.498 1.00 74.02 ?  270 ASP B N     1 
ATOM   7718  C  CA    . ASP B 1 270 ? 122.749 121.341 133.320 1.00 74.33 ?  270 ASP B CA    1 
ATOM   7719  C  C     . ASP B 1 270 ? 123.927 122.309 133.344 1.00 73.93 ?  270 ASP B C     1 
ATOM   7720  O  O     . ASP B 1 270 ? 123.848 123.408 133.901 1.00 75.43 ?  270 ASP B O     1 
ATOM   7721  C  CB    . ASP B 1 270 ? 121.925 121.544 132.049 1.00 73.65 ?  270 ASP B CB    1 
ATOM   7722  C  CG    . ASP B 1 270 ? 122.538 120.867 130.839 1.00 76.84 ?  270 ASP B CG    1 
ATOM   7723  O  OD1   . ASP B 1 270 ? 123.708 121.161 130.516 1.00 75.94 ?  270 ASP B OD1   1 
ATOM   7724  O  OD2   . ASP B 1 270 ? 121.847 120.040 130.206 1.00 75.61 -1 270 ASP B OD2   1 
ATOM   7725  N  N     . GLU B 1 271 ? 125.035 121.887 132.731 1.00 74.27 ?  271 GLU B N     1 
ATOM   7726  C  CA    . GLU B 1 271 ? 126.244 122.703 132.735 1.00 75.67 ?  271 GLU B CA    1 
ATOM   7727  C  C     . GLU B 1 271 ? 126.081 124.000 131.953 1.00 73.53 ?  271 GLU B C     1 
ATOM   7728  O  O     . GLU B 1 271 ? 126.852 124.940 132.173 1.00 73.03 ?  271 GLU B O     1 
ATOM   7729  C  CB    . GLU B 1 271 ? 127.421 121.903 132.175 1.00 73.87 ?  271 GLU B CB    1 
ATOM   7730  C  CG    . GLU B 1 271 ? 127.894 120.783 133.088 1.00 73.21 ?  271 GLU B CG    1 
ATOM   7731  C  CD    . GLU B 1 271 ? 128.431 121.296 134.410 1.00 75.05 ?  271 GLU B CD    1 
ATOM   7732  O  OE1   . GLU B 1 271 ? 129.092 122.356 134.417 1.00 75.43 ?  271 GLU B OE1   1 
ATOM   7733  O  OE2   . GLU B 1 271 ? 128.191 120.640 135.446 1.00 74.89 -1 271 GLU B OE2   1 
ATOM   7734  N  N     . ASP B 1 272 ? 125.105 124.078 131.051 1.00 69.75 ?  272 ASP B N     1 
ATOM   7735  C  CA    . ASP B 1 272 ? 124.802 125.321 130.357 1.00 71.73 ?  272 ASP B CA    1 
ATOM   7736  C  C     . ASP B 1 272 ? 123.826 126.198 131.130 1.00 70.44 ?  272 ASP B C     1 
ATOM   7737  O  O     . ASP B 1 272 ? 123.477 127.283 130.654 1.00 66.88 ?  272 ASP B O     1 
ATOM   7738  C  CB    . ASP B 1 272 ? 124.252 125.031 128.953 1.00 70.85 ?  272 ASP B CB    1 
ATOM   7739  C  CG    . ASP B 1 272 ? 122.816 124.537 128.972 1.00 73.30 ?  272 ASP B CG    1 
ATOM   7740  O  OD1   . ASP B 1 272 ? 122.413 123.892 129.961 1.00 72.91 ?  272 ASP B OD1   1 
ATOM   7741  O  OD2   . ASP B 1 272 ? 122.088 124.798 127.991 1.00 70.51 -1 272 ASP B OD2   1 
ATOM   7742  N  N     . VAL B 1 273 ? 123.366 125.744 132.297 1.00 66.23 ?  273 VAL B N     1 
ATOM   7743  C  CA    . VAL B 1 273 ? 122.503 126.526 133.169 1.00 66.52 ?  273 VAL B CA    1 
ATOM   7744  C  C     . VAL B 1 273 ? 123.158 126.791 134.519 1.00 64.95 ?  273 VAL B C     1 
ATOM   7745  O  O     . VAL B 1 273 ? 123.035 127.892 135.068 1.00 66.14 ?  273 VAL B O     1 
ATOM   7746  C  CB    . VAL B 1 273 ? 121.135 125.834 133.358 1.00 68.18 ?  273 VAL B CB    1 
ATOM   7747  C  CG1   . VAL B 1 273 ? 120.248 126.640 134.297 1.00 62.76 ?  273 VAL B CG1   1 
ATOM   7748  C  CG2   . VAL B 1 273 ? 120.454 125.629 132.016 1.00 65.62 ?  273 VAL B CG2   1 
ATOM   7749  N  N     . ARG B 1 274 ? 123.865 125.803 135.063 1.00 62.96 ?  274 ARG B N     1 
ATOM   7750  C  CA    . ARG B 1 274 ? 124.432 125.914 136.400 1.00 61.76 ?  274 ARG B CA    1 
ATOM   7751  C  C     . ARG B 1 274 ? 125.494 127.005 136.463 1.00 62.60 ?  274 ARG B C     1 
ATOM   7752  O  O     . ARG B 1 274 ? 126.309 127.160 135.550 1.00 62.96 ?  274 ARG B O     1 
ATOM   7753  C  CB    . ARG B 1 274 ? 125.032 124.569 136.820 1.00 65.11 ?  274 ARG B CB    1 
ATOM   7754  C  CG    . ARG B 1 274 ? 126.190 124.668 137.800 1.00 62.82 ?  274 ARG B CG    1 
ATOM   7755  C  CD    . ARG B 1 274 ? 126.277 123.439 138.689 1.00 63.74 ?  274 ARG B CD    1 
ATOM   7756  N  NE    . ARG B 1 274 ? 126.718 122.262 137.951 1.00 66.77 ?  274 ARG B NE    1 
ATOM   7757  C  CZ    . ARG B 1 274 ? 125.978 121.180 137.753 1.00 68.61 ?  274 ARG B CZ    1 
ATOM   7758  N  NH1   . ARG B 1 274 ? 124.748 121.086 138.231 1.00 67.06 1  274 ARG B NH1   1 
ATOM   7759  N  NH2   . ARG B 1 274 ? 126.484 120.166 137.057 1.00 66.55 ?  274 ARG B NH2   1 
ATOM   7760  N  N     . VAL B 1 275 ? 125.474 127.767 137.555 1.00 49.50 ?  275 VAL B N     1 
ATOM   7761  C  CA    . VAL B 1 275 ? 126.507 128.746 137.874 1.00 46.65 ?  275 VAL B CA    1 
ATOM   7762  C  C     . VAL B 1 275 ? 127.181 128.308 139.167 1.00 49.29 ?  275 VAL B C     1 
ATOM   7763  O  O     . VAL B 1 275 ? 126.514 127.843 140.099 1.00 54.55 ?  275 VAL B O     1 
ATOM   7764  C  CB    . VAL B 1 275 ? 125.933 130.171 137.997 1.00 45.30 ?  275 VAL B CB    1 
ATOM   7765  C  CG1   . VAL B 1 275 ? 125.504 130.689 136.634 1.00 41.64 ?  275 VAL B CG1   1 
ATOM   7766  C  CG2   . VAL B 1 275 ? 124.764 130.198 138.964 1.00 48.00 ?  275 VAL B CG2   1 
ATOM   7767  N  N     . LYS B 1 276 ? 128.505 128.440 139.218 1.00 43.13 ?  276 LYS B N     1 
ATOM   7768  C  CA    . LYS B 1 276 ? 129.298 127.894 140.315 1.00 44.19 ?  276 LYS B CA    1 
ATOM   7769  C  C     . LYS B 1 276 ? 129.722 128.948 141.329 1.00 42.13 ?  276 LYS B C     1 
ATOM   7770  O  O     . LYS B 1 276 ? 129.568 128.742 142.536 1.00 48.13 ?  276 LYS B O     1 
ATOM   7771  C  CB    . LYS B 1 276 ? 130.547 127.171 139.779 1.00 45.94 ?  276 LYS B CB    1 
ATOM   7772  C  CG    . LYS B 1 276 ? 130.307 125.826 139.073 1.00 47.42 ?  276 LYS B CG    1 
ATOM   7773  C  CD    . LYS B 1 276 ? 129.630 125.917 137.703 1.00 48.40 ?  276 LYS B CD    1 
ATOM   7774  C  CE    . LYS B 1 276 ? 130.094 127.122 136.896 1.00 45.33 ?  276 LYS B CE    1 
ATOM   7775  N  NZ    . LYS B 1 276 ? 129.755 126.978 135.453 1.00 49.22 1  276 LYS B NZ    1 
ATOM   7776  N  N     . THR B 1 277 ? 130.260 130.074 140.869 1.00 38.02 ?  277 THR B N     1 
ATOM   7777  C  CA    . THR B 1 277 ? 130.811 131.094 141.749 1.00 39.22 ?  277 THR B CA    1 
ATOM   7778  C  C     . THR B 1 277 ? 129.868 132.269 141.959 1.00 38.73 ?  277 THR B C     1 
ATOM   7779  O  O     . THR B 1 277 ? 130.293 133.304 142.484 1.00 39.15 ?  277 THR B O     1 
ATOM   7780  C  CB    . THR B 1 277 ? 132.148 131.596 141.203 1.00 41.69 ?  277 THR B CB    1 
ATOM   7781  O  OG1   . THR B 1 277 ? 131.916 132.446 140.071 1.00 33.70 ?  277 THR B OG1   1 
ATOM   7782  C  CG2   . THR B 1 277 ? 133.021 130.424 140.788 1.00 39.64 ?  277 THR B CG2   1 
ATOM   7783  N  N     . LEU B 1 278 ? 128.606 132.139 141.566 1.00 34.18 ?  278 LEU B N     1 
ATOM   7784  C  CA    . LEU B 1 278 ? 127.635 133.225 141.649 1.00 28.24 ?  278 LEU B CA    1 
ATOM   7785  C  C     . LEU B 1 278 ? 126.553 132.841 142.648 1.00 24.52 ?  278 LEU B C     1 
ATOM   7786  O  O     . LEU B 1 278 ? 125.687 132.015 142.343 1.00 36.61 ?  278 LEU B O     1 
ATOM   7787  C  CB    . LEU B 1 278 ? 127.032 133.519 140.276 1.00 30.67 ?  278 LEU B CB    1 
ATOM   7788  C  CG    . LEU B 1 278 ? 126.445 134.914 140.062 1.00 28.70 ?  278 LEU B CG    1 
ATOM   7789  C  CD1   . LEU B 1 278 ? 127.547 135.924 139.825 1.00 24.89 ?  278 LEU B CD1   1 
ATOM   7790  C  CD2   . LEU B 1 278 ? 125.473 134.904 138.899 1.00 27.96 ?  278 LEU B CD2   1 
ATOM   7791  N  N     . SER B 1 279 ? 126.605 133.435 143.836 1.00 24.89 ?  279 SER B N     1 
ATOM   7792  C  CA    . SER B 1 279 ? 125.527 133.278 144.800 1.00 17.98 ?  279 SER B CA    1 
ATOM   7793  C  C     . SER B 1 279 ? 124.268 133.961 144.283 1.00 21.42 ?  279 SER B C     1 
ATOM   7794  O  O     . SER B 1 279 ? 124.327 134.897 143.485 1.00 30.82 ?  279 SER B O     1 
ATOM   7795  C  CB    . SER B 1 279 ? 125.925 133.868 146.149 1.00 18.46 ?  279 SER B CB    1 
ATOM   7796  O  OG    . SER B 1 279 ? 127.141 133.311 146.612 1.00 31.78 ?  279 SER B OG    1 
ATOM   7797  N  N     . ILE B 1 280 ? 123.116 133.479 144.736 1.00 19.86 ?  280 ILE B N     1 
ATOM   7798  C  CA    . ILE B 1 280 ? 121.837 134.007 144.288 1.00 20.27 ?  280 ILE B CA    1 
ATOM   7799  C  C     . ILE B 1 280 ? 121.028 134.451 145.495 1.00 12.37 ?  280 ILE B C     1 
ATOM   7800  O  O     . ILE B 1 280 ? 121.049 133.805 146.547 1.00 25.03 ?  280 ILE B O     1 
ATOM   7801  C  CB    . ILE B 1 280 ? 121.049 132.984 143.441 1.00 15.42 ?  280 ILE B CB    1 
ATOM   7802  C  CG1   . ILE B 1 280 ? 120.743 131.715 144.234 1.00 21.88 ?  280 ILE B CG1   1 
ATOM   7803  C  CG2   . ILE B 1 280 ? 121.816 132.640 142.191 1.00 16.03 ?  280 ILE B CG2   1 
ATOM   7804  C  CD1   . ILE B 1 280 ? 119.538 130.968 143.712 1.00 15.40 ?  280 ILE B CD1   1 
ATOM   7805  N  N     . GLY B 1 281 ? 120.346 135.572 145.349 1.00 6.93  ?  281 GLY B N     1 
ATOM   7806  C  CA    . GLY B 1 281 ? 119.411 136.035 146.359 1.00 6.77  ?  281 GLY B CA    1 
ATOM   7807  C  C     . GLY B 1 281 ? 118.092 136.398 145.719 1.00 4.21  ?  281 GLY B C     1 
ATOM   7808  O  O     . GLY B 1 281 ? 118.054 136.960 144.628 1.00 20.89 ?  281 GLY B O     1 
ATOM   7809  N  N     . VAL B 1 282 ? 117.007 136.063 146.408 1.00 13.07 ?  282 VAL B N     1 
ATOM   7810  C  CA    . VAL B 1 282 ? 115.658 136.325 145.925 1.00 16.12 ?  282 VAL B CA    1 
ATOM   7811  C  C     . VAL B 1 282 ? 115.058 137.448 146.757 1.00 12.86 ?  282 VAL B C     1 
ATOM   7812  O  O     . VAL B 1 282 ? 115.110 137.415 147.992 1.00 21.68 ?  282 VAL B O     1 
ATOM   7813  C  CB    . VAL B 1 282 ? 114.782 135.062 145.978 1.00 16.31 ?  282 VAL B CB    1 
ATOM   7814  C  CG1   . VAL B 1 282 ? 113.325 135.414 145.755 1.00 20.40 ?  282 VAL B CG1   1 
ATOM   7815  C  CG2   . VAL B 1 282 ? 115.239 134.077 144.928 1.00 22.87 ?  282 VAL B CG2   1 
ATOM   7816  N  N     . VAL B 1 283 ? 114.502 138.445 146.079 1.00 2.61  ?  283 VAL B N     1 
ATOM   7817  C  CA    . VAL B 1 283 ? 113.819 139.559 146.722 1.00 9.73  ?  283 VAL B CA    1 
ATOM   7818  C  C     . VAL B 1 283 ? 112.327 139.268 146.717 1.00 12.01 ?  283 VAL B C     1 
ATOM   7819  O  O     . VAL B 1 283 ? 111.737 139.028 145.658 1.00 22.77 ?  283 VAL B O     1 
ATOM   7820  C  CB    . VAL B 1 283 ? 114.129 140.885 146.008 1.00 8.36  ?  283 VAL B CB    1 
ATOM   7821  C  CG1   . VAL B 1 283 ? 113.650 142.051 146.839 1.00 10.05 ?  283 VAL B CG1   1 
ATOM   7822  C  CG2   . VAL B 1 283 ? 115.618 140.993 145.735 1.00 9.21  ?  283 VAL B CG2   1 
ATOM   7823  N  N     . ILE B 1 284 ? 111.719 139.281 147.899 1.00 16.01 ?  284 ILE B N     1 
ATOM   7824  C  CA    . ILE B 1 284 ? 110.316 138.908 148.044 1.00 17.63 ?  284 ILE B CA    1 
ATOM   7825  C  C     . ILE B 1 284 ? 109.521 140.079 148.610 1.00 21.20 ?  284 ILE B C     1 
ATOM   7826  O  O     . ILE B 1 284 ? 109.685 140.426 149.788 1.00 24.03 ?  284 ILE B O     1 
ATOM   7827  C  CB    . ILE B 1 284 ? 110.161 137.665 148.934 1.00 14.12 ?  284 ILE B CB    1 
ATOM   7828  C  CG1   . ILE B 1 284 ? 111.044 136.529 148.422 1.00 17.29 ?  284 ILE B CG1   1 
ATOM   7829  C  CG2   . ILE B 1 284 ? 108.707 137.231 148.991 1.00 15.92 ?  284 ILE B CG2   1 
ATOM   7830  C  CD1   . ILE B 1 284 ? 110.880 135.241 149.185 1.00 20.09 ?  284 ILE B CD1   1 
ATOM   7831  N  N     . PRO B 1 285 ? 108.664 140.715 147.819 1.00 20.06 ?  285 PRO B N     1 
ATOM   7832  C  CA    . PRO B 1 285 ? 107.754 141.720 148.374 1.00 29.69 ?  285 PRO B CA    1 
ATOM   7833  C  C     . PRO B 1 285 ? 106.663 141.072 149.210 1.00 28.16 ?  285 PRO B C     1 
ATOM   7834  O  O     . PRO B 1 285 ? 106.437 139.860 149.165 1.00 23.12 ?  285 PRO B O     1 
ATOM   7835  C  CB    . PRO B 1 285 ? 107.167 142.400 147.132 1.00 22.68 ?  285 PRO B CB    1 
ATOM   7836  C  CG    . PRO B 1 285 ? 108.084 142.035 146.013 1.00 20.66 ?  285 PRO B CG    1 
ATOM   7837  C  CD    . PRO B 1 285 ? 108.620 140.685 146.349 1.00 14.72 ?  285 PRO B CD    1 
ATOM   7838  N  N     . ASP B 1 286 ? 105.978 141.907 149.994 1.00 31.68 ?  286 ASP B N     1 
ATOM   7839  C  CA    . ASP B 1 286 ? 104.865 141.421 150.802 1.00 25.85 ?  286 ASP B CA    1 
ATOM   7840  C  C     . ASP B 1 286 ? 103.732 140.875 149.946 1.00 32.58 ?  286 ASP B C     1 
ATOM   7841  O  O     . ASP B 1 286 ? 102.940 140.061 150.432 1.00 36.13 ?  286 ASP B O     1 
ATOM   7842  C  CB    . ASP B 1 286 ? 104.334 142.535 151.703 1.00 27.89 ?  286 ASP B CB    1 
ATOM   7843  C  CG    . ASP B 1 286 ? 104.936 142.501 153.091 1.00 42.45 ?  286 ASP B CG    1 
ATOM   7844  O  OD1   . ASP B 1 286 ? 105.879 141.715 153.315 1.00 38.68 ?  286 ASP B OD1   1 
ATOM   7845  O  OD2   . ASP B 1 286 ? 104.471 143.268 153.959 1.00 45.98 -1 286 ASP B OD2   1 
ATOM   7846  N  N     . LYS B 1 287 ? 103.634 141.311 148.688 1.00 35.56 ?  287 LYS B N     1 
ATOM   7847  C  CA    . LYS B 1 287 ? 102.578 140.822 147.809 1.00 29.84 ?  287 LYS B CA    1 
ATOM   7848  C  C     . LYS B 1 287 ? 102.707 139.324 147.568 1.00 31.94 ?  287 LYS B C     1 
ATOM   7849  O  O     . LYS B 1 287 ? 101.704 138.603 147.552 1.00 37.47 ?  287 LYS B O     1 
ATOM   7850  C  CB    . LYS B 1 287 ? 102.607 141.581 146.482 1.00 29.52 ?  287 LYS B CB    1 
ATOM   7851  C  CG    . LYS B 1 287 ? 101.362 141.388 145.636 1.00 27.75 ?  287 LYS B CG    1 
ATOM   7852  C  CD    . LYS B 1 287 ? 100.117 141.760 146.419 1.00 34.61 ?  287 LYS B CD    1 
ATOM   7853  C  CE    . LYS B 1 287 ? 98.879  141.715 145.547 1.00 35.33 ?  287 LYS B CE    1 
ATOM   7854  N  NZ    . LYS B 1 287 ? 97.703  142.312 146.234 1.00 36.98 1  287 LYS B NZ    1 
ATOM   7855  N  N     . PHE B 1 288 ? 103.934 138.837 147.372 1.00 31.64 ?  288 PHE B N     1 
ATOM   7856  C  CA    . PHE B 1 288 ? 104.132 137.407 147.153 1.00 25.08 ?  288 PHE B CA    1 
ATOM   7857  C  C     . PHE B 1 288 ? 103.743 136.598 148.382 1.00 26.26 ?  288 PHE B C     1 
ATOM   7858  O  O     . PHE B 1 288 ? 103.111 135.541 148.263 1.00 36.76 ?  288 PHE B O     1 
ATOM   7859  C  CB    . PHE B 1 288 ? 105.584 137.132 146.768 1.00 26.32 ?  288 PHE B CB    1 
ATOM   7860  C  CG    . PHE B 1 288 ? 105.832 135.722 146.321 1.00 26.81 ?  288 PHE B CG    1 
ATOM   7861  C  CD1   . PHE B 1 288 ? 106.174 134.742 147.236 1.00 23.51 ?  288 PHE B CD1   1 
ATOM   7862  C  CD2   . PHE B 1 288 ? 105.720 135.377 144.987 1.00 24.59 ?  288 PHE B CD2   1 
ATOM   7863  C  CE1   . PHE B 1 288 ? 106.401 133.448 146.829 1.00 23.18 ?  288 PHE B CE1   1 
ATOM   7864  C  CE2   . PHE B 1 288 ? 105.949 134.084 144.574 1.00 30.28 ?  288 PHE B CE2   1 
ATOM   7865  C  CZ    . PHE B 1 288 ? 106.289 133.118 145.497 1.00 29.49 ?  288 PHE B CZ    1 
ATOM   7866  N  N     . VAL B 1 289 ? 104.118 137.071 149.571 1.00 33.44 ?  289 VAL B N     1 
ATOM   7867  C  CA    . VAL B 1 289 ? 103.766 136.362 150.794 1.00 30.03 ?  289 VAL B CA    1 
ATOM   7868  C  C     . VAL B 1 289 ? 102.259 136.384 151.005 1.00 32.62 ?  289 VAL B C     1 
ATOM   7869  O  O     . VAL B 1 289 ? 101.672 135.411 151.490 1.00 35.56 ?  289 VAL B O     1 
ATOM   7870  C  CB    . VAL B 1 289 ? 104.522 136.961 151.993 1.00 32.52 ?  289 VAL B CB    1 
ATOM   7871  C  CG1   . VAL B 1 289 ? 104.166 136.224 153.273 1.00 31.58 ?  289 VAL B CG1   1 
ATOM   7872  C  CG2   . VAL B 1 289 ? 106.020 136.913 151.747 1.00 25.79 ?  289 VAL B CG2   1 
ATOM   7873  N  N     . GLU B 1 290 ? 101.606 137.490 150.643 1.00 36.62 ?  290 GLU B N     1 
ATOM   7874  C  CA    . GLU B 1 290 ? 100.154 137.560 150.747 1.00 33.24 ?  290 GLU B CA    1 
ATOM   7875  C  C     . GLU B 1 290 ? 99.479  136.596 149.779 1.00 37.81 ?  290 GLU B C     1 
ATOM   7876  O  O     . GLU B 1 290 ? 98.483  135.952 150.128 1.00 45.39 ?  290 GLU B O     1 
ATOM   7877  C  CB    . GLU B 1 290 ? 99.683  138.993 150.500 1.00 36.09 ?  290 GLU B CB    1 
ATOM   7878  C  CG    . GLU B 1 290 ? 98.178  139.174 150.545 1.00 39.32 ?  290 GLU B CG    1 
ATOM   7879  C  CD    . GLU B 1 290 ? 97.766  140.631 150.469 1.00 48.27 ?  290 GLU B CD    1 
ATOM   7880  O  OE1   . GLU B 1 290 ? 98.166  141.313 149.502 1.00 46.35 ?  290 GLU B OE1   1 
ATOM   7881  O  OE2   . GLU B 1 290 ? 97.039  141.094 151.373 1.00 49.09 -1 290 GLU B OE2   1 
ATOM   7882  N  N     . LEU B 1 291 ? 100.003 136.488 148.555 1.00 30.84 ?  291 LEU B N     1 
ATOM   7883  C  CA    . LEU B 1 291 ? 99.433  135.561 147.582 1.00 27.61 ?  291 LEU B CA    1 
ATOM   7884  C  C     . LEU B 1 291 ? 99.628  134.115 148.014 1.00 34.77 ?  291 LEU B C     1 
ATOM   7885  O  O     . LEU B 1 291 ? 98.722  133.288 147.862 1.00 38.54 ?  291 LEU B O     1 
ATOM   7886  C  CB    . LEU B 1 291 ? 100.051 135.794 146.204 1.00 32.42 ?  291 LEU B CB    1 
ATOM   7887  C  CG    . LEU B 1 291 ? 99.739  137.128 145.526 1.00 33.84 ?  291 LEU B CG    1 
ATOM   7888  C  CD1   . LEU B 1 291 ? 100.707 137.377 144.386 1.00 26.96 ?  291 LEU B CD1   1 
ATOM   7889  C  CD2   . LEU B 1 291 ? 98.304  137.160 145.036 1.00 31.97 ?  291 LEU B CD2   1 
ATOM   7890  N  N     . ALA B 1 292 ? 100.807 133.786 148.546 1.00 41.06 ?  292 ALA B N     1 
ATOM   7891  C  CA    . ALA B 1 292 ? 101.054 132.429 149.023 1.00 31.29 ?  292 ALA B CA    1 
ATOM   7892  C  C     . ALA B 1 292 ? 100.229 132.112 150.263 1.00 31.33 ?  292 ALA B C     1 
ATOM   7893  O  O     . ALA B 1 292 ? 99.803  130.967 150.447 1.00 38.52 ?  292 ALA B O     1 
ATOM   7894  C  CB    . ALA B 1 292 ? 102.541 132.235 149.312 1.00 27.35 ?  292 ALA B CB    1 
ATOM   7895  N  N     . ARG B 1 293 ? 99.999  133.106 151.122 1.00 36.05 ?  293 ARG B N     1 
ATOM   7896  C  CA    . ARG B 1 293 ? 99.219  132.888 152.334 1.00 36.19 ?  293 ARG B CA    1 
ATOM   7897  C  C     . ARG B 1 293 ? 97.788  132.485 152.006 1.00 41.29 ?  293 ARG B C     1 
ATOM   7898  O  O     . ARG B 1 293 ? 97.228  131.582 152.637 1.00 47.95 ?  293 ARG B O     1 
ATOM   7899  C  CB    . ARG B 1 293 ? 99.243  134.153 153.192 1.00 37.33 ?  293 ARG B CB    1 
ATOM   7900  C  CG    . ARG B 1 293 ? 98.296  134.151 154.373 1.00 37.72 ?  293 ARG B CG    1 
ATOM   7901  C  CD    . ARG B 1 293 ? 98.229  135.535 154.988 1.00 38.99 ?  293 ARG B CD    1 
ATOM   7902  N  NE    . ARG B 1 293 ? 99.558  136.113 155.140 1.00 45.33 ?  293 ARG B NE    1 
ATOM   7903  C  CZ    . ARG B 1 293 ? 99.894  137.336 154.750 1.00 43.13 ?  293 ARG B CZ    1 
ATOM   7904  N  NH1   . ARG B 1 293 ? 99.016  138.148 154.187 1.00 42.09 1  293 ARG B NH1   1 
ATOM   7905  N  NH2   . ARG B 1 293 ? 101.144 137.752 154.928 1.00 40.00 ?  293 ARG B NH2   1 
ATOM   7906  N  N     . GLU B 1 294 ? 97.184  133.140 151.020 1.00 48.58 ?  294 GLU B N     1 
ATOM   7907  C  CA    . GLU B 1 294 ? 95.816  132.852 150.613 1.00 47.69 ?  294 GLU B CA    1 
ATOM   7908  C  C     . GLU B 1 294 ? 95.736  131.802 149.514 1.00 45.66 ?  294 GLU B C     1 
ATOM   7909  O  O     . GLU B 1 294 ? 94.635  131.515 149.033 1.00 48.04 ?  294 GLU B O     1 
ATOM   7910  C  CB    . GLU B 1 294 ? 95.127  134.138 150.153 1.00 44.43 ?  294 GLU B CB    1 
ATOM   7911  C  CG    . GLU B 1 294 ? 95.007  135.194 151.238 1.00 48.49 ?  294 GLU B CG    1 
ATOM   7912  C  CD    . GLU B 1 294 ? 95.023  136.601 150.680 1.00 55.04 ?  294 GLU B CD    1 
ATOM   7913  O  OE1   . GLU B 1 294 ? 95.161  136.747 149.447 1.00 56.38 ?  294 GLU B OE1   1 
ATOM   7914  O  OE2   . GLU B 1 294 ? 94.902  137.558 151.472 1.00 54.30 -1 294 GLU B OE2   1 
ATOM   7915  N  N     . ASP B 1 295 ? 96.872  131.239 149.101 1.00 44.07 ?  295 ASP B N     1 
ATOM   7916  C  CA    . ASP B 1 295 ? 96.952  130.181 148.095 1.00 43.93 ?  295 ASP B CA    1 
ATOM   7917  C  C     . ASP B 1 295 ? 96.417  130.619 146.736 1.00 49.15 ?  295 ASP B C     1 
ATOM   7918  O  O     . ASP B 1 295 ? 96.125  129.776 145.882 1.00 47.46 ?  295 ASP B O     1 
ATOM   7919  C  CB    . ASP B 1 295 ? 96.230  128.909 148.557 1.00 45.64 ?  295 ASP B CB    1 
ATOM   7920  C  CG    . ASP B 1 295 ? 96.996  127.646 148.213 1.00 52.77 ?  295 ASP B CG    1 
ATOM   7921  O  OD1   . ASP B 1 295 ? 97.895  127.711 147.350 1.00 54.24 ?  295 ASP B OD1   1 
ATOM   7922  O  OD2   . ASP B 1 295 ? 96.696  126.587 148.802 1.00 50.23 -1 295 ASP B OD2   1 
ATOM   7923  N  N     . LYS B 1 296 ? 96.277  131.923 146.513 1.00 49.66 ?  296 LYS B N     1 
ATOM   7924  C  CA    . LYS B 1 296 ? 95.899  132.413 145.195 1.00 47.19 ?  296 LYS B CA    1 
ATOM   7925  C  C     . LYS B 1 296 ? 97.041  132.198 144.213 1.00 45.50 ?  296 LYS B C     1 
ATOM   7926  O  O     . LYS B 1 296 ? 98.212  132.391 144.550 1.00 51.87 ?  296 LYS B O     1 
ATOM   7927  C  CB    . LYS B 1 296 ? 95.537  133.896 145.255 1.00 46.04 ?  296 LYS B CB    1 
ATOM   7928  C  CG    . LYS B 1 296 ? 95.000  134.356 146.596 1.00 47.76 ?  296 LYS B CG    1 
ATOM   7929  C  CD    . LYS B 1 296 ? 93.966  135.454 146.433 1.00 49.04 ?  296 LYS B CD    1 
ATOM   7930  C  CE    . LYS B 1 296 ? 92.594  134.880 146.123 1.00 51.74 ?  296 LYS B CE    1 
ATOM   7931  N  NZ    . LYS B 1 296 ? 92.089  134.015 147.225 1.00 50.32 1  296 LYS B NZ    1 
ATOM   7932  N  N     . ALA B 1 297 ? 96.701  131.796 142.994 1.00 45.38 ?  297 ALA B N     1 
ATOM   7933  C  CA    . ALA B 1 297 ? 97.716  131.601 141.969 1.00 46.15 ?  297 ALA B CA    1 
ATOM   7934  C  C     . ALA B 1 297 ? 98.307  132.946 141.564 1.00 45.62 ?  297 ALA B C     1 
ATOM   7935  O  O     . ALA B 1 297 ? 97.576  133.890 141.251 1.00 53.38 ?  297 ALA B O     1 
ATOM   7936  C  CB    . ALA B 1 297 ? 97.119  130.890 140.759 1.00 44.20 ?  297 ALA B CB    1 
ATOM   7937  N  N     . ALA B 1 298 ? 99.632  133.031 141.573 1.00 38.81 ?  298 ALA B N     1 
ATOM   7938  C  CA    . ALA B 1 298 ? 100.339 134.283 141.351 1.00 39.74 ?  298 ALA B CA    1 
ATOM   7939  C  C     . ALA B 1 298 ? 100.842 134.376 139.917 1.00 37.91 ?  298 ALA B C     1 
ATOM   7940  O  O     . ALA B 1 298 ? 100.824 133.409 139.153 1.00 41.21 ?  298 ALA B O     1 
ATOM   7941  C  CB    . ALA B 1 298 ? 101.504 134.421 142.335 1.00 42.58 ?  298 ALA B CB    1 
ATOM   7942  N  N     . TYR B 1 299 ? 101.303 135.570 139.559 1.00 38.47 ?  299 TYR B N     1 
ATOM   7943  C  CA    . TYR B 1 299 ? 101.807 135.864 138.226 1.00 31.67 ?  299 TYR B CA    1 
ATOM   7944  C  C     . TYR B 1 299 ? 103.217 136.424 138.325 1.00 33.77 ?  299 TYR B C     1 
ATOM   7945  O  O     . TYR B 1 299 ? 103.478 137.319 139.136 1.00 41.45 ?  299 TYR B O     1 
ATOM   7946  C  CB    . TYR B 1 299 ? 100.904 136.868 137.507 1.00 32.93 ?  299 TYR B CB    1 
ATOM   7947  C  CG    . TYR B 1 299 ? 99.641  136.272 136.935 1.00 35.07 ?  299 TYR B CG    1 
ATOM   7948  C  CD1   . TYR B 1 299 ? 99.686  135.430 135.833 1.00 37.58 ?  299 TYR B CD1   1 
ATOM   7949  C  CD2   . TYR B 1 299 ? 98.403  136.558 137.492 1.00 36.23 ?  299 TYR B CD2   1 
ATOM   7950  C  CE1   . TYR B 1 299 ? 98.535  134.887 135.307 1.00 41.02 ?  299 TYR B CE1   1 
ATOM   7951  C  CE2   . TYR B 1 299 ? 97.247  136.019 136.972 1.00 39.48 ?  299 TYR B CE2   1 
ATOM   7952  C  CZ    . TYR B 1 299 ? 97.317  135.185 135.879 1.00 44.62 ?  299 TYR B CZ    1 
ATOM   7953  O  OH    . TYR B 1 299 ? 96.164  134.646 135.356 1.00 45.44 ?  299 TYR B OH    1 
ATOM   7954  N  N     . VAL B 1 300 ? 104.120 135.897 137.506 1.00 32.57 ?  300 VAL B N     1 
ATOM   7955  C  CA    . VAL B 1 300 ? 105.430 136.498 137.289 1.00 28.85 ?  300 VAL B CA    1 
ATOM   7956  C  C     . VAL B 1 300 ? 105.377 137.244 135.967 1.00 27.75 ?  300 VAL B C     1 
ATOM   7957  O  O     . VAL B 1 300 ? 104.743 136.786 135.009 1.00 32.37 ?  300 VAL B O     1 
ATOM   7958  C  CB    . VAL B 1 300 ? 106.552 135.443 137.299 1.00 24.24 ?  300 VAL B CB    1 
ATOM   7959  C  CG1   . VAL B 1 300 ? 106.843 135.001 138.721 1.00 26.78 ?  300 VAL B CG1   1 
ATOM   7960  C  CG2   . VAL B 1 300 ? 106.179 134.257 136.430 1.00 31.98 ?  300 VAL B CG2   1 
ATOM   7961  N  N     . PHE B 1 301 ? 106.032 138.395 135.907 1.00 30.11 ?  301 PHE B N     1 
ATOM   7962  C  CA    . PHE B 1 301 ? 105.849 139.329 134.809 1.00 23.39 ?  301 PHE B CA    1 
ATOM   7963  C  C     . PHE B 1 301 ? 107.126 139.473 133.997 1.00 31.95 ?  301 PHE B C     1 
ATOM   7964  O  O     . PHE B 1 301 ? 108.236 139.359 134.523 1.00 33.95 ?  301 PHE B O     1 
ATOM   7965  C  CB    . PHE B 1 301 ? 105.412 140.698 135.327 1.00 24.46 ?  301 PHE B CB    1 
ATOM   7966  C  CG    . PHE B 1 301 ? 104.250 140.641 136.270 1.00 31.13 ?  301 PHE B CG    1 
ATOM   7967  C  CD1   . PHE B 1 301 ? 102.954 140.607 135.790 1.00 28.85 ?  301 PHE B CD1   1 
ATOM   7968  C  CD2   . PHE B 1 301 ? 104.454 140.607 137.638 1.00 27.61 ?  301 PHE B CD2   1 
ATOM   7969  C  CE1   . PHE B 1 301 ? 101.884 140.546 136.655 1.00 30.97 ?  301 PHE B CE1   1 
ATOM   7970  C  CE2   . PHE B 1 301 ? 103.387 140.546 138.506 1.00 28.61 ?  301 PHE B CE2   1 
ATOM   7971  C  CZ    . PHE B 1 301 ? 102.100 140.518 138.014 1.00 33.66 ?  301 PHE B CZ    1 
ATOM   7972  N  N     . TYR B 1 302 ? 106.951 139.719 132.704 1.00 31.27 ?  302 TYR B N     1 
ATOM   7973  C  CA    . TYR B 1 302 ? 108.072 140.058 131.842 1.00 28.12 ?  302 TYR B CA    1 
ATOM   7974  C  C     . TYR B 1 302 ? 108.420 141.526 132.049 1.00 29.09 ?  302 TYR B C     1 
ATOM   7975  O  O     . TYR B 1 302 ? 107.586 142.393 131.769 1.00 32.21 ?  302 TYR B O     1 
ATOM   7976  C  CB    . TYR B 1 302 ? 107.728 139.794 130.382 1.00 29.30 ?  302 TYR B CB    1 
ATOM   7977  C  CG    . TYR B 1 302 ? 107.575 138.329 130.031 1.00 31.34 ?  302 TYR B CG    1 
ATOM   7978  C  CD1   . TYR B 1 302 ? 106.440 137.621 130.400 1.00 30.03 ?  302 TYR B CD1   1 
ATOM   7979  C  CD2   . TYR B 1 302 ? 108.563 137.657 129.327 1.00 29.42 ?  302 TYR B CD2   1 
ATOM   7980  C  CE1   . TYR B 1 302 ? 106.294 136.288 130.079 1.00 30.43 ?  302 TYR B CE1   1 
ATOM   7981  C  CE2   . TYR B 1 302 ? 108.426 136.323 129.004 1.00 31.36 ?  302 TYR B CE2   1 
ATOM   7982  C  CZ    . TYR B 1 302 ? 107.290 135.644 129.382 1.00 34.48 ?  302 TYR B CZ    1 
ATOM   7983  O  OH    . TYR B 1 302 ? 107.148 134.313 129.063 1.00 34.45 ?  302 TYR B OH    1 
ATOM   7984  N  N     . PRO B 1 303 ? 109.616 141.846 132.548 1.00 26.70 ?  303 PRO B N     1 
ATOM   7985  C  CA    . PRO B 1 303 ? 109.906 143.242 132.918 1.00 30.11 ?  303 PRO B CA    1 
ATOM   7986  C  C     . PRO B 1 303 ? 109.845 144.224 131.762 1.00 28.10 ?  303 PRO B C     1 
ATOM   7987  O  O     . PRO B 1 303 ? 109.465 145.383 131.974 1.00 33.19 ?  303 PRO B O     1 
ATOM   7988  C  CB    . PRO B 1 303 ? 111.321 143.154 133.505 1.00 29.93 ?  303 PRO B CB    1 
ATOM   7989  C  CG    . PRO B 1 303 ? 111.449 141.750 133.956 1.00 27.96 ?  303 PRO B CG    1 
ATOM   7990  C  CD    . PRO B 1 303 ? 110.695 140.934 132.955 1.00 23.22 ?  303 PRO B CD    1 
ATOM   7991  N  N     . HIS B 1 304 ? 110.215 143.810 130.550 1.00 29.44 ?  304 HIS B N     1 
ATOM   7992  C  CA    . HIS B 1 304 ? 110.245 144.762 129.444 1.00 27.98 ?  304 HIS B CA    1 
ATOM   7993  C  C     . HIS B 1 304 ? 108.845 145.192 129.031 1.00 34.11 ?  304 HIS B C     1 
ATOM   7994  O  O     . HIS B 1 304 ? 108.653 146.338 128.619 1.00 41.97 ?  304 HIS B O     1 
ATOM   7995  C  CB    . HIS B 1 304 ? 110.994 144.179 128.249 1.00 29.58 ?  304 HIS B CB    1 
ATOM   7996  C  CG    . HIS B 1 304 ? 111.321 145.195 127.199 1.00 33.21 ?  304 HIS B CG    1 
ATOM   7997  N  ND1   . HIS B 1 304 ? 111.900 146.409 127.496 1.00 33.55 ?  304 HIS B ND1   1 
ATOM   7998  C  CD2   . HIS B 1 304 ? 111.139 145.183 125.859 1.00 34.93 ?  304 HIS B CD2   1 
ATOM   7999  C  CE1   . HIS B 1 304 ? 112.068 147.099 126.383 1.00 32.26 ?  304 HIS B CE1   1 
ATOM   8000  N  NE2   . HIS B 1 304 ? 111.613 146.378 125.375 1.00 34.44 ?  304 HIS B NE2   1 
ATOM   8001  N  N     . THR B 1 305 ? 107.859 144.299 129.135 1.00 33.07 ?  305 THR B N     1 
ATOM   8002  C  CA    . THR B 1 305 ? 106.483 144.697 128.863 1.00 32.53 ?  305 THR B CA    1 
ATOM   8003  C  C     . THR B 1 305 ? 106.015 145.758 129.850 1.00 29.67 ?  305 THR B C     1 
ATOM   8004  O  O     . THR B 1 305 ? 105.359 146.732 129.464 1.00 35.87 ?  305 THR B O     1 
ATOM   8005  C  CB    . THR B 1 305 ? 105.564 143.477 128.908 1.00 31.15 ?  305 THR B CB    1 
ATOM   8006  O  OG1   . THR B 1 305 ? 105.465 143.002 130.255 1.00 29.56 ?  305 THR B OG1   1 
ATOM   8007  C  CG2   . THR B 1 305 ? 106.115 142.373 128.026 1.00 31.52 ?  305 THR B CG2   1 
ATOM   8008  N  N     . ILE B 1 306 ? 106.356 145.591 131.129 1.00 35.97 ?  306 ILE B N     1 
ATOM   8009  C  CA    . ILE B 1 306 ? 105.996 146.583 132.136 1.00 29.61 ?  306 ILE B CA    1 
ATOM   8010  C  C     . ILE B 1 306 ? 106.701 147.905 131.860 1.00 28.38 ?  306 ILE B C     1 
ATOM   8011  O  O     . ILE B 1 306 ? 106.101 148.980 131.975 1.00 35.85 ?  306 ILE B O     1 
ATOM   8012  C  CB    . ILE B 1 306 ? 106.318 146.047 133.542 1.00 27.13 ?  306 ILE B CB    1 
ATOM   8013  C  CG1   . ILE B 1 306 ? 105.288 144.994 133.950 1.00 27.32 ?  306 ILE B CG1   1 
ATOM   8014  C  CG2   . ILE B 1 306 ? 106.364 147.178 134.558 1.00 30.70 ?  306 ILE B CG2   1 
ATOM   8015  C  CD1   . ILE B 1 306 ? 105.604 144.305 135.242 1.00 29.91 ?  306 ILE B CD1   1 
ATOM   8016  N  N     . TYR B 1 307 ? 107.981 147.847 131.491 1.00 30.49 ?  307 TYR B N     1 
ATOM   8017  C  CA    . TYR B 1 307 ? 108.720 149.067 131.185 1.00 31.96 ?  307 TYR B CA    1 
ATOM   8018  C  C     . TYR B 1 307 ? 108.125 149.789 129.982 1.00 35.66 ?  307 TYR B C     1 
ATOM   8019  O  O     . TYR B 1 307 ? 108.040 151.021 129.966 1.00 39.51 ?  307 TYR B O     1 
ATOM   8020  C  CB    . TYR B 1 307 ? 110.193 148.743 130.941 1.00 26.23 ?  307 TYR B CB    1 
ATOM   8021  C  CG    . TYR B 1 307 ? 111.044 149.961 130.689 1.00 35.96 ?  307 TYR B CG    1 
ATOM   8022  C  CD1   . TYR B 1 307 ? 111.463 150.766 131.738 1.00 31.13 ?  307 TYR B CD1   1 
ATOM   8023  C  CD2   . TYR B 1 307 ? 111.424 150.311 129.401 1.00 37.14 ?  307 TYR B CD2   1 
ATOM   8024  C  CE1   . TYR B 1 307 ? 112.240 151.882 131.511 1.00 31.45 ?  307 TYR B CE1   1 
ATOM   8025  C  CE2   . TYR B 1 307 ? 112.200 151.425 129.166 1.00 36.70 ?  307 TYR B CE2   1 
ATOM   8026  C  CZ    . TYR B 1 307 ? 112.605 152.207 130.224 1.00 37.64 ?  307 TYR B CZ    1 
ATOM   8027  O  OH    . TYR B 1 307 ? 113.379 153.319 129.992 1.00 40.14 ?  307 TYR B OH    1 
ATOM   8028  N  N     . LYS B 1 308 ? 107.721 149.036 128.958 1.00 39.05 ?  308 LYS B N     1 
ATOM   8029  C  CA    . LYS B 1 308 ? 107.112 149.647 127.781 1.00 32.40 ?  308 LYS B CA    1 
ATOM   8030  C  C     . LYS B 1 308 ? 105.747 150.240 128.106 1.00 28.74 ?  308 LYS B C     1 
ATOM   8031  O  O     . LYS B 1 308 ? 105.386 151.301 127.584 1.00 37.26 ?  308 LYS B O     1 
ATOM   8032  C  CB    . LYS B 1 308 ? 106.993 148.613 126.663 1.00 32.55 ?  308 LYS B CB    1 
ATOM   8033  C  CG    . LYS B 1 308 ? 108.205 148.539 125.752 1.00 33.55 ?  308 LYS B CG    1 
ATOM   8034  C  CD    . LYS B 1 308 ? 108.326 147.175 125.083 1.00 37.52 ?  308 LYS B CD    1 
ATOM   8035  C  CE    . LYS B 1 308 ? 106.975 146.490 124.935 1.00 38.18 ?  308 LYS B CE    1 
ATOM   8036  N  NZ    . LYS B 1 308 ? 107.102 145.009 124.871 1.00 39.44 1  308 LYS B NZ    1 
ATOM   8037  N  N     . GLU B 1 309 ? 104.976 149.571 128.963 1.00 30.88 ?  309 GLU B N     1 
ATOM   8038  C  CA    . GLU B 1 309 ? 103.627 150.040 129.258 1.00 35.01 ?  309 GLU B CA    1 
ATOM   8039  C  C     . GLU B 1 309 ? 103.637 151.261 130.170 1.00 39.29 ?  309 GLU B C     1 
ATOM   8040  O  O     . GLU B 1 309 ? 102.848 152.192 129.976 1.00 42.53 ?  309 GLU B O     1 
ATOM   8041  C  CB    . GLU B 1 309 ? 102.810 148.910 129.883 1.00 31.66 ?  309 GLU B CB    1 
ATOM   8042  C  CG    . GLU B 1 309 ? 101.415 149.316 130.322 1.00 37.92 ?  309 GLU B CG    1 
ATOM   8043  C  CD    . GLU B 1 309 ? 100.513 149.682 129.161 1.00 44.26 ?  309 GLU B CD    1 
ATOM   8044  O  OE1   . GLU B 1 309 ? 100.861 149.361 128.005 1.00 44.90 ?  309 GLU B OE1   1 
ATOM   8045  O  OE2   . GLU B 1 309 ? 99.453  150.295 129.405 1.00 42.88 -1 309 GLU B OE2   1 
ATOM   8046  N  N     . TYR B 1 310 ? 104.519 151.280 131.170 1.00 38.41 ?  310 TYR B N     1 
ATOM   8047  C  CA    . TYR B 1 310 ? 104.481 152.308 132.200 1.00 32.71 ?  310 TYR B CA    1 
ATOM   8048  C  C     . TYR B 1 310 ? 105.671 153.256 132.176 1.00 31.48 ?  310 TYR B C     1 
ATOM   8049  O  O     . TYR B 1 310 ? 105.651 154.256 132.900 1.00 37.24 ?  310 TYR B O     1 
ATOM   8050  C  CB    . TYR B 1 310 ? 104.385 151.656 133.587 1.00 34.92 ?  310 TYR B CB    1 
ATOM   8051  C  CG    . TYR B 1 310 ? 103.174 150.771 133.753 1.00 35.19 ?  310 TYR B CG    1 
ATOM   8052  C  CD1   . TYR B 1 310 ? 101.937 151.310 134.077 1.00 31.87 ?  310 TYR B CD1   1 
ATOM   8053  C  CD2   . TYR B 1 310 ? 103.262 149.398 133.571 1.00 30.33 ?  310 TYR B CD2   1 
ATOM   8054  C  CE1   . TYR B 1 310 ? 100.826 150.507 134.223 1.00 34.98 ?  310 TYR B CE1   1 
ATOM   8055  C  CE2   . TYR B 1 310 ? 102.156 148.588 133.713 1.00 31.20 ?  310 TYR B CE2   1 
ATOM   8056  C  CZ    . TYR B 1 310 ? 100.942 149.147 134.040 1.00 35.71 ?  310 TYR B CZ    1 
ATOM   8057  O  OH    . TYR B 1 310 ? 99.837  148.343 134.184 1.00 36.16 ?  310 TYR B OH    1 
ATOM   8058  N  N     . GLY B 1 311 ? 106.697 152.977 131.378 1.00 27.99 ?  311 GLY B N     1 
ATOM   8059  C  CA    . GLY B 1 311 ? 107.882 153.805 131.380 1.00 30.48 ?  311 GLY B CA    1 
ATOM   8060  C  C     . GLY B 1 311 ? 108.764 153.647 132.596 1.00 31.62 ?  311 GLY B C     1 
ATOM   8061  O  O     . GLY B 1 311 ? 109.761 154.368 132.714 1.00 40.98 ?  311 GLY B O     1 
ATOM   8062  N  N     . GLN B 1 312 ? 108.429 152.734 133.502 1.00 31.69 ?  312 GLN B N     1 
ATOM   8063  C  CA    . GLN B 1 312 ? 109.210 152.480 134.700 1.00 30.03 ?  312 GLN B CA    1 
ATOM   8064  C  C     . GLN B 1 312 ? 109.514 150.995 134.789 1.00 31.15 ?  312 GLN B C     1 
ATOM   8065  O  O     . GLN B 1 312 ? 108.731 150.158 134.333 1.00 39.00 ?  312 GLN B O     1 
ATOM   8066  C  CB    . GLN B 1 312 ? 108.468 152.930 135.964 1.00 34.29 ?  312 GLN B CB    1 
ATOM   8067  C  CG    . GLN B 1 312 ? 108.025 154.378 135.945 1.00 37.13 ?  312 GLN B CG    1 
ATOM   8068  C  CD    . GLN B 1 312 ? 106.962 154.668 136.984 1.00 39.55 ?  312 GLN B CD    1 
ATOM   8069  O  OE1   . GLN B 1 312 ? 105.776 154.750 136.668 1.00 38.28 ?  312 GLN B OE1   1 
ATOM   8070  N  NE2   . GLN B 1 312 ? 107.383 154.822 138.232 1.00 37.71 ?  312 GLN B NE2   1 
ATOM   8071  N  N     . HIS B 1 313 ? 110.661 150.675 135.378 1.00 28.09 ?  313 HIS B N     1 
ATOM   8072  C  CA    . HIS B 1 313 ? 111.027 149.283 135.584 1.00 28.27 ?  313 HIS B CA    1 
ATOM   8073  C  C     . HIS B 1 313 ? 110.092 148.631 136.595 1.00 32.03 ?  313 HIS B C     1 
ATOM   8074  O  O     . HIS B 1 313 ? 109.552 149.285 137.488 1.00 34.17 ?  313 HIS B O     1 
ATOM   8075  C  CB    . HIS B 1 313 ? 112.474 149.177 136.060 1.00 26.18 ?  313 HIS B CB    1 
ATOM   8076  C  CG    . HIS B 1 313 ? 113.479 149.567 135.024 1.00 27.23 ?  313 HIS B CG    1 
ATOM   8077  N  ND1   . HIS B 1 313 ? 113.758 148.783 133.925 1.00 30.43 ?  313 HIS B ND1   1 
ATOM   8078  C  CD2   . HIS B 1 313 ? 114.277 150.656 134.920 1.00 28.25 ?  313 HIS B CD2   1 
ATOM   8079  C  CE1   . HIS B 1 313 ? 114.682 149.374 133.188 1.00 27.83 ?  313 HIS B CE1   1 
ATOM   8080  N  NE2   . HIS B 1 313 ? 115.014 150.511 133.770 1.00 32.42 ?  313 HIS B NE2   1 
ATOM   8081  N  N     . MET B 1 314 ? 109.901 147.321 136.438 1.00 34.99 ?  314 MET B N     1 
ATOM   8082  C  CA    . MET B 1 314 ? 108.999 146.595 137.325 1.00 29.03 ?  314 MET B CA    1 
ATOM   8083  C  C     . MET B 1 314 ? 109.498 146.629 138.765 1.00 34.23 ?  314 MET B C     1 
ATOM   8084  O  O     . MET B 1 314 ? 108.702 146.755 139.702 1.00 38.94 ?  314 MET B O     1 
ATOM   8085  C  CB    . MET B 1 314 ? 108.831 145.156 136.836 1.00 26.60 ?  314 MET B CB    1 
ATOM   8086  C  CG    . MET B 1 314 ? 108.299 144.188 137.874 1.00 27.15 ?  314 MET B CG    1 
ATOM   8087  S  SD    . MET B 1 314 ? 108.690 142.476 137.474 1.00 43.44 ?  314 MET B SD    1 
ATOM   8088  C  CE    . MET B 1 314 ? 110.350 142.344 138.133 1.00 34.29 ?  314 MET B CE    1 
ATOM   8089  N  N     . ASP B 1 315 ? 110.812 146.525 138.961 1.00 34.31 ?  315 ASP B N     1 
ATOM   8090  C  CA    . ASP B 1 315 ? 111.375 146.592 140.303 1.00 34.44 ?  315 ASP B CA    1 
ATOM   8091  C  C     . ASP B 1 315 ? 111.481 148.015 140.841 1.00 28.83 ?  315 ASP B C     1 
ATOM   8092  O  O     . ASP B 1 315 ? 111.794 148.191 142.023 1.00 38.87 ?  315 ASP B O     1 
ATOM   8093  C  CB    . ASP B 1 315 ? 112.734 145.865 140.336 1.00 29.64 ?  315 ASP B CB    1 
ATOM   8094  C  CG    . ASP B 1 315 ? 113.907 146.710 139.830 1.00 33.54 ?  315 ASP B CG    1 
ATOM   8095  O  OD1   . ASP B 1 315 ? 113.737 147.867 139.395 1.00 40.00 ?  315 ASP B OD1   1 
ATOM   8096  O  OD2   . ASP B 1 315 ? 115.042 146.192 139.881 1.00 35.00 -1 315 ASP B OD2   1 
ATOM   8097  N  N     . GLU B 1 316 ? 111.227 149.025 140.010 1.00 24.99 ?  316 GLU B N     1 
ATOM   8098  C  CA    . GLU B 1 316 ? 111.160 150.406 140.465 1.00 27.13 ?  316 GLU B CA    1 
ATOM   8099  C  C     . GLU B 1 316 ? 109.787 150.787 141.000 1.00 35.65 ?  316 GLU B C     1 
ATOM   8100  O  O     . GLU B 1 316 ? 109.631 151.896 141.522 1.00 35.99 ?  316 GLU B O     1 
ATOM   8101  C  CB    . GLU B 1 316 ? 111.538 151.354 139.325 1.00 31.43 ?  316 GLU B CB    1 
ATOM   8102  C  CG    . GLU B 1 316 ? 112.454 152.488 139.736 1.00 34.63 ?  316 GLU B CG    1 
ATOM   8103  C  CD    . GLU B 1 316 ? 113.850 152.016 140.059 1.00 39.24 ?  316 GLU B CD    1 
ATOM   8104  O  OE1   . GLU B 1 316 ? 114.308 151.045 139.425 1.00 40.91 ?  316 GLU B OE1   1 
ATOM   8105  O  OE2   . GLU B 1 316 ? 114.492 152.618 140.946 1.00 38.33 -1 316 GLU B OE2   1 
ATOM   8106  N  N     . MET B 1 317 ? 108.800 149.906 140.886 1.00 38.87 ?  317 MET B N     1 
ATOM   8107  C  CA    . MET B 1 317 ? 107.430 150.196 141.273 1.00 34.88 ?  317 MET B CA    1 
ATOM   8108  C  C     . MET B 1 317 ? 107.017 149.342 142.465 1.00 38.69 ?  317 MET B C     1 
ATOM   8109  O  O     . MET B 1 317 ? 107.585 148.279 142.728 1.00 39.26 ?  317 MET B O     1 
ATOM   8110  C  CB    . MET B 1 317 ? 106.473 149.958 140.100 1.00 35.43 ?  317 MET B CB    1 
ATOM   8111  C  CG    . MET B 1 317 ? 106.918 150.619 138.807 1.00 37.07 ?  317 MET B CG    1 
ATOM   8112  S  SD    . MET B 1 317 ? 106.285 149.790 137.342 1.00 48.33 ?  317 MET B SD    1 
ATOM   8113  C  CE    . MET B 1 317 ? 104.781 150.717 137.070 1.00 39.01 ?  317 MET B CE    1 
ATOM   8114  N  N     . ASP B 1 318 ? 106.009 149.828 143.185 1.00 40.07 ?  318 ASP B N     1 
ATOM   8115  C  CA    . ASP B 1 318 ? 105.501 149.141 144.367 1.00 37.58 ?  318 ASP B CA    1 
ATOM   8116  C  C     . ASP B 1 318 ? 104.579 148.014 143.921 1.00 42.08 ?  318 ASP B C     1 
ATOM   8117  O  O     . ASP B 1 318 ? 103.486 148.265 143.406 1.00 44.38 ?  318 ASP B O     1 
ATOM   8118  C  CB    . ASP B 1 318 ? 104.769 150.124 145.278 1.00 39.27 ?  318 ASP B CB    1 
ATOM   8119  C  CG    . ASP B 1 318 ? 104.371 149.507 146.601 1.00 49.10 ?  318 ASP B CG    1 
ATOM   8120  O  OD1   . ASP B 1 318 ? 105.112 148.635 147.102 1.00 46.36 ?  318 ASP B OD1   1 
ATOM   8121  O  OD2   . ASP B 1 318 ? 103.315 149.894 147.142 1.00 50.01 -1 318 ASP B OD2   1 
ATOM   8122  N  N     . MET B 1 319 ? 105.017 146.769 144.124 1.00 40.62 ?  319 MET B N     1 
ATOM   8123  C  CA    . MET B 1 319 ? 104.224 145.628 143.682 1.00 35.55 ?  319 MET B CA    1 
ATOM   8124  C  C     . MET B 1 319 ? 102.907 145.519 144.439 1.00 36.85 ?  319 MET B C     1 
ATOM   8125  O  O     . MET B 1 319 ? 101.937 144.972 143.906 1.00 42.15 ?  319 MET B O     1 
ATOM   8126  C  CB    . MET B 1 319 ? 105.025 144.337 143.836 1.00 35.05 ?  319 MET B CB    1 
ATOM   8127  C  CG    . MET B 1 319 ? 104.505 143.190 142.987 1.00 37.88 ?  319 MET B CG    1 
ATOM   8128  S  SD    . MET B 1 319 ? 104.596 143.520 141.219 1.00 47.61 ?  319 MET B SD    1 
ATOM   8129  C  CE    . MET B 1 319 ? 106.368 143.601 140.988 1.00 41.96 ?  319 MET B CE    1 
ATOM   8130  N  N     . ASN B 1 320 ? 102.845 146.047 145.662 1.00 39.09 ?  320 ASN B N     1 
ATOM   8131  C  CA    . ASN B 1 320 ? 101.613 145.959 146.439 1.00 39.65 ?  320 ASN B CA    1 
ATOM   8132  C  C     . ASN B 1 320 ? 100.474 146.710 145.760 1.00 46.07 ?  320 ASN B C     1 
ATOM   8133  O  O     . ASN B 1 320 ? 99.329  146.242 145.754 1.00 46.18 ?  320 ASN B O     1 
ATOM   8134  C  CB    . ASN B 1 320 ? 101.848 146.490 147.853 1.00 40.73 ?  320 ASN B CB    1 
ATOM   8135  C  CG    . ASN B 1 320 ? 102.926 145.719 148.589 1.00 43.14 ?  320 ASN B CG    1 
ATOM   8136  O  OD1   . ASN B 1 320 ? 102.755 144.543 148.905 1.00 42.76 ?  320 ASN B OD1   1 
ATOM   8137  N  ND2   . ASN B 1 320 ? 104.044 146.380 148.862 1.00 43.71 ?  320 ASN B ND2   1 
ATOM   8138  N  N     . GLU B 1 321 ? 100.766 147.873 145.182 1.00 46.25 ?  321 GLU B N     1 
ATOM   8139  C  CA    . GLU B 1 321 ? 99.751  148.630 144.461 1.00 44.91 ?  321 GLU B CA    1 
ATOM   8140  C  C     . GLU B 1 321 ? 99.728  148.320 142.971 1.00 43.62 ?  321 GLU B C     1 
ATOM   8141  O  O     . GLU B 1 321 ? 98.681  148.468 142.331 1.00 45.23 ?  321 GLU B O     1 
ATOM   8142  C  CB    . GLU B 1 321 ? 99.968  150.133 144.659 1.00 43.47 ?  321 GLU B CB    1 
ATOM   8143  C  CG    . GLU B 1 321 ? 101.302 150.643 144.141 1.00 47.11 ?  321 GLU B CG    1 
ATOM   8144  C  CD    . GLU B 1 321 ? 101.197 152.017 143.509 1.00 51.86 ?  321 GLU B CD    1 
ATOM   8145  O  OE1   . GLU B 1 321 ? 100.061 152.490 143.294 1.00 49.66 ?  321 GLU B OE1   1 
ATOM   8146  O  OE2   . GLU B 1 321 ? 102.251 152.624 143.225 1.00 51.96 -1 321 GLU B OE2   1 
ATOM   8147  N  N     . MET B 1 322 ? 100.854 147.892 142.404 1.00 40.70 ?  322 MET B N     1 
ATOM   8148  C  CA    . MET B 1 322 ? 100.962 147.704 140.966 1.00 35.62 ?  322 MET B CA    1 
ATOM   8149  C  C     . MET B 1 322 ? 100.670 146.283 140.506 1.00 37.11 ?  322 MET B C     1 
ATOM   8150  O  O     . MET B 1 322 ? 100.580 146.059 139.298 1.00 47.12 ?  322 MET B O     1 
ATOM   8151  C  CB    . MET B 1 322 ? 102.363 148.100 140.483 1.00 35.35 ?  322 MET B CB    1 
ATOM   8152  C  CG    . MET B 1 322 ? 102.585 149.596 140.351 1.00 39.64 ?  322 MET B CG    1 
ATOM   8153  S  SD    . MET B 1 322 ? 101.095 150.485 139.875 1.00 50.65 ?  322 MET B SD    1 
ATOM   8154  C  CE    . MET B 1 322 ? 101.162 150.323 138.094 1.00 39.32 ?  322 MET B CE    1 
ATOM   8155  N  N     . TYR B 1 323 ? 100.523 145.321 141.420 1.00 37.53 ?  323 TYR B N     1 
ATOM   8156  C  CA    . TYR B 1 323 ? 100.361 143.931 141.001 1.00 33.11 ?  323 TYR B CA    1 
ATOM   8157  C  C     . TYR B 1 323 ? 99.033  143.721 140.284 1.00 40.15 ?  323 TYR B C     1 
ATOM   8158  O  O     . TYR B 1 323 ? 98.979  143.072 139.233 1.00 43.00 ?  323 TYR B O     1 
ATOM   8159  C  CB    . TYR B 1 323 ? 100.475 143.003 142.210 1.00 34.53 ?  323 TYR B CB    1 
ATOM   8160  C  CG    . TYR B 1 323 ? 100.214 141.546 141.894 1.00 37.76 ?  323 TYR B CG    1 
ATOM   8161  C  CD1   . TYR B 1 323 ? 101.217 140.739 141.377 1.00 31.61 ?  323 TYR B CD1   1 
ATOM   8162  C  CD2   . TYR B 1 323 ? 98.966  140.979 142.116 1.00 37.36 ?  323 TYR B CD2   1 
ATOM   8163  C  CE1   . TYR B 1 323 ? 100.983 139.411 141.088 1.00 28.11 ?  323 TYR B CE1   1 
ATOM   8164  C  CE2   . TYR B 1 323 ? 98.724  139.652 141.829 1.00 33.00 ?  323 TYR B CE2   1 
ATOM   8165  C  CZ    . TYR B 1 323 ? 99.736  138.874 141.317 1.00 32.57 ?  323 TYR B CZ    1 
ATOM   8166  O  OH    . TYR B 1 323 ? 99.499  137.552 141.030 1.00 38.21 ?  323 TYR B OH    1 
ATOM   8167  N  N     . ASP B 1 324 ? 97.948  144.261 140.842 1.00 43.32 ?  324 ASP B N     1 
ATOM   8168  C  CA    . ASP B 1 324 ? 96.644  144.119 140.205 1.00 38.89 ?  324 ASP B CA    1 
ATOM   8169  C  C     . ASP B 1 324 ? 96.609  144.834 138.862 1.00 41.91 ?  324 ASP B C     1 
ATOM   8170  O  O     . ASP B 1 324 ? 96.016  144.334 137.900 1.00 47.99 ?  324 ASP B O     1 
ATOM   8171  C  CB    . ASP B 1 324 ? 95.548  144.649 141.128 1.00 42.11 ?  324 ASP B CB    1 
ATOM   8172  C  CG    . ASP B 1 324 ? 95.384  143.808 142.376 1.00 45.33 ?  324 ASP B CG    1 
ATOM   8173  O  OD1   . ASP B 1 324 ? 95.529  142.572 142.283 1.00 45.34 ?  324 ASP B OD1   1 
ATOM   8174  O  OD2   . ASP B 1 324 ? 95.110  144.382 143.450 1.00 46.45 -1 324 ASP B OD2   1 
ATOM   8175  N  N     . LYS B 1 325 ? 97.237  146.008 138.779 1.00 42.05 ?  325 LYS B N     1 
ATOM   8176  C  CA    . LYS B 1 325 ? 97.297  146.728 137.511 1.00 41.84 ?  325 LYS B CA    1 
ATOM   8177  C  C     . LYS B 1 325 ? 98.100  145.955 136.474 1.00 41.15 ?  325 LYS B C     1 
ATOM   8178  O  O     . LYS B 1 325 ? 97.730  145.921 135.295 1.00 46.54 ?  325 LYS B O     1 
ATOM   8179  C  CB    . LYS B 1 325 ? 97.887  148.120 137.728 1.00 39.41 ?  325 LYS B CB    1 
ATOM   8180  C  CG    . LYS B 1 325 ? 97.126  148.950 138.745 1.00 38.15 ?  325 LYS B CG    1 
ATOM   8181  C  CD    . LYS B 1 325 ? 97.013  150.400 138.306 1.00 43.84 ?  325 LYS B CD    1 
ATOM   8182  C  CE    . LYS B 1 325 ? 97.651  151.338 139.315 1.00 44.36 ?  325 LYS B CE    1 
ATOM   8183  N  NZ    . LYS B 1 325 ? 96.910  151.350 140.606 1.00 46.04 1  325 LYS B NZ    1 
ATOM   8184  N  N     . PHE B 1 326 ? 99.206  145.336 136.890 1.00 39.33 ?  326 PHE B N     1 
ATOM   8185  C  CA    . PHE B 1 326 ? 99.988  144.512 135.974 1.00 36.16 ?  326 PHE B CA    1 
ATOM   8186  C  C     . PHE B 1 326 ? 99.176  143.325 135.479 1.00 36.41 ?  326 PHE B C     1 
ATOM   8187  O  O     . PHE B 1 326 ? 99.190  143.008 134.285 1.00 44.28 ?  326 PHE B O     1 
ATOM   8188  C  CB    . PHE B 1 326 ? 101.263 144.020 136.661 1.00 34.73 ?  326 PHE B CB    1 
ATOM   8189  C  CG    . PHE B 1 326 ? 102.252 145.103 136.977 1.00 32.72 ?  326 PHE B CG    1 
ATOM   8190  C  CD1   . PHE B 1 326 ? 102.156 146.351 136.390 1.00 34.49 ?  326 PHE B CD1   1 
ATOM   8191  C  CD2   . PHE B 1 326 ? 103.286 144.866 137.867 1.00 36.10 ?  326 PHE B CD2   1 
ATOM   8192  C  CE1   . PHE B 1 326 ? 103.070 147.340 136.687 1.00 33.27 ?  326 PHE B CE1   1 
ATOM   8193  C  CE2   . PHE B 1 326 ? 104.202 145.850 138.164 1.00 39.21 ?  326 PHE B CE2   1 
ATOM   8194  C  CZ    . PHE B 1 326 ? 104.094 147.089 137.572 1.00 39.45 ?  326 PHE B CZ    1 
ATOM   8195  N  N     . VAL B 1 327 ? 98.461  142.655 136.387 1.00 40.83 ?  327 VAL B N     1 
ATOM   8196  C  CA    . VAL B 1 327 ? 97.695  141.472 136.010 1.00 43.25 ?  327 VAL B CA    1 
ATOM   8197  C  C     . VAL B 1 327 ? 96.550  141.848 135.076 1.00 43.55 ?  327 VAL B C     1 
ATOM   8198  O  O     . VAL B 1 327 ? 96.290  141.159 134.081 1.00 45.72 ?  327 VAL B O     1 
ATOM   8199  C  CB    . VAL B 1 327 ? 97.189  140.741 137.267 1.00 37.68 ?  327 VAL B CB    1 
ATOM   8200  C  CG1   . VAL B 1 327 ? 96.216  139.640 136.890 1.00 40.71 ?  327 VAL B CG1   1 
ATOM   8201  C  CG2   . VAL B 1 327 ? 98.357  140.168 138.049 1.00 31.33 ?  327 VAL B CG2   1 
ATOM   8202  N  N     . ASP B 1 328 ? 95.857  142.947 135.367 1.00 44.04 ?  328 ASP B N     1 
ATOM   8203  C  CA    . ASP B 1 328 ? 94.726  143.371 134.553 1.00 45.35 ?  328 ASP B CA    1 
ATOM   8204  C  C     . ASP B 1 328 ? 95.142  144.061 133.263 1.00 45.87 ?  328 ASP B C     1 
ATOM   8205  O  O     . ASP B 1 328 ? 94.284  144.297 132.406 1.00 49.89 ?  328 ASP B O     1 
ATOM   8206  C  CB    . ASP B 1 328 ? 93.817  144.302 135.358 1.00 45.98 ?  328 ASP B CB    1 
ATOM   8207  C  CG    . ASP B 1 328 ? 93.016  143.564 136.410 1.00 52.99 ?  328 ASP B CG    1 
ATOM   8208  O  OD1   . ASP B 1 328 ? 92.937  142.321 136.333 1.00 52.45 ?  328 ASP B OD1   1 
ATOM   8209  O  OD2   . ASP B 1 328 ? 92.466  144.228 137.314 1.00 51.64 -1 328 ASP B OD2   1 
ATOM   8210  N  N     . ASN B 1 329 ? 96.416  144.394 133.103 1.00 40.44 ?  329 ASN B N     1 
ATOM   8211  C  CA    . ASN B 1 329 ? 96.872  145.045 131.883 1.00 39.47 ?  329 ASN B CA    1 
ATOM   8212  C  C     . ASN B 1 329 ? 97.102  144.001 130.798 1.00 47.37 ?  329 ASN B C     1 
ATOM   8213  O  O     . ASN B 1 329 ? 97.963  143.130 130.965 1.00 44.71 ?  329 ASN B O     1 
ATOM   8214  C  CB    . ASN B 1 329 ? 98.153  145.825 132.138 1.00 36.96 ?  329 ASN B CB    1 
ATOM   8215  C  CG    . ASN B 1 329 ? 98.369  146.936 131.131 1.00 42.80 ?  329 ASN B CG    1 
ATOM   8216  O  OD1   . ASN B 1 329 ? 98.733  146.686 129.984 1.00 47.29 ?  329 ASN B OD1   1 
ATOM   8217  N  ND2   . ASN B 1 329 ? 98.145  148.172 131.558 1.00 40.27 ?  329 ASN B ND2   1 
ATOM   8218  N  N     . PRO B 1 330 ? 96.361  144.042 129.687 1.00 49.24 ?  330 PRO B N     1 
ATOM   8219  C  CA    . PRO B 1 330 ? 96.605  143.071 128.609 1.00 43.76 ?  330 PRO B CA    1 
ATOM   8220  C  C     . PRO B 1 330 ? 97.947  143.247 127.926 1.00 41.32 ?  330 PRO B C     1 
ATOM   8221  O  O     . PRO B 1 330 ? 98.465  142.276 127.360 1.00 44.94 ?  330 PRO B O     1 
ATOM   8222  C  CB    . PRO B 1 330 ? 95.447  143.327 127.638 1.00 46.22 ?  330 PRO B CB    1 
ATOM   8223  C  CG    . PRO B 1 330 ? 95.052  144.738 127.896 1.00 43.83 ?  330 PRO B CG    1 
ATOM   8224  C  CD    . PRO B 1 330 ? 95.262  144.965 129.362 1.00 42.32 ?  330 PRO B CD    1 
ATOM   8225  N  N     . ARG B 1 331 ? 98.525  144.446 127.957 1.00 39.59 ?  331 ARG B N     1 
ATOM   8226  C  CA    . ARG B 1 331 ? 99.806  144.701 127.314 1.00 42.99 ?  331 ARG B CA    1 
ATOM   8227  C  C     . ARG B 1 331 ? 100.992 144.286 128.175 1.00 42.42 ?  331 ARG B C     1 
ATOM   8228  O  O     . ARG B 1 331 ? 102.133 144.362 127.707 1.00 41.85 ?  331 ARG B O     1 
ATOM   8229  C  CB    . ARG B 1 331 ? 99.917  146.183 126.948 1.00 40.58 ?  331 ARG B CB    1 
ATOM   8230  C  CG    . ARG B 1 331 ? 98.766  146.683 126.092 1.00 41.00 ?  331 ARG B CG    1 
ATOM   8231  C  CD    . ARG B 1 331 ? 98.771  148.203 125.978 1.00 41.46 ?  331 ARG B CD    1 
ATOM   8232  N  NE    . ARG B 1 331 ? 98.037  148.893 127.037 1.00 41.04 ?  331 ARG B NE    1 
ATOM   8233  C  CZ    . ARG B 1 331 ? 96.799  148.621 127.436 1.00 45.31 ?  331 ARG B CZ    1 
ATOM   8234  N  NH1   . ARG B 1 331 ? 96.046  147.724 126.820 1.00 45.36 1  331 ARG B NH1   1 
ATOM   8235  N  NH2   . ARG B 1 331 ? 96.291  149.290 128.467 1.00 42.03 ?  331 ARG B NH2   1 
ATOM   8236  N  N     . VAL B 1 332 ? 100.753 143.860 129.410 1.00 37.76 ?  332 VAL B N     1 
ATOM   8237  C  CA    . VAL B 1 332 ? 101.792 143.325 130.281 1.00 34.85 ?  332 VAL B CA    1 
ATOM   8238  C  C     . VAL B 1 332 ? 101.741 141.807 130.183 1.00 38.85 ?  332 VAL B C     1 
ATOM   8239  O  O     . VAL B 1 332 ? 100.694 141.196 130.425 1.00 40.26 ?  332 VAL B O     1 
ATOM   8240  C  CB    . VAL B 1 332 ? 101.609 143.796 131.732 1.00 35.51 ?  332 VAL B CB    1 
ATOM   8241  C  CG1   . VAL B 1 332 ? 102.457 142.960 132.673 1.00 37.32 ?  332 VAL B CG1   1 
ATOM   8242  C  CG2   . VAL B 1 332 ? 101.963 145.268 131.861 1.00 34.26 ?  332 VAL B CG2   1 
ATOM   8243  N  N     . LYS B 1 333 ? 102.864 141.197 129.817 1.00 34.79 ?  333 LYS B N     1 
ATOM   8244  C  CA    . LYS B 1 333 ? 102.934 139.753 129.645 1.00 31.33 ?  333 LYS B CA    1 
ATOM   8245  C  C     . LYS B 1 333 ? 103.293 139.079 130.963 1.00 34.52 ?  333 LYS B C     1 
ATOM   8246  O  O     . LYS B 1 333 ? 104.140 139.567 131.717 1.00 35.76 ?  333 LYS B O     1 
ATOM   8247  C  CB    . LYS B 1 333 ? 103.955 139.390 128.566 1.00 30.40 ?  333 LYS B CB    1 
ATOM   8248  C  CG    . LYS B 1 333 ? 103.819 137.975 128.037 1.00 37.96 ?  333 LYS B CG    1 
ATOM   8249  C  CD    . LYS B 1 333 ? 104.958 137.624 127.095 1.00 38.66 ?  333 LYS B CD    1 
ATOM   8250  C  CE    . LYS B 1 333 ? 104.887 136.171 126.663 1.00 38.80 ?  333 LYS B CE    1 
ATOM   8251  N  NZ    . LYS B 1 333 ? 105.985 135.817 125.724 1.00 40.45 1  333 LYS B NZ    1 
ATOM   8252  N  N     . LYS B 1 334 ? 102.639 137.951 131.236 1.00 37.10 ?  334 LYS B N     1 
ATOM   8253  C  CA    . LYS B 1 334 ? 102.826 137.239 132.491 1.00 32.47 ?  334 LYS B CA    1 
ATOM   8254  C  C     . LYS B 1 334 ? 102.515 135.765 132.280 1.00 35.58 ?  334 LYS B C     1 
ATOM   8255  O  O     . LYS B 1 334 ? 101.867 135.382 131.304 1.00 43.50 ?  334 LYS B O     1 
ATOM   8256  C  CB    . LYS B 1 334 ? 101.929 137.812 133.591 1.00 33.98 ?  334 LYS B CB    1 
ATOM   8257  C  CG    . LYS B 1 334 ? 100.456 137.820 133.220 1.00 35.77 ?  334 LYS B CG    1 
ATOM   8258  C  CD    . LYS B 1 334 ? 99.682  138.875 133.982 1.00 33.80 ?  334 LYS B CD    1 
ATOM   8259  C  CE    . LYS B 1 334 ? 99.515  140.129 133.150 1.00 37.85 ?  334 LYS B CE    1 
ATOM   8260  N  NZ    . LYS B 1 334 ? 98.522  139.958 132.055 1.00 37.62 1  334 LYS B NZ    1 
ATOM   8261  N  N     . GLU B 1 335 ? 102.995 134.934 133.207 1.00 38.13 ?  335 GLU B N     1 
ATOM   8262  C  CA    . GLU B 1 335 ? 102.575 133.542 133.290 1.00 43.58 ?  335 GLU B CA    1 
ATOM   8263  C  C     . GLU B 1 335 ? 102.166 133.216 134.717 1.00 41.91 ?  335 GLU B C     1 
ATOM   8264  O  O     . GLU B 1 335 ? 102.750 133.731 135.674 1.00 44.95 ?  335 GLU B O     1 
ATOM   8265  C  CB    . GLU B 1 335 ? 103.662 132.553 132.857 1.00 39.57 ?  335 GLU B CB    1 
ATOM   8266  C  CG    . GLU B 1 335 ? 105.083 133.001 133.057 1.00 40.04 ?  335 GLU B CG    1 
ATOM   8267  C  CD    . GLU B 1 335 ? 106.055 132.111 132.313 1.00 47.14 ?  335 GLU B CD    1 
ATOM   8268  O  OE1   . GLU B 1 335 ? 107.008 131.611 132.948 1.00 44.33 ?  335 GLU B OE1   1 
ATOM   8269  O  OE2   . GLU B 1 335 ? 105.865 131.904 131.095 1.00 46.65 -1 335 GLU B OE2   1 
ATOM   8270  N  N     . LYS B 1 336 ? 101.164 132.353 134.847 1.00 38.84 ?  336 LYS B N     1 
ATOM   8271  C  CA    . LYS B 1 336 ? 100.703 131.922 136.157 1.00 30.35 ?  336 LYS B CA    1 
ATOM   8272  C  C     . LYS B 1 336 ? 101.770 131.087 136.853 1.00 37.36 ?  336 LYS B C     1 
ATOM   8273  O  O     . LYS B 1 336 ? 102.455 130.275 136.226 1.00 40.56 ?  336 LYS B O     1 
ATOM   8274  C  CB    . LYS B 1 336 ? 99.417  131.108 136.021 1.00 40.33 ?  336 LYS B CB    1 
ATOM   8275  C  CG    . LYS B 1 336 ? 98.626  130.968 137.306 1.00 43.04 ?  336 LYS B CG    1 
ATOM   8276  C  CD    . LYS B 1 336 ? 97.682  132.139 137.482 1.00 44.70 ?  336 LYS B CD    1 
ATOM   8277  C  CE    . LYS B 1 336 ? 96.320  131.837 136.882 1.00 41.52 ?  336 LYS B CE    1 
ATOM   8278  N  NZ    . LYS B 1 336 ? 95.464  131.059 137.816 1.00 41.81 1  336 LYS B NZ    1 
ATOM   8279  N  N     . ILE B 1 337 ? 101.913 131.297 138.161 1.00 38.68 ?  337 ILE B N     1 
ATOM   8280  C  CA    . ILE B 1 337 ? 102.750 130.463 139.011 1.00 36.88 ?  337 ILE B CA    1 
ATOM   8281  C  C     . ILE B 1 337 ? 101.965 130.137 140.273 1.00 39.62 ?  337 ILE B C     1 
ATOM   8282  O  O     . ILE B 1 337 ? 100.949 130.760 140.581 1.00 45.76 ?  337 ILE B O     1 
ATOM   8283  C  CB    . ILE B 1 337 ? 104.093 131.131 139.374 1.00 35.97 ?  337 ILE B CB    1 
ATOM   8284  C  CG1   . ILE B 1 337 ? 103.850 132.478 140.056 1.00 37.24 ?  337 ILE B CG1   1 
ATOM   8285  C  CG2   . ILE B 1 337 ? 104.973 131.283 138.145 1.00 37.46 ?  337 ILE B CG2   1 
ATOM   8286  C  CD1   . ILE B 1 337 ? 104.864 132.815 141.121 1.00 33.60 ?  337 ILE B CD1   1 
ATOM   8287  N  N     . ASN B 1 338 ? 102.451 129.140 141.005 1.00 38.80 ?  338 ASN B N     1 
ATOM   8288  C  CA    . ASN B 1 338 ? 101.914 128.844 142.323 1.00 34.32 ?  338 ASN B CA    1 
ATOM   8289  C  C     . ASN B 1 338 ? 102.862 129.418 143.361 1.00 35.85 ?  338 ASN B C     1 
ATOM   8290  O  O     . ASN B 1 338 ? 103.977 128.900 143.518 1.00 42.95 ?  338 ASN B O     1 
ATOM   8291  C  CB    . ASN B 1 338 ? 101.748 127.340 142.520 1.00 35.42 ?  338 ASN B CB    1 
ATOM   8292  C  CG    . ASN B 1 338 ? 100.771 127.002 143.627 1.00 39.78 ?  338 ASN B CG    1 
ATOM   8293  O  OD1   . ASN B 1 338 ? 100.297 127.884 144.342 1.00 41.66 ?  338 ASN B OD1   1 
ATOM   8294  N  ND2   . ASN B 1 338 ? 100.462 125.720 143.773 1.00 39.95 ?  338 ASN B ND2   1 
ATOM   8295  N  N     . PRO B 1 339 ? 102.487 130.484 144.073 1.00 36.61 ?  339 PRO B N     1 
ATOM   8296  C  CA    . PRO B 1 339 ? 103.415 131.072 145.051 1.00 34.86 ?  339 PRO B CA    1 
ATOM   8297  C  C     . PRO B 1 339 ? 103.803 130.121 146.166 1.00 32.01 ?  339 PRO B C     1 
ATOM   8298  O  O     . PRO B 1 339 ? 104.942 130.182 146.647 1.00 36.23 ?  339 PRO B O     1 
ATOM   8299  C  CB    . PRO B 1 339 ? 102.640 132.285 145.581 1.00 33.12 ?  339 PRO B CB    1 
ATOM   8300  C  CG    . PRO B 1 339 ? 101.217 131.963 145.327 1.00 36.79 ?  339 PRO B CG    1 
ATOM   8301  C  CD    . PRO B 1 339 ? 101.192 131.183 144.052 1.00 36.01 ?  339 PRO B CD    1 
ATOM   8302  N  N     . ARG B 1 340 ? 102.897 129.243 146.597 1.00 33.55 ?  340 ARG B N     1 
ATOM   8303  C  CA    . ARG B 1 340 ? 103.254 128.262 147.616 1.00 32.24 ?  340 ARG B CA    1 
ATOM   8304  C  C     . ARG B 1 340 ? 104.249 127.247 147.072 1.00 33.47 ?  340 ARG B C     1 
ATOM   8305  O  O     . ARG B 1 340 ? 105.178 126.841 147.779 1.00 39.77 ?  340 ARG B O     1 
ATOM   8306  C  CB    . ARG B 1 340 ? 102.003 127.565 148.142 1.00 31.38 ?  340 ARG B CB    1 
ATOM   8307  C  CG    . ARG B 1 340 ? 101.167 128.434 149.054 1.00 29.58 ?  340 ARG B CG    1 
ATOM   8308  C  CD    . ARG B 1 340 ? 100.290 127.605 149.971 1.00 31.39 ?  340 ARG B CD    1 
ATOM   8309  N  NE    . ARG B 1 340 ? 99.353  128.443 150.709 1.00 33.49 ?  340 ARG B NE    1 
ATOM   8310  C  CZ    . ARG B 1 340 ? 98.473  127.988 151.588 1.00 35.94 ?  340 ARG B CZ    1 
ATOM   8311  N  NH1   . ARG B 1 340 ? 98.380  126.699 151.871 1.00 35.30 1  340 ARG B NH1   1 
ATOM   8312  N  NH2   . ARG B 1 340 ? 97.662  128.848 152.198 1.00 36.79 ?  340 ARG B NH2   1 
ATOM   8313  N  N     . LYS B 1 341 ? 104.072 126.826 145.820 1.00 34.62 ?  341 LYS B N     1 
ATOM   8314  C  CA    . LYS B 1 341 ? 105.046 125.933 145.204 1.00 33.59 ?  341 LYS B CA    1 
ATOM   8315  C  C     . LYS B 1 341 ? 106.395 126.620 145.046 1.00 30.60 ?  341 LYS B C     1 
ATOM   8316  O  O     . LYS B 1 341 ? 107.441 125.988 145.220 1.00 32.98 ?  341 LYS B O     1 
ATOM   8317  C  CB    . LYS B 1 341 ? 104.530 125.437 143.854 1.00 37.60 ?  341 LYS B CB    1 
ATOM   8318  C  CG    . LYS B 1 341 ? 103.485 124.334 143.948 1.00 38.96 ?  341 LYS B CG    1 
ATOM   8319  C  CD    . LYS B 1 341 ? 103.647 123.510 145.217 1.00 40.97 ?  341 LYS B CD    1 
ATOM   8320  C  CE    . LYS B 1 341 ? 102.689 122.332 145.239 1.00 41.70 ?  341 LYS B CE    1 
ATOM   8321  N  NZ    . LYS B 1 341 ? 103.396 121.056 145.536 1.00 40.34 1  341 LYS B NZ    1 
ATOM   8322  N  N     . LEU B 1 342 ? 106.393 127.914 144.722 1.00 32.33 ?  342 LEU B N     1 
ATOM   8323  C  CA    . LEU B 1 342 ? 107.648 128.654 144.644 1.00 29.16 ?  342 LEU B CA    1 
ATOM   8324  C  C     . LEU B 1 342 ? 108.317 128.755 146.010 1.00 29.99 ?  342 LEU B C     1 
ATOM   8325  O  O     . LEU B 1 342 ? 109.543 128.641 146.114 1.00 38.62 ?  342 LEU B O     1 
ATOM   8326  C  CB    . LEU B 1 342 ? 107.404 130.044 144.056 1.00 28.81 ?  342 LEU B CB    1 
ATOM   8327  C  CG    . LEU B 1 342 ? 108.634 130.761 143.496 1.00 29.11 ?  342 LEU B CG    1 
ATOM   8328  C  CD1   . LEU B 1 342 ? 109.486 129.807 142.679 1.00 28.49 ?  342 LEU B CD1   1 
ATOM   8329  C  CD2   . LEU B 1 342 ? 108.224 131.959 142.660 1.00 28.15 ?  342 LEU B CD2   1 
ATOM   8330  N  N     . LEU B 1 343 ? 107.531 128.966 147.067 1.00 27.61 ?  343 LEU B N     1 
ATOM   8331  C  CA    . LEU B 1 343 ? 108.089 128.989 148.417 1.00 29.13 ?  343 LEU B CA    1 
ATOM   8332  C  C     . LEU B 1 343 ? 108.680 127.638 148.796 1.00 28.50 ?  343 LEU B C     1 
ATOM   8333  O  O     . LEU B 1 343 ? 109.756 127.566 149.403 1.00 32.52 ?  343 LEU B O     1 
ATOM   8334  C  CB    . LEU B 1 343 ? 107.011 129.396 149.420 1.00 31.73 ?  343 LEU B CB    1 
ATOM   8335  C  CG    . LEU B 1 343 ? 106.923 130.874 149.794 1.00 32.63 ?  343 LEU B CG    1 
ATOM   8336  C  CD1   . LEU B 1 343 ? 105.778 131.100 150.763 1.00 27.04 ?  343 LEU B CD1   1 
ATOM   8337  C  CD2   . LEU B 1 343 ? 108.235 131.355 150.388 1.00 33.94 ?  343 LEU B CD2   1 
ATOM   8338  N  N     . GLU B 1 344 ? 107.982 126.553 148.459 1.00 34.65 ?  344 GLU B N     1 
ATOM   8339  C  CA    . GLU B 1 344 ? 108.502 125.221 148.746 1.00 32.82 ?  344 GLU B CA    1 
ATOM   8340  C  C     . GLU B 1 344 ? 109.770 124.945 147.948 1.00 29.44 ?  344 GLU B C     1 
ATOM   8341  O  O     . GLU B 1 344 ? 110.694 124.297 148.447 1.00 34.99 ?  344 GLU B O     1 
ATOM   8342  C  CB    . GLU B 1 344 ? 107.436 124.167 148.457 1.00 35.28 ?  344 GLU B CB    1 
ATOM   8343  C  CG    . GLU B 1 344 ? 106.197 124.291 149.327 1.00 36.66 ?  344 GLU B CG    1 
ATOM   8344  C  CD    . GLU B 1 344 ? 105.091 123.349 148.900 1.00 45.78 ?  344 GLU B CD    1 
ATOM   8345  O  OE1   . GLU B 1 344 ? 105.404 122.273 148.350 1.00 44.97 ?  344 GLU B OE1   1 
ATOM   8346  O  OE2   . GLU B 1 344 ? 103.907 123.687 149.112 1.00 43.83 -1 344 GLU B OE2   1 
ATOM   8347  N  N     . LYS B 1 345 ? 109.828 125.428 146.706 1.00 29.73 ?  345 LYS B N     1 
ATOM   8348  C  CA    . LYS B 1 345 ? 111.044 125.298 145.912 1.00 28.05 ?  345 LYS B CA    1 
ATOM   8349  C  C     . LYS B 1 345 ? 112.192 126.080 146.533 1.00 33.02 ?  345 LYS B C     1 
ATOM   8350  O  O     . LYS B 1 345 ? 113.335 125.611 146.549 1.00 36.04 ?  345 LYS B O     1 
ATOM   8351  C  CB    . LYS B 1 345 ? 110.782 125.766 144.481 1.00 29.85 ?  345 LYS B CB    1 
ATOM   8352  C  CG    . LYS B 1 345 ? 111.969 125.623 143.551 1.00 30.65 ?  345 LYS B CG    1 
ATOM   8353  C  CD    . LYS B 1 345 ? 111.627 126.090 142.150 1.00 29.51 ?  345 LYS B CD    1 
ATOM   8354  C  CE    . LYS B 1 345 ? 112.842 126.039 141.247 1.00 34.19 ?  345 LYS B CE    1 
ATOM   8355  N  NZ    . LYS B 1 345 ? 112.547 126.573 139.892 1.00 34.65 1  345 LYS B NZ    1 
ATOM   8356  N  N     . LEU B 1 346 ? 111.904 127.277 147.053 1.00 33.81 ?  346 LEU B N     1 
ATOM   8357  C  CA    . LEU B 1 346 ? 112.923 128.053 147.752 1.00 27.40 ?  346 LEU B CA    1 
ATOM   8358  C  C     . LEU B 1 346 ? 113.449 127.293 148.961 1.00 25.79 ?  346 LEU B C     1 
ATOM   8359  O  O     . LEU B 1 346 ? 114.661 127.215 149.180 1.00 28.42 ?  346 LEU B O     1 
ATOM   8360  C  CB    . LEU B 1 346 ? 112.352 129.403 148.186 1.00 27.66 ?  346 LEU B CB    1 
ATOM   8361  C  CG    . LEU B 1 346 ? 112.036 130.452 147.123 1.00 26.18 ?  346 LEU B CG    1 
ATOM   8362  C  CD1   . LEU B 1 346 ? 111.384 131.662 147.764 1.00 30.49 ?  346 LEU B CD1   1 
ATOM   8363  C  CD2   . LEU B 1 346 ? 113.291 130.851 146.385 1.00 27.88 ?  346 LEU B CD2   1 
ATOM   8364  N  N     . ALA B 1 347 ? 112.543 126.722 149.757 1.00 26.69 ?  347 ALA B N     1 
ATOM   8365  C  CA    . ALA B 1 347 ? 112.964 125.984 150.944 1.00 20.04 ?  347 ALA B CA    1 
ATOM   8366  C  C     . ALA B 1 347 ? 113.768 124.745 150.572 1.00 27.48 ?  347 ALA B C     1 
ATOM   8367  O  O     . ALA B 1 347 ? 114.763 124.421 151.230 1.00 35.93 ?  347 ALA B O     1 
ATOM   8368  C  CB    . ALA B 1 347 ? 111.749 125.604 151.785 1.00 19.98 ?  347 ALA B CB    1 
ATOM   8369  N  N     . MET B 1 348 ? 113.349 124.035 149.522 1.00 33.95 ?  348 MET B N     1 
ATOM   8370  C  CA    . MET B 1 348 ? 114.094 122.867 149.065 1.00 31.21 ?  348 MET B CA    1 
ATOM   8371  C  C     . MET B 1 348 ? 115.490 123.253 148.598 1.00 31.70 ?  348 MET B C     1 
ATOM   8372  O  O     . MET B 1 348 ? 116.472 122.567 148.910 1.00 40.09 ?  348 MET B O     1 
ATOM   8373  C  CB    . MET B 1 348 ? 113.319 122.166 147.947 1.00 33.42 ?  348 MET B CB    1 
ATOM   8374  C  CG    . MET B 1 348 ? 114.086 121.069 147.230 1.00 40.99 ?  348 MET B CG    1 
ATOM   8375  S  SD    . MET B 1 348 ? 114.807 121.609 145.666 1.00 60.89 ?  348 MET B SD    1 
ATOM   8376  C  CE    . MET B 1 348 ? 113.433 122.498 144.939 1.00 38.33 ?  348 MET B CE    1 
ATOM   8377  N  N     . LEU B 1 349 ? 115.599 124.357 147.856 1.00 26.74 ?  349 LEU B N     1 
ATOM   8378  C  CA    . LEU B 1 349 ? 116.902 124.809 147.389 1.00 27.33 ?  349 LEU B CA    1 
ATOM   8379  C  C     . LEU B 1 349 ? 117.794 125.224 148.551 1.00 28.95 ?  349 LEU B C     1 
ATOM   8380  O  O     . LEU B 1 349 ? 119.001 124.963 148.537 1.00 32.49 ?  349 LEU B O     1 
ATOM   8381  C  CB    . LEU B 1 349 ? 116.726 125.964 146.408 1.00 27.93 ?  349 LEU B CB    1 
ATOM   8382  C  CG    . LEU B 1 349 ? 116.672 125.562 144.937 1.00 33.81 ?  349 LEU B CG    1 
ATOM   8383  C  CD1   . LEU B 1 349 ? 115.832 126.554 144.171 1.00 34.75 ?  349 LEU B CD1   1 
ATOM   8384  C  CD2   . LEU B 1 349 ? 118.071 125.478 144.357 1.00 33.96 ?  349 LEU B CD2   1 
ATOM   8385  N  N     . ARG B 1 350 ? 117.224 125.888 149.559 1.00 26.35 ?  350 ARG B N     1 
ATOM   8386  C  CA    . ARG B 1 350 ? 118.017 126.277 150.720 1.00 22.58 ?  350 ARG B CA    1 
ATOM   8387  C  C     . ARG B 1 350 ? 118.458 125.065 151.529 1.00 30.68 ?  350 ARG B C     1 
ATOM   8388  O  O     . ARG B 1 350 ? 119.571 125.053 152.067 1.00 41.06 ?  350 ARG B O     1 
ATOM   8389  C  CB    . ARG B 1 350 ? 117.235 127.250 151.600 1.00 25.27 ?  350 ARG B CB    1 
ATOM   8390  C  CG    . ARG B 1 350 ? 116.795 128.514 150.885 1.00 24.47 ?  350 ARG B CG    1 
ATOM   8391  C  CD    . ARG B 1 350 ? 116.397 129.593 151.866 1.00 26.29 ?  350 ARG B CD    1 
ATOM   8392  N  NE    . ARG B 1 350 ? 117.471 130.557 152.062 1.00 33.09 ?  350 ARG B NE    1 
ATOM   8393  C  CZ    . ARG B 1 350 ? 117.864 131.005 153.245 1.00 28.82 ?  350 ARG B CZ    1 
ATOM   8394  N  NH1   . ARG B 1 350 ? 117.310 130.575 154.365 1.00 26.87 1  350 ARG B NH1   1 
ATOM   8395  N  NH2   . ARG B 1 350 ? 118.843 131.902 153.305 1.00 32.13 ?  350 ARG B NH2   1 
ATOM   8396  N  N     . SER B 1 351 ? 117.606 124.046 151.637 1.00 33.84 ?  351 SER B N     1 
ATOM   8397  C  CA    . SER B 1 351 ? 118.019 122.811 152.294 1.00 33.14 ?  351 SER B CA    1 
ATOM   8398  C  C     . SER B 1 351 ? 119.150 122.135 151.531 1.00 34.19 ?  351 SER B C     1 
ATOM   8399  O  O     . SER B 1 351 ? 120.113 121.649 152.134 1.00 42.75 ?  351 SER B O     1 
ATOM   8400  C  CB    . SER B 1 351 ? 116.828 121.862 152.430 1.00 34.41 ?  351 SER B CB    1 
ATOM   8401  O  OG    . SER B 1 351 ? 115.852 122.387 153.311 1.00 44.10 ?  351 SER B OG    1 
ATOM   8402  N  N     . GLU B 1 352 ? 119.050 122.096 150.201 1.00 34.56 ?  352 GLU B N     1 
ATOM   8403  C  CA    . GLU B 1 352 ? 120.039 121.371 149.410 1.00 35.03 ?  352 GLU B CA    1 
ATOM   8404  C  C     . GLU B 1 352 ? 121.375 122.105 149.354 1.00 35.91 ?  352 GLU B C     1 
ATOM   8405  O  O     . GLU B 1 352 ? 122.433 121.486 149.513 1.00 44.61 ?  352 GLU B O     1 
ATOM   8406  C  CB    . GLU B 1 352 ? 119.501 121.127 148.003 1.00 36.46 ?  352 GLU B CB    1 
ATOM   8407  C  CG    . GLU B 1 352 ? 118.435 120.048 147.935 1.00 39.07 ?  352 GLU B CG    1 
ATOM   8408  C  CD    . GLU B 1 352 ? 117.690 120.049 146.617 1.00 47.81 ?  352 GLU B CD    1 
ATOM   8409  O  OE1   . GLU B 1 352 ? 117.936 120.959 145.797 1.00 44.81 ?  352 GLU B OE1   1 
ATOM   8410  O  OE2   . GLU B 1 352 ? 116.864 119.140 146.399 1.00 45.72 -1 352 GLU B OE2   1 
ATOM   8411  N  N     . SER B 1 353 ? 121.354 123.420 149.128 1.00 36.06 ?  353 SER B N     1 
ATOM   8412  C  CA    . SER B 1 353 ? 122.574 124.169 148.862 1.00 36.19 ?  353 SER B CA    1 
ATOM   8413  C  C     . SER B 1 353 ? 122.747 125.432 149.691 1.00 30.27 ?  353 SER B C     1 
ATOM   8414  O  O     . SER B 1 353 ? 123.789 126.083 149.564 1.00 32.66 ?  353 SER B O     1 
ATOM   8415  C  CB    . SER B 1 353 ? 122.648 124.555 147.376 1.00 37.72 ?  353 SER B CB    1 
ATOM   8416  O  OG    . SER B 1 353 ? 121.672 125.530 147.056 1.00 35.84 ?  353 SER B OG    1 
ATOM   8417  N  N     . GLY B 1 354 ? 121.776 125.806 150.522 1.00 25.89 ?  354 GLY B N     1 
ATOM   8418  C  CA    . GLY B 1 354 ? 121.860 127.034 151.284 1.00 27.51 ?  354 GLY B CA    1 
ATOM   8419  C  C     . GLY B 1 354 ? 121.428 128.277 150.542 1.00 23.43 ?  354 GLY B C     1 
ATOM   8420  O  O     . GLY B 1 354 ? 121.406 129.359 151.141 1.00 27.53 ?  354 GLY B O     1 
ATOM   8421  N  N     . TYR B 1 355 ? 121.081 128.162 149.269 1.00 26.70 ?  355 TYR B N     1 
ATOM   8422  C  CA    . TYR B 1 355 ? 120.666 129.266 148.423 1.00 16.72 ?  355 TYR B CA    1 
ATOM   8423  C  C     . TYR B 1 355 ? 119.185 129.151 148.093 1.00 24.56 ?  355 TYR B C     1 
ATOM   8424  O  O     . TYR B 1 355 ? 118.618 128.055 148.122 1.00 29.05 ?  355 TYR B O     1 
ATOM   8425  C  CB    . TYR B 1 355 ? 121.484 129.281 147.124 1.00 19.98 ?  355 TYR B CB    1 
ATOM   8426  C  CG    . TYR B 1 355 ? 122.926 129.675 147.318 1.00 28.27 ?  355 TYR B CG    1 
ATOM   8427  C  CD1   . TYR B 1 355 ? 123.261 130.865 147.948 1.00 25.74 ?  355 TYR B CD1   1 
ATOM   8428  C  CD2   . TYR B 1 355 ? 123.953 128.858 146.874 1.00 30.44 ?  355 TYR B CD2   1 
ATOM   8429  C  CE1   . TYR B 1 355 ? 124.577 131.226 148.127 1.00 27.80 ?  355 TYR B CE1   1 
ATOM   8430  C  CE2   . TYR B 1 355 ? 125.274 129.213 147.050 1.00 29.65 ?  355 TYR B CE2   1 
ATOM   8431  C  CZ    . TYR B 1 355 ? 125.579 130.400 147.677 1.00 30.27 ?  355 TYR B CZ    1 
ATOM   8432  O  OH    . TYR B 1 355 ? 126.893 130.762 147.857 1.00 34.28 ?  355 TYR B OH    1 
ATOM   8433  N  N     . PRO B 1 356 ? 118.520 130.263 147.766 1.00 27.49 ?  356 PRO B N     1 
ATOM   8434  C  CA    . PRO B 1 356 ? 119.012 131.643 147.677 1.00 15.66 ?  356 PRO B CA    1 
ATOM   8435  C  C     . PRO B 1 356 ? 118.971 132.402 148.994 1.00 16.09 ?  356 PRO B C     1 
ATOM   8436  O  O     . PRO B 1 356 ? 118.374 131.955 149.966 1.00 24.60 ?  356 PRO B O     1 
ATOM   8437  C  CB    . PRO B 1 356 ? 118.051 132.266 146.664 1.00 18.31 ?  356 PRO B CB    1 
ATOM   8438  C  CG    . PRO B 1 356 ? 116.756 131.590 146.974 1.00 22.80 ?  356 PRO B CG    1 
ATOM   8439  C  CD    . PRO B 1 356 ? 117.125 130.164 147.300 1.00 13.71 ?  356 PRO B CD    1 
ATOM   8440  N  N     . TYR B 1 357 ? 119.614 133.563 149.048 1.00 21.55 ?  357 TYR B N     1 
ATOM   8441  C  CA    . TYR B 1 357 ? 119.325 134.512 150.110 1.00 13.99 ?  357 TYR B CA    1 
ATOM   8442  C  C     . TYR B 1 357 ? 117.904 135.029 149.935 1.00 17.78 ?  357 TYR B C     1 
ATOM   8443  O  O     . TYR B 1 357 ? 117.431 135.214 148.811 1.00 26.50 ?  357 TYR B O     1 
ATOM   8444  C  CB    . TYR B 1 357 ? 120.309 135.684 150.090 1.00 12.95 ?  357 TYR B CB    1 
ATOM   8445  C  CG    . TYR B 1 357 ? 121.763 135.326 149.875 1.00 16.72 ?  357 TYR B CG    1 
ATOM   8446  C  CD1   . TYR B 1 357 ? 122.292 134.140 150.358 1.00 17.56 ?  357 TYR B CD1   1 
ATOM   8447  C  CD2   . TYR B 1 357 ? 122.613 136.187 149.196 1.00 19.44 ?  357 TYR B CD2   1 
ATOM   8448  C  CE1   . TYR B 1 357 ? 123.615 133.818 150.171 1.00 19.94 ?  357 TYR B CE1   1 
ATOM   8449  C  CE2   . TYR B 1 357 ? 123.940 135.873 149.001 1.00 15.34 ?  357 TYR B CE2   1 
ATOM   8450  C  CZ    . TYR B 1 357 ? 124.436 134.687 149.491 1.00 24.11 ?  357 TYR B CZ    1 
ATOM   8451  O  OH    . TYR B 1 357 ? 125.759 134.365 149.304 1.00 31.95 ?  357 TYR B OH    1 
ATOM   8452  N  N     . ILE B 1 358 ? 117.216 135.253 151.046 1.00 25.86 ?  358 ILE B N     1 
ATOM   8453  C  CA    . ILE B 1 358 ? 115.860 135.784 151.029 1.00 18.22 ?  358 ILE B CA    1 
ATOM   8454  C  C     . ILE B 1 358 ? 115.911 137.213 151.545 1.00 19.32 ?  358 ILE B C     1 
ATOM   8455  O  O     . ILE B 1 358 ? 116.339 137.453 152.679 1.00 24.72 ?  358 ILE B O     1 
ATOM   8456  C  CB    . ILE B 1 358 ? 114.897 134.931 151.868 1.00 18.88 ?  358 ILE B CB    1 
ATOM   8457  C  CG1   . ILE B 1 358 ? 114.924 133.472 151.408 1.00 15.46 ?  358 ILE B CG1   1 
ATOM   8458  C  CG2   . ILE B 1 358 ? 113.492 135.499 151.794 1.00 17.41 ?  358 ILE B CG2   1 
ATOM   8459  C  CD1   . ILE B 1 358 ? 114.463 133.268 149.986 1.00 21.51 ?  358 ILE B CD1   1 
ATOM   8460  N  N     . MET B 1 359 ? 115.481 138.157 150.717 1.00 13.23 ?  359 MET B N     1 
ATOM   8461  C  CA    . MET B 1 359 ? 115.353 139.553 151.110 1.00 2.07  ?  359 MET B CA    1 
ATOM   8462  C  C     . MET B 1 359 ? 113.879 139.925 151.071 1.00 7.01  ?  359 MET B C     1 
ATOM   8463  O  O     . MET B 1 359 ? 113.259 139.907 150.003 1.00 20.50 ?  359 MET B O     1 
ATOM   8464  C  CB    . MET B 1 359 ? 116.172 140.462 150.196 1.00 10.80 ?  359 MET B CB    1 
ATOM   8465  C  CG    . MET B 1 359 ? 116.110 141.933 150.568 1.00 9.94  ?  359 MET B CG    1 
ATOM   8466  S  SD    . MET B 1 359 ? 116.113 143.028 149.142 1.00 38.89 ?  359 MET B SD    1 
ATOM   8467  C  CE    . MET B 1 359 ? 115.186 144.417 149.773 1.00 16.35 ?  359 MET B CE    1 
ATOM   8468  N  N     . PHE B 1 360 ? 113.319 140.243 152.233 1.00 13.11 ?  360 PHE B N     1 
ATOM   8469  C  CA    . PHE B 1 360 ? 111.916 140.638 152.328 1.00 5.13  ?  360 PHE B CA    1 
ATOM   8470  C  C     . PHE B 1 360 ? 111.830 142.121 151.997 1.00 13.75 ?  360 PHE B C     1 
ATOM   8471  O  O     . PHE B 1 360 ? 112.153 142.974 152.824 1.00 21.20 ?  360 PHE B O     1 
ATOM   8472  C  CB    . PHE B 1 360 ? 111.365 140.322 153.712 1.00 11.94 ?  360 PHE B CB    1 
ATOM   8473  C  CG    . PHE B 1 360 ? 111.352 138.855 154.031 1.00 16.25 ?  360 PHE B CG    1 
ATOM   8474  C  CD1   . PHE B 1 360 ? 110.563 137.980 153.302 1.00 19.55 ?  360 PHE B CD1   1 
ATOM   8475  C  CD2   . PHE B 1 360 ? 112.146 138.346 155.044 1.00 13.35 ?  360 PHE B CD2   1 
ATOM   8476  C  CE1   . PHE B 1 360 ? 110.557 136.630 153.588 1.00 18.52 ?  360 PHE B CE1   1 
ATOM   8477  C  CE2   . PHE B 1 360 ? 112.143 136.998 155.333 1.00 18.20 ?  360 PHE B CE2   1 
ATOM   8478  C  CZ    . PHE B 1 360 ? 111.347 136.139 154.605 1.00 15.01 ?  360 PHE B CZ    1 
ATOM   8479  N  N     . GLN B 1 361 ? 111.380 142.421 150.776 1.00 18.99 ?  361 GLN B N     1 
ATOM   8480  C  CA    . GLN B 1 361 ? 111.478 143.775 150.239 1.00 9.60  ?  361 GLN B CA    1 
ATOM   8481  C  C     . GLN B 1 361 ? 110.726 144.785 151.096 1.00 9.13  ?  361 GLN B C     1 
ATOM   8482  O  O     . GLN B 1 361 ? 111.232 145.879 151.366 1.00 14.03 ?  361 GLN B O     1 
ATOM   8483  C  CB    . GLN B 1 361 ? 110.950 143.797 148.803 1.00 19.01 ?  361 GLN B CB    1 
ATOM   8484  C  CG    . GLN B 1 361 ? 110.786 145.182 148.211 1.00 20.19 ?  361 GLN B CG    1 
ATOM   8485  C  CD    . GLN B 1 361 ? 111.749 145.450 147.078 1.00 20.87 ?  361 GLN B CD    1 
ATOM   8486  O  OE1   . GLN B 1 361 ? 111.891 144.641 146.165 1.00 30.14 ?  361 GLN B OE1   1 
ATOM   8487  N  NE2   . GLN B 1 361 ? 112.423 146.591 147.132 1.00 20.20 ?  361 GLN B NE2   1 
ATOM   8488  N  N     . ASP B 1 362 ? 109.514 144.442 151.530 1.00 23.19 ?  362 ASP B N     1 
ATOM   8489  C  CA    . ASP B 1 362 ? 108.706 145.391 152.284 1.00 13.79 ?  362 ASP B CA    1 
ATOM   8490  C  C     . ASP B 1 362 ? 109.126 145.501 153.743 1.00 13.78 ?  362 ASP B C     1 
ATOM   8491  O  O     . ASP B 1 362 ? 108.850 146.525 154.373 1.00 23.01 ?  362 ASP B O     1 
ATOM   8492  C  CB    . ASP B 1 362 ? 107.227 145.018 152.185 1.00 16.01 ?  362 ASP B CB    1 
ATOM   8493  C  CG    . ASP B 1 362 ? 106.715 145.054 150.757 1.00 27.61 ?  362 ASP B CG    1 
ATOM   8494  O  OD1   . ASP B 1 362 ? 107.540 144.954 149.824 1.00 24.96 ?  362 ASP B OD1   1 
ATOM   8495  O  OD2   . ASP B 1 362 ? 105.492 145.202 150.562 1.00 37.15 -1 362 ASP B OD2   1 
ATOM   8496  N  N     . ASN B 1 363 ? 109.780 144.477 154.294 1.00 28.56 ?  363 ASN B N     1 
ATOM   8497  C  CA    . ASN B 1 363 ? 110.374 144.619 155.618 1.00 13.54 ?  363 ASN B CA    1 
ATOM   8498  C  C     . ASN B 1 363 ? 111.514 145.629 155.595 1.00 19.84 ?  363 ASN B C     1 
ATOM   8499  O  O     . ASN B 1 363 ? 111.678 146.411 156.538 1.00 25.82 ?  363 ASN B O     1 
ATOM   8500  C  CB    . ASN B 1 363 ? 110.869 143.265 156.126 1.00 10.51 ?  363 ASN B CB    1 
ATOM   8501  C  CG    . ASN B 1 363 ? 109.755 142.410 156.685 1.00 17.88 ?  363 ASN B CG    1 
ATOM   8502  O  OD1   . ASN B 1 363 ? 108.630 142.873 156.859 1.00 22.12 ?  363 ASN B OD1   1 
ATOM   8503  N  ND2   . ASN B 1 363 ? 110.063 141.153 156.974 1.00 20.62 ?  363 ASN B ND2   1 
ATOM   8504  N  N     . VAL B 1 364 ? 112.313 145.619 154.528 1.00 17.04 ?  364 VAL B N     1 
ATOM   8505  C  CA    . VAL B 1 364 ? 113.407 146.574 154.403 1.00 10.09 ?  364 VAL B CA    1 
ATOM   8506  C  C     . VAL B 1 364 ? 112.867 147.986 154.222 1.00 19.58 ?  364 VAL B C     1 
ATOM   8507  O  O     . VAL B 1 364 ? 113.311 148.930 154.886 1.00 25.50 ?  364 VAL B O     1 
ATOM   8508  C  CB    . VAL B 1 364 ? 114.330 146.178 153.237 1.00 0.06  ?  364 VAL B CB    1 
ATOM   8509  C  CG1   . VAL B 1 364 ? 115.530 147.095 153.184 1.00 7.05  ?  364 VAL B CG1   1 
ATOM   8510  C  CG2   . VAL B 1 364 ? 114.763 144.734 153.367 1.00 3.59  ?  364 VAL B CG2   1 
ATOM   8511  N  N     . ASN B 1 365 ? 111.898 148.152 153.324 1.00 14.89 ?  365 ASN B N     1 
ATOM   8512  C  CA    . ASN B 1 365 ? 111.487 149.479 152.886 1.00 4.58  ?  365 ASN B CA    1 
ATOM   8513  C  C     . ASN B 1 365 ? 110.451 150.128 153.790 1.00 12.69 ?  365 ASN B C     1 
ATOM   8514  O  O     . ASN B 1 365 ? 110.220 151.335 153.664 1.00 24.10 ?  365 ASN B O     1 
ATOM   8515  C  CB    . ASN B 1 365 ? 110.950 149.408 151.458 1.00 18.94 ?  365 ASN B CB    1 
ATOM   8516  C  CG    . ASN B 1 365 ? 112.024 149.048 150.456 1.00 16.80 ?  365 ASN B CG    1 
ATOM   8517  O  OD1   . ASN B 1 365 ? 113.057 149.709 150.377 1.00 14.28 ?  365 ASN B OD1   1 
ATOM   8518  N  ND2   . ASN B 1 365 ? 111.789 147.995 149.688 1.00 18.87 ?  365 ASN B ND2   1 
ATOM   8519  N  N     . LYS B 1 366 ? 109.821 149.374 154.694 1.00 16.21 ?  366 LYS B N     1 
ATOM   8520  C  CA    . LYS B 1 366 ? 108.887 149.989 155.628 1.00 19.85 ?  366 LYS B CA    1 
ATOM   8521  C  C     . LYS B 1 366 ? 109.604 150.776 156.714 1.00 20.14 ?  366 LYS B C     1 
ATOM   8522  O  O     . LYS B 1 366 ? 108.997 151.659 157.329 1.00 30.80 ?  366 LYS B O     1 
ATOM   8523  C  CB    . LYS B 1 366 ? 107.982 148.926 156.251 1.00 16.52 ?  366 LYS B CB    1 
ATOM   8524  C  CG    . LYS B 1 366 ? 108.619 148.130 157.373 1.00 25.80 ?  366 LYS B CG    1 
ATOM   8525  C  CD    . LYS B 1 366 ? 107.565 147.396 158.180 1.00 28.53 ?  366 LYS B CD    1 
ATOM   8526  C  CE    . LYS B 1 366 ? 106.678 146.548 157.285 1.00 23.89 ?  366 LYS B CE    1 
ATOM   8527  N  NZ    . LYS B 1 366 ? 105.779 145.666 158.079 1.00 28.97 1  366 LYS B NZ    1 
ATOM   8528  N  N     . VAL B 1 367 ? 110.880 150.481 156.955 1.00 26.19 ?  367 VAL B N     1 
ATOM   8529  C  CA    . VAL B 1 367 ? 111.704 151.202 157.911 1.00 18.01 ?  367 VAL B CA    1 
ATOM   8530  C  C     . VAL B 1 367 ? 112.885 151.886 157.237 1.00 17.99 ?  367 VAL B C     1 
ATOM   8531  O  O     . VAL B 1 367 ? 113.750 152.435 157.915 1.00 23.59 ?  367 VAL B O     1 
ATOM   8532  C  CB    . VAL B 1 367 ? 112.186 150.271 159.042 1.00 14.88 ?  367 VAL B CB    1 
ATOM   8533  C  CG1   . VAL B 1 367 ? 111.014 149.837 159.901 1.00 17.71 ?  367 VAL B CG1   1 
ATOM   8534  C  CG2   . VAL B 1 367 ? 112.893 149.070 158.458 1.00 8.15  ?  367 VAL B CG2   1 
ATOM   8535  N  N     . HIS B 1 368 ? 112.940 151.851 155.908 1.00 17.51 ?  368 HIS B N     1 
ATOM   8536  C  CA    . HIS B 1 368 ? 114.023 152.491 155.178 1.00 3.61  ?  368 HIS B CA    1 
ATOM   8537  C  C     . HIS B 1 368 ? 113.914 154.004 155.305 1.00 17.40 ?  368 HIS B C     1 
ATOM   8538  O  O     . HIS B 1 368 ? 112.836 154.579 155.132 1.00 30.35 ?  368 HIS B O     1 
ATOM   8539  C  CB    . HIS B 1 368 ? 113.983 152.074 153.710 1.00 10.78 ?  368 HIS B CB    1 
ATOM   8540  C  CG    . HIS B 1 368 ? 115.148 152.561 152.908 1.00 6.15  ?  368 HIS B CG    1 
ATOM   8541  N  ND1   . HIS B 1 368 ? 115.038 152.919 151.584 1.00 18.67 ?  368 HIS B ND1   1 
ATOM   8542  C  CD2   . HIS B 1 368 ? 116.445 152.749 153.243 1.00 7.27  ?  368 HIS B CD2   1 
ATOM   8543  C  CE1   . HIS B 1 368 ? 116.219 153.306 151.134 1.00 17.56 ?  368 HIS B CE1   1 
ATOM   8544  N  NE2   . HIS B 1 368 ? 117.089 153.213 152.122 1.00 16.59 ?  368 HIS B NE2   1 
ATOM   8545  N  N     . ALA B 1 369 ? 115.036 154.649 155.612 1.00 20.81 ?  369 ALA B N     1 
ATOM   8546  C  CA    . ALA B 1 369 ? 115.057 156.084 155.851 1.00 13.95 ?  369 ALA B CA    1 
ATOM   8547  C  C     . ALA B 1 369 ? 115.291 156.902 154.590 1.00 25.08 ?  369 ALA B C     1 
ATOM   8548  O  O     . ALA B 1 369 ? 115.205 158.132 154.648 1.00 32.91 ?  369 ALA B O     1 
ATOM   8549  C  CB    . ALA B 1 369 ? 116.132 156.427 156.884 1.00 11.15 ?  369 ALA B CB    1 
ATOM   8550  N  N     . ASN B 1 370 ? 115.571 156.262 153.460 1.00 18.57 ?  370 ASN B N     1 
ATOM   8551  C  CA    . ASN B 1 370 ? 115.919 156.958 152.229 1.00 12.01 ?  370 ASN B CA    1 
ATOM   8552  C  C     . ASN B 1 370 ? 115.082 156.453 151.066 1.00 13.34 ?  370 ASN B C     1 
ATOM   8553  O  O     . ASN B 1 370 ? 115.582 156.262 149.956 1.00 24.87 ?  370 ASN B O     1 
ATOM   8554  C  CB    . ASN B 1 370 ? 117.407 156.812 151.925 1.00 12.83 ?  370 ASN B CB    1 
ATOM   8555  C  CG    . ASN B 1 370 ? 118.284 157.443 152.987 1.00 12.83 ?  370 ASN B CG    1 
ATOM   8556  O  OD1   . ASN B 1 370 ? 118.229 158.649 153.215 1.00 29.53 ?  370 ASN B OD1   1 
ATOM   8557  N  ND2   . ASN B 1 370 ? 119.098 156.627 153.641 1.00 12.13 ?  370 ASN B ND2   1 
ATOM   8558  N  N     . ASN B 1 371 ? 113.787 156.231 151.302 1.00 19.78 ?  371 ASN B N     1 
ATOM   8559  C  CA    . ASN B 1 371 ? 112.898 155.802 150.229 1.00 11.60 ?  371 ASN B CA    1 
ATOM   8560  C  C     . ASN B 1 371 ? 112.710 156.878 149.170 1.00 16.37 ?  371 ASN B C     1 
ATOM   8561  O  O     . ASN B 1 371 ? 112.358 156.553 148.032 1.00 26.99 ?  371 ASN B O     1 
ATOM   8562  C  CB    . ASN B 1 371 ? 111.538 155.392 150.795 1.00 9.05  ?  371 ASN B CB    1 
ATOM   8563  C  CG    . ASN B 1 371 ? 111.530 153.974 151.321 1.00 17.59 ?  371 ASN B CG    1 
ATOM   8564  O  OD1   . ASN B 1 371 ? 112.379 153.163 150.961 1.00 23.47 ?  371 ASN B OD1   1 
ATOM   8565  N  ND2   . ASN B 1 371 ? 110.569 153.669 152.181 1.00 24.49 ?  371 ASN B ND2   1 
ATOM   8566  N  N     . HIS B 1 372 ? 112.926 158.147 149.523 1.00 19.85 ?  372 HIS B N     1 
ATOM   8567  C  CA    . HIS B 1 372 ? 112.853 159.217 148.534 1.00 19.82 ?  372 HIS B CA    1 
ATOM   8568  C  C     . HIS B 1 372 ? 113.943 159.067 147.482 1.00 22.75 ?  372 HIS B C     1 
ATOM   8569  O  O     . HIS B 1 372 ? 113.705 159.298 146.291 1.00 28.09 ?  372 HIS B O     1 
ATOM   8570  C  CB    . HIS B 1 372 ? 112.956 160.576 149.225 1.00 23.38 ?  372 HIS B CB    1 
ATOM   8571  C  CG    . HIS B 1 372 ? 114.286 160.828 149.862 1.00 22.20 ?  372 HIS B CG    1 
ATOM   8572  N  ND1   . HIS B 1 372 ? 114.762 160.077 150.914 1.00 21.74 ?  372 HIS B ND1   1 
ATOM   8573  C  CD2   . HIS B 1 372 ? 115.246 161.743 149.590 1.00 24.73 ?  372 HIS B CD2   1 
ATOM   8574  C  CE1   . HIS B 1 372 ? 115.957 160.515 151.262 1.00 20.00 ?  372 HIS B CE1   1 
ATOM   8575  N  NE2   . HIS B 1 372 ? 116.273 161.529 150.477 1.00 23.90 ?  372 HIS B NE2   1 
ATOM   8576  N  N     . ILE B 1 373 ? 115.153 158.695 147.906 1.00 16.66 ?  373 ILE B N     1 
ATOM   8577  C  CA    . ILE B 1 373 ? 116.232 158.450 146.954 1.00 19.92 ?  373 ILE B CA    1 
ATOM   8578  C  C     . ILE B 1 373 ? 115.889 157.261 146.071 1.00 21.25 ?  373 ILE B C     1 
ATOM   8579  O  O     . ILE B 1 373 ? 115.956 157.335 144.839 1.00 37.31 ?  373 ILE B O     1 
ATOM   8580  C  CB    . ILE B 1 373 ? 117.562 158.230 147.699 1.00 24.82 ?  373 ILE B CB    1 
ATOM   8581  C  CG1   . ILE B 1 373 ? 117.962 159.491 148.462 1.00 21.51 ?  373 ILE B CG1   1 
ATOM   8582  C  CG2   . ILE B 1 373 ? 118.656 157.815 146.731 1.00 21.97 ?  373 ILE B CG2   1 
ATOM   8583  C  CD1   . ILE B 1 373 ? 119.007 159.252 149.519 1.00 18.19 ?  373 ILE B CD1   1 
ATOM   8584  N  N     . SER B 1 374 ? 115.497 156.153 146.694 1.00 15.22 ?  374 SER B N     1 
ATOM   8585  C  CA    . SER B 1 374 ? 115.101 154.925 146.023 1.00 10.77 ?  374 SER B CA    1 
ATOM   8586  C  C     . SER B 1 374 ? 114.673 153.935 147.092 1.00 20.36 ?  374 SER B C     1 
ATOM   8587  O  O     . SER B 1 374 ? 115.040 154.066 148.263 1.00 23.07 ?  374 SER B O     1 
ATOM   8588  C  CB    . SER B 1 374 ? 116.235 154.335 145.181 1.00 21.86 ?  374 SER B CB    1 
ATOM   8589  O  OG    . SER B 1 374 ? 115.768 153.279 144.366 1.00 35.99 ?  374 SER B OG    1 
ATOM   8590  N  N     . LYS B 1 375 ? 113.890 152.946 146.680 1.00 26.47 ?  375 LYS B N     1 
ATOM   8591  C  CA    . LYS B 1 375 ? 113.643 151.805 147.541 1.00 12.12 ?  375 LYS B CA    1 
ATOM   8592  C  C     . LYS B 1 375 ? 114.851 150.874 147.518 1.00 15.13 ?  375 LYS B C     1 
ATOM   8593  O  O     . LYS B 1 375 ? 115.641 150.864 146.571 1.00 28.03 ?  375 LYS B O     1 
ATOM   8594  C  CB    . LYS B 1 375 ? 112.390 151.053 147.094 1.00 14.41 ?  375 LYS B CB    1 
ATOM   8595  C  CG    . LYS B 1 375 ? 111.120 151.882 147.110 1.00 18.59 ?  375 LYS B CG    1 
ATOM   8596  C  CD    . LYS B 1 375 ? 110.556 151.997 148.509 1.00 21.94 ?  375 LYS B CD    1 
ATOM   8597  C  CE    . LYS B 1 375 ? 109.040 152.008 148.492 1.00 23.73 ?  375 LYS B CE    1 
ATOM   8598  N  NZ    . LYS B 1 375 ? 108.507 153.394 148.401 1.00 26.61 1  375 LYS B NZ    1 
ATOM   8599  N  N     . VAL B 1 376 ? 115.000 150.095 148.582 1.00 12.10 ?  376 VAL B N     1 
ATOM   8600  C  CA    . VAL B 1 376 ? 116.024 149.057 148.613 1.00 13.01 ?  376 VAL B CA    1 
ATOM   8601  C  C     . VAL B 1 376 ? 115.514 147.876 147.798 1.00 15.90 ?  376 VAL B C     1 
ATOM   8602  O  O     . VAL B 1 376 ? 114.496 147.267 148.137 1.00 25.73 ?  376 VAL B O     1 
ATOM   8603  C  CB    . VAL B 1 376 ? 116.357 148.639 150.051 1.00 9.66  ?  376 VAL B CB    1 
ATOM   8604  C  CG1   . VAL B 1 376 ? 117.441 147.572 150.058 1.00 5.98  ?  376 VAL B CG1   1 
ATOM   8605  C  CG2   . VAL B 1 376 ? 116.780 149.843 150.869 1.00 6.35  ?  376 VAL B CG2   1 
ATOM   8606  N  N     . LYS B 1 377 ? 116.219 147.554 146.715 1.00 14.65 ?  377 LYS B N     1 
ATOM   8607  C  CA    . LYS B 1 377 ? 115.773 146.516 145.798 1.00 13.59 ?  377 LYS B CA    1 
ATOM   8608  C  C     . LYS B 1 377 ? 116.516 145.202 145.961 1.00 8.55  ?  377 LYS B C     1 
ATOM   8609  O  O     . LYS B 1 377 ? 115.992 144.163 145.549 1.00 25.31 ?  377 LYS B O     1 
ATOM   8610  C  CB    . LYS B 1 377 ? 115.921 146.989 144.349 1.00 16.40 ?  377 LYS B CB    1 
ATOM   8611  C  CG    . LYS B 1 377 ? 115.106 148.216 144.010 1.00 9.68  ?  377 LYS B CG    1 
ATOM   8612  C  CD    . LYS B 1 377 ? 115.724 148.949 142.841 1.00 20.92 ?  377 LYS B CD    1 
ATOM   8613  C  CE    . LYS B 1 377 ? 115.601 150.446 143.006 1.00 25.14 ?  377 LYS B CE    1 
ATOM   8614  N  NZ    . LYS B 1 377 ? 116.523 151.181 142.100 1.00 23.03 1  377 LYS B NZ    1 
ATOM   8615  N  N     . PHE B 1 378 ? 117.710 145.220 146.543 1.00 6.05  ?  378 PHE B N     1 
ATOM   8616  C  CA    . PHE B 1 378 ? 118.509 144.011 146.683 1.00 5.14  ?  378 PHE B CA    1 
ATOM   8617  C  C     . PHE B 1 378 ? 119.571 144.254 147.744 1.00 10.46 ?  378 PHE B C     1 
ATOM   8618  O  O     . PHE B 1 378 ? 119.734 145.366 148.248 1.00 14.98 ?  378 PHE B O     1 
ATOM   8619  C  CB    . PHE B 1 378 ? 119.132 143.586 145.348 1.00 2.96  ?  378 PHE B CB    1 
ATOM   8620  C  CG    . PHE B 1 378 ? 120.229 144.492 144.858 1.00 7.80  ?  378 PHE B CG    1 
ATOM   8621  C  CD1   . PHE B 1 378 ? 120.000 145.843 144.653 1.00 14.95 ?  378 PHE B CD1   1 
ATOM   8622  C  CD2   . PHE B 1 378 ? 121.483 143.984 144.573 1.00 4.48  ?  378 PHE B CD2   1 
ATOM   8623  C  CE1   . PHE B 1 378 ? 121.002 146.667 144.194 1.00 6.75  ?  378 PHE B CE1   1 
ATOM   8624  C  CE2   . PHE B 1 378 ? 122.488 144.806 144.111 1.00 7.80  ?  378 PHE B CE2   1 
ATOM   8625  C  CZ    . PHE B 1 378 ? 122.247 146.148 143.922 1.00 9.48  ?  378 PHE B CZ    1 
ATOM   8626  N  N     . SER B 1 379 ? 120.291 143.191 148.077 1.00 2.51  ?  379 SER B N     1 
ATOM   8627  C  CA    . SER B 1 379 ? 121.299 143.206 149.125 1.00 7.97  ?  379 SER B CA    1 
ATOM   8628  C  C     . SER B 1 379 ? 122.650 142.811 148.541 1.00 8.40  ?  379 SER B C     1 
ATOM   8629  O  O     . SER B 1 379 ? 122.798 142.612 147.335 1.00 19.01 ?  379 SER B O     1 
ATOM   8630  C  CB    . SER B 1 379 ? 120.902 142.271 150.270 1.00 6.80  ?  379 SER B CB    1 
ATOM   8631  O  OG    . SER B 1 379 ? 121.397 142.748 151.505 1.00 10.43 ?  379 SER B OG    1 
ATOM   8632  N  N     . ASN B 1 380 ? 123.642 142.701 149.416 1.00 10.17 ?  380 ASN B N     1 
ATOM   8633  C  CA    . ASN B 1 380 ? 125.005 142.402 149.007 1.00 7.85  ?  380 ASN B CA    1 
ATOM   8634  C  C     . ASN B 1 380 ? 125.231 140.892 149.016 1.00 13.89 ?  380 ASN B C     1 
ATOM   8635  O  O     . ASN B 1 380 ? 124.295 140.096 149.127 1.00 20.08 ?  380 ASN B O     1 
ATOM   8636  C  CB    . ASN B 1 380 ? 126.002 143.132 149.903 1.00 8.11  ?  380 ASN B CB    1 
ATOM   8637  C  CG    . ASN B 1 380 ? 125.950 142.664 151.338 1.00 8.77  ?  380 ASN B CG    1 
ATOM   8638  O  OD1   . ASN B 1 380 ? 124.875 142.447 151.892 1.00 22.19 ?  380 ASN B OD1   1 
ATOM   8639  N  ND2   . ASN B 1 380 ? 127.114 142.524 151.956 1.00 17.17 ?  380 ASN B ND2   1 
ATOM   8640  N  N     . LEU B 1 381 ? 126.494 140.485 148.884 1.00 19.78 ?  381 LEU B N     1 
ATOM   8641  C  CA    . LEU B 1 381 ? 126.841 139.071 148.896 1.00 8.77  ?  381 LEU B CA    1 
ATOM   8642  C  C     . LEU B 1 381 ? 126.648 138.441 150.269 1.00 6.62  ?  381 LEU B C     1 
ATOM   8643  O  O     . LEU B 1 381 ? 126.488 137.220 150.360 1.00 22.70 ?  381 LEU B O     1 
ATOM   8644  C  CB    . LEU B 1 381 ? 128.286 138.904 148.420 1.00 17.60 ?  381 LEU B CB    1 
ATOM   8645  C  CG    . LEU B 1 381 ? 128.964 137.534 148.433 1.00 20.47 ?  381 LEU B CG    1 
ATOM   8646  C  CD1   . LEU B 1 381 ? 128.246 136.552 147.528 1.00 22.72 ?  381 LEU B CD1   1 
ATOM   8647  C  CD2   . LEU B 1 381 ? 130.414 137.675 148.025 1.00 15.48 ?  381 LEU B CD2   1 
ATOM   8648  N  N     . CYS B 1 382 ? 126.644 139.242 151.332 1.00 21.44 ?  382 CYS B N     1 
ATOM   8649  C  CA    . CYS B 1 382 ? 126.470 138.741 152.687 1.00 3.70  ?  382 CYS B CA    1 
ATOM   8650  C  C     . CYS B 1 382 ? 125.101 139.062 153.269 1.00 12.64 ?  382 CYS B C     1 
ATOM   8651  O  O     . CYS B 1 382 ? 124.847 138.730 154.431 1.00 23.34 ?  382 CYS B O     1 
ATOM   8652  C  CB    . CYS B 1 382 ? 127.571 139.296 153.598 1.00 20.70 ?  382 CYS B CB    1 
ATOM   8653  S  SG    . CYS B 1 382 ? 129.254 139.001 153.005 1.00 37.09 ?  382 CYS B SG    1 
ATOM   8654  N  N     . SER B 1 383 ? 124.224 139.716 152.502 1.00 15.80 ?  383 SER B N     1 
ATOM   8655  C  CA    . SER B 1 383 ? 122.810 139.884 152.838 1.00 11.02 ?  383 SER B CA    1 
ATOM   8656  C  C     . SER B 1 383 ? 122.583 140.801 154.038 1.00 18.31 ?  383 SER B C     1 
ATOM   8657  O  O     . SER B 1 383 ? 121.607 140.634 154.771 1.00 27.77 ?  383 SER B O     1 
ATOM   8658  C  CB    . SER B 1 383 ? 122.131 138.532 153.079 1.00 8.16  ?  383 SER B CB    1 
ATOM   8659  O  OG    . SER B 1 383 ? 122.182 137.727 151.917 1.00 36.35 ?  383 SER B OG    1 
ATOM   8660  N  N     . GLU B 1 384 ? 123.460 141.775 154.263 1.00 11.76 ?  384 GLU B N     1 
ATOM   8661  C  CA    . GLU B 1 384 ? 123.246 142.739 155.331 1.00 9.89  ?  384 GLU B CA    1 
ATOM   8662  C  C     . GLU B 1 384 ? 123.234 144.186 154.862 1.00 16.66 ?  384 GLU B C     1 
ATOM   8663  O  O     . GLU B 1 384 ? 122.764 145.052 155.606 1.00 26.21 ?  384 GLU B O     1 
ATOM   8664  C  CB    . GLU B 1 384 ? 124.305 142.574 156.434 1.00 9.21  ?  384 GLU B CB    1 
ATOM   8665  C  CG    . GLU B 1 384 ? 125.481 143.526 156.341 1.00 11.23 ?  384 GLU B CG    1 
ATOM   8666  C  CD    . GLU B 1 384 ? 126.537 143.052 155.374 1.00 22.17 ?  384 GLU B CD    1 
ATOM   8667  O  OE1   . GLU B 1 384 ? 126.459 141.886 154.945 1.00 23.44 ?  384 GLU B OE1   1 
ATOM   8668  O  OE2   . GLU B 1 384 ? 127.447 143.840 155.050 1.00 29.48 -1 384 GLU B OE2   1 
ATOM   8669  N  N     . VAL B 1 385 ? 123.719 144.473 153.662 1.00 11.10 ?  385 VAL B N     1 
ATOM   8670  C  CA    . VAL B 1 385 ? 123.737 145.832 153.138 1.00 2.81  ?  385 VAL B CA    1 
ATOM   8671  C  C     . VAL B 1 385 ? 122.412 146.093 152.439 1.00 17.93 ?  385 VAL B C     1 
ATOM   8672  O  O     . VAL B 1 385 ? 122.077 145.427 151.455 1.00 25.12 ?  385 VAL B O     1 
ATOM   8673  C  CB    . VAL B 1 385 ? 124.917 146.045 152.180 1.00 5.27  ?  385 VAL B CB    1 
ATOM   8674  C  CG1   . VAL B 1 385 ? 124.829 147.410 151.551 1.00 8.53  ?  385 VAL B CG1   1 
ATOM   8675  C  CG2   . VAL B 1 385 ? 126.223 145.894 152.923 1.00 8.98  ?  385 VAL B CG2   1 
ATOM   8676  N  N     . LEU B 1 386 ? 121.655 147.064 152.951 1.00 19.30 ?  386 LEU B N     1 
ATOM   8677  C  CA    . LEU B 1 386 ? 120.324 147.394 152.442 1.00 2.15  ?  386 LEU B CA    1 
ATOM   8678  C  C     . LEU B 1 386 ? 120.252 148.907 152.274 1.00 5.61  ?  386 LEU B C     1 
ATOM   8679  O  O     . LEU B 1 386 ? 119.889 149.628 153.206 1.00 12.33 ?  386 LEU B O     1 
ATOM   8680  C  CB    . LEU B 1 386 ? 119.244 146.871 153.377 1.00 5.81  ?  386 LEU B CB    1 
ATOM   8681  C  CG    . LEU B 1 386 ? 119.198 145.349 153.485 1.00 0.77  ?  386 LEU B CG    1 
ATOM   8682  C  CD1   . LEU B 1 386 ? 118.196 144.927 154.524 1.00 7.88  ?  386 LEU B CD1   1 
ATOM   8683  C  CD2   . LEU B 1 386 ? 118.867 144.735 152.138 1.00 6.73  ?  386 LEU B CD2   1 
ATOM   8684  N  N     . GLN B 1 387 ? 120.597 149.385 151.082 1.00 13.17 ?  387 GLN B N     1 
ATOM   8685  C  CA    . GLN B 1 387 ? 120.671 150.808 150.802 1.00 3.15  ?  387 GLN B CA    1 
ATOM   8686  C  C     . GLN B 1 387 ? 119.968 151.119 149.488 1.00 8.38  ?  387 GLN B C     1 
ATOM   8687  O  O     . GLN B 1 387 ? 119.773 150.247 148.640 1.00 22.69 ?  387 GLN B O     1 
ATOM   8688  C  CB    . GLN B 1 387 ? 122.127 151.288 150.745 1.00 0.56  ?  387 GLN B CB    1 
ATOM   8689  C  CG    . GLN B 1 387 ? 122.931 150.927 151.973 1.00 4.37  ?  387 GLN B CG    1 
ATOM   8690  C  CD    . GLN B 1 387 ? 124.331 151.479 151.932 1.00 10.53 ?  387 GLN B CD    1 
ATOM   8691  O  OE1   . GLN B 1 387 ? 124.644 152.351 151.125 1.00 20.68 ?  387 GLN B OE1   1 
ATOM   8692  N  NE2   . GLN B 1 387 ? 125.188 150.974 152.805 1.00 9.52  ?  387 GLN B NE2   1 
ATOM   8693  N  N     . ALA B 1 388 ? 119.580 152.381 149.340 1.00 9.62  ?  388 ALA B N     1 
ATOM   8694  C  CA    . ALA B 1 388 ? 118.964 152.839 148.102 1.00 7.64  ?  388 ALA B CA    1 
ATOM   8695  C  C     . ALA B 1 388 ? 119.982 152.854 146.972 1.00 14.26 ?  388 ALA B C     1 
ATOM   8696  O  O     . ALA B 1 388 ? 121.136 153.252 147.156 1.00 25.40 ?  388 ALA B O     1 
ATOM   8697  C  CB    . ALA B 1 388 ? 118.369 154.233 148.290 1.00 11.59 ?  388 ALA B CB    1 
ATOM   8698  N  N     . SER B 1 389 ? 119.550 152.420 145.793 1.00 19.81 ?  389 SER B N     1 
ATOM   8699  C  CA    . SER B 1 389 ? 120.397 152.394 144.613 1.00 8.84  ?  389 SER B CA    1 
ATOM   8700  C  C     . SER B 1 389 ? 119.649 152.993 143.433 1.00 12.83 ?  389 SER B C     1 
ATOM   8701  O  O     . SER B 1 389 ? 118.420 152.933 143.359 1.00 23.31 ?  389 SER B O     1 
ATOM   8702  C  CB    . SER B 1 389 ? 120.844 150.968 144.270 1.00 17.11 ?  389 SER B CB    1 
ATOM   8703  O  OG    . SER B 1 389 ? 119.744 150.076 144.264 1.00 23.86 ?  389 SER B OG    1 
ATOM   8704  N  N     . GLN B 1 390 ? 120.407 153.573 142.509 1.00 22.95 ?  390 GLN B N     1 
ATOM   8705  C  CA    . GLN B 1 390 ? 119.866 154.097 141.265 1.00 12.92 ?  390 GLN B CA    1 
ATOM   8706  C  C     . GLN B 1 390 ? 120.635 153.472 140.115 1.00 14.09 ?  390 GLN B C     1 
ATOM   8707  O  O     . GLN B 1 390 ? 121.870 153.463 140.123 1.00 25.00 ?  390 GLN B O     1 
ATOM   8708  C  CB    . GLN B 1 390 ? 119.961 155.623 141.214 1.00 10.67 ?  390 GLN B CB    1 
ATOM   8709  C  CG    . GLN B 1 390 ? 118.999 156.320 142.154 1.00 11.92 ?  390 GLN B CG    1 
ATOM   8710  C  CD    . GLN B 1 390 ? 119.161 157.822 142.148 1.00 26.59 ?  390 GLN B CD    1 
ATOM   8711  O  OE1   . GLN B 1 390 ? 120.084 158.356 141.533 1.00 33.24 ?  390 GLN B OE1   1 
ATOM   8712  N  NE2   . GLN B 1 390 ? 118.265 158.515 142.838 1.00 18.02 ?  390 GLN B NE2   1 
ATOM   8713  N  N     . VAL B 1 391 ? 119.908 152.942 139.133 1.00 26.31 ?  391 VAL B N     1 
ATOM   8714  C  CA    . VAL B 1 391 ? 120.553 152.256 138.023 1.00 20.02 ?  391 VAL B CA    1 
ATOM   8715  C  C     . VAL B 1 391 ? 121.225 153.275 137.112 1.00 25.64 ?  391 VAL B C     1 
ATOM   8716  O  O     . VAL B 1 391 ? 120.722 154.387 136.905 1.00 22.59 ?  391 VAL B O     1 
ATOM   8717  C  CB    . VAL B 1 391 ? 119.535 151.388 137.260 1.00 15.69 ?  391 VAL B CB    1 
ATOM   8718  C  CG1   . VAL B 1 391 ? 118.552 152.249 136.481 1.00 16.52 ?  391 VAL B CG1   1 
ATOM   8719  C  CG2   . VAL B 1 391 ? 120.252 150.408 136.346 1.00 17.13 ?  391 VAL B CG2   1 
ATOM   8720  N  N     . SER B 1 392 ? 122.389 152.908 136.591 1.00 32.86 ?  392 SER B N     1 
ATOM   8721  C  CA    . SER B 1 392 ? 123.121 153.757 135.668 1.00 21.49 ?  392 SER B CA    1 
ATOM   8722  C  C     . SER B 1 392 ? 122.730 153.435 134.233 1.00 28.88 ?  392 SER B C     1 
ATOM   8723  O  O     . SER B 1 392 ? 122.434 152.288 133.890 1.00 31.81 ?  392 SER B O     1 
ATOM   8724  C  CB    . SER B 1 392 ? 124.629 153.583 135.846 1.00 25.83 ?  392 SER B CB    1 
ATOM   8725  O  OG    . SER B 1 392 ? 125.014 153.806 137.190 1.00 36.93 ?  392 SER B OG    1 
ATOM   8726  N  N     . SER B 1 393 ? 122.730 154.463 133.397 1.00 35.47 ?  393 SER B N     1 
ATOM   8727  C  CA    . SER B 1 393 ? 122.431 154.331 131.975 1.00 28.19 ?  393 SER B CA    1 
ATOM   8728  C  C     . SER B 1 393 ? 123.749 154.470 131.220 1.00 32.27 ?  393 SER B C     1 
ATOM   8729  O  O     . SER B 1 393 ? 124.146 155.569 130.828 1.00 35.82 ?  393 SER B O     1 
ATOM   8730  C  CB    . SER B 1 393 ? 121.411 155.369 131.528 1.00 31.94 ?  393 SER B CB    1 
ATOM   8731  O  OG    . SER B 1 393 ? 120.334 155.448 132.445 1.00 43.25 ?  393 SER B OG    1 
ATOM   8732  N  N     . TYR B 1 394 ? 124.429 153.345 131.022 1.00 32.45 ?  394 TYR B N     1 
ATOM   8733  C  CA    . TYR B 1 394 ? 125.673 153.327 130.263 1.00 29.04 ?  394 TYR B CA    1 
ATOM   8734  C  C     . TYR B 1 394 ? 125.329 153.294 128.780 1.00 30.77 ?  394 TYR B C     1 
ATOM   8735  O  O     . TYR B 1 394 ? 124.794 152.300 128.280 1.00 34.55 ?  394 TYR B O     1 
ATOM   8736  C  CB    . TYR B 1 394 ? 126.530 152.132 130.664 1.00 28.80 ?  394 TYR B CB    1 
ATOM   8737  C  CG    . TYR B 1 394 ? 126.967 152.160 132.110 1.00 28.49 ?  394 TYR B CG    1 
ATOM   8738  C  CD1   . TYR B 1 394 ? 127.935 153.054 132.547 1.00 29.28 ?  394 TYR B CD1   1 
ATOM   8739  C  CD2   . TYR B 1 394 ? 126.407 151.295 133.039 1.00 25.63 ?  394 TYR B CD2   1 
ATOM   8740  C  CE1   . TYR B 1 394 ? 128.335 153.083 133.867 1.00 29.53 ?  394 TYR B CE1   1 
ATOM   8741  C  CE2   . TYR B 1 394 ? 126.800 151.316 134.360 1.00 26.56 ?  394 TYR B CE2   1 
ATOM   8742  C  CZ    . TYR B 1 394 ? 127.762 152.211 134.769 1.00 36.49 ?  394 TYR B CZ    1 
ATOM   8743  O  OH    . TYR B 1 394 ? 128.155 152.233 136.088 1.00 40.21 ?  394 TYR B OH    1 
ATOM   8744  N  N     . THR B 1 395 ? 125.627 154.382 128.084 1.00 38.04 ?  395 THR B N     1 
ATOM   8745  C  CA    . THR B 1 395 ? 125.251 154.553 126.691 1.00 33.83 ?  395 THR B CA    1 
ATOM   8746  C  C     . THR B 1 395 ? 126.369 154.040 125.786 1.00 37.74 ?  395 THR B C     1 
ATOM   8747  O  O     . THR B 1 395 ? 127.295 153.355 126.228 1.00 34.98 ?  395 THR B O     1 
ATOM   8748  C  CB    . THR B 1 395 ? 124.925 156.018 126.422 1.00 36.13 ?  395 THR B CB    1 
ATOM   8749  O  OG1   . THR B 1 395 ? 126.090 156.816 126.664 1.00 37.24 ?  395 THR B OG1   1 
ATOM   8750  C  CG2   . THR B 1 395 ? 123.806 156.486 127.336 1.00 35.65 ?  395 THR B CG2   1 
ATOM   8751  N  N     . ASP B 1 396 ? 126.287 154.365 124.498 1.00 40.82 ?  396 ASP B N     1 
ATOM   8752  C  CA    . ASP B 1 396 ? 127.324 153.975 123.558 1.00 34.89 ?  396 ASP B CA    1 
ATOM   8753  C  C     . ASP B 1 396 ? 128.641 154.668 123.902 1.00 39.22 ?  396 ASP B C     1 
ATOM   8754  O  O     . ASP B 1 396 ? 128.705 155.568 124.742 1.00 46.61 ?  396 ASP B O     1 
ATOM   8755  C  CB    . ASP B 1 396 ? 126.902 154.304 122.127 1.00 39.86 ?  396 ASP B CB    1 
ATOM   8756  C  CG    . ASP B 1 396 ? 125.695 153.506 121.676 1.00 45.72 ?  396 ASP B CG    1 
ATOM   8757  O  OD1   . ASP B 1 396 ? 125.675 152.278 121.904 1.00 42.96 ?  396 ASP B OD1   1 
ATOM   8758  O  OD2   . ASP B 1 396 ? 124.770 154.103 121.090 1.00 46.25 -1 396 ASP B OD2   1 
ATOM   8759  N  N     . TYR B 1 397 ? 129.707 154.229 123.231 1.00 32.24 ?  397 TYR B N     1 
ATOM   8760  C  CA    . TYR B 1 397 ? 131.044 154.715 123.559 1.00 34.09 ?  397 TYR B CA    1 
ATOM   8761  C  C     . TYR B 1 397 ? 131.162 156.218 123.335 1.00 34.30 ?  397 TYR B C     1 
ATOM   8762  O  O     . TYR B 1 397 ? 131.780 156.925 124.139 1.00 41.35 ?  397 TYR B O     1 
ATOM   8763  C  CB    . TYR B 1 397 ? 132.089 153.960 122.737 1.00 32.22 ?  397 TYR B CB    1 
ATOM   8764  C  CG    . TYR B 1 397 ? 133.506 154.447 122.934 1.00 31.70 ?  397 TYR B CG    1 
ATOM   8765  C  CD1   . TYR B 1 397 ? 134.022 155.480 122.162 1.00 32.38 ?  397 TYR B CD1   1 
ATOM   8766  C  CD2   . TYR B 1 397 ? 134.331 153.871 123.890 1.00 28.43 ?  397 TYR B CD2   1 
ATOM   8767  C  CE1   . TYR B 1 397 ? 135.311 155.926 122.339 1.00 33.34 ?  397 TYR B CE1   1 
ATOM   8768  C  CE2   . TYR B 1 397 ? 135.623 154.312 124.073 1.00 30.86 ?  397 TYR B CE2   1 
ATOM   8769  C  CZ    . TYR B 1 397 ? 136.108 155.339 123.295 1.00 36.04 ?  397 TYR B CZ    1 
ATOM   8770  O  OH    . TYR B 1 397 ? 137.396 155.783 123.472 1.00 39.42 ?  397 TYR B OH    1 
ATOM   8771  N  N     . ASP B 1 398 ? 130.583 156.724 122.246 1.00 43.33 ?  398 ASP B N     1 
ATOM   8772  C  CA    . ASP B 1 398 ? 130.712 158.143 121.934 1.00 43.51 ?  398 ASP B CA    1 
ATOM   8773  C  C     . ASP B 1 398 ? 129.848 159.010 122.841 1.00 47.22 ?  398 ASP B C     1 
ATOM   8774  O  O     . ASP B 1 398 ? 130.175 160.179 123.072 1.00 49.56 ?  398 ASP B O     1 
ATOM   8775  C  CB    . ASP B 1 398 ? 130.355 158.392 120.469 1.00 45.31 ?  398 ASP B CB    1 
ATOM   8776  C  CG    . ASP B 1 398 ? 129.131 157.613 120.028 1.00 49.08 ?  398 ASP B CG    1 
ATOM   8777  O  OD1   . ASP B 1 398 ? 129.115 156.377 120.209 1.00 47.02 ?  398 ASP B OD1   1 
ATOM   8778  O  OD2   . ASP B 1 398 ? 128.187 158.233 119.497 1.00 51.13 -1 398 ASP B OD2   1 
ATOM   8779  N  N     . GLU B 1 399 ? 128.754 158.464 123.360 1.00 46.85 ?  399 GLU B N     1 
ATOM   8780  C  CA    . GLU B 1 399 ? 127.804 159.231 124.149 1.00 42.12 ?  399 GLU B CA    1 
ATOM   8781  C  C     . GLU B 1 399 ? 128.250 159.327 125.606 1.00 48.56 ?  399 GLU B C     1 
ATOM   8782  O  O     . GLU B 1 399 ? 129.188 158.660 126.047 1.00 48.89 ?  399 GLU B O     1 
ATOM   8783  C  CB    . GLU B 1 399 ? 126.413 158.607 124.058 1.00 44.22 ?  399 GLU B CB    1 
ATOM   8784  C  CG    . GLU B 1 399 ? 125.732 158.808 122.720 1.00 48.53 ?  399 GLU B CG    1 
ATOM   8785  C  CD    . GLU B 1 399 ? 124.725 157.721 122.414 1.00 52.02 ?  399 GLU B CD    1 
ATOM   8786  O  OE1   . GLU B 1 399 ? 124.157 157.152 123.369 1.00 50.37 ?  399 GLU B OE1   1 
ATOM   8787  O  OE2   . GLU B 1 399 ? 124.500 157.437 121.219 1.00 53.71 -1 399 GLU B OE2   1 
ATOM   8788  N  N     . GLU B 1 400 ? 127.556 160.179 126.356 1.00 47.89 ?  400 GLU B N     1 
ATOM   8789  C  CA    . GLU B 1 400 ? 127.831 160.381 127.772 1.00 41.02 ?  400 GLU B CA    1 
ATOM   8790  C  C     . GLU B 1 400 ? 126.931 159.478 128.607 1.00 44.36 ?  400 GLU B C     1 
ATOM   8791  O  O     . GLU B 1 400 ? 125.715 159.438 128.397 1.00 43.18 ?  400 GLU B O     1 
ATOM   8792  C  CB    . GLU B 1 400 ? 127.615 161.843 128.161 1.00 41.65 ?  400 GLU B CB    1 
ATOM   8793  C  CG    . GLU B 1 400 ? 128.801 162.750 127.884 1.00 47.55 ?  400 GLU B CG    1 
ATOM   8794  C  CD    . GLU B 1 400 ? 130.048 162.332 128.639 1.00 52.56 ?  400 GLU B CD    1 
ATOM   8795  O  OE1   . GLU B 1 400 ? 129.924 161.903 129.805 1.00 52.78 ?  400 GLU B OE1   1 
ATOM   8796  O  OE2   . GLU B 1 400 ? 131.153 162.438 128.068 1.00 49.93 -1 400 GLU B OE2   1 
ATOM   8797  N  N     . ASP B 1 401 ? 127.532 158.760 129.550 1.00 42.88 ?  401 ASP B N     1 
ATOM   8798  C  CA    . ASP B 1 401 ? 126.780 157.860 130.409 1.00 37.73 ?  401 ASP B CA    1 
ATOM   8799  C  C     . ASP B 1 401 ? 126.031 158.635 131.486 1.00 39.48 ?  401 ASP B C     1 
ATOM   8800  O  O     . ASP B 1 401 ? 126.457 159.706 131.924 1.00 43.20 ?  401 ASP B O     1 
ATOM   8801  C  CB    . ASP B 1 401 ? 127.709 156.841 131.066 1.00 37.41 ?  401 ASP B CB    1 
ATOM   8802  C  CG    . ASP B 1 401 ? 128.400 155.947 130.062 1.00 40.11 ?  401 ASP B CG    1 
ATOM   8803  O  OD1   . ASP B 1 401 ? 127.774 155.602 129.038 1.00 44.10 ?  401 ASP B OD1   1 
ATOM   8804  O  OD2   . ASP B 1 401 ? 129.572 155.590 130.295 1.00 40.53 -1 401 ASP B OD2   1 
ATOM   8805  N  N     . GLU B 1 402 ? 124.903 158.074 131.912 1.00 38.02 ?  402 GLU B N     1 
ATOM   8806  C  CA    . GLU B 1 402 ? 124.114 158.619 133.013 1.00 32.62 ?  402 GLU B CA    1 
ATOM   8807  C  C     . GLU B 1 402 ? 124.434 157.794 134.254 1.00 34.97 ?  402 GLU B C     1 
ATOM   8808  O  O     . GLU B 1 402 ? 123.897 156.701 134.444 1.00 39.72 ?  402 GLU B O     1 
ATOM   8809  C  CB    . GLU B 1 402 ? 122.624 158.590 132.688 1.00 37.87 ?  402 GLU B CB    1 
ATOM   8810  C  CG    . GLU B 1 402 ? 121.929 159.956 132.554 1.00 41.50 ?  402 GLU B CG    1 
ATOM   8811  C  CD    . GLU B 1 402 ? 122.014 160.869 133.782 1.00 48.02 ?  402 GLU B CD    1 
ATOM   8812  O  OE1   . GLU B 1 402 ? 121.215 161.827 133.840 1.00 46.69 ?  402 GLU B OE1   1 
ATOM   8813  O  OE2   . GLU B 1 402 ? 122.835 160.644 134.696 1.00 49.75 -1 402 GLU B OE2   1 
ATOM   8814  N  N     . ILE B 1 403 ? 125.308 158.325 135.100 1.00 32.50 ?  403 ILE B N     1 
ATOM   8815  C  CA    . ILE B 1 403 ? 125.807 157.586 136.253 1.00 28.63 ?  403 ILE B CA    1 
ATOM   8816  C  C     . ILE B 1 403 ? 124.787 157.660 137.382 1.00 31.15 ?  403 ILE B C     1 
ATOM   8817  O  O     . ILE B 1 403 ? 124.327 158.746 137.752 1.00 32.16 ?  403 ILE B O     1 
ATOM   8818  C  CB    . ILE B 1 403 ? 127.169 158.137 136.697 1.00 23.85 ?  403 ILE B CB    1 
ATOM   8819  C  CG1   . ILE B 1 403 ? 128.218 157.901 135.607 1.00 26.86 ?  403 ILE B CG1   1 
ATOM   8820  C  CG2   . ILE B 1 403 ? 127.593 157.506 138.004 1.00 23.30 ?  403 ILE B CG2   1 
ATOM   8821  C  CD1   . ILE B 1 403 ? 128.291 156.473 135.129 1.00 31.86 ?  403 ILE B CD1   1 
ATOM   8822  N  N     . GLY B 1 404 ? 124.434 156.505 137.928 1.00 26.12 ?  404 GLY B N     1 
ATOM   8823  C  CA    . GLY B 1 404 ? 123.535 156.389 139.057 1.00 14.51 ?  404 GLY B CA    1 
ATOM   8824  C  C     . GLY B 1 404 ? 124.275 156.202 140.364 1.00 21.90 ?  404 GLY B C     1 
ATOM   8825  O  O     . GLY B 1 404 ? 125.397 156.686 140.547 1.00 34.25 ?  404 GLY B O     1 
ATOM   8826  N  N     . LEU B 1 405 ? 123.639 155.490 141.290 1.00 25.58 ?  405 LEU B N     1 
ATOM   8827  C  CA    . LEU B 1 405 ? 124.210 155.212 142.603 1.00 9.14  ?  405 LEU B CA    1 
ATOM   8828  C  C     . LEU B 1 405 ? 124.302 153.707 142.796 1.00 12.56 ?  405 LEU B C     1 
ATOM   8829  O  O     . LEU B 1 405 ? 123.280 153.015 142.791 1.00 20.84 ?  405 LEU B O     1 
ATOM   8830  C  CB    . LEU B 1 405 ? 123.369 155.841 143.713 1.00 19.52 ?  405 LEU B CB    1 
ATOM   8831  C  CG    . LEU B 1 405 ? 123.178 157.357 143.667 1.00 17.62 ?  405 LEU B CG    1 
ATOM   8832  C  CD1   . LEU B 1 405 ? 122.212 157.802 144.747 1.00 25.45 ?  405 LEU B CD1   1 
ATOM   8833  C  CD2   . LEU B 1 405 ? 124.509 158.071 143.810 1.00 19.08 ?  405 LEU B CD2   1 
ATOM   8834  N  N     . ASP B 1 406 ? 125.521 153.207 142.977 1.00 24.10 ?  406 ASP B N     1 
ATOM   8835  C  CA    . ASP B 1 406 ? 125.763 151.807 143.289 1.00 12.26 ?  406 ASP B CA    1 
ATOM   8836  C  C     . ASP B 1 406 ? 126.315 151.695 144.703 1.00 23.28 ?  406 ASP B C     1 
ATOM   8837  O  O     . ASP B 1 406 ? 127.221 152.439 145.087 1.00 34.31 ?  406 ASP B O     1 
ATOM   8838  C  CB    . ASP B 1 406 ? 126.733 151.173 142.292 1.00 18.39 ?  406 ASP B CB    1 
ATOM   8839  C  CG    . ASP B 1 406 ? 126.075 150.831 140.971 1.00 35.02 ?  406 ASP B CG    1 
ATOM   8840  O  OD1   . ASP B 1 406 ? 124.840 150.975 140.860 1.00 37.66 ?  406 ASP B OD1   1 
ATOM   8841  O  OD2   . ASP B 1 406 ? 126.797 150.416 140.041 1.00 32.49 -1 406 ASP B OD2   1 
ATOM   8842  N  N     . ILE B 1 407 ? 125.781 150.752 145.463 1.00 30.17 ?  407 ILE B N     1 
ATOM   8843  C  CA    . ILE B 1 407 ? 126.010 150.704 146.901 1.00 17.45 ?  407 ILE B CA    1 
ATOM   8844  C  C     . ILE B 1 407 ? 127.386 150.127 147.204 1.00 16.83 ?  407 ILE B C     1 
ATOM   8845  O  O     . ILE B 1 407 ? 127.828 149.155 146.579 1.00 24.89 ?  407 ILE B O     1 
ATOM   8846  C  CB    . ILE B 1 407 ? 124.902 149.888 147.587 1.00 10.96 ?  407 ILE B CB    1 
ATOM   8847  C  CG1   . ILE B 1 407 ? 123.528 150.468 147.261 1.00 4.34  ?  407 ILE B CG1   1 
ATOM   8848  C  CG2   . ILE B 1 407 ? 125.113 149.859 149.073 1.00 16.64 ?  407 ILE B CG2   1 
ATOM   8849  C  CD1   . ILE B 1 407 ? 122.483 149.417 147.028 1.00 18.14 ?  407 ILE B CD1   1 
ATOM   8850  N  N     . SER B 1 408 ? 128.066 150.737 148.170 1.00 28.19 ?  408 SER B N     1 
ATOM   8851  C  CA    . SER B 1 408 ? 129.317 150.209 148.711 1.00 25.83 ?  408 SER B CA    1 
ATOM   8852  C  C     . SER B 1 408 ? 129.539 150.857 150.066 1.00 27.97 ?  408 SER B C     1 
ATOM   8853  O  O     . SER B 1 408 ? 129.759 152.070 150.137 1.00 38.52 ?  408 SER B O     1 
ATOM   8854  C  CB    . SER B 1 408 ? 130.488 150.495 147.773 1.00 30.99 ?  408 SER B CB    1 
ATOM   8855  O  OG    . SER B 1 408 ? 131.140 151.703 148.126 1.00 34.38 ?  408 SER B OG    1 
ATOM   8856  N  N     . CYS B 1 409 ? 129.484 150.067 151.133 1.00 21.98 ?  409 CYS B N     1 
ATOM   8857  C  CA    . CYS B 1 409 ? 129.622 150.596 152.481 1.00 31.49 ?  409 CYS B CA    1 
ATOM   8858  C  C     . CYS B 1 409 ? 130.822 149.968 153.177 1.00 26.72 ?  409 CYS B C     1 
ATOM   8859  O  O     . CYS B 1 409 ? 131.259 148.863 152.846 1.00 25.56 ?  409 CYS B O     1 
ATOM   8860  C  CB    . CYS B 1 409 ? 128.344 150.374 153.306 1.00 27.84 ?  409 CYS B CB    1 
ATOM   8861  S  SG    . CYS B 1 409 ? 128.284 148.858 154.275 1.00 38.82 ?  409 CYS B SG    1 
ATOM   8862  N  N     . ASN B 1 410 ? 131.354 150.702 154.149 1.00 22.62 ?  410 ASN B N     1 
ATOM   8863  C  CA    . ASN B 1 410 ? 132.560 150.319 154.868 1.00 22.90 ?  410 ASN B CA    1 
ATOM   8864  C  C     . ASN B 1 410 ? 132.169 149.633 156.168 1.00 24.05 ?  410 ASN B C     1 
ATOM   8865  O  O     . ASN B 1 410 ? 131.283 150.110 156.882 1.00 31.21 ?  410 ASN B O     1 
ATOM   8866  C  CB    . ASN B 1 410 ? 133.425 151.547 155.142 1.00 28.30 ?  410 ASN B CB    1 
ATOM   8867  C  CG    . ASN B 1 410 ? 133.320 152.582 154.041 1.00 37.57 ?  410 ASN B CG    1 
ATOM   8868  O  OD1   . ASN B 1 410 ? 134.263 152.786 153.279 1.00 42.49 ?  410 ASN B OD1   1 
ATOM   8869  N  ND2   . ASN B 1 410 ? 132.182 153.258 153.968 1.00 31.73 ?  410 ASN B ND2   1 
ATOM   8870  N  N     . LEU B 1 411 ? 132.834 148.525 156.474 1.00 16.74 ?  411 LEU B N     1 
ATOM   8871  C  CA    . LEU B 1 411 ? 132.424 147.643 157.556 1.00 9.81  ?  411 LEU B CA    1 
ATOM   8872  C  C     . LEU B 1 411 ? 133.312 147.814 158.781 1.00 13.17 ?  411 LEU B C     1 
ATOM   8873  O  O     . LEU B 1 411 ? 134.527 147.995 158.667 1.00 24.64 ?  411 LEU B O     1 
ATOM   8874  C  CB    . LEU B 1 411 ? 132.459 146.184 157.101 1.00 20.83 ?  411 LEU B CB    1 
ATOM   8875  C  CG    . LEU B 1 411 ? 131.614 145.796 155.891 1.00 19.90 ?  411 LEU B CG    1 
ATOM   8876  C  CD1   . LEU B 1 411 ? 131.387 144.304 155.882 1.00 25.47 ?  411 LEU B CD1   1 
ATOM   8877  C  CD2   . LEU B 1 411 ? 130.289 146.518 155.936 1.00 18.66 ?  411 LEU B CD2   1 
ATOM   8878  N  N     . GLY B 1 412 ? 132.684 147.764 159.951 1.00 18.40 ?  412 GLY B N     1 
ATOM   8879  C  CA    . GLY B 1 412 ? 133.396 147.703 161.212 1.00 4.64  ?  412 GLY B CA    1 
ATOM   8880  C  C     . GLY B 1 412 ? 132.511 147.024 162.231 1.00 11.43 ?  412 GLY B C     1 
ATOM   8881  O  O     . GLY B 1 412 ? 131.282 147.046 162.122 1.00 29.68 ?  412 GLY B O     1 
ATOM   8882  N  N     . SER B 1 413 ? 133.145 146.412 163.227 1.00 13.53 ?  413 SER B N     1 
ATOM   8883  C  CA    . SER B 1 413 ? 132.420 145.625 164.215 1.00 14.25 ?  413 SER B CA    1 
ATOM   8884  C  C     . SER B 1 413 ? 132.815 146.033 165.623 1.00 15.86 ?  413 SER B C     1 
ATOM   8885  O  O     . SER B 1 413 ? 134.001 146.049 165.961 1.00 23.31 ?  413 SER B O     1 
ATOM   8886  C  CB    . SER B 1 413 ? 132.671 144.129 164.022 1.00 10.59 ?  413 SER B CB    1 
ATOM   8887  O  OG    . SER B 1 413 ? 131.966 143.647 162.898 1.00 30.53 ?  413 SER B OG    1 
ATOM   8888  N  N     . LEU B 1 414 ? 131.817 146.359 166.437 1.00 17.46 ?  414 LEU B N     1 
ATOM   8889  C  CA    . LEU B 1 414 ? 132.033 146.483 167.869 1.00 9.58  ?  414 LEU B CA    1 
ATOM   8890  C  C     . LEU B 1 414 ? 132.116 145.102 168.498 1.00 20.99 ?  414 LEU B C     1 
ATOM   8891  O  O     . LEU B 1 414 ? 131.356 144.196 168.147 1.00 27.41 ?  414 LEU B O     1 
ATOM   8892  C  CB    . LEU B 1 414 ? 130.900 147.272 168.520 1.00 19.06 ?  414 LEU B CB    1 
ATOM   8893  C  CG    . LEU B 1 414 ? 130.443 148.573 167.868 1.00 20.59 ?  414 LEU B CG    1 
ATOM   8894  C  CD1   . LEU B 1 414 ? 129.182 149.064 168.545 1.00 23.38 ?  414 LEU B CD1   1 
ATOM   8895  C  CD2   . LEU B 1 414 ? 131.533 149.620 167.947 1.00 25.08 ?  414 LEU B CD2   1 
ATOM   8896  N  N     . ASN B 1 415 ? 133.048 144.938 169.426 1.00 30.18 ?  415 ASN B N     1 
ATOM   8897  C  CA    . ASN B 1 415 ? 133.097 143.744 170.260 1.00 26.52 ?  415 ASN B CA    1 
ATOM   8898  C  C     . ASN B 1 415 ? 132.181 143.986 171.452 1.00 24.97 ?  415 ASN B C     1 
ATOM   8899  O  O     . ASN B 1 415 ? 132.508 144.777 172.341 1.00 29.48 ?  415 ASN B O     1 
ATOM   8900  C  CB    . ASN B 1 415 ? 134.527 143.448 170.699 1.00 21.57 ?  415 ASN B CB    1 
ATOM   8901  C  CG    . ASN B 1 415 ? 134.702 142.037 171.213 1.00 21.47 ?  415 ASN B CG    1 
ATOM   8902  O  OD1   . ASN B 1 415 ? 133.958 141.581 172.079 1.00 37.85 ?  415 ASN B OD1   1 
ATOM   8903  N  ND2   . ASN B 1 415 ? 135.693 141.335 170.682 1.00 29.64 ?  415 ASN B ND2   1 
ATOM   8904  N  N     . ILE B 1 416 ? 131.029 143.313 171.462 1.00 17.78 ?  416 ILE B N     1 
ATOM   8905  C  CA    . ILE B 1 416 ? 130.014 143.579 172.478 1.00 21.17 ?  416 ILE B CA    1 
ATOM   8906  C  C     . ILE B 1 416 ? 130.551 143.265 173.868 1.00 28.90 ?  416 ILE B C     1 
ATOM   8907  O  O     . ILE B 1 416 ? 130.285 143.996 174.829 1.00 27.87 ?  416 ILE B O     1 
ATOM   8908  C  CB    . ILE B 1 416 ? 128.729 142.790 172.165 1.00 27.96 ?  416 ILE B CB    1 
ATOM   8909  C  CG1   . ILE B 1 416 ? 128.058 143.352 170.911 1.00 20.31 ?  416 ILE B CG1   1 
ATOM   8910  C  CG2   . ILE B 1 416 ? 127.764 142.833 173.334 1.00 9.74  ?  416 ILE B CG2   1 
ATOM   8911  C  CD1   . ILE B 1 416 ? 126.875 142.549 170.434 1.00 15.27 ?  416 ILE B CD1   1 
ATOM   8912  N  N     . LEU B 1 417 ? 131.327 142.189 173.997 1.00 21.36 ?  417 LEU B N     1 
ATOM   8913  C  CA    . LEU B 1 417 ? 131.886 141.832 175.298 1.00 26.32 ?  417 LEU B CA    1 
ATOM   8914  C  C     . LEU B 1 417 ? 132.853 142.900 175.799 1.00 30.42 ?  417 LEU B C     1 
ATOM   8915  O  O     . LEU B 1 417 ? 132.766 143.340 176.952 1.00 38.35 ?  417 LEU B O     1 
ATOM   8916  C  CB    . LEU B 1 417 ? 132.582 140.475 175.213 1.00 29.69 ?  417 LEU B CB    1 
ATOM   8917  C  CG    . LEU B 1 417 ? 133.413 140.046 176.423 1.00 30.91 ?  417 LEU B CG    1 
ATOM   8918  C  CD1   . LEU B 1 417 ? 132.536 139.408 177.482 1.00 28.98 ?  417 LEU B CD1   1 
ATOM   8919  C  CD2   . LEU B 1 417 ? 134.519 139.097 176.000 1.00 35.30 ?  417 LEU B CD2   1 
ATOM   8920  N  N     . ASN B 1 418 ? 133.776 143.338 174.943 1.00 30.35 ?  418 ASN B N     1 
ATOM   8921  C  CA    . ASN B 1 418 ? 134.775 144.316 175.357 1.00 27.79 ?  418 ASN B CA    1 
ATOM   8922  C  C     . ASN B 1 418 ? 134.188 145.713 175.506 1.00 29.87 ?  418 ASN B C     1 
ATOM   8923  O  O     . ASN B 1 418 ? 134.609 146.465 176.391 1.00 34.48 ?  418 ASN B O     1 
ATOM   8924  C  CB    . ASN B 1 418 ? 135.933 144.334 174.362 1.00 25.73 ?  418 ASN B CB    1 
ATOM   8925  C  CG    . ASN B 1 418 ? 136.779 143.082 174.438 1.00 26.42 ?  418 ASN B CG    1 
ATOM   8926  O  OD1   . ASN B 1 418 ? 136.971 142.517 175.512 1.00 34.90 ?  418 ASN B OD1   1 
ATOM   8927  N  ND2   . ASN B 1 418 ? 137.286 142.639 173.297 1.00 30.58 ?  418 ASN B ND2   1 
ATOM   8928  N  N     . VAL B 1 419 ? 133.232 146.078 174.652 1.00 32.67 ?  419 VAL B N     1 
ATOM   8929  C  CA    . VAL B 1 419 ? 132.555 147.361 174.799 1.00 31.64 ?  419 VAL B CA    1 
ATOM   8930  C  C     . VAL B 1 419 ? 131.730 147.381 176.079 1.00 30.72 ?  419 VAL B C     1 
ATOM   8931  O  O     . VAL B 1 419 ? 131.661 148.399 176.777 1.00 33.42 ?  419 VAL B O     1 
ATOM   8932  C  CB    . VAL B 1 419 ? 131.692 147.643 173.555 1.00 28.04 ?  419 VAL B CB    1 
ATOM   8933  C  CG1   . VAL B 1 419 ? 130.668 148.719 173.839 1.00 33.19 ?  419 VAL B CG1   1 
ATOM   8934  C  CG2   . VAL B 1 419 ? 132.569 148.041 172.386 1.00 24.47 ?  419 VAL B CG2   1 
ATOM   8935  N  N     . MET B 1 420 ? 131.111 146.250 176.417 1.00 36.25 ?  420 MET B N     1 
ATOM   8936  C  CA    . MET B 1 420 ? 130.265 146.184 177.601 1.00 33.76 ?  420 MET B CA    1 
ATOM   8937  C  C     . MET B 1 420 ? 131.099 146.173 178.876 1.00 31.81 ?  420 MET B C     1 
ATOM   8938  O  O     . MET B 1 420 ? 130.726 146.798 179.874 1.00 34.69 ?  420 MET B O     1 
ATOM   8939  C  CB    . MET B 1 420 ? 129.377 144.943 177.523 1.00 33.22 ?  420 MET B CB    1 
ATOM   8940  C  CG    . MET B 1 420 ? 127.982 145.199 176.977 1.00 24.56 ?  420 MET B CG    1 
ATOM   8941  S  SD    . MET B 1 420 ? 127.366 146.853 177.320 1.00 41.26 ?  420 MET B SD    1 
ATOM   8942  C  CE    . MET B 1 420 ? 126.630 146.590 178.926 1.00 33.19 ?  420 MET B CE    1 
ATOM   8943  N  N     . GLU B 1 421 ? 132.236 145.469 178.861 1.00 39.01 ?  421 GLU B N     1 
ATOM   8944  C  CA    . GLU B 1 421 ? 133.092 145.424 180.041 1.00 38.31 ?  421 GLU B CA    1 
ATOM   8945  C  C     . GLU B 1 421 ? 133.797 146.755 180.281 1.00 36.84 ?  421 GLU B C     1 
ATOM   8946  O  O     . GLU B 1 421 ? 134.100 147.093 181.429 1.00 39.33 ?  421 GLU B O     1 
ATOM   8947  C  CB    . GLU B 1 421 ? 134.107 144.285 179.912 1.00 33.75 ?  421 GLU B CB    1 
ATOM   8948  C  CG    . GLU B 1 421 ? 135.369 144.641 179.143 1.00 38.99 ?  421 GLU B CG    1 
ATOM   8949  C  CD    . GLU B 1 421 ? 136.448 143.583 179.256 1.00 46.20 ?  421 GLU B CD    1 
ATOM   8950  O  OE1   . GLU B 1 421 ? 137.233 143.630 180.226 1.00 43.21 ?  421 GLU B OE1   1 
ATOM   8951  O  OE2   . GLU B 1 421 ? 136.513 142.704 178.371 1.00 43.32 -1 421 GLU B OE2   1 
ATOM   8952  N  N     . HIS B 1 422 ? 134.066 147.517 179.222 1.00 36.68 ?  422 HIS B N     1 
ATOM   8953  C  CA    . HIS B 1 422 ? 134.684 148.828 179.354 1.00 37.50 ?  422 HIS B CA    1 
ATOM   8954  C  C     . HIS B 1 422 ? 133.672 149.940 179.590 1.00 41.79 ?  422 HIS B C     1 
ATOM   8955  O  O     . HIS B 1 422 ? 134.080 151.077 179.852 1.00 45.27 ?  422 HIS B O     1 
ATOM   8956  C  CB    . HIS B 1 422 ? 135.510 149.160 178.107 1.00 35.17 ?  422 HIS B CB    1 
ATOM   8957  C  CG    . HIS B 1 422 ? 136.879 148.555 178.105 1.00 38.00 ?  422 HIS B CG    1 
ATOM   8958  N  ND1   . HIS B 1 422 ? 137.093 147.197 178.027 1.00 39.87 ?  422 HIS B ND1   1 
ATOM   8959  C  CD2   . HIS B 1 422 ? 138.105 149.125 178.168 1.00 40.59 ?  422 HIS B CD2   1 
ATOM   8960  C  CE1   . HIS B 1 422 ? 138.392 146.955 178.045 1.00 41.07 ?  422 HIS B CE1   1 
ATOM   8961  N  NE2   . HIS B 1 422 ? 139.028 148.108 178.130 1.00 42.75 ?  422 HIS B NE2   1 
ATOM   8962  N  N     . LYS B 1 423 ? 132.374 149.638 179.507 1.00 43.51 ?  423 LYS B N     1 
ATOM   8963  C  CA    . LYS B 1 423 ? 131.314 150.631 179.678 1.00 44.04 ?  423 LYS B CA    1 
ATOM   8964  C  C     . LYS B 1 423 ? 131.503 151.804 178.721 1.00 47.14 ?  423 LYS B C     1 
ATOM   8965  O  O     . LYS B 1 423 ? 131.322 152.968 179.083 1.00 48.45 ?  423 LYS B O     1 
ATOM   8966  C  CB    . LYS B 1 423 ? 131.242 151.114 181.128 1.00 43.16 ?  423 LYS B CB    1 
ATOM   8967  C  CG    . LYS B 1 423 ? 130.660 150.100 182.094 1.00 44.78 ?  423 LYS B CG    1 
ATOM   8968  C  CD    . LYS B 1 423 ? 131.675 149.710 183.155 1.00 48.99 ?  423 LYS B CD    1 
ATOM   8969  C  CE    . LYS B 1 423 ? 131.207 148.504 183.954 1.00 47.55 ?  423 LYS B CE    1 
ATOM   8970  N  NZ    . LYS B 1 423 ? 131.695 147.223 183.373 1.00 42.92 1  423 LYS B NZ    1 
ATOM   8971  N  N     . SER B 1 424 ? 131.865 151.490 177.482 1.00 32.45 ?  424 SER B N     1 
ATOM   8972  C  CA    . SER B 1 424 ? 132.247 152.488 176.490 1.00 32.35 ?  424 SER B CA    1 
ATOM   8973  C  C     . SER B 1 424 ? 131.462 152.300 175.200 1.00 36.47 ?  424 SER B C     1 
ATOM   8974  O  O     . SER B 1 424 ? 132.026 152.250 174.107 1.00 38.35 ?  424 SER B O     1 
ATOM   8975  C  CB    . SER B 1 424 ? 133.746 152.425 176.215 1.00 36.99 ?  424 SER B CB    1 
ATOM   8976  O  OG    . SER B 1 424 ? 134.090 151.232 175.534 1.00 34.67 ?  424 SER B OG    1 
ATOM   8977  N  N     . ILE B 1 425 ? 130.138 152.183 175.308 1.00 35.88 ?  425 ILE B N     1 
ATOM   8978  C  CA    . ILE B 1 425 ? 129.315 152.103 174.103 1.00 28.36 ?  425 ILE B CA    1 
ATOM   8979  C  C     . ILE B 1 425 ? 129.419 153.398 173.308 1.00 34.18 ?  425 ILE B C     1 
ATOM   8980  O  O     . ILE B 1 425 ? 129.660 153.386 172.097 1.00 39.14 ?  425 ILE B O     1 
ATOM   8981  C  CB    . ILE B 1 425 ? 127.854 151.782 174.462 1.00 33.41 ?  425 ILE B CB    1 
ATOM   8982  C  CG1   . ILE B 1 425 ? 127.730 150.356 174.994 1.00 33.95 ?  425 ILE B CG1   1 
ATOM   8983  C  CG2   . ILE B 1 425 ? 126.958 151.969 173.249 1.00 29.70 ?  425 ILE B CG2   1 
ATOM   8984  C  CD1   . ILE B 1 425 ? 126.312 149.951 175.314 1.00 34.91 ?  425 ILE B CD1   1 
ATOM   8985  N  N     . GLU B 1 426 ? 129.267 154.535 173.988 1.00 32.69 ?  426 GLU B N     1 
ATOM   8986  C  CA    . GLU B 1 426 ? 129.273 155.823 173.299 1.00 31.07 ?  426 GLU B CA    1 
ATOM   8987  C  C     . GLU B 1 426 ? 130.617 156.096 172.638 1.00 31.81 ?  426 GLU B C     1 
ATOM   8988  O  O     . GLU B 1 426 ? 130.682 156.415 171.445 1.00 42.23 ?  426 GLU B O     1 
ATOM   8989  C  CB    . GLU B 1 426 ? 128.922 156.935 174.286 1.00 32.52 ?  426 GLU B CB    1 
ATOM   8990  C  CG    . GLU B 1 426 ? 129.273 158.329 173.805 1.00 33.06 ?  426 GLU B CG    1 
ATOM   8991  C  CD    . GLU B 1 426 ? 129.076 159.376 174.880 1.00 42.02 ?  426 GLU B CD    1 
ATOM   8992  O  OE1   . GLU B 1 426 ? 128.771 158.996 176.029 1.00 42.80 ?  426 GLU B OE1   1 
ATOM   8993  O  OE2   . GLU B 1 426 ? 129.230 160.577 174.580 1.00 46.74 -1 426 GLU B OE2   1 
ATOM   8994  N  N     . LYS B 1 427 ? 131.705 155.973 173.401 1.00 33.13 ?  427 LYS B N     1 
ATOM   8995  C  CA    . LYS B 1 427 ? 133.024 156.306 172.876 1.00 31.12 ?  427 LYS B CA    1 
ATOM   8996  C  C     . LYS B 1 427 ? 133.429 155.360 171.755 1.00 32.71 ?  427 LYS B C     1 
ATOM   8997  O  O     . LYS B 1 427 ? 133.936 155.803 170.717 1.00 37.83 ?  427 LYS B O     1 
ATOM   8998  C  CB    . LYS B 1 427 ? 134.084 156.295 173.988 1.00 34.87 ?  427 LYS B CB    1 
ATOM   8999  C  CG    . LYS B 1 427 ? 134.045 157.453 175.014 1.00 41.24 ?  427 LYS B CG    1 
ATOM   9000  C  CD    . LYS B 1 427 ? 132.792 157.567 175.899 1.00 40.26 ?  427 LYS B CD    1 
ATOM   9001  C  CE    . LYS B 1 427 ? 132.236 156.214 176.335 1.00 36.14 ?  427 LYS B CE    1 
ATOM   9002  N  NZ    . LYS B 1 427 ? 131.131 156.347 177.322 1.00 40.00 1  427 LYS B NZ    1 
ATOM   9003  N  N     . THR B 1 428 ? 133.216 154.056 171.943 1.00 28.98 ?  428 THR B N     1 
ATOM   9004  C  CA    . THR B 1 428 ? 133.560 153.101 170.896 1.00 24.30 ?  428 THR B CA    1 
ATOM   9005  C  C     . THR B 1 428 ? 132.726 153.328 169.645 1.00 26.69 ?  428 THR B C     1 
ATOM   9006  O  O     . THR B 1 428 ? 133.253 153.283 168.528 1.00 34.84 ?  428 THR B O     1 
ATOM   9007  C  CB    . THR B 1 428 ? 133.388 151.666 171.394 1.00 21.44 ?  428 THR B CB    1 
ATOM   9008  O  OG1   . THR B 1 428 ? 134.055 151.511 172.652 1.00 25.87 ?  428 THR B OG1   1 
ATOM   9009  C  CG2   . THR B 1 428 ? 133.972 150.690 170.393 1.00 27.34 ?  428 THR B CG2   1 
ATOM   9010  N  N     . VAL B 1 429 ? 131.425 153.578 169.807 1.00 26.34 ?  429 VAL B N     1 
ATOM   9011  C  CA    . VAL B 1 429 ? 130.567 153.799 168.647 1.00 23.04 ?  429 VAL B CA    1 
ATOM   9012  C  C     . VAL B 1 429 ? 131.008 155.041 167.887 1.00 24.84 ?  429 VAL B C     1 
ATOM   9013  O  O     . VAL B 1 429 ? 131.100 155.030 166.654 1.00 30.08 ?  429 VAL B O     1 
ATOM   9014  C  CB    . VAL B 1 429 ? 129.090 153.891 169.078 1.00 24.85 ?  429 VAL B CB    1 
ATOM   9015  C  CG1   . VAL B 1 429 ? 128.276 154.610 168.025 1.00 23.31 ?  429 VAL B CG1   1 
ATOM   9016  C  CG2   . VAL B 1 429 ? 128.519 152.510 169.309 1.00 26.10 ?  429 VAL B CG2   1 
ATOM   9017  N  N     . LYS B 1 430 ? 131.307 156.125 168.604 1.00 29.56 ?  430 LYS B N     1 
ATOM   9018  C  CA    . LYS B 1 430 ? 131.680 157.364 167.930 1.00 24.43 ?  430 LYS B CA    1 
ATOM   9019  C  C     . LYS B 1 430 ? 133.041 157.249 167.252 1.00 23.08 ?  430 LYS B C     1 
ATOM   9020  O  O     . LYS B 1 430 ? 133.219 157.729 166.126 1.00 31.25 ?  430 LYS B O     1 
ATOM   9021  C  CB    . LYS B 1 430 ? 131.651 158.524 168.923 1.00 26.41 ?  430 LYS B CB    1 
ATOM   9022  C  CG    . LYS B 1 430 ? 130.246 158.857 169.395 1.00 23.26 ?  430 LYS B CG    1 
ATOM   9023  C  CD    . LYS B 1 430 ? 130.188 160.185 170.119 1.00 31.44 ?  430 LYS B CD    1 
ATOM   9024  C  CE    . LYS B 1 430 ? 128.755 160.549 170.459 1.00 34.84 ?  430 LYS B CE    1 
ATOM   9025  N  NZ    . LYS B 1 430 ? 128.673 161.808 171.245 1.00 36.10 1  430 LYS B NZ    1 
ATOM   9026  N  N     . LEU B 1 431 ? 134.013 156.609 167.907 1.00 30.77 ?  431 LEU B N     1 
ATOM   9027  C  CA    . LEU B 1 431 ? 135.319 156.429 167.280 1.00 22.41 ?  431 LEU B CA    1 
ATOM   9028  C  C     . LEU B 1 431 ? 135.233 155.497 166.076 1.00 23.25 ?  431 LEU B C     1 
ATOM   9029  O  O     . LEU B 1 431 ? 135.901 155.724 165.060 1.00 32.08 ?  431 LEU B O     1 
ATOM   9030  C  CB    . LEU B 1 431 ? 136.323 155.901 168.302 1.00 30.91 ?  431 LEU B CB    1 
ATOM   9031  C  CG    . LEU B 1 431 ? 137.168 156.947 169.028 1.00 32.90 ?  431 LEU B CG    1 
ATOM   9032  C  CD1   . LEU B 1 431 ? 137.977 156.297 170.136 1.00 28.93 ?  431 LEU B CD1   1 
ATOM   9033  C  CD2   . LEU B 1 431 ? 138.076 157.673 168.054 1.00 34.52 ?  431 LEU B CD2   1 
ATOM   9034  N  N     . ALA B 1 432 ? 134.422 154.440 166.171 1.00 25.20 ?  432 ALA B N     1 
ATOM   9035  C  CA    . ALA B 1 432 ? 134.218 153.555 165.033 1.00 20.02 ?  432 ALA B CA    1 
ATOM   9036  C  C     . ALA B 1 432 ? 133.546 154.289 163.883 1.00 25.84 ?  432 ALA B C     1 
ATOM   9037  O  O     . ALA B 1 432 ? 133.886 154.071 162.716 1.00 29.63 ?  432 ALA B O     1 
ATOM   9038  C  CB    . ALA B 1 432 ? 133.391 152.343 165.456 1.00 24.13 ?  432 ALA B CB    1 
ATOM   9039  N  N     . THR B 1 433 ? 132.584 155.161 164.194 1.00 27.18 ?  433 THR B N     1 
ATOM   9040  C  CA    . THR B 1 433 ? 131.956 155.977 163.162 1.00 17.25 ?  433 THR B CA    1 
ATOM   9041  C  C     . THR B 1 433 ? 132.974 156.888 162.492 1.00 25.04 ?  433 THR B C     1 
ATOM   9042  O  O     . THR B 1 433 ? 132.968 157.040 161.266 1.00 33.17 ?  433 THR B O     1 
ATOM   9043  C  CB    . THR B 1 433 ? 130.815 156.796 163.769 1.00 24.03 ?  433 THR B CB    1 
ATOM   9044  O  OG1   . THR B 1 433 ? 129.871 155.915 164.387 1.00 32.99 ?  433 THR B OG1   1 
ATOM   9045  C  CG2   . THR B 1 433 ? 130.109 157.612 162.699 1.00 24.11 ?  433 THR B CG2   1 
ATOM   9046  N  N     . ASP B 1 434 ? 133.860 157.500 163.279 1.00 24.94 ?  434 ASP B N     1 
ATOM   9047  C  CA    . ASP B 1 434 ? 134.898 158.352 162.705 1.00 18.95 ?  434 ASP B CA    1 
ATOM   9048  C  C     . ASP B 1 434 ? 135.830 157.558 161.796 1.00 19.23 ?  434 ASP B C     1 
ATOM   9049  O  O     . ASP B 1 434 ? 136.184 158.016 160.702 1.00 26.71 ?  434 ASP B O     1 
ATOM   9050  C  CB    . ASP B 1 434 ? 135.692 159.033 163.818 1.00 25.35 ?  434 ASP B CB    1 
ATOM   9051  C  CG    . ASP B 1 434 ? 134.890 160.088 164.544 1.00 31.05 ?  434 ASP B CG    1 
ATOM   9052  O  OD1   . ASP B 1 434 ? 133.972 160.666 163.928 1.00 36.85 ?  434 ASP B OD1   1 
ATOM   9053  O  OD2   . ASP B 1 434 ? 135.177 160.340 165.732 1.00 33.18 -1 434 ASP B OD2   1 
ATOM   9054  N  N     . SER B 1 435 ? 136.238 156.365 162.231 1.00 22.83 ?  435 SER B N     1 
ATOM   9055  C  CA    . SER B 1 435 ? 137.134 155.545 161.418 1.00 15.90 ?  435 SER B CA    1 
ATOM   9056  C  C     . SER B 1 435 ? 136.458 155.088 160.131 1.00 23.26 ?  435 SER B C     1 
ATOM   9057  O  O     . SER B 1 435 ? 137.077 155.098 159.059 1.00 31.44 ?  435 SER B O     1 
ATOM   9058  C  CB    . SER B 1 435 ? 137.623 154.344 162.228 1.00 21.15 ?  435 SER B CB    1 
ATOM   9059  O  OG    . SER B 1 435 ? 136.574 153.424 162.465 1.00 22.23 ?  435 SER B OG    1 
ATOM   9060  N  N     . LEU B 1 436 ? 135.191 154.679 160.215 1.00 18.81 ?  436 LEU B N     1 
ATOM   9061  C  CA    . LEU B 1 436 ? 134.459 154.272 159.022 1.00 11.47 ?  436 LEU B CA    1 
ATOM   9062  C  C     . LEU B 1 436 ? 134.257 155.445 158.075 1.00 19.15 ?  436 LEU B C     1 
ATOM   9063  O  O     . LEU B 1 436 ? 134.334 155.284 156.852 1.00 31.33 ?  436 LEU B O     1 
ATOM   9064  C  CB    . LEU B 1 436 ? 133.118 153.659 159.419 1.00 22.51 ?  436 LEU B CB    1 
ATOM   9065  C  CG    . LEU B 1 436 ? 133.194 152.298 160.107 1.00 18.95 ?  436 LEU B CG    1 
ATOM   9066  C  CD1   . LEU B 1 436 ? 131.909 152.008 160.856 1.00 16.54 ?  436 LEU B CD1   1 
ATOM   9067  C  CD2   . LEU B 1 436 ? 133.485 151.214 159.094 1.00 20.71 ?  436 LEU B CD2   1 
ATOM   9068  N  N     . THR B 1 437 ? 134.004 156.636 158.620 1.00 22.48 ?  437 THR B N     1 
ATOM   9069  C  CA    . THR B 1 437 ? 133.915 157.830 157.790 1.00 19.89 ?  437 THR B CA    1 
ATOM   9070  C  C     . THR B 1 437 ? 135.231 158.098 157.075 1.00 24.99 ?  437 THR B C     1 
ATOM   9071  O  O     . THR B 1 437 ? 135.241 158.415 155.881 1.00 35.50 ?  437 THR B O     1 
ATOM   9072  C  CB    . THR B 1 437 ? 133.515 159.032 158.643 1.00 15.98 ?  437 THR B CB    1 
ATOM   9073  O  OG1   . THR B 1 437 ? 132.288 158.747 159.323 1.00 16.78 ?  437 THR B OG1   1 
ATOM   9074  C  CG2   . THR B 1 437 ? 133.335 160.264 157.780 1.00 21.42 ?  437 THR B CG2   1 
ATOM   9075  N  N     . HIS B 1 438 ? 136.354 157.974 157.788 1.00 18.58 ?  438 HIS B N     1 
ATOM   9076  C  CA    . HIS B 1 438 ? 137.654 158.172 157.154 1.00 18.73 ?  438 HIS B CA    1 
ATOM   9077  C  C     . HIS B 1 438 ? 137.882 157.161 156.038 1.00 20.69 ?  438 HIS B C     1 
ATOM   9078  O  O     . HIS B 1 438 ? 138.369 157.516 154.957 1.00 32.55 ?  438 HIS B O     1 
ATOM   9079  C  CB    . HIS B 1 438 ? 138.771 158.079 158.192 1.00 25.97 ?  438 HIS B CB    1 
ATOM   9080  C  CG    . HIS B 1 438 ? 140.144 158.140 157.601 1.00 28.78 ?  438 HIS B CG    1 
ATOM   9081  N  ND1   . HIS B 1 438 ? 140.785 159.329 157.328 1.00 26.69 ?  438 HIS B ND1   1 
ATOM   9082  C  CD2   . HIS B 1 438 ? 140.994 157.159 157.215 1.00 30.25 ?  438 HIS B CD2   1 
ATOM   9083  C  CE1   . HIS B 1 438 ? 141.972 159.078 156.807 1.00 27.89 ?  438 HIS B CE1   1 
ATOM   9084  N  NE2   . HIS B 1 438 ? 142.123 157.769 156.727 1.00 30.94 ?  438 HIS B NE2   1 
ATOM   9085  N  N     . VAL B 1 439 ? 137.536 155.896 156.280 1.00 23.92 ?  439 VAL B N     1 
ATOM   9086  C  CA    . VAL B 1 439 ? 137.690 154.874 155.247 1.00 17.52 ?  439 VAL B CA    1 
ATOM   9087  C  C     . VAL B 1 439 ? 136.820 155.205 154.041 1.00 27.55 ?  439 VAL B C     1 
ATOM   9088  O  O     . VAL B 1 439 ? 137.226 155.010 152.890 1.00 34.37 ?  439 VAL B O     1 
ATOM   9089  C  CB    . VAL B 1 439 ? 137.366 153.481 155.818 1.00 22.88 ?  439 VAL B CB    1 
ATOM   9090  C  CG1   . VAL B 1 439 ? 137.344 152.439 154.713 1.00 25.20 ?  439 VAL B CG1   1 
ATOM   9091  C  CG2   . VAL B 1 439 ? 138.372 153.100 156.882 1.00 21.17 ?  439 VAL B CG2   1 
ATOM   9092  N  N     . SER B 1 440 ? 135.609 155.710 154.287 1.00 27.83 ?  440 SER B N     1 
ATOM   9093  C  CA    . SER B 1 440 ? 134.726 156.090 153.189 1.00 17.71 ?  440 SER B CA    1 
ATOM   9094  C  C     . SER B 1 440 ? 135.313 157.232 152.369 1.00 23.44 ?  440 SER B C     1 
ATOM   9095  O  O     . SER B 1 440 ? 135.287 157.194 151.134 1.00 33.92 ?  440 SER B O     1 
ATOM   9096  C  CB    . SER B 1 440 ? 133.351 156.471 153.740 1.00 26.57 ?  440 SER B CB    1 
ATOM   9097  O  OG    . SER B 1 440 ? 132.393 156.578 152.703 1.00 33.83 ?  440 SER B OG    1 
ATOM   9098  N  N     . GLU B 1 441 ? 135.844 158.261 153.037 1.00 24.94 ?  441 GLU B N     1 
ATOM   9099  C  CA    . GLU B 1 441 ? 136.412 159.394 152.307 1.00 20.17 ?  441 GLU B CA    1 
ATOM   9100  C  C     . GLU B 1 441 ? 137.662 158.998 151.532 1.00 29.91 ?  441 GLU B C     1 
ATOM   9101  O  O     . GLU B 1 441 ? 137.873 159.468 150.409 1.00 41.35 ?  441 GLU B O     1 
ATOM   9102  C  CB    . GLU B 1 441 ? 136.726 160.558 153.249 1.00 22.01 ?  441 GLU B CB    1 
ATOM   9103  C  CG    . GLU B 1 441 ? 135.674 160.859 154.294 1.00 30.91 ?  441 GLU B CG    1 
ATOM   9104  C  CD    . GLU B 1 441 ? 134.362 161.323 153.695 1.00 42.82 ?  441 GLU B CD    1 
ATOM   9105  O  OE1   . GLU B 1 441 ? 134.246 162.524 153.374 1.00 39.73 ?  441 GLU B OE1   1 
ATOM   9106  O  OE2   . GLU B 1 441 ? 133.443 160.490 153.548 1.00 47.27 -1 441 GLU B OE2   1 
ATOM   9107  N  N     . THR B 1 442 ? 138.503 158.142 152.107 1.00 32.89 ?  442 THR B N     1 
ATOM   9108  C  CA    . THR B 1 442 ? 139.760 157.795 151.454 1.00 29.78 ?  442 THR B CA    1 
ATOM   9109  C  C     . THR B 1 442 ? 139.600 156.729 150.379 1.00 29.77 ?  442 THR B C     1 
ATOM   9110  O  O     . THR B 1 442 ? 140.591 156.376 149.731 1.00 38.02 ?  442 THR B O     1 
ATOM   9111  C  CB    . THR B 1 442 ? 140.788 157.329 152.489 1.00 31.77 ?  442 THR B CB    1 
ATOM   9112  O  OG1   . THR B 1 442 ? 140.301 156.161 153.161 1.00 38.47 ?  442 THR B OG1   1 
ATOM   9113  C  CG2   . THR B 1 442 ? 141.051 158.426 153.504 1.00 28.66 ?  442 THR B CG2   1 
ATOM   9114  N  N     . THR B 1 443 ? 138.394 156.214 150.169 1.00 33.92 ?  443 THR B N     1 
ATOM   9115  C  CA    . THR B 1 443 ? 138.147 155.213 149.141 1.00 37.93 ?  443 THR B CA    1 
ATOM   9116  C  C     . THR B 1 443 ? 137.789 155.910 147.834 1.00 38.05 ?  443 THR B C     1 
ATOM   9117  O  O     . THR B 1 443 ? 136.831 156.687 147.780 1.00 39.87 ?  443 THR B O     1 
ATOM   9118  C  CB    . THR B 1 443 ? 137.027 154.264 149.562 1.00 36.18 ?  443 THR B CB    1 
ATOM   9119  O  OG1   . THR B 1 443 ? 137.386 153.612 150.786 1.00 40.97 ?  443 THR B OG1   1 
ATOM   9120  C  CG2   . THR B 1 443 ? 136.794 153.215 148.489 1.00 29.03 ?  443 THR B CG2   1 
ATOM   9121  N  N     . ASP B 1 444 ? 138.560 155.630 146.785 1.00 46.08 ?  444 ASP B N     1 
ATOM   9122  C  CA    . ASP B 1 444 ? 138.286 156.151 145.448 1.00 44.30 ?  444 ASP B CA    1 
ATOM   9123  C  C     . ASP B 1 444 ? 138.488 155.015 144.457 1.00 47.74 ?  444 ASP B C     1 
ATOM   9124  O  O     . ASP B 1 444 ? 139.607 154.515 144.305 1.00 49.21 ?  444 ASP B O     1 
ATOM   9125  C  CB    . ASP B 1 444 ? 139.187 157.340 145.114 1.00 47.29 ?  444 ASP B CB    1 
ATOM   9126  C  CG    . ASP B 1 444 ? 138.542 158.301 144.136 1.00 51.21 ?  444 ASP B CG    1 
ATOM   9127  O  OD1   . ASP B 1 444 ? 137.419 158.768 144.413 1.00 48.14 ?  444 ASP B OD1   1 
ATOM   9128  O  OD2   . ASP B 1 444 ? 139.160 158.590 143.089 1.00 52.79 -1 444 ASP B OD2   1 
ATOM   9129  N  N     . ILE B 1 445 ? 137.414 154.607 143.789 1.00 38.65 ?  445 ILE B N     1 
ATOM   9130  C  CA    . ILE B 1 445 ? 137.445 153.495 142.848 1.00 40.61 ?  445 ILE B CA    1 
ATOM   9131  C  C     . ILE B 1 445 ? 137.301 154.068 141.445 1.00 45.93 ?  445 ILE B C     1 
ATOM   9132  O  O     . ILE B 1 445 ? 136.311 154.743 141.137 1.00 48.01 ?  445 ILE B O     1 
ATOM   9133  C  CB    . ILE B 1 445 ? 136.345 152.470 143.160 1.00 38.89 ?  445 ILE B CB    1 
ATOM   9134  C  CG1   . ILE B 1 445 ? 136.837 151.492 144.225 1.00 38.21 ?  445 ILE B CG1   1 
ATOM   9135  C  CG2   . ILE B 1 445 ? 135.960 151.698 141.913 1.00 41.28 ?  445 ILE B CG2   1 
ATOM   9136  C  CD1   . ILE B 1 445 ? 135.762 151.034 145.169 1.00 37.47 ?  445 ILE B CD1   1 
ATOM   9137  N  N     . ARG B 1 446 ? 138.293 153.807 140.596 1.00 46.10 ?  446 ARG B N     1 
ATOM   9138  C  CA    . ARG B 1 446 ? 138.421 154.499 139.323 1.00 46.88 ?  446 ARG B CA    1 
ATOM   9139  C  C     . ARG B 1 446 ? 137.705 153.807 138.171 1.00 48.00 ?  446 ARG B C     1 
ATOM   9140  O  O     . ARG B 1 446 ? 137.647 154.372 137.074 1.00 43.19 ?  446 ARG B O     1 
ATOM   9141  C  CB    . ARG B 1 446 ? 139.904 154.668 138.966 1.00 43.09 ?  446 ARG B CB    1 
ATOM   9142  C  CG    . ARG B 1 446 ? 140.819 154.879 140.166 1.00 41.76 ?  446 ARG B CG    1 
ATOM   9143  C  CD    . ARG B 1 446 ? 140.557 156.161 140.972 1.00 46.98 ?  446 ARG B CD    1 
ATOM   9144  N  NE    . ARG B 1 446 ? 140.742 157.396 140.216 1.00 48.53 ?  446 ARG B NE    1 
ATOM   9145  C  CZ    . ARG B 1 446 ? 139.796 158.032 139.535 1.00 49.20 ?  446 ARG B CZ    1 
ATOM   9146  N  NH1   . ARG B 1 446 ? 138.540 157.621 139.543 1.00 45.47 1  446 ARG B NH1   1 
ATOM   9147  N  NH2   . ARG B 1 446 ? 140.116 159.127 138.852 1.00 41.80 ?  446 ARG B NH2   1 
ATOM   9148  N  N     . ASN B 1 447 ? 137.158 152.612 138.382 1.00 37.86 ?  447 ASN B N     1 
ATOM   9149  C  CA    . ASN B 1 447 ? 136.518 151.871 137.306 1.00 30.21 ?  447 ASN B CA    1 
ATOM   9150  C  C     . ASN B 1 447 ? 135.060 151.537 137.582 1.00 33.78 ?  447 ASN B C     1 
ATOM   9151  O  O     . ASN B 1 447 ? 134.443 150.826 136.783 1.00 41.74 ?  447 ASN B O     1 
ATOM   9152  C  CB    . ASN B 1 447 ? 137.294 150.582 137.014 1.00 35.06 ?  447 ASN B CB    1 
ATOM   9153  C  CG    . ASN B 1 447 ? 138.367 150.780 135.966 1.00 33.26 ?  447 ASN B CG    1 
ATOM   9154  O  OD1   . ASN B 1 447 ? 138.070 150.934 134.783 1.00 39.91 ?  447 ASN B OD1   1 
ATOM   9155  N  ND2   . ASN B 1 447 ? 139.621 150.779 136.396 1.00 29.19 ?  447 ASN B ND2   1 
ATOM   9156  N  N     . ALA B 1 448 ? 134.495 152.022 138.686 1.00 35.20 ?  448 ALA B N     1 
ATOM   9157  C  CA    . ALA B 1 448 ? 133.075 151.877 138.997 1.00 30.98 ?  448 ALA B CA    1 
ATOM   9158  C  C     . ALA B 1 448 ? 132.529 153.275 139.248 1.00 34.36 ?  448 ALA B C     1 
ATOM   9159  O  O     . ALA B 1 448 ? 132.520 153.751 140.393 1.00 35.04 ?  448 ALA B O     1 
ATOM   9160  C  CB    . ALA B 1 448 ? 132.859 150.968 140.203 1.00 26.58 ?  448 ALA B CB    1 
ATOM   9161  N  N     . PRO B 1 449 ? 132.078 153.976 138.203 1.00 32.91 ?  449 PRO B N     1 
ATOM   9162  C  CA    . PRO B 1 449 ? 131.663 155.375 138.398 1.00 25.26 ?  449 PRO B CA    1 
ATOM   9163  C  C     . PRO B 1 449 ? 130.470 155.522 139.322 1.00 30.13 ?  449 PRO B C     1 
ATOM   9164  O  O     . PRO B 1 449 ? 130.411 156.482 140.099 1.00 29.44 ?  449 PRO B O     1 
ATOM   9165  C  CB    . PRO B 1 449 ? 131.346 155.860 136.976 1.00 27.13 ?  449 PRO B CB    1 
ATOM   9166  C  CG    . PRO B 1 449 ? 131.542 154.687 136.068 1.00 30.35 ?  449 PRO B CG    1 
ATOM   9167  C  CD    . PRO B 1 449 ? 131.701 153.456 136.880 1.00 24.54 ?  449 PRO B CD    1 
ATOM   9168  N  N     . ALA B 1 450 ? 129.514 154.592 139.263 1.00 32.95 ?  450 ALA B N     1 
ATOM   9169  C  CA    . ALA B 1 450 ? 128.351 154.677 140.139 1.00 19.72 ?  450 ALA B CA    1 
ATOM   9170  C  C     . ALA B 1 450 ? 128.726 154.383 141.583 1.00 27.50 ?  450 ALA B C     1 
ATOM   9171  O  O     . ALA B 1 450 ? 128.218 155.030 142.505 1.00 33.23 ?  450 ALA B O     1 
ATOM   9172  C  CB    . ALA B 1 450 ? 127.261 153.724 139.654 1.00 23.31 ?  450 ALA B CB    1 
ATOM   9173  N  N     . VAL B 1 451 ? 129.625 153.420 141.800 1.00 29.00 ?  451 VAL B N     1 
ATOM   9174  C  CA    . VAL B 1 451 ? 130.092 153.124 143.152 1.00 19.78 ?  451 VAL B CA    1 
ATOM   9175  C  C     . VAL B 1 451 ? 130.806 154.334 143.738 1.00 24.03 ?  451 VAL B C     1 
ATOM   9176  O  O     . VAL B 1 451 ? 130.576 154.715 144.891 1.00 36.06 ?  451 VAL B O     1 
ATOM   9177  C  CB    . VAL B 1 451 ? 131.002 151.882 143.147 1.00 28.00 ?  451 VAL B CB    1 
ATOM   9178  C  CG1   . VAL B 1 451 ? 131.836 151.824 144.413 1.00 28.64 ?  451 VAL B CG1   1 
ATOM   9179  C  CG2   . VAL B 1 451 ? 130.180 150.619 142.992 1.00 23.50 ?  451 VAL B CG2   1 
ATOM   9180  N  N     . ARG B 1 452 ? 131.680 154.959 142.948 1.00 25.98 ?  452 ARG B N     1 
ATOM   9181  C  CA    . ARG B 1 452 ? 132.403 156.136 143.420 1.00 23.15 ?  452 ARG B CA    1 
ATOM   9182  C  C     . ARG B 1 452 ? 131.456 157.298 143.695 1.00 22.13 ?  452 ARG B C     1 
ATOM   9183  O  O     . ARG B 1 452 ? 131.586 157.990 144.714 1.00 36.39 ?  452 ARG B O     1 
ATOM   9184  C  CB    . ARG B 1 452 ? 133.468 156.529 142.394 1.00 23.46 ?  452 ARG B CB    1 
ATOM   9185  C  CG    . ARG B 1 452 ? 134.280 157.755 142.760 1.00 31.33 ?  452 ARG B CG    1 
ATOM   9186  C  CD    . ARG B 1 452 ? 134.570 158.604 141.534 1.00 29.52 ?  452 ARG B CD    1 
ATOM   9187  N  NE    . ARG B 1 452 ? 133.537 158.454 140.516 1.00 41.86 ?  452 ARG B NE    1 
ATOM   9188  C  CZ    . ARG B 1 452 ? 132.484 159.249 140.388 1.00 41.89 ?  452 ARG B CZ    1 
ATOM   9189  N  NH1   . ARG B 1 452 ? 132.294 160.281 141.194 1.00 34.62 1  452 ARG B NH1   1 
ATOM   9190  N  NH2   . ARG B 1 452 ? 131.596 159.002 139.429 1.00 28.38 ?  452 ARG B NH2   1 
ATOM   9191  N  N     . ARG B 1 453 ? 130.488 157.524 142.803 1.00 23.37 ?  453 ARG B N     1 
ATOM   9192  C  CA    . ARG B 1 453 ? 129.533 158.607 143.005 1.00 22.37 ?  453 ARG B CA    1 
ATOM   9193  C  C     . ARG B 1 453 ? 128.698 158.381 144.258 1.00 29.71 ?  453 ARG B C     1 
ATOM   9194  O  O     . ARG B 1 453 ? 128.467 159.315 145.035 1.00 32.37 ?  453 ARG B O     1 
ATOM   9195  C  CB    . ARG B 1 453 ? 128.633 158.750 141.776 1.00 25.06 ?  453 ARG B CB    1 
ATOM   9196  C  CG    . ARG B 1 453 ? 127.436 159.658 141.986 1.00 25.17 ?  453 ARG B CG    1 
ATOM   9197  C  CD    . ARG B 1 453 ? 126.805 160.059 140.669 1.00 24.76 ?  453 ARG B CD    1 
ATOM   9198  N  NE    . ARG B 1 453 ? 125.408 159.646 140.586 1.00 27.52 ?  453 ARG B NE    1 
ATOM   9199  C  CZ    . ARG B 1 453 ? 124.391 160.337 141.082 1.00 29.14 ?  453 ARG B CZ    1 
ATOM   9200  N  NH1   . ARG B 1 453 ? 124.576 161.485 141.710 1.00 30.68 1  453 ARG B NH1   1 
ATOM   9201  N  NH2   . ARG B 1 453 ? 123.158 159.862 140.944 1.00 25.55 ?  453 ARG B NH2   1 
ATOM   9202  N  N     . ALA B 1 454 ? 128.242 157.146 144.478 1.00 31.94 ?  454 ALA B N     1 
ATOM   9203  C  CA    . ALA B 1 454 ? 127.444 156.859 145.662 1.00 20.44 ?  454 ALA B CA    1 
ATOM   9204  C  C     . ALA B 1 454 ? 128.278 156.919 146.932 1.00 20.06 ?  454 ALA B C     1 
ATOM   9205  O  O     . ALA B 1 454 ? 127.766 157.307 147.984 1.00 29.70 ?  454 ALA B O     1 
ATOM   9206  C  CB    . ALA B 1 454 ? 126.772 155.496 145.528 1.00 22.79 ?  454 ALA B CB    1 
ATOM   9207  N  N     . ASN B 1 455 ? 129.553 156.538 146.864 1.00 26.92 ?  455 ASN B N     1 
ATOM   9208  C  CA    . ASN B 1 455 ? 130.422 156.685 148.025 1.00 20.39 ?  455 ASN B CA    1 
ATOM   9209  C  C     . ASN B 1 455 ? 130.622 158.154 148.372 1.00 26.77 ?  455 ASN B C     1 
ATOM   9210  O  O     . ASN B 1 455 ? 130.630 158.525 149.550 1.00 39.86 ?  455 ASN B O     1 
ATOM   9211  C  CB    . ASN B 1 455 ? 131.764 156.002 147.766 1.00 20.18 ?  455 ASN B CB    1 
ATOM   9212  C  CG    . ASN B 1 455 ? 132.672 156.023 148.978 1.00 29.85 ?  455 ASN B CG    1 
ATOM   9213  O  OD1   . ASN B 1 455 ? 132.416 155.344 149.970 1.00 38.69 ?  455 ASN B OD1   1 
ATOM   9214  N  ND2   . ASN B 1 455 ? 133.742 156.804 148.902 1.00 29.79 ?  455 ASN B ND2   1 
ATOM   9215  N  N     . LYS B 1 456 ? 130.786 159.004 147.357 1.00 27.60 ?  456 LYS B N     1 
ATOM   9216  C  CA    . LYS B 1 456 ? 130.969 160.427 147.614 1.00 26.83 ?  456 LYS B CA    1 
ATOM   9217  C  C     . LYS B 1 456 ? 129.686 161.090 148.101 1.00 26.99 ?  456 LYS B C     1 
ATOM   9218  O  O     . LYS B 1 456 ? 129.740 162.003 148.931 1.00 31.45 ?  456 LYS B O     1 
ATOM   9219  C  CB    . LYS B 1 456 ? 131.480 161.123 146.354 1.00 24.22 ?  456 LYS B CB    1 
ATOM   9220  C  CG    . LYS B 1 456 ? 132.448 162.259 146.627 1.00 29.52 ?  456 LYS B CG    1 
ATOM   9221  C  CD    . LYS B 1 456 ? 131.738 163.604 146.615 1.00 35.87 ?  456 LYS B CD    1 
ATOM   9222  C  CE    . LYS B 1 456 ? 132.644 164.715 147.121 1.00 37.12 ?  456 LYS B CE    1 
ATOM   9223  N  NZ    . LYS B 1 456 ? 132.573 164.862 148.601 1.00 31.89 1  456 LYS B NZ    1 
ATOM   9224  N  N     . ALA B 1 457 ? 128.531 160.655 147.602 1.00 25.36 ?  457 ALA B N     1 
ATOM   9225  C  CA    . ALA B 1 457 ? 127.265 161.312 147.903 1.00 17.19 ?  457 ALA B CA    1 
ATOM   9226  C  C     . ALA B 1 457 ? 126.617 160.789 149.179 1.00 23.78 ?  457 ALA B C     1 
ATOM   9227  O  O     . ALA B 1 457 ? 126.284 161.569 150.077 1.00 27.47 ?  457 ALA B O     1 
ATOM   9228  C  CB    . ALA B 1 457 ? 126.305 161.145 146.723 1.00 20.86 ?  457 ALA B CB    1 
ATOM   9229  N  N     . MET B 1 458 ? 126.427 159.473 149.269 1.00 34.34 ?  458 MET B N     1 
ATOM   9230  C  CA    . MET B 1 458 ? 125.705 158.878 150.386 1.00 17.01 ?  458 MET B CA    1 
ATOM   9231  C  C     . MET B 1 458 ? 126.540 158.868 151.660 1.00 25.08 ?  458 MET B C     1 
ATOM   9232  O  O     . MET B 1 458 ? 125.997 159.053 152.755 1.00 33.26 ?  458 MET B O     1 
ATOM   9233  C  CB    . MET B 1 458 ? 125.273 157.459 150.024 1.00 18.15 ?  458 MET B CB    1 
ATOM   9234  C  CG    . MET B 1 458 ? 124.526 157.344 148.702 1.00 21.57 ?  458 MET B CG    1 
ATOM   9235  S  SD    . MET B 1 458 ? 122.737 157.510 148.859 1.00 35.77 ?  458 MET B SD    1 
ATOM   9236  C  CE    . MET B 1 458 ? 122.544 159.288 148.809 1.00 27.87 ?  458 MET B CE    1 
ATOM   9237  N  N     . LYS B 1 459 ? 127.849 158.650 151.537 1.00 15.58 ?  459 LYS B N     1 
ATOM   9238  C  CA    . LYS B 1 459 ? 128.747 158.553 152.688 1.00 18.95 ?  459 LYS B CA    1 
ATOM   9239  C  C     . LYS B 1 459 ? 128.262 157.493 153.674 1.00 20.49 ?  459 LYS B C     1 
ATOM   9240  O  O     . LYS B 1 459 ? 128.339 157.661 154.892 1.00 32.27 ?  459 LYS B O     1 
ATOM   9241  C  CB    . LYS B 1 459 ? 128.908 159.907 153.382 1.00 26.05 ?  459 LYS B CB    1 
ATOM   9242  C  CG    . LYS B 1 459 ? 129.352 161.031 152.466 1.00 31.44 ?  459 LYS B CG    1 
ATOM   9243  C  CD    . LYS B 1 459 ? 128.607 162.313 152.784 1.00 23.51 ?  459 LYS B CD    1 
ATOM   9244  C  CE    . LYS B 1 459 ? 128.942 163.407 151.791 1.00 27.85 ?  459 LYS B CE    1 
ATOM   9245  N  NZ    . LYS B 1 459 ? 128.204 164.664 152.086 1.00 33.22 1  459 LYS B NZ    1 
ATOM   9246  N  N     . SER B 1 460 ? 127.754 156.387 153.139 1.00 16.22 ?  460 SER B N     1 
ATOM   9247  C  CA    . SER B 1 460 ? 127.197 155.334 153.971 1.00 9.49  ?  460 SER B CA    1 
ATOM   9248  C  C     . SER B 1 460 ? 128.302 154.466 154.557 1.00 19.62 ?  460 SER B C     1 
ATOM   9249  O  O     . SER B 1 460 ? 129.288 154.150 153.886 1.00 32.72 ?  460 SER B O     1 
ATOM   9250  C  CB    . SER B 1 460 ? 126.232 154.467 153.164 1.00 17.17 ?  460 SER B CB    1 
ATOM   9251  O  OG    . SER B 1 460 ? 126.929 153.687 152.212 1.00 26.49 ?  460 SER B OG    1 
ATOM   9252  N  N     . ILE B 1 461 ? 128.127 154.082 155.820 1.00 19.65 ?  461 ILE B N     1 
ATOM   9253  C  CA    . ILE B 1 461 ? 129.058 153.209 156.516 1.00 15.15 ?  461 ILE B CA    1 
ATOM   9254  C  C     . ILE B 1 461 ? 128.267 152.062 157.125 1.00 20.77 ?  461 ILE B C     1 
ATOM   9255  O  O     . ILE B 1 461 ? 127.049 152.135 157.289 1.00 23.59 ?  461 ILE B O     1 
ATOM   9256  C  CB    . ILE B 1 461 ? 129.858 153.949 157.608 1.00 12.55 ?  461 ILE B CB    1 
ATOM   9257  C  CG1   . ILE B 1 461 ? 128.907 154.595 158.616 1.00 7.21  ?  461 ILE B CG1   1 
ATOM   9258  C  CG2   . ILE B 1 461 ? 130.769 154.992 156.987 1.00 18.35 ?  461 ILE B CG2   1 
ATOM   9259  C  CD1   . ILE B 1 461 ? 129.577 155.049 159.884 1.00 12.29 ?  461 ILE B CD1   1 
ATOM   9260  N  N     . GLY B 1 462 ? 128.972 150.982 157.434 1.00 20.59 ?  462 GLY B N     1 
ATOM   9261  C  CA    . GLY B 1 462 ? 128.350 149.903 158.169 1.00 9.98  ?  462 GLY B CA    1 
ATOM   9262  C  C     . GLY B 1 462 ? 129.089 149.590 159.450 1.00 11.74 ?  462 GLY B C     1 
ATOM   9263  O  O     . GLY B 1 462 ? 130.206 149.070 159.416 1.00 27.20 ?  462 GLY B O     1 
ATOM   9264  N  N     . LEU B 1 463 ? 128.471 149.886 160.587 1.00 12.75 ?  463 LEU B N     1 
ATOM   9265  C  CA    . LEU B 1 463 ? 129.039 149.576 161.893 1.00 8.74  ?  463 LEU B CA    1 
ATOM   9266  C  C     . LEU B 1 463 ? 128.281 148.389 162.466 1.00 20.47 ?  463 LEU B C     1 
ATOM   9267  O  O     . LEU B 1 463 ? 127.128 148.524 162.888 1.00 28.83 ?  463 LEU B O     1 
ATOM   9268  C  CB    . LEU B 1 463 ? 128.968 150.782 162.826 1.00 18.78 ?  463 LEU B CB    1 
ATOM   9269  C  CG    . LEU B 1 463 ? 129.429 150.520 164.260 1.00 16.77 ?  463 LEU B CG    1 
ATOM   9270  C  CD1   . LEU B 1 463 ? 130.859 150.014 164.269 1.00 3.19  ?  463 LEU B CD1   1 
ATOM   9271  C  CD2   . LEU B 1 463 ? 129.292 151.771 165.111 1.00 16.93 ?  463 LEU B CD2   1 
ATOM   9272  N  N     . GLY B 1 464 ? 128.928 147.225 162.481 1.00 22.67 ?  464 GLY B N     1 
ATOM   9273  C  CA    . GLY B 1 464 ? 128.331 146.015 162.995 1.00 13.17 ?  464 GLY B CA    1 
ATOM   9274  C  C     . GLY B 1 464 ? 128.710 145.746 164.439 1.00 9.46  ?  464 GLY B C     1 
ATOM   9275  O  O     . GLY B 1 464 ? 129.348 146.555 165.116 1.00 18.19 ?  464 GLY B O     1 
ATOM   9276  N  N     . ALA B 1 465 ? 128.297 144.575 164.910 1.00 15.21 ?  465 ALA B N     1 
ATOM   9277  C  CA    . ALA B 1 465 ? 128.622 144.114 166.248 1.00 8.92  ?  465 ALA B CA    1 
ATOM   9278  C  C     . ALA B 1 465 ? 128.910 142.623 166.187 1.00 16.15 ?  465 ALA B C     1 
ATOM   9279  O  O     . ALA B 1 465 ? 128.467 141.920 165.278 1.00 33.48 ?  465 ALA B O     1 
ATOM   9280  C  CB    . ALA B 1 465 ? 127.491 144.403 167.242 1.00 18.90 ?  465 ALA B CB    1 
ATOM   9281  N  N     . MET B 1 466 ? 129.667 142.150 167.170 1.00 22.79 ?  466 MET B N     1 
ATOM   9282  C  CA    . MET B 1 466 ? 130.013 140.741 167.262 1.00 19.06 ?  466 MET B CA    1 
ATOM   9283  C  C     . MET B 1 466 ? 130.151 140.380 168.733 1.00 18.39 ?  466 MET B C     1 
ATOM   9284  O  O     . MET B 1 466 ? 130.054 141.238 169.614 1.00 23.63 ?  466 MET B O     1 
ATOM   9285  C  CB    . MET B 1 466 ? 131.295 140.437 166.483 1.00 24.49 ?  466 MET B CB    1 
ATOM   9286  C  CG    . MET B 1 466 ? 132.552 140.906 167.180 1.00 27.81 ?  466 MET B CG    1 
ATOM   9287  S  SD    . MET B 1 466 ? 133.986 140.959 166.098 1.00 41.52 ?  466 MET B SD    1 
ATOM   9288  C  CE    . MET B 1 466 ? 134.906 142.268 166.888 1.00 25.51 ?  466 MET B CE    1 
ATOM   9289  N  N     . ASN B 1 467 ? 130.372 139.091 168.993 1.00 16.44 ?  467 ASN B N     1 
ATOM   9290  C  CA    . ASN B 1 467 ? 130.526 138.563 170.348 1.00 22.64 ?  467 ASN B CA    1 
ATOM   9291  C  C     . ASN B 1 467 ? 129.267 138.762 171.184 1.00 26.97 ?  467 ASN B C     1 
ATOM   9292  O  O     . ASN B 1 467 ? 129.342 138.965 172.397 1.00 26.62 ?  467 ASN B O     1 
ATOM   9293  C  CB    . ASN B 1 467 ? 131.736 139.179 171.058 1.00 21.75 ?  467 ASN B CB    1 
ATOM   9294  C  CG    . ASN B 1 467 ? 132.463 138.185 171.933 1.00 27.21 ?  467 ASN B CG    1 
ATOM   9295  O  OD1   . ASN B 1 467 ? 132.135 137.001 171.952 1.00 27.28 ?  467 ASN B OD1   1 
ATOM   9296  N  ND2   . ASN B 1 467 ? 133.464 138.661 172.662 1.00 30.72 ?  467 ASN B ND2   1 
ATOM   9297  N  N     . LEU B 1 468 ? 128.099 138.721 170.543 1.00 17.65 ?  468 LEU B N     1 
ATOM   9298  C  CA    . LEU B 1 468 ? 126.851 138.780 171.296 1.00 14.70 ?  468 LEU B CA    1 
ATOM   9299  C  C     . LEU B 1 468 ? 126.646 137.506 172.104 1.00 29.01 ?  468 LEU B C     1 
ATOM   9300  O  O     . LEU B 1 468 ? 126.379 137.558 173.310 1.00 33.40 ?  468 LEU B O     1 
ATOM   9301  C  CB    . LEU B 1 468 ? 125.675 139.010 170.348 1.00 24.99 ?  468 LEU B CB    1 
ATOM   9302  C  CG    . LEU B 1 468 ? 124.298 139.063 171.010 1.00 19.41 ?  468 LEU B CG    1 
ATOM   9303  C  CD1   . LEU B 1 468 ? 124.240 140.182 172.033 1.00 16.93 ?  468 LEU B CD1   1 
ATOM   9304  C  CD2   . LEU B 1 468 ? 123.202 139.223 169.974 1.00 16.14 ?  468 LEU B CD2   1 
ATOM   9305  N  N     . HIS B 1 469 ? 126.790 136.348 171.456 1.00 31.57 ?  469 HIS B N     1 
ATOM   9306  C  CA    . HIS B 1 469 ? 126.617 135.087 172.164 1.00 16.43 ?  469 HIS B CA    1 
ATOM   9307  C  C     . HIS B 1 469 ? 127.726 134.870 173.182 1.00 27.60 ?  469 HIS B C     1 
ATOM   9308  O  O     . HIS B 1 469 ? 127.479 134.338 174.266 1.00 38.08 ?  469 HIS B O     1 
ATOM   9309  C  CB    . HIS B 1 469 ? 126.562 133.923 171.177 1.00 15.93 ?  469 HIS B CB    1 
ATOM   9310  C  CG    . HIS B 1 469 ? 126.015 132.663 171.771 1.00 20.95 ?  469 HIS B CG    1 
ATOM   9311  N  ND1   . HIS B 1 469 ? 126.063 131.450 171.121 1.00 33.35 ?  469 HIS B ND1   1 
ATOM   9312  C  CD2   . HIS B 1 469 ? 125.407 132.429 172.957 1.00 27.48 ?  469 HIS B CD2   1 
ATOM   9313  C  CE1   . HIS B 1 469 ? 125.509 130.523 171.881 1.00 26.03 ?  469 HIS B CE1   1 
ATOM   9314  N  NE2   . HIS B 1 469 ? 125.103 131.092 173.002 1.00 25.19 ?  469 HIS B NE2   1 
ATOM   9315  N  N     . GLY B 1 470 ? 128.953 135.270 172.851 1.00 20.38 ?  470 GLY B N     1 
ATOM   9316  C  CA    . GLY B 1 470 ? 130.032 135.165 173.818 1.00 23.00 ?  470 GLY B CA    1 
ATOM   9317  C  C     . GLY B 1 470 ? 129.785 136.013 175.049 1.00 16.85 ?  470 GLY B C     1 
ATOM   9318  O  O     . GLY B 1 470 ? 129.972 135.555 176.179 1.00 35.43 ?  470 GLY B O     1 
ATOM   9319  N  N     . TYR B 1 471 ? 129.343 137.255 174.848 1.00 17.13 ?  471 TYR B N     1 
ATOM   9320  C  CA    . TYR B 1 471 ? 129.051 138.128 175.978 1.00 20.16 ?  471 TYR B CA    1 
ATOM   9321  C  C     . TYR B 1 471 ? 127.901 137.583 176.815 1.00 25.71 ?  471 TYR B C     1 
ATOM   9322  O  O     . TYR B 1 471 ? 127.940 137.642 178.049 1.00 30.05 ?  471 TYR B O     1 
ATOM   9323  C  CB    . TYR B 1 471 ? 128.727 139.539 175.491 1.00 25.45 ?  471 TYR B CB    1 
ATOM   9324  C  CG    . TYR B 1 471 ? 128.145 140.418 176.571 1.00 24.40 ?  471 TYR B CG    1 
ATOM   9325  C  CD1   . TYR B 1 471 ? 128.960 140.989 177.538 1.00 25.10 ?  471 TYR B CD1   1 
ATOM   9326  C  CD2   . TYR B 1 471 ? 126.781 140.654 176.642 1.00 15.35 ?  471 TYR B CD2   1 
ATOM   9327  C  CE1   . TYR B 1 471 ? 128.433 141.782 178.533 1.00 22.93 ?  471 TYR B CE1   1 
ATOM   9328  C  CE2   . TYR B 1 471 ? 126.247 141.438 177.638 1.00 19.90 ?  471 TYR B CE2   1 
ATOM   9329  C  CZ    . TYR B 1 471 ? 127.075 142.003 178.576 1.00 26.35 ?  471 TYR B CZ    1 
ATOM   9330  O  OH    . TYR B 1 471 ? 126.541 142.793 179.565 1.00 36.38 ?  471 TYR B OH    1 
ATOM   9331  N  N     . LEU B 1 472 ? 126.861 137.060 176.161 1.00 28.49 ?  472 LEU B N     1 
ATOM   9332  C  CA    . LEU B 1 472 ? 125.709 136.554 176.900 1.00 21.62 ?  472 LEU B CA    1 
ATOM   9333  C  C     . LEU B 1 472 ? 126.058 135.288 177.675 1.00 28.12 ?  472 LEU B C     1 
ATOM   9334  O  O     . LEU B 1 472 ? 125.700 135.149 178.850 1.00 35.09 ?  472 LEU B O     1 
ATOM   9335  C  CB    . LEU B 1 472 ? 124.542 136.298 175.945 1.00 23.44 ?  472 LEU B CB    1 
ATOM   9336  C  CG    . LEU B 1 472 ? 123.900 137.532 175.307 1.00 25.83 ?  472 LEU B CG    1 
ATOM   9337  C  CD1   . LEU B 1 472 ? 122.943 137.121 174.201 1.00 24.57 ?  472 LEU B CD1   1 
ATOM   9338  C  CD2   . LEU B 1 472 ? 123.192 138.378 176.351 1.00 22.97 ?  472 LEU B CD2   1 
ATOM   9339  N  N     . ALA B 1 473 ? 126.759 134.351 177.033 1.00 24.54 ?  473 ALA B N     1 
ATOM   9340  C  CA    . ALA B 1 473 ? 127.118 133.103 177.693 1.00 24.14 ?  473 ALA B CA    1 
ATOM   9341  C  C     . ALA B 1 473 ? 128.127 133.325 178.809 1.00 32.15 ?  473 ALA B C     1 
ATOM   9342  O  O     . ALA B 1 473 ? 128.086 132.622 179.825 1.00 39.89 ?  473 ALA B O     1 
ATOM   9343  C  CB    . ALA B 1 473 ? 127.662 132.110 176.668 1.00 25.75 ?  473 ALA B CB    1 
ATOM   9344  N  N     . GLN B 1 474 ? 129.036 134.287 178.647 1.00 31.34 ?  474 GLN B N     1 
ATOM   9345  C  CA    . GLN B 1 474 ? 129.968 134.612 179.717 1.00 29.33 ?  474 GLN B CA    1 
ATOM   9346  C  C     . GLN B 1 474 ? 129.320 135.414 180.836 1.00 29.76 ?  474 GLN B C     1 
ATOM   9347  O  O     . GLN B 1 474 ? 129.961 135.632 181.870 1.00 40.96 ?  474 GLN B O     1 
ATOM   9348  C  CB    . GLN B 1 474 ? 131.167 135.376 179.155 1.00 31.56 ?  474 GLN B CB    1 
ATOM   9349  C  CG    . GLN B 1 474 ? 132.123 134.502 178.366 1.00 29.28 ?  474 GLN B CG    1 
ATOM   9350  C  CD    . GLN B 1 474 ? 133.230 135.295 177.708 1.00 36.08 ?  474 GLN B CD    1 
ATOM   9351  O  OE1   . GLN B 1 474 ? 134.099 135.843 178.382 1.00 42.48 ?  474 GLN B OE1   1 
ATOM   9352  N  NE2   . GLN B 1 474 ? 133.205 135.356 176.383 1.00 36.55 ?  474 GLN B NE2   1 
ATOM   9353  N  N     . ASN B 1 475 ? 128.076 135.856 180.657 1.00 32.74 ?  475 ASN B N     1 
ATOM   9354  C  CA    . ASN B 1 475 ? 127.327 136.550 181.694 1.00 35.35 ?  475 ASN B CA    1 
ATOM   9355  C  C     . ASN B 1 475 ? 126.146 135.733 182.201 1.00 36.04 ?  475 ASN B C     1 
ATOM   9356  O  O     . ASN B 1 475 ? 125.277 136.278 182.889 1.00 38.28 ?  475 ASN B O     1 
ATOM   9357  C  CB    . ASN B 1 475 ? 126.847 137.909 181.184 1.00 34.60 ?  475 ASN B CB    1 
ATOM   9358  C  CG    . ASN B 1 475 ? 127.975 138.906 181.038 1.00 32.50 ?  475 ASN B CG    1 
ATOM   9359  O  OD1   . ASN B 1 475 ? 128.230 139.705 181.937 1.00 39.35 ?  475 ASN B OD1   1 
ATOM   9360  N  ND2   . ASN B 1 475 ? 128.663 138.857 179.905 1.00 28.42 ?  475 ASN B ND2   1 
ATOM   9361  N  N     . GLY B 1 476 ? 126.092 134.446 181.877 1.00 35.89 ?  476 GLY B N     1 
ATOM   9362  C  CA    . GLY B 1 476 ? 125.023 133.581 182.344 1.00 32.40 ?  476 GLY B CA    1 
ATOM   9363  C  C     . GLY B 1 476 ? 123.654 133.905 181.788 1.00 35.20 ?  476 GLY B C     1 
ATOM   9364  O  O     . GLY B 1 476 ? 122.663 133.857 182.528 1.00 42.73 ?  476 GLY B O     1 
ATOM   9365  N  N     . ILE B 1 477 ? 123.571 134.236 180.502 1.00 32.50 ?  477 ILE B N     1 
ATOM   9366  C  CA    . ILE B 1 477 ? 122.306 134.539 179.846 1.00 32.21 ?  477 ILE B CA    1 
ATOM   9367  C  C     . ILE B 1 477 ? 122.173 133.646 178.621 1.00 32.56 ?  477 ILE B C     1 
ATOM   9368  O  O     . ILE B 1 477 ? 123.064 133.623 177.766 1.00 36.67 ?  477 ILE B O     1 
ATOM   9369  C  CB    . ILE B 1 477 ? 122.206 136.024 179.449 1.00 27.66 ?  477 ILE B CB    1 
ATOM   9370  C  CG1   . ILE B 1 477 ? 122.187 136.911 180.694 1.00 30.97 ?  477 ILE B CG1   1 
ATOM   9371  C  CG2   . ILE B 1 477 ? 120.969 136.269 178.611 1.00 26.18 ?  477 ILE B CG2   1 
ATOM   9372  C  CD1   . ILE B 1 477 ? 122.788 138.278 180.478 1.00 33.59 ?  477 ILE B CD1   1 
ATOM   9373  N  N     . ALA B 1 478 ? 121.070 132.909 178.544 1.00 33.33 ?  478 ALA B N     1 
ATOM   9374  C  CA    . ALA B 1 478 ? 120.811 132.074 177.380 1.00 28.73 ?  478 ALA B CA    1 
ATOM   9375  C  C     . ALA B 1 478 ? 120.477 132.942 176.176 1.00 34.04 ?  478 ALA B C     1 
ATOM   9376  O  O     . ALA B 1 478 ? 119.813 133.973 176.301 1.00 38.65 ?  478 ALA B O     1 
ATOM   9377  C  CB    . ALA B 1 478 ? 119.669 131.101 177.665 1.00 29.59 ?  478 ALA B CB    1 
ATOM   9378  N  N     . TYR B 1 479 ? 120.943 132.515 175.000 1.00 29.89 ?  479 TYR B N     1 
ATOM   9379  C  CA    . TYR B 1 479 ? 120.741 133.304 173.788 1.00 21.31 ?  479 TYR B CA    1 
ATOM   9380  C  C     . TYR B 1 479 ? 119.260 133.447 173.457 1.00 33.73 ?  479 TYR B C     1 
ATOM   9381  O  O     . TYR B 1 479 ? 118.818 134.512 173.009 1.00 36.22 ?  479 TYR B O     1 
ATOM   9382  C  CB    . TYR B 1 479 ? 121.498 132.664 172.626 1.00 19.78 ?  479 TYR B CB    1 
ATOM   9383  C  CG    . TYR B 1 479 ? 121.568 133.510 171.376 1.00 26.75 ?  479 TYR B CG    1 
ATOM   9384  C  CD1   . TYR B 1 479 ? 120.591 133.417 170.393 1.00 30.18 ?  479 TYR B CD1   1 
ATOM   9385  C  CD2   . TYR B 1 479 ? 122.620 134.393 171.171 1.00 23.61 ?  479 TYR B CD2   1 
ATOM   9386  C  CE1   . TYR B 1 479 ? 120.656 134.186 169.249 1.00 23.94 ?  479 TYR B CE1   1 
ATOM   9387  C  CE2   . TYR B 1 479 ? 122.693 135.164 170.031 1.00 22.72 ?  479 TYR B CE2   1 
ATOM   9388  C  CZ    . TYR B 1 479 ? 121.709 135.057 169.074 1.00 30.34 ?  479 TYR B CZ    1 
ATOM   9389  O  OH    . TYR B 1 479 ? 121.778 135.823 167.935 1.00 35.04 ?  479 TYR B OH    1 
ATOM   9390  N  N     . GLU B 1 480 ? 118.477 132.388 173.665 1.00 36.31 ?  480 GLU B N     1 
ATOM   9391  C  CA    . GLU B 1 480 ? 117.049 132.432 173.382 1.00 31.16 ?  480 GLU B CA    1 
ATOM   9392  C  C     . GLU B 1 480 ? 116.236 133.047 174.509 1.00 33.32 ?  480 GLU B C     1 
ATOM   9393  O  O     . GLU B 1 480 ? 115.022 133.216 174.352 1.00 38.14 ?  480 GLU B O     1 
ATOM   9394  C  CB    . GLU B 1 480 ? 116.515 131.026 173.106 1.00 34.29 ?  480 GLU B CB    1 
ATOM   9395  C  CG    . GLU B 1 480 ? 117.246 130.264 172.028 1.00 35.17 ?  480 GLU B CG    1 
ATOM   9396  C  CD    . GLU B 1 480 ? 117.219 128.772 172.277 1.00 43.07 ?  480 GLU B CD    1 
ATOM   9397  O  OE1   . GLU B 1 480 ? 118.004 128.298 173.123 1.00 44.45 ?  480 GLU B OE1   1 
ATOM   9398  O  OE2   . GLU B 1 480 ? 116.412 128.072 171.631 1.00 39.62 -1 480 GLU B OE2   1 
ATOM   9399  N  N     . SER B 1 481 ? 116.861 133.375 175.634 1.00 31.50 ?  481 SER B N     1 
ATOM   9400  C  CA    . SER B 1 481 ? 116.121 133.890 176.770 1.00 32.57 ?  481 SER B CA    1 
ATOM   9401  C  C     . SER B 1 481 ? 115.578 135.287 176.471 1.00 36.64 ?  481 SER B C     1 
ATOM   9402  O  O     . SER B 1 481 ? 116.154 136.028 175.669 1.00 38.79 ?  481 SER B O     1 
ATOM   9403  C  CB    . SER B 1 481 ? 117.011 133.931 178.008 1.00 30.75 ?  481 SER B CB    1 
ATOM   9404  O  OG    . SER B 1 481 ? 117.814 135.096 178.019 1.00 35.20 ?  481 SER B OG    1 
ATOM   9405  N  N     . PRO B 1 482 ? 114.455 135.661 177.088 1.00 42.31 ?  482 PRO B N     1 
ATOM   9406  C  CA    . PRO B 1 482 ? 113.971 137.041 176.940 1.00 37.58 ?  482 PRO B CA    1 
ATOM   9407  C  C     . PRO B 1 482 ? 114.948 138.076 177.463 1.00 32.77 ?  482 PRO B C     1 
ATOM   9408  O  O     . PRO B 1 482 ? 114.941 139.218 176.988 1.00 36.90 ?  482 PRO B O     1 
ATOM   9409  C  CB    . PRO B 1 482 ? 112.662 137.039 177.744 1.00 35.59 ?  482 PRO B CB    1 
ATOM   9410  C  CG    . PRO B 1 482 ? 112.243 135.612 177.780 1.00 37.34 ?  482 PRO B CG    1 
ATOM   9411  C  CD    . PRO B 1 482 ? 113.511 134.821 177.842 1.00 37.93 ?  482 PRO B CD    1 
ATOM   9412  N  N     . GLU B 1 483 ? 115.790 137.712 178.433 1.00 35.62 ?  483 GLU B N     1 
ATOM   9413  C  CA    . GLU B 1 483 ? 116.793 138.645 178.935 1.00 32.90 ?  483 GLU B CA    1 
ATOM   9414  C  C     . GLU B 1 483 ? 117.849 138.942 177.878 1.00 30.00 ?  483 GLU B C     1 
ATOM   9415  O  O     . GLU B 1 483 ? 118.360 140.064 177.801 1.00 36.41 ?  483 GLU B O     1 
ATOM   9416  C  CB    . GLU B 1 483 ? 117.439 138.085 180.202 1.00 37.13 ?  483 GLU B CB    1 
ATOM   9417  C  CG    . GLU B 1 483 ? 116.483 137.949 181.374 1.00 39.21 ?  483 GLU B CG    1 
ATOM   9418  C  CD    . GLU B 1 483 ? 115.870 136.566 181.467 1.00 45.79 ?  483 GLU B CD    1 
ATOM   9419  O  OE1   . GLU B 1 483 ? 115.996 135.793 180.497 1.00 42.62 ?  483 GLU B OE1   1 
ATOM   9420  O  OE2   . GLU B 1 483 ? 115.258 136.253 182.510 1.00 44.24 -1 483 GLU B OE2   1 
ATOM   9421  N  N     . ALA B 1 484 ? 118.195 137.947 177.060 1.00 28.45 ?  484 ALA B N     1 
ATOM   9422  C  CA    . ALA B 1 484 ? 119.132 138.185 175.966 1.00 29.24 ?  484 ALA B CA    1 
ATOM   9423  C  C     . ALA B 1 484 ? 118.563 139.177 174.962 1.00 29.55 ?  484 ALA B C     1 
ATOM   9424  O  O     . ALA B 1 484 ? 119.270 140.081 174.502 1.00 31.34 ?  484 ALA B O     1 
ATOM   9425  C  CB    . ALA B 1 484 ? 119.480 136.869 175.278 1.00 21.96 ?  484 ALA B CB    1 
ATOM   9426  N  N     . ARG B 1 485 ? 117.285 139.026 174.613 1.00 26.43 ?  485 ARG B N     1 
ATOM   9427  C  CA    . ARG B 1 485 ? 116.651 139.987 173.719 1.00 26.24 ?  485 ARG B CA    1 
ATOM   9428  C  C     . ARG B 1 485 ? 116.533 141.356 174.367 1.00 24.75 ?  485 ARG B C     1 
ATOM   9429  O  O     . ARG B 1 485 ? 116.640 142.373 173.678 1.00 35.19 ?  485 ARG B O     1 
ATOM   9430  C  CB    . ARG B 1 485 ? 115.278 139.477 173.286 1.00 28.25 ?  485 ARG B CB    1 
ATOM   9431  C  CG    . ARG B 1 485 ? 115.336 138.374 172.250 1.00 26.08 ?  485 ARG B CG    1 
ATOM   9432  C  CD    . ARG B 1 485 ? 113.965 138.093 171.667 1.00 25.72 ?  485 ARG B CD    1 
ATOM   9433  N  NE    . ARG B 1 485 ? 113.031 137.597 172.671 1.00 29.58 ?  485 ARG B NE    1 
ATOM   9434  C  CZ    . ARG B 1 485 ? 112.998 136.346 173.111 1.00 33.69 ?  485 ARG B CZ    1 
ATOM   9435  N  NH1   . ARG B 1 485 ? 113.833 135.429 172.652 1.00 35.12 1  485 ARG B NH1   1 
ATOM   9436  N  NH2   . ARG B 1 485 ? 112.101 136.008 174.033 1.00 29.72 ?  485 ARG B NH2   1 
ATOM   9437  N  N     . ASP B 1 486 ? 116.318 141.405 175.681 1.00 30.77 ?  486 ASP B N     1 
ATOM   9438  C  CA    . ASP B 1 486 ? 116.289 142.683 176.387 1.00 30.72 ?  486 ASP B CA    1 
ATOM   9439  C  C     . ASP B 1 486 ? 117.639 143.386 176.299 1.00 30.06 ?  486 ASP B C     1 
ATOM   9440  O  O     . ASP B 1 486 ? 117.714 144.594 176.022 1.00 32.61 ?  486 ASP B O     1 
ATOM   9441  C  CB    . ASP B 1 486 ? 115.883 142.448 177.841 1.00 34.22 ?  486 ASP B CB    1 
ATOM   9442  C  CG    . ASP B 1 486 ? 115.579 143.729 178.576 1.00 43.15 ?  486 ASP B CG    1 
ATOM   9443  O  OD1   . ASP B 1 486 ? 114.837 144.571 178.030 1.00 45.20 ?  486 ASP B OD1   1 
ATOM   9444  O  OD2   . ASP B 1 486 ? 116.076 143.887 179.709 1.00 34.53 -1 486 ASP B OD2   1 
ATOM   9445  N  N     . PHE B 1 487 ? 118.723 142.639 176.522 1.00 26.92 ?  487 PHE B N     1 
ATOM   9446  C  CA    . PHE B 1 487 ? 120.051 143.224 176.389 1.00 23.40 ?  487 PHE B CA    1 
ATOM   9447  C  C     . PHE B 1 487 ? 120.313 143.679 174.964 1.00 28.27 ?  487 PHE B C     1 
ATOM   9448  O  O     . PHE B 1 487 ? 120.891 144.746 174.748 1.00 30.97 ?  487 PHE B O     1 
ATOM   9449  C  CB    . PHE B 1 487 ? 121.143 142.248 176.814 1.00 24.72 ?  487 PHE B CB    1 
ATOM   9450  C  CG    . PHE B 1 487 ? 122.502 142.650 176.321 1.00 28.11 ?  487 PHE B CG    1 
ATOM   9451  C  CD1   . PHE B 1 487 ? 123.187 143.686 176.931 1.00 21.12 ?  487 PHE B CD1   1 
ATOM   9452  C  CD2   . PHE B 1 487 ? 123.073 142.034 175.220 1.00 27.86 ?  487 PHE B CD2   1 
ATOM   9453  C  CE1   . PHE B 1 487 ? 124.422 144.083 176.470 1.00 23.42 ?  487 PHE B CE1   1 
ATOM   9454  C  CE2   . PHE B 1 487 ? 124.309 142.432 174.758 1.00 26.23 ?  487 PHE B CE2   1 
ATOM   9455  C  CZ    . PHE B 1 487 ? 124.982 143.459 175.383 1.00 25.18 ?  487 PHE B CZ    1 
ATOM   9456  N  N     . ALA B 1 488 ? 119.940 142.862 173.977 1.00 26.01 ?  488 ALA B N     1 
ATOM   9457  C  CA    . ALA B 1 488 ? 120.156 143.254 172.588 1.00 20.12 ?  488 ALA B CA    1 
ATOM   9458  C  C     . ALA B 1 488 ? 119.391 144.526 172.261 1.00 29.34 ?  488 ALA B C     1 
ATOM   9459  O  O     . ALA B 1 488 ? 119.932 145.443 171.632 1.00 38.20 ?  488 ALA B O     1 
ATOM   9460  C  CB    . ALA B 1 488 ? 119.745 142.121 171.651 1.00 21.50 ?  488 ALA B CB    1 
ATOM   9461  N  N     . ASN B 1 489 ? 118.137 144.607 172.708 1.00 28.70 ?  489 ASN B N     1 
ATOM   9462  C  CA    . ASN B 1 489 ? 117.332 145.805 172.512 1.00 26.11 ?  489 ASN B CA    1 
ATOM   9463  C  C     . ASN B 1 489 ? 118.032 147.033 173.072 1.00 20.40 ?  489 ASN B C     1 
ATOM   9464  O  O     . ASN B 1 489 ? 118.246 148.019 172.358 1.00 29.68 ?  489 ASN B O     1 
ATOM   9465  C  CB    . ASN B 1 489 ? 115.968 145.608 173.175 1.00 21.16 ?  489 ASN B CB    1 
ATOM   9466  C  CG    . ASN B 1 489 ? 114.905 146.521 172.616 1.00 32.36 ?  489 ASN B CG    1 
ATOM   9467  O  OD1   . ASN B 1 489 ? 114.634 146.519 171.416 1.00 39.21 ?  489 ASN B OD1   1 
ATOM   9468  N  ND2   . ASN B 1 489 ? 114.281 147.299 173.489 1.00 31.79 ?  489 ASN B ND2   1 
ATOM   9469  N  N     . THR B 1 490 ? 118.434 146.976 174.344 1.00 22.72 ?  490 THR B N     1 
ATOM   9470  C  CA    . THR B 1 490 ? 119.042 148.147 174.971 1.00 22.67 ?  490 THR B CA    1 
ATOM   9471  C  C     . THR B 1 490 ? 120.382 148.494 174.328 1.00 24.87 ?  490 THR B C     1 
ATOM   9472  O  O     . THR B 1 490 ? 120.647 149.660 174.009 1.00 21.06 ?  490 THR B O     1 
ATOM   9473  C  CB    . THR B 1 490 ? 119.212 147.914 176.471 1.00 33.48 ?  490 THR B CB    1 
ATOM   9474  O  OG1   . THR B 1 490 ? 117.968 147.476 177.027 1.00 39.12 ?  490 THR B OG1   1 
ATOM   9475  C  CG2   . THR B 1 490 ? 119.648 149.196 177.161 1.00 27.80 ?  490 THR B CG2   1 
ATOM   9476  N  N     . PHE B 1 491 ? 121.233 147.487 174.119 1.00 25.08 ?  491 PHE B N     1 
ATOM   9477  C  CA    . PHE B 1 491 ? 122.571 147.721 173.591 1.00 19.01 ?  491 PHE B CA    1 
ATOM   9478  C  C     . PHE B 1 491 ? 122.516 148.322 172.197 1.00 25.49 ?  491 PHE B C     1 
ATOM   9479  O  O     . PHE B 1 491 ? 123.221 149.292 171.899 1.00 33.73 ?  491 PHE B O     1 
ATOM   9480  C  CB    . PHE B 1 491 ? 123.358 146.409 173.580 1.00 23.13 ?  491 PHE B CB    1 
ATOM   9481  C  CG    . PHE B 1 491 ? 124.742 146.530 173.003 1.00 25.07 ?  491 PHE B CG    1 
ATOM   9482  C  CD1   . PHE B 1 491 ? 125.817 146.848 173.813 1.00 23.22 ?  491 PHE B CD1   1 
ATOM   9483  C  CD2   . PHE B 1 491 ? 124.970 146.315 171.653 1.00 20.50 ?  491 PHE B CD2   1 
ATOM   9484  C  CE1   . PHE B 1 491 ? 127.088 146.960 173.289 1.00 14.85 ?  491 PHE B CE1   1 
ATOM   9485  C  CE2   . PHE B 1 491 ? 126.237 146.428 171.125 1.00 15.76 ?  491 PHE B CE2   1 
ATOM   9486  C  CZ    . PHE B 1 491 ? 127.298 146.751 171.945 1.00 19.74 ?  491 PHE B CZ    1 
ATOM   9487  N  N     . PHE B 1 492 ? 121.684 147.760 171.321 1.00 20.89 ?  492 PHE B N     1 
ATOM   9488  C  CA    . PHE B 1 492 ? 121.634 148.274 169.965 1.00 12.88 ?  492 PHE B CA    1 
ATOM   9489  C  C     . PHE B 1 492 ? 120.843 149.568 169.860 1.00 10.87 ?  492 PHE B C     1 
ATOM   9490  O  O     . PHE B 1 492 ? 121.120 150.364 168.959 1.00 24.78 ?  492 PHE B O     1 
ATOM   9491  C  CB    . PHE B 1 492 ? 121.091 147.200 169.027 1.00 14.12 ?  492 PHE B CB    1 
ATOM   9492  C  CG    . PHE B 1 492 ? 122.086 146.115 168.740 1.00 16.24 ?  492 PHE B CG    1 
ATOM   9493  C  CD1   . PHE B 1 492 ? 123.103 146.318 167.826 1.00 10.13 ?  492 PHE B CD1   1 
ATOM   9494  C  CD2   . PHE B 1 492 ? 122.034 144.911 169.418 1.00 18.24 ?  492 PHE B CD2   1 
ATOM   9495  C  CE1   . PHE B 1 492 ? 124.030 145.331 167.573 1.00 8.63  ?  492 PHE B CE1   1 
ATOM   9496  C  CE2   . PHE B 1 492 ? 122.959 143.920 169.169 1.00 12.97 ?  492 PHE B CE2   1 
ATOM   9497  C  CZ    . PHE B 1 492 ? 123.957 144.130 168.245 1.00 15.74 ?  492 PHE B CZ    1 
ATOM   9498  N  N     . MET B 1 493 ? 119.912 149.834 170.783 1.00 14.89 ?  493 MET B N     1 
ATOM   9499  C  CA    . MET B 1 493 ? 119.346 151.175 170.858 1.00 17.34 ?  493 MET B CA    1 
ATOM   9500  C  C     . MET B 1 493 ? 120.423 152.194 171.197 1.00 22.68 ?  493 MET B C     1 
ATOM   9501  O  O     . MET B 1 493 ? 120.475 153.273 170.601 1.00 29.67 ?  493 MET B O     1 
ATOM   9502  C  CB    . MET B 1 493 ? 118.234 151.233 171.901 1.00 19.23 ?  493 MET B CB    1 
ATOM   9503  C  CG    . MET B 1 493 ? 117.611 152.615 172.034 1.00 18.99 ?  493 MET B CG    1 
ATOM   9504  S  SD    . MET B 1 493 ? 118.197 153.550 173.462 1.00 37.89 ?  493 MET B SD    1 
ATOM   9505  C  CE    . MET B 1 493 ? 118.214 152.287 174.726 1.00 27.76 ?  493 MET B CE    1 
ATOM   9506  N  N     . MET B 1 494 ? 121.294 151.868 172.157 1.00 22.12 ?  494 MET B N     1 
ATOM   9507  C  CA    . MET B 1 494 ? 122.383 152.777 172.505 1.00 17.02 ?  494 MET B CA    1 
ATOM   9508  C  C     . MET B 1 494 ? 123.348 152.955 171.339 1.00 18.65 ?  494 MET B C     1 
ATOM   9509  O  O     . MET B 1 494 ? 123.820 154.070 171.076 1.00 31.25 ?  494 MET B O     1 
ATOM   9510  C  CB    . MET B 1 494 ? 123.128 152.266 173.737 1.00 23.61 ?  494 MET B CB    1 
ATOM   9511  C  CG    . MET B 1 494 ? 122.266 152.116 174.975 1.00 22.05 ?  494 MET B CG    1 
ATOM   9512  S  SD    . MET B 1 494 ? 123.234 151.789 176.457 1.00 42.56 ?  494 MET B SD    1 
ATOM   9513  C  CE    . MET B 1 494 ? 124.458 153.088 176.349 1.00 31.53 ?  494 MET B CE    1 
ATOM   9514  N  N     . VAL B 1 495 ? 123.662 151.864 170.639 1.00 19.82 ?  495 VAL B N     1 
ATOM   9515  C  CA    . VAL B 1 495 ? 124.555 151.945 169.487 1.00 13.54 ?  495 VAL B CA    1 
ATOM   9516  C  C     . VAL B 1 495 ? 123.954 152.838 168.411 1.00 18.91 ?  495 VAL B C     1 
ATOM   9517  O  O     . VAL B 1 495 ? 124.641 153.691 167.840 1.00 31.74 ?  495 VAL B O     1 
ATOM   9518  C  CB    . VAL B 1 495 ? 124.862 150.535 168.949 1.00 15.39 ?  495 VAL B CB    1 
ATOM   9519  C  CG1   . VAL B 1 495 ? 125.497 150.614 167.571 1.00 13.43 ?  495 VAL B CG1   1 
ATOM   9520  C  CG2   . VAL B 1 495 ? 125.764 149.788 169.913 1.00 14.04 ?  495 VAL B CG2   1 
ATOM   9521  N  N     . ASN B 1 496 ? 122.662 152.663 168.124 1.00 25.04 ?  496 ASN B N     1 
ATOM   9522  C  CA    . ASN B 1 496 ? 121.994 153.513 167.145 1.00 14.39 ?  496 ASN B CA    1 
ATOM   9523  C  C     . ASN B 1 496 ? 121.980 154.965 167.594 1.00 17.48 ?  496 ASN B C     1 
ATOM   9524  O  O     . ASN B 1 496 ? 122.220 155.873 166.792 1.00 27.82 ?  496 ASN B O     1 
ATOM   9525  C  CB    . ASN B 1 496 ? 120.569 153.011 166.908 1.00 13.17 ?  496 ASN B CB    1 
ATOM   9526  C  CG    . ASN B 1 496 ? 119.978 153.525 165.616 1.00 14.73 ?  496 ASN B CG    1 
ATOM   9527  O  OD1   . ASN B 1 496 ? 120.661 153.605 164.598 1.00 25.58 ?  496 ASN B OD1   1 
ATOM   9528  N  ND2   . ASN B 1 496 ? 118.700 153.872 165.650 1.00 17.11 ?  496 ASN B ND2   1 
ATOM   9529  N  N     . PHE B 1 497 ? 121.703 155.204 168.878 1.00 18.74 ?  497 PHE B N     1 
ATOM   9530  C  CA    . PHE B 1 497 ? 121.671 156.563 169.402 1.00 12.68 ?  497 PHE B CA    1 
ATOM   9531  C  C     . PHE B 1 497 ? 123.010 157.254 169.203 1.00 24.73 ?  497 PHE B C     1 
ATOM   9532  O  O     . PHE B 1 497 ? 123.074 158.376 168.690 1.00 30.72 ?  497 PHE B O     1 
ATOM   9533  C  CB    . PHE B 1 497 ? 121.298 156.535 170.886 1.00 15.59 ?  497 PHE B CB    1 
ATOM   9534  C  CG    . PHE B 1 497 ? 121.194 157.893 171.515 1.00 19.96 ?  497 PHE B CG    1 
ATOM   9535  C  CD1   . PHE B 1 497 ? 120.004 158.597 171.479 1.00 29.44 ?  497 PHE B CD1   1 
ATOM   9536  C  CD2   . PHE B 1 497 ? 122.282 158.461 172.155 1.00 22.87 ?  497 PHE B CD2   1 
ATOM   9537  C  CE1   . PHE B 1 497 ? 119.905 159.843 172.059 1.00 27.07 ?  497 PHE B CE1   1 
ATOM   9538  C  CE2   . PHE B 1 497 ? 122.187 159.707 172.736 1.00 25.28 ?  497 PHE B CE2   1 
ATOM   9539  C  CZ    . PHE B 1 497 ? 120.998 160.398 172.688 1.00 28.44 ?  497 PHE B CZ    1 
ATOM   9540  N  N     . TYR B 1 498 ? 124.095 156.585 169.585 1.00 28.15 ?  498 TYR B N     1 
ATOM   9541  C  CA    . TYR B 1 498 ? 125.398 157.228 169.514 1.00 19.30 ?  498 TYR B CA    1 
ATOM   9542  C  C     . TYR B 1 498 ? 125.926 157.295 168.088 1.00 24.34 ?  498 TYR B C     1 
ATOM   9543  O  O     . TYR B 1 498 ? 126.661 158.228 167.759 1.00 35.03 ?  498 TYR B O     1 
ATOM   9544  C  CB    . TYR B 1 498 ? 126.376 156.523 170.451 1.00 20.21 ?  498 TYR B CB    1 
ATOM   9545  C  CG    . TYR B 1 498 ? 126.054 156.815 171.895 1.00 26.02 ?  498 TYR B CG    1 
ATOM   9546  C  CD1   . TYR B 1 498 ? 126.014 158.121 172.360 1.00 29.24 ?  498 TYR B CD1   1 
ATOM   9547  C  CD2   . TYR B 1 498 ? 125.753 155.793 172.784 1.00 25.53 ?  498 TYR B CD2   1 
ATOM   9548  C  CE1   . TYR B 1 498 ? 125.704 158.402 173.673 1.00 29.00 ?  498 TYR B CE1   1 
ATOM   9549  C  CE2   . TYR B 1 498 ? 125.442 156.065 174.100 1.00 26.42 ?  498 TYR B CE2   1 
ATOM   9550  C  CZ    . TYR B 1 498 ? 125.420 157.373 174.539 1.00 33.24 ?  498 TYR B CZ    1 
ATOM   9551  O  OH    . TYR B 1 498 ? 125.112 157.653 175.850 1.00 37.24 ?  498 TYR B OH    1 
ATOM   9552  N  N     . SER B 1 499 ? 125.529 156.367 167.215 1.00 18.28 ?  499 SER B N     1 
ATOM   9553  C  CA    . SER B 1 499 ? 125.910 156.487 165.812 1.00 10.43 ?  499 SER B CA    1 
ATOM   9554  C  C     . SER B 1 499 ? 125.183 157.648 165.144 1.00 18.82 ?  499 SER B C     1 
ATOM   9555  O  O     . SER B 1 499 ? 125.787 158.398 164.369 1.00 27.20 ?  499 SER B O     1 
ATOM   9556  C  CB    . SER B 1 499 ? 125.638 155.177 165.075 1.00 8.27  ?  499 SER B CB    1 
ATOM   9557  O  OG    . SER B 1 499 ? 124.260 155.011 164.811 1.00 24.13 ?  499 SER B OG    1 
ATOM   9558  N  N     . ILE B 1 500 ? 123.894 157.828 165.446 1.00 16.69 ?  500 ILE B N     1 
ATOM   9559  C  CA    . ILE B 1 500 ? 123.162 158.983 164.930 1.00 20.33 ?  500 ILE B CA    1 
ATOM   9560  C  C     . ILE B 1 500 ? 123.759 160.272 165.472 1.00 21.42 ?  500 ILE B C     1 
ATOM   9561  O  O     . ILE B 1 500 ? 123.909 161.260 164.743 1.00 26.70 ?  500 ILE B O     1 
ATOM   9562  C  CB    . ILE B 1 500 ? 121.665 158.873 165.274 1.00 24.31 ?  500 ILE B CB    1 
ATOM   9563  C  CG1   . ILE B 1 500 ? 121.021 157.707 164.535 1.00 21.83 ?  500 ILE B CG1   1 
ATOM   9564  C  CG2   . ILE B 1 500 ? 120.942 160.158 164.920 1.00 19.07 ?  500 ILE B CG2   1 
ATOM   9565  C  CD1   . ILE B 1 500 ? 119.681 157.323 165.095 1.00 18.71 ?  500 ILE B CD1   1 
ATOM   9566  N  N     . GLN B 1 501 ? 124.097 160.288 166.764 1.00 29.10 ?  501 GLN B N     1 
ATOM   9567  C  CA    . GLN B 1 501 ? 124.684 161.481 167.360 1.00 25.39 ?  501 GLN B CA    1 
ATOM   9568  C  C     . GLN B 1 501 ? 126.026 161.817 166.723 1.00 26.73 ?  501 GLN B C     1 
ATOM   9569  O  O     . GLN B 1 501 ? 126.298 162.980 166.415 1.00 39.62 ?  501 GLN B O     1 
ATOM   9570  C  CB    . GLN B 1 501 ? 124.839 161.293 168.867 1.00 30.32 ?  501 GLN B CB    1 
ATOM   9571  C  CG    . GLN B 1 501 ? 124.699 162.576 169.658 1.00 29.00 ?  501 GLN B CG    1 
ATOM   9572  C  CD    . GLN B 1 501 ? 124.860 162.359 171.144 1.00 33.80 ?  501 GLN B CD    1 
ATOM   9573  O  OE1   . GLN B 1 501 ? 125.879 161.842 171.598 1.00 39.72 ?  501 GLN B OE1   1 
ATOM   9574  N  NE2   . GLN B 1 501 ? 123.853 162.753 171.912 1.00 34.98 ?  501 GLN B NE2   1 
ATOM   9575  N  N     . ARG B 1 502 ? 126.875 160.810 166.506 1.00 31.15 ?  502 ARG B N     1 
ATOM   9576  C  CA    . ARG B 1 502 ? 128.165 161.059 165.874 1.00 23.02 ?  502 ARG B CA    1 
ATOM   9577  C  C     . ARG B 1 502 ? 127.998 161.508 164.430 1.00 22.55 ?  502 ARG B C     1 
ATOM   9578  O  O     . ARG B 1 502 ? 128.742 162.370 163.956 1.00 30.10 ?  502 ARG B O     1 
ATOM   9579  C  CB    . ARG B 1 502 ? 129.043 159.812 165.949 1.00 20.77 ?  502 ARG B CB    1 
ATOM   9580  C  CG    . ARG B 1 502 ? 130.494 160.074 165.592 1.00 25.50 ?  502 ARG B CG    1 
ATOM   9581  C  CD    . ARG B 1 502 ? 131.056 161.226 166.404 1.00 28.07 ?  502 ARG B CD    1 
ATOM   9582  N  NE    . ARG B 1 502 ? 132.339 161.683 165.888 1.00 28.04 ?  502 ARG B NE    1 
ATOM   9583  C  CZ    . ARG B 1 502 ? 132.730 162.949 165.869 1.00 27.28 ?  502 ARG B CZ    1 
ATOM   9584  N  NH1   . ARG B 1 502 ? 131.958 163.918 166.331 1.00 32.98 1  502 ARG B NH1   1 
ATOM   9585  N  NH2   . ARG B 1 502 ? 133.926 163.251 165.373 1.00 29.36 ?  502 ARG B NH2   1 
ATOM   9586  N  N     . SER B 1 503 ? 127.035 160.932 163.710 1.00 23.22 ?  503 SER B N     1 
ATOM   9587  C  CA    . SER B 1 503 ? 126.797 161.348 162.333 1.00 22.24 ?  503 SER B CA    1 
ATOM   9588  C  C     . SER B 1 503 ? 126.325 162.795 162.267 1.00 26.36 ?  503 SER B C     1 
ATOM   9589  O  O     . SER B 1 503 ? 126.781 163.568 161.418 1.00 33.93 ?  503 SER B O     1 
ATOM   9590  C  CB    . SER B 1 503 ? 125.779 160.413 161.684 1.00 16.91 ?  503 SER B CB    1 
ATOM   9591  O  OG    . SER B 1 503 ? 125.909 160.405 160.276 1.00 25.82 ?  503 SER B OG    1 
ATOM   9592  N  N     . ALA B 1 504 ? 125.421 163.185 163.167 1.00 25.08 ?  504 ALA B N     1 
ATOM   9593  C  CA    . ALA B 1 504 ? 124.973 164.572 163.208 1.00 22.29 ?  504 ALA B CA    1 
ATOM   9594  C  C     . ALA B 1 504 ? 126.100 165.506 163.631 1.00 31.28 ?  504 ALA B C     1 
ATOM   9595  O  O     . ALA B 1 504 ? 126.195 166.634 163.137 1.00 38.19 ?  504 ALA B O     1 
ATOM   9596  C  CB    . ALA B 1 504 ? 123.775 164.707 164.146 1.00 22.33 ?  504 ALA B CB    1 
ATOM   9597  N  N     . GLU B 1 505 ? 126.967 165.055 164.540 1.00 29.93 ?  505 GLU B N     1 
ATOM   9598  C  CA    . GLU B 1 505 ? 128.120 165.859 164.934 1.00 26.45 ?  505 GLU B CA    1 
ATOM   9599  C  C     . GLU B 1 505 ? 129.081 166.058 163.769 1.00 34.37 ?  505 GLU B C     1 
ATOM   9600  O  O     . GLU B 1 505 ? 129.620 167.154 163.585 1.00 39.07 ?  505 GLU B O     1 
ATOM   9601  C  CB    . GLU B 1 505 ? 128.836 165.200 166.113 1.00 26.96 ?  505 GLU B CB    1 
ATOM   9602  C  CG    . GLU B 1 505 ? 128.146 165.399 167.449 1.00 31.27 ?  505 GLU B CG    1 
ATOM   9603  C  CD    . GLU B 1 505 ? 128.572 164.373 168.480 1.00 37.60 ?  505 GLU B CD    1 
ATOM   9604  O  OE1   . GLU B 1 505 ? 129.478 163.568 168.183 1.00 39.01 ?  505 GLU B OE1   1 
ATOM   9605  O  OE2   . GLU B 1 505 ? 128.000 164.373 169.590 1.00 41.19 -1 505 GLU B OE2   1 
ATOM   9606  N  N     . ILE B 1 506 ? 129.315 165.008 162.980 1.00 32.03 ?  506 ILE B N     1 
ATOM   9607  C  CA    . ILE B 1 506 ? 130.168 165.133 161.802 1.00 26.15 ?  506 ILE B CA    1 
ATOM   9608  C  C     . ILE B 1 506 ? 129.531 166.067 160.782 1.00 26.57 ?  506 ILE B C     1 
ATOM   9609  O  O     . ILE B 1 506 ? 130.219 166.871 160.142 1.00 37.47 ?  506 ILE B O     1 
ATOM   9610  C  CB    . ILE B 1 506 ? 130.456 163.744 161.202 1.00 27.51 ?  506 ILE B CB    1 
ATOM   9611  C  CG1   . ILE B 1 506 ? 131.282 162.902 162.176 1.00 32.53 ?  506 ILE B CG1   1 
ATOM   9612  C  CG2   . ILE B 1 506 ? 131.182 163.868 159.873 1.00 24.74 ?  506 ILE B CG2   1 
ATOM   9613  C  CD1   . ILE B 1 506 ? 131.345 161.436 161.815 1.00 24.63 ?  506 ILE B CD1   1 
ATOM   9614  N  N     . ALA B 1 507 ? 128.210 165.977 160.611 1.00 29.52 ?  507 ALA B N     1 
ATOM   9615  C  CA    . ALA B 1 507 ? 127.520 166.887 159.702 1.00 29.58 ?  507 ALA B CA    1 
ATOM   9616  C  C     . ALA B 1 507 ? 127.653 168.333 160.162 1.00 31.40 ?  507 ALA B C     1 
ATOM   9617  O  O     . ALA B 1 507 ? 127.856 169.237 159.346 1.00 37.98 ?  507 ALA B O     1 
ATOM   9618  C  CB    . ALA B 1 507 ? 126.049 166.493 159.584 1.00 26.16 ?  507 ALA B CB    1 
ATOM   9619  N  N     . LYS B 1 508 ? 127.533 168.571 161.470 1.00 35.98 ?  508 LYS B N     1 
ATOM   9620  C  CA    . LYS B 1 508 ? 127.710 169.915 162.007 1.00 36.46 ?  508 LYS B CA    1 
ATOM   9621  C  C     . LYS B 1 508 ? 129.141 170.407 161.818 1.00 39.38 ?  508 LYS B C     1 
ATOM   9622  O  O     . LYS B 1 508 ? 129.363 171.574 161.477 1.00 43.84 ?  508 LYS B O     1 
ATOM   9623  C  CB    . LYS B 1 508 ? 127.324 169.937 163.485 1.00 41.04 ?  508 LYS B CB    1 
ATOM   9624  C  CG    . LYS B 1 508 ? 127.533 171.274 164.169 1.00 38.72 ?  508 LYS B CG    1 
ATOM   9625  C  CD    . LYS B 1 508 ? 127.361 171.151 165.671 1.00 39.11 ?  508 LYS B CD    1 
ATOM   9626  C  CE    . LYS B 1 508 ? 127.408 172.510 166.347 1.00 41.74 ?  508 LYS B CE    1 
ATOM   9627  N  NZ    . LYS B 1 508 ? 126.579 172.544 167.583 1.00 46.13 1  508 LYS B NZ    1 
ATOM   9628  N  N     . GLU B 1 509 ? 130.124 169.532 162.042 1.00 42.09 ?  509 GLU B N     1 
ATOM   9629  C  CA    . GLU B 1 509 ? 131.522 169.929 161.909 1.00 40.27 ?  509 GLU B CA    1 
ATOM   9630  C  C     . GLU B 1 509 ? 131.871 170.261 160.465 1.00 42.88 ?  509 GLU B C     1 
ATOM   9631  O  O     . GLU B 1 509 ? 132.533 171.270 160.197 1.00 49.18 ?  509 GLU B O     1 
ATOM   9632  C  CB    . GLU B 1 509 ? 132.431 168.819 162.436 1.00 37.70 ?  509 GLU B CB    1 
ATOM   9633  C  CG    . GLU B 1 509 ? 132.736 168.913 163.922 1.00 46.70 ?  509 GLU B CG    1 
ATOM   9634  C  CD    . GLU B 1 509 ? 133.010 167.557 164.547 1.00 50.17 ?  509 GLU B CD    1 
ATOM   9635  O  OE1   . GLU B 1 509 ? 133.597 166.693 163.864 1.00 48.52 ?  509 GLU B OE1   1 
ATOM   9636  O  OE2   . GLU B 1 509 ? 132.637 167.356 165.723 1.00 45.41 -1 509 GLU B OE2   1 
ATOM   9637  N  N     . LYS B 1 510 ? 131.441 169.425 159.523 1.00 38.56 ?  510 LYS B N     1 
ATOM   9638  C  CA    . LYS B 1 510 ? 131.727 169.638 158.113 1.00 32.84 ?  510 LYS B CA    1 
ATOM   9639  C  C     . LYS B 1 510 ? 130.705 170.531 157.425 1.00 38.42 ?  510 LYS B C     1 
ATOM   9640  O  O     . LYS B 1 510 ? 130.923 170.919 156.273 1.00 46.93 ?  510 LYS B O     1 
ATOM   9641  C  CB    . LYS B 1 510 ? 131.800 168.293 157.383 1.00 29.42 ?  510 LYS B CB    1 
ATOM   9642  C  CG    . LYS B 1 510 ? 132.757 167.300 158.011 1.00 32.23 ?  510 LYS B CG    1 
ATOM   9643  C  CD    . LYS B 1 510 ? 132.960 166.091 157.118 1.00 35.69 ?  510 LYS B CD    1 
ATOM   9644  C  CE    . LYS B 1 510 ? 133.947 165.111 157.729 1.00 39.38 ?  510 LYS B CE    1 
ATOM   9645  N  NZ    . LYS B 1 510 ? 134.662 164.323 156.691 1.00 41.14 1  510 LYS B NZ    1 
ATOM   9646  N  N     . GLY B 1 511 ? 129.605 170.865 158.096 1.00 36.32 ?  511 GLY B N     1 
ATOM   9647  C  CA    . GLY B 1 511 ? 128.577 171.686 157.490 1.00 37.95 ?  511 GLY B CA    1 
ATOM   9648  C  C     . GLY B 1 511 ? 127.843 171.044 156.339 1.00 40.49 ?  511 GLY B C     1 
ATOM   9649  O  O     . GLY B 1 511 ? 127.133 171.742 155.610 1.00 43.77 ?  511 GLY B O     1 
ATOM   9650  N  N     . GLU B 1 512 ? 127.986 169.734 156.151 1.00 34.43 ?  512 GLU B N     1 
ATOM   9651  C  CA    . GLU B 1 512 ? 127.372 169.038 155.031 1.00 30.22 ?  512 GLU B CA    1 
ATOM   9652  C  C     . GLU B 1 512 ? 126.735 167.745 155.511 1.00 31.48 ?  512 GLU B C     1 
ATOM   9653  O  O     . GLU B 1 512 ? 127.260 167.077 156.405 1.00 36.31 ?  512 GLU B O     1 
ATOM   9654  C  CB    . GLU B 1 512 ? 128.398 168.733 153.935 1.00 33.01 ?  512 GLU B CB    1 
ATOM   9655  C  CG    . GLU B 1 512 ? 129.660 168.066 154.448 1.00 32.71 ?  512 GLU B CG    1 
ATOM   9656  C  CD    . GLU B 1 512 ? 130.464 167.413 153.344 1.00 38.28 ?  512 GLU B CD    1 
ATOM   9657  O  OE1   . GLU B 1 512 ? 129.875 167.085 152.292 1.00 37.92 ?  512 GLU B OE1   1 
ATOM   9658  O  OE2   . GLU B 1 512 ? 131.685 167.222 153.528 1.00 39.66 -1 512 GLU B OE2   1 
ATOM   9659  N  N     . THR B 1 513 ? 125.602 167.404 154.912 1.00 34.26 ?  513 THR B N     1 
ATOM   9660  C  CA    . THR B 1 513 ? 124.919 166.139 155.125 1.00 32.81 ?  513 THR B CA    1 
ATOM   9661  C  C     . THR B 1 513 ? 125.134 165.252 153.904 1.00 28.84 ?  513 THR B C     1 
ATOM   9662  O  O     . THR B 1 513 ? 125.855 165.609 152.970 1.00 38.58 ?  513 THR B O     1 
ATOM   9663  C  CB    . THR B 1 513 ? 123.431 166.371 155.389 1.00 31.71 ?  513 THR B CB    1 
ATOM   9664  O  OG1   . THR B 1 513 ? 122.799 166.837 154.192 1.00 33.73 ?  513 THR B OG1   1 
ATOM   9665  C  CG2   . THR B 1 513 ? 123.252 167.411 156.473 1.00 29.90 ?  513 THR B CG2   1 
ATOM   9666  N  N     . PHE B 1 514 ? 124.507 164.080 153.910 1.00 22.87 ?  514 PHE B N     1 
ATOM   9667  C  CA    . PHE B 1 514 ? 124.593 163.259 152.716 1.00 25.65 ?  514 PHE B CA    1 
ATOM   9668  C  C     . PHE B 1 514 ? 123.616 163.770 151.663 1.00 25.87 ?  514 PHE B C     1 
ATOM   9669  O  O     . PHE B 1 514 ? 122.673 164.507 151.957 1.00 32.72 ?  514 PHE B O     1 
ATOM   9670  C  CB    . PHE B 1 514 ? 124.336 161.781 153.028 1.00 20.36 ?  514 PHE B CB    1 
ATOM   9671  C  CG    . PHE B 1 514 ? 122.955 161.481 153.541 1.00 20.87 ?  514 PHE B CG    1 
ATOM   9672  C  CD1   . PHE B 1 514 ? 122.656 161.603 154.885 1.00 18.94 ?  514 PHE B CD1   1 
ATOM   9673  C  CD2   . PHE B 1 514 ? 121.965 161.039 152.680 1.00 20.33 ?  514 PHE B CD2   1 
ATOM   9674  C  CE1   . PHE B 1 514 ? 121.396 161.308 155.358 1.00 13.71 ?  514 PHE B CE1   1 
ATOM   9675  C  CE2   . PHE B 1 514 ? 120.702 160.743 153.149 1.00 17.18 ?  514 PHE B CE2   1 
ATOM   9676  C  CZ    . PHE B 1 514 ? 120.418 160.879 154.488 1.00 16.99 ?  514 PHE B CZ    1 
ATOM   9677  N  N     . ASP B 1 515 ? 123.872 163.389 150.414 1.00 27.24 ?  515 ASP B N     1 
ATOM   9678  C  CA    . ASP B 1 515 ? 123.060 163.883 149.312 1.00 29.97 ?  515 ASP B CA    1 
ATOM   9679  C  C     . ASP B 1 515 ? 121.619 163.414 149.457 1.00 33.38 ?  515 ASP B C     1 
ATOM   9680  O  O     . ASP B 1 515 ? 121.355 162.254 149.784 1.00 43.02 ?  515 ASP B O     1 
ATOM   9681  C  CB    . ASP B 1 515 ? 123.642 163.423 147.977 1.00 31.84 ?  515 ASP B CB    1 
ATOM   9682  C  CG    . ASP B 1 515 ? 124.872 164.214 147.580 1.00 34.96 ?  515 ASP B CG    1 
ATOM   9683  O  OD1   . ASP B 1 515 ? 125.472 164.866 148.459 1.00 34.91 ?  515 ASP B OD1   1 
ATOM   9684  O  OD2   . ASP B 1 515 ? 125.240 164.183 146.387 1.00 37.22 -1 515 ASP B OD2   1 
ATOM   9685  N  N     . GLN B 1 516 ? 120.686 164.336 149.211 1.00 33.32 ?  516 GLN B N     1 
ATOM   9686  C  CA    . GLN B 1 516 ? 119.253 164.081 149.350 1.00 29.64 ?  516 GLN B CA    1 
ATOM   9687  C  C     . GLN B 1 516 ? 118.894 163.677 150.779 1.00 32.54 ?  516 GLN B C     1 
ATOM   9688  O  O     . GLN B 1 516 ? 118.016 162.842 151.004 1.00 39.69 ?  516 GLN B O     1 
ATOM   9689  C  CB    . GLN B 1 516 ? 118.776 163.026 148.349 1.00 27.02 ?  516 GLN B CB    1 
ATOM   9690  C  CG    . GLN B 1 516 ? 119.099 163.353 146.904 1.00 30.65 ?  516 GLN B CG    1 
ATOM   9691  C  CD    . GLN B 1 516 ? 118.985 162.146 145.997 1.00 38.64 ?  516 GLN B CD    1 
ATOM   9692  O  OE1   . GLN B 1 516 ? 117.890 161.774 145.576 1.00 37.40 ?  516 GLN B OE1   1 
ATOM   9693  N  NE2   . GLN B 1 516 ? 120.118 161.523 145.697 1.00 38.99 ?  516 GLN B NE2   1 
ATOM   9694  N  N     . TYR B 1 517 ? 119.585 164.271 151.754 1.00 27.08 ?  517 TYR B N     1 
ATOM   9695  C  CA    . TYR B 1 517 ? 119.226 164.043 153.150 1.00 23.87 ?  517 TYR B CA    1 
ATOM   9696  C  C     . TYR B 1 517 ? 117.881 164.676 153.482 1.00 33.52 ?  517 TYR B C     1 
ATOM   9697  O  O     . TYR B 1 517 ? 117.115 164.134 154.286 1.00 42.64 ?  517 TYR B O     1 
ATOM   9698  C  CB    . TYR B 1 517 ? 120.312 164.589 154.078 1.00 21.30 ?  517 TYR B CB    1 
ATOM   9699  C  CG    . TYR B 1 517 ? 119.794 164.997 155.442 1.00 30.35 ?  517 TYR B CG    1 
ATOM   9700  C  CD1   . TYR B 1 517 ? 119.647 164.062 156.457 1.00 21.55 ?  517 TYR B CD1   1 
ATOM   9701  C  CD2   . TYR B 1 517 ? 119.452 166.318 155.713 1.00 31.64 ?  517 TYR B CD2   1 
ATOM   9702  C  CE1   . TYR B 1 517 ? 119.171 164.428 157.700 1.00 28.97 ?  517 TYR B CE1   1 
ATOM   9703  C  CE2   . TYR B 1 517 ? 118.973 166.689 156.950 1.00 27.98 ?  517 TYR B CE2   1 
ATOM   9704  C  CZ    . TYR B 1 517 ? 118.834 165.741 157.940 1.00 32.53 ?  517 TYR B CZ    1 
ATOM   9705  O  OH    . TYR B 1 517 ? 118.361 166.112 159.175 1.00 37.96 ?  517 TYR B OH    1 
ATOM   9706  N  N     . GLU B 1 518 ? 117.583 165.827 152.875 1.00 31.78 ?  518 GLU B N     1 
ATOM   9707  C  CA    . GLU B 1 518 ? 116.400 166.601 153.237 1.00 35.03 ?  518 GLU B CA    1 
ATOM   9708  C  C     . GLU B 1 518 ? 115.105 165.833 153.018 1.00 37.14 ?  518 GLU B C     1 
ATOM   9709  O  O     . GLU B 1 518 ? 114.108 166.119 153.688 1.00 41.81 ?  518 GLU B O     1 
ATOM   9710  C  CB    . GLU B 1 518 ? 116.370 167.910 152.444 1.00 33.49 ?  518 GLU B CB    1 
ATOM   9711  C  CG    . GLU B 1 518 ? 117.712 168.630 152.366 1.00 37.43 ?  518 GLU B CG    1 
ATOM   9712  C  CD    . GLU B 1 518 ? 118.599 168.113 151.247 1.00 46.20 ?  518 GLU B CD    1 
ATOM   9713  O  OE1   . GLU B 1 518 ? 118.113 168.009 150.100 1.00 44.98 ?  518 GLU B OE1   1 
ATOM   9714  O  OE2   . GLU B 1 518 ? 119.779 167.803 151.515 1.00 40.78 -1 518 GLU B OE2   1 
ATOM   9715  N  N     . GLY B 1 519 ? 115.091 164.872 152.098 1.00 28.86 ?  519 GLY B N     1 
ATOM   9716  C  CA    . GLY B 1 519 ? 113.927 164.032 151.913 1.00 23.81 ?  519 GLY B CA    1 
ATOM   9717  C  C     . GLY B 1 519 ? 113.850 162.824 152.814 1.00 25.57 ?  519 GLY B C     1 
ATOM   9718  O  O     . GLY B 1 519 ? 112.835 162.123 152.807 1.00 33.54 ?  519 GLY B O     1 
ATOM   9719  N  N     . SER B 1 520 ? 114.892 162.565 153.598 1.00 25.82 ?  520 SER B N     1 
ATOM   9720  C  CA    . SER B 1 520 ? 114.946 161.367 154.418 1.00 23.88 ?  520 SER B CA    1 
ATOM   9721  C  C     . SER B 1 520 ? 114.032 161.490 155.634 1.00 26.94 ?  520 SER B C     1 
ATOM   9722  O  O     . SER B 1 520 ? 113.576 162.577 156.000 1.00 27.18 ?  520 SER B O     1 
ATOM   9723  C  CB    . SER B 1 520 ? 116.380 161.090 154.869 1.00 21.54 ?  520 SER B CB    1 
ATOM   9724  O  OG    . SER B 1 520 ? 116.913 162.192 155.581 1.00 26.70 ?  520 SER B OG    1 
ATOM   9725  N  N     . THR B 1 521 ? 113.761 160.343 156.259 1.00 24.19 ?  521 THR B N     1 
ATOM   9726  C  CA    . THR B 1 521 ? 112.974 160.328 157.485 1.00 24.61 ?  521 THR B CA    1 
ATOM   9727  C  C     . THR B 1 521 ? 113.722 160.950 158.653 1.00 28.11 ?  521 THR B C     1 
ATOM   9728  O  O     . THR B 1 521 ? 113.089 161.355 159.634 1.00 32.01 ?  521 THR B O     1 
ATOM   9729  C  CB    . THR B 1 521 ? 112.561 158.899 157.830 1.00 28.66 ?  521 THR B CB    1 
ATOM   9730  O  OG1   . THR B 1 521 ? 113.720 158.140 158.191 1.00 30.86 ?  521 THR B OG1   1 
ATOM   9731  C  CG2   . THR B 1 521 ? 111.889 158.244 156.640 1.00 19.23 ?  521 THR B CG2   1 
ATOM   9732  N  N     . TYR B 1 522 ? 115.052 161.022 158.576 1.00 27.68 ?  522 TYR B N     1 
ATOM   9733  C  CA    . TYR B 1 522 ? 115.809 161.769 159.573 1.00 19.35 ?  522 TYR B CA    1 
ATOM   9734  C  C     . TYR B 1 522 ? 115.455 163.249 159.533 1.00 26.13 ?  522 TYR B C     1 
ATOM   9735  O  O     . TYR B 1 522 ? 115.302 163.889 160.580 1.00 31.32 ?  522 TYR B O     1 
ATOM   9736  C  CB    . TYR B 1 522 ? 117.307 161.584 159.345 1.00 21.34 ?  522 TYR B CB    1 
ATOM   9737  C  CG    . TYR B 1 522 ? 117.782 160.155 159.413 1.00 21.56 ?  522 TYR B CG    1 
ATOM   9738  C  CD1   . TYR B 1 522 ? 117.730 159.444 160.601 1.00 20.11 ?  522 TYR B CD1   1 
ATOM   9739  C  CD2   . TYR B 1 522 ? 118.308 159.525 158.294 1.00 22.80 ?  522 TYR B CD2   1 
ATOM   9740  C  CE1   . TYR B 1 522 ? 118.179 158.145 160.673 1.00 24.06 ?  522 TYR B CE1   1 
ATOM   9741  C  CE2   . TYR B 1 522 ? 118.755 158.225 158.356 1.00 19.98 ?  522 TYR B CE2   1 
ATOM   9742  C  CZ    . TYR B 1 522 ? 118.686 157.539 159.547 1.00 25.74 ?  522 TYR B CZ    1 
ATOM   9743  O  OH    . TYR B 1 522 ? 119.130 156.242 159.614 1.00 29.11 ?  522 TYR B OH    1 
ATOM   9744  N  N     . ALA B 1 523 ? 115.333 163.810 158.329 1.00 33.00 ?  523 ALA B N     1 
ATOM   9745  C  CA    . ALA B 1 523 ? 115.022 165.228 158.193 1.00 26.34 ?  523 ALA B CA    1 
ATOM   9746  C  C     . ALA B 1 523 ? 113.611 165.536 158.674 1.00 30.52 ?  523 ALA B C     1 
ATOM   9747  O  O     . ALA B 1 523 ? 113.383 166.557 159.331 1.00 34.10 ?  523 ALA B O     1 
ATOM   9748  C  CB    . ALA B 1 523 ? 115.202 165.664 156.740 1.00 24.96 ?  523 ALA B CB    1 
ATOM   9749  N  N     . THR B 1 524 ? 112.652 164.667 158.356 1.00 30.85 ?  524 THR B N     1 
ATOM   9750  C  CA    . THR B 1 524 ? 111.267 164.890 158.749 1.00 26.94 ?  524 THR B CA    1 
ATOM   9751  C  C     . THR B 1 524 ? 110.974 164.453 160.176 1.00 34.75 ?  524 THR B C     1 
ATOM   9752  O  O     . THR B 1 524 ? 109.892 164.760 160.688 1.00 41.72 ?  524 THR B O     1 
ATOM   9753  C  CB    . THR B 1 524 ? 110.323 164.159 157.791 1.00 33.13 ?  524 THR B CB    1 
ATOM   9754  O  OG1   . THR B 1 524 ? 110.274 162.769 158.133 1.00 35.03 ?  524 THR B OG1   1 
ATOM   9755  C  CG2   . THR B 1 524 ? 110.806 164.303 156.359 1.00 32.61 ?  524 THR B CG2   1 
ATOM   9756  N  N     . GLY B 1 525 ? 111.899 163.753 160.829 1.00 29.82 ?  525 GLY B N     1 
ATOM   9757  C  CA    . GLY B 1 525 ? 111.688 163.284 162.180 1.00 27.05 ?  525 GLY B CA    1 
ATOM   9758  C  C     . GLY B 1 525 ? 110.881 162.011 162.298 1.00 33.85 ?  525 GLY B C     1 
ATOM   9759  O  O     . GLY B 1 525 ? 110.692 161.520 163.418 1.00 32.98 ?  525 GLY B O     1 
ATOM   9760  N  N     . GLU B 1 526 ? 110.398 161.461 161.183 1.00 37.62 ?  526 GLU B N     1 
ATOM   9761  C  CA    . GLU B 1 526 ? 109.636 160.220 161.226 1.00 35.57 ?  526 GLU B CA    1 
ATOM   9762  C  C     . GLU B 1 526 ? 110.490 159.047 161.689 1.00 35.56 ?  526 GLU B C     1 
ATOM   9763  O  O     . GLU B 1 526 ? 109.954 158.076 162.235 1.00 41.96 ?  526 GLU B O     1 
ATOM   9764  C  CB    . GLU B 1 526 ? 109.030 159.949 159.844 1.00 36.25 ?  526 GLU B CB    1 
ATOM   9765  C  CG    . GLU B 1 526 ? 108.419 158.572 159.656 1.00 36.93 ?  526 GLU B CG    1 
ATOM   9766  C  CD    . GLU B 1 526 ? 108.406 158.137 158.204 1.00 44.72 ?  526 GLU B CD    1 
ATOM   9767  O  OE1   . GLU B 1 526 ? 108.349 159.019 157.321 1.00 43.21 ?  526 GLU B OE1   1 
ATOM   9768  O  OE2   . GLU B 1 526 ? 108.455 156.917 157.946 1.00 42.49 -1 526 GLU B OE2   1 
ATOM   9769  N  N     . TYR B 1 527 ? 111.809 159.131 161.510 1.00 35.15 ?  527 TYR B N     1 
ATOM   9770  C  CA    . TYR B 1 527 ? 112.696 158.068 161.970 1.00 25.96 ?  527 TYR B CA    1 
ATOM   9771  C  C     . TYR B 1 527 ? 112.646 157.919 163.486 1.00 28.26 ?  527 TYR B C     1 
ATOM   9772  O  O     . TYR B 1 527 ? 112.672 156.800 164.009 1.00 35.04 ?  527 TYR B O     1 
ATOM   9773  C  CB    . TYR B 1 527 ? 114.125 158.349 161.507 1.00 23.59 ?  527 TYR B CB    1 
ATOM   9774  C  CG    . TYR B 1 527 ? 115.121 157.288 161.907 1.00 28.20 ?  527 TYR B CG    1 
ATOM   9775  C  CD1   . TYR B 1 527 ? 115.366 156.196 161.089 1.00 23.69 ?  527 TYR B CD1   1 
ATOM   9776  C  CD2   . TYR B 1 527 ? 115.817 157.377 163.106 1.00 28.68 ?  527 TYR B CD2   1 
ATOM   9777  C  CE1   . TYR B 1 527 ? 116.273 155.226 161.450 1.00 23.79 ?  527 TYR B CE1   1 
ATOM   9778  C  CE2   . TYR B 1 527 ? 116.724 156.410 163.475 1.00 24.28 ?  527 TYR B CE2   1 
ATOM   9779  C  CZ    . TYR B 1 527 ? 116.948 155.338 162.644 1.00 23.27 ?  527 TYR B CZ    1 
ATOM   9780  O  OH    . TYR B 1 527 ? 117.854 154.371 163.008 1.00 32.61 ?  527 TYR B OH    1 
ATOM   9781  N  N     . PHE B 1 528 ? 112.577 159.035 164.205 1.00 32.99 ?  528 PHE B N     1 
ATOM   9782  C  CA    . PHE B 1 528 ? 112.708 159.050 165.654 1.00 27.64 ?  528 PHE B CA    1 
ATOM   9783  C  C     . PHE B 1 528 ? 111.393 158.796 166.382 1.00 36.60 ?  528 PHE B C     1 
ATOM   9784  O  O     . PHE B 1 528 ? 111.355 158.915 167.609 1.00 46.33 ?  528 PHE B O     1 
ATOM   9785  C  CB    . PHE B 1 528 ? 113.292 160.388 166.113 1.00 30.83 ?  528 PHE B CB    1 
ATOM   9786  C  CG    . PHE B 1 528 ? 114.639 160.696 165.530 1.00 33.47 ?  528 PHE B CG    1 
ATOM   9787  C  CD1   . PHE B 1 528 ? 115.794 160.271 166.161 1.00 24.97 ?  528 PHE B CD1   1 
ATOM   9788  C  CD2   . PHE B 1 528 ? 114.752 161.418 164.354 1.00 34.19 ?  528 PHE B CD2   1 
ATOM   9789  C  CE1   . PHE B 1 528 ? 117.034 160.555 165.628 1.00 28.35 ?  528 PHE B CE1   1 
ATOM   9790  C  CE2   . PHE B 1 528 ? 115.990 161.703 163.818 1.00 33.73 ?  528 PHE B CE2   1 
ATOM   9791  C  CZ    . PHE B 1 528 ? 117.132 161.272 164.457 1.00 31.75 ?  528 PHE B CZ    1 
ATOM   9792  N  N     . ASP B 1 529 ? 110.322 158.455 165.661 1.00 37.70 ?  529 ASP B N     1 
ATOM   9793  C  CA    . ASP B 1 529 ? 109.010 158.331 166.291 1.00 35.02 ?  529 ASP B CA    1 
ATOM   9794  C  C     . ASP B 1 529 ? 109.005 157.250 167.366 1.00 38.65 ?  529 ASP B C     1 
ATOM   9795  O  O     . ASP B 1 529 ? 108.600 157.493 168.510 1.00 42.72 ?  529 ASP B O     1 
ATOM   9796  C  CB    . ASP B 1 529 ? 107.952 158.036 165.230 1.00 32.50 ?  529 ASP B CB    1 
ATOM   9797  C  CG    . ASP B 1 529 ? 107.747 159.192 164.275 1.00 43.06 ?  529 ASP B CG    1 
ATOM   9798  O  OD1   . ASP B 1 529 ? 108.207 160.312 164.585 1.00 42.20 ?  529 ASP B OD1   1 
ATOM   9799  O  OD2   . ASP B 1 529 ? 107.126 158.981 163.212 1.00 48.54 -1 529 ASP B OD2   1 
ATOM   9800  N  N     . LYS B 1 530 ? 109.462 156.046 167.017 1.00 39.76 ?  530 LYS B N     1 
ATOM   9801  C  CA    . LYS B 1 530 ? 109.482 154.954 167.982 1.00 35.45 ?  530 LYS B CA    1 
ATOM   9802  C  C     . LYS B 1 530 ? 110.484 155.189 169.101 1.00 38.94 ?  530 LYS B C     1 
ATOM   9803  O  O     . LYS B 1 530 ? 110.375 154.559 170.156 1.00 43.21 ?  530 LYS B O     1 
ATOM   9804  C  CB    . LYS B 1 530 ? 109.791 153.635 167.276 1.00 37.18 ?  530 LYS B CB    1 
ATOM   9805  C  CG    . LYS B 1 530 ? 111.258 153.256 167.282 1.00 32.74 ?  530 LYS B CG    1 
ATOM   9806  C  CD    . LYS B 1 530 ? 111.489 151.988 166.493 1.00 38.19 ?  530 LYS B CD    1 
ATOM   9807  C  CE    . LYS B 1 530 ? 112.920 151.521 166.614 1.00 34.66 ?  530 LYS B CE    1 
ATOM   9808  N  NZ    . LYS B 1 530 ? 113.444 151.124 165.284 1.00 43.09 1  530 LYS B NZ    1 
ATOM   9809  N  N     . TYR B 1 531 ? 111.454 156.074 168.898 1.00 39.67 ?  531 TYR B N     1 
ATOM   9810  C  CA    . TYR B 1 531 ? 112.436 156.366 169.930 1.00 32.48 ?  531 TYR B CA    1 
ATOM   9811  C  C     . TYR B 1 531 ? 111.983 157.472 170.867 1.00 31.41 ?  531 TYR B C     1 
ATOM   9812  O  O     . TYR B 1 531 ? 112.324 157.446 172.055 1.00 40.60 ?  531 TYR B O     1 
ATOM   9813  C  CB    . TYR B 1 531 ? 113.771 156.742 169.289 1.00 27.04 ?  531 TYR B CB    1 
ATOM   9814  C  CG    . TYR B 1 531 ? 114.522 155.564 168.718 1.00 32.01 ?  531 TYR B CG    1 
ATOM   9815  C  CD1   . TYR B 1 531 ? 114.915 154.509 169.529 1.00 26.09 ?  531 TYR B CD1   1 
ATOM   9816  C  CD2   . TYR B 1 531 ? 114.838 155.505 167.368 1.00 28.89 ?  531 TYR B CD2   1 
ATOM   9817  C  CE1   . TYR B 1 531 ? 115.602 153.433 169.015 1.00 31.55 ?  531 TYR B CE1   1 
ATOM   9818  C  CE2   . TYR B 1 531 ? 115.526 154.432 166.845 1.00 25.44 ?  531 TYR B CE2   1 
ATOM   9819  C  CZ    . TYR B 1 531 ? 115.905 153.399 167.673 1.00 31.42 ?  531 TYR B CZ    1 
ATOM   9820  O  OH    . TYR B 1 531 ? 116.592 152.326 167.159 1.00 30.43 ?  531 TYR B OH    1 
ATOM   9821  N  N     . VAL B 1 532 ? 111.224 158.447 170.359 1.00 38.40 ?  532 VAL B N     1 
ATOM   9822  C  CA    . VAL B 1 532 ? 110.638 159.472 171.217 1.00 34.75 ?  532 VAL B CA    1 
ATOM   9823  C  C     . VAL B 1 532 ? 109.315 159.037 171.819 1.00 39.86 ?  532 VAL B C     1 
ATOM   9824  O  O     . VAL B 1 532 ? 108.762 159.758 172.660 1.00 47.83 ?  532 VAL B O     1 
ATOM   9825  C  CB    . VAL B 1 532 ? 110.422 160.793 170.452 1.00 40.64 ?  532 VAL B CB    1 
ATOM   9826  C  CG1   . VAL B 1 532 ? 111.720 161.262 169.819 1.00 37.44 ?  532 VAL B CG1   1 
ATOM   9827  C  CG2   . VAL B 1 532 ? 109.334 160.628 169.404 1.00 37.46 ?  532 VAL B CG2   1 
ATOM   9828  N  N     . SER B 1 533 ? 108.784 157.884 171.412 1.00 40.67 ?  533 SER B N     1 
ATOM   9829  C  CA    . SER B 1 533 ? 107.542 157.370 171.972 1.00 40.28 ?  533 SER B CA    1 
ATOM   9830  C  C     . SER B 1 533 ? 107.725 156.162 172.876 1.00 41.24 ?  533 SER B C     1 
ATOM   9831  O  O     . SER B 1 533 ? 106.969 156.008 173.836 1.00 46.20 ?  533 SER B O     1 
ATOM   9832  C  CB    . SER B 1 533 ? 106.566 156.997 170.849 1.00 45.12 ?  533 SER B CB    1 
ATOM   9833  O  OG    . SER B 1 533 ? 106.855 155.711 170.331 1.00 46.69 ?  533 SER B OG    1 
ATOM   9834  N  N     . THR B 1 534 ? 108.705 155.306 172.599 1.00 46.10 ?  534 THR B N     1 
ATOM   9835  C  CA    . THR B 1 534 ? 108.918 154.077 173.350 1.00 41.87 ?  534 THR B CA    1 
ATOM   9836  C  C     . THR B 1 534 ? 110.235 154.156 174.109 1.00 41.15 ?  534 THR B C     1 
ATOM   9837  O  O     . THR B 1 534 ? 111.221 154.703 173.606 1.00 49.01 ?  534 THR B O     1 
ATOM   9838  C  CB    . THR B 1 534 ? 108.925 152.855 172.421 1.00 42.71 ?  534 THR B CB    1 
ATOM   9839  O  OG1   . THR B 1 534 ? 107.786 152.904 171.555 1.00 42.40 ?  534 THR B OG1   1 
ATOM   9840  C  CG2   . THR B 1 534 ? 108.886 151.564 173.225 1.00 43.68 ?  534 THR B CG2   1 
ATOM   9841  N  N     . ASP B 1 535 ? 110.243 153.608 175.319 1.00 43.04 ?  535 ASP B N     1 
ATOM   9842  C  CA    . ASP B 1 535 ? 111.442 153.528 176.141 1.00 42.66 ?  535 ASP B CA    1 
ATOM   9843  C  C     . ASP B 1 535 ? 112.117 152.184 175.908 1.00 45.35 ?  535 ASP B C     1 
ATOM   9844  O  O     . ASP B 1 535 ? 111.464 151.137 175.965 1.00 47.18 ?  535 ASP B O     1 
ATOM   9845  C  CB    . ASP B 1 535 ? 111.100 153.701 177.622 1.00 41.53 ?  535 ASP B CB    1 
ATOM   9846  C  CG    . ASP B 1 535 ? 112.332 153.855 178.489 1.00 47.31 ?  535 ASP B CG    1 
ATOM   9847  O  OD1   . ASP B 1 535 ? 113.057 154.858 178.323 1.00 48.84 ?  535 ASP B OD1   1 
ATOM   9848  O  OD2   . ASP B 1 535 ? 112.574 152.973 179.338 1.00 47.75 -1 535 ASP B OD2   1 
ATOM   9849  N  N     . PHE B 1 536 ? 113.424 152.216 175.646 1.00 40.14 ?  536 PHE B N     1 
ATOM   9850  C  CA    . PHE B 1 536 ? 114.185 151.014 175.334 1.00 34.91 ?  536 PHE B CA    1 
ATOM   9851  C  C     . PHE B 1 536 ? 115.173 150.649 176.438 1.00 35.66 ?  536 PHE B C     1 
ATOM   9852  O  O     . PHE B 1 536 ? 116.167 149.966 176.175 1.00 43.03 ?  536 PHE B O     1 
ATOM   9853  C  CB    . PHE B 1 536 ? 114.911 151.181 173.999 1.00 34.94 ?  536 PHE B CB    1 
ATOM   9854  C  CG    . PHE B 1 536 ? 113.993 151.222 172.812 1.00 31.98 ?  536 PHE B CG    1 
ATOM   9855  C  CD1   . PHE B 1 536 ? 113.622 150.057 172.166 1.00 32.97 ?  536 PHE B CD1   1 
ATOM   9856  C  CD2   . PHE B 1 536 ? 113.499 152.426 172.344 1.00 32.10 ?  536 PHE B CD2   1 
ATOM   9857  C  CE1   . PHE B 1 536 ? 112.777 150.091 171.076 1.00 31.04 ?  536 PHE B CE1   1 
ATOM   9858  C  CE2   . PHE B 1 536 ? 112.653 152.464 171.253 1.00 39.85 ?  536 PHE B CE2   1 
ATOM   9859  C  CZ    . PHE B 1 536 ? 112.293 151.295 170.619 1.00 30.69 ?  536 PHE B CZ    1 
ATOM   9860  N  N     . SER B 1 537 ? 114.922 151.099 177.665 1.00 36.35 ?  537 SER B N     1 
ATOM   9861  C  CA    . SER B 1 537 ? 115.711 150.665 178.802 1.00 34.06 ?  537 SER B CA    1 
ATOM   9862  C  C     . SER B 1 537 ? 115.417 149.197 179.106 1.00 38.38 ?  537 SER B C     1 
ATOM   9863  O  O     . SER B 1 537 ? 114.351 148.685 178.757 1.00 41.45 ?  537 SER B O     1 
ATOM   9864  C  CB    . SER B 1 537 ? 115.405 151.534 180.020 1.00 34.61 ?  537 SER B CB    1 
ATOM   9865  O  OG    . SER B 1 537 ? 114.049 151.410 180.406 1.00 39.68 ?  537 SER B OG    1 
ATOM   9866  N  N     . PRO B 1 538 ? 116.356 148.492 179.737 1.00 37.30 ?  538 PRO B N     1 
ATOM   9867  C  CA    . PRO B 1 538 ? 116.131 147.071 180.025 1.00 35.39 ?  538 PRO B CA    1 
ATOM   9868  C  C     . PRO B 1 538 ? 114.937 146.867 180.945 1.00 40.61 ?  538 PRO B C     1 
ATOM   9869  O  O     . PRO B 1 538 ? 114.691 147.652 181.863 1.00 39.18 ?  538 PRO B O     1 
ATOM   9870  C  CB    . PRO B 1 538 ? 117.439 146.631 180.695 1.00 35.57 ?  538 PRO B CB    1 
ATOM   9871  C  CG    . PRO B 1 538 ? 118.441 147.662 180.311 1.00 34.04 ?  538 PRO B CG    1 
ATOM   9872  C  CD    . PRO B 1 538 ? 117.678 148.939 180.203 1.00 36.00 ?  538 PRO B CD    1 
ATOM   9873  N  N     . LYS B 1 539 ? 114.190 145.796 180.685 1.00 45.36 ?  539 LYS B N     1 
ATOM   9874  C  CA    . LYS B 1 539 ? 113.037 145.429 181.495 1.00 45.52 ?  539 LYS B CA    1 
ATOM   9875  C  C     . LYS B 1 539 ? 113.374 144.408 182.572 1.00 47.99 ?  539 LYS B C     1 
ATOM   9876  O  O     . LYS B 1 539 ? 112.488 144.022 183.339 1.00 48.24 ?  539 LYS B O     1 
ATOM   9877  C  CB    . LYS B 1 539 ? 111.916 144.883 180.604 1.00 45.74 ?  539 LYS B CB    1 
ATOM   9878  C  CG    . LYS B 1 539 ? 111.890 145.470 179.204 1.00 43.95 ?  539 LYS B CG    1 
ATOM   9879  C  CD    . LYS B 1 539 ? 111.327 146.882 179.203 1.00 48.13 ?  539 LYS B CD    1 
ATOM   9880  C  CE    . LYS B 1 539 ? 110.525 147.153 177.940 1.00 49.03 ?  539 LYS B CE    1 
ATOM   9881  N  NZ    . LYS B 1 539 ? 111.387 147.192 176.727 1.00 49.69 1  539 LYS B NZ    1 
ATOM   9882  N  N     . TYR B 1 540 ? 114.625 143.966 182.646 1.00 45.89 ?  540 TYR B N     1 
ATOM   9883  C  CA    . TYR B 1 540 ? 115.060 142.974 183.615 1.00 43.91 ?  540 TYR B CA    1 
ATOM   9884  C  C     . TYR B 1 540 ? 116.151 143.565 184.494 1.00 46.08 ?  540 TYR B C     1 
ATOM   9885  O  O     . TYR B 1 540 ? 117.026 144.289 184.010 1.00 47.79 ?  540 TYR B O     1 
ATOM   9886  C  CB    . TYR B 1 540 ? 115.568 141.709 182.919 1.00 44.43 ?  540 TYR B CB    1 
ATOM   9887  C  CG    . TYR B 1 540 ? 114.492 140.952 182.176 1.00 47.68 ?  540 TYR B CG    1 
ATOM   9888  C  CD1   . TYR B 1 540 ? 114.174 141.268 180.862 1.00 44.57 ?  540 TYR B CD1   1 
ATOM   9889  C  CD2   . TYR B 1 540 ? 113.789 139.926 182.790 1.00 48.48 ?  540 TYR B CD2   1 
ATOM   9890  C  CE1   . TYR B 1 540 ? 113.190 140.581 180.181 1.00 43.43 ?  540 TYR B CE1   1 
ATOM   9891  C  CE2   . TYR B 1 540 ? 112.803 139.233 182.116 1.00 45.36 ?  540 TYR B CE2   1 
ATOM   9892  C  CZ    . TYR B 1 540 ? 112.507 139.565 180.812 1.00 44.75 ?  540 TYR B CZ    1 
ATOM   9893  O  OH    . TYR B 1 540 ? 111.526 138.878 180.139 1.00 49.48 ?  540 TYR B OH    1 
ATOM   9894  N  N     . GLU B 1 541 ? 116.087 143.256 185.791 1.00 49.92 ?  541 GLU B N     1 
ATOM   9895  C  CA    . GLU B 1 541 ? 117.065 143.792 186.732 1.00 45.77 ?  541 GLU B CA    1 
ATOM   9896  C  C     . GLU B 1 541 ? 118.470 143.297 186.411 1.00 46.72 ?  541 GLU B C     1 
ATOM   9897  O  O     . GLU B 1 541 ? 119.446 144.045 186.550 1.00 46.88 ?  541 GLU B O     1 
ATOM   9898  C  CB    . GLU B 1 541 ? 116.676 143.420 188.162 1.00 46.79 ?  541 GLU B CB    1 
ATOM   9899  C  CG    . GLU B 1 541 ? 117.513 144.101 189.232 1.00 48.67 ?  541 GLU B CG    1 
ATOM   9900  C  CD    . GLU B 1 541 ? 118.378 143.124 190.004 1.00 53.09 ?  541 GLU B CD    1 
ATOM   9901  O  OE1   . GLU B 1 541 ? 118.202 141.901 189.821 1.00 50.43 ?  541 GLU B OE1   1 
ATOM   9902  O  OE2   . GLU B 1 541 ? 119.232 143.579 190.793 1.00 53.20 -1 541 GLU B OE2   1 
ATOM   9903  N  N     . LYS B 1 542 ? 118.595 142.036 185.991 1.00 43.44 ?  542 LYS B N     1 
ATOM   9904  C  CA    . LYS B 1 542 ? 119.904 141.505 185.624 1.00 39.82 ?  542 LYS B CA    1 
ATOM   9905  C  C     . LYS B 1 542 ? 120.488 142.249 184.431 1.00 44.78 ?  542 LYS B C     1 
ATOM   9906  O  O     . LYS B 1 542 ? 121.680 142.580 184.418 1.00 42.69 ?  542 LYS B O     1 
ATOM   9907  C  CB    . LYS B 1 542 ? 119.798 140.010 185.323 1.00 41.29 ?  542 LYS B CB    1 
ATOM   9908  C  CG    . LYS B 1 542 ? 121.087 139.390 184.814 1.00 43.38 ?  542 LYS B CG    1 
ATOM   9909  C  CD    . LYS B 1 542 ? 120.972 137.880 184.698 1.00 41.03 ?  542 LYS B CD    1 
ATOM   9910  C  CE    . LYS B 1 542 ? 122.316 137.252 184.372 1.00 44.05 ?  542 LYS B CE    1 
ATOM   9911  N  NZ    . LYS B 1 542 ? 122.276 135.769 184.480 1.00 44.68 1  542 LYS B NZ    1 
ATOM   9912  N  N     . ILE B 1 543 ? 119.665 142.522 183.418 1.00 43.71 ?  543 ILE B N     1 
ATOM   9913  C  CA    . ILE B 1 543 ? 120.144 143.251 182.248 1.00 37.51 ?  543 ILE B CA    1 
ATOM   9914  C  C     . ILE B 1 543 ? 120.443 144.701 182.605 1.00 37.39 ?  543 ILE B C     1 
ATOM   9915  O  O     . ILE B 1 543 ? 121.438 145.274 182.146 1.00 37.90 ?  543 ILE B O     1 
ATOM   9916  C  CB    . ILE B 1 543 ? 119.124 143.148 181.101 1.00 36.35 ?  543 ILE B CB    1 
ATOM   9917  C  CG1   . ILE B 1 543 ? 118.804 141.684 180.796 1.00 39.05 ?  543 ILE B CG1   1 
ATOM   9918  C  CG2   . ILE B 1 543 ? 119.652 143.844 179.864 1.00 36.17 ?  543 ILE B CG2   1 
ATOM   9919  C  CD1   . ILE B 1 543 ? 120.025 140.815 180.609 1.00 33.21 ?  543 ILE B CD1   1 
ATOM   9920  N  N     . ALA B 1 544 ? 119.588 145.320 183.424 1.00 35.49 ?  544 ALA B N     1 
ATOM   9921  C  CA    . ALA B 1 544 ? 119.834 146.696 183.842 1.00 39.29 ?  544 ALA B CA    1 
ATOM   9922  C  C     . ALA B 1 544 ? 121.116 146.813 184.655 1.00 44.33 ?  544 ALA B C     1 
ATOM   9923  O  O     . ALA B 1 544 ? 121.749 147.875 184.665 1.00 48.55 ?  544 ALA B O     1 
ATOM   9924  C  CB    . ALA B 1 544 ? 118.646 147.222 184.645 1.00 40.47 ?  544 ALA B CB    1 
ATOM   9925  N  N     . ASN B 1 545 ? 121.513 145.740 185.341 1.00 45.04 ?  545 ASN B N     1 
ATOM   9926  C  CA    . ASN B 1 545 ? 122.778 145.753 186.066 1.00 45.81 ?  545 ASN B CA    1 
ATOM   9927  C  C     . ASN B 1 545 ? 123.966 145.654 185.120 1.00 44.60 ?  545 ASN B C     1 
ATOM   9928  O  O     . ASN B 1 545 ? 125.065 146.111 185.458 1.00 46.40 ?  545 ASN B O     1 
ATOM   9929  C  CB    . ASN B 1 545 ? 122.815 144.615 187.085 1.00 47.28 ?  545 ASN B CB    1 
ATOM   9930  C  CG    . ASN B 1 545 ? 121.978 144.906 188.313 1.00 49.62 ?  545 ASN B CG    1 
ATOM   9931  O  OD1   . ASN B 1 545 ? 121.773 146.064 188.678 1.00 48.80 ?  545 ASN B OD1   1 
ATOM   9932  N  ND2   . ASN B 1 545 ? 121.490 143.854 188.960 1.00 44.89 ?  545 ASN B ND2   1 
ATOM   9933  N  N     . LEU B 1 546 ? 123.772 145.058 183.941 1.00 44.21 ?  546 LEU B N     1 
ATOM   9934  C  CA    . LEU B 1 546 ? 124.856 144.969 182.969 1.00 37.40 ?  546 LEU B CA    1 
ATOM   9935  C  C     . LEU B 1 546 ? 125.267 146.344 182.463 1.00 37.79 ?  546 LEU B C     1 
ATOM   9936  O  O     . LEU B 1 546 ? 126.430 146.551 182.102 1.00 39.54 ?  546 LEU B O     1 
ATOM   9937  C  CB    . LEU B 1 546 ? 124.441 144.080 181.797 1.00 36.36 ?  546 LEU B CB    1 
ATOM   9938  C  CG    . LEU B 1 546 ? 124.101 142.623 182.113 1.00 38.55 ?  546 LEU B CG    1 
ATOM   9939  C  CD1   . LEU B 1 546 ? 123.618 141.912 180.862 1.00 37.37 ?  546 LEU B CD1   1 
ATOM   9940  C  CD2   . LEU B 1 546 ? 125.299 141.906 182.709 1.00 37.55 ?  546 LEU B CD2   1 
ATOM   9941  N  N     . PHE B 1 547 ? 124.335 147.296 182.441 1.00 39.72 ?  547 PHE B N     1 
ATOM   9942  C  CA    . PHE B 1 547 ? 124.591 148.644 181.953 1.00 38.97 ?  547 PHE B CA    1 
ATOM   9943  C  C     . PHE B 1 547 ? 124.913 149.618 183.079 1.00 40.70 ?  547 PHE B C     1 
ATOM   9944  O  O     . PHE B 1 547 ? 124.812 150.834 182.884 1.00 44.69 ?  547 PHE B O     1 
ATOM   9945  C  CB    . PHE B 1 547 ? 123.394 149.149 181.146 1.00 37.62 ?  547 PHE B CB    1 
ATOM   9946  C  CG    . PHE B 1 547 ? 123.183 148.420 179.850 1.00 39.12 ?  547 PHE B CG    1 
ATOM   9947  C  CD1   . PHE B 1 547 ? 122.400 147.280 179.800 1.00 37.61 ?  547 PHE B CD1   1 
ATOM   9948  C  CD2   . PHE B 1 547 ? 123.764 148.877 178.680 1.00 38.44 ?  547 PHE B CD2   1 
ATOM   9949  C  CE1   . PHE B 1 547 ? 122.202 146.610 178.608 1.00 38.08 ?  547 PHE B CE1   1 
ATOM   9950  C  CE2   . PHE B 1 547 ? 123.569 148.211 177.487 1.00 33.49 ?  547 PHE B CE2   1 
ATOM   9951  C  CZ    . PHE B 1 547 ? 122.788 147.077 177.452 1.00 35.40 ?  547 PHE B CZ    1 
ATOM   9952  N  N     . GLU B 1 548 ? 125.284 149.110 184.251 1.00 47.33 ?  548 GLU B N     1 
ATOM   9953  C  CA    . GLU B 1 548 ? 125.624 149.976 185.370 1.00 48.82 ?  548 GLU B CA    1 
ATOM   9954  C  C     . GLU B 1 548 ? 126.844 150.824 185.035 1.00 52.47 ?  548 GLU B C     1 
ATOM   9955  O  O     . GLU B 1 548 ? 127.794 150.354 184.403 1.00 52.34 ?  548 GLU B O     1 
ATOM   9956  C  CB    . GLU B 1 548 ? 125.889 149.143 186.625 1.00 47.67 ?  548 GLU B CB    1 
ATOM   9957  C  CG    . GLU B 1 548 ? 124.666 148.924 187.498 1.00 50.67 ?  548 GLU B CG    1 
ATOM   9958  C  CD    . GLU B 1 548 ? 124.887 147.853 188.548 1.00 56.24 ?  548 GLU B CD    1 
ATOM   9959  O  OE1   . GLU B 1 548 ? 125.790 147.012 188.359 1.00 55.02 ?  548 GLU B OE1   1 
ATOM   9960  O  OE2   . GLU B 1 548 ? 124.160 147.853 189.564 1.00 55.23 -1 548 GLU B OE2   1 
ATOM   9961  N  N     . GLY B 1 549 ? 126.814 152.083 185.461 1.00 50.26 ?  549 GLY B N     1 
ATOM   9962  C  CA    . GLY B 1 549 ? 127.870 153.012 185.120 1.00 49.92 ?  549 GLY B CA    1 
ATOM   9963  C  C     . GLY B 1 549 ? 127.818 153.527 183.703 1.00 51.73 ?  549 GLY B C     1 
ATOM   9964  O  O     . GLY B 1 549 ? 128.805 154.105 183.233 1.00 54.70 ?  549 GLY B O     1 
ATOM   9965  N  N     . MET B 1 550 ? 126.701 153.335 183.007 1.00 48.89 ?  550 MET B N     1 
ATOM   9966  C  CA    . MET B 1 550 ? 126.558 153.734 181.615 1.00 44.47 ?  550 MET B CA    1 
ATOM   9967  C  C     . MET B 1 550 ? 125.178 154.337 181.420 1.00 46.73 ?  550 MET B C     1 
ATOM   9968  O  O     . MET B 1 550 ? 124.172 153.707 181.754 1.00 52.25 ?  550 MET B O     1 
ATOM   9969  C  CB    . MET B 1 550 ? 126.754 152.535 180.684 1.00 44.64 ?  550 MET B CB    1 
ATOM   9970  C  CG    . MET B 1 550 ? 127.449 152.862 179.383 1.00 51.54 ?  550 MET B CG    1 
ATOM   9971  S  SD    . MET B 1 550 ? 127.583 151.421 178.314 1.00 60.33 ?  550 MET B SD    1 
ATOM   9972  C  CE    . MET B 1 550 ? 127.596 150.092 179.513 1.00 48.02 ?  550 MET B CE    1 
ATOM   9973  N  N     . HIS B 1 551 ? 125.131 155.553 180.882 1.00 42.96 ?  551 HIS B N     1 
ATOM   9974  C  CA    . HIS B 1 551 ? 123.863 156.244 180.697 1.00 43.58 ?  551 HIS B CA    1 
ATOM   9975  C  C     . HIS B 1 551 ? 123.126 155.661 179.498 1.00 46.12 ?  551 HIS B C     1 
ATOM   9976  O  O     . HIS B 1 551 ? 123.596 155.764 178.360 1.00 44.91 ?  551 HIS B O     1 
ATOM   9977  C  CB    . HIS B 1 551 ? 124.086 157.742 180.508 1.00 41.99 ?  551 HIS B CB    1 
ATOM   9978  C  CG    . HIS B 1 551 ? 122.852 158.484 180.100 1.00 46.24 ?  551 HIS B CG    1 
ATOM   9979  N  ND1   . HIS B 1 551 ? 121.886 158.873 181.003 1.00 49.73 ?  551 HIS B ND1   1 
ATOM   9980  C  CD2   . HIS B 1 551 ? 122.424 158.903 178.886 1.00 46.93 ?  551 HIS B CD2   1 
ATOM   9981  C  CE1   . HIS B 1 551 ? 120.916 159.500 180.362 1.00 47.40 ?  551 HIS B CE1   1 
ATOM   9982  N  NE2   . HIS B 1 551 ? 121.219 159.533 179.077 1.00 46.40 ?  551 HIS B NE2   1 
ATOM   9983  N  N     . ILE B 1 552 ? 121.976 155.051 179.755 1.00 40.04 ?  552 ILE B N     1 
ATOM   9984  C  CA    . ILE B 1 552 ? 121.120 154.512 178.705 1.00 37.77 ?  552 ILE B CA    1 
ATOM   9985  C  C     . ILE B 1 552 ? 120.252 155.653 178.179 1.00 38.12 ?  552 ILE B C     1 
ATOM   9986  O  O     . ILE B 1 552 ? 119.550 156.293 178.978 1.00 37.71 ?  552 ILE B O     1 
ATOM   9987  C  CB    . ILE B 1 552 ? 120.257 153.357 179.224 1.00 36.38 ?  552 ILE B CB    1 
ATOM   9988  C  CG1   . ILE B 1 552 ? 121.149 152.230 179.743 1.00 35.67 ?  552 ILE B CG1   1 
ATOM   9989  C  CG2   . ILE B 1 552 ? 119.328 152.850 178.135 1.00 36.34 ?  552 ILE B CG2   1 
ATOM   9990  C  CD1   . ILE B 1 552 ? 120.415 151.208 180.568 1.00 38.89 ?  552 ILE B CD1   1 
ATOM   9991  N  N     . PRO B 1 553 ? 120.283 155.948 176.880 1.00 40.67 ?  553 PRO B N     1 
ATOM   9992  C  CA    . PRO B 1 553 ? 119.480 157.061 176.358 1.00 37.77 ?  553 PRO B CA    1 
ATOM   9993  C  C     . PRO B 1 553 ? 117.999 156.862 176.637 1.00 40.06 ?  553 PRO B C     1 
ATOM   9994  O  O     . PRO B 1 553 ? 117.457 155.766 176.485 1.00 41.00 ?  553 PRO B O     1 
ATOM   9995  C  CB    . PRO B 1 553 ? 119.777 157.036 174.856 1.00 34.16 ?  553 PRO B CB    1 
ATOM   9996  C  CG    . PRO B 1 553 ? 121.102 156.370 174.748 1.00 32.33 ?  553 PRO B CG    1 
ATOM   9997  C  CD    . PRO B 1 553 ? 121.143 155.355 175.845 1.00 33.34 ?  553 PRO B CD    1 
ATOM   9998  N  N     . THR B 1 554 ? 117.347 157.945 177.041 1.00 43.12 ?  554 THR B N     1 
ATOM   9999  C  CA    . THR B 1 554 ? 115.937 157.929 177.380 1.00 41.44 ?  554 THR B CA    1 
ATOM   10000 C  C     . THR B 1 554 ? 115.123 158.544 176.247 1.00 38.99 ?  554 THR B C     1 
ATOM   10001 O  O     . THR B 1 554 ? 115.640 158.875 175.177 1.00 37.79 ?  554 THR B O     1 
ATOM   10002 C  CB    . THR B 1 554 ? 115.692 158.674 178.694 1.00 37.55 ?  554 THR B CB    1 
ATOM   10003 O  OG1   . THR B 1 554 ? 115.816 160.084 178.474 1.00 43.39 ?  554 THR B OG1   1 
ATOM   10004 C  CG2   . THR B 1 554 ? 116.701 158.242 179.743 1.00 36.57 ?  554 THR B CG2   1 
ATOM   10005 N  N     . THR B 1 555 ? 113.820 158.688 176.489 1.00 42.76 ?  555 THR B N     1 
ATOM   10006 C  CA    . THR B 1 555 ? 112.955 159.349 175.520 1.00 39.77 ?  555 THR B CA    1 
ATOM   10007 C  C     . THR B 1 555 ? 113.336 160.816 175.354 1.00 40.86 ?  555 THR B C     1 
ATOM   10008 O  O     . THR B 1 555 ? 113.333 161.341 174.235 1.00 44.26 ?  555 THR B O     1 
ATOM   10009 C  CB    . THR B 1 555 ? 111.494 159.201 175.947 1.00 43.88 ?  555 THR B CB    1 
ATOM   10010 O  OG1   . THR B 1 555 ? 111.036 157.882 175.625 1.00 42.11 ?  555 THR B OG1   1 
ATOM   10011 C  CG2   . THR B 1 555 ? 110.615 160.219 175.247 1.00 42.31 ?  555 THR B CG2   1 
ATOM   10012 N  N     . GLU B 1 556 ? 113.677 161.493 176.453 1.00 37.54 ?  556 GLU B N     1 
ATOM   10013 C  CA    . GLU B 1 556 ? 114.112 162.883 176.362 1.00 41.22 ?  556 GLU B CA    1 
ATOM   10014 C  C     . GLU B 1 556 ? 115.436 163.004 175.616 1.00 41.20 ?  556 GLU B C     1 
ATOM   10015 O  O     . GLU B 1 556 ? 115.631 163.943 174.835 1.00 45.19 ?  556 GLU B O     1 
ATOM   10016 C  CB    . GLU B 1 556 ? 114.221 163.491 177.759 1.00 42.16 ?  556 GLU B CB    1 
ATOM   10017 C  CG    . GLU B 1 556 ? 112.882 163.713 178.449 1.00 43.79 ?  556 GLU B CG    1 
ATOM   10018 C  CD    . GLU B 1 556 ? 111.813 164.235 177.506 1.00 46.68 ?  556 GLU B CD    1 
ATOM   10019 O  OE1   . GLU B 1 556 ? 111.780 165.459 177.262 1.00 44.65 ?  556 GLU B OE1   1 
ATOM   10020 O  OE2   . GLU B 1 556 ? 110.999 163.424 177.015 1.00 46.96 -1 556 GLU B OE2   1 
ATOM   10021 N  N     . ASP B 1 557 ? 116.360 162.069 175.849 1.00 39.92 ?  557 ASP B N     1 
ATOM   10022 C  CA    . ASP B 1 557 ? 117.611 162.064 175.099 1.00 35.53 ?  557 ASP B CA    1 
ATOM   10023 C  C     . ASP B 1 557 ? 117.354 161.865 173.612 1.00 36.19 ?  557 ASP B C     1 
ATOM   10024 O  O     . ASP B 1 557 ? 118.002 162.499 172.771 1.00 39.67 ?  557 ASP B O     1 
ATOM   10025 C  CB    . ASP B 1 557 ? 118.541 160.973 175.630 1.00 35.05 ?  557 ASP B CB    1 
ATOM   10026 C  CG    . ASP B 1 557 ? 119.026 161.255 177.035 1.00 42.94 ?  557 ASP B CG    1 
ATOM   10027 O  OD1   . ASP B 1 557 ? 119.585 162.348 177.264 1.00 44.87 ?  557 ASP B OD1   1 
ATOM   10028 O  OD2   . ASP B 1 557 ? 118.852 160.382 177.910 1.00 43.75 -1 557 ASP B OD2   1 
ATOM   10029 N  N     . TRP B 1 558 ? 116.407 160.993 173.269 1.00 30.30 ?  558 TRP B N     1 
ATOM   10030 C  CA    . TRP B 1 558 ? 116.072 160.787 171.865 1.00 26.01 ?  558 TRP B CA    1 
ATOM   10031 C  C     . TRP B 1 558 ? 115.397 162.009 171.257 1.00 31.95 ?  558 TRP B C     1 
ATOM   10032 O  O     . TRP B 1 558 ? 115.615 162.308 170.081 1.00 37.89 ?  558 TRP B O     1 
ATOM   10033 C  CB    . TRP B 1 558 ? 115.190 159.551 171.717 1.00 32.42 ?  558 TRP B CB    1 
ATOM   10034 C  CG    . TRP B 1 558 ? 115.974 158.290 171.564 1.00 28.63 ?  558 TRP B CG    1 
ATOM   10035 C  CD1   . TRP B 1 558 ? 116.134 157.306 172.492 1.00 25.06 ?  558 TRP B CD1   1 
ATOM   10036 C  CD2   . TRP B 1 558 ? 116.709 157.875 170.408 1.00 29.59 ?  558 TRP B CD2   1 
ATOM   10037 N  NE1   . TRP B 1 558 ? 116.922 156.303 171.986 1.00 31.93 ?  558 TRP B NE1   1 
ATOM   10038 C  CE2   . TRP B 1 558 ? 117.285 156.627 170.707 1.00 29.94 ?  558 TRP B CE2   1 
ATOM   10039 C  CE3   . TRP B 1 558 ? 116.927 158.434 169.146 1.00 30.69 ?  558 TRP B CE3   1 
ATOM   10040 C  CZ2   . TRP B 1 558 ? 118.068 155.930 169.792 1.00 25.80 ?  558 TRP B CZ2   1 
ATOM   10041 C  CZ3   . TRP B 1 558 ? 117.705 157.742 168.241 1.00 28.24 ?  558 TRP B CZ3   1 
ATOM   10042 C  CH2   . TRP B 1 558 ? 118.265 156.504 168.567 1.00 23.67 ?  558 TRP B CH2   1 
ATOM   10043 N  N     . LYS B 1 559 ? 114.579 162.727 172.031 1.00 36.67 ?  559 LYS B N     1 
ATOM   10044 C  CA    . LYS B 1 559 ? 114.010 163.977 171.535 1.00 34.56 ?  559 LYS B CA    1 
ATOM   10045 C  C     . LYS B 1 559 ? 115.095 165.018 171.291 1.00 37.87 ?  559 LYS B C     1 
ATOM   10046 O  O     . LYS B 1 559 ? 115.056 165.748 170.293 1.00 38.90 ?  559 LYS B O     1 
ATOM   10047 C  CB    . LYS B 1 559 ? 112.971 164.509 172.519 1.00 37.71 ?  559 LYS B CB    1 
ATOM   10048 C  CG    . LYS B 1 559 ? 111.644 163.777 172.476 1.00 42.19 ?  559 LYS B CG    1 
ATOM   10049 C  CD    . LYS B 1 559 ? 110.727 164.240 173.593 1.00 38.05 ?  559 LYS B CD    1 
ATOM   10050 C  CE    . LYS B 1 559 ? 109.526 163.325 173.733 1.00 41.69 ?  559 LYS B CE    1 
ATOM   10051 N  NZ    . LYS B 1 559 ? 109.005 163.311 175.127 1.00 39.05 1  559 LYS B NZ    1 
ATOM   10052 N  N     . LYS B 1 560 ? 116.071 165.102 172.197 1.00 34.00 ?  560 LYS B N     1 
ATOM   10053 C  CA    . LYS B 1 560 ? 117.191 166.014 171.996 1.00 33.62 ?  560 LYS B CA    1 
ATOM   10054 C  C     . LYS B 1 560 ? 117.990 165.634 170.756 1.00 38.20 ?  560 LYS B C     1 
ATOM   10055 O  O     . LYS B 1 560 ? 118.412 166.507 169.989 1.00 42.72 ?  560 LYS B O     1 
ATOM   10056 C  CB    . LYS B 1 560 ? 118.087 166.024 173.234 1.00 37.36 ?  560 LYS B CB    1 
ATOM   10057 C  CG    . LYS B 1 560 ? 117.646 167.001 174.308 1.00 37.70 ?  560 LYS B CG    1 
ATOM   10058 C  CD    . LYS B 1 560 ? 118.421 166.790 175.597 1.00 42.97 ?  560 LYS B CD    1 
ATOM   10059 C  CE    . LYS B 1 560 ? 117.512 166.896 176.810 1.00 39.49 ?  560 LYS B CE    1 
ATOM   10060 N  NZ    . LYS B 1 560 ? 117.649 165.717 177.710 1.00 44.10 1  560 LYS B NZ    1 
ATOM   10061 N  N     . LEU B 1 561 ? 118.206 164.335 170.542 1.00 36.05 ?  561 LEU B N     1 
ATOM   10062 C  CA    . LEU B 1 561 ? 118.899 163.885 169.339 1.00 30.62 ?  561 LEU B CA    1 
ATOM   10063 C  C     . LEU B 1 561 ? 118.098 164.205 168.084 1.00 34.86 ?  561 LEU B C     1 
ATOM   10064 O  O     . LEU B 1 561 ? 118.670 164.569 167.052 1.00 39.07 ?  561 LEU B O     1 
ATOM   10065 C  CB    . LEU B 1 561 ? 119.185 162.386 169.423 1.00 30.75 ?  561 LEU B CB    1 
ATOM   10066 C  CG    . LEU B 1 561 ? 119.989 161.818 168.253 1.00 32.12 ?  561 LEU B CG    1 
ATOM   10067 C  CD1   . LEU B 1 561 ? 121.290 162.579 168.093 1.00 28.52 ?  561 LEU B CD1   1 
ATOM   10068 C  CD2   . LEU B 1 561 ? 120.250 160.338 168.445 1.00 29.41 ?  561 LEU B CD2   1 
ATOM   10069 N  N     . LYS B 1 562 ? 116.774 164.057 168.147 1.00 30.80 ?  562 LYS B N     1 
ATOM   10070 C  CA    . LYS B 1 562 ? 115.927 164.402 167.011 1.00 32.43 ?  562 LYS B CA    1 
ATOM   10071 C  C     . LYS B 1 562 ? 116.030 165.884 166.679 1.00 37.34 ?  562 LYS B C     1 
ATOM   10072 O  O     . LYS B 1 562 ? 116.145 166.262 165.507 1.00 41.07 ?  562 LYS B O     1 
ATOM   10073 C  CB    . LYS B 1 562 ? 114.479 164.017 167.315 1.00 30.73 ?  562 LYS B CB    1 
ATOM   10074 C  CG    . LYS B 1 562 ? 113.470 164.459 166.276 1.00 31.43 ?  562 LYS B CG    1 
ATOM   10075 C  CD    . LYS B 1 562 ? 112.061 164.141 166.740 1.00 29.50 ?  562 LYS B CD    1 
ATOM   10076 C  CE    . LYS B 1 562 ? 111.040 164.391 165.649 1.00 35.36 ?  562 LYS B CE    1 
ATOM   10077 N  NZ    . LYS B 1 562 ? 109.763 163.683 165.932 1.00 39.56 1  562 LYS B NZ    1 
ATOM   10078 N  N     . ALA B 1 563 ? 116.005 166.739 167.704 1.00 33.87 ?  563 ALA B N     1 
ATOM   10079 C  CA    . ALA B 1 563 ? 116.173 168.171 167.476 1.00 30.54 ?  563 ALA B CA    1 
ATOM   10080 C  C     . ALA B 1 563 ? 117.551 168.480 166.903 1.00 33.60 ?  563 ALA B C     1 
ATOM   10081 O  O     . ALA B 1 563 ? 117.685 169.312 165.999 1.00 40.23 ?  563 ALA B O     1 
ATOM   10082 C  CB    . ALA B 1 563 ? 115.947 168.939 168.777 1.00 34.80 ?  563 ALA B CB    1 
ATOM   10083 N  N     . PHE B 1 564 ? 118.588 167.813 167.417 1.00 36.35 ?  564 PHE B N     1 
ATOM   10084 C  CA    . PHE B 1 564 ? 119.942 168.031 166.920 1.00 31.55 ?  564 PHE B CA    1 
ATOM   10085 C  C     . PHE B 1 564 ? 120.069 167.620 165.458 1.00 36.66 ?  564 PHE B C     1 
ATOM   10086 O  O     . PHE B 1 564 ? 120.721 168.310 164.666 1.00 41.78 ?  564 PHE B O     1 
ATOM   10087 C  CB    . PHE B 1 564 ? 120.937 167.259 167.787 1.00 32.48 ?  564 PHE B CB    1 
ATOM   10088 C  CG    . PHE B 1 564 ? 122.367 167.663 167.582 1.00 35.64 ?  564 PHE B CG    1 
ATOM   10089 C  CD1   . PHE B 1 564 ? 122.860 168.827 168.146 1.00 35.29 ?  564 PHE B CD1   1 
ATOM   10090 C  CD2   . PHE B 1 564 ? 123.221 166.874 166.833 1.00 39.70 ?  564 PHE B CD2   1 
ATOM   10091 C  CE1   . PHE B 1 564 ? 124.176 169.196 167.962 1.00 41.01 ?  564 PHE B CE1   1 
ATOM   10092 C  CE2   . PHE B 1 564 ? 124.537 167.239 166.645 1.00 38.51 ?  564 PHE B CE2   1 
ATOM   10093 C  CZ    . PHE B 1 564 ? 125.017 168.403 167.209 1.00 38.19 ?  564 PHE B CZ    1 
ATOM   10094 N  N     . VAL B 1 565 ? 119.453 166.499 165.084 1.00 32.89 ?  565 VAL B N     1 
ATOM   10095 C  CA    . VAL B 1 565 ? 119.516 166.033 163.703 1.00 29.38 ?  565 VAL B CA    1 
ATOM   10096 C  C     . VAL B 1 565 ? 118.724 166.958 162.790 1.00 35.25 ?  565 VAL B C     1 
ATOM   10097 O  O     . VAL B 1 565 ? 119.139 167.244 161.661 1.00 39.02 ?  565 VAL B O     1 
ATOM   10098 C  CB    . VAL B 1 565 ? 119.025 164.576 163.614 1.00 29.93 ?  565 VAL B CB    1 
ATOM   10099 C  CG1   . VAL B 1 565 ? 118.671 164.208 162.183 1.00 32.07 ?  565 VAL B CG1   1 
ATOM   10100 C  CG2   . VAL B 1 565 ? 120.081 163.637 164.159 1.00 32.11 ?  565 VAL B CG2   1 
ATOM   10101 N  N     . ALA B 1 566 ? 117.576 167.449 163.263 1.00 36.92 ?  566 ALA B N     1 
ATOM   10102 C  CA    . ALA B 1 566 ? 116.809 168.405 162.472 1.00 34.67 ?  566 ALA B CA    1 
ATOM   10103 C  C     . ALA B 1 566 ? 117.592 169.693 162.257 1.00 37.50 ?  566 ALA B C     1 
ATOM   10104 O  O     . ALA B 1 566 ? 117.545 170.285 161.173 1.00 43.33 ?  566 ALA B O     1 
ATOM   10105 C  CB    . ALA B 1 566 ? 115.472 168.697 163.152 1.00 34.64 ?  566 ALA B CB    1 
ATOM   10106 N  N     . GLU B 1 567 ? 118.317 170.144 163.281 1.00 38.02 ?  567 GLU B N     1 
ATOM   10107 C  CA    . GLU B 1 567 ? 119.065 171.390 163.168 1.00 37.40 ?  567 GLU B CA    1 
ATOM   10108 C  C     . GLU B 1 567 ? 120.290 171.232 162.274 1.00 42.54 ?  567 GLU B C     1 
ATOM   10109 O  O     . GLU B 1 567 ? 120.549 172.074 161.406 1.00 50.47 ?  567 GLU B O     1 
ATOM   10110 C  CB    . GLU B 1 567 ? 119.479 171.874 164.557 1.00 39.50 ?  567 GLU B CB    1 
ATOM   10111 C  CG    . GLU B 1 567 ? 120.182 173.216 164.562 1.00 42.29 ?  567 GLU B CG    1 
ATOM   10112 C  CD    . GLU B 1 567 ? 120.742 173.568 165.926 1.00 49.53 ?  567 GLU B CD    1 
ATOM   10113 O  OE1   . GLU B 1 567 ? 120.318 172.945 166.921 1.00 50.64 ?  567 GLU B OE1   1 
ATOM   10114 O  OE2   . GLU B 1 567 ? 121.601 174.470 166.003 1.00 46.30 -1 567 GLU B OE2   1 
ATOM   10115 N  N     . HIS B 1 568 ? 121.056 170.157 162.464 1.00 44.69 ?  568 HIS B N     1 
ATOM   10116 C  CA    . HIS B 1 568 ? 122.370 170.034 161.850 1.00 40.43 ?  568 HIS B CA    1 
ATOM   10117 C  C     . HIS B 1 568 ? 122.443 168.992 160.744 1.00 35.70 ?  568 HIS B C     1 
ATOM   10118 O  O     . HIS B 1 568 ? 123.446 168.952 160.024 1.00 44.65 ?  568 HIS B O     1 
ATOM   10119 C  CB    . HIS B 1 568 ? 123.421 169.702 162.917 1.00 39.32 ?  568 HIS B CB    1 
ATOM   10120 C  CG    . HIS B 1 568 ? 123.660 170.811 163.892 1.00 39.80 ?  568 HIS B CG    1 
ATOM   10121 N  ND1   . HIS B 1 568 ? 123.286 170.731 165.216 1.00 41.70 ?  568 HIS B ND1   1 
ATOM   10122 C  CD2   . HIS B 1 568 ? 124.220 172.033 163.733 1.00 40.68 ?  568 HIS B CD2   1 
ATOM   10123 C  CE1   . HIS B 1 568 ? 123.615 171.851 165.833 1.00 41.70 ?  568 HIS B CE1   1 
ATOM   10124 N  NE2   . HIS B 1 568 ? 124.184 172.657 164.956 1.00 46.63 ?  568 HIS B NE2   1 
ATOM   10125 N  N     . GLY B 1 569 ? 121.430 168.160 160.588 1.00 30.82 ?  569 GLY B N     1 
ATOM   10126 C  CA    . GLY B 1 569 ? 121.464 167.151 159.555 1.00 29.68 ?  569 GLY B CA    1 
ATOM   10127 C  C     . GLY B 1 569 ? 122.179 165.892 159.991 1.00 30.05 ?  569 GLY B C     1 
ATOM   10128 O  O     . GLY B 1 569 ? 122.554 165.702 161.151 1.00 38.28 ?  569 GLY B O     1 
ATOM   10129 N  N     . MET B 1 570 ? 122.364 165.007 159.019 1.00 26.75 ?  570 MET B N     1 
ATOM   10130 C  CA    . MET B 1 570 ? 122.935 163.690 159.253 1.00 22.89 ?  570 MET B CA    1 
ATOM   10131 C  C     . MET B 1 570 ? 123.967 163.420 158.170 1.00 24.69 ?  570 MET B C     1 
ATOM   10132 O  O     . MET B 1 570 ? 123.673 163.580 156.982 1.00 30.73 ?  570 MET B O     1 
ATOM   10133 C  CB    . MET B 1 570 ? 121.828 162.632 159.250 1.00 31.01 ?  570 MET B CB    1 
ATOM   10134 C  CG    . MET B 1 570 ? 121.338 162.248 160.637 1.00 24.56 ?  570 MET B CG    1 
ATOM   10135 S  SD    . MET B 1 570 ? 120.903 160.513 160.800 1.00 46.73 ?  570 MET B SD    1 
ATOM   10136 C  CE    . MET B 1 570 ? 122.506 159.756 160.877 1.00 26.89 ?  570 MET B CE    1 
ATOM   10137 N  N     . TYR B 1 571 ? 125.177 163.030 158.576 1.00 21.99 ?  571 TYR B N     1 
ATOM   10138 C  CA    . TYR B 1 571 ? 126.267 162.902 157.615 1.00 13.75 ?  571 TYR B CA    1 
ATOM   10139 C  C     . TYR B 1 571 ? 126.208 161.602 156.824 1.00 22.97 ?  571 TYR B C     1 
ATOM   10140 O  O     . TYR B 1 571 ? 126.587 161.583 155.650 1.00 21.03 ?  571 TYR B O     1 
ATOM   10141 C  CB    . TYR B 1 571 ? 127.617 163.009 158.323 1.00 18.76 ?  571 TYR B CB    1 
ATOM   10142 C  CG    . TYR B 1 571 ? 128.789 163.108 157.374 1.00 21.18 ?  571 TYR B CG    1 
ATOM   10143 C  CD1   . TYR B 1 571 ? 129.077 164.297 156.717 1.00 23.79 ?  571 TYR B CD1   1 
ATOM   10144 C  CD2   . TYR B 1 571 ? 129.605 162.013 157.130 1.00 21.32 ?  571 TYR B CD2   1 
ATOM   10145 C  CE1   . TYR B 1 571 ? 130.144 164.390 155.848 1.00 22.28 ?  571 TYR B CE1   1 
ATOM   10146 C  CE2   . TYR B 1 571 ? 130.672 162.097 156.264 1.00 23.34 ?  571 TYR B CE2   1 
ATOM   10147 C  CZ    . TYR B 1 571 ? 130.938 163.288 155.627 1.00 28.65 ?  571 TYR B CZ    1 
ATOM   10148 O  OH    . TYR B 1 571 ? 132.004 163.374 154.762 1.00 30.16 ?  571 TYR B OH    1 
ATOM   10149 N  N     . HIS B 1 572 ? 125.744 160.518 157.437 1.00 25.77 ?  572 HIS B N     1 
ATOM   10150 C  CA    . HIS B 1 572 ? 125.713 159.207 156.802 1.00 11.39 ?  572 HIS B CA    1 
ATOM   10151 C  C     . HIS B 1 572 ? 124.277 158.814 156.499 1.00 16.85 ?  572 HIS B C     1 
ATOM   10152 O  O     . HIS B 1 572 ? 123.419 158.846 157.388 1.00 31.90 ?  572 HIS B O     1 
ATOM   10153 C  CB    . HIS B 1 572 ? 126.368 158.145 157.690 1.00 12.19 ?  572 HIS B CB    1 
ATOM   10154 C  CG    . HIS B 1 572 ? 127.691 158.554 158.254 1.00 9.40  ?  572 HIS B CG    1 
ATOM   10155 N  ND1   . HIS B 1 572 ? 127.819 159.186 159.471 1.00 15.89 ?  572 HIS B ND1   1 
ATOM   10156 C  CD2   . HIS B 1 572 ? 128.946 158.415 157.770 1.00 13.40 ?  572 HIS B CD2   1 
ATOM   10157 C  CE1   . HIS B 1 572 ? 129.095 159.422 159.712 1.00 14.22 ?  572 HIS B CE1   1 
ATOM   10158 N  NE2   . HIS B 1 572 ? 129.800 158.965 158.694 1.00 24.57 ?  572 HIS B NE2   1 
ATOM   10159 N  N     . SER B 1 573 ? 124.019 158.449 155.242 1.00 10.81 ?  573 SER B N     1 
ATOM   10160 C  CA    . SER B 1 573 ? 122.712 157.907 154.889 1.00 8.56  ?  573 SER B CA    1 
ATOM   10161 C  C     . SER B 1 573 ? 122.458 156.597 155.616 1.00 17.12 ?  573 SER B C     1 
ATOM   10162 O  O     . SER B 1 573 ? 121.335 156.321 156.050 1.00 29.36 ?  573 SER B O     1 
ATOM   10163 C  CB    . SER B 1 573 ? 122.615 157.706 153.379 1.00 13.78 ?  573 SER B CB    1 
ATOM   10164 O  OG    . SER B 1 573 ? 123.814 157.158 152.868 1.00 25.31 ?  573 SER B OG    1 
ATOM   10165 N  N     . TYR B 1 574 ? 123.493 155.775 155.751 1.00 14.91 ?  574 TYR B N     1 
ATOM   10166 C  CA    . TYR B 1 574 ? 123.414 154.493 156.425 1.00 0.00  ?  574 TYR B CA    1 
ATOM   10167 C  C     . TYR B 1 574 ? 124.612 154.357 157.347 1.00 10.00 ?  574 TYR B C     1 
ATOM   10168 O  O     . TYR B 1 574 ? 125.722 154.767 156.998 1.00 19.34 ?  574 TYR B O     1 
ATOM   10169 C  CB    . TYR B 1 574 ? 123.375 153.349 155.412 1.00 10.33 ?  574 TYR B CB    1 
ATOM   10170 C  CG    . TYR B 1 574 ? 122.302 153.524 154.365 1.00 0.00  ?  574 TYR B CG    1 
ATOM   10171 C  CD1   . TYR B 1 574 ? 121.021 153.035 154.570 1.00 3.61  ?  574 TYR B CD1   1 
ATOM   10172 C  CD2   . TYR B 1 574 ? 122.565 154.192 153.177 1.00 3.57  ?  574 TYR B CD2   1 
ATOM   10173 C  CE1   . TYR B 1 574 ? 120.037 153.199 153.622 1.00 5.96  ?  574 TYR B CE1   1 
ATOM   10174 C  CE2   . TYR B 1 574 ? 121.585 154.362 152.223 1.00 10.55 ?  574 TYR B CE2   1 
ATOM   10175 C  CZ    . TYR B 1 574 ? 120.324 153.861 152.450 1.00 2.73  ?  574 TYR B CZ    1 
ATOM   10176 O  OH    . TYR B 1 574 ? 119.344 154.022 151.504 1.00 15.62 ?  574 TYR B OH    1 
ATOM   10177 N  N     . ARG B 1 575 ? 124.384 153.791 158.525 1.00 12.14 ?  575 ARG B N     1 
ATOM   10178 C  CA    . ARG B 1 575 ? 125.413 153.727 159.554 1.00 0.00  ?  575 ARG B CA    1 
ATOM   10179 C  C     . ARG B 1 575 ? 125.701 152.324 160.051 1.00 11.16 ?  575 ARG B C     1 
ATOM   10180 O  O     . ARG B 1 575 ? 126.864 151.980 160.267 1.00 23.55 ?  575 ARG B O     1 
ATOM   10181 C  CB    . ARG B 1 575 ? 125.009 154.593 160.748 1.00 13.58 ?  575 ARG B CB    1 
ATOM   10182 C  CG    . ARG B 1 575 ? 124.898 156.062 160.444 1.00 8.83  ?  575 ARG B CG    1 
ATOM   10183 C  CD    . ARG B 1 575 ? 124.059 156.741 161.494 1.00 11.19 ?  575 ARG B CD    1 
ATOM   10184 N  NE    . ARG B 1 575 ? 122.648 156.406 161.351 1.00 16.96 ?  575 ARG B NE    1 
ATOM   10185 C  CZ    . ARG B 1 575 ? 121.991 155.566 162.136 1.00 11.69 ?  575 ARG B CZ    1 
ATOM   10186 N  NH1   . ARG B 1 575 ? 122.592 154.943 163.135 1.00 11.22 1  575 ARG B NH1   1 
ATOM   10187 N  NH2   . ARG B 1 575 ? 120.700 155.346 161.916 1.00 11.31 ?  575 ARG B NH2   1 
ATOM   10188 N  N     . LEU B 1 576 ? 124.675 151.500 160.239 1.00 21.07 ?  576 LEU B N     1 
ATOM   10189 C  CA    . LEU B 1 576 ? 124.807 150.238 160.950 1.00 12.04 ?  576 LEU B CA    1 
ATOM   10190 C  C     . LEU B 1 576 ? 124.404 149.086 160.045 1.00 4.46  ?  576 LEU B C     1 
ATOM   10191 O  O     . LEU B 1 576 ? 123.315 149.101 159.464 1.00 20.33 ?  576 LEU B O     1 
ATOM   10192 C  CB    . LEU B 1 576 ? 123.946 150.239 162.215 1.00 7.86  ?  576 LEU B CB    1 
ATOM   10193 C  CG    . LEU B 1 576 ? 124.088 151.451 163.135 1.00 7.05  ?  576 LEU B CG    1 
ATOM   10194 C  CD1   . LEU B 1 576 ? 123.069 151.391 164.256 1.00 12.34 ?  576 LEU B CD1   1 
ATOM   10195 C  CD2   . LEU B 1 576 ? 125.492 151.534 163.696 1.00 11.05 ?  576 LEU B CD2   1 
ATOM   10196 N  N     . CYS B 1 577 ? 125.286 148.100 159.923 1.00 10.65 ?  577 CYS B N     1 
ATOM   10197 C  CA    . CYS B 1 577 ? 124.966 146.838 159.273 1.00 7.20  ?  577 CYS B CA    1 
ATOM   10198 C  C     . CYS B 1 577 ? 125.816 145.761 159.925 1.00 21.29 ?  577 CYS B C     1 
ATOM   10199 O  O     . CYS B 1 577 ? 127.019 145.952 160.117 1.00 26.91 ?  577 CYS B O     1 
ATOM   10200 C  CB    . CYS B 1 577 ? 125.208 146.896 157.758 1.00 4.23  ?  577 CYS B CB    1 
ATOM   10201 S  SG    . CYS B 1 577 ? 126.922 146.748 157.201 1.00 34.79 ?  577 CYS B SG    1 
ATOM   10202 N  N     . ILE B 1 578 ? 125.191 144.645 160.279 1.00 15.00 ?  578 ILE B N     1 
ATOM   10203 C  CA    . ILE B 1 578 ? 125.855 143.578 161.016 1.00 12.69 ?  578 ILE B CA    1 
ATOM   10204 C  C     . ILE B 1 578 ? 126.299 142.530 160.002 1.00 5.09  ?  578 ILE B C     1 
ATOM   10205 O  O     . ILE B 1 578 ? 125.519 141.667 159.595 1.00 20.00 ?  578 ILE B O     1 
ATOM   10206 C  CB    . ILE B 1 578 ? 124.952 142.990 162.102 1.00 10.95 ?  578 ILE B CB    1 
ATOM   10207 C  CG1   . ILE B 1 578 ? 124.430 144.108 163.006 1.00 2.62  ?  578 ILE B CG1   1 
ATOM   10208 C  CG2   . ILE B 1 578 ? 125.711 141.978 162.931 1.00 8.83  ?  578 ILE B CG2   1 
ATOM   10209 C  CD1   . ILE B 1 578 ? 123.705 143.612 164.227 1.00 9.60  ?  578 ILE B CD1   1 
ATOM   10210 N  N     . ALA B 1 579 ? 127.560 142.615 159.591 1.00 14.77 ?  579 ALA B N     1 
ATOM   10211 C  CA    . ALA B 1 579 ? 128.178 141.673 158.674 1.00 4.76  ?  579 ALA B CA    1 
ATOM   10212 C  C     . ALA B 1 579 ? 128.529 140.373 159.394 1.00 18.65 ?  579 ALA B C     1 
ATOM   10213 O  O     . ALA B 1 579 ? 128.567 140.326 160.624 1.00 31.68 ?  579 ALA B O     1 
ATOM   10214 C  CB    . ALA B 1 579 ? 129.425 142.297 158.059 1.00 9.76  ?  579 ALA B CB    1 
ATOM   10215 N  N     . PRO B 1 580 ? 128.769 139.289 158.647 1.00 25.93 ?  580 PRO B N     1 
ATOM   10216 C  CA    . PRO B 1 580 ? 129.110 138.013 159.304 1.00 23.57 ?  580 PRO B CA    1 
ATOM   10217 C  C     . PRO B 1 580 ? 130.374 138.057 160.153 1.00 31.60 ?  580 PRO B C     1 
ATOM   10218 O  O     . PRO B 1 580 ? 130.444 137.334 161.155 1.00 37.76 ?  580 PRO B O     1 
ATOM   10219 C  CB    . PRO B 1 580 ? 129.256 137.036 158.126 1.00 23.45 ?  580 PRO B CB    1 
ATOM   10220 C  CG    . PRO B 1 580 ? 129.315 137.878 156.900 1.00 23.60 ?  580 PRO B CG    1 
ATOM   10221 C  CD    . PRO B 1 580 ? 128.548 139.113 157.202 1.00 20.84 ?  580 PRO B CD    1 
ATOM   10222 N  N     . THR B 1 581 ? 131.366 138.873 159.793 1.00 24.16 ?  581 THR B N     1 
ATOM   10223 C  CA    . THR B 1 581 ? 132.633 138.979 160.529 1.00 33.88 ?  581 THR B CA    1 
ATOM   10224 C  C     . THR B 1 581 ? 133.294 137.607 160.684 1.00 32.21 ?  581 THR B C     1 
ATOM   10225 O  O     . THR B 1 581 ? 133.459 137.077 161.782 1.00 34.51 ?  581 THR B O     1 
ATOM   10226 C  CB    . THR B 1 581 ? 132.447 139.639 161.901 1.00 28.70 ?  581 THR B CB    1 
ATOM   10227 O  OG1   . THR B 1 581 ? 132.022 138.658 162.854 1.00 24.16 ?  581 THR B OG1   1 
ATOM   10228 C  CG2   . THR B 1 581 ? 131.433 140.763 161.834 1.00 31.20 ?  581 THR B CG2   1 
ATOM   10229 N  N     . GLY B 1 582 ? 133.667 137.046 159.538 1.00 31.94 ?  582 GLY B N     1 
ATOM   10230 C  CA    . GLY B 1 582 ? 134.149 135.681 159.486 1.00 34.72 ?  582 GLY B CA    1 
ATOM   10231 C  C     . GLY B 1 582 ? 135.463 135.414 160.191 1.00 37.48 ?  582 GLY B C     1 
ATOM   10232 O  O     . GLY B 1 582 ? 135.493 134.690 161.191 1.00 41.71 ?  582 GLY B O     1 
ATOM   10233 N  N     . SER B 1 583 ? 136.557 135.988 159.692 1.00 37.76 ?  583 SER B N     1 
ATOM   10234 C  CA    . SER B 1 583 ? 137.883 135.637 160.187 1.00 42.54 ?  583 SER B CA    1 
ATOM   10235 C  C     . SER B 1 583 ? 138.390 136.573 161.275 1.00 39.80 ?  583 SER B C     1 
ATOM   10236 O  O     . SER B 1 583 ? 139.234 136.164 162.081 1.00 39.77 ?  583 SER B O     1 
ATOM   10237 C  CB    . SER B 1 583 ? 138.888 135.613 159.033 1.00 47.40 ?  583 SER B CB    1 
ATOM   10238 O  OG    . SER B 1 583 ? 138.777 134.412 158.287 1.00 49.21 ?  583 SER B OG    1 
ATOM   10239 N  N     . ILE B 1 584 ? 137.907 137.816 161.320 1.00 33.05 ?  584 ILE B N     1 
ATOM   10240 C  CA    . ILE B 1 584 ? 138.318 138.740 162.371 1.00 28.91 ?  584 ILE B CA    1 
ATOM   10241 C  C     . ILE B 1 584 ? 137.773 138.358 163.736 1.00 31.88 ?  584 ILE B C     1 
ATOM   10242 O  O     . ILE B 1 584 ? 138.232 138.899 164.747 1.00 36.84 ?  584 ILE B O     1 
ATOM   10243 C  CB    . ILE B 1 584 ? 137.886 140.184 162.038 1.00 36.81 ?  584 ILE B CB    1 
ATOM   10244 C  CG1   . ILE B 1 584 ? 136.391 140.236 161.715 1.00 34.43 ?  584 ILE B CG1   1 
ATOM   10245 C  CG2   . ILE B 1 584 ? 138.723 140.746 160.902 1.00 32.57 ?  584 ILE B CG2   1 
ATOM   10246 C  CD1   . ILE B 1 584 ? 135.838 141.639 161.604 1.00 33.31 ?  584 ILE B CD1   1 
ATOM   10247 N  N     . SER B 1 585 ? 136.800 137.446 163.794 1.00 31.76 ?  585 SER B N     1 
ATOM   10248 C  CA    . SER B 1 585 ? 136.263 137.020 165.080 1.00 29.12 ?  585 SER B CA    1 
ATOM   10249 C  C     . SER B 1 585 ? 137.277 136.204 165.869 1.00 28.92 ?  585 SER B C     1 
ATOM   10250 O  O     . SER B 1 585 ? 137.322 136.300 167.099 1.00 29.13 ?  585 SER B O     1 
ATOM   10251 C  CB    . SER B 1 585 ? 134.978 136.221 164.874 1.00 32.20 ?  585 SER B CB    1 
ATOM   10252 O  OG    . SER B 1 585 ? 135.196 135.111 164.022 1.00 36.22 ?  585 SER B OG    1 
ATOM   10253 N  N     . TYR B 1 586 ? 138.089 135.392 165.186 1.00 35.47 ?  586 TYR B N     1 
ATOM   10254 C  CA    . TYR B 1 586 ? 139.129 134.639 165.878 1.00 36.44 ?  586 TYR B CA    1 
ATOM   10255 C  C     . TYR B 1 586 ? 140.159 135.570 166.499 1.00 34.72 ?  586 TYR B C     1 
ATOM   10256 O  O     . TYR B 1 586 ? 140.555 135.389 167.655 1.00 41.06 ?  586 TYR B O     1 
ATOM   10257 C  CB    . TYR B 1 586 ? 139.814 133.670 164.915 1.00 32.67 ?  586 TYR B CB    1 
ATOM   10258 C  CG    . TYR B 1 586 ? 138.900 132.643 164.296 1.00 33.53 ?  586 TYR B CG    1 
ATOM   10259 C  CD1   . TYR B 1 586 ? 138.305 132.868 163.064 1.00 36.90 ?  586 TYR B CD1   1 
ATOM   10260 C  CD2   . TYR B 1 586 ? 138.635 131.445 164.941 1.00 35.45 ?  586 TYR B CD2   1 
ATOM   10261 C  CE1   . TYR B 1 586 ? 137.471 131.931 162.491 1.00 39.70 ?  586 TYR B CE1   1 
ATOM   10262 C  CE2   . TYR B 1 586 ? 137.802 130.500 164.377 1.00 37.85 ?  586 TYR B CE2   1 
ATOM   10263 C  CZ    . TYR B 1 586 ? 137.222 130.748 163.153 1.00 39.59 ?  586 TYR B CZ    1 
ATOM   10264 O  OH    . TYR B 1 586 ? 136.392 129.810 162.587 1.00 44.24 ?  586 TYR B OH    1 
ATOM   10265 N  N     . VAL B 1 587 ? 140.598 136.580 165.743 1.00 29.79 ?  587 VAL B N     1 
ATOM   10266 C  CA    . VAL B 1 587 ? 141.610 137.510 166.236 1.00 24.81 ?  587 VAL B CA    1 
ATOM   10267 C  C     . VAL B 1 587 ? 141.096 138.257 167.459 1.00 30.49 ?  587 VAL B C     1 
ATOM   10268 O  O     . VAL B 1 587 ? 141.844 138.512 168.411 1.00 39.87 ?  587 VAL B O     1 
ATOM   10269 C  CB    . VAL B 1 587 ? 142.026 138.479 165.114 1.00 31.15 ?  587 VAL B CB    1 
ATOM   10270 C  CG1   . VAL B 1 587 ? 143.022 139.499 165.630 1.00 34.30 ?  587 VAL B CG1   1 
ATOM   10271 C  CG2   . VAL B 1 587 ? 142.603 137.709 163.940 1.00 31.54 ?  587 VAL B CG2   1 
ATOM   10272 N  N     . GLN B 1 588 ? 139.815 138.611 167.458 1.00 34.77 ?  588 GLN B N     1 
ATOM   10273 C  CA    . GLN B 1 588 ? 139.214 139.341 168.563 1.00 29.40 ?  588 GLN B CA    1 
ATOM   10274 C  C     . GLN B 1 588 ? 138.768 138.436 169.701 1.00 34.28 ?  588 GLN B C     1 
ATOM   10275 O  O     . GLN B 1 588 ? 138.272 138.948 170.710 1.00 36.74 ?  588 GLN B O     1 
ATOM   10276 C  CB    . GLN B 1 588 ? 138.022 140.157 168.062 1.00 22.63 ?  588 GLN B CB    1 
ATOM   10277 C  CG    . GLN B 1 588 ? 138.410 141.388 167.272 1.00 24.46 ?  588 GLN B CG    1 
ATOM   10278 C  CD    . GLN B 1 588 ? 138.480 142.627 168.136 1.00 29.18 ?  588 GLN B CD    1 
ATOM   10279 O  OE1   . GLN B 1 588 ? 137.643 142.832 169.013 1.00 29.62 ?  588 GLN B OE1   1 
ATOM   10280 N  NE2   . GLN B 1 588 ? 139.481 143.462 167.894 1.00 33.47 ?  588 GLN B NE2   1 
ATOM   10281 N  N     . SER B 1 589 ? 138.940 137.122 169.567 1.00 34.31 ?  589 SER B N     1 
ATOM   10282 C  CA    . SER B 1 589 ? 138.445 136.148 170.537 1.00 28.15 ?  589 SER B CA    1 
ATOM   10283 C  C     . SER B 1 589 ? 136.962 136.388 170.808 1.00 31.62 ?  589 SER B C     1 
ATOM   10284 O  O     . SER B 1 589 ? 136.530 136.634 171.935 1.00 35.30 ?  589 SER B O     1 
ATOM   10285 C  CB    . SER B 1 589 ? 139.265 136.191 171.828 1.00 36.32 ?  589 SER B CB    1 
ATOM   10286 O  OG    . SER B 1 589 ? 139.156 134.975 172.544 1.00 45.26 ?  589 SER B OG    1 
ATOM   10287 N  N     . SER B 1 590 ? 136.183 136.325 169.733 1.00 30.54 ?  590 SER B N     1 
ATOM   10288 C  CA    . SER B 1 590 ? 134.778 136.688 169.773 1.00 23.07 ?  590 SER B CA    1 
ATOM   10289 C  C     . SER B 1 590 ? 133.969 135.700 168.950 1.00 28.21 ?  590 SER B C     1 
ATOM   10290 O  O     . SER B 1 590 ? 134.483 135.075 168.019 1.00 36.37 ?  590 SER B O     1 
ATOM   10291 C  CB    . SER B 1 590 ? 134.560 138.109 169.240 1.00 26.65 ?  590 SER B CB    1 
ATOM   10292 O  OG    . SER B 1 590 ? 134.376 138.104 167.839 1.00 36.42 ?  590 SER B OG    1 
ATOM   10293 N  N     . THR B 1 591 ? 132.698 135.555 169.311 1.00 30.26 ?  591 THR B N     1 
ATOM   10294 C  CA    . THR B 1 591 ? 131.771 134.784 168.497 1.00 27.61 ?  591 THR B CA    1 
ATOM   10295 C  C     . THR B 1 591 ? 131.357 135.605 167.283 1.00 30.48 ?  591 THR B C     1 
ATOM   10296 O  O     . THR B 1 591 ? 131.241 136.832 167.355 1.00 25.23 ?  591 THR B O     1 
ATOM   10297 C  CB    . THR B 1 591 ? 130.544 134.373 169.310 1.00 28.23 ?  591 THR B CB    1 
ATOM   10298 O  OG1   . THR B 1 591 ? 129.747 135.526 169.601 1.00 36.89 ?  591 THR B OG1   1 
ATOM   10299 C  CG2   . THR B 1 591 ? 130.974 133.721 170.612 1.00 26.83 ?  591 THR B CG2   1 
ATOM   10300 N  N     . ALA B 1 592 ? 131.145 134.922 166.162 1.00 26.62 ?  592 ALA B N     1 
ATOM   10301 C  CA    . ALA B 1 592 ? 130.936 135.610 164.895 1.00 25.14 ?  592 ALA B CA    1 
ATOM   10302 C  C     . ALA B 1 592 ? 129.610 136.357 164.892 1.00 24.71 ?  592 ALA B C     1 
ATOM   10303 O  O     . ALA B 1 592 ? 128.544 135.756 165.060 1.00 32.62 ?  592 ALA B O     1 
ATOM   10304 C  CB    . ALA B 1 592 ? 130.980 134.612 163.741 1.00 31.49 ?  592 ALA B CB    1 
ATOM   10305 N  N     . SER B 1 593 ? 129.685 137.670 164.699 1.00 27.77 ?  593 SER B N     1 
ATOM   10306 C  CA    . SER B 1 593 ? 128.518 138.536 164.485 1.00 16.57 ?  593 SER B CA    1 
ATOM   10307 C  C     . SER B 1 593 ? 127.576 138.416 165.684 1.00 14.42 ?  593 SER B C     1 
ATOM   10308 O  O     . SER B 1 593 ? 128.010 138.146 166.811 1.00 29.93 ?  593 SER B O     1 
ATOM   10309 C  CB    . SER B 1 593 ? 127.888 138.195 163.149 1.00 28.74 ?  593 SER B CB    1 
ATOM   10310 O  OG    . SER B 1 593 ? 126.767 139.012 162.887 1.00 24.93 ?  593 SER B OG    1 
ATOM   10311 N  N     . VAL B 1 594 ? 126.279 138.617 165.452 1.00 20.91 ?  594 VAL B N     1 
ATOM   10312 C  CA    . VAL B 1 594 ? 125.266 138.421 166.479 1.00 17.98 ?  594 VAL B CA    1 
ATOM   10313 C  C     . VAL B 1 594 ? 124.674 137.018 166.423 1.00 15.70 ?  594 VAL B C     1 
ATOM   10314 O  O     . VAL B 1 594 ? 123.744 136.710 167.172 1.00 25.92 ?  594 VAL B O     1 
ATOM   10315 C  CB    . VAL B 1 594 ? 124.161 139.485 166.376 1.00 23.80 ?  594 VAL B CB    1 
ATOM   10316 C  CG1   . VAL B 1 594 ? 124.692 140.841 166.807 1.00 14.10 ?  594 VAL B CG1   1 
ATOM   10317 C  CG2   . VAL B 1 594 ? 123.612 139.546 164.963 1.00 22.03 ?  594 VAL B CG2   1 
ATOM   10318 N  N     . MET B 1 595 ? 125.197 136.162 165.551 1.00 25.63 ?  595 MET B N     1 
ATOM   10319 C  CA    . MET B 1 595 ? 124.704 134.802 165.441 1.00 19.42 ?  595 MET B CA    1 
ATOM   10320 C  C     . MET B 1 595 ? 125.133 133.976 166.651 1.00 24.87 ?  595 MET B C     1 
ATOM   10321 O  O     . MET B 1 595 ? 126.166 134.250 167.267 1.00 32.63 ?  595 MET B O     1 
ATOM   10322 C  CB    . MET B 1 595 ? 125.231 134.146 164.166 1.00 22.58 ?  595 MET B CB    1 
ATOM   10323 C  CG    . MET B 1 595 ? 124.780 134.772 162.849 1.00 24.99 ?  595 MET B CG    1 
ATOM   10324 S  SD    . MET B 1 595 ? 123.105 134.374 162.299 1.00 37.28 ?  595 MET B SD    1 
ATOM   10325 C  CE    . MET B 1 595 ? 122.096 135.436 163.325 1.00 16.63 ?  595 MET B CE    1 
ATOM   10326 N  N     . PRO B 1 596 ? 124.356 132.958 167.012 1.00 32.04 ?  596 PRO B N     1 
ATOM   10327 C  CA    . PRO B 1 596 ? 124.817 132.010 168.028 1.00 20.66 ?  596 PRO B CA    1 
ATOM   10328 C  C     . PRO B 1 596 ? 125.879 131.080 167.462 1.00 31.12 ?  596 PRO B C     1 
ATOM   10329 O  O     . PRO B 1 596 ? 126.025 130.917 166.248 1.00 37.74 ?  596 PRO B O     1 
ATOM   10330 C  CB    . PRO B 1 596 ? 123.545 131.248 168.405 1.00 22.35 ?  596 PRO B CB    1 
ATOM   10331 C  CG    . PRO B 1 596 ? 122.700 131.317 167.186 1.00 27.79 ?  596 PRO B CG    1 
ATOM   10332 C  CD    . PRO B 1 596 ? 123.004 132.635 166.525 1.00 32.26 ?  596 PRO B CD    1 
ATOM   10333 N  N     . ILE B 1 597 ? 126.635 130.467 168.372 1.00 28.45 ?  597 ILE B N     1 
ATOM   10334 C  CA    . ILE B 1 597 ? 127.768 129.645 167.967 1.00 28.60 ?  597 ILE B CA    1 
ATOM   10335 C  C     . ILE B 1 597 ? 127.276 128.359 167.316 1.00 37.55 ?  597 ILE B C     1 
ATOM   10336 O  O     . ILE B 1 597 ? 126.290 127.752 167.753 1.00 40.72 ?  597 ILE B O     1 
ATOM   10337 C  CB    . ILE B 1 597 ? 128.678 129.349 169.172 1.00 33.65 ?  597 ILE B CB    1 
ATOM   10338 C  CG1   . ILE B 1 597 ? 127.904 128.611 170.265 1.00 34.53 ?  597 ILE B CG1   1 
ATOM   10339 C  CG2   . ILE B 1 597 ? 129.260 130.636 169.717 1.00 31.62 ?  597 ILE B CG2   1 
ATOM   10340 C  CD1   . ILE B 1 597 ? 128.764 127.723 171.122 1.00 33.96 ?  597 ILE B CD1   1 
ATOM   10341 N  N     . MET B 1 598 ? 127.959 127.949 166.247 1.00 44.87 ?  598 MET B N     1 
ATOM   10342 C  CA    . MET B 1 598 ? 127.624 126.690 165.592 1.00 41.70 ?  598 MET B CA    1 
ATOM   10343 C  C     . MET B 1 598 ? 128.079 125.501 166.427 1.00 38.38 ?  598 MET B C     1 
ATOM   10344 O  O     . MET B 1 598 ? 127.331 124.534 166.611 1.00 46.97 ?  598 MET B O     1 
ATOM   10345 C  CB    . MET B 1 598 ? 128.254 126.642 164.201 1.00 40.80 ?  598 MET B CB    1 
ATOM   10346 C  CG    . MET B 1 598 ? 127.842 127.783 163.295 1.00 39.04 ?  598 MET B CG    1 
ATOM   10347 S  SD    . MET B 1 598 ? 128.161 127.432 161.558 1.00 59.89 ?  598 MET B SD    1 
ATOM   10348 C  CE    . MET B 1 598 ? 129.541 128.528 161.247 1.00 42.97 ?  598 MET B CE    1 
ATOM   10349 N  N     . GLU B 1 599 ? 129.305 125.556 166.942 1.00 42.37 ?  599 GLU B N     1 
ATOM   10350 C  CA    . GLU B 1 599 ? 129.877 124.491 167.751 1.00 42.26 ?  599 GLU B CA    1 
ATOM   10351 C  C     . GLU B 1 599 ? 130.477 125.085 169.014 1.00 40.25 ?  599 GLU B C     1 
ATOM   10352 O  O     . GLU B 1 599 ? 130.946 126.225 169.019 1.00 46.11 ?  599 GLU B O     1 
ATOM   10353 C  CB    . GLU B 1 599 ? 130.960 123.715 166.987 1.00 44.07 ?  599 GLU B CB    1 
ATOM   10354 C  CG    . GLU B 1 599 ? 130.830 123.775 165.476 1.00 43.73 ?  599 GLU B CG    1 
ATOM   10355 C  CD    . GLU B 1 599 ? 132.012 123.146 164.766 1.00 50.12 ?  599 GLU B CD    1 
ATOM   10356 O  OE1   . GLU B 1 599 ? 132.484 122.083 165.219 1.00 49.97 ?  599 GLU B OE1   1 
ATOM   10357 O  OE2   . GLU B 1 599 ? 132.469 123.717 163.754 1.00 48.55 -1 599 GLU B OE2   1 
ATOM   10358 N  N     . ARG B 1 600 ? 130.455 124.304 170.095 1.00 43.29 ?  600 ARG B N     1 
ATOM   10359 C  CA    . ARG B 1 600 ? 131.080 124.754 171.334 1.00 35.78 ?  600 ARG B CA    1 
ATOM   10360 C  C     . ARG B 1 600 ? 132.596 124.778 171.203 1.00 37.20 ?  600 ARG B C     1 
ATOM   10361 O  O     . ARG B 1 600 ? 133.251 125.742 171.617 1.00 41.36 ?  600 ARG B O     1 
ATOM   10362 C  CB    . ARG B 1 600 ? 130.652 123.860 172.495 1.00 38.87 ?  600 ARG B CB    1 
ATOM   10363 C  CG    . ARG B 1 600 ? 129.325 124.256 173.100 1.00 39.64 ?  600 ARG B CG    1 
ATOM   10364 C  CD    . ARG B 1 600 ? 129.095 123.553 174.416 1.00 36.65 ?  600 ARG B CD    1 
ATOM   10365 N  NE    . ARG B 1 600 ? 127.777 123.838 174.968 1.00 36.86 ?  600 ARG B NE    1 
ATOM   10366 C  CZ    . ARG B 1 600 ? 126.666 123.208 174.615 1.00 40.58 ?  600 ARG B CZ    1 
ATOM   10367 N  NH1   . ARG B 1 600 ? 126.675 122.254 173.699 1.00 39.73 1  600 ARG B NH1   1 
ATOM   10368 N  NH2   . ARG B 1 600 ? 125.518 123.542 175.195 1.00 41.50 ?  600 ARG B NH2   1 
ATOM   10369 N  N     . ILE B 1 601 ? 133.172 123.726 170.630 1.00 49.15 ?  601 ILE B N     1 
ATOM   10370 C  CA    . ILE B 1 601 ? 134.600 123.653 170.359 1.00 43.12 ?  601 ILE B CA    1 
ATOM   10371 C  C     . ILE B 1 601 ? 134.781 123.403 168.872 1.00 43.56 ?  601 ILE B C     1 
ATOM   10372 O  O     . ILE B 1 601 ? 134.203 122.460 168.319 1.00 46.37 ?  601 ILE B O     1 
ATOM   10373 C  CB    . ILE B 1 601 ? 135.285 122.557 171.194 1.00 40.56 ?  601 ILE B CB    1 
ATOM   10374 C  CG1   . ILE B 1 601 ? 135.012 122.786 172.681 1.00 42.38 ?  601 ILE B CG1   1 
ATOM   10375 C  CG2   . ILE B 1 601 ? 136.775 122.550 170.921 1.00 41.67 ?  601 ILE B CG2   1 
ATOM   10376 C  CD1   . ILE B 1 601 ? 135.236 121.575 173.544 1.00 44.89 ?  601 ILE B CD1   1 
ATOM   10377 N  N     . GLU B 1 602 ? 135.578 124.246 168.229 1.00 53.69 ?  602 GLU B N     1 
ATOM   10378 C  CA    . GLU B 1 602 ? 135.718 124.254 166.780 1.00 50.17 ?  602 GLU B CA    1 
ATOM   10379 C  C     . GLU B 1 602 ? 136.892 123.370 166.380 1.00 53.61 ?  602 GLU B C     1 
ATOM   10380 O  O     . GLU B 1 602 ? 138.035 123.639 166.765 1.00 57.39 ?  602 GLU B O     1 
ATOM   10381 C  CB    . GLU B 1 602 ? 135.915 125.683 166.281 1.00 50.44 ?  602 GLU B CB    1 
ATOM   10382 C  CG    . GLU B 1 602 ? 135.545 125.907 164.837 1.00 50.20 ?  602 GLU B CG    1 
ATOM   10383 C  CD    . GLU B 1 602 ? 135.507 127.376 164.476 1.00 56.99 ?  602 GLU B CD    1 
ATOM   10384 O  OE1   . GLU B 1 602 ? 134.682 128.111 165.058 1.00 55.91 ?  602 GLU B OE1   1 
ATOM   10385 O  OE2   . GLU B 1 602 ? 136.304 127.796 163.613 1.00 58.72 -1 602 GLU B OE2   1 
ATOM   10386 N  N     . GLU B 1 603 ? 136.610 122.321 165.613 1.00 56.22 ?  603 GLU B N     1 
ATOM   10387 C  CA    . GLU B 1 603 ? 137.631 121.401 165.125 1.00 55.13 ?  603 GLU B CA    1 
ATOM   10388 C  C     . GLU B 1 603 ? 137.952 121.742 163.675 1.00 57.66 ?  603 GLU B C     1 
ATOM   10389 O  O     . GLU B 1 603 ? 137.088 121.618 162.800 1.00 59.08 ?  603 GLU B O     1 
ATOM   10390 C  CB    . GLU B 1 603 ? 137.164 119.949 165.240 1.00 58.25 ?  603 GLU B CB    1 
ATOM   10391 C  CG    . GLU B 1 603 ? 136.659 119.553 166.617 1.00 60.56 ?  603 GLU B CG    1 
ATOM   10392 C  CD    . GLU B 1 603 ? 135.152 119.666 166.745 1.00 60.85 ?  603 GLU B CD    1 
ATOM   10393 O  OE1   . GLU B 1 603 ? 134.470 119.766 165.703 1.00 54.69 ?  603 GLU B OE1   1 
ATOM   10394 O  OE2   . GLU B 1 603 ? 134.650 119.650 167.888 1.00 59.56 -1 603 GLU B OE2   1 
ATOM   10395 N  N     . ARG B 1 604 ? 139.187 122.167 163.427 1.00 60.93 ?  604 ARG B N     1 
ATOM   10396 C  CA    . ARG B 1 604 ? 139.640 122.539 162.096 1.00 61.64 ?  604 ARG B CA    1 
ATOM   10397 C  C     . ARG B 1 604 ? 141.023 121.964 161.832 1.00 62.36 ?  604 ARG B C     1 
ATOM   10398 O  O     . ARG B 1 604 ? 141.800 121.720 162.757 1.00 61.58 ?  604 ARG B O     1 
ATOM   10399 C  CB    . ARG B 1 604 ? 139.663 124.063 161.913 1.00 61.50 ?  604 ARG B CB    1 
ATOM   10400 C  CG    . ARG B 1 604 ? 138.301 124.718 162.038 1.00 61.72 ?  604 ARG B CG    1 
ATOM   10401 C  CD    . ARG B 1 604 ? 137.595 124.717 160.688 1.00 61.06 ?  604 ARG B CD    1 
ATOM   10402 N  NE    . ARG B 1 604 ? 136.520 125.699 160.615 1.00 64.58 ?  604 ARG B NE    1 
ATOM   10403 C  CZ    . ARG B 1 604 ? 135.376 125.615 161.279 1.00 62.16 ?  604 ARG B CZ    1 
ATOM   10404 N  NH1   . ARG B 1 604 ? 135.075 124.552 162.006 1.00 59.27 1  604 ARG B NH1   1 
ATOM   10405 N  NH2   . ARG B 1 604 ? 134.501 126.613 161.191 1.00 60.26 ?  604 ARG B NH2   1 
ATOM   10406 N  N     . THR B 1 605 ? 141.317 121.752 160.553 1.00 68.88 ?  605 THR B N     1 
ATOM   10407 C  CA    . THR B 1 605 ? 142.596 121.215 160.109 1.00 69.05 ?  605 THR B CA    1 
ATOM   10408 C  C     . THR B 1 605 ? 143.320 122.275 159.292 1.00 68.94 ?  605 THR B C     1 
ATOM   10409 O  O     . THR B 1 605 ? 142.782 122.770 158.295 1.00 68.34 ?  605 THR B O     1 
ATOM   10410 C  CB    . THR B 1 605 ? 142.400 119.945 159.280 1.00 68.77 ?  605 THR B CB    1 
ATOM   10411 O  OG1   . THR B 1 605 ? 141.796 118.929 160.090 1.00 68.65 ?  605 THR B OG1   1 
ATOM   10412 C  CG2   . THR B 1 605 ? 143.735 119.443 158.755 1.00 69.06 ?  605 THR B CG2   1 
ATOM   10413 N  N     . TYR B 1 606 ? 144.531 122.620 159.715 1.00 70.93 ?  606 TYR B N     1 
ATOM   10414 C  CA    . TYR B 1 606 ? 145.382 123.560 158.996 1.00 72.42 ?  606 TYR B CA    1 
ATOM   10415 C  C     . TYR B 1 606 ? 146.658 122.834 158.599 1.00 73.83 ?  606 TYR B C     1 
ATOM   10416 O  O     . TYR B 1 606 ? 147.363 122.298 159.462 1.00 71.71 ?  606 TYR B O     1 
ATOM   10417 C  CB    . TYR B 1 606 ? 145.688 124.790 159.851 1.00 70.45 ?  606 TYR B CB    1 
ATOM   10418 C  CG    . TYR B 1 606 ? 144.460 125.611 160.168 1.00 71.00 ?  606 TYR B CG    1 
ATOM   10419 C  CD1   . TYR B 1 606 ? 143.940 126.503 159.240 1.00 68.19 ?  606 TYR B CD1   1 
ATOM   10420 C  CD2   . TYR B 1 606 ? 143.814 125.484 161.389 1.00 71.01 ?  606 TYR B CD2   1 
ATOM   10421 C  CE1   . TYR B 1 606 ? 142.814 127.251 159.523 1.00 69.99 ?  606 TYR B CE1   1 
ATOM   10422 C  CE2   . TYR B 1 606 ? 142.689 126.226 161.681 1.00 68.85 ?  606 TYR B CE2   1 
ATOM   10423 C  CZ    . TYR B 1 606 ? 142.194 127.108 160.745 1.00 72.54 ?  606 TYR B CZ    1 
ATOM   10424 O  OH    . TYR B 1 606 ? 141.071 127.849 161.034 1.00 74.18 ?  606 TYR B OH    1 
ATOM   10425 N  N     . GLY B 1 607 ? 146.955 122.827 157.305 1.00 79.93 ?  607 GLY B N     1 
ATOM   10426 C  CA    . GLY B 1 607 ? 148.039 121.990 156.820 1.00 79.31 ?  607 GLY B CA    1 
ATOM   10427 C  C     . GLY B 1 607 ? 147.706 120.530 157.051 1.00 79.82 ?  607 GLY B C     1 
ATOM   10428 O  O     . GLY B 1 607 ? 146.612 120.059 156.723 1.00 79.29 ?  607 GLY B O     1 
ATOM   10429 N  N     . ASN B 1 608 ? 148.658 119.796 157.625 1.00 81.39 ?  608 ASN B N     1 
ATOM   10430 C  CA    . ASN B 1 608 ? 148.460 118.393 157.961 1.00 82.54 ?  608 ASN B CA    1 
ATOM   10431 C  C     . ASN B 1 608 ? 148.129 118.189 159.434 1.00 83.77 ?  608 ASN B C     1 
ATOM   10432 O  O     . ASN B 1 608 ? 147.974 117.045 159.872 1.00 83.08 ?  608 ASN B O     1 
ATOM   10433 C  CB    . ASN B 1 608 ? 149.699 117.580 157.580 1.00 83.72 ?  608 ASN B CB    1 
ATOM   10434 C  CG    . ASN B 1 608 ? 149.978 117.607 156.089 1.00 84.36 ?  608 ASN B CG    1 
ATOM   10435 O  OD1   . ASN B 1 608 ? 149.145 118.052 155.298 1.00 82.31 ?  608 ASN B OD1   1 
ATOM   10436 N  ND2   . ASN B 1 608 ? 151.152 117.128 155.697 1.00 83.01 ?  608 ASN B ND2   1 
ATOM   10437 N  N     . SER B 1 609 ? 148.012 119.267 160.204 1.00 76.85 ?  609 SER B N     1 
ATOM   10438 C  CA    . SER B 1 609 ? 147.746 119.193 161.632 1.00 76.36 ?  609 SER B CA    1 
ATOM   10439 C  C     . SER B 1 609 ? 146.359 119.743 161.938 1.00 74.44 ?  609 SER B C     1 
ATOM   10440 O  O     . SER B 1 609 ? 145.965 120.789 161.412 1.00 74.33 ?  609 SER B O     1 
ATOM   10441 C  CB    . SER B 1 609 ? 148.802 119.966 162.427 1.00 73.85 ?  609 SER B CB    1 
ATOM   10442 O  OG    . SER B 1 609 ? 148.767 121.347 162.112 1.00 73.50 ?  609 SER B OG    1 
ATOM   10443 N  N     . LYS B 1 610 ? 145.625 119.031 162.787 1.00 64.40 ?  610 LYS B N     1 
ATOM   10444 C  CA    . LYS B 1 610 ? 144.285 119.433 163.185 1.00 63.80 ?  610 LYS B CA    1 
ATOM   10445 C  C     . LYS B 1 610 ? 144.337 120.304 164.434 1.00 63.31 ?  610 LYS B C     1 
ATOM   10446 O  O     . LYS B 1 610 ? 145.152 120.079 165.334 1.00 64.06 ?  610 LYS B O     1 
ATOM   10447 C  CB    . LYS B 1 610 ? 143.407 118.196 163.405 1.00 64.70 ?  610 LYS B CB    1 
ATOM   10448 C  CG    . LYS B 1 610 ? 143.372 117.650 164.822 1.00 63.25 ?  610 LYS B CG    1 
ATOM   10449 C  CD    . LYS B 1 610 ? 142.865 116.215 164.824 1.00 64.78 ?  610 LYS B CD    1 
ATOM   10450 C  CE    . LYS B 1 610 ? 143.554 115.374 165.889 1.00 64.56 ?  610 LYS B CE    1 
ATOM   10451 N  NZ    . LYS B 1 610 ? 143.105 115.704 167.266 1.00 64.14 1  610 LYS B NZ    1 
ATOM   10452 N  N     . THR B 1 611 ? 143.482 121.323 164.465 1.00 63.68 ?  611 THR B N     1 
ATOM   10453 C  CA    . THR B 1 611 ? 143.464 122.309 165.534 1.00 61.02 ?  611 THR B CA    1 
ATOM   10454 C  C     . THR B 1 611 ? 142.095 122.336 166.197 1.00 56.76 ?  611 THR B C     1 
ATOM   10455 O  O     . THR B 1 611 ? 141.079 122.006 165.577 1.00 60.25 ?  611 THR B O     1 
ATOM   10456 C  CB    . THR B 1 611 ? 143.810 123.708 165.008 1.00 61.00 ?  611 THR B CB    1 
ATOM   10457 O  OG1   . THR B 1 611 ? 144.771 123.601 163.951 1.00 61.18 ?  611 THR B OG1   1 
ATOM   10458 C  CG2   . THR B 1 611 ? 144.396 124.554 166.116 1.00 60.84 ?  611 THR B CG2   1 
ATOM   10459 N  N     . TYR B 1 612 ? 142.075 122.733 167.467 1.00 51.00 ?  612 TYR B N     1 
ATOM   10460 C  CA    . TYR B 1 612 ? 140.856 122.804 168.258 1.00 52.40 ?  612 TYR B CA    1 
ATOM   10461 C  C     . TYR B 1 612 ? 140.683 124.220 168.783 1.00 54.60 ?  612 TYR B C     1 
ATOM   10462 O  O     . TYR B 1 612 ? 141.616 124.792 169.356 1.00 53.52 ?  612 TYR B O     1 
ATOM   10463 C  CB    . TYR B 1 612 ? 140.905 121.807 169.414 1.00 54.04 ?  612 TYR B CB    1 
ATOM   10464 C  CG    . TYR B 1 612 ? 140.906 120.374 168.947 1.00 57.49 ?  612 TYR B CG    1 
ATOM   10465 C  CD1   . TYR B 1 612 ? 139.832 119.855 168.239 1.00 55.55 ?  612 TYR B CD1   1 
ATOM   10466 C  CD2   . TYR B 1 612 ? 141.995 119.549 169.184 1.00 56.40 ?  612 TYR B CD2   1 
ATOM   10467 C  CE1   . TYR B 1 612 ? 139.832 118.548 167.800 1.00 54.86 ?  612 TYR B CE1   1 
ATOM   10468 C  CE2   . TYR B 1 612 ? 142.006 118.244 168.747 1.00 59.31 ?  612 TYR B CE2   1 
ATOM   10469 C  CZ    . TYR B 1 612 ? 140.922 117.746 168.057 1.00 59.22 ?  612 TYR B CZ    1 
ATOM   10470 O  OH    . TYR B 1 612 ? 140.928 116.443 167.620 1.00 60.84 ?  612 TYR B OH    1 
ATOM   10471 N  N     . TYR B 1 613 ? 139.494 124.782 168.588 1.00 51.35 ?  613 TYR B N     1 
ATOM   10472 C  CA    . TYR B 1 613 ? 139.191 126.147 169.010 1.00 45.38 ?  613 TYR B CA    1 
ATOM   10473 C  C     . TYR B 1 613 ? 137.930 126.164 169.863 1.00 43.07 ?  613 TYR B C     1 
ATOM   10474 O  O     . TYR B 1 613 ? 136.813 126.193 169.320 1.00 43.80 ?  613 TYR B O     1 
ATOM   10475 C  CB    . TYR B 1 613 ? 139.035 127.073 167.811 1.00 42.88 ?  613 TYR B CB    1 
ATOM   10476 C  CG    . TYR B 1 613 ? 138.684 128.493 168.188 1.00 43.43 ?  613 TYR B CG    1 
ATOM   10477 C  CD1   . TYR B 1 613 ? 139.433 129.186 169.129 1.00 42.09 ?  613 TYR B CD1   1 
ATOM   10478 C  CD2   . TYR B 1 613 ? 137.606 129.141 167.603 1.00 45.50 ?  613 TYR B CD2   1 
ATOM   10479 C  CE1   . TYR B 1 613 ? 139.117 130.483 169.475 1.00 44.64 ?  613 TYR B CE1   1 
ATOM   10480 C  CE2   . TYR B 1 613 ? 137.283 130.437 167.944 1.00 45.24 ?  613 TYR B CE2   1 
ATOM   10481 C  CZ    . TYR B 1 613 ? 138.042 131.103 168.879 1.00 48.46 ?  613 TYR B CZ    1 
ATOM   10482 O  OH    . TYR B 1 613 ? 137.723 132.396 169.220 1.00 47.39 ?  613 TYR B OH    1 
ATOM   10483 N  N     . PRO B 1 614 ? 138.060 126.140 171.185 1.00 39.22 ?  614 PRO B N     1 
ATOM   10484 C  CA    . PRO B 1 614 ? 136.890 126.367 172.035 1.00 42.67 ?  614 PRO B CA    1 
ATOM   10485 C  C     . PRO B 1 614 ? 136.372 127.783 171.855 1.00 41.86 ?  614 PRO B C     1 
ATOM   10486 O  O     . PRO B 1 614 ? 137.129 128.714 171.566 1.00 42.89 ?  614 PRO B O     1 
ATOM   10487 C  CB    . PRO B 1 614 ? 137.426 126.147 173.457 1.00 39.16 ?  614 PRO B CB    1 
ATOM   10488 C  CG    . PRO B 1 614 ? 138.769 125.506 173.288 1.00 42.11 ?  614 PRO B CG    1 
ATOM   10489 C  CD    . PRO B 1 614 ? 139.289 125.965 171.971 1.00 40.31 ?  614 PRO B CD    1 
ATOM   10490 N  N     . MET B 1 615 ? 135.065 127.941 172.020 1.00 40.49 ?  615 MET B N     1 
ATOM   10491 C  CA    . MET B 1 615 ? 134.474 129.261 171.889 1.00 40.16 ?  615 MET B CA    1 
ATOM   10492 C  C     . MET B 1 615 ? 135.010 130.180 172.985 1.00 44.34 ?  615 MET B C     1 
ATOM   10493 O  O     . MET B 1 615 ? 135.283 129.722 174.100 1.00 42.90 ?  615 MET B O     1 
ATOM   10494 C  CB    . MET B 1 615 ? 132.949 129.180 171.946 1.00 38.52 ?  615 MET B CB    1 
ATOM   10495 C  CG    . MET B 1 615 ? 132.333 128.758 170.623 1.00 41.18 ?  615 MET B CG    1 
ATOM   10496 S  SD    . MET B 1 615 ? 133.363 129.279 169.236 1.00 52.06 ?  615 MET B SD    1 
ATOM   10497 C  CE    . MET B 1 615 ? 132.391 128.736 167.839 1.00 41.46 ?  615 MET B CE    1 
ATOM   10498 N  N     . PRO B 1 616 ? 135.197 131.466 172.696 1.00 45.96 ?  616 PRO B N     1 
ATOM   10499 C  CA    . PRO B 1 616 ? 135.862 132.355 173.658 1.00 39.83 ?  616 PRO B CA    1 
ATOM   10500 C  C     . PRO B 1 616 ? 135.095 132.441 174.968 1.00 41.31 ?  616 PRO B C     1 
ATOM   10501 O  O     . PRO B 1 616 ? 133.905 132.762 174.991 1.00 42.63 ?  616 PRO B O     1 
ATOM   10502 C  CB    . PRO B 1 616 ? 135.890 133.704 172.931 1.00 36.23 ?  616 PRO B CB    1 
ATOM   10503 C  CG    . PRO B 1 616 ? 135.701 133.369 171.491 1.00 41.50 ?  616 PRO B CG    1 
ATOM   10504 C  CD    . PRO B 1 616 ? 134.831 132.168 171.455 1.00 40.52 ?  616 PRO B CD    1 
ATOM   10505 N  N     . GLY B 1 617 ? 135.795 132.163 176.063 1.00 40.43 ?  617 GLY B N     1 
ATOM   10506 C  CA    . GLY B 1 617 ? 135.188 132.149 177.373 1.00 36.58 ?  617 GLY B CA    1 
ATOM   10507 C  C     . GLY B 1 617 ? 134.510 130.854 177.753 1.00 41.88 ?  617 GLY B C     1 
ATOM   10508 O  O     . GLY B 1 617 ? 133.890 130.793 178.822 1.00 45.55 ?  617 GLY B O     1 
ATOM   10509 N  N     . LEU B 1 618 ? 134.602 129.821 176.919 1.00 44.70 ?  618 LEU B N     1 
ATOM   10510 C  CA    . LEU B 1 618 ? 134.002 128.537 177.249 1.00 38.50 ?  618 LEU B CA    1 
ATOM   10511 C  C     . LEU B 1 618 ? 134.709 127.911 178.443 1.00 39.94 ?  618 LEU B C     1 
ATOM   10512 O  O     . LEU B 1 618 ? 135.939 127.905 178.528 1.00 44.64 ?  618 LEU B O     1 
ATOM   10513 C  CB    . LEU B 1 618 ? 134.065 127.593 176.049 1.00 38.04 ?  618 LEU B CB    1 
ATOM   10514 C  CG    . LEU B 1 618 ? 133.385 126.233 176.194 1.00 40.00 ?  618 LEU B CG    1 
ATOM   10515 C  CD1   . LEU B 1 618 ? 131.902 126.400 176.461 1.00 41.29 ?  618 LEU B CD1   1 
ATOM   10516 C  CD2   . LEU B 1 618 ? 133.613 125.394 174.952 1.00 40.82 ?  618 LEU B CD2   1 
ATOM   10517 N  N     . ALA B 1 619 ? 133.917 127.381 179.368 1.00 47.78 ?  619 ALA B N     1 
ATOM   10518 C  CA    . ALA B 1 619 ? 134.434 126.736 180.564 1.00 47.23 ?  619 ALA B CA    1 
ATOM   10519 C  C     . ALA B 1 619 ? 133.393 125.735 181.045 1.00 49.90 ?  619 ALA B C     1 
ATOM   10520 O  O     . ALA B 1 619 ? 132.437 125.415 180.332 1.00 54.00 ?  619 ALA B O     1 
ATOM   10521 C  CB    . ALA B 1 619 ? 134.783 127.777 181.636 1.00 46.77 ?  619 ALA B CB    1 
ATOM   10522 N  N     . SER B 1 620 ? 133.583 125.227 182.261 1.00 56.15 ?  620 SER B N     1 
ATOM   10523 C  CA    . SER B 1 620 ? 132.612 124.304 182.834 1.00 55.66 ?  620 SER B CA    1 
ATOM   10524 C  C     . SER B 1 620 ? 131.374 125.034 183.339 1.00 55.44 ?  620 SER B C     1 
ATOM   10525 O  O     . SER B 1 620 ? 130.257 124.516 183.232 1.00 57.57 ?  620 SER B O     1 
ATOM   10526 C  CB    . SER B 1 620 ? 133.258 123.501 183.963 1.00 57.26 ?  620 SER B CB    1 
ATOM   10527 O  OG    . SER B 1 620 ? 134.495 122.953 183.547 1.00 59.15 ?  620 SER B OG    1 
ATOM   10528 N  N     . ASN B 1 621 ? 131.553 126.237 183.890 1.00 50.85 ?  621 ASN B N     1 
ATOM   10529 C  CA    . ASN B 1 621 ? 130.427 126.957 184.479 1.00 52.15 ?  621 ASN B CA    1 
ATOM   10530 C  C     . ASN B 1 621 ? 129.473 127.481 183.411 1.00 54.39 ?  621 ASN B C     1 
ATOM   10531 O  O     . ASN B 1 621 ? 128.254 127.502 183.619 1.00 56.25 ?  621 ASN B O     1 
ATOM   10532 C  CB    . ASN B 1 621 ? 130.937 128.100 185.358 1.00 53.65 ?  621 ASN B CB    1 
ATOM   10533 C  CG    . ASN B 1 621 ? 131.660 129.171 184.564 1.00 57.66 ?  621 ASN B CG    1 
ATOM   10534 O  OD1   . ASN B 1 621 ? 132.692 128.912 183.947 1.00 59.16 ?  621 ASN B OD1   1 
ATOM   10535 N  ND2   . ASN B 1 621 ? 131.120 130.385 184.579 1.00 55.87 ?  621 ASN B ND2   1 
ATOM   10536 N  N     . ASN B 1 622 ? 130.002 127.910 182.265 1.00 46.91 ?  622 ASN B N     1 
ATOM   10537 C  CA    . ASN B 1 622 ? 129.189 128.474 181.194 1.00 45.83 ?  622 ASN B CA    1 
ATOM   10538 C  C     . ASN B 1 622 ? 129.071 127.539 179.996 1.00 47.47 ?  622 ASN B C     1 
ATOM   10539 O  O     . ASN B 1 622 ? 128.806 127.997 178.882 1.00 53.86 ?  622 ASN B O     1 
ATOM   10540 C  CB    . ASN B 1 622 ? 129.744 129.836 180.766 1.00 46.81 ?  622 ASN B CB    1 
ATOM   10541 C  CG    . ASN B 1 622 ? 131.157 129.756 180.203 1.00 46.56 ?  622 ASN B CG    1 
ATOM   10542 O  OD1   . ASN B 1 622 ? 131.660 128.681 179.883 1.00 52.25 ?  622 ASN B OD1   1 
ATOM   10543 N  ND2   . ASN B 1 622 ? 131.804 130.908 180.087 1.00 43.47 ?  622 ASN B ND2   1 
ATOM   10544 N  N     . TRP B 1 623 ? 129.273 126.236 180.205 1.00 41.95 ?  623 TRP B N     1 
ATOM   10545 C  CA    . TRP B 1 623 ? 129.243 125.294 179.091 1.00 40.84 ?  623 TRP B CA    1 
ATOM   10546 C  C     . TRP B 1 623 ? 127.868 125.246 178.437 1.00 42.27 ?  623 TRP B C     1 
ATOM   10547 O  O     . TRP B 1 623 ? 127.760 125.235 177.205 1.00 42.30 ?  623 TRP B O     1 
ATOM   10548 C  CB    . TRP B 1 623 ? 129.654 123.903 179.573 1.00 45.73 ?  623 TRP B CB    1 
ATOM   10549 C  CG    . TRP B 1 623 ? 129.472 122.826 178.548 1.00 43.63 ?  623 TRP B CG    1 
ATOM   10550 C  CD1   . TRP B 1 623 ? 128.355 122.071 178.342 1.00 40.76 ?  623 TRP B CD1   1 
ATOM   10551 C  CD2   . TRP B 1 623 ? 130.439 122.379 177.591 1.00 42.24 ?  623 TRP B CD2   1 
ATOM   10552 N  NE1   . TRP B 1 623 ? 128.565 121.186 177.316 1.00 42.99 ?  623 TRP B NE1   1 
ATOM   10553 C  CE2   . TRP B 1 623 ? 129.838 121.352 176.839 1.00 40.39 ?  623 TRP B CE2   1 
ATOM   10554 C  CE3   . TRP B 1 623 ? 131.755 122.748 177.299 1.00 39.81 ?  623 TRP B CE3   1 
ATOM   10555 C  CZ2   . TRP B 1 623 ? 130.506 120.692 175.812 1.00 38.39 ?  623 TRP B CZ2   1 
ATOM   10556 C  CZ3   . TRP B 1 623 ? 132.415 122.091 176.279 1.00 42.86 ?  623 TRP B CZ3   1 
ATOM   10557 C  CH2   . TRP B 1 623 ? 131.791 121.075 175.547 1.00 42.62 ?  623 TRP B CH2   1 
ATOM   10558 N  N     . PHE B 1 624 ? 126.806 125.218 179.239 1.00 48.20 ?  624 PHE B N     1 
ATOM   10559 C  CA    . PHE B 1 624 ? 125.462 125.077 178.701 1.00 45.50 ?  624 PHE B CA    1 
ATOM   10560 C  C     . PHE B 1 624 ? 124.828 126.403 178.305 1.00 45.25 ?  624 PHE B C     1 
ATOM   10561 O  O     . PHE B 1 624 ? 123.771 126.398 177.666 1.00 52.40 ?  624 PHE B O     1 
ATOM   10562 C  CB    . PHE B 1 624 ? 124.567 124.349 179.708 1.00 49.11 ?  624 PHE B CB    1 
ATOM   10563 C  CG    . PHE B 1 624 ? 124.826 122.871 179.776 1.00 50.34 ?  624 PHE B CG    1 
ATOM   10564 C  CD1   . PHE B 1 624 ? 124.443 122.040 178.736 1.00 44.39 ?  624 PHE B CD1   1 
ATOM   10565 C  CD2   . PHE B 1 624 ? 125.468 122.316 180.870 1.00 48.19 ?  624 PHE B CD2   1 
ATOM   10566 C  CE1   . PHE B 1 624 ? 124.685 120.683 178.791 1.00 44.64 ?  624 PHE B CE1   1 
ATOM   10567 C  CE2   . PHE B 1 624 ? 125.713 120.958 180.930 1.00 49.33 ?  624 PHE B CE2   1 
ATOM   10568 C  CZ    . PHE B 1 624 ? 125.320 120.140 179.889 1.00 48.15 ?  624 PHE B CZ    1 
ATOM   10569 N  N     . PHE B 1 625 ? 125.441 127.531 178.662 1.00 39.83 ?  625 PHE B N     1 
ATOM   10570 C  CA    . PHE B 1 625 ? 125.036 128.802 178.081 1.00 37.08 ?  625 PHE B CA    1 
ATOM   10571 C  C     . PHE B 1 625 ? 125.586 128.985 176.677 1.00 36.39 ?  625 PHE B C     1 
ATOM   10572 O  O     . PHE B 1 625 ? 125.067 129.813 175.922 1.00 41.33 ?  625 PHE B O     1 
ATOM   10573 C  CB    . PHE B 1 625 ? 125.479 129.965 178.969 1.00 32.77 ?  625 PHE B CB    1 
ATOM   10574 C  CG    . PHE B 1 625 ? 124.695 130.086 180.240 1.00 35.96 ?  625 PHE B CG    1 
ATOM   10575 C  CD1   . PHE B 1 625 ? 123.352 130.417 180.207 1.00 37.62 ?  625 PHE B CD1   1 
ATOM   10576 C  CD2   . PHE B 1 625 ? 125.298 129.872 181.467 1.00 37.97 ?  625 PHE B CD2   1 
ATOM   10577 C  CE1   . PHE B 1 625 ? 122.625 130.531 181.374 1.00 40.00 ?  625 PHE B CE1   1 
ATOM   10578 C  CE2   . PHE B 1 625 ? 124.576 129.986 182.637 1.00 37.58 ?  625 PHE B CE2   1 
ATOM   10579 C  CZ    . PHE B 1 625 ? 123.238 130.317 182.590 1.00 40.99 ?  625 PHE B CZ    1 
ATOM   10580 N  N     . TYR B 1 626 ? 126.619 128.232 176.313 1.00 29.50 ?  626 TYR B N     1 
ATOM   10581 C  CA    . TYR B 1 626 ? 127.135 128.219 174.947 1.00 33.44 ?  626 TYR B CA    1 
ATOM   10582 C  C     . TYR B 1 626 ? 126.392 127.195 174.098 1.00 30.15 ?  626 TYR B C     1 
ATOM   10583 O  O     . TYR B 1 626 ? 126.989 126.343 173.447 1.00 36.11 ?  626 TYR B O     1 
ATOM   10584 C  CB    . TYR B 1 626 ? 128.632 127.935 174.960 1.00 32.29 ?  626 TYR B CB    1 
ATOM   10585 C  CG    . TYR B 1 626 ? 129.484 129.173 175.077 1.00 34.18 ?  626 TYR B CG    1 
ATOM   10586 C  CD1   . TYR B 1 626 ? 129.690 130.002 173.985 1.00 35.39 ?  626 TYR B CD1   1 
ATOM   10587 C  CD2   . TYR B 1 626 ? 130.082 129.513 176.282 1.00 34.34 ?  626 TYR B CD2   1 
ATOM   10588 C  CE1   . TYR B 1 626 ? 130.469 131.135 174.088 1.00 35.36 ?  626 TYR B CE1   1 
ATOM   10589 C  CE2   . TYR B 1 626 ? 130.861 130.644 176.395 1.00 31.69 ?  626 TYR B CE2   1 
ATOM   10590 C  CZ    . TYR B 1 626 ? 131.051 131.450 175.295 1.00 30.87 ?  626 TYR B CZ    1 
ATOM   10591 O  OH    . TYR B 1 626 ? 131.824 132.578 175.402 1.00 38.82 ?  626 TYR B OH    1 
ATOM   10592 N  N     . LYS B 1 627 ? 125.066 127.281 174.113 1.00 33.87 ?  627 LYS B N     1 
ATOM   10593 C  CA    . LYS B 1 627 ? 124.242 126.346 173.363 1.00 34.18 ?  627 LYS B CA    1 
ATOM   10594 C  C     . LYS B 1 627 ? 124.518 126.478 171.872 1.00 37.69 ?  627 LYS B C     1 
ATOM   10595 O  O     . LYS B 1 627 ? 124.594 127.587 171.338 1.00 44.50 ?  627 LYS B O     1 
ATOM   10596 C  CB    . LYS B 1 627 ? 122.767 126.604 173.666 1.00 37.36 ?  627 LYS B CB    1 
ATOM   10597 C  CG    . LYS B 1 627 ? 121.801 125.615 173.049 1.00 37.26 ?  627 LYS B CG    1 
ATOM   10598 C  CD    . LYS B 1 627 ? 120.408 125.815 173.619 1.00 32.29 ?  627 LYS B CD    1 
ATOM   10599 C  CE    . LYS B 1 627 ? 119.407 124.873 172.985 1.00 39.91 ?  627 LYS B CE    1 
ATOM   10600 N  NZ    . LYS B 1 627 ? 118.043 125.064 173.547 1.00 41.71 1  627 LYS B NZ    1 
ATOM   10601 N  N     . GLU B 1 628 ? 124.688 125.343 171.203 1.00 39.03 ?  628 GLU B N     1 
ATOM   10602 C  CA    . GLU B 1 628 ? 124.972 125.364 169.776 1.00 35.29 ?  628 GLU B CA    1 
ATOM   10603 C  C     . GLU B 1 628 ? 123.758 125.855 168.999 1.00 40.27 ?  628 GLU B C     1 
ATOM   10604 O  O     . GLU B 1 628 ? 122.609 125.659 169.404 1.00 45.56 ?  628 GLU B O     1 
ATOM   10605 C  CB    . GLU B 1 628 ? 125.392 123.979 169.292 1.00 39.70 ?  628 GLU B CB    1 
ATOM   10606 C  CG    . GLU B 1 628 ? 126.579 123.403 170.043 1.00 41.43 ?  628 GLU B CG    1 
ATOM   10607 C  CD    . GLU B 1 628 ? 127.346 122.383 169.229 1.00 47.84 ?  628 GLU B CD    1 
ATOM   10608 O  OE1   . GLU B 1 628 ? 126.824 121.945 168.181 1.00 43.73 ?  628 GLU B OE1   1 
ATOM   10609 O  OE2   . GLU B 1 628 ? 128.471 122.021 169.632 1.00 45.74 -1 628 GLU B OE2   1 
ATOM   10610 N  N     . ALA B 1 629 ? 124.030 126.513 167.870 1.00 41.50 ?  629 ALA B N     1 
ATOM   10611 C  CA    . ALA B 1 629 ? 122.964 127.133 167.090 1.00 32.10 ?  629 ALA B CA    1 
ATOM   10612 C  C     . ALA B 1 629 ? 121.971 126.099 166.576 1.00 37.00 ?  629 ALA B C     1 
ATOM   10613 O  O     . ALA B 1 629 ? 120.762 126.357 166.536 1.00 44.16 ?  629 ALA B O     1 
ATOM   10614 C  CB    . ALA B 1 629 ? 123.564 127.925 165.930 1.00 30.45 ?  629 ALA B CB    1 
ATOM   10615 N  N     . TYR B 1 630 ? 122.460 124.927 166.170 1.00 40.68 ?  630 TYR B N     1 
ATOM   10616 C  CA    . TYR B 1 630 ? 121.568 123.895 165.650 1.00 39.14 ?  630 TYR B CA    1 
ATOM   10617 C  C     . TYR B 1 630 ? 120.628 123.366 166.726 1.00 42.65 ?  630 TYR B C     1 
ATOM   10618 O  O     . TYR B 1 630 ? 119.482 123.015 166.425 1.00 49.05 ?  630 TYR B O     1 
ATOM   10619 C  CB    . TYR B 1 630 ? 122.385 122.758 165.045 1.00 37.55 ?  630 TYR B CB    1 
ATOM   10620 C  CG    . TYR B 1 630 ? 123.324 123.213 163.955 1.00 37.64 ?  630 TYR B CG    1 
ATOM   10621 C  CD1   . TYR B 1 630 ? 122.871 123.400 162.657 1.00 38.02 ?  630 TYR B CD1   1 
ATOM   10622 C  CD2   . TYR B 1 630 ? 124.661 123.463 164.224 1.00 37.73 ?  630 TYR B CD2   1 
ATOM   10623 C  CE1   . TYR B 1 630 ? 123.724 123.818 161.658 1.00 38.57 ?  630 TYR B CE1   1 
ATOM   10624 C  CE2   . TYR B 1 630 ? 125.522 123.881 163.230 1.00 40.36 ?  630 TYR B CE2   1 
ATOM   10625 C  CZ    . TYR B 1 630 ? 125.047 124.057 161.950 1.00 45.55 ?  630 TYR B CZ    1 
ATOM   10626 O  OH    . TYR B 1 630 ? 125.900 124.473 160.955 1.00 51.53 ?  630 TYR B OH    1 
ATOM   10627 N  N     . ASP B 1 631 ? 121.086 123.302 167.975 1.00 42.26 ?  631 ASP B N     1 
ATOM   10628 C  CA    . ASP B 1 631 ? 120.228 122.876 169.074 1.00 37.01 ?  631 ASP B CA    1 
ATOM   10629 C  C     . ASP B 1 631 ? 119.194 123.926 169.453 1.00 43.14 ?  631 ASP B C     1 
ATOM   10630 O  O     . ASP B 1 631 ? 118.296 123.628 170.247 1.00 47.63 ?  631 ASP B O     1 
ATOM   10631 C  CB    . ASP B 1 631 ? 121.075 122.530 170.299 1.00 41.58 ?  631 ASP B CB    1 
ATOM   10632 C  CG    . ASP B 1 631 ? 122.097 121.448 170.015 1.00 48.57 ?  631 ASP B CG    1 
ATOM   10633 O  OD1   . ASP B 1 631 ? 121.792 120.533 169.222 1.00 49.25 ?  631 ASP B OD1   1 
ATOM   10634 O  OD2   . ASP B 1 631 ? 123.206 121.513 170.586 1.00 50.10 -1 631 ASP B OD2   1 
ATOM   10635 N  N     . MET B 1 632 ? 119.292 125.132 168.909 1.00 37.56 ?  632 MET B N     1 
ATOM   10636 C  CA    . MET B 1 632 ? 118.432 126.237 169.297 1.00 38.15 ?  632 MET B CA    1 
ATOM   10637 C  C     . MET B 1 632 ? 117.122 126.216 168.521 1.00 37.21 ?  632 MET B C     1 
ATOM   10638 O  O     . MET B 1 632 ? 116.998 125.586 167.469 1.00 36.18 ?  632 MET B O     1 
ATOM   10639 C  CB    . MET B 1 632 ? 119.138 127.571 169.067 1.00 36.52 ?  632 MET B CB    1 
ATOM   10640 C  CG    . MET B 1 632 ? 119.791 128.148 170.300 1.00 35.34 ?  632 MET B CG    1 
ATOM   10641 S  SD    . MET B 1 632 ? 121.133 129.267 169.899 1.00 45.68 ?  632 MET B SD    1 
ATOM   10642 C  CE    . MET B 1 632 ? 121.974 129.347 171.473 1.00 33.51 ?  632 MET B CE    1 
ATOM   10643 N  N     . ASP B 1 633 ? 116.135 126.924 169.063 1.00 37.50 ?  633 ASP B N     1 
ATOM   10644 C  CA    . ASP B 1 633 ? 114.879 127.152 168.364 1.00 33.40 ?  633 ASP B CA    1 
ATOM   10645 C  C     . ASP B 1 633 ? 115.056 128.330 167.415 1.00 36.19 ?  633 ASP B C     1 
ATOM   10646 O  O     . ASP B 1 633 ? 115.304 129.456 167.858 1.00 43.42 ?  633 ASP B O     1 
ATOM   10647 C  CB    . ASP B 1 633 ? 113.754 127.423 169.360 1.00 30.86 ?  633 ASP B CB    1 
ATOM   10648 C  CG    . ASP B 1 633 ? 112.396 127.524 168.696 1.00 40.37 ?  633 ASP B CG    1 
ATOM   10649 O  OD1   . ASP B 1 633 ? 112.284 127.183 167.500 1.00 43.37 ?  633 ASP B OD1   1 
ATOM   10650 O  OD2   . ASP B 1 633 ? 111.437 127.951 169.371 1.00 41.05 -1 633 ASP B OD2   1 
ATOM   10651 N  N     . MET B 1 634 ? 114.935 128.071 166.111 1.00 30.22 ?  634 MET B N     1 
ATOM   10652 C  CA    . MET B 1 634 ? 115.133 129.130 165.129 1.00 23.54 ?  634 MET B CA    1 
ATOM   10653 C  C     . MET B 1 634 ? 114.109 130.246 165.264 1.00 26.50 ?  634 MET B C     1 
ATOM   10654 O  O     . MET B 1 634 ? 114.382 131.369 164.832 1.00 31.39 ?  634 MET B O     1 
ATOM   10655 C  CB    . MET B 1 634 ? 115.096 128.554 163.714 1.00 26.08 ?  634 MET B CB    1 
ATOM   10656 C  CG    . MET B 1 634 ? 116.408 127.936 163.272 1.00 31.31 ?  634 MET B CG    1 
ATOM   10657 S  SD    . MET B 1 634 ? 117.800 129.071 163.449 1.00 43.09 ?  634 MET B SD    1 
ATOM   10658 C  CE    . MET B 1 634 ? 118.705 128.300 164.790 1.00 29.75 ?  634 MET B CE    1 
ATOM   10659 N  N     . PHE B 1 635 ? 112.943 129.969 165.848 1.00 26.09 ?  635 PHE B N     1 
ATOM   10660 C  CA    . PHE B 1 635 ? 111.983 131.037 166.106 1.00 23.44 ?  635 PHE B CA    1 
ATOM   10661 C  C     . PHE B 1 635 ? 112.535 132.035 167.116 1.00 21.59 ?  635 PHE B C     1 
ATOM   10662 O  O     . PHE B 1 635 ? 112.369 133.249 166.956 1.00 26.28 ?  635 PHE B O     1 
ATOM   10663 C  CB    . PHE B 1 635 ? 110.660 130.449 166.595 1.00 27.07 ?  635 PHE B CB    1 
ATOM   10664 C  CG    . PHE B 1 635 ? 109.687 130.155 165.491 1.00 30.07 ?  635 PHE B CG    1 
ATOM   10665 C  CD1   . PHE B 1 635 ? 110.108 129.541 164.325 1.00 26.06 ?  635 PHE B CD1   1 
ATOM   10666 C  CD2   . PHE B 1 635 ? 108.352 130.495 165.618 1.00 25.64 ?  635 PHE B CD2   1 
ATOM   10667 C  CE1   . PHE B 1 635 ? 109.217 129.270 163.307 1.00 24.41 ?  635 PHE B CE1   1 
ATOM   10668 C  CE2   . PHE B 1 635 ? 107.456 130.226 164.602 1.00 28.30 ?  635 PHE B CE2   1 
ATOM   10669 C  CZ    . PHE B 1 635 ? 107.890 129.611 163.446 1.00 25.18 ?  635 PHE B CZ    1 
ATOM   10670 N  N     . LYS B 1 636 ? 113.209 131.545 168.157 1.00 27.48 ?  636 LYS B N     1 
ATOM   10671 C  CA    . LYS B 1 636 ? 113.794 132.446 169.143 1.00 30.38 ?  636 LYS B CA    1 
ATOM   10672 C  C     . LYS B 1 636 ? 114.989 133.202 168.577 1.00 26.86 ?  636 LYS B C     1 
ATOM   10673 O  O     . LYS B 1 636 ? 115.221 134.359 168.944 1.00 36.77 ?  636 LYS B O     1 
ATOM   10674 C  CB    . LYS B 1 636 ? 114.190 131.662 170.391 1.00 30.54 ?  636 LYS B CB    1 
ATOM   10675 C  CG    . LYS B 1 636 ? 113.030 130.926 171.039 1.00 29.29 ?  636 LYS B CG    1 
ATOM   10676 C  CD    . LYS B 1 636 ? 112.536 131.657 172.273 1.00 34.76 ?  636 LYS B CD    1 
ATOM   10677 C  CE    . LYS B 1 636 ? 111.084 131.325 172.567 1.00 33.40 ?  636 LYS B CE    1 
ATOM   10678 N  NZ    . LYS B 1 636 ? 110.264 132.552 172.764 1.00 35.79 1  636 LYS B NZ    1 
ATOM   10679 N  N     . VAL B 1 637 ? 115.753 132.575 167.683 1.00 24.28 ?  637 VAL B N     1 
ATOM   10680 C  CA    . VAL B 1 637 ? 116.831 133.290 167.004 1.00 17.58 ?  637 VAL B CA    1 
ATOM   10681 C  C     . VAL B 1 637 ? 116.256 134.381 166.110 1.00 27.32 ?  637 VAL B C     1 
ATOM   10682 O  O     . VAL B 1 637 ? 116.807 135.486 166.020 1.00 31.76 ?  637 VAL B O     1 
ATOM   10683 C  CB    . VAL B 1 637 ? 117.709 132.303 166.214 1.00 21.70 ?  637 VAL B CB    1 
ATOM   10684 C  CG1   . VAL B 1 637 ? 118.853 133.035 165.538 1.00 22.34 ?  637 VAL B CG1   1 
ATOM   10685 C  CG2   . VAL B 1 637 ? 118.234 131.214 167.133 1.00 23.89 ?  637 VAL B CG2   1 
ATOM   10686 N  N     . VAL B 1 638 ? 115.141 134.090 165.436 1.00 25.42 ?  638 VAL B N     1 
ATOM   10687 C  CA    . VAL B 1 638 ? 114.448 135.109 164.655 1.00 22.70 ?  638 VAL B CA    1 
ATOM   10688 C  C     . VAL B 1 638 ? 113.999 136.249 165.558 1.00 19.58 ?  638 VAL B C     1 
ATOM   10689 O  O     . VAL B 1 638 ? 114.106 137.426 165.198 1.00 30.46 ?  638 VAL B O     1 
ATOM   10690 C  CB    . VAL B 1 638 ? 113.255 134.492 163.900 1.00 24.93 ?  638 VAL B CB    1 
ATOM   10691 C  CG1   . VAL B 1 638 ? 112.307 135.578 163.427 1.00 14.67 ?  638 VAL B CG1   1 
ATOM   10692 C  CG2   . VAL B 1 638 ? 113.727 133.655 162.729 1.00 23.91 ?  638 VAL B CG2   1 
ATOM   10693 N  N     . ASP B 1 639 ? 113.479 135.915 166.739 1.00 17.63 ?  639 ASP B N     1 
ATOM   10694 C  CA    . ASP B 1 639 ? 113.055 136.941 167.686 1.00 21.91 ?  639 ASP B CA    1 
ATOM   10695 C  C     . ASP B 1 639 ? 114.224 137.826 168.099 1.00 26.76 ?  639 ASP B C     1 
ATOM   10696 O  O     . ASP B 1 639 ? 114.094 139.053 168.160 1.00 34.74 ?  639 ASP B O     1 
ATOM   10697 C  CB    . ASP B 1 639 ? 112.424 136.286 168.914 1.00 25.22 ?  639 ASP B CB    1 
ATOM   10698 C  CG    . ASP B 1 639 ? 110.973 135.918 168.697 1.00 36.03 ?  639 ASP B CG    1 
ATOM   10699 O  OD1   . ASP B 1 639 ? 110.292 136.609 167.912 1.00 33.39 ?  639 ASP B OD1   1 
ATOM   10700 O  OD2   . ASP B 1 639 ? 110.511 134.936 169.314 1.00 39.17 -1 639 ASP B OD2   1 
ATOM   10701 N  N     . MET B 1 640 ? 115.378 137.216 168.375 1.00 24.69 ?  640 MET B N     1 
ATOM   10702 C  CA    . MET B 1 640 ? 116.564 137.985 168.739 1.00 17.97 ?  640 MET B CA    1 
ATOM   10703 C  C     . MET B 1 640 ? 117.000 138.907 167.605 1.00 23.27 ?  640 MET B C     1 
ATOM   10704 O  O     . MET B 1 640 ? 117.275 140.094 167.822 1.00 32.90 ?  640 MET B O     1 
ATOM   10705 C  CB    . MET B 1 640 ? 117.699 137.037 169.121 1.00 22.73 ?  640 MET B CB    1 
ATOM   10706 C  CG    . MET B 1 640 ? 119.073 137.675 169.082 1.00 28.17 ?  640 MET B CG    1 
ATOM   10707 S  SD    . MET B 1 640 ? 119.362 138.752 170.492 1.00 39.52 ?  640 MET B SD    1 
ATOM   10708 C  CE    . MET B 1 640 ? 119.786 137.548 171.740 1.00 26.08 ?  640 MET B CE    1 
ATOM   10709 N  N     . ILE B 1 641 ? 117.067 138.376 166.383 1.00 28.94 ?  641 ILE B N     1 
ATOM   10710 C  CA    . ILE B 1 641 ? 117.540 139.178 165.261 1.00 21.13 ?  641 ILE B CA    1 
ATOM   10711 C  C     . ILE B 1 641 ? 116.559 140.298 164.944 1.00 19.87 ?  641 ILE B C     1 
ATOM   10712 O  O     . ILE B 1 641 ? 116.969 141.402 164.567 1.00 29.61 ?  641 ILE B O     1 
ATOM   10713 C  CB    . ILE B 1 641 ? 117.809 138.284 164.038 1.00 25.85 ?  641 ILE B CB    1 
ATOM   10714 C  CG1   . ILE B 1 641 ? 118.857 137.227 164.383 1.00 18.83 ?  641 ILE B CG1   1 
ATOM   10715 C  CG2   . ILE B 1 641 ? 118.294 139.113 162.861 1.00 18.72 ?  641 ILE B CG2   1 
ATOM   10716 C  CD1   . ILE B 1 641 ? 120.068 137.785 165.098 1.00 20.70 ?  641 ILE B CD1   1 
ATOM   10717 N  N     . ALA B 1 642 ? 115.257 140.048 165.097 1.00 17.45 ?  642 ALA B N     1 
ATOM   10718 C  CA    . ALA B 1 642 ? 114.270 141.101 164.897 1.00 20.38 ?  642 ALA B CA    1 
ATOM   10719 C  C     . ALA B 1 642 ? 114.345 142.148 165.998 1.00 21.19 ?  642 ALA B C     1 
ATOM   10720 O  O     . ALA B 1 642 ? 114.074 143.328 165.748 1.00 25.52 ?  642 ALA B O     1 
ATOM   10721 C  CB    . ALA B 1 642 ? 112.867 140.501 164.827 1.00 15.88 ?  642 ALA B CB    1 
ATOM   10722 N  N     . THR B 1 643 ? 114.690 141.737 167.218 1.00 21.94 ?  643 THR B N     1 
ATOM   10723 C  CA    . THR B 1 643 ? 114.947 142.708 168.275 1.00 18.28 ?  643 THR B CA    1 
ATOM   10724 C  C     . THR B 1 643 ? 116.133 143.595 167.923 1.00 24.19 ?  643 THR B C     1 
ATOM   10725 O  O     . THR B 1 643 ? 116.095 144.812 168.134 1.00 26.56 ?  643 THR B O     1 
ATOM   10726 C  CB    . THR B 1 643 ? 115.192 141.986 169.599 1.00 17.26 ?  643 THR B CB    1 
ATOM   10727 O  OG1   . THR B 1 643 ? 114.066 141.156 169.905 1.00 22.86 ?  643 THR B OG1   1 
ATOM   10728 C  CG2   . THR B 1 643 ? 115.396 142.985 170.717 1.00 17.83 ?  643 THR B CG2   1 
ATOM   10729 N  N     . ILE B 1 644 ? 117.200 142.999 167.389 1.00 22.78 ?  644 ILE B N     1 
ATOM   10730 C  CA    . ILE B 1 644 ? 118.349 143.790 166.963 1.00 10.33 ?  644 ILE B CA    1 
ATOM   10731 C  C     . ILE B 1 644 ? 118.014 144.600 165.715 1.00 16.72 ?  644 ILE B C     1 
ATOM   10732 O  O     . ILE B 1 644 ? 118.419 145.760 165.586 1.00 22.18 ?  644 ILE B O     1 
ATOM   10733 C  CB    . ILE B 1 644 ? 119.570 142.882 166.734 1.00 12.86 ?  644 ILE B CB    1 
ATOM   10734 C  CG1   . ILE B 1 644 ? 119.882 142.076 167.994 1.00 16.38 ?  644 ILE B CG1   1 
ATOM   10735 C  CG2   . ILE B 1 644 ? 120.772 143.706 166.326 1.00 8.54  ?  644 ILE B CG2   1 
ATOM   10736 C  CD1   . ILE B 1 644 ? 120.746 140.869 167.733 1.00 22.52 ?  644 ILE B CD1   1 
ATOM   10737 N  N     . GLN B 1 645 ? 117.267 144.002 164.780 1.00 12.43 ?  645 GLN B N     1 
ATOM   10738 C  CA    . GLN B 1 645 ? 117.024 144.638 163.487 1.00 13.88 ?  645 GLN B CA    1 
ATOM   10739 C  C     . GLN B 1 645 ? 116.277 145.957 163.624 1.00 17.48 ?  645 GLN B C     1 
ATOM   10740 O  O     . GLN B 1 645 ? 116.422 146.841 162.772 1.00 29.59 ?  645 GLN B O     1 
ATOM   10741 C  CB    . GLN B 1 645 ? 116.247 143.686 162.577 1.00 12.98 ?  645 GLN B CB    1 
ATOM   10742 C  CG    . GLN B 1 645 ? 116.042 144.194 161.163 1.00 3.84  ?  645 GLN B CG    1 
ATOM   10743 C  CD    . GLN B 1 645 ? 117.304 144.124 160.335 1.00 19.17 ?  645 GLN B CD    1 
ATOM   10744 O  OE1   . GLN B 1 645 ? 118.065 145.084 160.262 1.00 13.42 ?  645 GLN B OE1   1 
ATOM   10745 N  NE2   . GLN B 1 645 ? 117.531 142.981 159.700 1.00 16.27 ?  645 GLN B NE2   1 
ATOM   10746 N  N     . GLN B 1 646 ? 115.488 146.120 164.684 1.00 19.98 ?  646 GLN B N     1 
ATOM   10747 C  CA    . GLN B 1 646 ? 114.734 147.354 164.854 1.00 11.37 ?  646 GLN B CA    1 
ATOM   10748 C  C     . GLN B 1 646 ? 115.617 148.547 165.195 1.00 11.49 ?  646 GLN B C     1 
ATOM   10749 O  O     . GLN B 1 646 ? 115.127 149.678 165.175 1.00 15.53 ?  646 GLN B O     1 
ATOM   10750 C  CB    . GLN B 1 646 ? 113.661 147.170 165.926 1.00 19.79 ?  646 GLN B CB    1 
ATOM   10751 C  CG    . GLN B 1 646 ? 114.177 147.229 167.344 1.00 22.80 ?  646 GLN B CG    1 
ATOM   10752 C  CD    . GLN B 1 646 ? 113.105 146.905 168.358 1.00 27.77 ?  646 GLN B CD    1 
ATOM   10753 O  OE1   . GLN B 1 646 ? 113.210 145.929 169.099 1.00 26.85 ?  646 GLN B OE1   1 
ATOM   10754 N  NE2   . GLN B 1 646 ? 112.061 147.724 168.397 1.00 23.34 ?  646 GLN B NE2   1 
ATOM   10755 N  N     . HIS B 1 647 ? 116.895 148.329 165.496 1.00 29.18 ?  647 HIS B N     1 
ATOM   10756 C  CA    . HIS B 1 647 ? 117.828 149.416 165.752 1.00 12.41 ?  647 HIS B CA    1 
ATOM   10757 C  C     . HIS B 1 647 ? 118.933 149.506 164.711 1.00 13.61 ?  647 HIS B C     1 
ATOM   10758 O  O     . HIS B 1 647 ? 119.806 150.371 164.831 1.00 27.00 ?  647 HIS B O     1 
ATOM   10759 C  CB    . HIS B 1 647 ? 118.449 149.268 167.148 1.00 5.67  ?  647 HIS B CB    1 
ATOM   10760 C  CG    . HIS B 1 647 ? 117.444 149.070 168.238 1.00 14.52 ?  647 HIS B CG    1 
ATOM   10761 N  ND1   . HIS B 1 647 ? 116.506 150.024 168.566 1.00 18.16 ?  647 HIS B ND1   1 
ATOM   10762 C  CD2   . HIS B 1 647 ? 117.231 148.029 169.076 1.00 12.29 ?  647 HIS B CD2   1 
ATOM   10763 C  CE1   . HIS B 1 647 ? 115.757 149.578 169.559 1.00 20.52 ?  647 HIS B CE1   1 
ATOM   10764 N  NE2   . HIS B 1 647 ? 116.178 148.371 169.887 1.00 15.87 ?  647 HIS B NE2   1 
ATOM   10765 N  N     . ILE B 1 648 ? 118.918 148.648 163.698 1.00 14.96 ?  648 ILE B N     1 
ATOM   10766 C  CA    . ILE B 1 648 ? 119.919 148.638 162.638 1.00 16.22 ?  648 ILE B CA    1 
ATOM   10767 C  C     . ILE B 1 648 ? 119.252 149.168 161.376 1.00 14.31 ?  648 ILE B C     1 
ATOM   10768 O  O     . ILE B 1 648 ? 118.224 148.635 160.943 1.00 28.02 ?  648 ILE B O     1 
ATOM   10769 C  CB    . ILE B 1 648 ? 120.488 147.227 162.421 1.00 10.01 ?  648 ILE B CB    1 
ATOM   10770 C  CG1   . ILE B 1 648 ? 121.112 146.694 163.714 1.00 10.50 ?  648 ILE B CG1   1 
ATOM   10771 C  CG2   . ILE B 1 648 ? 121.513 147.223 161.305 1.00 3.67  ?  648 ILE B CG2   1 
ATOM   10772 C  CD1   . ILE B 1 648 ? 122.241 147.540 164.247 1.00 4.55  ?  648 ILE B CD1   1 
ATOM   10773 N  N     . ASP B 1 649 ? 119.827 150.222 160.790 1.00 7.88  ?  649 ASP B N     1 
ATOM   10774 C  CA    . ASP B 1 649 ? 119.195 150.837 159.626 1.00 9.36  ?  649 ASP B CA    1 
ATOM   10775 C  C     . ASP B 1 649 ? 119.349 149.978 158.379 1.00 7.99  ?  649 ASP B C     1 
ATOM   10776 O  O     . ASP B 1 649 ? 118.445 149.944 157.537 1.00 32.55 ?  649 ASP B O     1 
ATOM   10777 C  CB    . ASP B 1 649 ? 119.757 152.241 159.388 1.00 21.54 ?  649 ASP B CB    1 
ATOM   10778 C  CG    . ASP B 1 649 ? 121.271 152.273 159.353 1.00 16.61 ?  649 ASP B CG    1 
ATOM   10779 O  OD1   . ASP B 1 649 ? 121.882 152.566 160.398 1.00 20.43 ?  649 ASP B OD1   1 
ATOM   10780 O  OD2   . ASP B 1 649 ? 121.850 152.017 158.279 1.00 28.60 -1 649 ASP B OD2   1 
ATOM   10781 N  N     . GLN B 1 650 ? 120.474 149.291 158.237 1.00 10.05 ?  650 GLN B N     1 
ATOM   10782 C  CA    . GLN B 1 650 ? 120.658 148.300 157.189 1.00 2.07  ?  650 GLN B CA    1 
ATOM   10783 C  C     . GLN B 1 650 ? 120.248 146.934 157.735 1.00 5.15  ?  650 GLN B C     1 
ATOM   10784 O  O     . GLN B 1 650 ? 119.588 146.842 158.772 1.00 22.73 ?  650 GLN B O     1 
ATOM   10785 C  CB    . GLN B 1 650 ? 122.098 148.337 156.677 1.00 9.86  ?  650 GLN B CB    1 
ATOM   10786 C  CG    . GLN B 1 650 ? 122.495 149.662 156.072 1.00 8.84  ?  650 GLN B CG    1 
ATOM   10787 C  CD    . GLN B 1 650 ? 123.860 149.616 155.437 1.00 14.00 ?  650 GLN B CD    1 
ATOM   10788 O  OE1   . GLN B 1 650 ? 124.055 148.969 154.411 1.00 17.40 ?  650 GLN B OE1   1 
ATOM   10789 N  NE2   . GLN B 1 650 ? 124.818 150.309 156.038 1.00 8.23  ?  650 GLN B NE2   1 
ATOM   10790 N  N     . GLY B 1 651 ? 120.599 145.858 157.035 1.00 12.16 ?  651 GLY B N     1 
ATOM   10791 C  CA    . GLY B 1 651 ? 120.214 144.528 157.452 1.00 13.22 ?  651 GLY B CA    1 
ATOM   10792 C  C     . GLY B 1 651 ? 121.248 143.850 158.331 1.00 7.23  ?  651 GLY B C     1 
ATOM   10793 O  O     . GLY B 1 651 ? 122.270 144.416 158.710 1.00 12.16 ?  651 GLY B O     1 
ATOM   10794 N  N     . ILE B 1 652 ? 120.947 142.597 158.663 1.00 20.05 ?  652 ILE B N     1 
ATOM   10795 C  CA    . ILE B 1 652 ? 121.800 141.745 159.479 1.00 4.72  ?  652 ILE B CA    1 
ATOM   10796 C  C     . ILE B 1 652 ? 121.980 140.426 158.744 1.00 13.37 ?  652 ILE B C     1 
ATOM   10797 O  O     . ILE B 1 652 ? 121.008 139.864 158.228 1.00 24.03 ?  652 ILE B O     1 
ATOM   10798 C  CB    . ILE B 1 652 ? 121.202 141.501 160.878 1.00 2.58  ?  652 ILE B CB    1 
ATOM   10799 C  CG1   . ILE B 1 652 ? 120.954 142.823 161.603 1.00 3.36  ?  652 ILE B CG1   1 
ATOM   10800 C  CG2   . ILE B 1 652 ? 122.099 140.594 161.700 1.00 7.53  ?  652 ILE B CG2   1 
ATOM   10801 C  CD1   . ILE B 1 652 ? 120.184 142.666 162.886 1.00 8.68  ?  652 ILE B CD1   1 
ATOM   10802 N  N     . SER B 1 653 ? 123.213 139.935 158.690 1.00 14.90 ?  653 SER B N     1 
ATOM   10803 C  CA    . SER B 1 653 ? 123.488 138.637 158.081 1.00 13.87 ?  653 SER B CA    1 
ATOM   10804 C  C     . SER B 1 653 ? 122.899 137.551 158.971 1.00 20.31 ?  653 SER B C     1 
ATOM   10805 O  O     . SER B 1 653 ? 123.477 137.184 159.996 1.00 26.45 ?  653 SER B O     1 
ATOM   10806 C  CB    . SER B 1 653 ? 124.986 138.443 157.887 1.00 16.66 ?  653 SER B CB    1 
ATOM   10807 O  OG    . SER B 1 653 ? 125.367 138.758 156.562 1.00 22.31 ?  653 SER B OG    1 
ATOM   10808 N  N     . PHE B 1 654 ? 121.740 137.033 158.579 1.00 23.30 ?  654 PHE B N     1 
ATOM   10809 C  CA    . PHE B 1 654 ? 120.970 136.093 159.387 1.00 6.98  ?  654 PHE B CA    1 
ATOM   10810 C  C     . PHE B 1 654 ? 121.085 134.705 158.768 1.00 18.15 ?  654 PHE B C     1 
ATOM   10811 O  O     . PHE B 1 654 ? 120.441 134.415 157.755 1.00 27.86 ?  654 PHE B O     1 
ATOM   10812 C  CB    . PHE B 1 654 ? 119.514 136.541 159.481 1.00 13.53 ?  654 PHE B CB    1 
ATOM   10813 C  CG    . PHE B 1 654 ? 118.683 135.728 160.431 1.00 17.85 ?  654 PHE B CG    1 
ATOM   10814 C  CD1   . PHE B 1 654 ? 119.275 134.883 161.353 1.00 21.93 ?  654 PHE B CD1   1 
ATOM   10815 C  CD2   . PHE B 1 654 ? 117.306 135.816 160.405 1.00 20.97 ?  654 PHE B CD2   1 
ATOM   10816 C  CE1   . PHE B 1 654 ? 118.512 134.139 162.221 1.00 18.47 ?  654 PHE B CE1   1 
ATOM   10817 C  CE2   . PHE B 1 654 ? 116.538 135.076 161.274 1.00 24.46 ?  654 PHE B CE2   1 
ATOM   10818 C  CZ    . PHE B 1 654 ? 117.143 134.237 162.184 1.00 16.24 ?  654 PHE B CZ    1 
ATOM   10819 N  N     . THR B 1 655 ? 121.887 133.849 159.391 1.00 22.48 ?  655 THR B N     1 
ATOM   10820 C  CA    . THR B 1 655 ? 122.057 132.474 158.946 1.00 19.91 ?  655 THR B CA    1 
ATOM   10821 C  C     . THR B 1 655 ? 121.070 131.575 159.678 1.00 20.63 ?  655 THR B C     1 
ATOM   10822 O  O     . THR B 1 655 ? 120.946 131.645 160.904 1.00 29.03 ?  655 THR B O     1 
ATOM   10823 C  CB    . THR B 1 655 ? 123.489 132.001 159.196 1.00 29.28 ?  655 THR B CB    1 
ATOM   10824 O  OG1   . THR B 1 655 ? 124.396 132.778 158.406 1.00 35.51 ?  655 THR B OG1   1 
ATOM   10825 C  CG2   . THR B 1 655 ? 123.643 130.534 158.830 1.00 29.23 ?  655 THR B CG2   1 
ATOM   10826 N  N     . LEU B 1 656 ? 120.363 130.739 158.923 1.00 31.41 ?  656 LEU B N     1 
ATOM   10827 C  CA    . LEU B 1 656 ? 119.481 129.735 159.499 1.00 31.82 ?  656 LEU B CA    1 
ATOM   10828 C  C     . LEU B 1 656 ? 120.278 128.474 159.788 1.00 28.18 ?  656 LEU B C     1 
ATOM   10829 O  O     . LEU B 1 656 ? 120.960 127.946 158.906 1.00 33.03 ?  656 LEU B O     1 
ATOM   10830 C  CB    . LEU B 1 656 ? 118.320 129.420 158.557 1.00 34.25 ?  656 LEU B CB    1 
ATOM   10831 C  CG    . LEU B 1 656 ? 117.367 130.567 158.231 1.00 34.34 ?  656 LEU B CG    1 
ATOM   10832 C  CD1   . LEU B 1 656 ? 116.126 130.038 157.530 1.00 29.57 ?  656 LEU B CD1   1 
ATOM   10833 C  CD2   . LEU B 1 656 ? 116.996 131.337 159.487 1.00 25.37 ?  656 LEU B CD2   1 
ATOM   10834 N  N     . PHE B 1 657 ? 120.195 127.997 161.023 1.00 30.01 ?  657 PHE B N     1 
ATOM   10835 C  CA    . PHE B 1 657 ? 120.888 126.790 161.455 1.00 27.17 ?  657 PHE B CA    1 
ATOM   10836 C  C     . PHE B 1 657 ? 119.844 125.700 161.639 1.00 36.86 ?  657 PHE B C     1 
ATOM   10837 O  O     . PHE B 1 657 ? 119.031 125.761 162.566 1.00 39.95 ?  657 PHE B O     1 
ATOM   10838 C  CB    . PHE B 1 657 ? 121.671 127.046 162.738 1.00 31.39 ?  657 PHE B CB    1 
ATOM   10839 C  CG    . PHE B 1 657 ? 122.619 128.203 162.642 1.00 38.03 ?  657 PHE B CG    1 
ATOM   10840 C  CD1   . PHE B 1 657 ? 123.887 128.033 162.116 1.00 32.64 ?  657 PHE B CD1   1 
ATOM   10841 C  CD2   . PHE B 1 657 ? 122.239 129.463 163.070 1.00 35.57 ?  657 PHE B CD2   1 
ATOM   10842 C  CE1   . PHE B 1 657 ? 124.760 129.094 162.024 1.00 34.17 ?  657 PHE B CE1   1 
ATOM   10843 C  CE2   . PHE B 1 657 ? 123.109 130.529 162.979 1.00 34.07 ?  657 PHE B CE2   1 
ATOM   10844 C  CZ    . PHE B 1 657 ? 124.371 130.344 162.455 1.00 38.39 ?  657 PHE B CZ    1 
ATOM   10845 N  N     . LEU B 1 658 ? 119.871 124.707 160.757 1.00 40.65 ?  658 LEU B N     1 
ATOM   10846 C  CA    . LEU B 1 658 ? 118.831 123.694 160.683 1.00 41.19 ?  658 LEU B CA    1 
ATOM   10847 C  C     . LEU B 1 658 ? 119.404 122.321 160.998 1.00 45.56 ?  658 LEU B C     1 
ATOM   10848 O  O     . LEU B 1 658 ? 120.580 122.045 160.744 1.00 48.21 ?  658 LEU B O     1 
ATOM   10849 C  CB    . LEU B 1 658 ? 118.187 123.672 159.293 1.00 41.13 ?  658 LEU B CB    1 
ATOM   10850 C  CG    . LEU B 1 658 ? 118.013 125.032 158.617 1.00 40.87 ?  658 LEU B CG    1 
ATOM   10851 C  CD1   . LEU B 1 658 ? 117.918 124.863 157.114 1.00 38.06 ?  658 LEU B CD1   1 
ATOM   10852 C  CD2   . LEU B 1 658 ? 116.788 125.746 159.159 1.00 41.11 ?  658 LEU B CD2   1 
ATOM   10853 N  N     . LYS B 1 659 ? 118.563 121.467 161.566 1.00 49.14 ?  659 LYS B N     1 
ATOM   10854 C  CA    . LYS B 1 659 ? 118.905 120.068 161.756 1.00 50.62 ?  659 LYS B CA    1 
ATOM   10855 C  C     . LYS B 1 659 ? 118.597 119.279 160.489 1.00 52.29 ?  659 LYS B C     1 
ATOM   10856 O  O     . LYS B 1 659 ? 117.869 119.735 159.605 1.00 52.44 ?  659 LYS B O     1 
ATOM   10857 C  CB    . LYS B 1 659 ? 118.143 119.483 162.946 1.00 49.58 ?  659 LYS B CB    1 
ATOM   10858 C  CG    . LYS B 1 659 ? 118.491 120.128 164.273 1.00 52.09 ?  659 LYS B CG    1 
ATOM   10859 C  CD    . LYS B 1 659 ? 117.977 119.310 165.443 1.00 52.73 ?  659 LYS B CD    1 
ATOM   10860 C  CE    . LYS B 1 659 ? 118.413 119.915 166.768 1.00 51.17 ?  659 LYS B CE    1 
ATOM   10861 N  NZ    . LYS B 1 659 ? 118.300 118.944 167.891 1.00 53.28 1  659 LYS B NZ    1 
ATOM   10862 N  N     . ASP B 1 660 ? 119.176 118.079 160.405 1.00 57.27 ?  660 ASP B N     1 
ATOM   10863 C  CA    . ASP B 1 660 ? 118.899 117.214 159.264 1.00 56.83 ?  660 ASP B CA    1 
ATOM   10864 C  C     . ASP B 1 660 ? 117.454 116.733 159.265 1.00 55.41 ?  660 ASP B C     1 
ATOM   10865 O  O     . ASP B 1 660 ? 116.897 116.444 158.201 1.00 55.37 ?  660 ASP B O     1 
ATOM   10866 C  CB    . ASP B 1 660 ? 119.857 116.023 159.258 1.00 57.50 ?  660 ASP B CB    1 
ATOM   10867 C  CG    . ASP B 1 660 ? 119.863 115.270 160.575 1.00 58.83 ?  660 ASP B CG    1 
ATOM   10868 O  OD1   . ASP B 1 660 ? 119.398 115.833 161.589 1.00 57.20 ?  660 ASP B OD1   1 
ATOM   10869 O  OD2   . ASP B 1 660 ? 120.336 114.114 160.597 1.00 59.06 -1 660 ASP B OD2   1 
ATOM   10870 N  N     . THR B 1 661 ? 116.834 116.645 160.442 1.00 52.39 ?  661 THR B N     1 
ATOM   10871 C  CA    . THR B 1 661 ? 115.455 116.187 160.541 1.00 53.63 ?  661 THR B CA    1 
ATOM   10872 C  C     . THR B 1 661 ? 114.447 117.237 160.096 1.00 56.03 ?  661 THR B C     1 
ATOM   10873 O  O     . THR B 1 661 ? 113.287 116.892 159.845 1.00 54.76 ?  661 THR B O     1 
ATOM   10874 C  CB    . THR B 1 661 ? 115.145 115.764 161.978 1.00 54.73 ?  661 THR B CB    1 
ATOM   10875 O  OG1   . THR B 1 661 ? 115.387 116.866 162.862 1.00 52.56 ?  661 THR B OG1   1 
ATOM   10876 C  CG2   . THR B 1 661 ? 116.021 114.593 162.386 1.00 54.63 ?  661 THR B CG2   1 
ATOM   10877 N  N     . MET B 1 662 ? 114.855 118.498 159.997 1.00 55.39 ?  662 MET B N     1 
ATOM   10878 C  CA    . MET B 1 662 ? 113.931 119.552 159.606 1.00 51.19 ?  662 MET B CA    1 
ATOM   10879 C  C     . MET B 1 662 ? 113.512 119.385 158.151 1.00 52.53 ?  662 MET B C     1 
ATOM   10880 O  O     . MET B 1 662 ? 114.335 119.091 157.279 1.00 53.26 ?  662 MET B O     1 
ATOM   10881 C  CB    . MET B 1 662 ? 114.568 120.923 159.821 1.00 51.81 ?  662 MET B CB    1 
ATOM   10882 C  CG    . MET B 1 662 ? 114.167 121.583 161.129 1.00 51.85 ?  662 MET B CG    1 
ATOM   10883 S  SD    . MET B 1 662 ? 115.131 123.058 161.502 1.00 60.76 ?  662 MET B SD    1 
ATOM   10884 C  CE    . MET B 1 662 ? 114.012 123.917 162.604 1.00 51.82 ?  662 MET B CE    1 
ATOM   10885 N  N     . THR B 1 663 ? 112.221 119.572 157.894 1.00 48.30 ?  663 THR B N     1 
ATOM   10886 C  CA    . THR B 1 663 ? 111.660 119.378 156.569 1.00 45.04 ?  663 THR B CA    1 
ATOM   10887 C  C     . THR B 1 663 ? 111.664 120.690 155.788 1.00 46.54 ?  663 THR B C     1 
ATOM   10888 O  O     . THR B 1 663 ? 112.118 121.732 156.264 1.00 49.48 ?  663 THR B O     1 
ATOM   10889 C  CB    . THR B 1 663 ? 110.241 118.820 156.669 1.00 41.89 ?  663 THR B CB    1 
ATOM   10890 O  OG1   . THR B 1 663 ? 109.554 119.450 157.757 1.00 42.37 ?  663 THR B OG1   1 
ATOM   10891 C  CG2   . THR B 1 663 ? 110.273 117.322 156.910 1.00 44.20 ?  663 THR B CG2   1 
ATOM   10892 N  N     . THR B 1 664 ? 111.152 120.630 154.558 1.00 41.28 ?  664 THR B N     1 
ATOM   10893 C  CA    . THR B 1 664 ? 110.934 121.845 153.781 1.00 38.99 ?  664 THR B CA    1 
ATOM   10894 C  C     . THR B 1 664 ? 109.908 122.746 154.460 1.00 38.44 ?  664 THR B C     1 
ATOM   10895 O  O     . THR B 1 664 ? 110.058 123.975 154.475 1.00 41.92 ?  664 THR B O     1 
ATOM   10896 C  CB    . THR B 1 664 ? 110.492 121.474 152.362 1.00 41.98 ?  664 THR B CB    1 
ATOM   10897 O  OG1   . THR B 1 664 ? 111.636 121.091 151.588 1.00 40.54 ?  664 THR B OG1   1 
ATOM   10898 C  CG2   . THR B 1 664 ? 109.779 122.629 151.678 1.00 41.48 ?  664 THR B CG2   1 
ATOM   10899 N  N     . ARG B 1 665 ? 108.870 122.147 155.047 1.00 39.22 ?  665 ARG B N     1 
ATOM   10900 C  CA    . ARG B 1 665 ? 107.847 122.930 155.731 1.00 38.75 ?  665 ARG B CA    1 
ATOM   10901 C  C     . ARG B 1 665 ? 108.430 123.692 156.912 1.00 41.96 ?  665 ARG B C     1 
ATOM   10902 O  O     . ARG B 1 665 ? 108.019 124.822 157.187 1.00 47.88 ?  665 ARG B O     1 
ATOM   10903 C  CB    . ARG B 1 665 ? 106.710 122.021 156.194 1.00 40.49 ?  665 ARG B CB    1 
ATOM   10904 C  CG    . ARG B 1 665 ? 105.404 122.752 156.446 1.00 37.78 ?  665 ARG B CG    1 
ATOM   10905 C  CD    . ARG B 1 665 ? 104.511 121.972 157.392 1.00 41.85 ?  665 ARG B CD    1 
ATOM   10906 N  NE    . ARG B 1 665 ? 104.797 122.280 158.787 1.00 46.72 ?  665 ARG B NE    1 
ATOM   10907 C  CZ    . ARG B 1 665 ? 104.004 121.966 159.801 1.00 48.71 ?  665 ARG B CZ    1 
ATOM   10908 N  NH1   . ARG B 1 665 ? 102.864 121.323 159.614 1.00 43.92 1  665 ARG B NH1   1 
ATOM   10909 N  NH2   . ARG B 1 665 ? 104.364 122.307 161.036 1.00 46.34 ?  665 ARG B NH2   1 
ATOM   10910 N  N     . ASP B 1 666 ? 109.384 123.093 157.627 1.00 39.87 ?  666 ASP B N     1 
ATOM   10911 C  CA    . ASP B 1 666 ? 109.988 123.781 158.764 1.00 35.12 ?  666 ASP B CA    1 
ATOM   10912 C  C     . ASP B 1 666 ? 110.812 124.983 158.316 1.00 40.01 ?  666 ASP B C     1 
ATOM   10913 O  O     . ASP B 1 666 ? 110.753 126.050 158.939 1.00 42.48 ?  666 ASP B O     1 
ATOM   10914 C  CB    . ASP B 1 666 ? 110.847 122.808 159.569 1.00 42.29 ?  666 ASP B CB    1 
ATOM   10915 C  CG    . ASP B 1 666 ? 110.030 121.706 160.208 1.00 49.42 ?  666 ASP B CG    1 
ATOM   10916 O  OD1   . ASP B 1 666 ? 108.906 121.993 160.670 1.00 46.16 ?  666 ASP B OD1   1 
ATOM   10917 O  OD2   . ASP B 1 666 ? 110.510 120.555 160.253 1.00 50.89 -1 666 ASP B OD2   1 
ATOM   10918 N  N     . LEU B 1 667 ? 111.583 124.834 157.237 1.00 35.25 ?  667 LEU B N     1 
ATOM   10919 C  CA    . LEU B 1 667 ? 112.337 125.965 156.708 1.00 28.35 ?  667 LEU B CA    1 
ATOM   10920 C  C     . LEU B 1 667 ? 111.399 127.065 156.228 1.00 30.94 ?  667 LEU B C     1 
ATOM   10921 O  O     . LEU B 1 667 ? 111.649 128.254 156.461 1.00 32.33 ?  667 LEU B O     1 
ATOM   10922 C  CB    . LEU B 1 667 ? 113.250 125.501 155.574 1.00 31.84 ?  667 LEU B CB    1 
ATOM   10923 C  CG    . LEU B 1 667 ? 114.630 126.152 155.441 1.00 33.11 ?  667 LEU B CG    1 
ATOM   10924 C  CD1   . LEU B 1 667 ? 115.455 125.413 154.406 1.00 33.42 ?  667 LEU B CD1   1 
ATOM   10925 C  CD2   . LEU B 1 667 ? 114.531 127.623 155.083 1.00 38.02 ?  667 LEU B CD2   1 
ATOM   10926 N  N     . ASN B 1 668 ? 110.310 126.686 155.556 1.00 36.62 ?  668 ASN B N     1 
ATOM   10927 C  CA    . ASN B 1 668 ? 109.332 127.674 155.117 1.00 23.50 ?  668 ASN B CA    1 
ATOM   10928 C  C     . ASN B 1 668 ? 108.690 128.380 156.303 1.00 22.91 ?  668 ASN B C     1 
ATOM   10929 O  O     . ASN B 1 668 ? 108.443 129.589 156.255 1.00 31.40 ?  668 ASN B O     1 
ATOM   10930 C  CB    . ASN B 1 668 ? 108.267 127.008 154.249 1.00 28.51 ?  668 ASN B CB    1 
ATOM   10931 C  CG    . ASN B 1 668 ? 108.687 126.893 152.803 1.00 33.12 ?  668 ASN B CG    1 
ATOM   10932 O  OD1   . ASN B 1 668 ? 108.414 125.891 152.144 1.00 40.18 ?  668 ASN B OD1   1 
ATOM   10933 N  ND2   . ASN B 1 668 ? 109.358 127.921 152.298 1.00 30.35 ?  668 ASN B ND2   1 
ATOM   10934 N  N     . ARG B 1 669 ? 108.402 127.640 157.373 1.00 31.32 ?  669 ARG B N     1 
ATOM   10935 C  CA    . ARG B 1 669 ? 107.839 128.250 158.572 1.00 32.98 ?  669 ARG B CA    1 
ATOM   10936 C  C     . ARG B 1 669 ? 108.812 129.241 159.191 1.00 29.08 ?  669 ARG B C     1 
ATOM   10937 O  O     . ARG B 1 669 ? 108.409 130.319 159.639 1.00 28.03 ?  669 ARG B O     1 
ATOM   10938 C  CB    . ARG B 1 669 ? 107.462 127.168 159.582 1.00 32.09 ?  669 ARG B CB    1 
ATOM   10939 C  CG    . ARG B 1 669 ? 105.975 126.906 159.675 1.00 28.78 ?  669 ARG B CG    1 
ATOM   10940 C  CD    . ARG B 1 669 ? 105.657 125.935 160.799 1.00 33.13 ?  669 ARG B CD    1 
ATOM   10941 N  NE    . ARG B 1 669 ? 105.622 126.584 162.105 1.00 35.06 ?  669 ARG B NE    1 
ATOM   10942 C  CZ    . ARG B 1 669 ? 104.701 127.457 162.491 1.00 36.71 ?  669 ARG B CZ    1 
ATOM   10943 N  NH1   . ARG B 1 669 ? 103.704 127.809 161.696 1.00 35.18 1  669 ARG B NH1   1 
ATOM   10944 N  NH2   . ARG B 1 669 ? 104.778 127.985 163.709 1.00 38.29 ?  669 ARG B NH2   1 
ATOM   10945 N  N     . ILE B 1 670 ? 110.100 128.891 159.229 1.00 25.86 ?  670 ILE B N     1 
ATOM   10946 C  CA    . ILE B 1 670 ? 111.101 129.818 159.750 1.00 25.29 ?  670 ILE B CA    1 
ATOM   10947 C  C     . ILE B 1 670 ? 111.157 131.078 158.894 1.00 24.13 ?  670 ILE B C     1 
ATOM   10948 O  O     . ILE B 1 670 ? 111.208 132.198 159.416 1.00 27.90 ?  670 ILE B O     1 
ATOM   10949 C  CB    . ILE B 1 670 ? 112.477 129.135 159.841 1.00 32.05 ?  670 ILE B CB    1 
ATOM   10950 C  CG1   . ILE B 1 670 ? 112.442 127.987 160.849 1.00 31.60 ?  670 ILE B CG1   1 
ATOM   10951 C  CG2   . ILE B 1 670 ? 113.546 130.140 160.234 1.00 28.90 ?  670 ILE B CG2   1 
ATOM   10952 C  CD1   . ILE B 1 670 ? 113.492 126.933 160.600 1.00 27.50 ?  670 ILE B CD1   1 
ATOM   10953 N  N     . ASP B 1 671 ? 111.140 130.917 157.568 1.00 25.07 ?  671 ASP B N     1 
ATOM   10954 C  CA    . ASP B 1 671 ? 111.175 132.077 156.679 1.00 20.62 ?  671 ASP B CA    1 
ATOM   10955 C  C     . ASP B 1 671 ? 109.944 132.958 156.859 1.00 21.54 ?  671 ASP B C     1 
ATOM   10956 O  O     . ASP B 1 671 ? 110.050 134.190 156.884 1.00 30.77 ?  671 ASP B O     1 
ATOM   10957 C  CB    . ASP B 1 671 ? 111.298 131.624 155.225 1.00 21.88 ?  671 ASP B CB    1 
ATOM   10958 C  CG    . ASP B 1 671 ? 112.522 130.765 154.981 1.00 40.20 ?  671 ASP B CG    1 
ATOM   10959 O  OD1   . ASP B 1 671 ? 113.463 130.822 155.798 1.00 39.79 ?  671 ASP B OD1   1 
ATOM   10960 O  OD2   . ASP B 1 671 ? 112.542 130.029 153.971 1.00 39.34 -1 671 ASP B OD2   1 
ATOM   10961 N  N     . LEU B 1 672 ? 108.767 132.346 156.993 1.00 21.76 ?  672 LEU B N     1 
ATOM   10962 C  CA    . LEU B 1 672 ? 107.540 133.120 157.140 1.00 16.89 ?  672 LEU B CA    1 
ATOM   10963 C  C     . LEU B 1 672 ? 107.459 133.799 158.499 1.00 18.59 ?  672 LEU B C     1 
ATOM   10964 O  O     . LEU B 1 672 ? 106.900 134.895 158.607 1.00 24.78 ?  672 LEU B O     1 
ATOM   10965 C  CB    . LEU B 1 672 ? 106.323 132.224 156.919 1.00 24.55 ?  672 LEU B CB    1 
ATOM   10966 C  CG    . LEU B 1 672 ? 106.159 131.679 155.501 1.00 24.78 ?  672 LEU B CG    1 
ATOM   10967 C  CD1   . LEU B 1 672 ? 105.209 130.494 155.489 1.00 20.61 ?  672 LEU B CD1   1 
ATOM   10968 C  CD2   . LEU B 1 672 ? 105.683 132.771 154.557 1.00 23.39 ?  672 LEU B CD2   1 
ATOM   10969 N  N     . TYR B 1 673 ? 107.997 133.172 159.546 1.00 22.69 ?  673 TYR B N     1 
ATOM   10970 C  CA    . TYR B 1 673 ? 108.040 133.828 160.847 1.00 14.92 ?  673 TYR B CA    1 
ATOM   10971 C  C     . TYR B 1 673 ? 109.049 134.967 160.852 1.00 18.79 ?  673 TYR B C     1 
ATOM   10972 O  O     . TYR B 1 673 ? 108.835 135.992 161.509 1.00 25.74 ?  673 TYR B O     1 
ATOM   10973 C  CB    . TYR B 1 673 ? 108.369 132.816 161.940 1.00 19.00 ?  673 TYR B CB    1 
ATOM   10974 C  CG    . TYR B 1 673 ? 108.397 133.416 163.325 1.00 20.29 ?  673 TYR B CG    1 
ATOM   10975 C  CD1   . TYR B 1 673 ? 107.252 133.958 163.889 1.00 22.11 ?  673 TYR B CD1   1 
ATOM   10976 C  CD2   . TYR B 1 673 ? 109.567 133.440 164.067 1.00 15.22 ?  673 TYR B CD2   1 
ATOM   10977 C  CE1   . TYR B 1 673 ? 107.272 134.507 165.152 1.00 20.83 ?  673 TYR B CE1   1 
ATOM   10978 C  CE2   . TYR B 1 673 ? 109.598 133.986 165.330 1.00 24.30 ?  673 TYR B CE2   1 
ATOM   10979 C  CZ    . TYR B 1 673 ? 108.448 134.517 165.869 1.00 25.45 ?  673 TYR B CZ    1 
ATOM   10980 O  OH    . TYR B 1 673 ? 108.476 135.063 167.130 1.00 29.84 ?  673 TYR B OH    1 
ATOM   10981 N  N     . ALA B 1 674 ? 110.162 134.801 160.136 1.00 21.72 ?  674 ALA B N     1 
ATOM   10982 C  CA    . ALA B 1 674 ? 111.103 135.902 159.968 1.00 12.28 ?  674 ALA B CA    1 
ATOM   10983 C  C     . ALA B 1 674 ? 110.449 137.068 159.241 1.00 17.86 ?  674 ALA B C     1 
ATOM   10984 O  O     . ALA B 1 674 ? 110.598 138.226 159.645 1.00 30.35 ?  674 ALA B O     1 
ATOM   10985 C  CB    . ALA B 1 674 ? 112.341 135.418 159.216 1.00 10.16 ?  674 ALA B CB    1 
ATOM   10986 N  N     . HIS B 1 675 ? 109.702 136.777 158.176 1.00 15.42 ?  675 HIS B N     1 
ATOM   10987 C  CA    . HIS B 1 675 ? 108.964 137.825 157.479 1.00 16.56 ?  675 HIS B CA    1 
ATOM   10988 C  C     . HIS B 1 675 ? 107.945 138.487 158.399 1.00 21.20 ?  675 HIS B C     1 
ATOM   10989 O  O     . HIS B 1 675 ? 107.775 139.710 158.373 1.00 26.90 ?  675 HIS B O     1 
ATOM   10990 C  CB    . HIS B 1 675 ? 108.278 137.243 156.245 1.00 18.38 ?  675 HIS B CB    1 
ATOM   10991 C  CG    . HIS B 1 675 ? 107.365 138.206 155.553 1.00 21.58 ?  675 HIS B CG    1 
ATOM   10992 N  ND1   . HIS B 1 675 ? 106.016 138.280 155.825 1.00 27.58 ?  675 HIS B ND1   1 
ATOM   10993 C  CD2   . HIS B 1 675 ? 107.608 139.139 154.603 1.00 15.77 ?  675 HIS B CD2   1 
ATOM   10994 C  CE1   . HIS B 1 675 ? 105.467 139.216 155.073 1.00 25.50 ?  675 HIS B CE1   1 
ATOM   10995 N  NE2   . HIS B 1 675 ? 106.412 139.752 154.322 1.00 29.27 ?  675 HIS B NE2   1 
ATOM   10996 N  N     . HIS B 1 676 ? 107.257 137.690 159.217 1.00 22.09 ?  676 HIS B N     1 
ATOM   10997 C  CA    . HIS B 1 676 ? 106.251 138.228 160.127 1.00 20.05 ?  676 HIS B CA    1 
ATOM   10998 C  C     . HIS B 1 676 ? 106.880 139.119 161.190 1.00 26.00 ?  676 HIS B C     1 
ATOM   10999 O  O     . HIS B 1 676 ? 106.291 140.130 161.587 1.00 25.33 ?  676 HIS B O     1 
ATOM   11000 C  CB    . HIS B 1 676 ? 105.479 137.080 160.775 1.00 24.17 ?  676 HIS B CB    1 
ATOM   11001 C  CG    . HIS B 1 676 ? 104.551 137.515 161.867 1.00 22.97 ?  676 HIS B CG    1 
ATOM   11002 N  ND1   . HIS B 1 676 ? 103.474 138.345 161.642 1.00 21.33 ?  676 HIS B ND1   1 
ATOM   11003 C  CD2   . HIS B 1 676 ? 104.538 137.232 163.190 1.00 25.21 ?  676 HIS B CD2   1 
ATOM   11004 C  CE1   . HIS B 1 676 ? 102.838 138.555 162.780 1.00 28.69 ?  676 HIS B CE1   1 
ATOM   11005 N  NE2   . HIS B 1 676 ? 103.464 137.892 163.735 1.00 27.27 ?  676 HIS B NE2   1 
ATOM   11006 N  N     . ARG B 1 677 ? 108.071 138.763 161.660 1.00 24.54 ?  677 ARG B N     1 
ATOM   11007 C  CA    . ARG B 1 677 ? 108.724 139.474 162.749 1.00 19.48 ?  677 ARG B CA    1 
ATOM   11008 C  C     . ARG B 1 677 ? 109.526 140.680 162.282 1.00 23.24 ?  677 ARG B C     1 
ATOM   11009 O  O     . ARG B 1 677 ? 110.154 141.345 163.112 1.00 30.96 ?  677 ARG B O     1 
ATOM   11010 C  CB    . ARG B 1 677 ? 109.635 138.521 163.524 1.00 19.00 ?  677 ARG B CB    1 
ATOM   11011 C  CG    . ARG B 1 677 ? 108.904 137.654 164.524 1.00 19.85 ?  677 ARG B CG    1 
ATOM   11012 C  CD    . ARG B 1 677 ? 108.352 138.481 165.669 1.00 23.48 ?  677 ARG B CD    1 
ATOM   11013 N  NE    . ARG B 1 677 ? 109.358 138.714 166.698 1.00 30.10 ?  677 ARG B NE    1 
ATOM   11014 C  CZ    . ARG B 1 677 ? 109.750 139.914 167.100 1.00 34.53 ?  677 ARG B CZ    1 
ATOM   11015 N  NH1   . ARG B 1 677 ? 109.239 141.018 166.582 1.00 29.29 1  677 ARG B NH1   1 
ATOM   11016 N  NH2   . ARG B 1 677 ? 110.681 140.009 168.044 1.00 29.06 ?  677 ARG B NH2   1 
ATOM   11017 N  N     . GLY B 1 678 ? 109.523 140.979 160.988 1.00 22.05 ?  678 GLY B N     1 
ATOM   11018 C  CA    . GLY B 1 678 ? 110.239 142.126 160.477 1.00 12.98 ?  678 GLY B CA    1 
ATOM   11019 C  C     . GLY B 1 678 ? 111.661 141.864 160.045 1.00 16.33 ?  678 GLY B C     1 
ATOM   11020 O  O     . GLY B 1 678 ? 112.420 142.822 159.865 1.00 24.40 ?  678 GLY B O     1 
ATOM   11021 N  N     . ILE B 1 679 ? 112.051 140.599 159.879 1.00 18.05 ?  679 ILE B N     1 
ATOM   11022 C  CA    . ILE B 1 679 ? 113.391 140.291 159.396 1.00 15.19 ?  679 ILE B CA    1 
ATOM   11023 C  C     . ILE B 1 679 ? 113.529 140.794 157.968 1.00 21.06 ?  679 ILE B C     1 
ATOM   11024 O  O     . ILE B 1 679 ? 112.646 140.582 157.129 1.00 28.13 ?  679 ILE B O     1 
ATOM   11025 C  CB    . ILE B 1 679 ? 113.663 138.783 159.498 1.00 13.44 ?  679 ILE B CB    1 
ATOM   11026 C  CG1   . ILE B 1 679 ? 113.751 138.352 160.965 1.00 13.99 ?  679 ILE B CG1   1 
ATOM   11027 C  CG2   . ILE B 1 679 ? 114.924 138.403 158.745 1.00 15.28 ?  679 ILE B CG2   1 
ATOM   11028 C  CD1   . ILE B 1 679 ? 114.862 139.009 161.723 1.00 18.66 ?  679 ILE B CD1   1 
ATOM   11029 N  N     . LYS B 1 680 ? 114.633 141.481 157.691 1.00 10.64 ?  680 LYS B N     1 
ATOM   11030 C  CA    . LYS B 1 680 ? 114.844 142.077 156.379 1.00 5.62  ?  680 LYS B CA    1 
ATOM   11031 C  C     . LYS B 1 680 ? 115.458 141.092 155.390 1.00 0.15  ?  680 LYS B C     1 
ATOM   11032 O  O     . LYS B 1 680 ? 115.008 140.998 154.247 1.00 19.15 ?  680 LYS B O     1 
ATOM   11033 C  CB    . LYS B 1 680 ? 115.730 143.316 156.507 1.00 11.81 ?  680 LYS B CB    1 
ATOM   11034 C  CG    . LYS B 1 680 ? 115.115 144.446 157.301 1.00 0.00  ?  680 LYS B CG    1 
ATOM   11035 C  CD    . LYS B 1 680 ? 115.997 145.676 157.253 1.00 2.10  ?  680 LYS B CD    1 
ATOM   11036 C  CE    . LYS B 1 680 ? 115.558 146.707 158.268 1.00 12.27 ?  680 LYS B CE    1 
ATOM   11037 N  NZ    . LYS B 1 680 ? 116.365 147.951 158.187 1.00 15.62 1  680 LYS B NZ    1 
ATOM   11038 N  N     . THR B 1 681 ? 116.487 140.364 155.810 1.00 6.84  ?  681 THR B N     1 
ATOM   11039 C  CA    . THR B 1 681 ? 117.173 139.427 154.935 1.00 7.07  ?  681 THR B CA    1 
ATOM   11040 C  C     . THR B 1 681 ? 117.454 138.138 155.689 1.00 12.62 ?  681 THR B C     1 
ATOM   11041 O  O     . THR B 1 681 ? 117.595 138.132 156.914 1.00 25.64 ?  681 THR B O     1 
ATOM   11042 C  CB    . THR B 1 681 ? 118.493 140.004 154.393 1.00 13.07 ?  681 THR B CB    1 
ATOM   11043 O  OG1   . THR B 1 681 ? 119.249 140.578 155.467 1.00 29.37 ?  681 THR B OG1   1 
ATOM   11044 C  CG2   . THR B 1 681 ? 118.233 141.068 153.343 1.00 7.92  ?  681 THR B CG2   1 
ATOM   11045 N  N     . ILE B 1 682 ? 117.532 137.040 154.942 1.00 13.30 ?  682 ILE B N     1 
ATOM   11046 C  CA    . ILE B 1 682 ? 117.962 135.750 155.464 1.00 8.69  ?  682 ILE B CA    1 
ATOM   11047 C  C     . ILE B 1 682 ? 119.180 135.308 154.666 1.00 17.51 ?  682 ILE B C     1 
ATOM   11048 O  O     . ILE B 1 682 ? 119.123 135.223 153.435 1.00 13.41 ?  682 ILE B O     1 
ATOM   11049 C  CB    . ILE B 1 682 ? 116.842 134.698 155.389 1.00 11.16 ?  682 ILE B CB    1 
ATOM   11050 C  CG1   . ILE B 1 682 ? 115.593 135.198 156.114 1.00 19.69 ?  682 ILE B CG1   1 
ATOM   11051 C  CG2   . ILE B 1 682 ? 117.311 133.400 155.999 1.00 18.50 ?  682 ILE B CG2   1 
ATOM   11052 C  CD1   . ILE B 1 682 ? 114.508 134.157 156.249 1.00 21.11 ?  682 ILE B CD1   1 
ATOM   11053 N  N     . TYR B 1 683 ? 120.279 135.032 155.367 1.00 23.45 ?  683 TYR B N     1 
ATOM   11054 C  CA    . TYR B 1 683 ? 121.552 134.791 154.690 1.00 18.72 ?  683 TYR B CA    1 
ATOM   11055 C  C     . TYR B 1 683 ? 121.680 133.352 154.200 1.00 21.31 ?  683 TYR B C     1 
ATOM   11056 O  O     . TYR B 1 683 ? 121.715 133.094 152.995 1.00 36.30 ?  683 TYR B O     1 
ATOM   11057 C  CB    . TYR B 1 683 ? 122.707 135.148 155.630 1.00 18.95 ?  683 TYR B CB    1 
ATOM   11058 C  CG    . TYR B 1 683 ? 124.068 135.159 154.978 1.00 13.76 ?  683 TYR B CG    1 
ATOM   11059 C  CD1   . TYR B 1 683 ? 124.203 135.344 153.610 1.00 10.60 ?  683 TYR B CD1   1 
ATOM   11060 C  CD2   . TYR B 1 683 ? 125.220 134.993 155.734 1.00 10.01 ?  683 TYR B CD2   1 
ATOM   11061 C  CE1   . TYR B 1 683 ? 125.442 135.357 153.014 1.00 19.38 ?  683 TYR B CE1   1 
ATOM   11062 C  CE2   . TYR B 1 683 ? 126.466 135.007 155.144 1.00 19.11 ?  683 TYR B CE2   1 
ATOM   11063 C  CZ    . TYR B 1 683 ? 126.570 135.191 153.784 1.00 21.30 ?  683 TYR B CZ    1 
ATOM   11064 O  OH    . TYR B 1 683 ? 127.809 135.205 153.187 1.00 23.65 ?  683 TYR B OH    1 
ATOM   11065 N  N     . TYR B 1 684 ? 121.725 132.397 155.121 1.00 29.13 ?  684 TYR B N     1 
ATOM   11066 C  CA    . TYR B 1 684 ? 122.114 131.044 154.767 1.00 22.22 ?  684 TYR B CA    1 
ATOM   11067 C  C     . TYR B 1 684 ? 121.246 130.045 155.508 1.00 37.02 ?  684 TYR B C     1 
ATOM   11068 O  O     . TYR B 1 684 ? 120.776 130.307 156.617 1.00 37.92 ?  684 TYR B O     1 
ATOM   11069 C  CB    . TYR B 1 684 ? 123.587 130.777 155.099 1.00 24.34 ?  684 TYR B CB    1 
ATOM   11070 C  CG    . TYR B 1 684 ? 124.526 130.922 153.929 1.00 25.68 ?  684 TYR B CG    1 
ATOM   11071 C  CD1   . TYR B 1 684 ? 124.169 130.471 152.667 1.00 26.99 ?  684 TYR B CD1   1 
ATOM   11072 C  CD2   . TYR B 1 684 ? 125.772 131.508 154.087 1.00 30.41 ?  684 TYR B CD2   1 
ATOM   11073 C  CE1   . TYR B 1 684 ? 125.027 130.601 151.594 1.00 33.90 ?  684 TYR B CE1   1 
ATOM   11074 C  CE2   . TYR B 1 684 ? 126.638 131.644 153.022 1.00 25.07 ?  684 TYR B CE2   1 
ATOM   11075 C  CZ    . TYR B 1 684 ? 126.261 131.189 151.779 1.00 30.64 ?  684 TYR B CZ    1 
ATOM   11076 O  OH    . TYR B 1 684 ? 127.121 131.323 150.714 1.00 35.44 ?  684 TYR B OH    1 
ATOM   11077 N  N     . ALA B 1 685 ? 121.043 128.896 154.879 1.00 37.12 ?  685 ALA B N     1 
ATOM   11078 C  CA    . ALA B 1 685 ? 120.398 127.749 155.504 1.00 33.67 ?  685 ALA B CA    1 
ATOM   11079 C  C     . ALA B 1 685 ? 121.492 126.709 155.729 1.00 34.24 ?  685 ALA B C     1 
ATOM   11080 O  O     . ALA B 1 685 ? 121.844 125.948 154.826 1.00 42.25 ?  685 ALA B O     1 
ATOM   11081 C  CB    . ALA B 1 685 ? 119.267 127.212 154.639 1.00 31.43 ?  685 ALA B CB    1 
ATOM   11082 N  N     . ARG B 1 686 ? 122.036 126.688 156.942 1.00 32.67 ?  686 ARG B N     1 
ATOM   11083 C  CA    . ARG B 1 686 ? 123.087 125.746 157.303 1.00 38.58 ?  686 ARG B CA    1 
ATOM   11084 C  C     . ARG B 1 686 ? 122.462 124.550 158.006 1.00 41.88 ?  686 ARG B C     1 
ATOM   11085 O  O     . ARG B 1 686 ? 121.807 124.704 159.043 1.00 42.46 ?  686 ARG B O     1 
ATOM   11086 C  CB    . ARG B 1 686 ? 124.130 126.415 158.196 1.00 40.04 ?  686 ARG B CB    1 
ATOM   11087 C  CG    . ARG B 1 686 ? 125.180 127.197 157.434 1.00 40.60 ?  686 ARG B CG    1 
ATOM   11088 C  CD    . ARG B 1 686 ? 126.432 127.396 158.269 1.00 44.30 ?  686 ARG B CD    1 
ATOM   11089 N  NE    . ARG B 1 686 ? 127.312 126.236 158.222 1.00 46.43 ?  686 ARG B NE    1 
ATOM   11090 C  CZ    . ARG B 1 686 ? 128.636 126.303 158.158 1.00 48.20 ?  686 ARG B CZ    1 
ATOM   11091 N  NH1   . ARG B 1 686 ? 129.267 127.464 158.111 1.00 43.79 1  686 ARG B NH1   1 
ATOM   11092 N  NH2   . ARG B 1 686 ? 129.342 125.176 158.135 1.00 47.81 ?  686 ARG B NH2   1 
ATOM   11093 N  N     . THR B 1 687 ? 122.665 123.363 157.446 1.00 46.89 ?  687 THR B N     1 
ATOM   11094 C  CA    . THR B 1 687 ? 122.089 122.134 157.970 1.00 50.40 ?  687 THR B CA    1 
ATOM   11095 C  C     . THR B 1 687 ? 123.173 121.290 158.627 1.00 49.85 ?  687 THR B C     1 
ATOM   11096 O  O     . THR B 1 687 ? 124.290 121.187 158.114 1.00 51.44 ?  687 THR B O     1 
ATOM   11097 C  CB    . THR B 1 687 ? 121.401 121.331 156.862 1.00 47.33 ?  687 THR B CB    1 
ATOM   11098 O  OG1   . THR B 1 687 ? 120.729 122.226 155.968 1.00 44.31 ?  687 THR B OG1   1 
ATOM   11099 C  CG2   . THR B 1 687 ? 120.390 120.366 157.455 1.00 45.39 ?  687 THR B CG2   1 
ATOM   11100 N  N     . LYS B 1 688 ? 122.835 120.694 159.766 1.00 47.38 ?  688 LYS B N     1 
ATOM   11101 C  CA    . LYS B 1 688 ? 123.769 119.837 160.487 1.00 49.75 ?  688 LYS B CA    1 
ATOM   11102 C  C     . LYS B 1 688 ? 123.624 118.385 160.047 1.00 54.70 ?  688 LYS B C     1 
ATOM   11103 O  O     . LYS B 1 688 ? 122.511 117.884 159.885 1.00 55.57 ?  688 LYS B O     1 
ATOM   11104 C  CB    . LYS B 1 688 ? 123.548 119.953 161.995 1.00 47.73 ?  688 LYS B CB    1 
ATOM   11105 C  CG    . LYS B 1 688 ? 124.649 119.321 162.828 1.00 49.97 ?  688 LYS B CG    1 
ATOM   11106 C  CD    . LYS B 1 688 ? 124.629 119.842 164.252 1.00 50.55 ?  688 LYS B CD    1 
ATOM   11107 C  CE    . LYS B 1 688 ? 125.857 119.388 165.022 1.00 52.82 ?  688 LYS B CE    1 
ATOM   11108 N  NZ    . LYS B 1 688 ? 125.900 119.979 166.388 1.00 54.26 ?  688 LYS B NZ    1 
ATOM   11109 N  N     . ASP C 2 37  ? 132.563 82.100  113.554 1.00 45.99 ?  16  ASP C N     1 
ATOM   11110 C  CA    . ASP C 2 37  ? 132.694 82.817  112.281 1.00 45.47 ?  16  ASP C CA    1 
ATOM   11111 C  C     . ASP C 2 37  ? 132.000 84.179  112.246 1.00 44.13 ?  16  ASP C C     1 
ATOM   11112 O  O     . ASP C 2 37  ? 132.125 84.910  111.261 1.00 44.46 ?  16  ASP C O     1 
ATOM   11113 C  CB    . ASP C 2 37  ? 132.156 81.949  111.141 1.00 45.90 ?  16  ASP C CB    1 
ATOM   11114 C  CG    . ASP C 2 37  ? 132.719 80.549  111.167 1.00 47.25 ?  16  ASP C CG    1 
ATOM   11115 O  OD1   . ASP C 2 37  ? 133.922 80.393  111.470 1.00 47.99 ?  16  ASP C OD1   1 
ATOM   11116 O  OD2   . ASP C 2 37  ? 131.953 79.603  110.888 1.00 49.50 -1 16  ASP C OD2   1 
ATOM   11117 N  N     . PHE C 2 38  ? 131.276 84.522  113.308 1.00 42.17 ?  17  PHE C N     1 
ATOM   11118 C  CA    . PHE C 2 38  ? 130.395 85.695  113.266 1.00 40.67 ?  17  PHE C CA    1 
ATOM   11119 C  C     . PHE C 2 38  ? 130.451 86.664  114.453 1.00 39.46 ?  17  PHE C C     1 
ATOM   11120 O  O     . PHE C 2 38  ? 130.101 87.836  114.301 1.00 39.17 ?  17  PHE C O     1 
ATOM   11121 C  CB    . PHE C 2 38  ? 128.942 85.256  113.011 1.00 40.24 ?  17  PHE C CB    1 
ATOM   11122 C  CG    . PHE C 2 38  ? 128.423 84.235  113.996 1.00 39.58 ?  17  PHE C CG    1 
ATOM   11123 C  CD1   . PHE C 2 38  ? 127.850 84.637  115.203 1.00 38.78 ?  17  PHE C CD1   1 
ATOM   11124 C  CD2   . PHE C 2 38  ? 128.494 82.871  113.711 1.00 39.43 ?  17  PHE C CD2   1 
ATOM   11125 C  CE1   . PHE C 2 38  ? 127.359 83.700  116.113 1.00 38.07 ?  17  PHE C CE1   1 
ATOM   11126 C  CE2   . PHE C 2 38  ? 128.007 81.923  114.616 1.00 39.10 ?  17  PHE C CE2   1 
ATOM   11127 C  CZ    . PHE C 2 38  ? 127.439 82.340  115.821 1.00 38.63 ?  17  PHE C CZ    1 
ATOM   11128 N  N     . THR C 2 39  ? 130.877 86.185  115.624 1.00 38.22 ?  18  THR C N     1 
ATOM   11129 C  CA    . THR C 2 39  ? 130.822 87.006  116.845 1.00 37.09 ?  18  THR C CA    1 
ATOM   11130 C  C     . THR C 2 39  ? 131.578 88.339  116.709 1.00 36.84 ?  18  THR C C     1 
ATOM   11131 O  O     . THR C 2 39  ? 131.049 89.397  117.088 1.00 36.13 ?  18  THR C O     1 
ATOM   11132 C  CB    . THR C 2 39  ? 131.232 86.219  118.124 1.00 36.59 ?  18  THR C CB    1 
ATOM   11133 O  OG1   . THR C 2 39  ? 130.175 85.325  118.480 1.00 36.50 ?  18  THR C OG1   1 
ATOM   11134 C  CG2   . THR C 2 39  ? 131.455 87.155  119.296 1.00 36.06 ?  18  THR C CG2   1 
ATOM   11135 N  N     . GLN C 2 40  ? 132.792 88.287  116.152 1.00 37.01 ?  19  GLN C N     1 
ATOM   11136 C  CA    . GLN C 2 40  ? 133.613 89.496  115.986 1.00 37.33 ?  19  GLN C CA    1 
ATOM   11137 C  C     . GLN C 2 40  ? 132.932 90.573  115.159 1.00 36.63 ?  19  GLN C C     1 
ATOM   11138 O  O     . GLN C 2 40  ? 132.979 91.750  115.513 1.00 36.10 ?  19  GLN C O     1 
ATOM   11139 C  CB    . GLN C 2 40  ? 134.989 89.179  115.401 1.00 38.24 ?  19  GLN C CB    1 
ATOM   11140 C  CG    . GLN C 2 40  ? 135.979 88.718  116.446 1.00 41.33 ?  19  GLN C CG    1 
ATOM   11141 C  CD    . GLN C 2 40  ? 137.394 89.193  116.179 1.00 45.15 ?  19  GLN C CD    1 
ATOM   11142 O  OE1   . GLN C 2 40  ? 137.821 89.318  115.025 1.00 47.33 ?  19  GLN C OE1   1 
ATOM   11143 N  NE2   . GLN C 2 40  ? 138.136 89.461  117.253 1.00 46.51 ?  19  GLN C NE2   1 
ATOM   11144 N  N     . MET C 2 41  ? 132.288 90.167  114.068 1.00 36.23 ?  20  MET C N     1 
ATOM   11145 C  CA    . MET C 2 41  ? 131.571 91.121  113.233 1.00 36.40 ?  20  MET C CA    1 
ATOM   11146 C  C     . MET C 2 41  ? 130.308 91.661  113.929 1.00 34.93 ?  20  MET C C     1 
ATOM   11147 O  O     . MET C 2 41  ? 129.968 92.830  113.761 1.00 34.20 ?  20  MET C O     1 
ATOM   11148 C  CB    . MET C 2 41  ? 131.328 90.575  111.809 1.00 37.35 ?  20  MET C CB    1 
ATOM   11149 C  CG    . MET C 2 41  ? 130.082 89.741  111.575 1.00 40.49 ?  20  MET C CG    1 
ATOM   11150 S  SD    . MET C 2 41  ? 129.871 89.391  109.801 1.00 48.68 ?  20  MET C SD    1 
ATOM   11151 C  CE    . MET C 2 41  ? 130.867 87.907  109.608 1.00 47.17 ?  20  MET C CE    1 
ATOM   11152 N  N     . PHE C 2 42  ? 129.652 90.831  114.745 1.00 33.75 ?  21  PHE C N     1 
ATOM   11153 C  CA    . PHE C 2 42  ? 128.539 91.316  115.574 1.00 32.62 ?  21  PHE C CA    1 
ATOM   11154 C  C     . PHE C 2 42  ? 129.013 92.249  116.683 1.00 32.59 ?  21  PHE C C     1 
ATOM   11155 O  O     . PHE C 2 42  ? 128.358 93.253  116.978 1.00 32.23 ?  21  PHE C O     1 
ATOM   11156 C  CB    . PHE C 2 42  ? 127.708 90.164  116.138 1.00 32.12 ?  21  PHE C CB    1 
ATOM   11157 C  CG    . PHE C 2 42  ? 126.700 89.624  115.167 1.00 31.04 ?  21  PHE C CG    1 
ATOM   11158 C  CD1   . PHE C 2 42  ? 125.387 90.094  115.172 1.00 30.75 ?  21  PHE C CD1   1 
ATOM   11159 C  CD2   . PHE C 2 42  ? 127.059 88.652  114.240 1.00 30.99 ?  21  PHE C CD2   1 
ATOM   11160 C  CE1   . PHE C 2 42  ? 124.444 89.597  114.265 1.00 30.30 ?  21  PHE C CE1   1 
ATOM   11161 C  CE2   . PHE C 2 42  ? 126.124 88.145  113.323 1.00 30.74 ?  21  PHE C CE2   1 
ATOM   11162 C  CZ    . PHE C 2 42  ? 124.816 88.619  113.338 1.00 30.48 ?  21  PHE C CZ    1 
ATOM   11163 N  N     . TYR C 2 43  ? 130.155 91.920  117.286 1.00 32.33 ?  22  TYR C N     1 
ATOM   11164 C  CA    . TYR C 2 43  ? 130.770 92.798  118.277 1.00 32.50 ?  22  TYR C CA    1 
ATOM   11165 C  C     . TYR C 2 43  ? 131.006 94.186  117.685 1.00 33.01 ?  22  TYR C C     1 
ATOM   11166 O  O     . TYR C 2 43  ? 130.600 95.193  118.272 1.00 32.50 ?  22  TYR C O     1 
ATOM   11167 C  CB    . TYR C 2 43  ? 132.080 92.209  118.836 1.00 32.53 ?  22  TYR C CB    1 
ATOM   11168 C  CG    . TYR C 2 43  ? 132.850 93.214  119.675 1.00 33.27 ?  22  TYR C CG    1 
ATOM   11169 C  CD1   . TYR C 2 43  ? 132.507 93.450  121.009 1.00 32.34 ?  22  TYR C CD1   1 
ATOM   11170 C  CD2   . TYR C 2 43  ? 133.894 93.957  119.120 1.00 33.71 ?  22  TYR C CD2   1 
ATOM   11171 C  CE1   . TYR C 2 43  ? 133.197 94.388  121.775 1.00 33.58 ?  22  TYR C CE1   1 
ATOM   11172 C  CE2   . TYR C 2 43  ? 134.590 94.904  119.874 1.00 35.12 ?  22  TYR C CE2   1 
ATOM   11173 C  CZ    . TYR C 2 43  ? 134.239 95.110  121.202 1.00 35.30 ?  22  TYR C CZ    1 
ATOM   11174 O  OH    . TYR C 2 43  ? 134.928 96.044  121.945 1.00 36.54 ?  22  TYR C OH    1 
ATOM   11175 N  N     . ASN C 2 44  ? 131.647 94.226  116.514 1.00 33.80 ?  23  ASN C N     1 
ATOM   11176 C  CA    . ASN C 2 44  ? 131.958 95.483  115.845 1.00 34.80 ?  23  ASN C CA    1 
ATOM   11177 C  C     . ASN C 2 44  ? 130.698 96.252  115.454 1.00 34.40 ?  23  ASN C C     1 
ATOM   11178 O  O     . ASN C 2 44  ? 130.632 97.463  115.635 1.00 33.99 ?  23  ASN C O     1 
ATOM   11179 C  CB    . ASN C 2 44  ? 132.859 95.251  114.621 1.00 35.46 ?  23  ASN C CB    1 
ATOM   11180 C  CG    . ASN C 2 44  ? 134.232 94.666  114.988 1.00 38.28 ?  23  ASN C CG    1 
ATOM   11181 O  OD1   . ASN C 2 44  ? 134.719 94.810  116.119 1.00 41.01 ?  23  ASN C OD1   1 
ATOM   11182 N  ND2   . ASN C 2 44  ? 134.863 94.007  114.018 1.00 39.13 ?  23  ASN C ND2   1 
ATOM   11183 N  N     . GLN C 2 45  ? 129.696 95.540  114.936 1.00 34.49 ?  24  GLN C N     1 
ATOM   11184 C  CA    . GLN C 2 45  ? 128.434 96.160  114.550 1.00 34.81 ?  24  GLN C CA    1 
ATOM   11185 C  C     . GLN C 2 45  ? 127.689 96.730  115.763 1.00 34.68 ?  24  GLN C C     1 
ATOM   11186 O  O     . GLN C 2 45  ? 127.195 97.860  115.718 1.00 34.59 ?  24  GLN C O     1 
ATOM   11187 C  CB    . GLN C 2 45  ? 127.557 95.173  113.772 1.00 34.83 ?  24  GLN C CB    1 
ATOM   11188 C  CG    . GLN C 2 45  ? 126.400 95.816  113.003 1.00 36.14 ?  24  GLN C CG    1 
ATOM   11189 C  CD    . GLN C 2 45  ? 126.855 96.814  111.934 1.00 38.04 ?  24  GLN C CD    1 
ATOM   11190 O  OE1   . GLN C 2 45  ? 127.944 96.694  111.366 1.00 38.57 ?  24  GLN C OE1   1 
ATOM   11191 N  NE2   . GLN C 2 45  ? 126.013 97.811  111.662 1.00 38.67 ?  24  GLN C NE2   1 
ATOM   11192 N  N     . ASN C 2 46  ? 127.623 95.963  116.848 1.00 34.71 ?  25  ASN C N     1 
ATOM   11193 C  CA    . ASN C 2 46  ? 126.948 96.431  118.059 1.00 34.99 ?  25  ASN C CA    1 
ATOM   11194 C  C     . ASN C 2 46  ? 127.590 97.688  118.647 1.00 35.69 ?  25  ASN C C     1 
ATOM   11195 O  O     . ASN C 2 46  ? 126.897 98.666  118.946 1.00 35.41 ?  25  ASN C O     1 
ATOM   11196 C  CB    . ASN C 2 46  ? 126.839 95.318  119.108 1.00 34.64 ?  25  ASN C CB    1 
ATOM   11197 C  CG    . ASN C 2 46  ? 125.676 94.387  118.842 1.00 34.71 ?  25  ASN C CG    1 
ATOM   11198 O  OD1   . ASN C 2 46  ? 124.584 94.595  119.364 1.00 35.68 ?  25  ASN C OD1   1 
ATOM   11199 N  ND2   . ASN C 2 46  ? 125.890 93.375  117.996 1.00 34.71 ?  25  ASN C ND2   1 
ATOM   11200 N  N     . VAL C 2 47  ? 128.912 97.678  118.786 1.00 36.69 ?  26  VAL C N     1 
ATOM   11201 C  CA    . VAL C 2 47  ? 129.597 98.828  119.380 1.00 38.00 ?  26  VAL C CA    1 
ATOM   11202 C  C     . VAL C 2 47  ? 129.578 100.067 118.474 1.00 38.90 ?  26  VAL C C     1 
ATOM   11203 O  O     . VAL C 2 47  ? 129.559 101.189 118.972 1.00 39.46 ?  26  VAL C O     1 
ATOM   11204 C  CB    . VAL C 2 47  ? 131.032 98.501  119.874 1.00 38.16 ?  26  VAL C CB    1 
ATOM   11205 C  CG1   . VAL C 2 47  ? 130.990 97.381  120.895 1.00 37.75 ?  26  VAL C CG1   1 
ATOM   11206 C  CG2   . VAL C 2 47  ? 131.963 98.158  118.713 1.00 38.81 ?  26  VAL C CG2   1 
ATOM   11207 N  N     . LYS C 2 48  ? 129.549 99.864  117.157 1.00 39.67 ?  27  LYS C N     1 
ATOM   11208 C  CA    . LYS C 2 48  ? 129.479 100.991 116.223 1.00 40.50 ?  27  LYS C CA    1 
ATOM   11209 C  C     . LYS C 2 48  ? 128.061 101.572 116.135 1.00 40.02 ?  27  LYS C C     1 
ATOM   11210 O  O     . LYS C 2 48  ? 127.862 102.676 115.623 1.00 40.55 ?  27  LYS C O     1 
ATOM   11211 C  CB    . LYS C 2 48  ? 130.011 100.603 114.830 1.00 41.23 ?  27  LYS C CB    1 
ATOM   11212 C  CG    . LYS C 2 48  ? 128.995 99.915  113.919 1.00 42.50 ?  27  LYS C CG    1 
ATOM   11213 C  CD    . LYS C 2 48  ? 129.562 99.613  112.524 1.00 44.92 ?  27  LYS C CD    1 
ATOM   11214 C  CE    . LYS C 2 48  ? 129.547 100.841 111.616 1.00 46.66 ?  27  LYS C CE    1 
ATOM   11215 N  NZ    . LYS C 2 48  ? 128.166 101.364 111.400 1.00 47.26 1  27  LYS C NZ    1 
ATOM   11216 N  N     . GLN C 2 49  ? 127.080 100.823 116.624 1.00 39.10 ?  28  GLN C N     1 
ATOM   11217 C  CA    . GLN C 2 49  ? 125.712 101.297 116.637 1.00 38.22 ?  28  GLN C CA    1 
ATOM   11218 C  C     . GLN C 2 49  ? 125.374 102.017 117.943 1.00 37.23 ?  28  GLN C C     1 
ATOM   11219 O  O     . GLN C 2 49  ? 124.251 102.491 118.097 1.00 37.40 ?  28  GLN C O     1 
ATOM   11220 C  CB    . GLN C 2 49  ? 124.723 100.152 116.361 1.00 38.69 ?  28  GLN C CB    1 
ATOM   11221 C  CG    . GLN C 2 49  ? 124.696 99.689  114.896 1.00 39.57 ?  28  GLN C CG    1 
ATOM   11222 C  CD    . GLN C 2 49  ? 123.583 98.692  114.584 1.00 41.20 ?  28  GLN C CD    1 
ATOM   11223 O  OE1   . GLN C 2 49  ? 123.499 98.184  113.465 1.00 42.94 ?  28  GLN C OE1   1 
ATOM   11224 N  NE2   . GLN C 2 49  ? 122.724 98.409  115.568 1.00 41.23 ?  28  GLN C NE2   1 
ATOM   11225 N  N     . PHE C 2 50  ? 126.340 102.117 118.862 1.00 35.83 ?  29  PHE C N     1 
ATOM   11226 C  CA    . PHE C 2 50  ? 126.080 102.719 120.178 1.00 34.51 ?  29  PHE C CA    1 
ATOM   11227 C  C     . PHE C 2 50  ? 125.483 104.126 120.090 1.00 33.81 ?  29  PHE C C     1 
ATOM   11228 O  O     . PHE C 2 50  ? 125.960 104.960 119.321 1.00 33.66 ?  29  PHE C O     1 
ATOM   11229 C  CB    . PHE C 2 50  ? 127.324 102.730 121.071 1.00 34.59 ?  29  PHE C CB    1 
ATOM   11230 C  CG    . PHE C 2 50  ? 127.075 103.315 122.450 1.00 34.59 ?  29  PHE C CG    1 
ATOM   11231 C  CD1   . PHE C 2 50  ? 126.336 102.608 123.405 1.00 34.34 ?  29  PHE C CD1   1 
ATOM   11232 C  CD2   . PHE C 2 50  ? 127.560 104.579 122.784 1.00 35.49 ?  29  PHE C CD2   1 
ATOM   11233 C  CE1   . PHE C 2 50  ? 126.095 103.147 124.678 1.00 33.88 ?  29  PHE C CE1   1 
ATOM   11234 C  CE2   . PHE C 2 50  ? 127.324 105.134 124.056 1.00 34.12 ?  29  PHE C CE2   1 
ATOM   11235 C  CZ    . PHE C 2 50  ? 126.592 104.417 125.002 1.00 33.87 ?  29  PHE C CZ    1 
ATOM   11236 N  N     . TRP C 2 51  ? 124.444 104.370 120.891 1.00 32.24 ?  30  TRP C N     1 
ATOM   11237 C  CA    . TRP C 2 51  ? 123.745 105.653 120.912 1.00 31.28 ?  30  TRP C CA    1 
ATOM   11238 C  C     . TRP C 2 51  ? 123.091 105.921 122.269 1.00 31.12 ?  30  TRP C C     1 
ATOM   11239 O  O     . TRP C 2 51  ? 122.945 105.001 123.084 1.00 30.71 ?  30  TRP C O     1 
ATOM   11240 C  CB    . TRP C 2 51  ? 122.701 105.716 119.788 1.00 30.85 ?  30  TRP C CB    1 
ATOM   11241 C  CG    . TRP C 2 51  ? 121.607 104.683 119.904 1.00 29.31 ?  30  TRP C CG    1 
ATOM   11242 C  CD1   . TRP C 2 51  ? 121.661 103.377 119.499 1.00 29.07 ?  30  TRP C CD1   1 
ATOM   11243 C  CD2   . TRP C 2 51  ? 120.310 104.869 120.480 1.00 28.33 ?  30  TRP C CD2   1 
ATOM   11244 N  NE1   . TRP C 2 51  ? 120.476 102.743 119.779 1.00 28.01 ?  30  TRP C NE1   1 
ATOM   11245 C  CE2   . TRP C 2 51  ? 119.627 103.634 120.380 1.00 27.67 ?  30  TRP C CE2   1 
ATOM   11246 C  CE3   . TRP C 2 51  ? 119.657 105.958 121.075 1.00 27.27 ?  30  TRP C CE3   1 
ATOM   11247 C  CZ2   . TRP C 2 51  ? 118.327 103.459 120.852 1.00 26.54 ?  30  TRP C CZ2   1 
ATOM   11248 C  CZ3   . TRP C 2 51  ? 118.359 105.786 121.535 1.00 27.07 ?  30  TRP C CZ3   1 
ATOM   11249 C  CH2   . TRP C 2 51  ? 117.710 104.541 121.427 1.00 26.52 ?  30  TRP C CH2   1 
ATOM   11250 N  N     . LEU C 2 52  ? 122.707 107.180 122.501 1.00 30.65 ?  31  LEU C N     1 
ATOM   11251 C  CA    . LEU C 2 52  ? 121.943 107.589 123.682 1.00 30.38 ?  31  LEU C CA    1 
ATOM   11252 C  C     . LEU C 2 52  ? 120.760 108.452 123.252 1.00 30.51 ?  31  LEU C C     1 
ATOM   11253 O  O     . LEU C 2 52  ? 120.902 109.257 122.331 1.00 30.77 ?  31  LEU C O     1 
ATOM   11254 C  CB    . LEU C 2 52  ? 122.830 108.373 124.663 1.00 30.45 ?  31  LEU C CB    1 
ATOM   11255 C  CG    . LEU C 2 52  ? 123.982 107.586 125.296 1.00 30.29 ?  31  LEU C CG    1 
ATOM   11256 C  CD1   . LEU C 2 52  ? 125.070 108.506 125.867 1.00 30.69 ?  31  LEU C CD1   1 
ATOM   11257 C  CD2   . LEU C 2 52  ? 123.462 106.601 126.355 1.00 29.91 ?  31  LEU C CD2   1 
ATOM   11258 N  N     . PRO C 2 53  ? 119.592 108.300 123.917 1.00 30.73 ?  32  PRO C N     1 
ATOM   11259 C  CA    . PRO C 2 53  ? 118.401 109.073 123.529 1.00 31.17 ?  32  PRO C CA    1 
ATOM   11260 C  C     . PRO C 2 53  ? 118.615 110.585 123.562 1.00 32.18 ?  32  PRO C C     1 
ATOM   11261 O  O     . PRO C 2 53  ? 118.000 111.309 122.761 1.00 32.66 ?  32  PRO C O     1 
ATOM   11262 C  CB    . PRO C 2 53  ? 117.351 108.666 124.570 1.00 30.99 ?  32  PRO C CB    1 
ATOM   11263 C  CG    . PRO C 2 53  ? 118.127 108.018 125.692 1.00 30.50 ?  32  PRO C CG    1 
ATOM   11264 C  CD    . PRO C 2 53  ? 119.301 107.378 125.034 1.00 30.46 ?  32  PRO C CD    1 
ATOM   11265 N  N     . GLU C 2 54  ? 119.488 111.048 124.460 1.00 32.62 ?  33  GLU C N     1 
ATOM   11266 C  CA    . GLU C 2 54  ? 119.801 112.480 124.593 1.00 33.44 ?  33  GLU C CA    1 
ATOM   11267 C  C     . GLU C 2 54  ? 120.427 113.094 123.335 1.00 33.59 ?  33  GLU C C     1 
ATOM   11268 O  O     . GLU C 2 54  ? 120.463 114.315 123.200 1.00 34.05 ?  33  GLU C O     1 
ATOM   11269 C  CB    . GLU C 2 54  ? 120.706 112.748 125.809 1.00 33.72 ?  33  GLU C CB    1 
ATOM   11270 C  CG    . GLU C 2 54  ? 120.016 112.601 127.179 1.00 34.53 ?  33  GLU C CG    1 
ATOM   11271 C  CD    . GLU C 2 54  ? 119.778 111.144 127.579 1.00 35.09 ?  33  GLU C CD    1 
ATOM   11272 O  OE1   . GLU C 2 54  ? 120.488 110.245 127.060 1.00 34.38 ?  33  GLU C OE1   1 
ATOM   11273 O  OE2   . GLU C 2 54  ? 118.877 110.900 128.414 1.00 35.53 -1 33  GLU C OE2   1 
ATOM   11274 N  N     . GLU C 2 55  ? 120.917 112.250 122.424 1.00 33.82 ?  34  GLU C N     1 
ATOM   11275 C  CA    . GLU C 2 55  ? 121.447 112.710 121.137 1.00 34.19 ?  34  GLU C CA    1 
ATOM   11276 C  C     . GLU C 2 55  ? 120.341 113.291 120.245 1.00 33.83 ?  34  GLU C C     1 
ATOM   11277 O  O     . GLU C 2 55  ? 120.620 114.056 119.323 1.00 33.93 ?  34  GLU C O     1 
ATOM   11278 C  CB    . GLU C 2 55  ? 122.154 111.569 120.382 1.00 34.52 ?  34  GLU C CB    1 
ATOM   11279 C  CG    . GLU C 2 55  ? 123.381 110.973 121.065 1.00 36.50 ?  34  GLU C CG    1 
ATOM   11280 C  CD    . GLU C 2 55  ? 124.172 110.055 120.138 1.00 40.03 ?  34  GLU C CD    1 
ATOM   11281 O  OE1   . GLU C 2 55  ? 125.017 110.558 119.364 1.00 42.43 ?  34  GLU C OE1   1 
ATOM   11282 O  OE2   . GLU C 2 55  ? 123.959 108.828 120.184 1.00 39.35 -1 34  GLU C OE2   1 
ATOM   11283 N  N     . ILE C 2 56  ? 119.098 112.891 120.515 1.00 33.31 ?  35  ILE C N     1 
ATOM   11284 C  CA    . ILE C 2 56  ? 117.922 113.298 119.742 1.00 33.14 ?  35  ILE C CA    1 
ATOM   11285 C  C     . ILE C 2 56  ? 117.092 114.282 120.574 1.00 32.58 ?  35  ILE C C     1 
ATOM   11286 O  O     . ILE C 2 56  ? 116.598 113.924 121.638 1.00 32.12 ?  35  ILE C O     1 
ATOM   11287 C  CB    . ILE C 2 56  ? 117.029 112.061 119.382 1.00 33.03 ?  35  ILE C CB    1 
ATOM   11288 C  CG1   . ILE C 2 56  ? 117.847 110.928 118.724 1.00 34.76 ?  35  ILE C CG1   1 
ATOM   11289 C  CG2   . ILE C 2 56  ? 115.822 112.465 118.526 1.00 33.61 ?  35  ILE C CG2   1 
ATOM   11290 C  CD1   . ILE C 2 56  ? 118.402 111.230 117.330 1.00 36.75 ?  35  ILE C CD1   1 
ATOM   11291 N  N     . ALA C 2 57  ? 116.952 115.517 120.098 1.00 32.36 ?  36  ALA C N     1 
ATOM   11292 C  CA    . ALA C 2 57  ? 116.103 116.504 120.772 1.00 32.17 ?  36  ALA C CA    1 
ATOM   11293 C  C     . ALA C 2 57  ? 114.629 116.229 120.454 1.00 31.76 ?  36  ALA C C     1 
ATOM   11294 O  O     . ALA C 2 57  ? 114.265 116.036 119.293 1.00 31.95 ?  36  ALA C O     1 
ATOM   11295 C  CB    . ALA C 2 57  ? 116.490 117.913 120.352 1.00 33.01 ?  36  ALA C CB    1 
ATOM   11296 N  N     . LEU C 2 58  ? 113.786 116.213 121.482 1.00 30.68 ?  37  LEU C N     1 
ATOM   11297 C  CA    . LEU C 2 58  ? 112.418 115.721 121.323 1.00 30.14 ?  37  LEU C CA    1 
ATOM   11298 C  C     . LEU C 2 58  ? 111.343 116.802 121.281 1.00 30.21 ?  37  LEU C C     1 
ATOM   11299 O  O     . LEU C 2 58  ? 110.190 116.519 120.929 1.00 29.91 ?  37  LEU C O     1 
ATOM   11300 C  CB    . LEU C 2 58  ? 112.096 114.685 122.406 1.00 29.46 ?  37  LEU C CB    1 
ATOM   11301 C  CG    . LEU C 2 58  ? 112.870 113.363 122.311 1.00 29.08 ?  37  LEU C CG    1 
ATOM   11302 C  CD1   . LEU C 2 58  ? 112.606 112.494 123.527 1.00 29.23 ?  37  LEU C CD1   1 
ATOM   11303 C  CD2   . LEU C 2 58  ? 112.525 112.604 121.030 1.00 28.84 ?  37  LEU C CD2   1 
ATOM   11304 N  N     . ASN C 2 59  ? 111.723 118.032 121.614 1.00 30.50 ?  38  ASN C N     1 
ATOM   11305 C  CA    . ASN C 2 59  ? 110.770 119.145 121.662 1.00 31.23 ?  38  ASN C CA    1 
ATOM   11306 C  C     . ASN C 2 59  ? 110.104 119.458 120.312 1.00 31.03 ?  38  ASN C C     1 
ATOM   11307 O  O     . ASN C 2 59  ? 109.039 120.067 120.272 1.00 30.82 ?  38  ASN C O     1 
ATOM   11308 C  CB    . ASN C 2 59  ? 111.403 120.397 122.299 1.00 31.98 ?  38  ASN C CB    1 
ATOM   11309 C  CG    . ASN C 2 59  ? 112.645 120.877 121.566 1.00 33.59 ?  38  ASN C CG    1 
ATOM   11310 O  OD1   . ASN C 2 59  ? 113.602 120.118 121.370 1.00 36.48 ?  38  ASN C OD1   1 
ATOM   11311 N  ND2   . ASN C 2 59  ? 112.644 122.146 121.170 1.00 34.77 ?  38  ASN C ND2   1 
ATOM   11312 N  N     . GLY C 2 60  ? 110.722 119.006 119.222 1.00 30.88 ?  39  GLY C N     1 
ATOM   11313 C  CA    . GLY C 2 60  ? 110.140 119.111 117.879 1.00 31.37 ?  39  GLY C CA    1 
ATOM   11314 C  C     . GLY C 2 60  ? 108.865 118.309 117.649 1.00 31.05 ?  39  GLY C C     1 
ATOM   11315 O  O     . GLY C 2 60  ? 108.061 118.681 116.805 1.00 31.21 ?  39  GLY C O     1 
ATOM   11316 N  N     . ASP C 2 61  ? 108.673 117.220 118.398 1.00 30.63 ?  40  ASP C N     1 
ATOM   11317 C  CA    . ASP C 2 61  ? 107.421 116.440 118.348 1.00 30.65 ?  40  ASP C CA    1 
ATOM   11318 C  C     . ASP C 2 61  ? 106.245 117.057 119.111 1.00 31.00 ?  40  ASP C C     1 
ATOM   11319 O  O     . ASP C 2 61  ? 105.123 116.558 119.004 1.00 30.91 ?  40  ASP C O     1 
ATOM   11320 C  CB    . ASP C 2 61  ? 107.631 115.023 118.894 1.00 30.00 ?  40  ASP C CB    1 
ATOM   11321 C  CG    . ASP C 2 61  ? 108.536 114.180 118.026 1.00 30.88 ?  40  ASP C CG    1 
ATOM   11322 O  OD1   . ASP C 2 61  ? 109.040 114.676 116.990 1.00 30.42 ?  40  ASP C OD1   1 
ATOM   11323 O  OD2   . ASP C 2 61  ? 108.747 113.006 118.397 1.00 31.17 -1 40  ASP C OD2   1 
ATOM   11324 N  N     . LEU C 2 62  ? 106.495 118.111 119.886 1.00 31.54 ?  41  LEU C N     1 
ATOM   11325 C  CA    . LEU C 2 62  ? 105.477 118.672 120.789 1.00 32.47 ?  41  LEU C CA    1 
ATOM   11326 C  C     . LEU C 2 62  ? 104.163 119.031 120.105 1.00 33.21 ?  41  LEU C C     1 
ATOM   11327 O  O     . LEU C 2 62  ? 103.083 118.766 120.644 1.00 32.84 ?  41  LEU C O     1 
ATOM   11328 C  CB    . LEU C 2 62  ? 106.013 119.887 121.549 1.00 33.14 ?  41  LEU C CB    1 
ATOM   11329 C  CG    . LEU C 2 62  ? 106.806 119.626 122.829 1.00 34.44 ?  41  LEU C CG    1 
ATOM   11330 C  CD1   . LEU C 2 62  ? 107.511 120.901 123.271 1.00 35.04 ?  41  LEU C CD1   1 
ATOM   11331 C  CD2   . LEU C 2 62  ? 105.891 119.090 123.937 1.00 35.52 ?  41  LEU C CD2   1 
ATOM   11332 N  N     . LEU C 2 63  ? 104.260 119.628 118.918 1.00 33.75 ?  42  LEU C N     1 
ATOM   11333 C  CA    . LEU C 2 63  ? 103.069 120.042 118.188 1.00 34.79 ?  42  LEU C CA    1 
ATOM   11334 C  C     . LEU C 2 63  ? 102.306 118.912 117.501 1.00 34.66 ?  42  LEU C C     1 
ATOM   11335 O  O     . LEU C 2 63  ? 101.084 118.856 117.623 1.00 34.67 ?  42  LEU C O     1 
ATOM   11336 C  CB    . LEU C 2 63  ? 103.375 121.181 117.212 1.00 35.27 ?  42  LEU C CB    1 
ATOM   11337 C  CG    . LEU C 2 63  ? 103.394 122.566 117.870 1.00 36.82 ?  42  LEU C CG    1 
ATOM   11338 C  CD1   . LEU C 2 63  ? 103.748 123.623 116.830 1.00 37.93 ?  42  LEU C CD1   1 
ATOM   11339 C  CD2   . LEU C 2 63  ? 102.060 122.907 118.531 1.00 37.85 ?  42  LEU C CD2   1 
ATOM   11340 N  N     . THR C 2 64  ? 102.998 118.019 116.787 1.00 34.70 ?  43  THR C N     1 
ATOM   11341 C  CA    . THR C 2 64  ? 102.299 116.879 116.169 1.00 35.10 ?  43  THR C CA    1 
ATOM   11342 C  C     . THR C 2 64  ? 101.664 115.957 117.222 1.00 34.78 ?  43  THR C C     1 
ATOM   11343 O  O     . THR C 2 64  ? 100.673 115.292 116.940 1.00 35.04 ?  43  THR C O     1 
ATOM   11344 C  CB    . THR C 2 64  ? 103.157 116.073 115.143 1.00 35.30 ?  43  THR C CB    1 
ATOM   11345 O  OG1   . THR C 2 64  ? 104.374 115.613 115.750 1.00 36.01 ?  43  THR C OG1   1 
ATOM   11346 C  CG2   . THR C 2 64  ? 103.476 116.920 113.912 1.00 35.96 ?  43  THR C CG2   1 
ATOM   11347 N  N     . TRP C 2 65  ? 102.215 115.949 118.438 1.00 34.63 ?  44  TRP C N     1 
ATOM   11348 C  CA    . TRP C 2 65  ? 101.633 115.192 119.555 1.00 34.37 ?  44  TRP C CA    1 
ATOM   11349 C  C     . TRP C 2 65  ? 100.352 115.851 120.063 1.00 35.13 ?  44  TRP C C     1 
ATOM   11350 O  O     . TRP C 2 65  ? 99.314  115.193 120.220 1.00 34.98 ?  44  TRP C O     1 
ATOM   11351 C  CB    . TRP C 2 65  ? 102.640 115.064 120.697 1.00 33.95 ?  44  TRP C CB    1 
ATOM   11352 C  CG    . TRP C 2 65  ? 102.063 114.494 121.954 1.00 33.26 ?  44  TRP C CG    1 
ATOM   11353 C  CD1   . TRP C 2 65  ? 101.720 115.179 123.086 1.00 32.51 ?  44  TRP C CD1   1 
ATOM   11354 C  CD2   . TRP C 2 65  ? 101.765 113.115 122.210 1.00 30.93 ?  44  TRP C CD2   1 
ATOM   11355 N  NE1   . TRP C 2 65  ? 101.230 114.309 124.037 1.00 31.66 ?  44  TRP C NE1   1 
ATOM   11356 C  CE2   . TRP C 2 65  ? 101.246 113.037 123.525 1.00 30.39 ?  44  TRP C CE2   1 
ATOM   11357 C  CE3   . TRP C 2 65  ? 101.891 111.938 121.460 1.00 30.36 ?  44  TRP C CE3   1 
ATOM   11358 C  CZ2   . TRP C 2 65  ? 100.844 111.830 124.100 1.00 29.16 ?  44  TRP C CZ2   1 
ATOM   11359 C  CZ3   . TRP C 2 65  ? 101.492 110.730 122.036 1.00 28.84 ?  44  TRP C CZ3   1 
ATOM   11360 C  CH2   . TRP C 2 65  ? 100.982 110.687 123.345 1.00 29.34 ?  44  TRP C CH2   1 
ATOM   11361 N  N     . LYS C 2 66  ? 100.446 117.151 120.334 1.00 35.69 ?  45  LYS C N     1 
ATOM   11362 C  CA    . LYS C 2 66  ? 99.311  117.962 120.748 1.00 36.38 ?  45  LYS C CA    1 
ATOM   11363 C  C     . LYS C 2 66  ? 98.103  117.784 119.821 1.00 36.24 ?  45  LYS C C     1 
ATOM   11364 O  O     . LYS C 2 66  ? 96.969  117.821 120.284 1.00 36.78 ?  45  LYS C O     1 
ATOM   11365 C  CB    . LYS C 2 66  ? 99.736  119.431 120.783 1.00 37.14 ?  45  LYS C CB    1 
ATOM   11366 C  CG    . LYS C 2 66  ? 98.671  120.410 121.246 1.00 38.91 ?  45  LYS C CG    1 
ATOM   11367 C  CD    . LYS C 2 66  ? 99.126  121.849 120.997 1.00 41.12 ?  45  LYS C CD    1 
ATOM   11368 C  CE    . LYS C 2 66  ? 98.256  122.839 121.752 1.00 43.00 ?  45  LYS C CE    1 
ATOM   11369 N  NZ    . LYS C 2 66  ? 98.101  122.449 123.186 1.00 44.38 1  45  LYS C NZ    1 
ATOM   11370 N  N     . TYR C 2 67  ? 98.370  117.554 118.532 1.00 36.03 ?  46  TYR C N     1 
ATOM   11371 C  CA    . TYR C 2 67  ? 97.351  117.498 117.470 1.00 36.03 ?  46  TYR C CA    1 
ATOM   11372 C  C     . TYR C 2 67  ? 96.651  116.143 117.304 1.00 35.25 ?  46  TYR C C     1 
ATOM   11373 O  O     . TYR C 2 67  ? 95.649  116.040 116.589 1.00 35.32 ?  46  TYR C O     1 
ATOM   11374 C  CB    . TYR C 2 67  ? 97.967  117.890 116.115 1.00 36.60 ?  46  TYR C CB    1 
ATOM   11375 C  CG    . TYR C 2 67  ? 98.517  119.308 116.026 1.00 37.85 ?  46  TYR C CG    1 
ATOM   11376 C  CD1   . TYR C 2 67  ? 98.197  120.268 116.986 1.00 38.97 ?  46  TYR C CD1   1 
ATOM   11377 C  CD2   . TYR C 2 67  ? 99.349  119.689 114.964 1.00 40.06 ?  46  TYR C CD2   1 
ATOM   11378 C  CE1   . TYR C 2 67  ? 98.704  121.564 116.914 1.00 40.36 ?  46  TYR C CE1   1 
ATOM   11379 C  CE2   . TYR C 2 67  ? 99.862  120.993 114.878 1.00 40.53 ?  46  TYR C CE2   1 
ATOM   11380 C  CZ    . TYR C 2 67  ? 99.528  121.925 115.861 1.00 41.43 ?  46  TYR C CZ    1 
ATOM   11381 O  OH    . TYR C 2 67  ? 100.008 123.221 115.802 1.00 41.48 ?  46  TYR C OH    1 
ATOM   11382 N  N     . LEU C 2 68  ? 97.189  115.105 117.938 1.00 33.80 ?  47  LEU C N     1 
ATOM   11383 C  CA    . LEU C 2 68  ? 96.585  113.779 117.865 1.00 32.77 ?  47  LEU C CA    1 
ATOM   11384 C  C     . LEU C 2 68  ? 95.332  113.722 118.729 1.00 31.84 ?  47  LEU C C     1 
ATOM   11385 O  O     . LEU C 2 68  ? 95.243  114.406 119.745 1.00 31.90 ?  47  LEU C O     1 
ATOM   11386 C  CB    . LEU C 2 68  ? 97.571  112.705 118.332 1.00 32.39 ?  47  LEU C CB    1 
ATOM   11387 C  CG    . LEU C 2 68  ? 98.867  112.426 117.568 1.00 32.68 ?  47  LEU C CG    1 
ATOM   11388 C  CD1   . LEU C 2 68  ? 99.641  111.320 118.278 1.00 33.03 ?  47  LEU C CD1   1 
ATOM   11389 C  CD2   . LEU C 2 68  ? 98.616  112.051 116.103 1.00 32.78 ?  47  LEU C CD2   1 
ATOM   11390 N  N     . GLY C 2 69  ? 94.375  112.891 118.332 1.00 30.99 ?  48  GLY C N     1 
ATOM   11391 C  CA    . GLY C 2 69  ? 93.195  112.639 119.157 1.00 30.58 ?  48  GLY C CA    1 
ATOM   11392 C  C     . GLY C 2 69  ? 93.540  111.950 120.471 1.00 29.87 ?  48  GLY C C     1 
ATOM   11393 O  O     . GLY C 2 69  ? 94.614  111.367 120.611 1.00 28.79 ?  48  GLY C O     1 
ATOM   11394 N  N     . LYS C 2 70  ? 92.633  112.027 121.439 1.00 29.89 ?  49  LYS C N     1 
ATOM   11395 C  CA    . LYS C 2 70  ? 92.845  111.382 122.734 1.00 29.49 ?  49  LYS C CA    1 
ATOM   11396 C  C     . LYS C 2 70  ? 93.050  109.862 122.597 1.00 28.74 ?  49  LYS C C     1 
ATOM   11397 O  O     . LYS C 2 70  ? 93.900  109.285 123.288 1.00 27.27 ?  49  LYS C O     1 
ATOM   11398 C  CB    . LYS C 2 70  ? 91.712  111.723 123.707 1.00 30.67 ?  49  LYS C CB    1 
ATOM   11399 C  CG    . LYS C 2 70  ? 91.862  113.129 124.340 1.00 33.73 ?  49  LYS C CG    1 
ATOM   11400 C  CD    . LYS C 2 70  ? 90.561  113.648 124.977 1.00 38.93 ?  49  LYS C CD    1 
ATOM   11401 C  CE    . LYS C 2 70  ? 90.273  113.038 126.355 1.00 41.04 ?  49  LYS C CE    1 
ATOM   11402 N  NZ    . LYS C 2 70  ? 91.177  113.544 127.431 1.00 42.21 1  49  LYS C NZ    1 
ATOM   11403 N  N     . ASN C 2 71  ? 92.283  109.238 121.697 1.00 27.54 ?  50  ASN C N     1 
ATOM   11404 C  CA    . ASN C 2 71  ? 92.435  107.814 121.387 1.00 27.00 ?  50  ASN C CA    1 
ATOM   11405 C  C     . ASN C 2 71  ? 93.832  107.470 120.870 1.00 26.19 ?  50  ASN C C     1 
ATOM   11406 O  O     . ASN C 2 71  ? 94.426  106.446 121.268 1.00 25.38 ?  50  ASN C O     1 
ATOM   11407 C  CB    . ASN C 2 71  ? 91.364  107.347 120.375 1.00 27.08 ?  50  ASN C CB    1 
ATOM   11408 C  CG    . ASN C 2 71  ? 91.422  108.098 119.024 1.00 28.69 ?  50  ASN C CG    1 
ATOM   11409 O  OD1   . ASN C 2 71  ? 91.569  109.334 118.965 1.00 30.45 ?  50  ASN C OD1   1 
ATOM   11410 N  ND2   . ASN C 2 71  ? 91.276  107.341 117.925 1.00 29.42 ?  50  ASN C ND2   1 
ATOM   11411 N  N     . GLU C 2 72  ? 94.346  108.326 119.989 1.00 24.91 ?  51  GLU C N     1 
ATOM   11412 C  CA    . GLU C 2 72  ? 95.656  108.117 119.384 1.00 24.97 ?  51  GLU C CA    1 
ATOM   11413 C  C     . GLU C 2 72  ? 96.779  108.246 120.419 1.00 24.45 ?  51  GLU C C     1 
ATOM   11414 O  O     . GLU C 2 72  ? 97.700  107.416 120.458 1.00 23.90 ?  51  GLU C O     1 
ATOM   11415 C  CB    . GLU C 2 72  ? 95.870  109.095 118.227 1.00 25.27 ?  51  GLU C CB    1 
ATOM   11416 C  CG    . GLU C 2 72  ? 94.933  108.871 117.042 1.00 26.16 ?  51  GLU C CG    1 
ATOM   11417 C  CD    . GLU C 2 72  ? 95.151  109.900 115.941 1.00 28.70 ?  51  GLU C CD    1 
ATOM   11418 O  OE1   . GLU C 2 72  ? 94.694  111.050 116.103 1.00 28.70 ?  51  GLU C OE1   1 
ATOM   11419 O  OE2   . GLU C 2 72  ? 95.779  109.560 114.914 1.00 28.92 -1 51  GLU C OE2   1 
ATOM   11420 N  N     . GLN C 2 73  ? 96.680  109.271 121.264 1.00 23.75 ?  52  GLN C N     1 
ATOM   11421 C  CA    . GLN C 2 73  ? 97.664  109.491 122.321 1.00 23.94 ?  52  GLN C CA    1 
ATOM   11422 C  C     . GLN C 2 73  ? 97.656  108.340 123.329 1.00 23.36 ?  52  GLN C C     1 
ATOM   11423 O  O     . GLN C 2 73  ? 98.708  107.924 123.800 1.00 22.95 ?  52  GLN C O     1 
ATOM   11424 C  CB    . GLN C 2 73  ? 97.400  110.815 123.054 1.00 24.28 ?  52  GLN C CB    1 
ATOM   11425 C  CG    . GLN C 2 73  ? 97.750  112.089 122.261 1.00 25.22 ?  52  GLN C CG    1 
ATOM   11426 C  CD    . GLN C 2 73  ? 97.559  113.375 123.074 1.00 29.02 ?  52  GLN C CD    1 
ATOM   11427 O  OE1   . GLN C 2 73  ? 97.152  113.336 124.233 1.00 32.08 ?  52  GLN C OE1   1 
ATOM   11428 N  NE2   . GLN C 2 73  ? 97.855  114.515 122.461 1.00 29.13 ?  52  GLN C NE2   1 
ATOM   11429 N  N     . ASP C 2 74  ? 96.460  107.859 123.671 1.00 23.02 ?  53  ASP C N     1 
ATOM   11430 C  CA    . ASP C 2 74  ? 96.301  106.755 124.610 1.00 23.44 ?  53  ASP C CA    1 
ATOM   11431 C  C     . ASP C 2 74  ? 96.985  105.490 124.077 1.00 23.00 ?  53  ASP C C     1 
ATOM   11432 O  O     . ASP C 2 74  ? 97.755  104.856 124.792 1.00 22.96 ?  53  ASP C O     1 
ATOM   11433 C  CB    . ASP C 2 74  ? 94.814  106.478 124.873 1.00 23.31 ?  53  ASP C CB    1 
ATOM   11434 C  CG    . ASP C 2 74  ? 94.597  105.457 125.971 1.00 25.80 ?  53  ASP C CG    1 
ATOM   11435 O  OD1   . ASP C 2 74  ? 95.024  105.705 127.128 1.00 27.95 ?  53  ASP C OD1   1 
ATOM   11436 O  OD2   . ASP C 2 74  ? 93.987  104.409 125.679 1.00 26.30 -1 53  ASP C OD2   1 
ATOM   11437 N  N     . THR C 2 75  ? 96.683  105.131 122.831 1.00 22.20 ?  54  THR C N     1 
ATOM   11438 C  CA    . THR C 2 75  ? 97.279  103.961 122.200 1.00 21.84 ?  54  THR C CA    1 
ATOM   11439 C  C     . THR C 2 75  ? 98.794  104.111 122.122 1.00 22.09 ?  54  THR C C     1 
ATOM   11440 O  O     . THR C 2 75  ? 99.525  103.179 122.442 1.00 21.88 ?  54  THR C O     1 
ATOM   11441 C  CB    . THR C 2 75  ? 96.669  103.683 120.797 1.00 21.74 ?  54  THR C CB    1 
ATOM   11442 O  OG1   . THR C 2 75  ? 95.294  103.329 120.958 1.00 22.09 ?  54  THR C OG1   1 
ATOM   11443 C  CG2   . THR C 2 75  ? 97.381  102.513 120.105 1.00 19.76 ?  54  THR C CG2   1 
ATOM   11444 N  N     . TYR C 2 76  ? 99.258  105.288 121.714 1.00 22.38 ?  55  TYR C N     1 
ATOM   11445 C  CA    . TYR C 2 76  ? 100.692 105.551 121.624 1.00 22.85 ?  55  TYR C CA    1 
ATOM   11446 C  C     . TYR C 2 76  ? 101.423 105.360 122.965 1.00 22.56 ?  55  TYR C C     1 
ATOM   11447 O  O     . TYR C 2 76  ? 102.459 104.701 123.003 1.00 21.97 ?  55  TYR C O     1 
ATOM   11448 C  CB    . TYR C 2 76  ? 100.939 106.950 121.078 1.00 23.57 ?  55  TYR C CB    1 
ATOM   11449 C  CG    . TYR C 2 76  ? 102.345 107.200 120.571 1.00 25.59 ?  55  TYR C CG    1 
ATOM   11450 C  CD1   . TYR C 2 76  ? 102.674 106.981 119.229 1.00 27.49 ?  55  TYR C CD1   1 
ATOM   11451 C  CD2   . TYR C 2 76  ? 103.335 107.688 121.422 1.00 27.70 ?  55  TYR C CD2   1 
ATOM   11452 C  CE1   . TYR C 2 76  ? 103.965 107.235 118.752 1.00 30.28 ?  55  TYR C CE1   1 
ATOM   11453 C  CE2   . TYR C 2 76  ? 104.633 107.941 120.958 1.00 30.38 ?  55  TYR C CE2   1 
ATOM   11454 C  CZ    . TYR C 2 76  ? 104.939 107.710 119.622 1.00 31.39 ?  55  TYR C CZ    1 
ATOM   11455 O  OH    . TYR C 2 76  ? 106.215 107.971 119.161 1.00 32.67 ?  55  TYR C OH    1 
ATOM   11456 N  N     . MET C 2 77  ? 100.890 105.938 124.043 1.00 23.14 ?  56  MET C N     1 
ATOM   11457 C  CA    . MET C 2 77  ? 101.493 105.815 125.384 1.00 23.90 ?  56  MET C CA    1 
ATOM   11458 C  C     . MET C 2 77  ? 101.571 104.355 125.810 1.00 23.24 ?  56  MET C C     1 
ATOM   11459 O  O     . MET C 2 77  ? 102.577 103.899 126.368 1.00 22.47 ?  56  MET C O     1 
ATOM   11460 C  CB    . MET C 2 77  ? 100.671 106.570 126.434 1.00 24.38 ?  56  MET C CB    1 
ATOM   11461 C  CG    . MET C 2 77  ? 100.609 108.082 126.278 1.00 28.52 ?  56  MET C CG    1 
ATOM   11462 S  SD    . MET C 2 77  ? 102.120 108.895 126.778 1.00 34.32 ?  56  MET C SD    1 
ATOM   11463 C  CE    . MET C 2 77  ? 102.154 108.555 128.541 1.00 33.84 ?  56  MET C CE    1 
ATOM   11464 N  N     . LYS C 2 78  ? 100.487 103.629 125.551 1.00 23.25 ?  57  LYS C N     1 
ATOM   11465 C  CA    . LYS C 2 78  ? 100.353 102.261 126.035 1.00 22.98 ?  57  LYS C CA    1 
ATOM   11466 C  C     . LYS C 2 78  ? 101.293 101.343 125.269 1.00 22.77 ?  57  LYS C C     1 
ATOM   11467 O  O     . LYS C 2 78  ? 101.961 100.499 125.859 1.00 22.56 ?  57  LYS C O     1 
ATOM   11468 C  CB    . LYS C 2 78  ? 98.890  101.808 125.961 1.00 22.99 ?  57  LYS C CB    1 
ATOM   11469 C  CG    . LYS C 2 78  ? 98.030  102.410 127.075 1.00 24.86 ?  57  LYS C CG    1 
ATOM   11470 C  CD    . LYS C 2 78  ? 96.541  102.117 126.891 1.00 27.37 ?  57  LYS C CD    1 
ATOM   11471 C  CE    . LYS C 2 78  ? 95.745  102.518 128.139 1.00 28.99 ?  57  LYS C CE    1 
ATOM   11472 N  NZ    . LYS C 2 78  ? 94.281  102.410 127.863 1.00 29.82 1  57  LYS C NZ    1 
ATOM   11473 N  N     . VAL C 2 79  ? 101.346 101.545 123.954 1.00 22.70 ?  58  VAL C N     1 
ATOM   11474 C  CA    . VAL C 2 79  ? 102.258 100.846 123.051 1.00 23.48 ?  58  VAL C CA    1 
ATOM   11475 C  C     . VAL C 2 79  ? 103.726 100.966 123.527 1.00 23.04 ?  58  VAL C C     1 
ATOM   11476 O  O     . VAL C 2 79  ? 104.430 99.947  123.682 1.00 22.83 ?  58  VAL C O     1 
ATOM   11477 C  CB    . VAL C 2 79  ? 102.016 101.371 121.601 1.00 24.24 ?  58  VAL C CB    1 
ATOM   11478 C  CG1   . VAL C 2 79  ? 103.287 101.464 120.777 1.00 25.71 ?  58  VAL C CG1   1 
ATOM   11479 C  CG2   . VAL C 2 79  ? 100.911 100.540 120.912 1.00 25.04 ?  58  VAL C CG2   1 
ATOM   11480 N  N     . LEU C 2 80  ? 104.165 102.190 123.807 1.00 22.84 ?  59  LEU C N     1 
ATOM   11481 C  CA    . LEU C 2 80  ? 105.537 102.417 124.266 1.00 23.35 ?  59  LEU C CA    1 
ATOM   11482 C  C     . LEU C 2 80  ? 105.766 101.840 125.667 1.00 22.75 ?  59  LEU C C     1 
ATOM   11483 O  O     . LEU C 2 80  ? 106.860 101.366 125.965 1.00 22.75 ?  59  LEU C O     1 
ATOM   11484 C  CB    . LEU C 2 80  ? 105.913 103.905 124.233 1.00 23.91 ?  59  LEU C CB    1 
ATOM   11485 C  CG    . LEU C 2 80  ? 106.052 104.698 122.919 1.00 26.63 ?  59  LEU C CG    1 
ATOM   11486 C  CD1   . LEU C 2 80  ? 106.846 105.972 123.160 1.00 26.99 ?  59  LEU C CD1   1 
ATOM   11487 C  CD2   . LEU C 2 80  ? 106.701 103.897 121.801 1.00 27.23 ?  59  LEU C CD2   1 
ATOM   11488 N  N     . ALA C 2 81  ? 104.729 101.859 126.508 1.00 22.28 ?  60  ALA C N     1 
ATOM   11489 C  CA    . ALA C 2 81  ? 104.806 101.272 127.850 1.00 22.21 ?  60  ALA C CA    1 
ATOM   11490 C  C     . ALA C 2 81  ? 104.998 99.753  127.785 1.00 22.07 ?  60  ALA C C     1 
ATOM   11491 O  O     . ALA C 2 81  ? 105.795 99.208  128.541 1.00 21.97 ?  60  ALA C O     1 
ATOM   11492 C  CB    . ALA C 2 81  ? 103.568 101.653 128.690 1.00 22.38 ?  60  ALA C CB    1 
ATOM   11493 N  N     . GLY C 2 82  ? 104.297 99.096  126.853 1.00 21.67 ?  61  GLY C N     1 
ATOM   11494 C  CA    . GLY C 2 82  ? 104.452 97.668  126.589 1.00 21.74 ?  61  GLY C CA    1 
ATOM   11495 C  C     . GLY C 2 82  ? 105.856 97.329  126.114 1.00 21.79 ?  61  GLY C C     1 
ATOM   11496 O  O     . GLY C 2 82  ? 106.432 96.303  126.505 1.00 21.93 ?  61  GLY C O     1 
ATOM   11497 N  N     . LEU C 2 83  ? 106.411 98.210  125.284 1.00 21.54 ?  62  LEU C N     1 
ATOM   11498 C  CA    . LEU C 2 83  ? 107.794 98.085  124.825 1.00 21.12 ?  62  LEU C CA    1 
ATOM   11499 C  C     . LEU C 2 83  ? 108.769 98.253  125.981 1.00 20.89 ?  62  LEU C C     1 
ATOM   11500 O  O     . LEU C 2 83  ? 109.738 97.497  126.080 1.00 20.84 ?  62  LEU C O     1 
ATOM   11501 C  CB    . LEU C 2 83  ? 108.115 99.108  123.729 1.00 21.23 ?  62  LEU C CB    1 
ATOM   11502 C  CG    . LEU C 2 83  ? 107.402 99.004  122.373 1.00 21.98 ?  62  LEU C CG    1 
ATOM   11503 C  CD1   . LEU C 2 83  ? 107.734 100.203 121.481 1.00 24.12 ?  62  LEU C CD1   1 
ATOM   11504 C  CD2   . LEU C 2 83  ? 107.738 97.714  121.651 1.00 22.03 ?  62  LEU C CD2   1 
ATOM   11505 N  N     . THR C 2 84  ? 108.511 99.241  126.839 1.00 19.93 ?  63  THR C N     1 
ATOM   11506 C  CA    . THR C 2 84  ? 109.362 99.501  127.998 1.00 19.71 ?  63  THR C CA    1 
ATOM   11507 C  C     . THR C 2 84  ? 109.450 98.273  128.890 1.00 19.63 ?  63  THR C C     1 
ATOM   11508 O  O     . THR C 2 84  ? 110.533 97.935  129.378 1.00 19.62 ?  63  THR C O     1 
ATOM   11509 C  CB    . THR C 2 84  ? 108.851 100.704 128.828 1.00 20.22 ?  63  THR C CB    1 
ATOM   11510 O  OG1   . THR C 2 84  ? 108.638 101.834 127.964 1.00 19.37 ?  63  THR C OG1   1 
ATOM   11511 C  CG2   . THR C 2 84  ? 109.839 101.057 129.913 1.00 19.45 ?  63  THR C CG2   1 
ATOM   11512 N  N     . LEU C 2 85  ? 108.314 97.614  129.104 1.00 19.66 ?  64  LEU C N     1 
ATOM   11513 C  CA    . LEU C 2 85  ? 108.264 96.417  129.940 1.00 20.51 ?  64  LEU C CA    1 
ATOM   11514 C  C     . LEU C 2 85  ? 109.135 95.302  129.353 1.00 20.84 ?  64  LEU C C     1 
ATOM   11515 O  O     . LEU C 2 85  ? 109.966 94.723  130.056 1.00 21.30 ?  64  LEU C O     1 
ATOM   11516 C  CB    . LEU C 2 85  ? 106.818 95.940  130.160 1.00 20.03 ?  64  LEU C CB    1 
ATOM   11517 C  CG    . LEU C 2 85  ? 106.699 94.653  131.010 1.00 21.43 ?  64  LEU C CG    1 
ATOM   11518 C  CD1   . LEU C 2 85  ? 107.166 94.869  132.468 1.00 21.61 ?  64  LEU C CD1   1 
ATOM   11519 C  CD2   . LEU C 2 85  ? 105.289 94.068  130.991 1.00 20.99 ?  64  LEU C CD2   1 
ATOM   11520 N  N     . LEU C 2 86  ? 108.949 95.023  128.068 1.00 21.37 ?  65  LEU C N     1 
ATOM   11521 C  CA    . LEU C 2 86  ? 109.748 94.022  127.358 1.00 21.92 ?  65  LEU C CA    1 
ATOM   11522 C  C     . LEU C 2 86  ? 111.260 94.281  127.463 1.00 21.76 ?  65  LEU C C     1 
ATOM   11523 O  O     . LEU C 2 86  ? 112.021 93.366  127.778 1.00 21.72 ?  65  LEU C O     1 
ATOM   11524 C  CB    . LEU C 2 86  ? 109.326 93.932  125.884 1.00 22.42 ?  65  LEU C CB    1 
ATOM   11525 C  CG    . LEU C 2 86  ? 107.947 93.365  125.485 1.00 24.26 ?  65  LEU C CG    1 
ATOM   11526 C  CD1   . LEU C 2 86  ? 107.742 93.520  123.979 1.00 24.67 ?  65  LEU C CD1   1 
ATOM   11527 C  CD2   . LEU C 2 86  ? 107.803 91.907  125.886 1.00 25.60 ?  65  LEU C CD2   1 
ATOM   11528 N  N     . ASP C 2 87  ? 111.688 95.517  127.197 1.00 21.75 ?  66  ASP C N     1 
ATOM   11529 C  CA    . ASP C 2 87  ? 113.110 95.894  127.318 1.00 21.99 ?  66  ASP C CA    1 
ATOM   11530 C  C     . ASP C 2 87  ? 113.648 95.851  128.752 1.00 21.76 ?  66  ASP C C     1 
ATOM   11531 O  O     . ASP C 2 87  ? 114.825 95.535  128.974 1.00 21.65 ?  66  ASP C O     1 
ATOM   11532 C  CB    . ASP C 2 87  ? 113.356 97.294  126.748 1.00 22.23 ?  66  ASP C CB    1 
ATOM   11533 C  CG    . ASP C 2 87  ? 113.793 97.267  125.310 1.00 24.59 ?  66  ASP C CG    1 
ATOM   11534 O  OD1   . ASP C 2 87  ? 114.636 96.414  124.949 1.00 27.46 ?  66  ASP C OD1   1 
ATOM   11535 O  OD2   . ASP C 2 87  ? 113.296 98.114  124.541 1.00 27.98 -1 66  ASP C OD2   1 
ATOM   11536 N  N     . THR C 2 88  ? 112.797 96.206  129.712 1.00 21.50 ?  67  THR C N     1 
ATOM   11537 C  CA    . THR C 2 88  ? 113.144 96.089  131.124 1.00 21.80 ?  67  THR C CA    1 
ATOM   11538 C  C     . THR C 2 88  ? 113.551 94.642  131.463 1.00 22.04 ?  67  THR C C     1 
ATOM   11539 O  O     . THR C 2 88  ? 114.600 94.412  132.082 1.00 22.21 ?  67  THR C O     1 
ATOM   11540 C  CB    . THR C 2 88  ? 111.989 96.569  132.020 1.00 22.15 ?  67  THR C CB    1 
ATOM   11541 O  OG1   . THR C 2 88  ? 111.707 97.938  131.723 1.00 22.23 ?  67  THR C OG1   1 
ATOM   11542 C  CG2   . THR C 2 88  ? 112.338 96.448  133.506 1.00 21.19 ?  67  THR C CG2   1 
ATOM   11543 N  N     . GLU C 2 89  ? 112.743 93.681  131.027 1.00 21.55 ?  68  GLU C N     1 
ATOM   11544 C  CA    . GLU C 2 89  ? 113.003 92.282  131.341 1.00 21.81 ?  68  GLU C CA    1 
ATOM   11545 C  C     . GLU C 2 89  ? 114.116 91.686  130.464 1.00 21.35 ?  68  GLU C C     1 
ATOM   11546 O  O     . GLU C 2 89  ? 114.899 90.861  130.929 1.00 21.34 ?  68  GLU C O     1 
ATOM   11547 C  CB    . GLU C 2 89  ? 111.708 91.464  131.298 1.00 22.25 ?  68  GLU C CB    1 
ATOM   11548 C  CG    . GLU C 2 89  ? 110.845 91.635  132.581 1.00 24.02 ?  68  GLU C CG    1 
ATOM   11549 C  CD    . GLU C 2 89  ? 111.633 91.366  133.865 1.00 25.78 ?  68  GLU C CD    1 
ATOM   11550 O  OE1   . GLU C 2 89  ? 112.367 90.357  133.928 1.00 26.69 ?  68  GLU C OE1   1 
ATOM   11551 O  OE2   . GLU C 2 89  ? 111.518 92.165  134.824 1.00 28.98 -1 68  GLU C OE2   1 
ATOM   11552 N  N     . GLN C 2 90  ? 114.214 92.146  129.218 1.00 20.82 ?  69  GLN C N     1 
ATOM   11553 C  CA    . GLN C 2 90  ? 115.289 91.716  128.332 1.00 21.28 ?  69  GLN C CA    1 
ATOM   11554 C  C     . GLN C 2 90  ? 116.651 92.180  128.859 1.00 21.24 ?  69  GLN C C     1 
ATOM   11555 O  O     . GLN C 2 90  ? 117.639 91.446  128.763 1.00 20.99 ?  69  GLN C O     1 
ATOM   11556 C  CB    . GLN C 2 90  ? 115.050 92.206  126.892 1.00 21.86 ?  69  GLN C CB    1 
ATOM   11557 C  CG    . GLN C 2 90  ? 115.936 91.507  125.835 1.00 24.29 ?  69  GLN C CG    1 
ATOM   11558 C  CD    . GLN C 2 90  ? 115.564 90.036  125.618 1.00 27.14 ?  69  GLN C CD    1 
ATOM   11559 O  OE1   . GLN C 2 90  ? 114.940 89.407  126.477 1.00 27.13 ?  69  GLN C OE1   1 
ATOM   11560 N  NE2   . GLN C 2 90  ? 115.966 89.482  124.471 1.00 27.69 ?  69  GLN C NE2   1 
ATOM   11561 N  N     . GLY C 2 91  ? 116.683 93.381  129.443 1.00 20.62 ?  70  GLY C N     1 
ATOM   11562 C  CA    . GLY C 2 91  ? 117.912 93.947  130.006 1.00 22.00 ?  70  GLY C CA    1 
ATOM   11563 C  C     . GLY C 2 91  ? 118.247 93.419  131.387 1.00 22.45 ?  70  GLY C C     1 
ATOM   11564 O  O     . GLY C 2 91  ? 119.402 93.094  131.649 1.00 23.53 ?  70  GLY C O     1 
ATOM   11565 N  N     . ASN C 2 92  ? 117.243 93.334  132.262 1.00 22.79 ?  71  ASN C N     1 
ATOM   11566 C  CA    . ASN C 2 92  ? 117.436 92.867  133.645 1.00 23.85 ?  71  ASN C CA    1 
ATOM   11567 C  C     . ASN C 2 92  ? 117.716 91.371  133.726 1.00 24.33 ?  71  ASN C C     1 
ATOM   11568 O  O     . ASN C 2 92  ? 118.484 90.925  134.586 1.00 24.17 ?  71  ASN C O     1 
ATOM   11569 C  CB    . ASN C 2 92  ? 116.195 93.145  134.503 1.00 23.74 ?  71  ASN C CB    1 
ATOM   11570 C  CG    . ASN C 2 92  ? 115.967 94.621  134.779 1.00 24.38 ?  71  ASN C CG    1 
ATOM   11571 O  OD1   . ASN C 2 92  ? 116.707 95.496  134.313 1.00 25.16 ?  71  ASN C OD1   1 
ATOM   11572 N  ND2   . ASN C 2 92  ? 114.923 94.904  135.540 1.00 24.07 ?  71  ASN C ND2   1 
ATOM   11573 N  N     . THR C 2 93  ? 117.095 90.603  132.828 1.00 23.97 ?  72  THR C N     1 
ATOM   11574 C  CA    . THR C 2 93  ? 116.992 89.149  133.015 1.00 24.97 ?  72  THR C CA    1 
ATOM   11575 C  C     . THR C 2 93  ? 117.470 88.364  131.802 1.00 24.52 ?  72  THR C C     1 
ATOM   11576 O  O     . THR C 2 93  ? 118.396 87.570  131.911 1.00 25.39 ?  72  THR C O     1 
ATOM   11577 C  CB    . THR C 2 93  ? 115.539 88.724  133.361 1.00 24.54 ?  72  THR C CB    1 
ATOM   11578 O  OG1   . THR C 2 93  ? 115.074 89.471  134.492 1.00 26.43 ?  72  THR C OG1   1 
ATOM   11579 C  CG2   . THR C 2 93  ? 115.464 87.241  133.688 1.00 26.83 ?  72  THR C CG2   1 
ATOM   11580 N  N     . GLY C 2 94  ? 116.838 88.602  130.662 1.00 24.37 ?  73  GLY C N     1 
ATOM   11581 C  CA    . GLY C 2 94  ? 117.035 87.791  129.450 1.00 24.24 ?  73  GLY C CA    1 
ATOM   11582 C  C     . GLY C 2 94  ? 118.457 87.771  128.934 1.00 24.94 ?  73  GLY C C     1 
ATOM   11583 O  O     . GLY C 2 94  ? 119.085 86.709  128.859 1.00 25.86 ?  73  GLY C O     1 
ATOM   11584 N  N     . MET C 2 95  ? 118.973 88.941  128.574 1.00 24.07 ?  74  MET C N     1 
ATOM   11585 C  CA    . MET C 2 95  ? 120.331 89.014  128.052 1.00 24.35 ?  74  MET C CA    1 
ATOM   11586 C  C     . MET C 2 95  ? 121.433 88.615  129.052 1.00 23.52 ?  74  MET C C     1 
ATOM   11587 O  O     . MET C 2 95  ? 122.326 87.871  128.661 1.00 23.40 ?  74  MET C O     1 
ATOM   11588 C  CB    . MET C 2 95  ? 120.607 90.367  127.394 1.00 24.38 ?  74  MET C CB    1 
ATOM   11589 C  CG    . MET C 2 95  ? 119.865 90.578  126.074 1.00 27.47 ?  74  MET C CG    1 
ATOM   11590 S  SD    . MET C 2 95  ? 120.386 89.359  124.836 1.00 32.54 ?  74  MET C SD    1 
ATOM   11591 C  CE    . MET C 2 95  ? 122.006 89.936  124.472 1.00 34.32 ?  74  MET C CE    1 
ATOM   11592 N  N     . PRO C 2 96  ? 121.373 89.092  130.328 1.00 23.36 ?  75  PRO C N     1 
ATOM   11593 C  CA    . PRO C 2 96  ? 122.369 88.651  131.328 1.00 23.27 ?  75  PRO C CA    1 
ATOM   11594 C  C     . PRO C 2 96  ? 122.376 87.148  131.587 1.00 23.77 ?  75  PRO C C     1 
ATOM   11595 O  O     . PRO C 2 96  ? 123.450 86.561  131.714 1.00 23.46 ?  75  PRO C O     1 
ATOM   11596 C  CB    . PRO C 2 96  ? 121.936 89.376  132.613 1.00 23.55 ?  75  PRO C CB    1 
ATOM   11597 C  CG    . PRO C 2 96  ? 121.222 90.594  132.135 1.00 23.85 ?  75  PRO C CG    1 
ATOM   11598 C  CD    . PRO C 2 96  ? 120.493 90.142  130.879 1.00 22.76 ?  75  PRO C CD    1 
ATOM   11599 N  N     . ILE C 2 97  ? 121.196 86.532  131.686 1.00 23.81 ?  76  ILE C N     1 
ATOM   11600 C  CA    . ILE C 2 97  ? 121.114 85.089  131.927 1.00 24.52 ?  76  ILE C CA    1 
ATOM   11601 C  C     . ILE C 2 97  ? 121.647 84.247  130.748 1.00 23.92 ?  76  ILE C C     1 
ATOM   11602 O  O     . ILE C 2 97  ? 122.372 83.263  130.952 1.00 23.99 ?  76  ILE C O     1 
ATOM   11603 C  CB    . ILE C 2 97  ? 119.691 84.651  132.377 1.00 24.49 ?  76  ILE C CB    1 
ATOM   11604 C  CG1   . ILE C 2 97  ? 119.753 83.330  133.141 1.00 27.08 ?  76  ILE C CG1   1 
ATOM   11605 C  CG2   . ILE C 2 97  ? 118.711 84.543  131.189 1.00 26.06 ?  76  ILE C CG2   1 
ATOM   11606 C  CD1   . ILE C 2 97  ? 118.583 83.145  134.096 1.00 31.37 ?  76  ILE C CD1   1 
ATOM   11607 N  N     . VAL C 2 98  ? 121.318 84.647  129.524 1.00 23.97 ?  77  VAL C N     1 
ATOM   11608 C  CA    . VAL C 2 98  ? 121.886 83.996  128.336 1.00 24.01 ?  77  VAL C CA    1 
ATOM   11609 C  C     . VAL C 2 98  ? 123.417 84.198  128.307 1.00 25.23 ?  77  VAL C C     1 
ATOM   11610 O  O     . VAL C 2 98  ? 124.168 83.251  128.056 1.00 25.77 ?  77  VAL C O     1 
ATOM   11611 C  CB    . VAL C 2 98  ? 121.209 84.490  127.032 1.00 23.98 ?  77  VAL C CB    1 
ATOM   11612 C  CG1   . VAL C 2 98  ? 121.981 84.030  125.798 1.00 23.17 ?  77  VAL C CG1   1 
ATOM   11613 C  CG2   . VAL C 2 98  ? 119.760 83.990  126.976 1.00 22.55 ?  77  VAL C CG2   1 
ATOM   11614 N  N     . ALA C 2 99  ? 123.874 85.412  128.621 1.00 25.42 ?  78  ALA C N     1 
ATOM   11615 C  CA    . ALA C 2 99  ? 125.320 85.680  128.706 1.00 26.72 ?  78  ALA C CA    1 
ATOM   11616 C  C     . ALA C 2 99  ? 126.010 84.725  129.685 1.00 27.46 ?  78  ALA C C     1 
ATOM   11617 O  O     . ALA C 2 99  ? 127.085 84.204  129.393 1.00 28.07 ?  78  ALA C O     1 
ATOM   11618 C  CB    . ALA C 2 99  ? 125.586 87.122  129.097 1.00 26.52 ?  78  ALA C CB    1 
ATOM   11619 N  N     . GLU C 2 100 ? 125.364 84.471  130.822 1.00 28.33 ?  79  GLU C N     1 
ATOM   11620 C  CA    . GLU C 2 100 ? 125.923 83.598  131.857 1.00 29.60 ?  79  GLU C CA    1 
ATOM   11621 C  C     . GLU C 2 100 ? 126.168 82.174  131.352 1.00 29.64 ?  79  GLU C C     1 
ATOM   11622 O  O     . GLU C 2 100 ? 127.163 81.536  131.716 1.00 29.72 ?  79  GLU C O     1 
ATOM   11623 C  CB    . GLU C 2 100 ? 125.022 83.583  133.092 1.00 29.70 ?  79  GLU C CB    1 
ATOM   11624 C  CG    . GLU C 2 100 ? 125.571 82.758  134.255 1.00 33.58 ?  79  GLU C CG    1 
ATOM   11625 C  CD    . GLU C 2 100 ? 124.615 82.643  135.426 1.00 37.83 ?  79  GLU C CD    1 
ATOM   11626 O  OE1   . GLU C 2 100 ? 123.564 83.329  135.445 1.00 40.64 ?  79  GLU C OE1   1 
ATOM   11627 O  OE2   . GLU C 2 100 ? 124.916 81.845  136.340 1.00 41.40 -1 79  GLU C OE2   1 
ATOM   11628 N  N     . HIS C 2 101 ? 125.271 81.685  130.499 1.00 29.43 ?  80  HIS C N     1 
ATOM   11629 C  CA    . HIS C 2 101 ? 125.304 80.287  130.089 1.00 29.74 ?  80  HIS C CA    1 
ATOM   11630 C  C     . HIS C 2 101 ? 126.032 80.014  128.772 1.00 30.18 ?  80  HIS C C     1 
ATOM   11631 O  O     . HIS C 2 101 ? 126.383 78.876  128.486 1.00 30.30 ?  80  HIS C O     1 
ATOM   11632 C  CB    . HIS C 2 101 ? 123.886 79.693  130.111 1.00 29.21 ?  80  HIS C CB    1 
ATOM   11633 C  CG    . HIS C 2 101 ? 123.339 79.532  131.496 1.00 29.60 ?  80  HIS C CG    1 
ATOM   11634 N  ND1   . HIS C 2 101 ? 122.596 80.509  132.125 1.00 30.06 ?  80  HIS C ND1   1 
ATOM   11635 C  CD2   . HIS C 2 101 ? 123.467 78.524  132.391 1.00 29.49 ?  80  HIS C CD2   1 
ATOM   11636 C  CE1   . HIS C 2 101 ? 122.277 80.104  133.343 1.00 29.56 ?  80  HIS C CE1   1 
ATOM   11637 N  NE2   . HIS C 2 101 ? 122.792 78.903  133.528 1.00 30.20 ?  80  HIS C NE2   1 
ATOM   11638 N  N     . VAL C 2 102 ? 126.271 81.061  127.986 1.00 30.70 ?  81  VAL C N     1 
ATOM   11639 C  CA    . VAL C 2 102 ? 126.984 80.939  126.717 1.00 31.47 ?  81  VAL C CA    1 
ATOM   11640 C  C     . VAL C 2 102 ? 128.489 81.007  126.969 1.00 32.45 ?  81  VAL C C     1 
ATOM   11641 O  O     . VAL C 2 102 ? 128.960 81.908  127.673 1.00 32.50 ?  81  VAL C O     1 
ATOM   11642 C  CB    . VAL C 2 102 ? 126.562 82.038  125.707 1.00 31.18 ?  81  VAL C CB    1 
ATOM   11643 C  CG1   . VAL C 2 102 ? 127.461 82.027  124.468 1.00 31.20 ?  81  VAL C CG1   1 
ATOM   11644 C  CG2   . VAL C 2 102 ? 125.111 81.845  125.289 1.00 31.28 ?  81  VAL C CG2   1 
ATOM   11645 N  N     . ASP C 2 103 ? 129.228 80.062  126.383 1.00 33.38 ?  82  ASP C N     1 
ATOM   11646 C  CA    . ASP C 2 103 ? 130.681 79.974  126.557 1.00 34.82 ?  82  ASP C CA    1 
ATOM   11647 C  C     . ASP C 2 103 ? 131.458 80.844  125.576 1.00 34.74 ?  82  ASP C C     1 
ATOM   11648 O  O     . ASP C 2 103 ? 131.089 80.957  124.400 1.00 35.00 ?  82  ASP C O     1 
ATOM   11649 C  CB    . ASP C 2 103 ? 131.155 78.518  126.443 1.00 35.82 ?  82  ASP C CB    1 
ATOM   11650 C  CG    . ASP C 2 103 ? 130.786 77.678  127.663 1.00 38.29 ?  82  ASP C CG    1 
ATOM   11651 O  OD1   . ASP C 2 103 ? 130.738 78.223  128.792 1.00 41.49 ?  82  ASP C OD1   1 
ATOM   11652 O  OD2   . ASP C 2 103 ? 130.546 76.468  127.493 1.00 41.10 -1 82  ASP C OD2   1 
ATOM   11653 N  N     . GLY C 2 104 ? 132.538 81.449  126.071 1.00 34.89 ?  83  GLY C N     1 
ATOM   11654 C  CA    . GLY C 2 104 ? 133.443 82.254  125.243 1.00 35.11 ?  83  GLY C CA    1 
ATOM   11655 C  C     . GLY C 2 104 ? 133.376 83.734  125.565 1.00 34.96 ?  83  GLY C C     1 
ATOM   11656 O  O     . GLY C 2 104 ? 132.304 84.339  125.486 1.00 34.57 ?  83  GLY C O     1 
ATOM   11657 N  N     . HIS C 2 105 ? 134.526 84.318  125.911 1.00 35.02 ?  84  HIS C N     1 
ATOM   11658 C  CA    . HIS C 2 105 ? 134.599 85.716  126.357 1.00 34.83 ?  84  HIS C CA    1 
ATOM   11659 C  C     . HIS C 2 105 ? 134.075 86.725  125.344 1.00 33.77 ?  84  HIS C C     1 
ATOM   11660 O  O     . HIS C 2 105 ? 133.471 87.730  125.725 1.00 33.25 ?  84  HIS C O     1 
ATOM   11661 C  CB    . HIS C 2 105 ? 136.018 86.091  126.801 1.00 36.09 ?  84  HIS C CB    1 
ATOM   11662 C  CG    . HIS C 2 105 ? 136.394 85.530  128.139 1.00 39.17 ?  84  HIS C CG    1 
ATOM   11663 N  ND1   . HIS C 2 105 ? 137.682 85.143  128.451 1.00 43.00 ?  84  HIS C ND1   1 
ATOM   11664 C  CD2   . HIS C 2 105 ? 135.646 85.270  129.240 1.00 41.84 ?  84  HIS C CD2   1 
ATOM   11665 C  CE1   . HIS C 2 105 ? 137.711 84.679  129.689 1.00 43.47 ?  84  HIS C CE1   1 
ATOM   11666 N  NE2   . HIS C 2 105 ? 136.489 84.745  130.190 1.00 43.10 ?  84  HIS C NE2   1 
ATOM   11667 N  N     . GLN C 2 106 ? 134.286 86.454  124.062 1.00 32.84 ?  85  GLN C N     1 
ATOM   11668 C  CA    . GLN C 2 106 ? 133.788 87.352  123.024 1.00 32.29 ?  85  GLN C CA    1 
ATOM   11669 C  C     . GLN C 2 106 ? 132.267 87.258  122.855 1.00 30.88 ?  85  GLN C C     1 
ATOM   11670 O  O     . GLN C 2 106 ? 131.596 88.283  122.683 1.00 30.44 ?  85  GLN C O     1 
ATOM   11671 C  CB    . GLN C 2 106 ? 134.493 87.101  121.700 1.00 32.85 ?  85  GLN C CB    1 
ATOM   11672 C  CG    . GLN C 2 106 ? 135.979 87.435  121.728 1.00 35.55 ?  85  GLN C CG    1 
ATOM   11673 C  CD    . GLN C 2 106 ? 136.665 87.073  120.438 1.00 38.12 ?  85  GLN C CD    1 
ATOM   11674 O  OE1   . GLN C 2 106 ? 136.097 87.227  119.357 1.00 39.96 ?  85  GLN C OE1   1 
ATOM   11675 N  NE2   . GLN C 2 106 ? 137.901 86.588  120.540 1.00 40.39 ?  85  GLN C NE2   1 
ATOM   11676 N  N     . ARG C 2 107 ? 131.731 86.039  122.899 1.00 29.75 ?  86  ARG C N     1 
ATOM   11677 C  CA    . ARG C 2 107 ? 130.277 85.845  122.850 1.00 28.87 ?  86  ARG C CA    1 
ATOM   11678 C  C     . ARG C 2 107 ? 129.633 86.525  124.051 1.00 28.16 ?  86  ARG C C     1 
ATOM   11679 O  O     . ARG C 2 107 ? 128.605 87.186  123.911 1.00 27.55 ?  86  ARG C O     1 
ATOM   11680 C  CB    . ARG C 2 107 ? 129.910 84.363  122.823 1.00 28.48 ?  86  ARG C CB    1 
ATOM   11681 C  CG    . ARG C 2 107 ? 130.226 83.689  121.500 1.00 29.86 ?  86  ARG C CG    1 
ATOM   11682 C  CD    . ARG C 2 107 ? 129.887 82.208  121.513 1.00 30.23 ?  86  ARG C CD    1 
ATOM   11683 N  NE    . ARG C 2 107 ? 129.776 81.736  120.138 1.00 33.04 ?  86  ARG C NE    1 
ATOM   11684 C  CZ    . ARG C 2 107 ? 129.160 80.628  119.763 1.00 31.54 ?  86  ARG C CZ    1 
ATOM   11685 N  NH1   . ARG C 2 107 ? 128.598 79.833  120.663 1.00 31.85 1  86  ARG C NH1   1 
ATOM   11686 N  NH2   . ARG C 2 107 ? 129.119 80.317  118.478 1.00 34.74 ?  86  ARG C NH2   1 
ATOM   11687 N  N     . LYS C 2 108 ? 130.250 86.372  125.221 1.00 27.65 ?  87  LYS C N     1 
ATOM   11688 C  CA    . LYS C 2 108 ? 129.754 87.028  126.436 1.00 27.96 ?  87  LYS C CA    1 
ATOM   11689 C  C     . LYS C 2 108 ? 129.811 88.546  126.351 1.00 27.75 ?  87  LYS C C     1 
ATOM   11690 O  O     . LYS C 2 108 ? 128.913 89.222  126.851 1.00 28.29 ?  87  LYS C O     1 
ATOM   11691 C  CB    . LYS C 2 108 ? 130.500 86.551  127.682 1.00 27.80 ?  87  LYS C CB    1 
ATOM   11692 C  CG    . LYS C 2 108 ? 130.205 85.114  128.058 1.00 29.04 ?  87  LYS C CG    1 
ATOM   11693 C  CD    . LYS C 2 108 ? 130.966 84.741  129.322 1.00 31.15 ?  87  LYS C CD    1 
ATOM   11694 C  CE    . LYS C 2 108 ? 130.870 83.254  129.609 1.00 32.05 ?  87  LYS C CE    1 
ATOM   11695 N  NZ    . LYS C 2 108 ? 129.551 82.914  130.198 1.00 30.88 1  87  LYS C NZ    1 
ATOM   11696 N  N     . ALA C 2 109 ? 130.858 89.081  125.722 1.00 27.69 ?  88  ALA C N     1 
ATOM   11697 C  CA    . ALA C 2 109 ? 130.985 90.534  125.544 1.00 27.46 ?  88  ALA C CA    1 
ATOM   11698 C  C     . ALA C 2 109 ? 129.876 91.120  124.666 1.00 26.87 ?  88  ALA C C     1 
ATOM   11699 O  O     . ALA C 2 109 ? 129.371 92.206  124.944 1.00 26.47 ?  88  ALA C O     1 
ATOM   11700 C  CB    . ALA C 2 109 ? 132.345 90.886  124.977 1.00 27.98 ?  88  ALA C CB    1 
ATOM   11701 N  N     . VAL C 2 110 ? 129.518 90.405  123.601 1.00 25.98 ?  89  VAL C N     1 
ATOM   11702 C  CA    . VAL C 2 110 ? 128.422 90.817  122.720 1.00 25.46 ?  89  VAL C CA    1 
ATOM   11703 C  C     . VAL C 2 110 ? 127.098 90.790  123.490 1.00 24.57 ?  89  VAL C C     1 
ATOM   11704 O  O     . VAL C 2 110 ? 126.348 91.771  123.488 1.00 23.62 ?  89  VAL C O     1 
ATOM   11705 C  CB    . VAL C 2 110 ? 128.344 89.926  121.456 1.00 25.80 ?  89  VAL C CB    1 
ATOM   11706 C  CG1   . VAL C 2 110 ? 127.060 90.193  120.658 1.00 25.44 ?  89  VAL C CG1   1 
ATOM   11707 C  CG2   . VAL C 2 110 ? 129.577 90.141  120.579 1.00 26.23 ?  89  VAL C CG2   1 
ATOM   11708 N  N     . LEU C 2 111 ? 126.835 89.679  124.176 1.00 24.33 ?  90  LEU C N     1 
ATOM   11709 C  CA    . LEU C 2 111 ? 125.593 89.541  124.938 1.00 23.93 ?  90  LEU C CA    1 
ATOM   11710 C  C     . LEU C 2 111 ? 125.477 90.551  126.080 1.00 23.77 ?  90  LEU C C     1 
ATOM   11711 O  O     . LEU C 2 111 ? 124.389 91.067  126.335 1.00 23.04 ?  90  LEU C O     1 
ATOM   11712 C  CB    . LEU C 2 111 ? 125.401 88.108  125.442 1.00 23.73 ?  90  LEU C CB    1 
ATOM   11713 C  CG    . LEU C 2 111 ? 125.240 87.058  124.339 1.00 24.50 ?  90  LEU C CG    1 
ATOM   11714 C  CD1   . LEU C 2 111 ? 125.527 85.662  124.871 1.00 24.02 ?  90  LEU C CD1   1 
ATOM   11715 C  CD2   . LEU C 2 111 ? 123.854 87.123  123.693 1.00 25.38 ?  90  LEU C CD2   1 
ATOM   11716 N  N     . ASN C 2 112 ? 126.591 90.820  126.769 1.00 24.24 ?  91  ASN C N     1 
ATOM   11717 C  CA    . ASN C 2 112 ? 126.629 91.877  127.792 1.00 24.95 ?  91  ASN C CA    1 
ATOM   11718 C  C     . ASN C 2 112 ? 126.344 93.268  127.231 1.00 24.25 ?  91  ASN C C     1 
ATOM   11719 O  O     . ASN C 2 112 ? 125.650 94.062  127.864 1.00 23.99 ?  91  ASN C O     1 
ATOM   11720 C  CB    . ASN C 2 112 ? 127.977 91.904  128.520 1.00 25.81 ?  91  ASN C CB    1 
ATOM   11721 C  CG    . ASN C 2 112 ? 128.022 90.945  129.678 1.00 29.96 ?  91  ASN C CG    1 
ATOM   11722 O  OD1   . ASN C 2 112 ? 127.699 91.316  130.808 1.00 35.44 ?  91  ASN C OD1   1 
ATOM   11723 N  ND2   . ASN C 2 112 ? 128.421 89.701  129.414 1.00 32.37 ?  91  ASN C ND2   1 
ATOM   11724 N  N     . PHE C 2 113 ? 126.914 93.567  126.065 1.00 23.60 ?  92  PHE C N     1 
ATOM   11725 C  CA    . PHE C 2 113 ? 126.652 94.836  125.393 1.00 23.32 ?  92  PHE C CA    1 
ATOM   11726 C  C     . PHE C 2 113 ? 125.169 94.973  125.019 1.00 22.63 ?  92  PHE C C     1 
ATOM   11727 O  O     . PHE C 2 113 ? 124.568 96.026  125.241 1.00 21.94 ?  92  PHE C O     1 
ATOM   11728 C  CB    . PHE C 2 113 ? 127.502 94.985  124.123 1.00 23.27 ?  92  PHE C CB    1 
ATOM   11729 C  CG    . PHE C 2 113 ? 127.455 96.368  123.535 1.00 24.66 ?  92  PHE C CG    1 
ATOM   11730 C  CD1   . PHE C 2 113 ? 128.371 97.347  123.948 1.00 25.72 ?  92  PHE C CD1   1 
ATOM   11731 C  CD2   . PHE C 2 113 ? 126.488 96.707  122.592 1.00 25.36 ?  92  PHE C CD2   1 
ATOM   11732 C  CE1   . PHE C 2 113 ? 128.321 98.638  123.420 1.00 25.92 ?  92  PHE C CE1   1 
ATOM   11733 C  CE2   . PHE C 2 113 ? 126.428 98.000  122.057 1.00 25.82 ?  92  PHE C CE2   1 
ATOM   11734 C  CZ    . PHE C 2 113 ? 127.343 98.967  122.476 1.00 25.80 ?  92  PHE C CZ    1 
ATOM   11735 N  N     . MET C 2 114 ? 124.605 93.914  124.432 1.00 22.03 ?  93  MET C N     1 
ATOM   11736 C  CA    . MET C 2 114 ? 123.176 93.883  124.090 1.00 22.14 ?  93  MET C CA    1 
ATOM   11737 C  C     . MET C 2 114 ? 122.280 94.088  125.324 1.00 21.64 ?  93  MET C C     1 
ATOM   11738 O  O     . MET C 2 114 ? 121.307 94.847  125.264 1.00 21.59 ?  93  MET C O     1 
ATOM   11739 C  CB    . MET C 2 114 ? 122.822 92.582  123.379 1.00 22.46 ?  93  MET C CB    1 
ATOM   11740 C  CG    . MET C 2 114 ? 123.430 92.458  121.991 1.00 23.80 ?  93  MET C CG    1 
ATOM   11741 S  SD    . MET C 2 114 ? 123.147 90.829  121.263 1.00 28.07 ?  93  MET C SD    1 
ATOM   11742 C  CE    . MET C 2 114 ? 123.668 91.169  119.561 1.00 26.42 ?  93  MET C CE    1 
ATOM   11743 N  N     . ALA C 2 115 ? 122.631 93.440  126.440 1.00 20.98 ?  94  ALA C N     1 
ATOM   11744 C  CA    . ALA C 2 115 ? 121.929 93.632  127.723 1.00 20.58 ?  94  ALA C CA    1 
ATOM   11745 C  C     . ALA C 2 115 ? 121.931 95.086  128.192 1.00 21.01 ?  94  ALA C C     1 
ATOM   11746 O  O     . ALA C 2 115 ? 120.906 95.609  128.667 1.00 21.06 ?  94  ALA C O     1 
ATOM   11747 C  CB    . ALA C 2 115 ? 122.543 92.717  128.810 1.00 20.83 ?  94  ALA C CB    1 
ATOM   11748 N  N     . MET C 2 116 ? 123.093 95.730  128.096 1.00 20.36 ?  95  MET C N     1 
ATOM   11749 C  CA    . MET C 2 116 ? 123.219 97.128  128.464 1.00 20.83 ?  95  MET C CA    1 
ATOM   11750 C  C     . MET C 2 116 ? 122.294 97.997  127.596 1.00 20.55 ?  95  MET C C     1 
ATOM   11751 O  O     . MET C 2 116 ? 121.585 98.862  128.108 1.00 20.70 ?  95  MET C O     1 
ATOM   11752 C  CB    . MET C 2 116 ? 124.685 97.568  128.347 1.00 20.64 ?  95  MET C CB    1 
ATOM   11753 C  CG    . MET C 2 116 ? 124.942 99.056  128.586 1.00 21.42 ?  95  MET C CG    1 
ATOM   11754 S  SD    . MET C 2 116 ? 124.562 100.059 127.136 1.00 22.51 ?  95  MET C SD    1 
ATOM   11755 C  CE    . MET C 2 116 ? 125.693 99.380  125.920 1.00 20.66 ?  95  MET C CE    1 
ATOM   11756 N  N     . MET C 2 117 ? 122.290 97.743  126.292 1.00 20.50 ?  96  MET C N     1 
ATOM   11757 C  CA    . MET C 2 117 ? 121.435 98.489  125.379 1.00 21.22 ?  96  MET C CA    1 
ATOM   11758 C  C     . MET C 2 117 ? 119.965 98.382  125.780 1.00 21.11 ?  96  MET C C     1 
ATOM   11759 O  O     . MET C 2 117 ? 119.255 99.390  125.789 1.00 20.71 ?  96  MET C O     1 
ATOM   11760 C  CB    . MET C 2 117 ? 121.646 98.042  123.926 1.00 21.35 ?  96  MET C CB    1 
ATOM   11761 C  CG    . MET C 2 117 ? 122.997 98.492  123.285 1.00 22.54 ?  96  MET C CG    1 
ATOM   11762 S  SD    . MET C 2 117 ? 123.346 100.264 123.341 1.00 24.89 ?  96  MET C SD    1 
ATOM   11763 C  CE    . MET C 2 117 ? 122.243 100.879 122.068 1.00 24.95 ?  96  MET C CE    1 
ATOM   11764 N  N     . GLU C 2 118 ? 119.527 97.172  126.131 1.00 21.18 ?  97  GLU C N     1 
ATOM   11765 C  CA    . GLU C 2 118 ? 118.136 96.923  126.523 1.00 21.99 ?  97  GLU C CA    1 
ATOM   11766 C  C     . GLU C 2 118 ? 117.668 97.837  127.657 1.00 22.10 ?  97  GLU C C     1 
ATOM   11767 O  O     . GLU C 2 118 ? 116.666 98.541  127.516 1.00 22.22 ?  97  GLU C O     1 
ATOM   11768 C  CB    . GLU C 2 118 ? 117.900 95.455  126.917 1.00 22.01 ?  97  GLU C CB    1 
ATOM   11769 C  CG    . GLU C 2 118 ? 118.326 94.381  125.908 1.00 24.38 ?  97  GLU C CG    1 
ATOM   11770 C  CD    . GLU C 2 118 ? 117.632 94.455  124.542 1.00 26.32 ?  97  GLU C CD    1 
ATOM   11771 O  OE1   . GLU C 2 118 ? 117.284 95.549  124.075 1.00 29.86 ?  97  GLU C OE1   1 
ATOM   11772 O  OE2   . GLU C 2 118 ? 117.480 93.402  123.900 1.00 29.19 -1 97  GLU C OE2   1 
ATOM   11773 N  N     . ASN C 2 119 ? 118.384 97.831  128.780 1.00 22.26 ?  98  ASN C N     1 
ATOM   11774 C  CA    . ASN C 2 119 ? 117.905 98.578  129.944 1.00 21.91 ?  98  ASN C CA    1 
ATOM   11775 C  C     . ASN C 2 119 ? 118.519 99.966  130.180 1.00 22.41 ?  98  ASN C C     1 
ATOM   11776 O  O     . ASN C 2 119 ? 117.863 100.840 130.744 1.00 23.07 ?  98  ASN C O     1 
ATOM   11777 C  CB    . ASN C 2 119 ? 117.833 97.708  131.218 1.00 21.93 ?  98  ASN C CB    1 
ATOM   11778 C  CG    . ASN C 2 119 ? 119.181 97.192  131.674 1.00 21.31 ?  98  ASN C CG    1 
ATOM   11779 O  OD1   . ASN C 2 119 ? 120.211 97.435  131.043 1.00 21.88 ?  98  ASN C OD1   1 
ATOM   11780 N  ND2   . ASN C 2 119 ? 119.180 96.479  132.799 1.00 21.73 ?  98  ASN C ND2   1 
ATOM   11781 N  N     . ALA C 2 120 ? 119.767 100.161 129.764 1.00 22.75 ?  99  ALA C N     1 
ATOM   11782 C  CA    . ALA C 2 120 ? 120.434 101.453 129.920 1.00 23.12 ?  99  ALA C CA    1 
ATOM   11783 C  C     . ALA C 2 120 ? 120.151 102.405 128.775 1.00 23.60 ?  99  ALA C C     1 
ATOM   11784 O  O     . ALA C 2 120 ? 120.256 103.623 128.956 1.00 24.14 ?  99  ALA C O     1 
ATOM   11785 C  CB    . ALA C 2 120 ? 121.954 101.284 130.123 1.00 23.28 ?  99  ALA C CB    1 
ATOM   11786 N  N     . VAL C 2 121 ? 119.789 101.869 127.604 1.00 23.23 ?  100 VAL C N     1 
ATOM   11787 C  CA    . VAL C 2 121 ? 119.504 102.733 126.443 1.00 23.74 ?  100 VAL C CA    1 
ATOM   11788 C  C     . VAL C 2 121 ? 118.049 102.675 125.976 1.00 23.62 ?  100 VAL C C     1 
ATOM   11789 O  O     . VAL C 2 121 ? 117.378 103.703 125.951 1.00 24.51 ?  100 VAL C O     1 
ATOM   11790 C  CB    . VAL C 2 121 ? 120.461 102.469 125.261 1.00 23.19 ?  100 VAL C CB    1 
ATOM   11791 C  CG1   . VAL C 2 121 ? 120.097 103.352 124.053 1.00 24.10 ?  100 VAL C CG1   1 
ATOM   11792 C  CG2   . VAL C 2 121 ? 121.916 102.716 125.691 1.00 23.48 ?  100 VAL C CG2   1 
ATOM   11793 N  N     . HIS C 2 122 ? 117.570 101.484 125.622 1.00 23.45 ?  101 HIS C N     1 
ATOM   11794 C  CA    . HIS C 2 122 ? 116.227 101.331 125.058 1.00 23.81 ?  101 HIS C CA    1 
ATOM   11795 C  C     . HIS C 2 122 ? 115.122 101.654 126.041 1.00 24.33 ?  101 HIS C C     1 
ATOM   11796 O  O     . HIS C 2 122 ? 114.284 102.516 125.758 1.00 24.80 ?  101 HIS C O     1 
ATOM   11797 C  CB    . HIS C 2 122 ? 116.000 99.928  124.504 1.00 23.30 ?  101 HIS C CB    1 
ATOM   11798 C  CG    . HIS C 2 122 ? 116.910 99.563  123.375 1.00 22.96 ?  101 HIS C CG    1 
ATOM   11799 N  ND1   . HIS C 2 122 ? 116.944 98.297  122.830 1.00 22.78 ?  101 HIS C ND1   1 
ATOM   11800 C  CD2   . HIS C 2 122 ? 117.843 100.287 122.713 1.00 23.25 ?  101 HIS C CD2   1 
ATOM   11801 C  CE1   . HIS C 2 122 ? 117.849 98.263  121.869 1.00 22.57 ?  101 HIS C CE1   1 
ATOM   11802 N  NE2   . HIS C 2 122 ? 118.408 99.456  121.777 1.00 21.75 ?  101 HIS C NE2   1 
ATOM   11803 N  N     . ALA C 2 123 ? 115.097 100.943 127.172 1.00 24.40 ?  102 ALA C N     1 
ATOM   11804 C  CA    . ALA C 2 123 ? 114.043 101.143 128.169 1.00 24.00 ?  102 ALA C CA    1 
ATOM   11805 C  C     . ALA C 2 123 ? 114.011 102.601 128.631 1.00 24.05 ?  102 ALA C C     1 
ATOM   11806 O  O     . ALA C 2 123 ? 112.936 103.171 128.802 1.00 23.89 ?  102 ALA C O     1 
ATOM   11807 C  CB    . ALA C 2 123 ? 114.219 100.192 129.352 1.00 23.73 ?  102 ALA C CB    1 
ATOM   11808 N  N     . LYS C 2 124 ? 115.187 103.201 128.807 1.00 24.36 ?  103 LYS C N     1 
ATOM   11809 C  CA    . LYS C 2 124 ? 115.292 104.598 129.245 1.00 24.31 ?  103 LYS C CA    1 
ATOM   11810 C  C     . LYS C 2 124 ? 114.789 105.618 128.216 1.00 23.84 ?  103 LYS C C     1 
ATOM   11811 O  O     . LYS C 2 124 ? 114.151 106.610 128.590 1.00 24.21 ?  103 LYS C O     1 
ATOM   11812 C  CB    . LYS C 2 124 ? 116.709 104.943 129.711 1.00 24.93 ?  103 LYS C CB    1 
ATOM   11813 C  CG    . LYS C 2 124 ? 116.802 106.321 130.382 1.00 26.37 ?  103 LYS C CG    1 
ATOM   11814 C  CD    . LYS C 2 124 ? 118.169 106.570 130.999 1.00 29.42 ?  103 LYS C CD    1 
ATOM   11815 C  CE    . LYS C 2 124 ? 118.282 108.012 131.503 1.00 31.51 ?  103 LYS C CE    1 
ATOM   11816 N  NZ    . LYS C 2 124 ? 118.220 109.007 130.392 1.00 32.37 1  103 LYS C NZ    1 
ATOM   11817 N  N     . SER C 2 125 ? 115.061 105.370 126.932 1.00 23.52 ?  104 SER C N     1 
ATOM   11818 C  CA    . SER C 2 125 ? 114.597 106.240 125.846 0.50 23.23 ?  104 SER C CA    1 
ATOM   11819 C  C     . SER C 2 125 ? 113.085 106.462 125.890 1.00 22.91 ?  104 SER C C     1 
ATOM   11820 O  O     . SER C 2 125 ? 112.600 107.540 125.570 1.00 22.33 ?  104 SER C O     1 
ATOM   11821 C  CB    . SER C 2 125 ? 114.981 105.659 124.480 0.50 23.25 ?  104 SER C CB    1 
ATOM   11822 O  OG    . SER C 2 125 ? 116.383 105.516 124.352 0.50 24.57 ?  104 SER C OG    1 
ATOM   11823 N  N     . TYR C 2 126 ? 112.334 105.431 126.272 1.00 22.72 ?  105 TYR C N     1 
ATOM   11824 C  CA    . TYR C 2 126 ? 110.879 105.573 126.340 1.00 23.34 ?  105 TYR C CA    1 
ATOM   11825 C  C     . TYR C 2 126 ? 110.469 106.586 127.383 1.00 23.32 ?  105 TYR C C     1 
ATOM   11826 O  O     . TYR C 2 126 ? 109.504 107.307 127.173 1.00 23.17 ?  105 TYR C O     1 
ATOM   11827 C  CB    . TYR C 2 126 ? 110.164 104.246 126.603 1.00 23.45 ?  105 TYR C CB    1 
ATOM   11828 C  CG    . TYR C 2 126 ? 110.472 103.167 125.592 1.00 25.16 ?  105 TYR C CG    1 
ATOM   11829 C  CD1   . TYR C 2 126 ? 110.155 103.326 124.246 1.00 26.75 ?  105 TYR C CD1   1 
ATOM   11830 C  CD2   . TYR C 2 126 ? 111.085 101.980 125.993 1.00 26.36 ?  105 TYR C CD2   1 
ATOM   11831 C  CE1   . TYR C 2 126 ? 110.457 102.325 123.315 1.00 28.22 ?  105 TYR C CE1   1 
ATOM   11832 C  CE2   . TYR C 2 126 ? 111.391 100.984 125.078 1.00 27.17 ?  105 TYR C CE2   1 
ATOM   11833 C  CZ    . TYR C 2 126 ? 111.063 101.155 123.746 1.00 29.26 ?  105 TYR C CZ    1 
ATOM   11834 O  OH    . TYR C 2 126 ? 111.355 100.155 122.840 1.00 30.76 ?  105 TYR C OH    1 
ATOM   11835 N  N     . SER C 2 127 ? 111.203 106.632 128.498 1.00 23.61 ?  106 SER C N     1 
ATOM   11836 C  CA    . SER C 2 127 ? 110.959 107.628 129.533 1.00 24.40 ?  106 SER C CA    1 
ATOM   11837 C  C     . SER C 2 127 ? 111.292 109.031 129.043 1.00 24.55 ?  106 SER C C     1 
ATOM   11838 O  O     . SER C 2 127 ? 110.637 109.981 129.444 1.00 24.74 ?  106 SER C O     1 
ATOM   11839 C  CB    . SER C 2 127 ? 111.723 107.317 130.819 1.00 24.54 ?  106 SER C CB    1 
ATOM   11840 O  OG    . SER C 2 127 ? 111.083 106.278 131.551 1.00 24.69 ?  106 SER C OG    1 
ATOM   11841 N  N     . ASN C 2 128 ? 112.308 109.156 128.190 1.00 25.28 ?  107 ASN C N     1 
ATOM   11842 C  CA    . ASN C 2 128 ? 112.632 110.449 127.577 1.00 25.88 ?  107 ASN C CA    1 
ATOM   11843 C  C     . ASN C 2 128 ? 111.460 110.922 126.726 1.00 25.48 ?  107 ASN C C     1 
ATOM   11844 O  O     . ASN C 2 128 ? 111.065 112.084 126.787 1.00 25.23 ?  107 ASN C O     1 
ATOM   11845 C  CB    . ASN C 2 128 ? 113.904 110.373 126.724 1.00 26.40 ?  107 ASN C CB    1 
ATOM   11846 C  CG    . ASN C 2 128 ? 115.181 110.363 127.555 1.00 27.90 ?  107 ASN C CG    1 
ATOM   11847 O  OD1   . ASN C 2 128 ? 115.209 109.860 128.679 1.00 30.62 ?  107 ASN C OD1   1 
ATOM   11848 N  ND2   . ASN C 2 128 ? 116.252 110.909 126.988 1.00 27.91 ?  107 ASN C ND2   1 
ATOM   11849 N  N     . ILE C 2 129 ? 110.902 110.005 125.942 1.00 25.44 ?  108 ILE C N     1 
ATOM   11850 C  CA    . ILE C 2 129 ? 109.722 110.322 125.138 1.00 25.48 ?  108 ILE C CA    1 
ATOM   11851 C  C     . ILE C 2 129 ? 108.538 110.701 126.043 1.00 25.93 ?  108 ILE C C     1 
ATOM   11852 O  O     . ILE C 2 129 ? 107.935 111.762 125.848 1.00 25.54 ?  108 ILE C O     1 
ATOM   11853 C  CB    . ILE C 2 129 ? 109.373 109.198 124.128 1.00 25.21 ?  108 ILE C CB    1 
ATOM   11854 C  CG1   . ILE C 2 129 ? 110.535 109.010 123.138 1.00 25.96 ?  108 ILE C CG1   1 
ATOM   11855 C  CG2   . ILE C 2 129 ? 108.057 109.519 123.387 1.00 24.43 ?  108 ILE C CG2   1 
ATOM   11856 C  CD1   . ILE C 2 129 ? 110.453 107.758 122.264 1.00 26.11 ?  108 ILE C CD1   1 
ATOM   11857 N  N     . PHE C 2 130 ? 108.225 109.859 127.032 1.00 26.04 ?  109 PHE C N     1 
ATOM   11858 C  CA    . PHE C 2 130 ? 107.123 110.139 127.972 1.00 26.66 ?  109 PHE C CA    1 
ATOM   11859 C  C     . PHE C 2 130 ? 107.273 111.496 128.664 1.00 27.38 ?  109 PHE C C     1 
ATOM   11860 O  O     . PHE C 2 130 ? 106.302 112.263 128.770 1.00 27.22 ?  109 PHE C O     1 
ATOM   11861 C  CB    . PHE C 2 130 ? 107.015 109.048 129.060 1.00 26.98 ?  109 PHE C CB    1 
ATOM   11862 C  CG    . PHE C 2 130 ? 106.507 107.714 128.570 1.00 27.46 ?  109 PHE C CG    1 
ATOM   11863 C  CD1   . PHE C 2 130 ? 105.644 107.622 127.483 1.00 28.57 ?  109 PHE C CD1   1 
ATOM   11864 C  CD2   . PHE C 2 130 ? 106.886 106.540 129.222 1.00 28.51 ?  109 PHE C CD2   1 
ATOM   11865 C  CE1   . PHE C 2 130 ? 105.181 106.383 127.042 1.00 29.17 ?  109 PHE C CE1   1 
ATOM   11866 C  CE2   . PHE C 2 130 ? 106.421 105.290 128.792 1.00 29.27 ?  109 PHE C CE2   1 
ATOM   11867 C  CZ    . PHE C 2 130 ? 105.565 105.209 127.704 1.00 28.83 ?  109 PHE C CZ    1 
ATOM   11868 N  N     . MET C 2 131 ? 108.484 111.796 129.134 1.00 27.52 ?  110 MET C N     1 
ATOM   11869 C  CA    . MET C 2 131 ? 108.721 113.022 129.905 1.00 29.07 ?  110 MET C CA    1 
ATOM   11870 C  C     . MET C 2 131 ? 108.581 114.288 129.077 1.00 29.58 ?  110 MET C C     1 
ATOM   11871 O  O     . MET C 2 131 ? 108.265 115.350 129.613 1.00 30.07 ?  110 MET C O     1 
ATOM   11872 C  CB    . MET C 2 131 ? 110.081 112.996 130.599 1.00 28.96 ?  110 MET C CB    1 
ATOM   11873 C  CG    . MET C 2 131 ? 110.081 112.181 131.875 1.00 31.09 ?  110 MET C CG    1 
ATOM   11874 S  SD    . MET C 2 131 ? 111.694 112.094 132.688 1.00 35.43 ?  110 MET C SD    1 
ATOM   11875 C  CE    . MET C 2 131 ? 112.665 111.161 131.507 1.00 33.13 ?  110 MET C CE    1 
ATOM   11876 N  N     . THR C 2 132 ? 108.811 114.161 127.776 1.00 30.25 ?  111 THR C N     1 
ATOM   11877 C  CA    . THR C 2 132 ? 108.628 115.262 126.834 1.00 30.97 ?  111 THR C CA    1 
ATOM   11878 C  C     . THR C 2 132 ? 107.146 115.504 126.529 1.00 31.36 ?  111 THR C C     1 
ATOM   11879 O  O     . THR C 2 132 ? 106.648 116.631 126.654 1.00 31.60 ?  111 THR C O     1 
ATOM   11880 C  CB    . THR C 2 132 ? 109.416 114.985 125.522 1.00 30.88 ?  111 THR C CB    1 
ATOM   11881 O  OG1   . THR C 2 132 ? 110.813 114.904 125.823 1.00 29.86 ?  111 THR C OG1   1 
ATOM   11882 C  CG2   . THR C 2 132 ? 109.195 116.091 124.478 1.00 31.44 ?  111 THR C CG2   1 
ATOM   11883 N  N     . LEU C 2 133 ? 106.448 114.441 126.143 1.00 31.34 ?  112 LEU C N     1 
ATOM   11884 C  CA    . LEU C 2 133 ? 105.086 114.556 125.617 1.00 31.68 ?  112 LEU C CA    1 
ATOM   11885 C  C     . LEU C 2 133 ? 103.960 114.597 126.654 1.00 31.96 ?  112 LEU C C     1 
ATOM   11886 O  O     . LEU C 2 133 ? 102.928 115.225 126.424 1.00 31.69 ?  112 LEU C O     1 
ATOM   11887 C  CB    . LEU C 2 133 ? 104.815 113.426 124.627 1.00 31.35 ?  112 LEU C CB    1 
ATOM   11888 C  CG    . LEU C 2 133 ? 105.816 113.238 123.482 1.00 32.14 ?  112 LEU C CG    1 
ATOM   11889 C  CD1   . LEU C 2 133 ? 105.412 112.034 122.663 1.00 32.15 ?  112 LEU C CD1   1 
ATOM   11890 C  CD2   . LEU C 2 133 ? 105.908 114.490 122.612 1.00 32.39 ?  112 LEU C CD2   1 
ATOM   11891 N  N     . ALA C 2 134 ? 104.157 113.930 127.786 1.00 32.12 ?  113 ALA C N     1 
ATOM   11892 C  CA    . ALA C 2 134 ? 103.062 113.688 128.716 1.00 32.53 ?  113 ALA C CA    1 
ATOM   11893 C  C     . ALA C 2 134 ? 103.289 114.289 130.097 1.00 33.15 ?  113 ALA C C     1 
ATOM   11894 O  O     . ALA C 2 134 ? 104.423 114.352 130.566 1.00 32.47 ?  113 ALA C O     1 
ATOM   11895 C  CB    . ALA C 2 134 ? 102.787 112.183 128.827 1.00 32.20 ?  113 ALA C CB    1 
ATOM   11896 N  N     . PRO C 2 135 ? 102.196 114.716 130.760 1.00 34.27 ?  114 PRO C N     1 
ATOM   11897 C  CA    . PRO C 2 135 ? 102.287 115.155 132.147 1.00 35.35 ?  114 PRO C CA    1 
ATOM   11898 C  C     . PRO C 2 135 ? 102.485 113.960 133.073 1.00 36.17 ?  114 PRO C C     1 
ATOM   11899 O  O     . PRO C 2 135 ? 102.119 112.836 132.721 1.00 35.92 ?  114 PRO C O     1 
ATOM   11900 C  CB    . PRO C 2 135 ? 100.937 115.838 132.399 1.00 35.48 ?  114 PRO C CB    1 
ATOM   11901 C  CG    . PRO C 2 135 ? 100.006 115.256 131.407 1.00 34.94 ?  114 PRO C CG    1 
ATOM   11902 C  CD    . PRO C 2 135 ? 100.819 114.794 130.234 1.00 34.50 ?  114 PRO C CD    1 
ATOM   11903 N  N     . THR C 2 136 ? 103.073 114.210 134.239 1.00 37.30 ?  115 THR C N     1 
ATOM   11904 C  CA    . THR C 2 136 ? 103.436 113.158 135.195 1.00 38.49 ?  115 THR C CA    1 
ATOM   11905 C  C     . THR C 2 136 ? 102.311 112.167 135.528 1.00 38.48 ?  115 THR C C     1 
ATOM   11906 O  O     . THR C 2 136 ? 102.571 110.968 135.673 1.00 38.74 ?  115 THR C O     1 
ATOM   11907 C  CB    . THR C 2 136 ? 103.987 113.772 136.498 1.00 38.95 ?  115 THR C CB    1 
ATOM   11908 O  OG1   . THR C 2 136 ? 105.031 114.693 136.171 1.00 40.08 ?  115 THR C OG1   1 
ATOM   11909 C  CG2   . THR C 2 136 ? 104.542 112.696 137.432 1.00 39.82 ?  115 THR C CG2   1 
ATOM   11910 N  N     . GLU C 2 137 ? 101.079 112.667 135.643 1.00 38.89 ?  116 GLU C N     1 
ATOM   11911 C  CA    . GLU C 2 137 ? 99.929  111.833 136.019 1.00 38.65 ?  116 GLU C CA    1 
ATOM   11912 C  C     . GLU C 2 137 ? 99.598  110.802 134.945 1.00 37.38 ?  116 GLU C C     1 
ATOM   11913 O  O     . GLU C 2 137 ? 99.243  109.667 135.256 1.00 37.22 ?  116 GLU C O     1 
ATOM   11914 C  CB    . GLU C 2 137 ? 98.685  112.675 136.378 1.00 39.52 ?  116 GLU C CB    1 
ATOM   11915 C  CG    . GLU C 2 137 ? 97.988  113.408 135.207 1.00 41.90 ?  116 GLU C CG    1 
ATOM   11916 C  CD    . GLU C 2 137 ? 97.943  114.937 135.363 1.00 46.43 ?  116 GLU C CD    1 
ATOM   11917 O  OE1   . GLU C 2 137 ? 98.635  115.491 136.250 1.00 47.84 ?  116 GLU C OE1   1 
ATOM   11918 O  OE2   . GLU C 2 137 ? 97.203  115.590 134.586 1.00 47.52 -1 116 GLU C OE2   1 
ATOM   11919 N  N     . THR C 2 138 ? 99.730  111.209 133.686 1.00 36.05 ?  117 THR C N     1 
ATOM   11920 C  CA    . THR C 2 138 ? 99.506  110.321 132.556 1.00 34.88 ?  117 THR C CA    1 
ATOM   11921 C  C     . THR C 2 138 ? 100.616 109.277 132.492 1.00 33.58 ?  117 THR C C     1 
ATOM   11922 O  O     . THR C 2 138 ? 100.356 108.113 132.174 1.00 33.61 ?  117 THR C O     1 
ATOM   11923 C  CB    . THR C 2 138 ? 99.426  111.104 131.239 1.00 34.85 ?  117 THR C CB    1 
ATOM   11924 O  OG1   . THR C 2 138 ? 98.472  112.163 131.383 1.00 35.98 ?  117 THR C OG1   1 
ATOM   11925 C  CG2   . THR C 2 138 ? 98.998  110.199 130.092 1.00 34.92 ?  117 THR C CG2   1 
ATOM   11926 N  N     . ILE C 2 139 ? 101.842 109.698 132.798 1.00 32.29 ?  118 ILE C N     1 
ATOM   11927 C  CA    . ILE C 2 139 ? 102.976 108.778 132.884 1.00 31.19 ?  118 ILE C CA    1 
ATOM   11928 C  C     . ILE C 2 139 ? 102.758 107.753 134.012 1.00 30.85 ?  118 ILE C C     1 
ATOM   11929 O  O     . ILE C 2 139 ? 102.900 106.551 133.789 1.00 29.77 ?  118 ILE C O     1 
ATOM   11930 C  CB    . ILE C 2 139 ? 104.339 109.516 133.043 1.00 31.25 ?  118 ILE C CB    1 
ATOM   11931 C  CG1   . ILE C 2 139 ? 104.590 110.481 131.871 1.00 30.12 ?  118 ILE C CG1   1 
ATOM   11932 C  CG2   . ILE C 2 139 ? 105.498 108.512 133.155 1.00 30.21 ?  118 ILE C CG2   1 
ATOM   11933 C  CD1   . ILE C 2 139 ? 105.849 111.352 132.039 1.00 29.41 ?  118 ILE C CD1   1 
ATOM   11934 N  N     . ASN C 2 140 ? 102.397 108.233 135.207 1.00 31.17 ?  119 ASN C N     1 
ATOM   11935 C  CA    . ASN C 2 140 ? 102.097 107.352 136.348 1.00 31.76 ?  119 ASN C CA    1 
ATOM   11936 C  C     . ASN C 2 140 ? 101.001 106.333 136.018 1.00 31.25 ?  119 ASN C C     1 
ATOM   11937 O  O     . ASN C 2 140 ? 101.142 105.147 136.316 1.00 31.47 ?  119 ASN C O     1 
ATOM   11938 C  CB    . ASN C 2 140 ? 101.680 108.152 137.592 1.00 32.65 ?  119 ASN C CB    1 
ATOM   11939 C  CG    . ASN C 2 140 ? 102.834 108.914 138.235 1.00 35.14 ?  119 ASN C CG    1 
ATOM   11940 O  OD1   . ASN C 2 140 ? 104.004 108.535 138.126 1.00 36.75 ?  119 ASN C OD1   1 
ATOM   11941 N  ND2   . ASN C 2 140 ? 102.492 109.995 138.942 1.00 38.05 ?  119 ASN C ND2   1 
ATOM   11942 N  N     . GLU C 2 141 ? 99.926  106.812 135.393 1.00 30.96 ?  120 GLU C N     1 
ATOM   11943 C  CA    . GLU C 2 141 ? 98.791  105.977 135.001 1.00 30.36 ?  120 GLU C CA    1 
ATOM   11944 C  C     . GLU C 2 141 ? 99.181  104.879 134.009 1.00 28.60 ?  120 GLU C C     1 
ATOM   11945 O  O     . GLU C 2 141 ? 98.737  103.742 134.146 1.00 27.94 ?  120 GLU C O     1 
ATOM   11946 C  CB    . GLU C 2 141 ? 97.667  106.833 134.410 1.00 30.86 ?  120 GLU C CB    1 
ATOM   11947 C  CG    . GLU C 2 141 ? 96.840  107.596 135.439 1.00 34.89 ?  120 GLU C CG    1 
ATOM   11948 C  CD    . GLU C 2 141 ? 95.872  108.580 134.797 1.00 39.82 ?  120 GLU C CD    1 
ATOM   11949 O  OE1   . GLU C 2 141 ? 95.636  108.489 133.566 1.00 41.95 ?  120 GLU C OE1   1 
ATOM   11950 O  OE2   . GLU C 2 141 ? 95.339  109.445 135.522 1.00 41.94 -1 120 GLU C OE2   1 
ATOM   11951 N  N     . VAL C 2 142 ? 100.002 105.208 133.015 1.00 27.29 ?  121 VAL C N     1 
ATOM   11952 C  CA    . VAL C 2 142 ? 100.383 104.182 132.020 1.00 25.89 ?  121 VAL C CA    1 
ATOM   11953 C  C     . VAL C 2 142 ? 101.278 103.089 132.615 1.00 25.11 ?  121 VAL C C     1 
ATOM   11954 O  O     . VAL C 2 142 ? 101.183 101.925 132.228 1.00 24.23 ?  121 VAL C O     1 
ATOM   11955 C  CB    . VAL C 2 142 ? 100.954 104.779 130.687 1.00 25.99 ?  121 VAL C CB    1 
ATOM   11956 C  CG1   . VAL C 2 142 ? 102.456 105.064 130.767 1.00 25.21 ?  121 VAL C CG1   1 
ATOM   11957 C  CG2   . VAL C 2 142 ? 100.673 103.838 129.526 1.00 25.78 ?  121 VAL C CG2   1 
ATOM   11958 N  N     . PHE C 2 143 ? 102.135 103.448 133.567 1.00 24.69 ?  122 PHE C N     1 
ATOM   11959 C  CA    . PHE C 2 143 ? 102.952 102.430 134.244 1.00 24.77 ?  122 PHE C CA    1 
ATOM   11960 C  C     . PHE C 2 143 ? 102.105 101.556 135.186 1.00 24.99 ?  122 PHE C C     1 
ATOM   11961 O  O     . PHE C 2 143 ? 102.361 100.361 135.338 1.00 24.73 ?  122 PHE C O     1 
ATOM   11962 C  CB    . PHE C 2 143 ? 104.170 103.051 134.940 1.00 24.83 ?  122 PHE C CB    1 
ATOM   11963 C  CG    . PHE C 2 143 ? 105.294 103.386 133.984 1.00 25.12 ?  122 PHE C CG    1 
ATOM   11964 C  CD1   . PHE C 2 143 ? 106.075 102.377 133.425 1.00 26.58 ?  122 PHE C CD1   1 
ATOM   11965 C  CD2   . PHE C 2 143 ? 105.555 104.700 133.628 1.00 24.49 ?  122 PHE C CD2   1 
ATOM   11966 C  CE1   . PHE C 2 143 ? 107.106 102.682 132.526 1.00 26.96 ?  122 PHE C CE1   1 
ATOM   11967 C  CE2   . PHE C 2 143 ? 106.576 105.015 132.742 1.00 25.79 ?  122 PHE C CE2   1 
ATOM   11968 C  CZ    . PHE C 2 143 ? 107.355 104.005 132.184 1.00 26.45 ?  122 PHE C CZ    1 
ATOM   11969 N  N     . GLU C 2 144 ? 101.082 102.152 135.795 1.00 25.22 ?  123 GLU C N     1 
ATOM   11970 C  CA    . GLU C 2 144 ? 100.096 101.371 136.549 1.00 25.72 ?  123 GLU C CA    1 
ATOM   11971 C  C     . GLU C 2 144 ? 99.324  100.435 135.621 1.00 25.08 ?  123 GLU C C     1 
ATOM   11972 O  O     . GLU C 2 144 ? 99.063  99.282  135.967 1.00 24.67 ?  123 GLU C O     1 
ATOM   11973 C  CB    . GLU C 2 144 ? 99.150  102.284 137.325 1.00 26.23 ?  123 GLU C CB    1 
ATOM   11974 C  CG    . GLU C 2 144 ? 99.825  102.953 138.511 1.00 29.96 ?  123 GLU C CG    1 
ATOM   11975 C  CD    . GLU C 2 144 ? 100.503 101.948 139.427 1.00 33.82 ?  123 GLU C CD    1 
ATOM   11976 O  OE1   . GLU C 2 144 ? 99.785  101.131 140.042 1.00 36.54 ?  123 GLU C OE1   1 
ATOM   11977 O  OE2   . GLU C 2 144 ? 101.749 101.961 139.519 1.00 35.84 -1 123 GLU C OE2   1 
ATOM   11978 N  N     . TRP C 2 145 ? 98.991  100.932 134.432 1.00 24.21 ?  124 TRP C N     1 
ATOM   11979 C  CA    . TRP C 2 145 ? 98.301  100.137 133.418 1.00 23.99 ?  124 TRP C CA    1 
ATOM   11980 C  C     . TRP C 2 145 ? 99.099  98.912  132.951 1.00 23.95 ?  124 TRP C C     1 
ATOM   11981 O  O     . TRP C 2 145 ? 98.506  97.840  132.722 1.00 23.31 ?  124 TRP C O     1 
ATOM   11982 C  CB    . TRP C 2 145 ? 97.897  101.013 132.221 1.00 24.13 ?  124 TRP C CB    1 
ATOM   11983 C  CG    . TRP C 2 145 ? 97.449  100.218 131.016 1.00 24.37 ?  124 TRP C CG    1 
ATOM   11984 C  CD1   . TRP C 2 145 ? 96.176  99.786  130.732 1.00 24.76 ?  124 TRP C CD1   1 
ATOM   11985 C  CD2   . TRP C 2 145 ? 98.277  99.770  129.935 1.00 23.31 ?  124 TRP C CD2   1 
ATOM   11986 N  NE1   . TRP C 2 145 ? 96.172  99.087  129.539 1.00 24.97 ?  124 TRP C NE1   1 
ATOM   11987 C  CE2   . TRP C 2 145 ? 97.444  99.066  129.030 1.00 24.20 ?  124 TRP C CE2   1 
ATOM   11988 C  CE3   . TRP C 2 145 ? 99.644  99.885  129.647 1.00 23.76 ?  124 TRP C CE3   1 
ATOM   11989 C  CZ2   . TRP C 2 145 ? 97.938  98.484  127.854 1.00 23.41 ?  124 TRP C CZ2   1 
ATOM   11990 C  CZ3   . TRP C 2 145 ? 100.136 99.303  128.480 1.00 23.29 ?  124 TRP C CZ3   1 
ATOM   11991 C  CH2   . TRP C 2 145 ? 99.278  98.616  127.595 1.00 22.93 ?  124 TRP C CH2   1 
ATOM   11992 N  N     . VAL C 2 146 ? 100.421 99.038  132.794 1.00 23.35 ?  125 VAL C N     1 
ATOM   11993 C  CA    . VAL C 2 146 ? 101.205 97.827  132.438 1.00 23.53 ?  125 VAL C CA    1 
ATOM   11994 C  C     . VAL C 2 146 ? 101.102 96.731  133.506 1.00 23.73 ?  125 VAL C C     1 
ATOM   11995 O  O     . VAL C 2 146 ? 100.957 95.566  133.165 1.00 23.03 ?  125 VAL C O     1 
ATOM   11996 C  CB    . VAL C 2 146 ? 102.691 98.068  131.893 1.00 23.63 ?  125 VAL C CB    1 
ATOM   11997 C  CG1   . VAL C 2 146 ? 103.047 99.519  131.710 1.00 24.40 ?  125 VAL C CG1   1 
ATOM   11998 C  CG2   . VAL C 2 146 ? 103.774 97.287  132.661 1.00 22.97 ?  125 VAL C CG2   1 
ATOM   11999 N  N     . LYS C 2 147 ? 101.118 97.120  134.784 1.00 24.06 ?  126 LYS C N     1 
ATOM   12000 C  CA    . LYS C 2 147 ? 101.055 96.150  135.891 1.00 25.41 ?  126 LYS C CA    1 
ATOM   12001 C  C     . LYS C 2 147 ? 99.771  95.318  135.901 1.00 25.82 ?  126 LYS C C     1 
ATOM   12002 O  O     . LYS C 2 147 ? 99.793  94.154  136.309 1.00 26.08 ?  126 LYS C O     1 
ATOM   12003 C  CB    . LYS C 2 147 ? 101.197 96.853  137.243 1.00 25.49 ?  126 LYS C CB    1 
ATOM   12004 C  CG    . LYS C 2 147 ? 102.559 97.454  137.519 1.00 27.52 ?  126 LYS C CG    1 
ATOM   12005 C  CD    . LYS C 2 147 ? 102.521 98.190  138.853 1.00 30.43 ?  126 LYS C CD    1 
ATOM   12006 C  CE    . LYS C 2 147 ? 103.722 99.096  139.029 1.00 33.10 ?  126 LYS C CE    1 
ATOM   12007 N  NZ    . LYS C 2 147 ? 103.589 99.885  140.284 1.00 34.86 1  126 LYS C NZ    1 
ATOM   12008 N  N     . GLN C 2 148 ? 98.665  95.914  135.456 1.00 26.45 ?  127 GLN C N     1 
ATOM   12009 C  CA    . GLN C 2 148 ? 97.350  95.270  135.534 1.00 26.85 ?  127 GLN C CA    1 
ATOM   12010 C  C     . GLN C 2 148 ? 96.829  94.724  134.203 1.00 26.01 ?  127 GLN C C     1 
ATOM   12011 O  O     . GLN C 2 148 ? 95.785  94.069  134.177 1.00 26.12 ?  127 GLN C O     1 
ATOM   12012 C  CB    . GLN C 2 148 ? 96.311  96.210  136.175 1.00 28.08 ?  127 GLN C CB    1 
ATOM   12013 C  CG    . GLN C 2 148 ? 96.029  97.502  135.401 1.00 30.69 ?  127 GLN C CG    1 
ATOM   12014 C  CD    . GLN C 2 148 ? 95.165  97.287  134.161 1.00 34.64 ?  127 GLN C CD    1 
ATOM   12015 O  OE1   . GLN C 2 148 ? 95.621  97.488  133.022 1.00 33.80 ?  127 GLN C OE1   1 
ATOM   12016 N  NE2   . GLN C 2 148 ? 93.911  96.865  134.373 1.00 36.24 ?  127 GLN C NE2   1 
ATOM   12017 N  N     . ASN C 2 149 ? 97.541  94.997  133.107 1.00 24.97 ?  128 ASN C N     1 
ATOM   12018 C  CA    . ASN C 2 149 ? 97.131  94.515  131.791 1.00 24.03 ?  128 ASN C CA    1 
ATOM   12019 C  C     . ASN C 2 149 ? 97.431  93.032  131.644 1.00 24.13 ?  128 ASN C C     1 
ATOM   12020 O  O     . ASN C 2 149 ? 98.597  92.636  131.732 1.00 22.93 ?  128 ASN C O     1 
ATOM   12021 C  CB    . ASN C 2 149 ? 97.859  95.276  130.694 1.00 23.97 ?  128 ASN C CB    1 
ATOM   12022 C  CG    . ASN C 2 149 ? 97.365  94.907  129.316 1.00 23.94 ?  128 ASN C CG    1 
ATOM   12023 O  OD1   . ASN C 2 149 ? 97.870  93.975  128.692 1.00 24.85 ?  128 ASN C OD1   1 
ATOM   12024 N  ND2   . ASN C 2 149 ? 96.337  95.604  128.851 1.00 24.76 ?  128 ASN C ND2   1 
ATOM   12025 N  N     . LYS C 2 150 ? 96.398  92.224  131.392 1.00 24.32 ?  129 LYS C N     1 
ATOM   12026 C  CA    . LYS C 2 150 ? 96.547  90.756  131.433 1.00 24.77 ?  129 LYS C CA    1 
ATOM   12027 C  C     . LYS C 2 150 ? 97.393  90.149  130.311 1.00 24.54 ?  129 LYS C C     1 
ATOM   12028 O  O     . LYS C 2 150 ? 98.064  89.138  130.523 1.00 24.17 ?  129 LYS C O     1 
ATOM   12029 C  CB    . LYS C 2 150 ? 95.190  90.050  131.551 1.00 25.27 ?  129 LYS C CB    1 
ATOM   12030 C  CG    . LYS C 2 150 ? 94.234  90.263  130.395 1.00 28.72 ?  129 LYS C CG    1 
ATOM   12031 C  CD    . LYS C 2 150 ? 93.094  89.246  130.474 1.00 33.40 ?  129 LYS C CD    1 
ATOM   12032 C  CE    . LYS C 2 150 ? 91.877  89.720  129.702 1.00 36.77 ?  129 LYS C CE    1 
ATOM   12033 N  NZ    . LYS C 2 150 ? 90.712  88.822  129.971 1.00 39.66 1  129 LYS C NZ    1 
ATOM   12034 N  N     . TYR C 2 151 ? 97.354  90.762  129.123 1.00 23.92 ?  130 TYR C N     1 
ATOM   12035 C  CA    . TYR C 2 151 ? 98.142  90.281  127.980 1.00 24.12 ?  130 TYR C CA    1 
ATOM   12036 C  C     . TYR C 2 151 ? 99.626  90.570  128.140 1.00 23.54 ?  130 TYR C C     1 
ATOM   12037 O  O     . TYR C 2 151 ? 100.477 89.740  127.787 1.00 23.32 ?  130 TYR C O     1 
ATOM   12038 C  CB    . TYR C 2 151 ? 97.600  90.874  126.666 1.00 24.53 ?  130 TYR C CB    1 
ATOM   12039 C  CG    . TYR C 2 151 ? 96.089  90.826  126.596 1.00 25.83 ?  130 TYR C CG    1 
ATOM   12040 C  CD1   . TYR C 2 151 ? 95.415  89.604  126.571 1.00 26.57 ?  130 TYR C CD1   1 
ATOM   12041 C  CD2   . TYR C 2 151 ? 95.331  92.003  126.600 1.00 27.87 ?  130 TYR C CD2   1 
ATOM   12042 C  CE1   . TYR C 2 151 ? 94.026  89.546  126.529 1.00 29.65 ?  130 TYR C CE1   1 
ATOM   12043 C  CE2   . TYR C 2 151 ? 93.932  91.956  126.561 1.00 29.91 ?  130 TYR C CE2   1 
ATOM   12044 C  CZ    . TYR C 2 151 ? 93.292  90.725  126.528 1.00 31.19 ?  130 TYR C CZ    1 
ATOM   12045 O  OH    . TYR C 2 151 ? 91.914  90.659  126.488 1.00 34.44 ?  130 TYR C OH    1 
ATOM   12046 N  N     . LEU C 2 152 ? 99.931  91.749  128.672 1.00 23.38 ?  131 LEU C N     1 
ATOM   12047 C  CA    . LEU C 2 152 ? 101.303 92.149  128.924 1.00 23.43 ?  131 LEU C CA    1 
ATOM   12048 C  C     . LEU C 2 152 ? 101.890 91.314  130.067 1.00 23.37 ?  131 LEU C C     1 
ATOM   12049 O  O     . LEU C 2 152 ? 103.036 90.862  129.981 1.00 23.05 ?  131 LEU C O     1 
ATOM   12050 C  CB    . LEU C 2 152 ? 101.337 93.642  129.249 1.00 23.73 ?  131 LEU C CB    1 
ATOM   12051 C  CG    . LEU C 2 152 ? 102.335 94.637  128.670 1.00 24.71 ?  131 LEU C CG    1 
ATOM   12052 C  CD1   . LEU C 2 152 ? 103.049 94.183  127.385 1.00 21.63 ?  131 LEU C CD1   1 
ATOM   12053 C  CD2   . LEU C 2 152 ? 101.627 95.953  128.447 1.00 26.87 ?  131 LEU C CD2   1 
ATOM   12054 N  N     . GLN C 2 153 ? 101.113 91.104  131.134 1.00 22.80 ?  132 GLN C N     1 
ATOM   12055 C  CA    . GLN C 2 153 ? 101.552 90.191  132.201 1.00 22.70 ?  132 GLN C CA    1 
ATOM   12056 C  C     . GLN C 2 153 ? 101.749 88.751  131.721 1.00 22.54 ?  132 GLN C C     1 
ATOM   12057 O  O     . GLN C 2 153 ? 102.754 88.114  132.071 1.00 21.73 ?  132 GLN C O     1 
ATOM   12058 C  CB    . GLN C 2 153 ? 100.638 90.254  133.428 1.00 23.07 ?  132 GLN C CB    1 
ATOM   12059 C  CG    . GLN C 2 153 ? 100.655 91.622  134.110 1.00 21.83 ?  132 GLN C CG    1 
ATOM   12060 C  CD    . GLN C 2 153 ? 102.050 92.056  134.568 1.00 22.34 ?  132 GLN C CD    1 
ATOM   12061 O  OE1   . GLN C 2 153 ? 102.780 91.289  135.199 1.00 24.07 ?  132 GLN C OE1   1 
ATOM   12062 N  NE2   . GLN C 2 153 ? 102.412 93.295  134.262 1.00 22.26 ?  132 GLN C NE2   1 
ATOM   12063 N  N     . LYS C 2 154 ? 100.810 88.242  130.918 1.00 22.53 ?  133 LYS C N     1 
ATOM   12064 C  CA    . LYS C 2 154 ? 100.959 86.894  130.369 1.00 22.84 ?  133 LYS C CA    1 
ATOM   12065 C  C     . LYS C 2 154 ? 102.232 86.749  129.531 1.00 22.42 ?  133 LYS C C     1 
ATOM   12066 O  O     . LYS C 2 154 ? 102.955 85.773  129.695 1.00 21.90 ?  133 LYS C O     1 
ATOM   12067 C  CB    . LYS C 2 154 ? 99.714  86.425  129.581 1.00 22.96 ?  133 LYS C CB    1 
ATOM   12068 C  CG    . LYS C 2 154 ? 99.822  84.974  129.019 1.00 23.45 ?  133 LYS C CG    1 
ATOM   12069 C  CD    . LYS C 2 154 ? 99.906  83.893  130.119 1.00 26.74 ?  133 LYS C CD    1 
ATOM   12070 C  CE    . LYS C 2 154 ? 99.966  82.482  129.520 1.00 27.93 ?  133 LYS C CE    1 
ATOM   12071 N  NZ    . LYS C 2 154 ? 100.253 81.423  130.525 1.00 27.86 1  133 LYS C NZ    1 
ATOM   12072 N  N     . LYS C 2 155 ? 102.523 87.717  128.656 1.00 22.77 ?  134 LYS C N     1 
ATOM   12073 C  CA    . LYS C 2 155 ? 103.687 87.567  127.776 1.00 22.87 ?  134 LYS C CA    1 
ATOM   12074 C  C     . LYS C 2 155 ? 104.997 87.648  128.553 1.00 22.30 ?  134 LYS C C     1 
ATOM   12075 O  O     . LYS C 2 155 ? 105.916 86.853  128.296 1.00 21.89 ?  134 LYS C O     1 
ATOM   12076 C  CB    . LYS C 2 155 ? 103.644 88.497  126.541 1.00 23.33 ?  134 LYS C CB    1 
ATOM   12077 C  CG    . LYS C 2 155 ? 103.975 89.952  126.758 1.00 24.25 ?  134 LYS C CG    1 
ATOM   12078 C  CD    . LYS C 2 155 ? 103.905 90.740  125.439 1.00 26.87 ?  134 LYS C CD    1 
ATOM   12079 C  CE    . LYS C 2 155 ? 102.481 91.198  125.142 1.00 28.26 ?  134 LYS C CE    1 
ATOM   12080 N  NZ    . LYS C 2 155 ? 102.479 92.216  124.048 1.00 28.97 1  134 LYS C NZ    1 
ATOM   12081 N  N     . ALA C 2 156 ? 105.057 88.562  129.521 1.00 21.96 ?  135 ALA C N     1 
ATOM   12082 C  CA    . ALA C 2 156 ? 106.184 88.624  130.472 1.00 22.43 ?  135 ALA C CA    1 
ATOM   12083 C  C     . ALA C 2 156 ? 106.342 87.339  131.287 1.00 22.02 ?  135 ALA C C     1 
ATOM   12084 O  O     . ALA C 2 156 ? 107.458 86.858  131.465 1.00 22.60 ?  135 ALA C O     1 
ATOM   12085 C  CB    . ALA C 2 156 ? 106.050 89.832  131.424 1.00 22.05 ?  135 ALA C CB    1 
ATOM   12086 N  N     . GLN C 2 157 ? 105.235 86.800  131.798 1.00 21.97 ?  136 GLN C N     1 
ATOM   12087 C  CA    . GLN C 2 157 ? 105.272 85.547  132.564 1.00 22.10 ?  136 GLN C CA    1 
ATOM   12088 C  C     . GLN C 2 157 ? 105.892 84.429  131.752 1.00 21.87 ?  136 GLN C C     1 
ATOM   12089 O  O     . GLN C 2 157 ? 106.717 83.674  132.264 1.00 21.75 ?  136 GLN C O     1 
ATOM   12090 C  CB    . GLN C 2 157 ? 103.871 85.100  132.979 1.00 22.50 ?  136 GLN C CB    1 
ATOM   12091 C  CG    . GLN C 2 157 ? 103.301 85.810  134.197 1.00 23.55 ?  136 GLN C CG    1 
ATOM   12092 C  CD    . GLN C 2 157 ? 101.794 85.638  134.266 1.00 26.93 ?  136 GLN C CD    1 
ATOM   12093 O  OE1   . GLN C 2 157 ? 101.252 84.684  133.710 1.00 26.36 ?  136 GLN C OE1   1 
ATOM   12094 N  NE2   . GLN C 2 157 ? 101.110 86.570  134.920 1.00 28.09 ?  136 GLN C NE2   1 
ATOM   12095 N  N     . MET C 2 158 ? 105.470 84.324  130.493 1.00 21.38 ?  137 MET C N     1 
ATOM   12096 C  CA    . MET C 2 158 ? 105.904 83.247  129.616 1.00 22.08 ?  137 MET C CA    1 
ATOM   12097 C  C     . MET C 2 158 ? 107.372 83.374  129.226 1.00 21.70 ?  137 MET C C     1 
ATOM   12098 O  O     . MET C 2 158 ? 108.115 82.390  129.220 1.00 21.83 ?  137 MET C O     1 
ATOM   12099 C  CB    . MET C 2 158 ? 105.061 83.226  128.345 1.00 22.05 ?  137 MET C CB    1 
ATOM   12100 C  CG    . MET C 2 158 ? 103.645 82.666  128.531 1.00 23.93 ?  137 MET C CG    1 
ATOM   12101 S  SD    . MET C 2 158 ? 102.685 82.903  127.022 1.00 27.75 ?  137 MET C SD    1 
ATOM   12102 C  CE    . MET C 2 158 ? 103.526 81.734  125.942 1.00 26.00 ?  137 MET C CE    1 
ATOM   12103 N  N     . ILE C 2 159 ? 107.776 84.583  128.863 1.00 20.90 ?  138 ILE C N     1 
ATOM   12104 C  CA    . ILE C 2 159 ? 109.134 84.796  128.391 1.00 20.60 ?  138 ILE C CA    1 
ATOM   12105 C  C     . ILE C 2 159 ? 110.125 84.678  129.553 1.00 20.36 ?  138 ILE C C     1 
ATOM   12106 O  O     . ILE C 2 159 ? 111.109 83.942  129.452 1.00 19.65 ?  138 ILE C O     1 
ATOM   12107 C  CB    . ILE C 2 159 ? 109.275 86.148  127.632 1.00 20.17 ?  138 ILE C CB    1 
ATOM   12108 C  CG1   . ILE C 2 159 ? 108.463 86.125  126.323 1.00 20.66 ?  138 ILE C CG1   1 
ATOM   12109 C  CG2   . ILE C 2 159 ? 110.754 86.519  127.432 1.00 20.62 ?  138 ILE C CG2   1 
ATOM   12110 C  CD1   . ILE C 2 159 ? 108.906 85.127  125.249 1.00 22.17 ?  138 ILE C CD1   1 
ATOM   12111 N  N     . VAL C 2 160 ? 109.848 85.377  130.654 1.00 19.58 ?  139 VAL C N     1 
ATOM   12112 C  CA    . VAL C 2 160 ? 110.738 85.383  131.819 1.00 19.88 ?  139 VAL C CA    1 
ATOM   12113 C  C     . VAL C 2 160 ? 110.778 83.999  132.474 1.00 19.44 ?  139 VAL C C     1 
ATOM   12114 O  O     . VAL C 2 160 ? 111.795 83.599  133.029 1.00 19.88 ?  139 VAL C O     1 
ATOM   12115 C  CB    . VAL C 2 160 ? 110.343 86.473  132.879 1.00 19.52 ?  139 VAL C CB    1 
ATOM   12116 C  CG1   . VAL C 2 160 ? 111.243 86.385  134.124 1.00 20.75 ?  139 VAL C CG1   1 
ATOM   12117 C  CG2   . VAL C 2 160 ? 110.456 87.872  132.283 1.00 20.03 ?  139 VAL C CG2   1 
ATOM   12118 N  N     . GLY C 2 161 ? 109.670 83.268  132.402 1.00 19.13 ?  140 GLY C N     1 
ATOM   12119 C  CA    . GLY C 2 161 ? 109.633 81.925  132.959 1.00 18.05 ?  140 GLY C CA    1 
ATOM   12120 C  C     . GLY C 2 161 ? 110.651 81.044  132.280 1.00 17.86 ?  140 GLY C C     1 
ATOM   12121 O  O     . GLY C 2 161 ? 111.385 80.296  132.935 1.00 17.47 ?  140 GLY C O     1 
ATOM   12122 N  N     . LEU C 2 162 ? 110.689 81.123  130.955 1.00 17.92 ?  141 LEU C N     1 
ATOM   12123 C  CA    . LEU C 2 162 ? 111.668 80.367  130.181 1.00 18.32 ?  141 LEU C CA    1 
ATOM   12124 C  C     . LEU C 2 162 ? 113.123 80.792  130.477 1.00 18.55 ?  141 LEU C C     1 
ATOM   12125 O  O     . LEU C 2 162 ? 113.999 79.936  130.604 1.00 18.49 ?  141 LEU C O     1 
ATOM   12126 C  CB    . LEU C 2 162 ? 111.346 80.472  128.684 1.00 18.50 ?  141 LEU C CB    1 
ATOM   12127 C  CG    . LEU C 2 162 ? 110.084 79.712  128.266 1.00 19.32 ?  141 LEU C CG    1 
ATOM   12128 C  CD1   . LEU C 2 162 ? 109.617 80.169  126.889 1.00 20.38 ?  141 LEU C CD1   1 
ATOM   12129 C  CD2   . LEU C 2 162 ? 110.316 78.199  128.300 1.00 19.94 ?  141 LEU C CD2   1 
ATOM   12130 N  N     . TYR C 2 163 ? 113.375 82.090  130.620 1.00 19.16 ?  142 TYR C N     1 
ATOM   12131 C  CA    . TYR C 2 163 ? 114.709 82.568  131.036 1.00 20.16 ?  142 TYR C CA    1 
ATOM   12132 C  C     . TYR C 2 163 ? 115.139 81.976  132.366 1.00 20.78 ?  142 TYR C C     1 
ATOM   12133 O  O     . TYR C 2 163 ? 116.290 81.564  132.538 1.00 20.36 ?  142 TYR C O     1 
ATOM   12134 C  CB    . TYR C 2 163 ? 114.756 84.101  131.158 1.00 20.34 ?  142 TYR C CB    1 
ATOM   12135 C  CG    . TYR C 2 163 ? 114.563 84.861  129.854 1.00 22.46 ?  142 TYR C CG    1 
ATOM   12136 C  CD1   . TYR C 2 163 ? 114.844 84.274  128.625 1.00 23.88 ?  142 TYR C CD1   1 
ATOM   12137 C  CD2   . TYR C 2 163 ? 114.109 86.175  129.860 1.00 22.41 ?  142 TYR C CD2   1 
ATOM   12138 C  CE1   . TYR C 2 163 ? 114.661 84.983  127.424 1.00 25.93 ?  142 TYR C CE1   1 
ATOM   12139 C  CE2   . TYR C 2 163 ? 113.930 86.886  128.676 1.00 22.07 ?  142 TYR C CE2   1 
ATOM   12140 C  CZ    . TYR C 2 163 ? 114.215 86.292  127.470 1.00 25.19 ?  142 TYR C CZ    1 
ATOM   12141 O  OH    . TYR C 2 163 ? 114.026 87.019  126.312 1.00 27.43 ?  142 TYR C OH    1 
ATOM   12142 N  N     . LYS C 2 164 ? 114.209 81.933  133.312 1.00 21.39 ?  143 LYS C N     1 
ATOM   12143 C  CA    . LYS C 2 164 ? 114.555 81.492  134.653 1.00 22.49 ?  143 LYS C CA    1 
ATOM   12144 C  C     . LYS C 2 164 ? 114.580 79.972  134.786 1.00 22.49 ?  143 LYS C C     1 
ATOM   12145 O  O     . LYS C 2 164 ? 115.075 79.449  135.779 1.00 22.45 ?  143 LYS C O     1 
ATOM   12146 C  CB    . LYS C 2 164 ? 113.677 82.175  135.699 1.00 23.16 ?  143 LYS C CB    1 
ATOM   12147 C  CG    . LYS C 2 164 ? 113.975 83.670  135.786 1.00 26.08 ?  143 LYS C CG    1 
ATOM   12148 C  CD    . LYS C 2 164 ? 113.560 84.261  137.101 1.00 30.38 ?  143 LYS C CD    1 
ATOM   12149 C  CE    . LYS C 2 164 ? 114.041 85.687  137.225 1.00 32.69 ?  143 LYS C CE    1 
ATOM   12150 N  NZ    . LYS C 2 164 ? 113.581 86.277  138.512 1.00 35.60 1  143 LYS C NZ    1 
ATOM   12151 N  N     . ALA C 2 165 ? 114.118 79.272  133.749 1.00 22.02 ?  144 ALA C N     1 
ATOM   12152 C  CA    . ALA C 2 165 ? 114.175 77.823  133.733 1.00 22.69 ?  144 ALA C CA    1 
ATOM   12153 C  C     . ALA C 2 165 ? 115.510 77.276  133.199 1.00 23.20 ?  144 ALA C C     1 
ATOM   12154 O  O     . ALA C 2 165 ? 115.750 76.077  133.261 1.00 23.80 ?  144 ALA C O     1 
ATOM   12155 C  CB    . ALA C 2 165 ? 112.977 77.241  132.941 1.00 21.79 ?  144 ALA C CB    1 
ATOM   12156 N  N     . ILE C 2 166 ? 116.380 78.143  132.676 1.00 23.97 ?  145 ILE C N     1 
ATOM   12157 C  CA    . ILE C 2 166 ? 117.680 77.685  132.171 1.00 24.29 ?  145 ILE C CA    1 
ATOM   12158 C  C     . ILE C 2 166 ? 118.463 76.976  133.280 1.00 25.49 ?  145 ILE C C     1 
ATOM   12159 O  O     . ILE C 2 166 ? 118.556 77.475  134.397 1.00 25.82 ?  145 ILE C O     1 
ATOM   12160 C  CB    . ILE C 2 166 ? 118.543 78.837  131.579 1.00 24.22 ?  145 ILE C CB    1 
ATOM   12161 C  CG1   . ILE C 2 166 ? 117.834 79.508  130.407 1.00 23.45 ?  145 ILE C CG1   1 
ATOM   12162 C  CG2   . ILE C 2 166 ? 119.904 78.309  131.123 1.00 23.42 ?  145 ILE C CG2   1 
ATOM   12163 C  CD1   . ILE C 2 166 ? 118.479 80.852  129.978 1.00 21.99 ?  145 ILE C CD1   1 
ATOM   12164 N  N     . GLN C 2 167 ? 118.973 75.792  132.970 1.00 26.83 ?  146 GLN C N     1 
ATOM   12165 C  CA    . GLN C 2 167 ? 119.778 75.032  133.915 1.00 28.85 ?  146 GLN C CA    1 
ATOM   12166 C  C     . GLN C 2 167 ? 121.209 75.021  133.413 1.00 29.77 ?  146 GLN C C     1 
ATOM   12167 O  O     . GLN C 2 167 ? 121.451 74.845  132.215 1.00 29.74 ?  146 GLN C O     1 
ATOM   12168 C  CB    . GLN C 2 167 ? 119.257 73.594  134.065 1.00 28.99 ?  146 GLN C CB    1 
ATOM   12169 C  CG    . GLN C 2 167 ? 117.935 73.470  134.825 1.00 30.30 ?  146 GLN C CG    1 
ATOM   12170 C  CD    . GLN C 2 167 ? 118.074 73.763  136.313 1.00 33.32 ?  146 GLN C CD    1 
ATOM   12171 O  OE1   . GLN C 2 167 ? 119.185 73.878  136.834 1.00 34.63 ?  146 GLN C OE1   1 
ATOM   12172 N  NE2   . GLN C 2 167 ? 116.943 73.862  137.007 1.00 32.32 ?  146 GLN C NE2   1 
ATOM   12173 N  N     . LYS C 2 168 ? 122.151 75.214  134.329 1.00 31.29 ?  147 LYS C N     1 
ATOM   12174 C  CA    . LYS C 2 168 ? 123.572 75.212  133.986 1.00 33.14 ?  147 LYS C CA    1 
ATOM   12175 C  C     . LYS C 2 168 ? 123.914 73.922  133.252 1.00 33.79 ?  147 LYS C C     1 
ATOM   12176 O  O     . LYS C 2 168 ? 123.396 72.851  133.582 1.00 34.06 ?  147 LYS C O     1 
ATOM   12177 C  CB    . LYS C 2 168 ? 124.425 75.373  135.242 1.00 33.44 ?  147 LYS C CB    1 
ATOM   12178 C  CG    . LYS C 2 168 ? 125.845 75.884  135.011 1.00 35.61 ?  147 LYS C CG    1 
ATOM   12179 C  CD    . LYS C 2 168 ? 126.559 76.041  136.349 1.00 38.40 ?  147 LYS C CD    1 
ATOM   12180 C  CE    . LYS C 2 168 ? 127.866 76.807  136.231 1.00 40.48 ?  147 LYS C CE    1 
ATOM   12181 N  NZ    . LYS C 2 168 ? 129.019 75.872  136.141 1.00 41.56 1  147 LYS C NZ    1 
ATOM   12182 N  N     . ASP C 2 169 ? 124.749 74.047  132.225 1.00 35.10 ?  148 ASP C N     1 
ATOM   12183 C  CA    . ASP C 2 169 ? 125.191 72.906  131.406 1.00 36.27 ?  148 ASP C CA    1 
ATOM   12184 C  C     . ASP C 2 169 ? 124.069 72.114  130.733 1.00 36.29 ?  148 ASP C C     1 
ATOM   12185 O  O     . ASP C 2 169 ? 124.283 70.990  130.276 1.00 36.95 ?  148 ASP C O     1 
ATOM   12186 C  CB    . ASP C 2 169 ? 126.062 71.957  132.236 1.00 37.15 ?  148 ASP C CB    1 
ATOM   12187 C  CG    . ASP C 2 169 ? 127.404 72.549  132.577 1.00 38.94 ?  148 ASP C CG    1 
ATOM   12188 O  OD1   . ASP C 2 169 ? 127.850 73.482  131.869 1.00 41.71 ?  148 ASP C OD1   1 
ATOM   12189 O  OD2   . ASP C 2 169 ? 128.013 72.078  133.559 1.00 41.64 -1 148 ASP C OD2   1 
ATOM   12190 N  N     . ASP C 2 170 ? 122.873 72.689  130.675 1.00 35.87 ?  149 ASP C N     1 
ATOM   12191 C  CA    . ASP C 2 170 ? 121.757 72.030  130.010 1.00 35.24 ?  149 ASP C CA    1 
ATOM   12192 C  C     . ASP C 2 170 ? 121.384 72.866  128.792 1.00 34.12 ?  149 ASP C C     1 
ATOM   12193 O  O     . ASP C 2 170 ? 120.712 73.910  128.900 1.00 33.52 ?  149 ASP C O     1 
ATOM   12194 C  CB    . ASP C 2 170 ? 120.585 71.828  130.976 1.00 36.09 ?  149 ASP C CB    1 
ATOM   12195 C  CG    . ASP C 2 170 ? 119.319 71.317  130.288 1.00 38.39 ?  149 ASP C CG    1 
ATOM   12196 O  OD1   . ASP C 2 170 ? 119.373 70.841  129.130 1.00 42.06 ?  149 ASP C OD1   1 
ATOM   12197 O  OD2   . ASP C 2 170 ? 118.250 71.382  130.927 1.00 42.21 -1 149 ASP C OD2   1 
ATOM   12198 N  N     . GLU C 2 171 ? 121.852 72.395  127.641 1.00 32.48 ?  150 GLU C N     1 
ATOM   12199 C  CA    . GLU C 2 171 ? 121.745 73.128  126.392 1.00 30.93 ?  150 GLU C CA    1 
ATOM   12200 C  C     . GLU C 2 171 ? 120.301 73.238  125.892 1.00 29.37 ?  150 GLU C C     1 
ATOM   12201 O  O     . GLU C 2 171 ? 119.959 74.197  125.201 1.00 28.99 ?  150 GLU C O     1 
ATOM   12202 C  CB    . GLU C 2 171 ? 122.676 72.527  125.321 1.00 31.30 ?  150 GLU C CB    1 
ATOM   12203 C  CG    . GLU C 2 171 ? 122.265 71.152  124.742 1.00 33.64 ?  150 GLU C CG    1 
ATOM   12204 C  CD    . GLU C 2 171 ? 123.376 70.463  123.913 1.00 36.40 ?  150 GLU C CD    1 
ATOM   12205 O  OE1   . GLU C 2 171 ? 124.468 71.047  123.736 1.00 38.62 ?  150 GLU C OE1   1 
ATOM   12206 O  OE2   . GLU C 2 171 ? 123.156 69.327  123.434 1.00 37.42 -1 150 GLU C OE2   1 
ATOM   12207 N  N     . ILE C 2 172 ? 119.463 72.261  126.239 1.00 27.68 ?  151 ILE C N     1 
ATOM   12208 C  CA    . ILE C 2 172 ? 118.064 72.275  125.807 1.00 26.26 ?  151 ILE C CA    1 
ATOM   12209 C  C     . ILE C 2 172 ? 117.282 73.397  126.495 1.00 24.85 ?  151 ILE C C     1 
ATOM   12210 O  O     . ILE C 2 172 ? 116.528 74.107  125.832 1.00 23.53 ?  151 ILE C O     1 
ATOM   12211 C  CB    . ILE C 2 172 ? 117.369 70.898  125.990 1.00 26.53 ?  151 ILE C CB    1 
ATOM   12212 C  CG1   . ILE C 2 172 ? 118.069 69.819  125.148 1.00 27.59 ?  151 ILE C CG1   1 
ATOM   12213 C  CG2   . ILE C 2 172 ? 115.862 70.979  125.677 1.00 26.51 ?  151 ILE C CG2   1 
ATOM   12214 C  CD1   . ILE C 2 172 ? 117.954 69.989  123.627 1.00 26.91 ?  151 ILE C CD1   1 
ATOM   12215 N  N     . SER C 2 173 ? 117.466 73.569  127.806 1.00 23.58 ?  152 SER C N     1 
ATOM   12216 C  CA    . SER C 2 173 ? 116.788 74.664  128.496 1.00 22.36 ?  152 SER C CA    1 
ATOM   12217 C  C     . SER C 2 173 ? 117.279 76.014  127.968 1.00 21.79 ?  152 SER C C     1 
ATOM   12218 O  O     . SER C 2 173 ? 116.507 76.977  127.888 1.00 20.91 ?  152 SER C O     1 
ATOM   12219 C  CB    . SER C 2 173 ? 116.925 74.564  130.021 1.00 22.43 ?  152 SER C CB    1 
ATOM   12220 O  OG    . SER C 2 173 ? 118.282 74.622  130.431 1.00 24.02 ?  152 SER C OG    1 
ATOM   12221 N  N     . LEU C 2 174 ? 118.563 76.073  127.613 1.00 21.65 ?  153 LEU C N     1 
ATOM   12222 C  CA    . LEU C 2 174 ? 119.153 77.282  127.044 1.00 21.86 ?  153 LEU C CA    1 
ATOM   12223 C  C     . LEU C 2 174 ? 118.548 77.595  125.673 1.00 21.98 ?  153 LEU C C     1 
ATOM   12224 O  O     . LEU C 2 174 ? 118.176 78.743  125.419 1.00 21.64 ?  153 LEU C O     1 
ATOM   12225 C  CB    . LEU C 2 174 ? 120.692 77.195  126.979 1.00 21.71 ?  153 LEU C CB    1 
ATOM   12226 C  CG    . LEU C 2 174 ? 121.477 78.384  126.392 1.00 22.04 ?  153 LEU C CG    1 
ATOM   12227 C  CD1   . LEU C 2 174 ? 121.106 79.717  127.042 1.00 21.99 ?  153 LEU C CD1   1 
ATOM   12228 C  CD2   . LEU C 2 174 ? 122.983 78.128  126.519 1.00 23.37 ?  153 LEU C CD2   1 
ATOM   12229 N  N     . PHE C 2 175 ? 118.445 76.580  124.809 1.00 22.17 ?  154 PHE C N     1 
ATOM   12230 C  CA    . PHE C 2 175 ? 117.793 76.721  123.488 1.00 22.02 ?  154 PHE C CA    1 
ATOM   12231 C  C     . PHE C 2 175 ? 116.384 77.291  123.606 1.00 21.86 ?  154 PHE C C     1 
ATOM   12232 O  O     . PHE C 2 175 ? 115.987 78.169  122.830 1.00 21.62 ?  154 PHE C O     1 
ATOM   12233 C  CB    . PHE C 2 175 ? 117.711 75.365  122.768 1.00 22.08 ?  154 PHE C CB    1 
ATOM   12234 C  CG    . PHE C 2 175 ? 116.905 75.397  121.484 1.00 21.99 ?  154 PHE C CG    1 
ATOM   12235 C  CD1   . PHE C 2 175 ? 117.489 75.824  120.288 1.00 20.87 ?  154 PHE C CD1   1 
ATOM   12236 C  CD2   . PHE C 2 175 ? 115.556 75.015  121.478 1.00 20.82 ?  154 PHE C CD2   1 
ATOM   12237 C  CE1   . PHE C 2 175 ? 116.746 75.884  119.107 1.00 20.27 ?  154 PHE C CE1   1 
ATOM   12238 C  CE2   . PHE C 2 175 ? 114.800 75.059  120.303 1.00 20.19 ?  154 PHE C CE2   1 
ATOM   12239 C  CZ    . PHE C 2 175 ? 115.400 75.490  119.106 1.00 20.93 ?  154 PHE C CZ    1 
ATOM   12240 N  N     . LYS C 2 176 ? 115.618 76.752  124.555 1.00 21.98 ?  155 LYS C N     1 
ATOM   12241 C  CA    . LYS C 2 176 ? 114.234 77.186  124.763 1.00 21.79 ?  155 LYS C CA    1 
ATOM   12242 C  C     . LYS C 2 176 ? 114.164 78.670  125.136 1.00 21.70 ?  155 LYS C C     1 
ATOM   12243 O  O     . LYS C 2 176 ? 113.321 79.411  124.611 1.00 21.10 ?  155 LYS C O     1 
ATOM   12244 C  CB    . LYS C 2 176 ? 113.547 76.306  125.816 1.00 22.00 ?  155 LYS C CB    1 
ATOM   12245 C  CG    . LYS C 2 176 ? 113.348 74.860  125.379 1.00 21.93 ?  155 LYS C CG    1 
ATOM   12246 C  CD    . LYS C 2 176 ? 112.728 74.018  126.481 1.00 23.06 ?  155 LYS C CD    1 
ATOM   12247 C  CE    . LYS C 2 176 ? 112.472 72.599  126.018 1.00 24.91 ?  155 LYS C CE    1 
ATOM   12248 N  NZ    . LYS C 2 176 ? 112.176 71.691  127.175 1.00 25.16 1  155 LYS C NZ    1 
ATOM   12249 N  N     . ALA C 2 177 ? 115.054 79.100  126.037 1.00 21.49 ?  156 ALA C N     1 
ATOM   12250 C  CA    . ALA C 2 177 ? 115.153 80.514  126.388 1.00 20.60 ?  156 ALA C CA    1 
ATOM   12251 C  C     . ALA C 2 177 ? 115.613 81.403  125.211 1.00 20.37 ?  156 ALA C C     1 
ATOM   12252 O  O     . ALA C 2 177 ? 115.141 82.523  125.070 1.00 19.61 ?  156 ALA C O     1 
ATOM   12253 C  CB    . ALA C 2 177 ? 116.056 80.716  127.600 1.00 20.88 ?  156 ALA C CB    1 
ATOM   12254 N  N     . MET C 2 178 ? 116.514 80.896  124.371 1.00 20.70 ?  157 MET C N     1 
ATOM   12255 C  CA    . MET C 2 178 ? 116.962 81.641  123.181 1.00 21.06 ?  157 MET C CA    1 
ATOM   12256 C  C     . MET C 2 178 ? 115.853 81.786  122.157 1.00 20.83 ?  157 MET C C     1 
ATOM   12257 O  O     . MET C 2 178 ? 115.795 82.794  121.444 1.00 21.28 ?  157 MET C O     1 
ATOM   12258 C  CB    . MET C 2 178 ? 118.177 80.976  122.510 1.00 20.68 ?  157 MET C CB    1 
ATOM   12259 C  CG    . MET C 2 178 ? 119.484 81.026  123.298 1.00 21.61 ?  157 MET C CG    1 
ATOM   12260 S  SD    . MET C 2 178 ? 120.744 79.997  122.509 1.00 24.32 ?  157 MET C SD    1 
ATOM   12261 C  CE    . MET C 2 178 ? 122.220 80.533  123.398 1.00 23.64 ?  157 MET C CE    1 
ATOM   12262 N  N     . VAL C 2 179 ? 114.994 80.772  122.046 1.00 20.76 ?  158 VAL C N     1 
ATOM   12263 C  CA    . VAL C 2 179 ? 113.822 80.864  121.166 1.00 20.14 ?  158 VAL C CA    1 
ATOM   12264 C  C     . VAL C 2 179 ? 112.895 81.964  121.692 1.00 20.35 ?  158 VAL C C     1 
ATOM   12265 O  O     . VAL C 2 179 ? 112.405 82.802  120.931 1.00 19.82 ?  158 VAL C O     1 
ATOM   12266 C  CB    . VAL C 2 179 ? 113.042 79.524  121.087 1.00 20.07 ?  158 VAL C CB    1 
ATOM   12267 C  CG1   . VAL C 2 179 ? 111.700 79.723  120.377 1.00 20.07 ?  158 VAL C CG1   1 
ATOM   12268 C  CG2   . VAL C 2 179 ? 113.869 78.464  120.366 1.00 20.57 ?  158 VAL C CG2   1 
ATOM   12269 N  N     . ALA C 2 180 ? 112.670 81.947  123.003 1.00 19.89 ?  159 ALA C N     1 
ATOM   12270 C  CA    . ALA C 2 180 ? 111.853 82.960  123.670 1.00 20.50 ?  159 ALA C CA    1 
ATOM   12271 C  C     . ALA C 2 180 ? 112.422 84.367  123.417 1.00 20.67 ?  159 ALA C C     1 
ATOM   12272 O  O     . ALA C 2 180 ? 111.676 85.290  123.084 1.00 21.27 ?  159 ALA C O     1 
ATOM   12273 C  CB    . ALA C 2 180 ? 111.796 82.675  125.155 1.00 20.03 ?  159 ALA C CB    1 
ATOM   12274 N  N     . SER C 2 181 ? 113.738 84.512  123.563 1.00 20.78 ?  160 SER C N     1 
ATOM   12275 C  CA    . SER C 2 181 ? 114.426 85.782  123.301 1.00 21.26 ?  160 SER C CA    1 
ATOM   12276 C  C     . SER C 2 181 ? 114.293 86.231  121.839 1.00 21.19 ?  160 SER C C     1 
ATOM   12277 O  O     . SER C 2 181 ? 113.986 87.388  121.576 1.00 20.89 ?  160 SER C O     1 
ATOM   12278 C  CB    . SER C 2 181 ? 115.903 85.701  123.715 1.00 21.42 ?  160 SER C CB    1 
ATOM   12279 O  OG    . SER C 2 181 ? 116.553 86.953  123.548 1.00 23.69 ?  160 SER C OG    1 
ATOM   12280 N  N     . VAL C 2 182 ? 114.523 85.323  120.884 1.00 20.99 ?  161 VAL C N     1 
ATOM   12281 C  CA    . VAL C 2 182 ? 114.283 85.675  119.480 1.00 21.18 ?  161 VAL C CA    1 
ATOM   12282 C  C     . VAL C 2 182 ? 112.826 86.120  119.264 1.00 21.15 ?  161 VAL C C     1 
ATOM   12283 O  O     . VAL C 2 182 ? 112.575 87.123  118.575 1.00 21.18 ?  161 VAL C O     1 
ATOM   12284 C  CB    . VAL C 2 182 ? 114.674 84.527  118.494 1.00 21.11 ?  161 VAL C CB    1 
ATOM   12285 C  CG1   . VAL C 2 182 ? 114.217 84.857  117.075 1.00 21.75 ?  161 VAL C CG1   1 
ATOM   12286 C  CG2   . VAL C 2 182 ? 116.183 84.289  118.524 1.00 20.98 ?  161 VAL C CG2   1 
ATOM   12287 N  N     . TYR C 2 183 ? 111.864 85.400  119.855 1.00 21.10 ?  162 TYR C N     1 
ATOM   12288 C  CA    . TYR C 2 183 ? 110.453 85.795  119.729 1.00 21.21 ?  162 TYR C CA    1 
ATOM   12289 C  C     . TYR C 2 183 ? 110.161 87.167  120.335 1.00 21.38 ?  162 TYR C C     1 
ATOM   12290 O  O     . TYR C 2 183 ? 109.318 87.900  119.830 1.00 20.97 ?  162 TYR C O     1 
ATOM   12291 C  CB    . TYR C 2 183 ? 109.485 84.747  120.315 1.00 21.50 ?  162 TYR C CB    1 
ATOM   12292 C  CG    . TYR C 2 183 ? 109.380 83.484  119.504 1.00 22.20 ?  162 TYR C CG    1 
ATOM   12293 C  CD1   . TYR C 2 183 ? 109.746 83.464  118.159 1.00 23.80 ?  162 TYR C CD1   1 
ATOM   12294 C  CD2   . TYR C 2 183 ? 108.893 82.303  120.075 1.00 23.71 ?  162 TYR C CD2   1 
ATOM   12295 C  CE1   . TYR C 2 183 ? 109.649 82.291  117.401 1.00 25.52 ?  162 TYR C CE1   1 
ATOM   12296 C  CE2   . TYR C 2 183 ? 108.789 81.137  119.333 1.00 24.01 ?  162 TYR C CE2   1 
ATOM   12297 C  CZ    . TYR C 2 183 ? 109.176 81.132  118.003 1.00 25.47 ?  162 TYR C CZ    1 
ATOM   12298 O  OH    . TYR C 2 183 ? 109.091 79.970  117.264 1.00 25.37 ?  162 TYR C OH    1 
ATOM   12299 N  N     . LEU C 2 184 ? 110.846 87.497  121.419 1.00 22.12 ?  163 LEU C N     1 
ATOM   12300 C  CA    . LEU C 2 184 ? 110.743 88.848  122.006 1.00 23.80 ?  163 LEU C CA    1 
ATOM   12301 C  C     . LEU C 2 184 ? 111.369 89.889  121.067 1.00 24.21 ?  163 LEU C C     1 
ATOM   12302 O  O     . LEU C 2 184 ? 110.759 90.905  120.807 1.00 24.72 ?  163 LEU C O     1 
ATOM   12303 C  CB    . LEU C 2 184 ? 111.397 88.897  123.391 1.00 23.52 ?  163 LEU C CB    1 
ATOM   12304 C  CG    . LEU C 2 184 ? 111.327 90.183  124.240 1.00 24.91 ?  163 LEU C CG    1 
ATOM   12305 C  CD1   . LEU C 2 184 ? 111.259 89.823  125.702 1.00 24.81 ?  163 LEU C CD1   1 
ATOM   12306 C  CD2   . LEU C 2 184 ? 112.494 91.146  123.982 1.00 26.39 ?  163 LEU C CD2   1 
ATOM   12307 N  N     . GLU C 2 185 ? 112.574 89.613  120.550 1.00 25.17 ?  164 GLU C N     1 
ATOM   12308 C  CA    . GLU C 2 185 ? 113.313 90.579  119.722 1.00 25.30 ?  164 GLU C CA    1 
ATOM   12309 C  C     . GLU C 2 185 ? 112.646 90.862  118.366 1.00 25.07 ?  164 GLU C C     1 
ATOM   12310 O  O     . GLU C 2 185 ? 112.565 92.018  117.917 1.00 24.49 ?  164 GLU C O     1 
ATOM   12311 C  CB    . GLU C 2 185 ? 114.756 90.088  119.456 1.00 26.17 ?  164 GLU C CB    1 
ATOM   12312 C  CG    . GLU C 2 185 ? 115.662 90.007  120.704 1.00 27.05 ?  164 GLU C CG    1 
ATOM   12313 C  CD    . GLU C 2 185 ? 116.189 91.373  121.160 1.00 29.23 ?  164 GLU C CD    1 
ATOM   12314 O  OE1   . GLU C 2 185 ? 115.861 92.420  120.533 1.00 28.79 ?  164 GLU C OE1   1 
ATOM   12315 O  OE2   . GLU C 2 185 ? 116.974 91.411  122.136 1.00 28.65 -1 164 GLU C OE2   1 
ATOM   12316 N  N     . SER C 2 186 ? 112.197 89.792  117.723 1.00 24.23 ?  165 SER C N     1 
ATOM   12317 C  CA    . SER C 2 186 ? 111.873 89.801  116.302 1.00 24.71 ?  165 SER C CA    1 
ATOM   12318 C  C     . SER C 2 186 ? 110.382 89.668  116.012 1.00 24.51 ?  165 SER C C     1 
ATOM   12319 O  O     . SER C 2 186 ? 109.966 89.816  114.865 1.00 24.87 ?  165 SER C O     1 
ATOM   12320 C  CB    . SER C 2 186 ? 112.627 88.667  115.594 1.00 25.06 ?  165 SER C CB    1 
ATOM   12321 O  OG    . SER C 2 186 ? 114.026 88.786  115.768 1.00 26.29 ?  165 SER C OG    1 
ATOM   12322 N  N     . PHE C 2 187 ? 109.592 89.375  117.041 1.00 24.71 ?  166 PHE C N     1 
ATOM   12323 C  CA    . PHE C 2 187 ? 108.145 89.215  116.900 1.00 25.69 ?  166 PHE C CA    1 
ATOM   12324 C  C     . PHE C 2 187 ? 107.359 90.119  117.862 1.00 25.87 ?  166 PHE C C     1 
ATOM   12325 O  O     . PHE C 2 187 ? 106.599 90.974  117.404 1.00 26.03 ?  166 PHE C O     1 
ATOM   12326 C  CB    . PHE C 2 187 ? 107.730 87.740  117.066 1.00 25.54 ?  166 PHE C CB    1 
ATOM   12327 C  CG    . PHE C 2 187 ? 106.236 87.526  117.199 1.00 26.64 ?  166 PHE C CG    1 
ATOM   12328 C  CD1   . PHE C 2 187 ? 105.361 87.894  116.169 1.00 25.90 ?  166 PHE C CD1   1 
ATOM   12329 C  CD2   . PHE C 2 187 ? 105.704 86.944  118.354 1.00 27.45 ?  166 PHE C CD2   1 
ATOM   12330 C  CE1   . PHE C 2 187 ? 103.972 87.700  116.293 1.00 25.64 ?  166 PHE C CE1   1 
ATOM   12331 C  CE2   . PHE C 2 187 ? 104.311 86.739  118.490 1.00 26.52 ?  166 PHE C CE2   1 
ATOM   12332 C  CZ    . PHE C 2 187 ? 103.450 87.117  117.457 1.00 27.18 ?  166 PHE C CZ    1 
ATOM   12333 N  N     . LEU C 2 188 ? 107.560 89.935  119.170 1.00 26.13 ?  167 LEU C N     1 
ATOM   12334 C  CA    . LEU C 2 188 ? 106.747 90.608  120.216 1.00 27.13 ?  167 LEU C CA    1 
ATOM   12335 C  C     . LEU C 2 188 ? 106.842 92.144  120.265 1.00 27.22 ?  167 LEU C C     1 
ATOM   12336 O  O     . LEU C 2 188 ? 105.875 92.816  120.650 1.00 28.03 ?  167 LEU C O     1 
ATOM   12337 C  CB    . LEU C 2 188 ? 107.076 90.056  121.613 1.00 26.89 ?  167 LEU C CB    1 
ATOM   12338 C  CG    . LEU C 2 188 ? 106.766 88.608  122.020 1.00 28.64 ?  167 LEU C CG    1 
ATOM   12339 C  CD1   . LEU C 2 188 ? 107.247 88.346  123.445 1.00 28.34 ?  167 LEU C CD1   1 
ATOM   12340 C  CD2   . LEU C 2 188 ? 105.289 88.274  121.900 1.00 27.90 ?  167 LEU C CD2   1 
ATOM   12341 N  N     . PHE C 2 189 ? 108.004 92.692  119.924 1.00 26.79 ?  168 PHE C N     1 
ATOM   12342 C  CA    . PHE C 2 189 ? 108.176 94.143  119.913 1.00 26.90 ?  168 PHE C CA    1 
ATOM   12343 C  C     . PHE C 2 189 ? 107.300 94.801  118.839 1.00 26.52 ?  168 PHE C C     1 
ATOM   12344 O  O     . PHE C 2 189 ? 107.007 96.001  118.914 1.00 26.02 ?  168 PHE C O     1 
ATOM   12345 C  CB    . PHE C 2 189 ? 109.643 94.533  119.644 1.00 27.03 ?  168 PHE C CB    1 
ATOM   12346 C  CG    . PHE C 2 189 ? 110.531 94.589  120.885 1.00 28.09 ?  168 PHE C CG    1 
ATOM   12347 C  CD1   . PHE C 2 189 ? 110.201 95.391  121.979 1.00 28.69 ?  168 PHE C CD1   1 
ATOM   12348 C  CD2   . PHE C 2 189 ? 111.735 93.895  120.918 1.00 29.15 ?  168 PHE C CD2   1 
ATOM   12349 C  CE1   . PHE C 2 189 ? 111.029 95.459  123.110 1.00 28.50 ?  168 PHE C CE1   1 
ATOM   12350 C  CE2   . PHE C 2 189 ? 112.577 93.953  122.044 1.00 30.19 ?  168 PHE C CE2   1 
ATOM   12351 C  CZ    . PHE C 2 189 ? 112.214 94.743  123.150 1.00 29.81 ?  168 PHE C CZ    1 
ATOM   12352 N  N     . TYR C 2 190 ? 106.900 94.026  117.831 1.00 26.18 ?  169 TYR C N     1 
ATOM   12353 C  CA    . TYR C 2 190 ? 106.382 94.640  116.613 1.00 26.24 ?  169 TYR C CA    1 
ATOM   12354 C  C     . TYR C 2 190 ? 104.938 95.164  116.670 1.00 25.94 ?  169 TYR C C     1 
ATOM   12355 O  O     . TYR C 2 190 ? 104.576 96.076  115.924 1.00 25.71 ?  169 TYR C O     1 
ATOM   12356 C  CB    . TYR C 2 190 ? 106.704 93.774  115.394 1.00 27.13 ?  169 TYR C CB    1 
ATOM   12357 C  CG    . TYR C 2 190 ? 108.165 93.937  115.032 1.00 28.07 ?  169 TYR C CG    1 
ATOM   12358 C  CD1   . TYR C 2 190 ? 109.155 93.181  115.670 1.00 29.54 ?  169 TYR C CD1   1 
ATOM   12359 C  CD2   . TYR C 2 190 ? 108.567 94.898  114.103 1.00 29.31 ?  169 TYR C CD2   1 
ATOM   12360 C  CE1   . TYR C 2 190 ? 110.508 93.354  115.360 1.00 30.44 ?  169 TYR C CE1   1 
ATOM   12361 C  CE2   . TYR C 2 190 ? 109.922 95.078  113.784 1.00 30.64 ?  169 TYR C CE2   1 
ATOM   12362 C  CZ    . TYR C 2 190 ? 110.884 94.305  114.421 1.00 30.40 ?  169 TYR C CZ    1 
ATOM   12363 O  OH    . TYR C 2 190 ? 112.214 94.484  114.119 1.00 28.85 ?  169 TYR C OH    1 
ATOM   12364 N  N     . SER C 2 191 ? 104.143 94.630  117.592 1.00 25.17 ?  170 SER C N     1 
ATOM   12365 C  CA    . SER C 2 191 ? 102.807 95.164  117.844 1.00 25.10 ?  170 SER C CA    1 
ATOM   12366 C  C     . SER C 2 191 ? 102.941 96.587  118.398 1.00 25.16 ?  170 SER C C     1 
ATOM   12367 O  O     . SER C 2 191 ? 102.065 97.430  118.179 1.00 25.30 ?  170 SER C O     1 
ATOM   12368 C  CB    . SER C 2 191 ? 102.029 94.265  118.806 1.00 24.56 ?  170 SER C CB    1 
ATOM   12369 O  OG    . SER C 2 191 ? 102.635 94.236  120.084 1.00 24.98 ?  170 SER C OG    1 
ATOM   12370 N  N     . GLY C 2 192 ? 104.054 96.826  119.101 1.00 24.32 ?  171 GLY C N     1 
ATOM   12371 C  CA    . GLY C 2 192 ? 104.424 98.134  119.626 1.00 23.97 ?  171 GLY C CA    1 
ATOM   12372 C  C     . GLY C 2 192 ? 105.073 99.043  118.596 1.00 23.85 ?  171 GLY C C     1 
ATOM   12373 O  O     . GLY C 2 192 ? 104.638 100.185 118.440 1.00 23.99 ?  171 GLY C O     1 
ATOM   12374 N  N     . PHE C 2 193 ? 106.084 98.542  117.886 1.00 23.28 ?  172 PHE C N     1 
ATOM   12375 C  CA    . PHE C 2 193 ? 106.794 99.325  116.858 1.00 23.85 ?  172 PHE C CA    1 
ATOM   12376 C  C     . PHE C 2 193 ? 105.894 99.869  115.747 1.00 23.72 ?  172 PHE C C     1 
ATOM   12377 O  O     . PHE C 2 193 ? 106.211 100.896 115.150 1.00 23.92 ?  172 PHE C O     1 
ATOM   12378 C  CB    . PHE C 2 193 ? 107.911 98.515  116.186 1.00 23.47 ?  172 PHE C CB    1 
ATOM   12379 C  CG    . PHE C 2 193 ? 109.135 98.301  117.049 1.00 24.32 ?  172 PHE C CG    1 
ATOM   12380 C  CD1   . PHE C 2 193 ? 109.444 99.170  118.097 1.00 22.28 ?  172 PHE C CD1   1 
ATOM   12381 C  CD2   . PHE C 2 193 ? 109.996 97.235  116.785 1.00 23.82 ?  172 PHE C CD2   1 
ATOM   12382 C  CE1   . PHE C 2 193 ? 110.578 98.970  118.893 1.00 23.41 ?  172 PHE C CE1   1 
ATOM   12383 C  CE2   . PHE C 2 193 ? 111.142 97.018  117.571 1.00 24.70 ?  172 PHE C CE2   1 
ATOM   12384 C  CZ    . PHE C 2 193 ? 111.435 97.894  118.629 1.00 24.87 ?  172 PHE C CZ    1 
ATOM   12385 N  N     . TYR C 2 194 ? 104.798 99.165  115.453 1.00 23.31 ?  173 TYR C N     1 
ATOM   12386 C  CA    . TYR C 2 194 ? 103.913 99.541  114.348 1.00 23.26 ?  173 TYR C CA    1 
ATOM   12387 C  C     . TYR C 2 194 ? 103.534 101.023 114.399 1.00 23.04 ?  173 TYR C C     1 
ATOM   12388 O  O     . TYR C 2 194 ? 103.601 101.726 113.387 1.00 23.47 ?  173 TYR C O     1 
ATOM   12389 C  CB    . TYR C 2 194 ? 102.633 98.687  114.323 1.00 23.13 ?  173 TYR C CB    1 
ATOM   12390 C  CG    . TYR C 2 194 ? 101.739 98.978  113.124 1.00 24.10 ?  173 TYR C CG    1 
ATOM   12391 C  CD1   . TYR C 2 194 ? 101.836 98.213  111.961 1.00 25.72 ?  173 TYR C CD1   1 
ATOM   12392 C  CD2   . TYR C 2 194 ? 100.819 100.028 113.146 1.00 27.04 ?  173 TYR C CD2   1 
ATOM   12393 C  CE1   . TYR C 2 194 ? 101.022 98.476  110.851 1.00 28.94 ?  173 TYR C CE1   1 
ATOM   12394 C  CE2   . TYR C 2 194 ? 100.004 100.307 112.033 1.00 27.84 ?  173 TYR C CE2   1 
ATOM   12395 C  CZ    . TYR C 2 194 ? 100.117 99.524  110.895 1.00 29.97 ?  173 TYR C CZ    1 
ATOM   12396 O  OH    . TYR C 2 194 ? 99.331  99.785  109.786 1.00 34.34 ?  173 TYR C OH    1 
ATOM   12397 N  N     . TYR C 2 195 ? 103.132 101.483 115.574 1.00 22.51 ?  174 TYR C N     1 
ATOM   12398 C  CA    . TYR C 2 195 ? 102.486 102.786 115.693 1.00 22.60 ?  174 TYR C CA    1 
ATOM   12399 C  C     . TYR C 2 195 ? 103.458 103.970 115.531 1.00 22.64 ?  174 TYR C C     1 
ATOM   12400 O  O     . TYR C 2 195 ? 103.153 104.891 114.765 1.00 22.39 ?  174 TYR C O     1 
ATOM   12401 C  CB    . TYR C 2 195 ? 101.665 102.860 116.980 1.00 22.32 ?  174 TYR C CB    1 
ATOM   12402 C  CG    . TYR C 2 195 ? 100.441 103.751 116.905 1.00 23.39 ?  174 TYR C CG    1 
ATOM   12403 C  CD1   . TYR C 2 195 ? 99.720  103.906 115.710 1.00 22.84 ?  174 TYR C CD1   1 
ATOM   12404 C  CD2   . TYR C 2 195 ? 99.982  104.410 118.043 1.00 22.23 ?  174 TYR C CD2   1 
ATOM   12405 C  CE1   . TYR C 2 195 ? 98.585  104.723 115.655 1.00 24.05 ?  174 TYR C CE1   1 
ATOM   12406 C  CE2   . TYR C 2 195 ? 98.842  105.216 118.003 1.00 24.11 ?  174 TYR C CE2   1 
ATOM   12407 C  CZ    . TYR C 2 195 ? 98.152  105.365 116.812 1.00 23.92 ?  174 TYR C CZ    1 
ATOM   12408 O  OH    . TYR C 2 195 ? 97.050  106.177 116.784 1.00 25.00 ?  174 TYR C OH    1 
ATOM   12409 N  N     . PRO C 2 196 ? 104.632 103.943 116.229 1.00 22.25 ?  175 PRO C N     1 
ATOM   12410 C  CA    . PRO C 2 196 ? 105.640 104.977 115.941 1.00 22.45 ?  175 PRO C CA    1 
ATOM   12411 C  C     . PRO C 2 196 ? 106.068 104.997 114.473 1.00 22.59 ?  175 PRO C C     1 
ATOM   12412 O  O     . PRO C 2 196 ? 106.279 106.083 113.919 1.00 22.19 ?  175 PRO C O     1 
ATOM   12413 C  CB    . PRO C 2 196 ? 106.830 104.597 116.834 1.00 22.25 ?  175 PRO C CB    1 
ATOM   12414 C  CG    . PRO C 2 196 ? 106.265 103.737 117.916 1.00 22.22 ?  175 PRO C CG    1 
ATOM   12415 C  CD    . PRO C 2 196 ? 105.060 103.046 117.326 1.00 22.32 ?  175 PRO C CD    1 
ATOM   12416 N  N     . LEU C 2 197 ? 106.185 103.819 113.852 1.00 21.92 ?  176 LEU C N     1 
ATOM   12417 C  CA    . LEU C 2 197 ? 106.546 103.734 112.435 1.00 22.35 ?  176 LEU C CA    1 
ATOM   12418 C  C     . LEU C 2 197 ? 105.434 104.294 111.541 1.00 22.60 ?  176 LEU C C     1 
ATOM   12419 O  O     . LEU C 2 197 ? 105.701 104.961 110.537 1.00 22.41 ?  176 LEU C O     1 
ATOM   12420 C  CB    . LEU C 2 197 ? 106.851 102.295 112.021 1.00 22.69 ?  176 LEU C CB    1 
ATOM   12421 C  CG    . LEU C 2 197 ? 108.049 101.550 112.626 1.00 23.68 ?  176 LEU C CG    1 
ATOM   12422 C  CD1   . LEU C 2 197 ? 108.102 100.121 112.061 1.00 23.70 ?  176 LEU C CD1   1 
ATOM   12423 C  CD2   . LEU C 2 197 ? 109.354 102.288 112.348 1.00 23.09 ?  176 LEU C CD2   1 
ATOM   12424 N  N     . TYR C 2 198 ? 104.189 104.014 111.920 1.00 22.64 ?  177 TYR C N     1 
ATOM   12425 C  CA    . TYR C 2 198 ? 103.018 104.471 111.186 1.00 22.92 ?  177 TYR C CA    1 
ATOM   12426 C  C     . TYR C 2 198 ? 102.984 106.011 111.170 1.00 23.68 ?  177 TYR C C     1 
ATOM   12427 O  O     . TYR C 2 198 ? 102.731 106.626 110.131 1.00 23.81 ?  177 TYR C O     1 
ATOM   12428 C  CB    . TYR C 2 198 ? 101.776 103.873 111.838 1.00 22.73 ?  177 TYR C CB    1 
ATOM   12429 C  CG    . TYR C 2 198 ? 100.441 104.256 111.260 1.00 22.91 ?  177 TYR C CG    1 
ATOM   12430 C  CD1   . TYR C 2 198 ? 100.003 103.715 110.050 1.00 23.49 ?  177 TYR C CD1   1 
ATOM   12431 C  CD2   . TYR C 2 198 ? 99.584  105.109 111.956 1.00 21.97 ?  177 TYR C CD2   1 
ATOM   12432 C  CE1   . TYR C 2 198 ? 98.753  104.042 109.525 1.00 23.57 ?  177 TYR C CE1   1 
ATOM   12433 C  CE2   . TYR C 2 198 ? 98.320  105.444 111.440 1.00 22.54 ?  177 TYR C CE2   1 
ATOM   12434 C  CZ    . TYR C 2 198 ? 97.919  104.909 110.225 1.00 22.88 ?  177 TYR C CZ    1 
ATOM   12435 O  OH    . TYR C 2 198 ? 96.676  105.215 109.702 1.00 23.17 ?  177 TYR C OH    1 
ATOM   12436 N  N     . PHE C 2 199 ? 103.285 106.628 112.306 1.00 23.50 ?  178 PHE C N     1 
ATOM   12437 C  CA    . PHE C 2 199 ? 103.375 108.088 112.365 1.00 24.60 ?  178 PHE C CA    1 
ATOM   12438 C  C     . PHE C 2 199 ? 104.589 108.675 111.633 1.00 24.72 ?  178 PHE C C     1 
ATOM   12439 O  O     . PHE C 2 199 ? 104.459 109.637 110.878 1.00 24.19 ?  178 PHE C O     1 
ATOM   12440 C  CB    . PHE C 2 199 ? 103.320 108.577 113.815 1.00 24.35 ?  178 PHE C CB    1 
ATOM   12441 C  CG    . PHE C 2 199 ? 101.944 108.528 114.409 1.00 26.36 ?  178 PHE C CG    1 
ATOM   12442 C  CD1   . PHE C 2 199 ? 100.843 108.998 113.693 1.00 28.53 ?  178 PHE C CD1   1 
ATOM   12443 C  CD2   . PHE C 2 199 ? 101.742 108.032 115.689 1.00 28.23 ?  178 PHE C CD2   1 
ATOM   12444 C  CE1   . PHE C 2 199 ? 99.557  108.949 114.242 1.00 29.37 ?  178 PHE C CE1   1 
ATOM   12445 C  CE2   . PHE C 2 199 ? 100.454 107.993 116.249 1.00 28.69 ?  178 PHE C CE2   1 
ATOM   12446 C  CZ    . PHE C 2 199 ? 99.371  108.448 115.527 1.00 28.43 ?  178 PHE C CZ    1 
ATOM   12447 N  N     . TYR C 2 200 ? 105.760 108.085 111.861 1.00 25.36 ?  179 TYR C N     1 
ATOM   12448 C  CA    . TYR C 2 200 ? 107.001 108.495 111.192 1.00 26.02 ?  179 TYR C CA    1 
ATOM   12449 C  C     . TYR C 2 200 ? 106.789 108.554 109.678 1.00 26.57 ?  179 TYR C C     1 
ATOM   12450 O  O     . TYR C 2 200 ? 107.188 109.517 109.016 1.00 26.30 ?  179 TYR C O     1 
ATOM   12451 C  CB    . TYR C 2 200 ? 108.128 107.505 111.519 1.00 26.19 ?  179 TYR C CB    1 
ATOM   12452 C  CG    . TYR C 2 200 ? 109.503 107.939 111.064 1.00 27.82 ?  179 TYR C CG    1 
ATOM   12453 C  CD1   . TYR C 2 200 ? 110.072 107.412 109.900 1.00 30.77 ?  179 TYR C CD1   1 
ATOM   12454 C  CD2   . TYR C 2 200 ? 110.243 108.869 111.799 1.00 29.20 ?  179 TYR C CD2   1 
ATOM   12455 C  CE1   . TYR C 2 200 ? 111.336 107.805 109.477 1.00 31.82 ?  179 TYR C CE1   1 
ATOM   12456 C  CE2   . TYR C 2 200 ? 111.506 109.271 111.388 1.00 30.44 ?  179 TYR C CE2   1 
ATOM   12457 C  CZ    . TYR C 2 200 ? 112.047 108.732 110.224 1.00 32.74 ?  179 TYR C CZ    1 
ATOM   12458 O  OH    . TYR C 2 200 ? 113.292 109.123 109.797 1.00 34.58 ?  179 TYR C OH    1 
ATOM   12459 N  N     . GLY C 2 201 ? 106.133 107.522 109.150 1.00 26.71 ?  180 GLY C N     1 
ATOM   12460 C  CA    . GLY C 2 201 ? 105.856 107.418 107.725 1.00 27.38 ?  180 GLY C CA    1 
ATOM   12461 C  C     . GLY C 2 201 ? 104.923 108.485 107.174 1.00 27.62 ?  180 GLY C C     1 
ATOM   12462 O  O     . GLY C 2 201 ? 104.889 108.694 105.974 1.00 28.25 ?  180 GLY C O     1 
ATOM   12463 N  N     . GLN C 2 202 ? 104.174 109.152 108.052 1.00 27.60 ?  181 GLN C N     1 
ATOM   12464 C  CA    . GLN C 2 202 ? 103.277 110.255 107.663 1.00 28.24 ?  181 GLN C CA    1 
ATOM   12465 C  C     . GLN C 2 202 ? 103.887 111.612 107.979 1.00 28.30 ?  181 GLN C C     1 
ATOM   12466 O  O     . GLN C 2 202 ? 103.214 112.636 107.836 1.00 27.98 ?  181 GLN C O     1 
ATOM   12467 C  CB    . GLN C 2 202 ? 101.952 110.183 108.426 1.00 27.90 ?  181 GLN C CB    1 
ATOM   12468 C  CG    . GLN C 2 202 ? 101.129 108.956 108.199 1.00 29.54 ?  181 GLN C CG    1 
ATOM   12469 C  CD    . GLN C 2 202 ? 99.909  108.932 109.093 1.00 31.54 ?  181 GLN C CD    1 
ATOM   12470 O  OE1   . GLN C 2 202 ? 98.977  109.722 108.915 1.00 32.11 ?  181 GLN C OE1   1 
ATOM   12471 N  NE2   . GLN C 2 202 ? 99.910  108.034 110.069 1.00 31.29 ?  181 GLN C NE2   1 
ATOM   12472 N  N     . GLY C 2 203 ? 105.132 111.610 108.452 1.00 28.14 ?  182 GLY C N     1 
ATOM   12473 C  CA    . GLY C 2 203 ? 105.823 112.830 108.839 1.00 28.38 ?  182 GLY C CA    1 
ATOM   12474 C  C     . GLY C 2 203 ? 105.364 113.373 110.176 1.00 28.71 ?  182 GLY C C     1 
ATOM   12475 O  O     . GLY C 2 203 ? 105.388 114.580 110.393 1.00 28.80 ?  182 GLY C O     1 
ATOM   12476 N  N     . LYS C 2 204 ? 104.930 112.479 111.063 1.00 28.24 ?  183 LYS C N     1 
ATOM   12477 C  CA    . LYS C 2 204 ? 104.444 112.865 112.378 1.00 28.48 ?  183 LYS C CA    1 
ATOM   12478 C  C     . LYS C 2 204 ? 105.269 112.187 113.468 1.00 27.82 ?  183 LYS C C     1 
ATOM   12479 O  O     . LYS C 2 204 ? 105.688 111.031 113.317 1.00 26.73 ?  183 LYS C O     1 
ATOM   12480 C  CB    . LYS C 2 204 ? 102.966 112.508 112.540 1.00 29.13 ?  183 LYS C CB    1 
ATOM   12481 C  CG    . LYS C 2 204 ? 102.029 113.284 111.614 1.00 30.41 ?  183 LYS C CG    1 
ATOM   12482 C  CD    . LYS C 2 204 ? 100.722 112.534 111.409 1.00 33.74 ?  183 LYS C CD    1 
ATOM   12483 C  CE    . LYS C 2 204 ? 99.748  113.348 110.543 1.00 36.26 ?  183 LYS C CE    1 
ATOM   12484 N  NZ    . LYS C 2 204 ? 98.458  112.617 110.378 1.00 39.17 1  183 LYS C NZ    1 
ATOM   12485 N  N     . LEU C 2 205 ? 105.493 112.916 114.560 1.00 27.77 ?  184 LEU C N     1 
ATOM   12486 C  CA    . LEU C 2 205 ? 106.291 112.432 115.694 1.00 27.79 ?  184 LEU C CA    1 
ATOM   12487 C  C     . LEU C 2 205 ? 107.640 111.875 115.232 1.00 27.85 ?  184 LEU C C     1 
ATOM   12488 O  O     . LEU C 2 205 ? 108.045 110.758 115.584 1.00 27.07 ?  184 LEU C O     1 
ATOM   12489 C  CB    . LEU C 2 205 ? 105.500 111.392 116.515 1.00 27.76 ?  184 LEU C CB    1 
ATOM   12490 C  CG    . LEU C 2 205 ? 104.138 111.858 117.046 1.00 28.62 ?  184 LEU C CG    1 
ATOM   12491 C  CD1   . LEU C 2 205 ? 103.400 110.720 117.721 1.00 29.18 ?  184 LEU C CD1   1 
ATOM   12492 C  CD2   . LEU C 2 205 ? 104.292 113.029 118.006 1.00 28.43 ?  184 LEU C CD2   1 
ATOM   12493 N  N     . MET C 2 206 ? 108.351 112.672 114.449 1.00 28.15 ?  185 MET C N     1 
ATOM   12494 C  CA    . MET C 2 206 ? 109.525 112.161 113.777 1.00 28.80 ?  185 MET C CA    1 
ATOM   12495 C  C     . MET C 2 206 ? 110.766 112.044 114.652 1.00 28.77 ?  185 MET C C     1 
ATOM   12496 O  O     . MET C 2 206 ? 111.644 111.236 114.354 1.00 28.79 ?  185 MET C O     1 
ATOM   12497 C  CB    . MET C 2 206 ? 109.781 112.954 112.509 1.00 29.96 ?  185 MET C CB    1 
ATOM   12498 C  CG    . MET C 2 206 ? 108.680 112.712 111.472 1.00 31.23 ?  185 MET C CG    1 
ATOM   12499 S  SD    . MET C 2 206 ? 109.233 113.198 109.859 1.00 40.10 ?  185 MET C SD    1 
ATOM   12500 C  CE    . MET C 2 206 ? 110.396 111.908 109.464 1.00 35.10 ?  185 MET C CE    1 
ATOM   12501 N  N     . GLN C 2 207 ? 110.830 112.813 115.734 1.00 28.62 ?  186 GLN C N     1 
ATOM   12502 C  CA    . GLN C 2 207 ? 111.963 112.717 116.660 1.00 29.10 ?  186 GLN C CA    1 
ATOM   12503 C  C     . GLN C 2 207 ? 111.856 111.455 117.519 1.00 28.52 ?  186 GLN C C     1 
ATOM   12504 O  O     . GLN C 2 207 ? 112.823 110.703 117.625 1.00 28.28 ?  186 GLN C O     1 
ATOM   12505 C  CB    . GLN C 2 207 ? 112.098 113.972 117.529 1.00 29.21 ?  186 GLN C CB    1 
ATOM   12506 C  CG    . GLN C 2 207 ? 112.401 115.248 116.742 1.00 31.41 ?  186 GLN C CG    1 
ATOM   12507 C  CD    . GLN C 2 207 ? 113.751 115.200 116.055 1.00 34.70 ?  186 GLN C CD    1 
ATOM   12508 O  OE1   . GLN C 2 207 ? 113.856 114.789 114.903 1.00 37.69 ?  186 GLN C OE1   1 
ATOM   12509 N  NE2   . GLN C 2 207 ? 114.798 115.593 116.771 1.00 34.75 ?  186 GLN C NE2   1 
ATOM   12510 N  N     . SER C 2 208 ? 110.678 111.234 118.115 1.00 28.38 ?  187 SER C N     1 
ATOM   12511 C  CA    . SER C 2 208 ? 110.352 109.975 118.798 1.00 28.25 ?  187 SER C CA    1 
ATOM   12512 C  C     . SER C 2 208 ? 110.557 108.805 117.843 1.00 28.00 ?  187 SER C C     1 
ATOM   12513 O  O     . SER C 2 208 ? 111.093 107.768 118.234 1.00 27.90 ?  187 SER C O     1 
ATOM   12514 C  CB    . SER C 2 208 ? 108.892 109.965 119.256 1.00 27.88 ?  187 SER C CB    1 
ATOM   12515 O  OG    . SER C 2 208 ? 108.627 110.995 120.185 1.00 30.27 ?  187 SER C OG    1 
ATOM   12516 N  N     . GLY C 2 209 ? 110.112 108.987 116.596 1.00 27.31 ?  188 GLY C N     1 
ATOM   12517 C  CA    . GLY C 2 209 ? 110.251 107.977 115.549 1.00 27.86 ?  188 GLY C CA    1 
ATOM   12518 C  C     . GLY C 2 209 ? 111.694 107.637 115.227 1.00 27.96 ?  188 GLY C C     1 
ATOM   12519 O  O     . GLY C 2 209 ? 112.013 106.480 114.928 1.00 27.84 ?  188 GLY C O     1 
ATOM   12520 N  N     . GLU C 2 210 ? 112.566 108.644 115.282 1.00 28.21 ?  189 GLU C N     1 
ATOM   12521 C  CA    . GLU C 2 210 ? 113.997 108.441 115.077 1.00 29.15 ?  189 GLU C CA    1 
ATOM   12522 C  C     . GLU C 2 210 ? 114.586 107.540 116.181 1.00 28.02 ?  189 GLU C C     1 
ATOM   12523 O  O     . GLU C 2 210 ? 115.377 106.635 115.908 1.00 27.15 ?  189 GLU C O     1 
ATOM   12524 C  CB    . GLU C 2 210 ? 114.718 109.791 115.031 1.00 30.17 ?  189 GLU C CB    1 
ATOM   12525 C  CG    . GLU C 2 210 ? 115.641 109.967 113.836 1.00 35.68 ?  189 GLU C CG    1 
ATOM   12526 C  CD    . GLU C 2 210 ? 114.890 110.312 112.546 1.00 40.25 ?  189 GLU C CD    1 
ATOM   12527 O  OE1   . GLU C 2 210 ? 114.226 111.374 112.476 1.00 42.98 ?  189 GLU C OE1   1 
ATOM   12528 O  OE2   . GLU C 2 210 ? 114.973 109.520 111.588 1.00 43.59 -1 189 GLU C OE2   1 
ATOM   12529 N  N     . ILE C 2 211 ? 114.192 107.795 117.426 1.00 27.57 ?  190 ILE C N     1 
ATOM   12530 C  CA    . ILE C 2 211 ? 114.582 106.938 118.551 1.00 27.47 ?  190 ILE C CA    1 
ATOM   12531 C  C     . ILE C 2 211 ? 114.136 105.489 118.329 1.00 26.69 ?  190 ILE C C     1 
ATOM   12532 O  O     . ILE C 2 211 ? 114.932 104.548 118.440 1.00 26.56 ?  190 ILE C O     1 
ATOM   12533 C  CB    . ILE C 2 211 ? 114.040 107.497 119.900 1.00 27.84 ?  190 ILE C CB    1 
ATOM   12534 C  CG1   . ILE C 2 211 ? 114.805 108.776 120.277 1.00 28.56 ?  190 ILE C CG1   1 
ATOM   12535 C  CG2   . ILE C 2 211 ? 114.125 106.425 121.011 1.00 27.27 ?  190 ILE C CG2   1 
ATOM   12536 C  CD1   . ILE C 2 211 ? 114.396 109.389 121.612 1.00 30.09 ?  190 ILE C CD1   1 
ATOM   12537 N  N     . ILE C 2 212 ? 112.868 105.322 117.974 1.00 26.33 ?  191 ILE C N     1 
ATOM   12538 C  CA    . ILE C 2 212 ? 112.288 104.004 117.738 1.00 25.96 ?  191 ILE C CA    1 
ATOM   12539 C  C     . ILE C 2 212 ? 113.010 103.244 116.616 1.00 25.46 ?  191 ILE C C     1 
ATOM   12540 O  O     . ILE C 2 212 ? 113.243 102.045 116.744 1.00 24.84 ?  191 ILE C O     1 
ATOM   12541 C  CB    . ILE C 2 212 ? 110.753 104.097 117.478 1.00 26.00 ?  191 ILE C CB    1 
ATOM   12542 C  CG1   . ILE C 2 212 ? 110.024 104.601 118.734 1.00 27.16 ?  191 ILE C CG1   1 
ATOM   12543 C  CG2   . ILE C 2 212 ? 110.172 102.765 117.023 1.00 26.87 ?  191 ILE C CG2   1 
ATOM   12544 C  CD1   . ILE C 2 212 ? 110.115 103.686 119.942 1.00 29.84 ?  191 ILE C CD1   1 
ATOM   12545 N  N     . ASN C 2 213 ? 113.361 103.940 115.531 1.00 25.35 ?  192 ASN C N     1 
ATOM   12546 C  CA    . ASN C 2 213 ? 114.120 103.327 114.435 1.00 25.60 ?  192 ASN C CA    1 
ATOM   12547 C  C     . ASN C 2 213 ? 115.499 102.845 114.872 1.00 25.14 ?  192 ASN C C     1 
ATOM   12548 O  O     . ASN C 2 213 ? 115.983 101.799 114.414 1.00 25.61 ?  192 ASN C O     1 
ATOM   12549 C  CB    . ASN C 2 213 ? 114.260 104.284 113.243 1.00 26.55 ?  192 ASN C CB    1 
ATOM   12550 C  CG    . ASN C 2 213 ? 113.087 104.202 112.292 1.00 28.10 ?  192 ASN C CG    1 
ATOM   12551 O  OD1   . ASN C 2 213 ? 112.832 103.158 111.681 1.00 31.67 ?  192 ASN C OD1   1 
ATOM   12552 N  ND2   . ASN C 2 213 ? 112.371 105.302 112.150 1.00 30.36 ?  192 ASN C ND2   1 
ATOM   12553 N  N     . LEU C 2 214 ? 116.131 103.603 115.760 1.00 24.54 ?  193 LEU C N     1 
ATOM   12554 C  CA    . LEU C 2 214 ? 117.416 103.183 116.325 1.00 24.40 ?  193 LEU C CA    1 
ATOM   12555 C  C     . LEU C 2 214 ? 117.255 101.935 117.194 1.00 23.55 ?  193 LEU C C     1 
ATOM   12556 O  O     . LEU C 2 214 ? 118.047 100.996 117.086 1.00 23.09 ?  193 LEU C O     1 
ATOM   12557 C  CB    . LEU C 2 214 ? 118.084 104.329 117.081 1.00 24.00 ?  193 LEU C CB    1 
ATOM   12558 C  CG    . LEU C 2 214 ? 118.649 105.467 116.203 1.00 25.69 ?  193 LEU C CG    1 
ATOM   12559 C  CD1   . LEU C 2 214 ? 119.029 106.689 117.039 1.00 26.28 ?  193 LEU C CD1   1 
ATOM   12560 C  CD2   . LEU C 2 214 ? 119.860 105.009 115.385 1.00 26.05 ?  193 LEU C CD2   1 
ATOM   12561 N  N     . ILE C 2 215 ? 116.222 101.925 118.042 1.00 23.19 ?  194 ILE C N     1 
ATOM   12562 C  CA    . ILE C 2 215 ? 115.875 100.744 118.839 1.00 22.88 ?  194 ILE C CA    1 
ATOM   12563 C  C     . ILE C 2 215 ? 115.622 99.547  117.907 1.00 23.81 ?  194 ILE C C     1 
ATOM   12564 O  O     . ILE C 2 215 ? 116.166 98.464  118.124 1.00 23.83 ?  194 ILE C O     1 
ATOM   12565 C  CB    . ILE C 2 215 ? 114.645 100.997 119.757 1.00 22.92 ?  194 ILE C CB    1 
ATOM   12566 C  CG1   . ILE C 2 215 ? 114.935 102.126 120.748 1.00 21.11 ?  194 ILE C CG1   1 
ATOM   12567 C  CG2   . ILE C 2 215 ? 114.219 99.721  120.498 1.00 21.89 ?  194 ILE C CG2   1 
ATOM   12568 C  CD1   . ILE C 2 215 ? 113.779 102.460 121.668 1.00 22.26 ?  194 ILE C CD1   1 
ATOM   12569 N  N     . LEU C 2 216 ? 114.836 99.754  116.850 1.00 24.23 ?  195 LEU C N     1 
ATOM   12570 C  CA    . LEU C 2 216 ? 114.491 98.664  115.930 1.00 25.41 ?  195 LEU C CA    1 
ATOM   12571 C  C     . LEU C 2 216 ? 115.722 98.115  115.207 1.00 25.63 ?  195 LEU C C     1 
ATOM   12572 O  O     . LEU C 2 216 ? 115.874 96.892  115.062 1.00 25.46 ?  195 LEU C O     1 
ATOM   12573 C  CB    . LEU C 2 216 ? 113.417 99.116  114.923 1.00 26.03 ?  195 LEU C CB    1 
ATOM   12574 C  CG    . LEU C 2 216 ? 112.852 98.133  113.888 1.00 28.00 ?  195 LEU C CG    1 
ATOM   12575 C  CD1   . LEU C 2 216 ? 111.502 98.643  113.411 1.00 31.45 ?  195 LEU C CD1   1 
ATOM   12576 C  CD2   . LEU C 2 216 ? 113.799 97.924  112.701 1.00 29.83 ?  195 LEU C CD2   1 
ATOM   12577 N  N     . ARG C 2 217 ? 116.594 99.016  114.765 1.00 25.98 ?  196 ARG C N     1 
ATOM   12578 C  CA    . ARG C 2 217 ? 117.861 98.640  114.147 1.00 26.73 ?  196 ARG C CA    1 
ATOM   12579 C  C     . ARG C 2 217 ? 118.683 97.722  115.086 1.00 25.95 ?  196 ARG C C     1 
ATOM   12580 O  O     . ARG C 2 217 ? 119.226 96.711  114.628 1.00 25.75 ?  196 ARG C O     1 
ATOM   12581 C  CB    . ARG C 2 217 ? 118.654 99.895  113.773 1.00 27.29 ?  196 ARG C CB    1 
ATOM   12582 C  CG    . ARG C 2 217 ? 119.876 99.664  112.872 1.00 30.12 ?  196 ARG C CG    1 
ATOM   12583 C  CD    . ARG C 2 217 ? 120.934 100.708 113.176 1.00 35.40 ?  196 ARG C CD    1 
ATOM   12584 N  NE    . ARG C 2 217 ? 121.061 100.833 114.629 1.00 39.87 ?  196 ARG C NE    1 
ATOM   12585 C  CZ    . ARG C 2 217 ? 121.712 101.792 115.276 1.00 40.55 ?  196 ARG C CZ    1 
ATOM   12586 N  NH1   . ARG C 2 217 ? 122.343 102.762 114.616 1.00 40.77 1  196 ARG C NH1   1 
ATOM   12587 N  NH2   . ARG C 2 217 ? 121.719 101.770 116.603 1.00 41.10 ?  196 ARG C NH2   1 
ATOM   12588 N  N     . ASP C 2 218 ? 118.750 98.069  116.376 1.00 24.70 ?  197 ASP C N     1 
ATOM   12589 C  CA    . ASP C 2 218 ? 119.403 97.222  117.395 1.00 24.55 ?  197 ASP C CA    1 
ATOM   12590 C  C     . ASP C 2 218 ? 118.712 95.850  117.533 1.00 24.23 ?  197 ASP C C     1 
ATOM   12591 O  O     . ASP C 2 218 ? 119.380 94.814  117.477 1.00 23.69 ?  197 ASP C O     1 
ATOM   12592 C  CB    . ASP C 2 218 ? 119.458 97.895  118.782 1.00 24.50 ?  197 ASP C CB    1 
ATOM   12593 C  CG    . ASP C 2 218 ? 120.367 99.137  118.833 1.00 25.84 ?  197 ASP C CG    1 
ATOM   12594 O  OD1   . ASP C 2 218 ? 121.305 99.277  118.017 1.00 26.91 ?  197 ASP C OD1   1 
ATOM   12595 O  OD2   . ASP C 2 218 ? 120.146 99.978  119.726 1.00 25.72 -1 197 ASP C OD2   1 
ATOM   12596 N  N     . GLU C 2 219 ? 117.384 95.838  117.687 1.00 23.92 ?  198 GLU C N     1 
ATOM   12597 C  CA    . GLU C 2 219 ? 116.686 94.565  117.934 1.00 24.20 ?  198 GLU C CA    1 
ATOM   12598 C  C     . GLU C 2 219 ? 116.839 93.606  116.768 1.00 24.02 ?  198 GLU C C     1 
ATOM   12599 O  O     . GLU C 2 219 ? 116.931 92.403  116.984 1.00 24.24 ?  198 GLU C O     1 
ATOM   12600 C  CB    . GLU C 2 219 ? 115.199 94.735  118.258 1.00 24.05 ?  198 GLU C CB    1 
ATOM   12601 C  CG    . GLU C 2 219 ? 114.816 95.908  119.144 1.00 25.03 ?  198 GLU C CG    1 
ATOM   12602 C  CD    . GLU C 2 219 ? 115.218 95.802  120.628 1.00 26.31 ?  198 GLU C CD    1 
ATOM   12603 O  OE1   . GLU C 2 219 ? 116.182 95.075  121.010 1.00 27.65 ?  198 GLU C OE1   1 
ATOM   12604 O  OE2   . GLU C 2 219 ? 114.548 96.511  121.428 1.00 26.87 -1 198 GLU C OE2   1 
ATOM   12605 N  N     . ALA C 2 220 ? 116.865 94.133  115.542 1.00 24.00 ?  199 ALA C N     1 
ATOM   12606 C  CA    . ALA C 2 220 ? 117.055 93.299  114.361 1.00 24.72 ?  199 ALA C CA    1 
ATOM   12607 C  C     . ALA C 2 220 ? 118.367 92.498  114.428 1.00 24.80 ?  199 ALA C C     1 
ATOM   12608 O  O     . ALA C 2 220 ? 118.372 91.295  114.152 1.00 25.04 ?  199 ALA C O     1 
ATOM   12609 C  CB    . ALA C 2 220 ? 116.983 94.137  113.060 1.00 24.66 ?  199 ALA C CB    1 
ATOM   12610 N  N     . ILE C 2 221 ? 119.462 93.156  114.802 1.00 24.85 ?  200 ILE C N     1 
ATOM   12611 C  CA    . ILE C 2 221 ? 120.753 92.460  114.943 1.00 25.07 ?  200 ILE C CA    1 
ATOM   12612 C  C     . ILE C 2 221 ? 120.804 91.567  116.192 1.00 23.86 ?  200 ILE C C     1 
ATOM   12613 O  O     . ILE C 2 221 ? 121.441 90.511  116.165 1.00 23.72 ?  200 ILE C O     1 
ATOM   12614 C  CB    . ILE C 2 221 ? 122.003 93.409  114.859 1.00 25.71 ?  200 ILE C CB    1 
ATOM   12615 C  CG1   . ILE C 2 221 ? 122.161 94.255  116.126 1.00 27.10 ?  200 ILE C CG1   1 
ATOM   12616 C  CG2   . ILE C 2 221 ? 121.958 94.263  113.577 1.00 27.18 ?  200 ILE C CG2   1 
ATOM   12617 C  CD1   . ILE C 2 221 ? 123.460 95.066  116.208 1.00 29.63 ?  200 ILE C CD1   1 
ATOM   12618 N  N     . HIS C 2 222 ? 120.124 91.978  117.263 1.00 22.79 ?  201 HIS C N     1 
ATOM   12619 C  CA    . HIS C 2 222 ? 120.007 91.136  118.476 1.00 22.48 ?  201 HIS C CA    1 
ATOM   12620 C  C     . HIS C 2 222 ? 119.285 89.825  118.174 1.00 22.04 ?  201 HIS C C     1 
ATOM   12621 O  O     . HIS C 2 222 ? 119.703 88.772  118.640 1.00 22.06 ?  201 HIS C O     1 
ATOM   12622 C  CB    . HIS C 2 222 ? 119.225 91.834  119.590 1.00 21.77 ?  201 HIS C CB    1 
ATOM   12623 C  CG    . HIS C 2 222 ? 119.890 93.043  120.156 1.00 21.76 ?  201 HIS C CG    1 
ATOM   12624 N  ND1   . HIS C 2 222 ? 119.374 93.727  121.233 1.00 20.70 ?  201 HIS C ND1   1 
ATOM   12625 C  CD2   . HIS C 2 222 ? 121.025 93.692  119.807 1.00 22.07 ?  201 HIS C CD2   1 
ATOM   12626 C  CE1   . HIS C 2 222 ? 120.154 94.752  121.519 1.00 22.26 ?  201 HIS C CE1   1 
ATOM   12627 N  NE2   . HIS C 2 222 ? 121.159 94.758  120.664 1.00 22.52 ?  201 HIS C NE2   1 
ATOM   12628 N  N     . GLY C 2 223 ? 118.181 89.907  117.429 1.00 22.35 ?  202 GLY C N     1 
ATOM   12629 C  CA    . GLY C 2 223 ? 117.406 88.725  117.019 1.00 22.01 ?  202 GLY C CA    1 
ATOM   12630 C  C     . GLY C 2 223 ? 118.184 87.773  116.115 1.00 22.73 ?  202 GLY C C     1 
ATOM   12631 O  O     . GLY C 2 223 ? 118.090 86.543  116.259 1.00 21.99 ?  202 GLY C O     1 
ATOM   12632 N  N     . VAL C 2 224 ? 118.960 88.332  115.184 1.00 22.45 ?  203 VAL C N     1 
ATOM   12633 C  CA    . VAL C 2 224 ? 119.810 87.512  114.319 1.00 22.54 ?  203 VAL C CA    1 
ATOM   12634 C  C     . VAL C 2 224 ? 120.881 86.789  115.139 1.00 22.28 ?  203 VAL C C     1 
ATOM   12635 O  O     . VAL C 2 224 ? 121.040 85.576  115.022 1.00 22.44 ?  203 VAL C O     1 
ATOM   12636 C  CB    . VAL C 2 224 ? 120.476 88.336  113.165 1.00 23.00 ?  203 VAL C CB    1 
ATOM   12637 C  CG1   . VAL C 2 224 ? 121.521 87.484  112.423 1.00 23.10 ?  203 VAL C CG1   1 
ATOM   12638 C  CG2   . VAL C 2 224 ? 119.409 88.856  112.163 1.00 23.14 ?  203 VAL C CG2   1 
ATOM   12639 N  N     . TYR C 2 225 ? 121.583 87.533  115.991 1.00 22.41 ?  204 TYR C N     1 
ATOM   12640 C  CA    . TYR C 2 225 ? 122.660 86.968  116.801 1.00 22.03 ?  204 TYR C CA    1 
ATOM   12641 C  C     . TYR C 2 225 ? 122.186 85.836  117.711 1.00 21.66 ?  204 TYR C C     1 
ATOM   12642 O  O     . TYR C 2 225 ? 122.746 84.730  117.676 1.00 21.72 ?  204 TYR C O     1 
ATOM   12643 C  CB    . TYR C 2 225 ? 123.383 88.050  117.619 1.00 22.22 ?  204 TYR C CB    1 
ATOM   12644 C  CG    . TYR C 2 225 ? 124.639 87.531  118.290 1.00 21.92 ?  204 TYR C CG    1 
ATOM   12645 C  CD1   . TYR C 2 225 ? 125.756 87.170  117.536 1.00 22.36 ?  204 TYR C CD1   1 
ATOM   12646 C  CD2   . TYR C 2 225 ? 124.703 87.393  119.678 1.00 21.43 ?  204 TYR C CD2   1 
ATOM   12647 C  CE1   . TYR C 2 225 ? 126.907 86.676  118.147 1.00 23.82 ?  204 TYR C CE1   1 
ATOM   12648 C  CE2   . TYR C 2 225 ? 125.854 86.907  120.307 1.00 21.49 ?  204 TYR C CE2   1 
ATOM   12649 C  CZ    . TYR C 2 225 ? 126.945 86.554  119.535 1.00 23.58 ?  204 TYR C CZ    1 
ATOM   12650 O  OH    . TYR C 2 225 ? 128.073 86.078  120.149 1.00 25.42 ?  204 TYR C OH    1 
ATOM   12651 N  N     . VAL C 2 226 ? 121.155 86.101  118.517 1.00 20.95 ?  205 VAL C N     1 
ATOM   12652 C  CA    . VAL C 2 226 ? 120.593 85.065  119.392 1.00 20.49 ?  205 VAL C CA    1 
ATOM   12653 C  C     . VAL C 2 226 ? 120.059 83.880  118.567 1.00 20.84 ?  205 VAL C C     1 
ATOM   12654 O  O     . VAL C 2 226 ? 120.247 82.714  118.941 1.00 21.10 ?  205 VAL C O     1 
ATOM   12655 C  CB    . VAL C 2 226 ? 119.535 85.631  120.379 1.00 20.57 ?  205 VAL C CB    1 
ATOM   12656 C  CG1   . VAL C 2 226 ? 118.945 84.511  121.237 1.00 20.35 ?  205 VAL C CG1   1 
ATOM   12657 C  CG2   . VAL C 2 226 ? 120.181 86.696  121.278 1.00 19.60 ?  205 VAL C CG2   1 
ATOM   12658 N  N     . GLY C 2 227 ? 119.448 84.176  117.424 1.00 21.08 ?  206 GLY C N     1 
ATOM   12659 C  CA    . GLY C 2 227 ? 119.035 83.126  116.480 1.00 21.43 ?  206 GLY C CA    1 
ATOM   12660 C  C     . GLY C 2 227 ? 120.164 82.197  116.056 1.00 21.95 ?  206 GLY C C     1 
ATOM   12661 O  O     . GLY C 2 227 ? 119.990 80.967  116.007 1.00 21.84 ?  206 GLY C O     1 
ATOM   12662 N  N     . LEU C 2 228 ? 121.328 82.772  115.753 1.00 22.09 ?  207 LEU C N     1 
ATOM   12663 C  CA    . LEU C 2 228 ? 122.490 81.963  115.373 1.00 22.96 ?  207 LEU C CA    1 
ATOM   12664 C  C     . LEU C 2 228 ? 122.978 81.067  116.522 1.00 22.60 ?  207 LEU C C     1 
ATOM   12665 O  O     . LEU C 2 228 ? 123.346 79.910  116.300 1.00 22.04 ?  207 LEU C O     1 
ATOM   12666 C  CB    . LEU C 2 228 ? 123.625 82.832  114.817 1.00 23.39 ?  207 LEU C CB    1 
ATOM   12667 C  CG    . LEU C 2 228 ? 123.380 83.557  113.481 1.00 24.35 ?  207 LEU C CG    1 
ATOM   12668 C  CD1   . LEU C 2 228 ? 124.406 84.685  113.300 1.00 25.01 ?  207 LEU C CD1   1 
ATOM   12669 C  CD2   . LEU C 2 228 ? 123.421 82.607  112.288 1.00 25.11 ?  207 LEU C CD2   1 
ATOM   12670 N  N     . LEU C 2 229 ? 122.952 81.586  117.748 1.00 22.37 ?  208 LEU C N     1 
ATOM   12671 C  CA    . LEU C 2 229 ? 123.306 80.772  118.927 1.00 22.62 ?  208 LEU C CA    1 
ATOM   12672 C  C     . LEU C 2 229 ? 122.323 79.621  119.159 1.00 22.77 ?  208 LEU C C     1 
ATOM   12673 O  O     . LEU C 2 229 ? 122.732 78.492  119.481 1.00 22.57 ?  208 LEU C O     1 
ATOM   12674 C  CB    . LEU C 2 229 ? 123.447 81.640  120.181 1.00 22.44 ?  208 LEU C CB    1 
ATOM   12675 C  CG    . LEU C 2 229 ? 124.472 82.781  120.099 1.00 23.54 ?  208 LEU C CG    1 
ATOM   12676 C  CD1   . LEU C 2 229 ? 124.440 83.625  121.370 1.00 23.37 ?  208 LEU C CD1   1 
ATOM   12677 C  CD2   . LEU C 2 229 ? 125.892 82.251  119.830 1.00 23.91 ?  208 LEU C CD2   1 
ATOM   12678 N  N     . ALA C 2 230 ? 121.032 79.904  118.985 1.00 22.42 ?  209 ALA C N     1 
ATOM   12679 C  CA    . ALA C 2 230 ? 119.995 78.878  119.087 1.00 22.02 ?  209 ALA C CA    1 
ATOM   12680 C  C     . ALA C 2 230 ? 120.199 77.771  118.048 1.00 22.58 ?  209 ALA C C     1 
ATOM   12681 O  O     . ALA C 2 230 ? 120.120 76.594  118.374 1.00 22.14 ?  209 ALA C O     1 
ATOM   12682 C  CB    . ALA C 2 230 ? 118.623 79.494  118.937 1.00 22.04 ?  209 ALA C CB    1 
ATOM   12683 N  N     . GLN C 2 231 ? 120.480 78.162  116.807 1.00 22.96 ?  210 GLN C N     1 
ATOM   12684 C  CA    . GLN C 2 231 ? 120.755 77.189  115.734 1.00 24.30 ?  210 GLN C CA    1 
ATOM   12685 C  C     . GLN C 2 231 ? 121.948 76.298  116.028 1.00 25.11 ?  210 GLN C C     1 
ATOM   12686 O  O     . GLN C 2 231 ? 121.946 75.117  115.662 1.00 24.97 ?  210 GLN C O     1 
ATOM   12687 C  CB    . GLN C 2 231 ? 120.955 77.897  114.398 1.00 24.38 ?  210 GLN C CB    1 
ATOM   12688 C  CG    . GLN C 2 231 ? 119.667 78.543  113.862 1.00 25.12 ?  210 GLN C CG    1 
ATOM   12689 C  CD    . GLN C 2 231 ? 119.882 79.239  112.535 1.00 28.08 ?  210 GLN C CD    1 
ATOM   12690 O  OE1   . GLN C 2 231 ? 120.363 78.631  111.578 1.00 27.83 ?  210 GLN C OE1   1 
ATOM   12691 N  NE2   . GLN C 2 231 ? 119.543 80.528  112.474 1.00 26.38 ?  210 GLN C NE2   1 
ATOM   12692 N  N     . GLU C 2 232 ? 122.968 76.857  116.683 1.00 25.80 ?  211 GLU C N     1 
ATOM   12693 C  CA    . GLU C 2 232 ? 124.126 76.064  117.108 1.00 27.16 ?  211 GLU C CA    1 
ATOM   12694 C  C     . GLU C 2 232 ? 123.699 74.890  117.983 1.00 26.47 ?  211 GLU C C     1 
ATOM   12695 O  O     . GLU C 2 232 ? 124.165 73.760  117.797 1.00 26.10 ?  211 GLU C O     1 
ATOM   12696 C  CB    . GLU C 2 232 ? 125.107 76.913  117.906 1.00 27.59 ?  211 GLU C CB    1 
ATOM   12697 C  CG    . GLU C 2 232 ? 126.170 77.583  117.091 1.00 32.55 ?  211 GLU C CG    1 
ATOM   12698 C  CD    . GLU C 2 232 ? 127.478 77.726  117.858 1.00 36.72 ?  211 GLU C CD    1 
ATOM   12699 O  OE1   . GLU C 2 232 ? 127.522 77.384  119.065 1.00 38.32 ?  211 GLU C OE1   1 
ATOM   12700 O  OE2   . GLU C 2 232 ? 128.466 78.177  117.245 1.00 40.62 -1 211 GLU C OE2   1 
ATOM   12701 N  N     . ILE C 2 233 ? 122.825 75.171  118.949 1.00 25.55 ?  212 ILE C N     1 
ATOM   12702 C  CA    . ILE C 2 233 ? 122.361 74.143  119.882 1.00 25.32 ?  212 ILE C CA    1 
ATOM   12703 C  C     . ILE C 2 233 ? 121.454 73.134  119.190 1.00 25.48 ?  212 ILE C C     1 
ATOM   12704 O  O     . ILE C 2 233 ? 121.642 71.923  119.330 1.00 25.82 ?  212 ILE C O     1 
ATOM   12705 C  CB    . ILE C 2 233 ? 121.659 74.755  121.115 1.00 25.39 ?  212 ILE C CB    1 
ATOM   12706 C  CG1   . ILE C 2 233 ? 122.679 75.528  121.955 1.00 24.37 ?  212 ILE C CG1   1 
ATOM   12707 C  CG2   . ILE C 2 233 ? 120.971 73.662  121.939 1.00 24.86 ?  212 ILE C CG2   1 
ATOM   12708 C  CD1   . ILE C 2 233 ? 122.048 76.495  122.944 1.00 25.10 ?  212 ILE C CD1   1 
ATOM   12709 N  N     . TYR C 2 234 ? 120.490 73.639  118.424 1.00 25.27 ?  213 TYR C N     1 
ATOM   12710 C  CA    . TYR C 2 234 ? 119.600 72.803  117.615 1.00 25.77 ?  213 TYR C CA    1 
ATOM   12711 C  C     . TYR C 2 234 ? 120.378 71.834  116.706 1.00 26.44 ?  213 TYR C C     1 
ATOM   12712 O  O     . TYR C 2 234 ? 120.018 70.661  116.580 1.00 26.29 ?  213 TYR C O     1 
ATOM   12713 C  CB    . TYR C 2 234 ? 118.681 73.709  116.780 1.00 25.67 ?  213 TYR C CB    1 
ATOM   12714 C  CG    . TYR C 2 234 ? 117.725 73.022  115.826 1.00 25.65 ?  213 TYR C CG    1 
ATOM   12715 C  CD1   . TYR C 2 234 ? 116.425 72.699  116.226 1.00 25.02 ?  213 TYR C CD1   1 
ATOM   12716 C  CD2   . TYR C 2 234 ? 118.100 72.747  114.502 1.00 26.59 ?  213 TYR C CD2   1 
ATOM   12717 C  CE1   . TYR C 2 234 ? 115.534 72.093  115.347 1.00 26.52 ?  213 TYR C CE1   1 
ATOM   12718 C  CE2   . TYR C 2 234 ? 117.217 72.134  113.612 1.00 27.00 ?  213 TYR C CE2   1 
ATOM   12719 C  CZ    . TYR C 2 234 ? 115.938 71.809  114.048 1.00 27.79 ?  213 TYR C CZ    1 
ATOM   12720 O  OH    . TYR C 2 234 ? 115.059 71.224  113.180 1.00 29.00 ?  213 TYR C OH    1 
ATOM   12721 N  N     . ASN C 2 235 ? 121.441 72.325  116.072 1.00 26.96 ?  214 ASN C N     1 
ATOM   12722 C  CA    . ASN C 2 235 ? 122.200 71.501  115.133 1.00 28.05 ?  214 ASN C CA    1 
ATOM   12723 C  C     . ASN C 2 235 ? 122.983 70.359  115.772 1.00 28.24 ?  214 ASN C C     1 
ATOM   12724 O  O     . ASN C 2 235 ? 123.414 69.446  115.073 1.00 28.63 ?  214 ASN C O     1 
ATOM   12725 C  CB    . ASN C 2 235 ? 123.094 72.361  114.227 1.00 28.38 ?  214 ASN C CB    1 
ATOM   12726 C  CG    . ASN C 2 235 ? 122.286 73.228  113.267 1.00 31.14 ?  214 ASN C CG    1 
ATOM   12727 O  OD1   . ASN C 2 235 ? 121.199 72.845  112.824 1.00 34.16 ?  214 ASN C OD1   1 
ATOM   12728 N  ND2   . ASN C 2 235 ? 122.815 74.402  112.945 1.00 32.42 ?  214 ASN C ND2   1 
ATOM   12729 N  N     . LYS C 2 236 ? 123.145 70.399  117.094 1.00 27.91 ?  215 LYS C N     1 
ATOM   12730 C  CA    . LYS C 2 236 ? 123.800 69.323  117.841 1.00 28.49 ?  215 LYS C CA    1 
ATOM   12731 C  C     . LYS C 2 236 ? 122.884 68.126  118.119 1.00 28.50 ?  215 LYS C C     1 
ATOM   12732 O  O     . LYS C 2 236 ? 123.352 67.058  118.519 1.00 28.98 ?  215 LYS C O     1 
ATOM   12733 C  CB    . LYS C 2 236 ? 124.357 69.848  119.168 1.00 28.10 ?  215 LYS C CB    1 
ATOM   12734 C  CG    . LYS C 2 236 ? 125.463 70.884  119.019 1.00 29.25 ?  215 LYS C CG    1 
ATOM   12735 C  CD    . LYS C 2 236 ? 125.981 71.343  120.372 1.00 30.19 ?  215 LYS C CD    1 
ATOM   12736 C  CE    . LYS C 2 236 ? 126.840 72.575  120.205 1.00 32.63 ?  215 LYS C CE    1 
ATOM   12737 N  NZ    . LYS C 2 236 ? 127.356 73.057  121.507 1.00 35.39 1  215 LYS C NZ    1 
ATOM   12738 N  N     . GLN C 2 237 ? 121.586 68.292  117.891 1.00 28.25 ?  216 GLN C N     1 
ATOM   12739 C  CA    . GLN C 2 237 ? 120.615 67.285  118.322 1.00 28.34 ?  216 GLN C CA    1 
ATOM   12740 C  C     . GLN C 2 237 ? 120.394 66.153  117.305 1.00 28.92 ?  216 GLN C C     1 
ATOM   12741 O  O     . GLN C 2 237 ? 120.692 66.302  116.119 1.00 28.53 ?  216 GLN C O     1 
ATOM   12742 C  CB    . GLN C 2 237 ? 119.289 67.965  118.695 1.00 27.68 ?  216 GLN C CB    1 
ATOM   12743 C  CG    . GLN C 2 237 ? 119.436 69.154  119.674 1.00 26.67 ?  216 GLN C CG    1 
ATOM   12744 C  CD    . GLN C 2 237 ? 120.255 68.832  120.919 1.00 25.32 ?  216 GLN C CD    1 
ATOM   12745 O  OE1   . GLN C 2 237 ? 120.084 67.779  121.540 1.00 25.49 ?  216 GLN C OE1   1 
ATOM   12746 N  NE2   . GLN C 2 237 ? 121.149 69.743  121.294 1.00 23.63 ?  216 GLN C NE2   1 
ATOM   12747 N  N     . THR C 2 238 ? 119.866 65.025  117.782 1.00 29.53 ?  217 THR C N     1 
ATOM   12748 C  CA    . THR C 2 238 ? 119.369 63.968  116.896 1.00 30.73 ?  217 THR C CA    1 
ATOM   12749 C  C     . THR C 2 238 ? 118.170 64.501  116.101 1.00 31.13 ?  217 THR C C     1 
ATOM   12750 O  O     . THR C 2 238 ? 117.576 65.531  116.469 1.00 30.17 ?  217 THR C O     1 
ATOM   12751 C  CB    . THR C 2 238 ? 118.882 62.736  117.680 1.00 30.79 ?  217 THR C CB    1 
ATOM   12752 O  OG1   . THR C 2 238 ? 117.698 63.079  118.412 1.00 31.16 ?  217 THR C OG1   1 
ATOM   12753 C  CG2   . THR C 2 238 ? 119.957 62.221  118.644 1.00 31.22 ?  217 THR C CG2   1 
ATOM   12754 N  N     . GLU C 2 239 ? 117.799 63.790  115.035 1.00 31.67 ?  218 GLU C N     1 
ATOM   12755 C  CA    . GLU C 2 239 ? 116.630 64.176  114.244 1.00 32.25 ?  218 GLU C CA    1 
ATOM   12756 C  C     . GLU C 2 239 ? 115.341 64.151  115.075 1.00 31.86 ?  218 GLU C C     1 
ATOM   12757 O  O     . GLU C 2 239 ? 114.483 65.027  114.932 1.00 31.09 ?  218 GLU C O     1 
ATOM   12758 C  CB    . GLU C 2 239 ? 116.508 63.313  112.976 1.00 33.29 ?  218 GLU C CB    1 
ATOM   12759 C  CG    . GLU C 2 239 ? 117.622 63.578  111.947 1.00 35.65 ?  218 GLU C CG    1 
ATOM   12760 C  CD    . GLU C 2 239 ? 117.666 65.036  111.474 1.00 39.17 ?  218 GLU C CD    1 
ATOM   12761 O  OE1   . GLU C 2 239 ? 116.590 65.601  111.148 1.00 41.08 ?  218 GLU C OE1   1 
ATOM   12762 O  OE2   . GLU C 2 239 ? 118.775 65.624  111.433 1.00 39.64 -1 218 GLU C OE2   1 
ATOM   12763 N  N     . GLU C 2 240 ? 115.238 63.165  115.966 1.00 31.72 ?  219 GLU C N     1 
ATOM   12764 C  CA    . GLU C 2 240 ? 114.098 63.029  116.863 1.00 31.76 ?  219 GLU C CA    1 
ATOM   12765 C  C     . GLU C 2 240 ? 113.992 64.228  117.817 1.00 30.21 ?  219 GLU C C     1 
ATOM   12766 O  O     . GLU C 2 240 ? 112.903 64.789  118.010 1.00 29.63 ?  219 GLU C O     1 
ATOM   12767 C  CB    . GLU C 2 240 ? 114.206 61.712  117.635 1.00 32.58 ?  219 GLU C CB    1 
ATOM   12768 C  CG    . GLU C 2 240 ? 112.967 61.334  118.432 1.00 36.93 ?  219 GLU C CG    1 
ATOM   12769 C  CD    . GLU C 2 240 ? 112.974 59.869  118.855 1.00 42.06 ?  219 GLU C CD    1 
ATOM   12770 O  OE1   . GLU C 2 240 ? 113.062 59.596  120.073 1.00 44.09 ?  219 GLU C OE1   1 
ATOM   12771 O  OE2   . GLU C 2 240 ? 112.898 58.988  117.967 1.00 44.45 -1 219 GLU C OE2   1 
ATOM   12772 N  N     . LYS C 2 241 ? 115.127 64.619  118.394 1.00 28.91 ?  220 LYS C N     1 
ATOM   12773 C  CA    . LYS C 2 241 ? 115.190 65.764  119.292 1.00 28.14 ?  220 LYS C CA    1 
ATOM   12774 C  C     . LYS C 2 241 ? 114.866 67.076  118.575 1.00 27.03 ?  220 LYS C C     1 
ATOM   12775 O  O     . LYS C 2 241 ? 114.148 67.921  119.120 1.00 26.72 ?  220 LYS C O     1 
ATOM   12776 C  CB    . LYS C 2 241 ? 116.557 65.853  119.977 1.00 27.83 ?  220 LYS C CB    1 
ATOM   12777 C  CG    . LYS C 2 241 ? 116.650 66.970  121.024 1.00 29.68 ?  220 LYS C CG    1 
ATOM   12778 C  CD    . LYS C 2 241 ? 116.431 66.454  122.440 1.00 33.58 ?  220 LYS C CD    1 
ATOM   12779 C  CE    . LYS C 2 241 ? 114.972 66.337  122.781 1.00 33.71 ?  220 LYS C CE    1 
ATOM   12780 N  NZ    . LYS C 2 241 ? 114.748 65.678  124.110 1.00 34.69 1  220 LYS C NZ    1 
ATOM   12781 N  N     . LYS C 2 242 ? 115.405 67.236  117.365 1.00 26.38 ?  221 LYS C N     1 
ATOM   12782 C  CA    . LYS C 2 242 ? 115.112 68.383  116.501 1.00 25.87 ?  221 LYS C CA    1 
ATOM   12783 C  C     . LYS C 2 242 ? 113.626 68.533  116.238 1.00 25.72 ?  221 LYS C C     1 
ATOM   12784 O  O     . LYS C 2 242 ? 113.090 69.648  116.306 1.00 24.52 ?  221 LYS C O     1 
ATOM   12785 C  CB    . LYS C 2 242 ? 115.848 68.275  115.164 1.00 25.83 ?  221 LYS C CB    1 
ATOM   12786 C  CG    . LYS C 2 242 ? 117.325 68.591  115.220 1.00 26.76 ?  221 LYS C CG    1 
ATOM   12787 C  CD    . LYS C 2 242 ? 117.910 68.580  113.811 1.00 28.40 ?  221 LYS C CD    1 
ATOM   12788 C  CE    . LYS C 2 242 ? 119.410 68.662  113.830 1.00 29.84 ?  221 LYS C CE    1 
ATOM   12789 N  NZ    . LYS C 2 242 ? 119.962 68.427  112.475 1.00 30.96 1  221 LYS C NZ    1 
ATOM   12790 N  N     . ALA C 2 243 ? 112.972 67.410  115.926 1.00 25.97 ?  222 ALA C N     1 
ATOM   12791 C  CA    . ALA C 2 243 ? 111.523 67.389  115.712 1.00 25.79 ?  222 ALA C CA    1 
ATOM   12792 C  C     . ALA C 2 243 ? 110.763 67.905  116.935 1.00 25.24 ?  222 ALA C C     1 
ATOM   12793 O  O     . ALA C 2 243 ? 109.798 68.669  116.792 1.00 25.37 ?  222 ALA C O     1 
ATOM   12794 C  CB    . ALA C 2 243 ? 111.052 65.989  115.315 1.00 26.17 ?  222 ALA C CB    1 
ATOM   12795 N  N     . GLU C 2 244 ? 111.207 67.522  118.130 1.00 25.02 ?  223 GLU C N     1 
ATOM   12796 C  CA    . GLU C 2 244 ? 110.607 68.032  119.373 1.00 25.08 ?  223 GLU C CA    1 
ATOM   12797 C  C     . GLU C 2 244 ? 110.865 69.536  119.577 1.00 24.70 ?  223 GLU C C     1 
ATOM   12798 O  O     . GLU C 2 244 ? 109.982 70.274  120.037 1.00 24.20 ?  223 GLU C O     1 
ATOM   12799 C  CB    . GLU C 2 244 ? 111.091 67.238  120.590 1.00 25.35 ?  223 GLU C CB    1 
ATOM   12800 C  CG    . GLU C 2 244 ? 110.443 67.697  121.909 1.00 26.67 ?  223 GLU C CG    1 
ATOM   12801 C  CD    . GLU C 2 244 ? 111.119 67.121  123.139 1.00 28.29 ?  223 GLU C CD    1 
ATOM   12802 O  OE1   . GLU C 2 244 ? 111.766 66.061  123.040 1.00 29.51 ?  223 GLU C OE1   1 
ATOM   12803 O  OE2   . GLU C 2 244 ? 111.002 67.737  124.215 1.00 29.09 -1 223 GLU C OE2   1 
ATOM   12804 N  N     . LEU C 2 245 ? 112.073 69.981  119.246 1.00 24.27 ?  224 LEU C N     1 
ATOM   12805 C  CA    . LEU C 2 245 ? 112.423 71.396  119.385 1.00 24.54 ?  224 LEU C CA    1 
ATOM   12806 C  C     . LEU C 2 245 ? 111.618 72.302  118.442 1.00 24.42 ?  224 LEU C C     1 
ATOM   12807 O  O     . LEU C 2 245 ? 111.224 73.406  118.827 1.00 24.10 ?  224 LEU C O     1 
ATOM   12808 C  CB    . LEU C 2 245 ? 113.941 71.607  119.229 1.00 23.86 ?  224 LEU C CB    1 
ATOM   12809 C  CG    . LEU C 2 245 ? 114.811 71.006  120.342 1.00 24.78 ?  224 LEU C CG    1 
ATOM   12810 C  CD1   . LEU C 2 245 ? 116.292 71.327  120.113 1.00 25.54 ?  224 LEU C CD1   1 
ATOM   12811 C  CD2   . LEU C 2 245 ? 114.376 71.472  121.739 1.00 25.29 ?  224 LEU C CD2   1 
ATOM   12812 N  N     . ARG C 2 246 ? 111.365 71.825  117.224 1.00 25.26 ?  225 ARG C N     1 
ATOM   12813 C  CA    . ARG C 2 246 ? 110.492 72.530  116.275 1.00 25.97 ?  225 ARG C CA    1 
ATOM   12814 C  C     . ARG C 2 246 ? 109.075 72.613  116.826 1.00 25.85 ?  225 ARG C C     1 
ATOM   12815 O  O     . ARG C 2 246 ? 108.435 73.662  116.733 1.00 25.01 ?  225 ARG C O     1 
ATOM   12816 C  CB    . ARG C 2 246 ? 110.495 71.862  114.883 1.00 26.65 ?  225 ARG C CB    1 
ATOM   12817 C  CG    . ARG C 2 246 ? 111.835 71.952  114.157 1.00 28.90 ?  225 ARG C CG    1 
ATOM   12818 C  CD    . ARG C 2 246 ? 111.736 71.642  112.644 1.00 31.26 ?  225 ARG C CD    1 
ATOM   12819 N  NE    . ARG C 2 246 ? 111.218 70.301  112.366 1.00 34.01 ?  225 ARG C NE    1 
ATOM   12820 C  CZ    . ARG C 2 246 ? 111.918 69.172  112.481 1.00 35.64 ?  225 ARG C CZ    1 
ATOM   12821 N  NH1   . ARG C 2 246 ? 113.185 69.194  112.876 1.00 36.11 1  225 ARG C NH1   1 
ATOM   12822 N  NH2   . ARG C 2 246 ? 111.342 68.008  112.199 1.00 37.05 ?  225 ARG C NH2   1 
ATOM   12823 N  N     . GLU C 2 247 ? 108.594 71.512  117.411 1.00 26.01 ?  226 GLU C N     1 
ATOM   12824 C  CA    . GLU C 2 247 ? 107.285 71.499  118.074 1.00 26.48 ?  226 GLU C CA    1 
ATOM   12825 C  C     . GLU C 2 247 ? 107.228 72.541  119.191 1.00 25.72 ?  226 GLU C C     1 
ATOM   12826 O  O     . GLU C 2 247 ? 106.262 73.312  119.280 1.00 25.16 ?  226 GLU C O     1 
ATOM   12827 C  CB    . GLU C 2 247 ? 106.957 70.120  118.653 1.00 27.18 ?  226 GLU C CB    1 
ATOM   12828 C  CG    . GLU C 2 247 ? 105.475 69.945  118.964 1.00 30.38 ?  226 GLU C CG    1 
ATOM   12829 C  CD    . GLU C 2 247 ? 105.189 69.128  120.210 1.00 35.77 ?  226 GLU C CD    1 
ATOM   12830 O  OE1   . GLU C 2 247 ? 105.992 68.243  120.576 1.00 38.02 ?  226 GLU C OE1   1 
ATOM   12831 O  OE2   . GLU C 2 247 ? 104.134 69.374  120.833 1.00 40.39 -1 226 GLU C OE2   1 
ATOM   12832 N  N     . PHE C 2 248 ? 108.263 72.562  120.033 1.00 24.71 ?  227 PHE C N     1 
ATOM   12833 C  CA    . PHE C 2 248 ? 108.351 73.555  121.102 1.00 23.71 ?  227 PHE C CA    1 
ATOM   12834 C  C     . PHE C 2 248 ? 108.265 74.970  120.526 1.00 23.14 ?  227 PHE C C     1 
ATOM   12835 O  O     . PHE C 2 248 ? 107.485 75.790  121.013 1.00 22.40 ?  227 PHE C O     1 
ATOM   12836 C  CB    . PHE C 2 248 ? 109.637 73.406  121.935 1.00 23.85 ?  227 PHE C CB    1 
ATOM   12837 C  CG    . PHE C 2 248 ? 109.922 74.606  122.803 1.00 23.64 ?  227 PHE C CG    1 
ATOM   12838 C  CD1   . PHE C 2 248 ? 109.294 74.744  124.043 1.00 23.07 ?  227 PHE C CD1   1 
ATOM   12839 C  CD2   . PHE C 2 248 ? 110.766 75.634  122.346 1.00 23.04 ?  227 PHE C CD2   1 
ATOM   12840 C  CE1   . PHE C 2 248 ? 109.528 75.862  124.843 1.00 22.73 ?  227 PHE C CE1   1 
ATOM   12841 C  CE2   . PHE C 2 248 ? 111.004 76.763  123.132 1.00 23.31 ?  227 PHE C CE2   1 
ATOM   12842 C  CZ    . PHE C 2 248 ? 110.386 76.880  124.388 1.00 21.51 ?  227 PHE C CZ    1 
ATOM   12843 N  N     . ALA C 2 249 ? 109.063 75.237  119.491 1.00 22.95 ?  228 ALA C N     1 
ATOM   12844 C  CA    . ALA C 2 249 ? 109.171 76.585  118.915 1.00 22.96 ?  228 ALA C CA    1 
ATOM   12845 C  C     . ALA C 2 249 ? 107.852 77.042  118.297 1.00 23.31 ?  228 ALA C C     1 
ATOM   12846 O  O     . ALA C 2 249 ? 107.433 78.186  118.483 1.00 22.63 ?  228 ALA C O     1 
ATOM   12847 C  CB    . ALA C 2 249 ? 110.294 76.639  117.881 1.00 22.40 ?  228 ALA C CB    1 
ATOM   12848 N  N     . ILE C 2 250 ? 107.209 76.138  117.567 1.00 23.66 ?  229 ILE C N     1 
ATOM   12849 C  CA    . ILE C 2 250 ? 105.937 76.434  116.907 1.00 25.00 ?  229 ILE C CA    1 
ATOM   12850 C  C     . ILE C 2 250 ? 104.781 76.553  117.910 1.00 24.64 ?  229 ILE C C     1 
ATOM   12851 O  O     . ILE C 2 250 ? 103.973 77.485  117.816 1.00 24.26 ?  229 ILE C O     1 
ATOM   12852 C  CB    . ILE C 2 250 ? 105.647 75.432  115.746 1.00 25.43 ?  229 ILE C CB    1 
ATOM   12853 C  CG1   . ILE C 2 250 ? 106.608 75.717  114.583 1.00 27.27 ?  229 ILE C CG1   1 
ATOM   12854 C  CG2   . ILE C 2 250 ? 104.190 75.587  115.229 1.00 27.62 ?  229 ILE C CG2   1 
ATOM   12855 C  CD1   . ILE C 2 250 ? 107.084 74.476  113.815 1.00 31.32 ?  229 ILE C CD1   1 
ATOM   12856 N  N     . ASP C 2 251 ? 104.720 75.644  118.883 1.00 24.78 ?  230 ASP C N     1 
ATOM   12857 C  CA    . ASP C 2 251 ? 103.724 75.756  119.966 1.00 25.20 ?  230 ASP C CA    1 
ATOM   12858 C  C     . ASP C 2 251 ? 103.868 77.064  120.743 1.00 24.08 ?  230 ASP C C     1 
ATOM   12859 O  O     . ASP C 2 251 ? 102.869 77.717  121.081 1.00 23.34 ?  230 ASP C O     1 
ATOM   12860 C  CB    . ASP C 2 251 ? 103.841 74.598  120.967 1.00 25.73 ?  230 ASP C CB    1 
ATOM   12861 C  CG    . ASP C 2 251 ? 103.275 73.300  120.439 1.00 28.78 ?  230 ASP C CG    1 
ATOM   12862 O  OD1   . ASP C 2 251 ? 102.685 73.285  119.334 1.00 29.99 ?  230 ASP C OD1   1 
ATOM   12863 O  OD2   . ASP C 2 251 ? 103.431 72.282  121.146 1.00 33.31 -1 230 ASP C OD2   1 
ATOM   12864 N  N     . LEU C 2 252 ? 105.111 77.435  121.040 1.00 22.98 ?  231 LEU C N     1 
ATOM   12865 C  CA    . LEU C 2 252 ? 105.364 78.674  121.777 1.00 21.63 ?  231 LEU C CA    1 
ATOM   12866 C  C     . LEU C 2 252 ? 104.962 79.882  120.939 1.00 21.66 ?  231 LEU C C     1 
ATOM   12867 O  O     . LEU C 2 252 ? 104.353 80.829  121.440 1.00 19.41 ?  231 LEU C O     1 
ATOM   12868 C  CB    . LEU C 2 252 ? 106.834 78.790  122.178 1.00 21.89 ?  231 LEU C CB    1 
ATOM   12869 C  CG    . LEU C 2 252 ? 107.273 80.086  122.885 1.00 21.33 ?  231 LEU C CG    1 
ATOM   12870 C  CD1   . LEU C 2 252 ? 106.475 80.330  124.184 1.00 20.89 ?  231 LEU C CD1   1 
ATOM   12871 C  CD2   . LEU C 2 252 ? 108.779 80.027  123.153 1.00 20.31 ?  231 LEU C CD2   1 
ATOM   12872 N  N     . LEU C 2 253 ? 105.316 79.846  119.658 1.00 22.28 ?  232 LEU C N     1 
ATOM   12873 C  CA    . LEU C 2 253 ? 104.982 80.952  118.768 1.00 23.05 ?  232 LEU C CA    1 
ATOM   12874 C  C     . LEU C 2 253 ? 103.471 81.147  118.691 1.00 23.36 ?  232 LEU C C     1 
ATOM   12875 O  O     . LEU C 2 253 ? 102.981 82.277  118.860 1.00 22.96 ?  232 LEU C O     1 
ATOM   12876 C  CB    . LEU C 2 253 ? 105.584 80.749  117.376 1.00 23.53 ?  232 LEU C CB    1 
ATOM   12877 C  CG    . LEU C 2 253 ? 105.277 81.886  116.394 1.00 25.63 ?  232 LEU C CG    1 
ATOM   12878 C  CD1   . LEU C 2 253 ? 105.907 83.205  116.840 1.00 25.88 ?  232 LEU C CD1   1 
ATOM   12879 C  CD2   . LEU C 2 253 ? 105.754 81.500  115.002 1.00 27.67 ?  232 LEU C CD2   1 
ATOM   12880 N  N     . ASN C 2 254 ? 102.741 80.053  118.455 1.00 23.55 ?  233 ASN C N     1 
ATOM   12881 C  CA    . ASN C 2 254 ? 101.268 80.098  118.417 1.00 24.61 ?  233 ASN C CA    1 
ATOM   12882 C  C     . ASN C 2 254 ? 100.636 80.614  119.712 1.00 23.57 ?  233 ASN C C     1 
ATOM   12883 O  O     . ASN C 2 254 ? 99.697  81.405  119.682 1.00 23.52 ?  233 ASN C O     1 
ATOM   12884 C  CB    . ASN C 2 254 ? 100.681 78.734  118.043 1.00 24.99 ?  233 ASN C CB    1 
ATOM   12885 C  CG    . ASN C 2 254 ? 100.626 78.514  116.537 1.00 28.92 ?  233 ASN C CG    1 
ATOM   12886 O  OD1   . ASN C 2 254 ? 100.017 79.290  115.798 1.00 33.75 ?  233 ASN C OD1   1 
ATOM   12887 N  ND2   . ASN C 2 254 ? 101.259 77.450  116.079 1.00 30.99 ?  233 ASN C ND2   1 
ATOM   12888 N  N     . GLN C 2 255 ? 101.158 80.167  120.851 1.00 23.22 ?  234 GLN C N     1 
ATOM   12889 C  CA    . GLN C 2 255 ? 100.654 80.634  122.135 1.00 22.54 ?  234 GLN C CA    1 
ATOM   12890 C  C     . GLN C 2 255 ? 100.889 82.147  122.323 1.00 22.00 ?  234 GLN C C     1 
ATOM   12891 O  O     . GLN C 2 255 ? 99.989  82.884  122.761 1.00 21.73 ?  234 GLN C O     1 
ATOM   12892 C  CB    . GLN C 2 255 ? 101.282 79.837  123.277 1.00 22.85 ?  234 GLN C CB    1 
ATOM   12893 C  CG    . GLN C 2 255 ? 100.590 80.049  124.608 1.00 23.87 ?  234 GLN C CG    1 
ATOM   12894 C  CD    . GLN C 2 255 ? 101.240 79.276  125.750 1.00 24.95 ?  234 GLN C CD    1 
ATOM   12895 O  OE1   . GLN C 2 255 ? 102.119 78.435  125.533 1.00 24.21 ?  234 GLN C OE1   1 
ATOM   12896 N  NE2   . GLN C 2 255 ? 100.824 79.583  126.981 1.00 25.97 ?  234 GLN C NE2   1 
ATOM   12897 N  N     . LEU C 2 256 ? 102.092 82.602  121.991 1.00 21.27 ?  235 LEU C N     1 
ATOM   12898 C  CA    . LEU C 2 256 ? 102.416 84.024  122.058 1.00 21.37 ?  235 LEU C CA    1 
ATOM   12899 C  C     . LEU C 2 256 ? 101.584 84.821  121.049 1.00 21.21 ?  235 LEU C C     1 
ATOM   12900 O  O     . LEU C 2 256 ? 101.114 85.919  121.344 1.00 20.75 ?  235 LEU C O     1 
ATOM   12901 C  CB    . LEU C 2 256 ? 103.912 84.236  121.786 1.00 20.93 ?  235 LEU C CB    1 
ATOM   12902 C  CG    . LEU C 2 256 ? 104.924 83.813  122.853 1.00 21.74 ?  235 LEU C CG    1 
ATOM   12903 C  CD1   . LEU C 2 256 ? 106.353 83.996  122.320 1.00 20.15 ?  235 LEU C CD1   1 
ATOM   12904 C  CD2   . LEU C 2 256 ? 104.736 84.577  124.163 1.00 20.90 ?  235 LEU C CD2   1 
ATOM   12905 N  N     . TYR C 2 257 ? 101.430 84.258  119.856 1.00 21.68 ?  236 TYR C N     1 
ATOM   12906 C  CA    . TYR C 2 257 ? 100.667 84.884  118.777 1.00 22.40 ?  236 TYR C CA    1 
ATOM   12907 C  C     . TYR C 2 257 ? 99.208  85.140  119.193 1.00 23.31 ?  236 TYR C C     1 
ATOM   12908 O  O     . TYR C 2 257 ? 98.707  86.273  119.057 1.00 22.99 ?  236 TYR C O     1 
ATOM   12909 C  CB    . TYR C 2 257 ? 100.746 84.029  117.509 1.00 22.81 ?  236 TYR C CB    1 
ATOM   12910 C  CG    . TYR C 2 257 ? 99.879  84.503  116.359 1.00 23.76 ?  236 TYR C CG    1 
ATOM   12911 C  CD1   . TYR C 2 257 ? 100.148 85.708  115.704 1.00 24.05 ?  236 TYR C CD1   1 
ATOM   12912 C  CD2   . TYR C 2 257 ? 98.784  83.752  115.937 1.00 24.04 ?  236 TYR C CD2   1 
ATOM   12913 C  CE1   . TYR C 2 257 ? 99.347  86.153  114.657 1.00 24.40 ?  236 TYR C CE1   1 
ATOM   12914 C  CE2   . TYR C 2 257 ? 97.979  84.189  114.887 1.00 26.30 ?  236 TYR C CE2   1 
ATOM   12915 C  CZ    . TYR C 2 257 ? 98.276  85.382  114.254 1.00 25.80 ?  236 TYR C CZ    1 
ATOM   12916 O  OH    . TYR C 2 257 ? 97.490  85.802  113.219 1.00 28.42 ?  236 TYR C OH    1 
ATOM   12917 N  N     . GLU C 2 258 ? 98.551  84.109  119.735 1.00 22.99 ?  237 GLU C N     1 
ATOM   12918 C  CA    . GLU C 2 258 ? 97.151  84.222  120.158 1.00 24.46 ?  237 GLU C CA    1 
ATOM   12919 C  C     . GLU C 2 258 ? 96.966  85.291  121.222 1.00 23.86 ?  237 GLU C C     1 
ATOM   12920 O  O     . GLU C 2 258 ? 96.007  86.061  121.173 1.00 24.01 ?  237 GLU C O     1 
ATOM   12921 C  CB    . GLU C 2 258 ? 96.586  82.869  120.624 1.00 25.21 ?  237 GLU C CB    1 
ATOM   12922 C  CG    . GLU C 2 258 ? 96.414  81.842  119.481 1.00 30.12 ?  237 GLU C CG    1 
ATOM   12923 C  CD    . GLU C 2 258 ? 95.354  82.257  118.456 1.00 35.29 ?  237 GLU C CD    1 
ATOM   12924 O  OE1   . GLU C 2 258 ? 94.391  82.970  118.823 1.00 37.71 ?  237 GLU C OE1   1 
ATOM   12925 O  OE2   . GLU C 2 258 ? 95.480  81.862  117.273 1.00 39.07 -1 237 GLU C OE2   1 
ATOM   12926 N  N     . ASN C 2 259 ? 97.903  85.358  122.167 1.00 23.25 ?  238 ASN C N     1 
ATOM   12927 C  CA    . ASN C 2 259 ? 97.898  86.415  123.175 1.00 23.10 ?  238 ASN C CA    1 
ATOM   12928 C  C     . ASN C 2 259 ? 98.136  87.802  122.547 1.00 22.68 ?  238 ASN C C     1 
ATOM   12929 O  O     . ASN C 2 259 ? 97.484  88.784  122.914 1.00 22.73 ?  238 ASN C O     1 
ATOM   12930 C  CB    . ASN C 2 259 ? 98.938  86.108  124.256 1.00 23.22 ?  238 ASN C CB    1 
ATOM   12931 C  CG    . ASN C 2 259 ? 98.958  87.149  125.357 1.00 24.46 ?  238 ASN C CG    1 
ATOM   12932 O  OD1   . ASN C 2 259 ? 98.025  87.245  126.159 1.00 26.28 ?  238 ASN C OD1   1 
ATOM   12933 N  ND2   . ASN C 2 259 ? 100.027 87.936  125.402 1.00 24.93 ?  238 ASN C ND2   1 
ATOM   12934 N  N     . GLU C 2 260 ? 99.049  87.874  121.581 1.00 22.64 ?  239 GLU C N     1 
ATOM   12935 C  CA    . GLU C 2 260 ? 99.375  89.145  120.932 1.00 23.18 ?  239 GLU C CA    1 
ATOM   12936 C  C     . GLU C 2 260 ? 98.189  89.697  120.123 1.00 23.40 ?  239 GLU C C     1 
ATOM   12937 O  O     . GLU C 2 260 ? 97.987  90.920  120.054 1.00 23.57 ?  239 GLU C O     1 
ATOM   12938 C  CB    . GLU C 2 260 ? 100.627 89.011  120.055 1.00 23.19 ?  239 GLU C CB    1 
ATOM   12939 C  CG    . GLU C 2 260 ? 101.420 90.329  119.882 1.00 24.33 ?  239 GLU C CG    1 
ATOM   12940 C  CD    . GLU C 2 260 ? 102.027 90.857  121.194 1.00 27.99 ?  239 GLU C CD    1 
ATOM   12941 O  OE1   . GLU C 2 260 ? 101.981 90.161  122.233 1.00 27.36 ?  239 GLU C OE1   1 
ATOM   12942 O  OE2   . GLU C 2 260 ? 102.552 91.992  121.191 1.00 28.98 -1 239 GLU C OE2   1 
ATOM   12943 N  N     . LEU C 2 261 ? 97.405  88.798  119.527 1.00 23.35 ?  240 LEU C N     1 
ATOM   12944 C  CA    . LEU C 2 261 ? 96.169  89.191  118.834 1.00 23.74 ?  240 LEU C CA    1 
ATOM   12945 C  C     . LEU C 2 261 ? 95.206  89.948  119.752 1.00 23.80 ?  240 LEU C C     1 
ATOM   12946 O  O     . LEU C 2 261 ? 94.688  91.017  119.390 1.00 23.33 ?  240 LEU C O     1 
ATOM   12947 C  CB    . LEU C 2 261 ? 95.460  87.973  118.235 1.00 24.09 ?  240 LEU C CB    1 
ATOM   12948 C  CG    . LEU C 2 261 ? 96.134  87.286  117.047 1.00 24.07 ?  240 LEU C CG    1 
ATOM   12949 C  CD1   . LEU C 2 261 ? 95.300  86.092  116.601 1.00 24.77 ?  240 LEU C CD1   1 
ATOM   12950 C  CD2   . LEU C 2 261 ? 96.351  88.274  115.883 1.00 24.38 ?  240 LEU C CD2   1 
ATOM   12951 N  N     . GLU C 2 262 ? 94.967  89.387  120.931 1.00 23.41 ?  241 GLU C N     1 
ATOM   12952 C  CA    . GLU C 2 262 ? 94.097  90.017  121.923 1.00 24.02 ?  241 GLU C CA    1 
ATOM   12953 C  C     . GLU C 2 262 ? 94.660  91.360  122.413 1.00 22.91 ?  241 GLU C C     1 
ATOM   12954 O  O     . GLU C 2 262 ? 93.917  92.321  122.565 1.00 22.94 ?  241 GLU C O     1 
ATOM   12955 C  CB    . GLU C 2 262 ? 93.878  89.067  123.101 1.00 24.92 ?  241 GLU C CB    1 
ATOM   12956 C  CG    . GLU C 2 262 ? 93.106  87.804  122.753 1.00 27.82 ?  241 GLU C CG    1 
ATOM   12957 C  CD    . GLU C 2 262 ? 92.888  86.910  123.960 1.00 33.08 ?  241 GLU C CD    1 
ATOM   12958 O  OE1   . GLU C 2 262 ? 93.810  86.147  124.331 1.00 36.94 ?  241 GLU C OE1   1 
ATOM   12959 O  OE2   . GLU C 2 262 ? 91.787  86.963  124.538 1.00 37.48 -1 241 GLU C OE2   1 
ATOM   12960 N  N     . TYR C 2 263 ? 95.970  91.405  122.665 1.00 21.84 ?  242 TYR C N     1 
ATOM   12961 C  CA    . TYR C 2 263 ? 96.678  92.632  123.028 1.00 21.66 ?  242 TYR C CA    1 
ATOM   12962 C  C     . TYR C 2 263 ? 96.535  93.686  121.937 1.00 21.28 ?  242 TYR C C     1 
ATOM   12963 O  O     . TYR C 2 263 ? 96.264  94.861  122.225 1.00 21.14 ?  242 TYR C O     1 
ATOM   12964 C  CB    . TYR C 2 263 ? 98.170  92.329  123.232 1.00 21.44 ?  242 TYR C CB    1 
ATOM   12965 C  CG    . TYR C 2 263 ? 99.046  93.506  123.639 1.00 21.89 ?  242 TYR C CG    1 
ATOM   12966 C  CD1   . TYR C 2 263 ? 98.941  94.075  124.909 1.00 22.52 ?  242 TYR C CD1   1 
ATOM   12967 C  CD2   . TYR C 2 263 ? 100.006 94.023  122.765 1.00 22.58 ?  242 TYR C CD2   1 
ATOM   12968 C  CE1   . TYR C 2 263 ? 99.758  95.138  125.293 1.00 22.67 ?  242 TYR C CE1   1 
ATOM   12969 C  CE2   . TYR C 2 263 ? 100.835 95.086  123.141 1.00 24.03 ?  242 TYR C CE2   1 
ATOM   12970 C  CZ    . TYR C 2 263 ? 100.707 95.629  124.415 1.00 23.75 ?  242 TYR C CZ    1 
ATOM   12971 O  OH    . TYR C 2 263 ? 101.510 96.683  124.805 1.00 26.82 ?  242 TYR C OH    1 
ATOM   12972 N  N     . THR C 2 264 ? 96.721  93.262  120.689 1.00 20.66 ?  243 THR C N     1 
ATOM   12973 C  CA    . THR C 2 264 ? 96.639  94.171  119.537 1.00 20.99 ?  243 THR C CA    1 
ATOM   12974 C  C     . THR C 2 264 ? 95.234  94.772  119.412 1.00 21.22 ?  243 THR C C     1 
ATOM   12975 O  O     . THR C 2 264 ? 95.086  95.992  119.244 1.00 20.95 ?  243 THR C O     1 
ATOM   12976 C  CB    . THR C 2 264 ? 97.053  93.454  118.223 1.00 20.58 ?  243 THR C CB    1 
ATOM   12977 O  OG1   . THR C 2 264 ? 98.437  93.101  118.300 1.00 20.84 ?  243 THR C OG1   1 
ATOM   12978 C  CG2   . THR C 2 264 ? 96.841  94.353  117.002 1.00 20.90 ?  243 THR C CG2   1 
ATOM   12979 N  N     . GLU C 2 265 ? 94.209  93.925  119.525 1.00 21.62 ?  244 GLU C N     1 
ATOM   12980 C  CA    . GLU C 2 265 ? 92.828  94.403  119.454 1.00 23.46 ?  244 GLU C CA    1 
ATOM   12981 C  C     . GLU C 2 265 ? 92.520  95.372  120.579 1.00 23.33 ?  244 GLU C C     1 
ATOM   12982 O  O     . GLU C 2 265 ? 91.895  96.413  120.370 1.00 22.86 ?  244 GLU C O     1 
ATOM   12983 C  CB    . GLU C 2 265 ? 91.828  93.246  119.474 1.00 24.31 ?  244 GLU C CB    1 
ATOM   12984 C  CG    . GLU C 2 265 ? 91.807  92.438  118.181 1.00 27.63 ?  244 GLU C CG    1 
ATOM   12985 C  CD    . GLU C 2 265 ? 90.796  91.296  118.220 1.00 33.27 ?  244 GLU C CD    1 
ATOM   12986 O  OE1   . GLU C 2 265 ? 89.765  91.424  118.918 1.00 35.56 ?  244 GLU C OE1   1 
ATOM   12987 O  OE2   . GLU C 2 265 ? 91.031  90.270  117.542 1.00 35.96 -1 244 GLU C OE2   1 
ATOM   12988 N  N     . ASP C 2 266 ? 92.975  95.027  121.774 1.00 23.36 ?  245 ASP C N     1 
ATOM   12989 C  CA    . ASP C 2 266 ? 92.772  95.870  122.940 1.00 24.18 ?  245 ASP C CA    1 
ATOM   12990 C  C     . ASP C 2 266 ? 93.353  97.284  122.747 1.00 23.96 ?  245 ASP C C     1 
ATOM   12991 O  O     . ASP C 2 266 ? 92.733  98.273  123.133 1.00 24.19 ?  245 ASP C O     1 
ATOM   12992 C  CB    . ASP C 2 266 ? 93.397  95.200  124.161 1.00 25.14 ?  245 ASP C CB    1 
ATOM   12993 C  CG    . ASP C 2 266 ? 93.020  95.878  125.442 1.00 27.35 ?  245 ASP C CG    1 
ATOM   12994 O  OD1   . ASP C 2 266 ? 91.807  96.012  125.708 1.00 28.45 ?  245 ASP C OD1   1 
ATOM   12995 O  OD2   . ASP C 2 266 ? 93.945  96.279  126.181 1.00 31.99 -1 245 ASP C OD2   1 
ATOM   12996 N  N     . LEU C 2 267 ? 94.528  97.375  122.136 1.00 23.34 ?  246 LEU C N     1 
ATOM   12997 C  CA    . LEU C 2 267 ? 95.183  98.671  121.931 1.00 23.53 ?  246 LEU C CA    1 
ATOM   12998 C  C     . LEU C 2 267 ? 94.721  99.429  120.696 1.00 22.94 ?  246 LEU C C     1 
ATOM   12999 O  O     . LEU C 2 267 ? 94.546  100.648 120.744 1.00 23.14 ?  246 LEU C O     1 
ATOM   13000 C  CB    . LEU C 2 267 ? 96.697  98.490  121.859 1.00 23.37 ?  246 LEU C CB    1 
ATOM   13001 C  CG    . LEU C 2 267 ? 97.426  98.147  123.160 1.00 26.17 ?  246 LEU C CG    1 
ATOM   13002 C  CD1   . LEU C 2 267 ? 98.905  98.037  122.863 1.00 27.31 ?  246 LEU C CD1   1 
ATOM   13003 C  CD2   . LEU C 2 267 ? 97.180  99.217  124.219 1.00 28.08 ?  246 LEU C CD2   1 
ATOM   13004 N  N     . TYR C 2 268 ? 94.550  98.711  119.590 1.00 22.46 ?  247 TYR C N     1 
ATOM   13005 C  CA    . TYR C 2 268 ? 94.347  99.355  118.295 1.00 22.00 ?  247 TYR C CA    1 
ATOM   13006 C  C     . TYR C 2 268 ? 92.919  99.535  117.809 1.00 22.26 ?  247 TYR C C     1 
ATOM   13007 O  O     . TYR C 2 268 ? 92.704  100.314 116.879 1.00 22.17 ?  247 TYR C O     1 
ATOM   13008 C  CB    . TYR C 2 268 ? 95.172  98.649  117.210 1.00 21.73 ?  247 TYR C CB    1 
ATOM   13009 C  CG    . TYR C 2 268 ? 96.657  98.888  117.334 1.00 21.49 ?  247 TYR C CG    1 
ATOM   13010 C  CD1   . TYR C 2 268 ? 97.492  97.924  117.909 1.00 19.45 ?  247 TYR C CD1   1 
ATOM   13011 C  CD2   . TYR C 2 268 ? 97.228  100.086 116.890 1.00 22.71 ?  247 TYR C CD2   1 
ATOM   13012 C  CE1   . TYR C 2 268 ? 98.866  98.148  118.034 1.00 20.30 ?  247 TYR C CE1   1 
ATOM   13013 C  CE2   . TYR C 2 268 ? 98.608  100.323 117.004 1.00 21.69 ?  247 TYR C CE2   1 
ATOM   13014 C  CZ    . TYR C 2 268 ? 99.415  99.343  117.563 1.00 21.40 ?  247 TYR C CZ    1 
ATOM   13015 O  OH    . TYR C 2 268 ? 100.763 99.570  117.667 1.00 22.11 ?  247 TYR C OH    1 
ATOM   13016 N  N     . ASP C 2 269 ? 91.949  98.819  118.388 1.00 22.40 ?  248 ASP C N     1 
ATOM   13017 C  CA    . ASP C 2 269 ? 90.549  98.994  117.962 1.00 22.75 ?  248 ASP C CA    1 
ATOM   13018 C  C     . ASP C 2 269 ? 90.098  100.452 118.062 1.00 22.55 ?  248 ASP C C     1 
ATOM   13019 O  O     . ASP C 2 269 ? 89.374  100.938 117.185 1.00 22.22 ?  248 ASP C O     1 
ATOM   13020 C  CB    . ASP C 2 269 ? 89.578  98.074  118.728 1.00 23.03 ?  248 ASP C CB    1 
ATOM   13021 C  CG    . ASP C 2 269 ? 89.548  96.657  118.180 1.00 25.02 ?  248 ASP C CG    1 
ATOM   13022 O  OD1   . ASP C 2 269 ? 90.108  96.398  117.094 1.00 26.85 ?  248 ASP C OD1   1 
ATOM   13023 O  OD2   . ASP C 2 269 ? 88.947  95.787  118.843 1.00 28.74 -1 248 ASP C OD2   1 
ATOM   13024 N  N     . GLN C 2 270 ? 90.536  101.148 119.114 1.00 22.21 ?  249 GLN C N     1 
ATOM   13025 C  CA    . GLN C 2 270 ? 90.141  102.562 119.310 1.00 22.39 ?  249 GLN C CA    1 
ATOM   13026 C  C     . GLN C 2 270 ? 90.745  103.539 118.291 1.00 21.65 ?  249 GLN C C     1 
ATOM   13027 O  O     . GLN C 2 270 ? 90.308  104.687 118.208 1.00 21.70 ?  249 GLN C O     1 
ATOM   13028 C  CB    . GLN C 2 270 ? 90.410  103.040 120.745 1.00 22.53 ?  249 GLN C CB    1 
ATOM   13029 C  CG    . GLN C 2 270 ? 91.892  103.020 121.198 1.00 22.73 ?  249 GLN C CG    1 
ATOM   13030 C  CD    . GLN C 2 270 ? 92.050  103.510 122.623 1.00 25.39 ?  249 GLN C CD    1 
ATOM   13031 O  OE1   . GLN C 2 270 ? 91.075  103.579 123.375 1.00 27.88 ?  249 GLN C OE1   1 
ATOM   13032 N  NE2   . GLN C 2 270 ? 93.274  103.863 123.006 1.00 24.88 ?  249 GLN C NE2   1 
ATOM   13033 N  N     . VAL C 2 271 ? 91.742  103.084 117.530 1.00 20.91 ?  250 VAL C N     1 
ATOM   13034 C  CA    . VAL C 2 271 ? 92.356  103.908 116.463 1.00 20.62 ?  250 VAL C CA    1 
ATOM   13035 C  C     . VAL C 2 271 ? 92.144  103.295 115.066 1.00 20.53 ?  250 VAL C C     1 
ATOM   13036 O  O     . VAL C 2 271 ? 92.615  103.837 114.053 1.00 20.05 ?  250 VAL C O     1 
ATOM   13037 C  CB    . VAL C 2 271 ? 93.871  104.241 116.734 1.00 20.32 ?  250 VAL C CB    1 
ATOM   13038 C  CG1   . VAL C 2 271 ? 94.023  105.106 117.981 1.00 20.35 ?  250 VAL C CG1   1 
ATOM   13039 C  CG2   . VAL C 2 271 ? 94.730  102.975 116.866 1.00 19.32 ?  250 VAL C CG2   1 
ATOM   13040 N  N     . GLY C 2 272 ? 91.422  102.173 115.028 1.00 20.29 ?  251 GLY C N     1 
ATOM   13041 C  CA    . GLY C 2 272 ? 90.970  101.566 113.773 1.00 20.51 ?  251 GLY C CA    1 
ATOM   13042 C  C     . GLY C 2 272 ? 92.007  100.765 113.002 1.00 20.99 ?  251 GLY C C     1 
ATOM   13043 O  O     . GLY C 2 272 ? 91.857  100.555 111.788 1.00 20.22 ?  251 GLY C O     1 
ATOM   13044 N  N     . LEU C 2 273 ? 93.059  100.315 113.693 1.00 20.76 ?  252 LEU C N     1 
ATOM   13045 C  CA    . LEU C 2 273 ? 94.219  99.747  112.997 1.00 21.38 ?  252 LEU C CA    1 
ATOM   13046 C  C     . LEU C 2 273 ? 94.528  98.281  113.287 1.00 21.86 ?  252 LEU C C     1 
ATOM   13047 O  O     . LEU C 2 273 ? 95.540  97.762  112.818 1.00 22.45 ?  252 LEU C O     1 
ATOM   13048 C  CB    . LEU C 2 273 ? 95.470  100.611 113.231 1.00 21.44 ?  252 LEU C CB    1 
ATOM   13049 C  CG    . LEU C 2 273 ? 95.434  102.084 112.819 1.00 22.02 ?  252 LEU C CG    1 
ATOM   13050 C  CD1   . LEU C 2 273 ? 96.745  102.756 113.213 1.00 22.86 ?  252 LEU C CD1   1 
ATOM   13051 C  CD2   . LEU C 2 273 ? 95.164  102.238 111.306 1.00 23.88 ?  252 LEU C CD2   1 
ATOM   13052 N  N     . SER C 2 274 ? 93.658  97.602  114.032 1.00 22.19 ?  253 SER C N     1 
ATOM   13053 C  CA    . SER C 2 274 ? 93.982  96.275  114.549 1.00 22.47 ?  253 SER C CA    1 
ATOM   13054 C  C     . SER C 2 274 ? 94.330  95.265  113.455 1.00 22.94 ?  253 SER C C     1 
ATOM   13055 O  O     . SER C 2 274 ? 95.310  94.537  113.572 1.00 22.07 ?  253 SER C O     1 
ATOM   13056 C  CB    . SER C 2 274 ? 92.839  95.744  115.420 1.00 22.91 ?  253 SER C CB    1 
ATOM   13057 O  OG    . SER C 2 274 ? 92.749  96.509  116.605 1.00 24.25 ?  253 SER C OG    1 
ATOM   13058 N  N     . HIS C 2 275 ? 93.545  95.255  112.380 1.00 24.59 ?  254 HIS C N     1 
ATOM   13059 C  CA    . HIS C 2 275 ? 93.764  94.314  111.275 1.00 25.66 ?  254 HIS C CA    1 
ATOM   13060 C  C     . HIS C 2 275 ? 95.117  94.545  110.583 1.00 26.01 ?  254 HIS C C     1 
ATOM   13061 O  O     . HIS C 2 275 ? 95.823  93.587  110.222 1.00 26.23 ?  254 HIS C O     1 
ATOM   13062 C  CB    . HIS C 2 275 ? 92.614  94.407  110.264 1.00 26.89 ?  254 HIS C CB    1 
ATOM   13063 C  CG    . HIS C 2 275 ? 92.706  93.408  109.152 1.00 29.10 ?  254 HIS C CG    1 
ATOM   13064 N  ND1   . HIS C 2 275 ? 92.827  92.052  109.377 1.00 32.70 ?  254 HIS C ND1   1 
ATOM   13065 C  CD2   . HIS C 2 275 ? 92.692  93.566  107.808 1.00 31.68 ?  254 HIS C CD2   1 
ATOM   13066 C  CE1   . HIS C 2 275 ? 92.887  91.420  108.219 1.00 33.55 ?  254 HIS C CE1   1 
ATOM   13067 N  NE2   . HIS C 2 275 ? 92.792  92.313  107.252 1.00 33.71 ?  254 HIS C NE2   1 
ATOM   13068 N  N     . ASP C 2 276 ? 95.464  95.814  110.401 1.00 25.93 ?  255 ASP C N     1 
ATOM   13069 C  CA    . ASP C 2 276 ? 96.739  96.202  109.808 1.00 26.65 ?  255 ASP C CA    1 
ATOM   13070 C  C     . ASP C 2 276 ? 97.931  95.757  110.657 1.00 25.61 ?  255 ASP C C     1 
ATOM   13071 O  O     . ASP C 2 276 ? 98.902  95.202  110.125 1.00 25.34 ?  255 ASP C O     1 
ATOM   13072 C  CB    . ASP C 2 276 ? 96.788  97.713  109.579 1.00 27.44 ?  255 ASP C CB    1 
ATOM   13073 C  CG    . ASP C 2 276 ? 96.806  98.075  108.111 1.00 32.09 ?  255 ASP C CG    1 
ATOM   13074 O  OD1   . ASP C 2 276 ? 97.565  97.427  107.349 1.00 36.67 ?  255 ASP C OD1   1 
ATOM   13075 O  OD2   . ASP C 2 276 ? 96.055  98.995  107.710 1.00 36.30 -1 255 ASP C OD2   1 
ATOM   13076 N  N     . VAL C 2 277 ? 97.847  96.005  111.969 1.00 24.17 ?  256 VAL C N     1 
ATOM   13077 C  CA    . VAL C 2 277 ? 98.897  95.596  112.910 1.00 23.71 ?  256 VAL C CA    1 
ATOM   13078 C  C     . VAL C 2 277 ? 99.060  94.073  112.919 1.00 23.48 ?  256 VAL C C     1 
ATOM   13079 O  O     . VAL C 2 277 ? 100.182 93.567  112.947 1.00 23.08 ?  256 VAL C O     1 
ATOM   13080 C  CB    . VAL C 2 277 ? 98.627  96.095  114.357 1.00 23.27 ?  256 VAL C CB    1 
ATOM   13081 C  CG1   . VAL C 2 277 ? 99.745  95.652  115.307 1.00 24.02 ?  256 VAL C CG1   1 
ATOM   13082 C  CG2   . VAL C 2 277 ? 98.479  97.611  114.394 1.00 23.35 ?  256 VAL C CG2   1 
ATOM   13083 N  N     . LYS C 2 278 ? 97.942  93.352  112.893 1.00 23.36 ?  257 LYS C N     1 
ATOM   13084 C  CA    . LYS C 2 278 ? 97.967  91.890  112.846 1.00 24.12 ?  257 LYS C CA    1 
ATOM   13085 C  C     . LYS C 2 278 ? 98.757  91.352  111.655 1.00 24.30 ?  257 LYS C C     1 
ATOM   13086 O  O     . LYS C 2 278 ? 99.518  90.383  111.790 1.00 24.37 ?  257 LYS C O     1 
ATOM   13087 C  CB    . LYS C 2 278 ? 96.552  91.314  112.846 1.00 24.22 ?  257 LYS C CB    1 
ATOM   13088 C  CG    . LYS C 2 278 ? 95.852  91.394  114.192 1.00 24.96 ?  257 LYS C CG    1 
ATOM   13089 C  CD    . LYS C 2 278 ? 94.409  90.932  114.044 1.00 26.34 ?  257 LYS C CD    1 
ATOM   13090 C  CE    . LYS C 2 278 ? 93.660  91.033  115.344 1.00 27.16 ?  257 LYS C CE    1 
ATOM   13091 N  NZ    . LYS C 2 278 ? 92.259  90.558  115.132 1.00 29.60 1  257 LYS C NZ    1 
ATOM   13092 N  N     . LYS C 2 279 ? 98.584  91.978  110.493 1.00 24.55 ?  258 LYS C N     1 
ATOM   13093 C  CA    . LYS C 2 279 ? 99.359  91.603  109.314 1.00 24.85 ?  258 LYS C CA    1 
ATOM   13094 C  C     . LYS C 2 279 ? 100.849 91.832  109.559 1.00 24.57 ?  258 LYS C C     1 
ATOM   13095 O  O     . LYS C 2 279 ? 101.675 91.007  109.172 1.00 24.07 ?  258 LYS C O     1 
ATOM   13096 C  CB    . LYS C 2 279 ? 98.901  92.395  108.089 1.00 25.30 ?  258 LYS C CB    1 
ATOM   13097 C  CG    . LYS C 2 279 ? 97.457  92.160  107.707 1.00 26.63 ?  258 LYS C CG    1 
ATOM   13098 C  CD    . LYS C 2 279 ? 97.111  93.000  106.484 1.00 29.30 ?  258 LYS C CD    1 
ATOM   13099 C  CE    . LYS C 2 279 ? 95.736  92.674  105.985 1.00 31.79 ?  258 LYS C CE    1 
ATOM   13100 N  NZ    . LYS C 2 279 ? 95.295  93.725  105.035 1.00 33.80 1  258 LYS C NZ    1 
ATOM   13101 N  N     . PHE C 2 280 ? 101.172 92.939  110.229 1.00 24.29 ?  259 PHE C N     1 
ATOM   13102 C  CA    . PHE C 2 280 ? 102.562 93.307  110.533 1.00 24.90 ?  259 PHE C CA    1 
ATOM   13103 C  C     . PHE C 2 280 ? 103.236 92.306  111.488 1.00 24.86 ?  259 PHE C C     1 
ATOM   13104 O  O     . PHE C 2 280 ? 104.389 91.914  111.277 1.00 24.68 ?  259 PHE C O     1 
ATOM   13105 C  CB    . PHE C 2 280 ? 102.599 94.737  111.090 1.00 24.70 ?  259 PHE C CB    1 
ATOM   13106 C  CG    . PHE C 2 280 ? 103.982 95.331  111.223 1.00 25.70 ?  259 PHE C CG    1 
ATOM   13107 C  CD1   . PHE C 2 280 ? 104.818 95.462  110.113 1.00 26.86 ?  259 PHE C CD1   1 
ATOM   13108 C  CD2   . PHE C 2 280 ? 104.431 95.805  112.462 1.00 26.19 ?  259 PHE C CD2   1 
ATOM   13109 C  CE1   . PHE C 2 280 ? 106.092 96.036  110.234 1.00 26.66 ?  259 PHE C CE1   1 
ATOM   13110 C  CE2   . PHE C 2 280 ? 105.696 96.386  112.590 1.00 26.52 ?  259 PHE C CE2   1 
ATOM   13111 C  CZ    . PHE C 2 280 ? 106.532 96.496  111.471 1.00 26.23 ?  259 PHE C CZ    1 
ATOM   13112 N  N     . ILE C 2 281 ? 102.515 91.887  112.529 1.00 25.53 ?  260 ILE C N     1 
ATOM   13113 C  CA    . ILE C 2 281 ? 103.077 90.938  113.492 1.00 26.21 ?  260 ILE C CA    1 
ATOM   13114 C  C     . ILE C 2 281 ? 103.282 89.546  112.879 1.00 26.47 ?  260 ILE C C     1 
ATOM   13115 O  O     . ILE C 2 281 ? 104.243 88.862  113.218 1.00 26.52 ?  260 ILE C O     1 
ATOM   13116 C  CB    . ILE C 2 281 ? 102.307 90.896  114.858 1.00 26.27 ?  260 ILE C CB    1 
ATOM   13117 C  CG1   . ILE C 2 281 ? 101.014 90.083  114.763 1.00 27.37 ?  260 ILE C CG1   1 
ATOM   13118 C  CG2   . ILE C 2 281 ? 102.071 92.326  115.391 1.00 26.92 ?  260 ILE C CG2   1 
ATOM   13119 C  CD1   . ILE C 2 281 ? 100.257 89.948  116.084 1.00 29.51 ?  260 ILE C CD1   1 
ATOM   13120 N  N     . ARG C 2 282 ? 102.409 89.154  111.949 1.00 26.57 ?  261 ARG C N     1 
ATOM   13121 C  CA    . ARG C 2 282 ? 102.579 87.888  111.230 1.00 26.84 ?  261 ARG C CA    1 
ATOM   13122 C  C     . ARG C 2 282 ? 103.822 87.929  110.341 1.00 27.34 ?  261 ARG C C     1 
ATOM   13123 O  O     . ARG C 2 282 ? 104.600 86.980  110.314 1.00 27.54 ?  261 ARG C O     1 
ATOM   13124 C  CB    . ARG C 2 282 ? 101.334 87.530  110.414 1.00 26.98 ?  261 ARG C CB    1 
ATOM   13125 C  CG    . ARG C 2 282 ? 100.203 86.933  111.228 1.00 26.53 ?  261 ARG C CG    1 
ATOM   13126 C  CD    . ARG C 2 282 ? 99.106  86.331  110.326 1.00 27.77 ?  261 ARG C CD    1 
ATOM   13127 N  NE    . ARG C 2 282 ? 98.344  87.348  109.606 1.00 28.67 ?  261 ARG C NE    1 
ATOM   13128 C  CZ    . ARG C 2 282 ? 97.285  87.993  110.101 1.00 29.68 ?  261 ARG C CZ    1 
ATOM   13129 N  NH1   . ARG C 2 282 ? 96.843  87.736  111.331 1.00 28.31 1  261 ARG C NH1   1 
ATOM   13130 N  NH2   . ARG C 2 282 ? 96.659  88.894  109.361 1.00 29.15 ?  261 ARG C NH2   1 
ATOM   13131 N  N     . TYR C 2 283 ? 103.997 89.043  109.633 1.00 27.78 ?  262 TYR C N     1 
ATOM   13132 C  CA    . TYR C 2 283 ? 105.198 89.311  108.843 1.00 28.18 ?  262 TYR C CA    1 
ATOM   13133 C  C     . TYR C 2 283 ? 106.472 89.133  109.689 1.00 27.08 ?  262 TYR C C     1 
ATOM   13134 O  O     . TYR C 2 283 ? 107.415 88.427  109.297 1.00 26.51 ?  262 TYR C O     1 
ATOM   13135 C  CB    . TYR C 2 283 ? 105.125 90.736  108.280 1.00 29.11 ?  262 TYR C CB    1 
ATOM   13136 C  CG    . TYR C 2 283 ? 106.299 91.140  107.422 1.00 32.56 ?  262 TYR C CG    1 
ATOM   13137 C  CD1   . TYR C 2 283 ? 106.427 90.664  106.116 1.00 36.59 ?  262 TYR C CD1   1 
ATOM   13138 C  CD2   . TYR C 2 283 ? 107.277 92.014  107.908 1.00 36.34 ?  262 TYR C CD2   1 
ATOM   13139 C  CE1   . TYR C 2 283 ? 107.508 91.037  105.311 1.00 39.47 ?  262 TYR C CE1   1 
ATOM   13140 C  CE2   . TYR C 2 283 ? 108.366 92.400  107.104 1.00 39.23 ?  262 TYR C CE2   1 
ATOM   13141 C  CZ    . TYR C 2 283 ? 108.470 91.903  105.809 1.00 40.48 ?  262 TYR C CZ    1 
ATOM   13142 O  OH    . TYR C 2 283 ? 109.530 92.263  105.008 1.00 44.00 ?  262 TYR C OH    1 
ATOM   13143 N  N     . ASN C 2 284 ? 106.481 89.755  110.860 1.00 26.08 ?  263 ASN C N     1 
ATOM   13144 C  CA    . ASN C 2 284 ? 107.632 89.670  111.745 1.00 25.73 ?  263 ASN C CA    1 
ATOM   13145 C  C     . ASN C 2 284 ? 107.806 88.322  112.448 1.00 25.24 ?  263 ASN C C     1 
ATOM   13146 O  O     . ASN C 2 284 ? 108.944 87.902  112.698 1.00 25.56 ?  263 ASN C O     1 
ATOM   13147 C  CB    . ASN C 2 284 ? 107.644 90.852  112.715 1.00 25.69 ?  263 ASN C CB    1 
ATOM   13148 C  CG    . ASN C 2 284 ? 108.065 92.136  112.035 1.00 26.39 ?  263 ASN C CG    1 
ATOM   13149 O  OD1   . ASN C 2 284 ? 109.248 92.343  111.755 1.00 26.91 ?  263 ASN C OD1   1 
ATOM   13150 N  ND2   . ASN C 2 284 ? 107.102 93.002  111.755 1.00 27.56 ?  263 ASN C ND2   1 
ATOM   13151 N  N     . ALA C 2 285 ? 106.701 87.630  112.738 1.00 24.51 ?  264 ALA C N     1 
ATOM   13152 C  CA    . ALA C 2 285 ? 106.779 86.231  113.200 1.00 24.19 ?  264 ALA C CA    1 
ATOM   13153 C  C     . ALA C 2 285 ? 107.586 85.345  112.230 1.00 24.63 ?  264 ALA C C     1 
ATOM   13154 O  O     . ALA C 2 285 ? 108.408 84.537  112.657 1.00 24.01 ?  264 ALA C O     1 
ATOM   13155 C  CB    . ALA C 2 285 ? 105.396 85.644  113.412 1.00 23.63 ?  264 ALA C CB    1 
ATOM   13156 N  N     . ASN C 2 286 ? 107.345 85.507  110.929 1.00 24.66 ?  265 ASN C N     1 
ATOM   13157 C  CA    . ASN C 2 286 ? 108.116 84.797  109.908 1.00 25.24 ?  265 ASN C CA    1 
ATOM   13158 C  C     . ASN C 2 286 ? 109.609 85.106  109.932 1.00 25.09 ?  265 ASN C C     1 
ATOM   13159 O  O     . ASN C 2 286 ? 110.430 84.208  109.682 1.00 24.14 ?  265 ASN C O     1 
ATOM   13160 C  CB    . ASN C 2 286 ? 107.551 85.057  108.499 1.00 25.62 ?  265 ASN C CB    1 
ATOM   13161 C  CG    . ASN C 2 286 ? 106.253 84.307  108.247 1.00 26.46 ?  265 ASN C CG    1 
ATOM   13162 O  OD1   . ASN C 2 286 ? 105.870 83.422  109.016 1.00 27.14 ?  265 ASN C OD1   1 
ATOM   13163 N  ND2   . ASN C 2 286 ? 105.555 84.674  107.169 1.00 27.89 ?  265 ASN C ND2   1 
ATOM   13164 N  N     . LYS C 2 287 ? 109.946 86.368  110.213 1.00 24.99 ?  266 LYS C N     1 
ATOM   13165 C  CA    . LYS C 2 287 ? 111.335 86.808  110.359 1.00 25.91 ?  266 LYS C CA    1 
ATOM   13166 C  C     . LYS C 2 287 ? 111.982 86.182  111.590 1.00 25.23 ?  266 LYS C C     1 
ATOM   13167 O  O     . LYS C 2 287 ? 113.152 85.795  111.548 1.00 25.34 ?  266 LYS C O     1 
ATOM   13168 C  CB    . LYS C 2 287 ? 111.432 88.329  110.479 1.00 25.96 ?  266 LYS C CB    1 
ATOM   13169 C  CG    . LYS C 2 287 ? 111.225 89.111  109.192 1.00 29.60 ?  266 LYS C CG    1 
ATOM   13170 C  CD    . LYS C 2 287 ? 111.615 90.575  109.435 1.00 34.20 ?  266 LYS C CD    1 
ATOM   13171 C  CE    . LYS C 2 287 ? 111.536 91.410  108.182 1.00 37.67 ?  266 LYS C CE    1 
ATOM   13172 N  NZ    . LYS C 2 287 ? 112.062 92.789  108.450 1.00 39.48 1  266 LYS C NZ    1 
ATOM   13173 N  N     . ALA C 2 288 ? 111.229 86.098  112.683 1.00 24.87 ?  267 ALA C N     1 
ATOM   13174 C  CA    . ALA C 2 288 ? 111.704 85.406  113.896 1.00 24.23 ?  267 ALA C CA    1 
ATOM   13175 C  C     . ALA C 2 288 ? 111.987 83.924  113.620 1.00 24.24 ?  267 ALA C C     1 
ATOM   13176 O  O     . ALA C 2 288 ? 113.038 83.406  114.002 1.00 23.96 ?  267 ALA C O     1 
ATOM   13177 C  CB    . ALA C 2 288 ? 110.704 85.556  115.027 1.00 24.23 ?  267 ALA C CB    1 
ATOM   13178 N  N     . LEU C 2 289 ? 111.054 83.245  112.953 1.00 24.63 ?  268 LEU C N     1 
ATOM   13179 C  CA    . LEU C 2 289 ? 111.267 81.847  112.568 1.00 25.14 ?  268 LEU C CA    1 
ATOM   13180 C  C     . LEU C 2 289 ? 112.511 81.712  111.705 1.00 25.58 ?  268 LEU C C     1 
ATOM   13181 O  O     . LEU C 2 289 ? 113.323 80.819  111.921 1.00 25.42 ?  268 LEU C O     1 
ATOM   13182 C  CB    . LEU C 2 289 ? 110.045 81.259  111.846 1.00 25.28 ?  268 LEU C CB    1 
ATOM   13183 C  CG    . LEU C 2 289 ? 108.841 80.951  112.741 1.00 25.93 ?  268 LEU C CG    1 
ATOM   13184 C  CD1   . LEU C 2 289 ? 107.575 80.817  111.918 1.00 26.50 ?  268 LEU C CD1   1 
ATOM   13185 C  CD2   . LEU C 2 289 ? 109.068 79.713  113.628 1.00 25.20 ?  268 LEU C CD2   1 
ATOM   13186 N  N     . MET C 2 290 ? 112.672 82.615  110.737 1.00 26.32 ?  269 MET C N     1 
ATOM   13187 C  CA    . MET C 2 290 ? 113.848 82.568  109.873 1.00 27.41 ?  269 MET C CA    1 
ATOM   13188 C  C     . MET C 2 290 ? 115.154 82.782  110.635 1.00 26.66 ?  269 MET C C     1 
ATOM   13189 O  O     . MET C 2 290 ? 116.152 82.118  110.343 1.00 26.69 ?  269 MET C O     1 
ATOM   13190 C  CB    . MET C 2 290 ? 113.707 83.525  108.694 1.00 28.28 ?  269 MET C CB    1 
ATOM   13191 C  CG    . MET C 2 290 ? 113.064 82.838  107.490 1.00 32.91 ?  269 MET C CG    1 
ATOM   13192 S  SD    . MET C 2 290 ? 112.567 83.989  106.205 1.00 42.49 ?  269 MET C SD    1 
ATOM   13193 C  CE    . MET C 2 290 ? 110.786 83.984  106.408 1.00 38.74 ?  269 MET C CE    1 
ATOM   13194 N  N     . ASN C 2 291 ? 115.134 83.673  111.627 1.00 25.48 ?  270 ASN C N     1 
ATOM   13195 C  CA    . ASN C 2 291 ? 116.291 83.893  112.510 1.00 25.39 ?  270 ASN C CA    1 
ATOM   13196 C  C     . ASN C 2 291 ? 116.691 82.618  113.271 1.00 25.18 ?  270 ASN C C     1 
ATOM   13197 O  O     . ASN C 2 291 ? 117.861 82.438  113.640 1.00 24.73 ?  270 ASN C O     1 
ATOM   13198 C  CB    . ASN C 2 291 ? 116.015 85.039  113.493 1.00 24.83 ?  270 ASN C CB    1 
ATOM   13199 C  CG    . ASN C 2 291 ? 116.088 86.420  112.831 1.00 25.58 ?  270 ASN C CG    1 
ATOM   13200 O  OD1   . ASN C 2 291 ? 116.571 86.564  111.712 1.00 25.58 ?  270 ASN C OD1   1 
ATOM   13201 N  ND2   . ASN C 2 291 ? 115.605 87.434  113.531 1.00 24.32 ?  270 ASN C ND2   1 
ATOM   13202 N  N     . LEU C 2 292 ? 115.706 81.737  113.467 1.00 25.09 ?  271 LEU C N     1 
ATOM   13203 C  CA    . LEU C 2 292 ? 115.890 80.427  114.106 1.00 25.46 ?  271 LEU C CA    1 
ATOM   13204 C  C     . LEU C 2 292 ? 116.186 79.279  113.126 1.00 26.18 ?  271 LEU C C     1 
ATOM   13205 O  O     . LEU C 2 292 ? 116.336 78.113  113.535 1.00 26.06 ?  271 LEU C O     1 
ATOM   13206 C  CB    . LEU C 2 292 ? 114.664 80.099  114.968 1.00 25.19 ?  271 LEU C CB    1 
ATOM   13207 C  CG    . LEU C 2 292 ? 114.443 81.016  116.183 1.00 25.03 ?  271 LEU C CG    1 
ATOM   13208 C  CD1   . LEU C 2 292 ? 113.068 80.796  116.772 1.00 24.50 ?  271 LEU C CD1   1 
ATOM   13209 C  CD2   . LEU C 2 292 ? 115.537 80.784  117.238 1.00 25.64 ?  271 LEU C CD2   1 
ATOM   13210 N  N     . GLY C 2 293 ? 116.275 79.608  111.838 1.00 26.71 ?  272 GLY C N     1 
ATOM   13211 C  CA    . GLY C 2 293 ? 116.536 78.609  110.794 1.00 28.06 ?  272 GLY C CA    1 
ATOM   13212 C  C     . GLY C 2 293 ? 115.332 77.773  110.388 1.00 29.34 ?  272 GLY C C     1 
ATOM   13213 O  O     . GLY C 2 293 ? 115.487 76.670  109.843 1.00 29.73 ?  272 GLY C O     1 
ATOM   13214 N  N     . PHE C 2 294 ? 114.133 78.291  110.649 1.00 29.88 ?  273 PHE C N     1 
ATOM   13215 C  CA    . PHE C 2 294 ? 112.890 77.597  110.322 1.00 31.24 ?  273 PHE C CA    1 
ATOM   13216 C  C     . PHE C 2 294 ? 112.167 78.275  109.150 1.00 32.42 ?  273 PHE C C     1 
ATOM   13217 O  O     . PHE C 2 294 ? 112.386 79.463  108.871 1.00 32.30 ?  273 PHE C O     1 
ATOM   13218 C  CB    . PHE C 2 294 ? 111.968 77.519  111.546 1.00 30.82 ?  273 PHE C CB    1 
ATOM   13219 C  CG    . PHE C 2 294 ? 112.560 76.769  112.721 1.00 30.93 ?  273 PHE C CG    1 
ATOM   13220 C  CD1   . PHE C 2 294 ? 113.154 75.519  112.554 1.00 30.85 ?  273 PHE C CD1   1 
ATOM   13221 C  CD2   . PHE C 2 294 ? 112.508 77.312  113.997 1.00 30.30 ?  273 PHE C CD2   1 
ATOM   13222 C  CE1   . PHE C 2 294 ? 113.702 74.836  113.638 1.00 30.75 ?  273 PHE C CE1   1 
ATOM   13223 C  CE2   . PHE C 2 294 ? 113.039 76.631  115.095 1.00 30.41 ?  273 PHE C CE2   1 
ATOM   13224 C  CZ    . PHE C 2 294 ? 113.633 75.388  114.916 1.00 30.88 ?  273 PHE C CZ    1 
ATOM   13225 N  N     . ASP C 2 295 ? 111.324 77.508  108.464 1.00 33.81 ?  274 ASP C N     1 
ATOM   13226 C  CA    . ASP C 2 295 ? 110.505 78.020  107.361 1.00 35.32 ?  274 ASP C CA    1 
ATOM   13227 C  C     . ASP C 2 295 ? 109.420 78.990  107.862 1.00 35.36 ?  274 ASP C C     1 
ATOM   13228 O  O     . ASP C 2 295 ? 108.923 78.831  108.974 1.00 34.78 ?  274 ASP C O     1 
ATOM   13229 C  CB    . ASP C 2 295 ? 109.830 76.857  106.620 1.00 35.95 ?  274 ASP C CB    1 
ATOM   13230 C  CG    . ASP C 2 295 ? 110.827 75.919  105.945 1.00 37.98 ?  274 ASP C CG    1 
ATOM   13231 O  OD1   . ASP C 2 295 ? 111.940 76.356  105.580 1.00 39.83 ?  274 ASP C OD1   1 
ATOM   13232 O  OD2   . ASP C 2 295 ? 110.483 74.729  105.776 1.00 40.03 -1 274 ASP C OD2   1 
ATOM   13233 N  N     . PRO C 2 296 ? 109.045 79.988  107.039 1.00 36.33 ?  275 PRO C N     1 
ATOM   13234 C  CA    . PRO C 2 296 ? 107.920 80.881  107.396 1.00 36.92 ?  275 PRO C CA    1 
ATOM   13235 C  C     . PRO C 2 296 ? 106.617 80.113  107.670 1.00 37.68 ?  275 PRO C C     1 
ATOM   13236 O  O     . PRO C 2 296 ? 106.348 79.100  107.019 1.00 38.07 ?  275 PRO C O     1 
ATOM   13237 C  CB    . PRO C 2 296 ? 107.768 81.778  106.158 1.00 36.82 ?  275 PRO C CB    1 
ATOM   13238 C  CG    . PRO C 2 296 ? 108.590 81.111  105.064 1.00 37.42 ?  275 PRO C CG    1 
ATOM   13239 C  CD    . PRO C 2 296 ? 109.689 80.393  105.776 1.00 36.41 ?  275 PRO C CD    1 
ATOM   13240 N  N     . TYR C 2 297 ? 105.825 80.597  108.628 1.00 38.10 ?  276 TYR C N     1 
ATOM   13241 C  CA    . TYR C 2 297 ? 104.616 79.899  109.091 1.00 38.96 ?  276 TYR C CA    1 
ATOM   13242 C  C     . TYR C 2 297 ? 103.322 80.571  108.617 1.00 39.71 ?  276 TYR C C     1 
ATOM   13243 O  O     . TYR C 2 297 ? 102.293 79.907  108.452 1.00 40.18 ?  276 TYR C O     1 
ATOM   13244 C  CB    . TYR C 2 297 ? 104.635 79.823  110.621 1.00 38.94 ?  276 TYR C CB    1 
ATOM   13245 C  CG    . TYR C 2 297 ? 103.524 79.046  111.294 1.00 39.64 ?  276 TYR C CG    1 
ATOM   13246 C  CD1   . TYR C 2 297 ? 103.583 77.655  111.412 1.00 40.43 ?  276 TYR C CD1   1 
ATOM   13247 C  CD2   . TYR C 2 297 ? 102.443 79.706  111.872 1.00 41.04 ?  276 TYR C CD2   1 
ATOM   13248 C  CE1   . TYR C 2 297 ? 102.568 76.941  112.052 1.00 41.69 ?  276 TYR C CE1   1 
ATOM   13249 C  CE2   . TYR C 2 297 ? 101.421 79.004  112.512 1.00 41.60 ?  276 TYR C CE2   1 
ATOM   13250 C  CZ    . TYR C 2 297 ? 101.493 77.624  112.603 1.00 41.92 ?  276 TYR C CZ    1 
ATOM   13251 O  OH    . TYR C 2 297 ? 100.486 76.936  113.245 1.00 42.52 ?  276 TYR C OH    1 
ATOM   13252 N  N     . PHE C 2 298 ? 103.369 81.883  108.413 1.00 39.85 ?  277 PHE C N     1 
ATOM   13253 C  CA    . PHE C 2 298 ? 102.191 82.625  107.978 1.00 40.77 ?  277 PHE C CA    1 
ATOM   13254 C  C     . PHE C 2 298 ? 102.312 83.009  106.511 1.00 41.95 ?  277 PHE C C     1 
ATOM   13255 O  O     . PHE C 2 298 ? 103.418 83.224  106.016 1.00 41.91 ?  277 PHE C O     1 
ATOM   13256 C  CB    . PHE C 2 298 ? 101.999 83.879  108.838 1.00 39.94 ?  277 PHE C CB    1 
ATOM   13257 C  CG    . PHE C 2 298 ? 101.732 83.589  110.290 1.00 39.09 ?  277 PHE C CG    1 
ATOM   13258 C  CD1   . PHE C 2 298 ? 102.713 83.814  111.248 1.00 37.84 ?  277 PHE C CD1   1 
ATOM   13259 C  CD2   . PHE C 2 298 ? 100.492 83.105  110.702 1.00 38.97 ?  277 PHE C CD2   1 
ATOM   13260 C  CE1   . PHE C 2 298 ? 102.473 83.555  112.595 1.00 37.46 ?  277 PHE C CE1   1 
ATOM   13261 C  CE2   . PHE C 2 298 ? 100.240 82.842  112.043 1.00 38.20 ?  277 PHE C CE2   1 
ATOM   13262 C  CZ    . PHE C 2 298 ? 101.233 83.068  112.994 1.00 37.91 ?  277 PHE C CZ    1 
ATOM   13263 N  N     . GLU C 2 299 ? 101.182 83.092  105.809 1.00 43.74 ?  278 GLU C N     1 
ATOM   13264 C  CA    . GLU C 2 299 ? 101.204 83.503  104.401 1.00 45.61 ?  278 GLU C CA    1 
ATOM   13265 C  C     . GLU C 2 299 ? 101.498 84.999  104.282 1.00 46.04 ?  278 GLU C C     1 
ATOM   13266 O  O     . GLU C 2 299 ? 101.150 85.781  105.166 1.00 45.88 ?  278 GLU C O     1 
ATOM   13267 C  CB    . GLU C 2 299 ? 99.895  83.156  103.685 1.00 46.43 ?  278 GLU C CB    1 
ATOM   13268 C  CG    . GLU C 2 299 ? 100.081 82.856  102.187 1.00 48.82 ?  278 GLU C CG    1 
ATOM   13269 C  CD    . GLU C 2 299 ? 98.804  83.002  101.375 1.00 51.86 ?  278 GLU C CD    1 
ATOM   13270 O  OE1   . GLU C 2 299 ? 98.863  82.793  100.142 1.00 53.35 ?  278 GLU C OE1   1 
ATOM   13271 O  OE2   . GLU C 2 299 ? 97.742  83.329  101.955 1.00 53.10 -1 278 GLU C OE2   1 
ATOM   13272 N  N     . GLU C 2 300 ? 102.153 85.380  103.187 1.00 47.16 ?  279 GLU C N     1 
ATOM   13273 C  CA    . GLU C 2 300 ? 102.493 86.781  102.913 1.00 47.75 ?  279 GLU C CA    1 
ATOM   13274 C  C     . GLU C 2 300 ? 101.251 87.657  102.688 1.00 47.71 ?  279 GLU C C     1 
ATOM   13275 O  O     . GLU C 2 300 ? 100.277 87.219  102.064 1.00 47.77 ?  279 GLU C O     1 
ATOM   13276 C  CB    . GLU C 2 300 ? 103.458 86.874  101.718 1.00 48.42 ?  279 GLU C CB    1 
ATOM   13277 C  CG    . GLU C 2 300 ? 103.009 86.107  100.468 1.00 50.63 ?  279 GLU C CG    1 
ATOM   13278 C  CD    . GLU C 2 300 ? 104.165 85.746  99.536  1.00 53.06 ?  279 GLU C CD    1 
ATOM   13279 O  OE1   . GLU C 2 300 ? 104.930 86.657  99.137  1.00 54.35 ?  279 GLU C OE1   1 
ATOM   13280 O  OE2   . GLU C 2 300 ? 104.300 84.549  99.193  1.00 53.32 -1 279 GLU C OE2   1 
ATOM   13281 N  N     . GLU C 2 301 ? 101.296 88.879  103.219 1.00 47.40 ?  280 GLU C N     1 
ATOM   13282 C  CA    . GLU C 2 301 ? 100.216 89.864  103.074 1.00 47.46 ?  280 GLU C CA    1 
ATOM   13283 C  C     . GLU C 2 301 ? 100.794 91.259  102.806 1.00 47.31 ?  280 GLU C C     1 
ATOM   13284 O  O     . GLU C 2 301 ? 101.946 91.533  103.153 1.00 47.21 ?  280 GLU C O     1 
ATOM   13285 C  CB    . GLU C 2 301 ? 99.348  89.914  104.339 1.00 47.19 ?  280 GLU C CB    1 
ATOM   13286 C  CG    . GLU C 2 301 ? 98.634  88.614  104.711 1.00 47.14 ?  280 GLU C CG    1 
ATOM   13287 C  CD    . GLU C 2 301 ? 98.232  88.571  106.183 1.00 47.21 ?  280 GLU C CD    1 
ATOM   13288 O  OE1   . GLU C 2 301 ? 97.026  88.707  106.473 1.00 46.97 ?  280 GLU C OE1   1 
ATOM   13289 O  OE2   . GLU C 2 301 ? 99.125  88.412  107.051 1.00 46.13 -1 280 GLU C OE2   1 
ATOM   13290 N  N     . ASP C 2 302 ? 99.995  92.135  102.195 1.00 47.15 ?  281 ASP C N     1 
ATOM   13291 C  CA    . ASP C 2 302 ? 100.417 93.517  101.944 1.00 47.04 ?  281 ASP C CA    1 
ATOM   13292 C  C     . ASP C 2 302 ? 100.385 94.338  103.237 1.00 46.05 ?  281 ASP C C     1 
ATOM   13293 O  O     . ASP C 2 302 ? 99.327  94.497  103.855 1.00 46.10 ?  281 ASP C O     1 
ATOM   13294 C  CB    . ASP C 2 302 ? 99.534  94.187  100.874 1.00 47.66 ?  281 ASP C CB    1 
ATOM   13295 C  CG    . ASP C 2 302 ? 99.810  93.675  99.458  1.00 49.53 ?  281 ASP C CG    1 
ATOM   13296 O  OD1   . ASP C 2 302 ? 100.975 93.350  99.137  1.00 50.58 ?  281 ASP C OD1   1 
ATOM   13297 O  OD2   . ASP C 2 302 ? 98.850  93.622  98.651  1.00 51.14 -1 281 ASP C OD2   1 
ATOM   13298 N  N     . ILE C 2 303 ? 101.549 94.840  103.642 1.00 44.96 ?  282 ILE C N     1 
ATOM   13299 C  CA    . ILE C 2 303 ? 101.675 95.707  104.819 1.00 43.99 ?  282 ILE C CA    1 
ATOM   13300 C  C     . ILE C 2 303 ? 101.388 97.158  104.423 1.00 43.53 ?  282 ILE C C     1 
ATOM   13301 O  O     . ILE C 2 303 ? 101.697 97.565  103.300 1.00 43.52 ?  282 ILE C O     1 
ATOM   13302 C  CB    . ILE C 2 303 ? 103.093 95.600  105.453 1.00 43.84 ?  282 ILE C CB    1 
ATOM   13303 C  CG1   . ILE C 2 303 ? 103.451 94.138  105.782 1.00 43.91 ?  282 ILE C CG1   1 
ATOM   13304 C  CG2   . ILE C 2 303 ? 103.236 96.516  106.682 1.00 43.55 ?  282 ILE C CG2   1 
ATOM   13305 C  CD1   . ILE C 2 303 ? 102.495 93.430  106.747 1.00 42.76 ?  282 ILE C CD1   1 
ATOM   13306 N  N     . ASN C 2 304 ? 100.791 97.927  105.335 1.00 42.51 ?  283 ASN C N     1 
ATOM   13307 C  CA    . ASN C 2 304 ? 100.516 99.344  105.097 1.00 41.93 ?  283 ASN C CA    1 
ATOM   13308 C  C     . ASN C 2 304 ? 101.778 100.057 104.585 1.00 41.78 ?  283 ASN C C     1 
ATOM   13309 O  O     . ASN C 2 304 ? 102.812 100.045 105.267 1.00 41.13 ?  283 ASN C O     1 
ATOM   13310 C  CB    . ASN C 2 304 ? 100.003 100.010 106.384 1.00 41.83 ?  283 ASN C CB    1 
ATOM   13311 C  CG    . ASN C 2 304 ? 99.245  101.312 106.124 1.00 41.27 ?  283 ASN C CG    1 
ATOM   13312 O  OD1   . ASN C 2 304 ? 99.673  102.159 105.343 1.00 41.28 ?  283 ASN C OD1   1 
ATOM   13313 N  ND2   . ASN C 2 304 ? 98.114  101.472 106.794 1.00 40.67 ?  283 ASN C ND2   1 
ATOM   13314 N  N     . PRO C 2 305 ? 101.705 100.662 103.374 1.00 41.74 ?  284 PRO C N     1 
ATOM   13315 C  CA    . PRO C 2 305 ? 102.895 101.296 102.785 1.00 41.82 ?  284 PRO C CA    1 
ATOM   13316 C  C     . PRO C 2 305 ? 103.424 102.471 103.616 1.00 41.56 ?  284 PRO C C     1 
ATOM   13317 O  O     . PRO C 2 305 ? 104.602 102.819 103.508 1.00 41.46 ?  284 PRO C O     1 
ATOM   13318 C  CB    . PRO C 2 305 ? 102.412 101.766 101.399 1.00 42.14 ?  284 PRO C CB    1 
ATOM   13319 C  CG    . PRO C 2 305 ? 100.933 101.829 101.497 1.00 42.59 ?  284 PRO C CG    1 
ATOM   13320 C  CD    . PRO C 2 305 ? 100.535 100.753 102.478 1.00 42.05 ?  284 PRO C CD    1 
ATOM   13321 N  N     . ILE C 2 306 ? 102.561 103.057 104.443 1.00 41.19 ?  285 ILE C N     1 
ATOM   13322 C  CA    . ILE C 2 306 ? 102.957 104.108 105.379 1.00 41.47 ?  285 ILE C CA    1 
ATOM   13323 C  C     . ILE C 2 306 ? 104.019 103.581 106.353 1.00 41.71 ?  285 ILE C C     1 
ATOM   13324 O  O     . ILE C 2 306 ? 105.037 104.231 106.585 1.00 41.38 ?  285 ILE C O     1 
ATOM   13325 C  CB    . ILE C 2 306 ? 101.740 104.647 106.178 1.00 41.22 ?  285 ILE C CB    1 
ATOM   13326 C  CG1   . ILE C 2 306 ? 100.711 105.285 105.234 1.00 41.27 ?  285 ILE C CG1   1 
ATOM   13327 C  CG2   . ILE C 2 306 ? 102.187 105.632 107.256 1.00 40.37 ?  285 ILE C CG2   1 
ATOM   13328 C  CD1   . ILE C 2 306 ? 99.344  105.495 105.871 1.00 41.85 ?  285 ILE C CD1   1 
ATOM   13329 N  N     . VAL C 2 307 ? 103.764 102.397 106.910 1.00 42.33 ?  286 VAL C N     1 
ATOM   13330 C  CA    . VAL C 2 307 ? 104.690 101.737 107.835 1.00 43.36 ?  286 VAL C CA    1 
ATOM   13331 C  C     . VAL C 2 307 ? 106.018 101.372 107.159 1.00 44.51 ?  286 VAL C C     1 
ATOM   13332 O  O     . VAL C 2 307 ? 107.072 101.442 107.788 1.00 44.57 ?  286 VAL C O     1 
ATOM   13333 C  CB    . VAL C 2 307 ? 104.026 100.510 108.506 1.00 42.97 ?  286 VAL C CB    1 
ATOM   13334 C  CG1   . VAL C 2 307 ? 105.063 99.606  109.194 1.00 42.86 ?  286 VAL C CG1   1 
ATOM   13335 C  CG2   . VAL C 2 307 ? 102.982 100.984 109.499 1.00 41.93 ?  286 VAL C CG2   1 
ATOM   13336 N  N     . LEU C 2 308 ? 105.951 101.012 105.878 1.00 46.21 ?  287 LEU C N     1 
ATOM   13337 C  CA    . LEU C 2 308 ? 107.136 100.712 105.061 1.00 47.66 ?  287 LEU C CA    1 
ATOM   13338 C  C     . LEU C 2 308 ? 107.979 101.957 104.785 1.00 48.82 ?  287 LEU C C     1 
ATOM   13339 O  O     . LEU C 2 308 ? 109.213 101.877 104.724 1.00 49.02 ?  287 LEU C O     1 
ATOM   13340 C  CB    . LEU C 2 308 ? 106.728 100.031 103.747 1.00 47.95 ?  287 LEU C CB    1 
ATOM   13341 C  CG    . LEU C 2 308 ? 106.650 98.495  103.708 1.00 48.23 ?  287 LEU C CG    1 
ATOM   13342 C  CD1   . LEU C 2 308 ? 106.371 97.851  105.074 1.00 48.10 ?  287 LEU C CD1   1 
ATOM   13343 C  CD2   . LEU C 2 308 ? 105.641 98.020  102.665 1.00 48.81 ?  287 LEU C CD2   1 
ATOM   13344 N  N     . ASN C 2 309 ? 107.307 103.097 104.616 1.00 49.80 ?  288 ASN C N     1 
ATOM   13345 C  CA    . ASN C 2 309 ? 107.977 104.394 104.574 1.00 51.09 ?  288 ASN C CA    1 
ATOM   13346 C  C     . ASN C 2 309 ? 108.526 104.818 105.940 1.00 51.08 ?  288 ASN C C     1 
ATOM   13347 O  O     . ASN C 2 309 ? 109.473 105.600 106.014 1.00 51.41 ?  288 ASN C O     1 
ATOM   13348 C  CB    . ASN C 2 309 ? 107.056 105.473 103.998 1.00 51.37 ?  288 ASN C CB    1 
ATOM   13349 C  CG    . ASN C 2 309 ? 107.009 105.449 102.484 1.00 53.22 ?  288 ASN C CG    1 
ATOM   13350 O  OD1   . ASN C 2 309 ? 106.866 104.388 101.867 1.00 54.39 ?  288 ASN C OD1   1 
ATOM   13351 N  ND2   . ASN C 2 309 ? 107.132 106.622 101.872 1.00 54.70 ?  288 ASN C ND2   1 
ATOM   13352 N  N     . GLY C 2 310 ? 107.927 104.296 107.010 1.00 51.25 ?  289 GLY C N     1 
ATOM   13353 C  CA    . GLY C 2 310 ? 108.429 104.494 108.372 1.00 51.35 ?  289 GLY C CA    1 
ATOM   13354 C  C     . GLY C 2 310 ? 109.783 103.840 108.616 1.00 51.86 ?  289 GLY C C     1 
ATOM   13355 O  O     . GLY C 2 310 ? 110.507 104.225 109.541 1.00 51.49 ?  289 GLY C O     1 
ATOM   13356 N  N     . LEU C 2 311 ? 110.122 102.848 107.791 1.00 52.45 ?  290 LEU C N     1 
ATOM   13357 C  CA    . LEU C 2 311 ? 111.417 102.168 107.868 1.00 52.99 ?  290 LEU C CA    1 
ATOM   13358 C  C     . LEU C 2 311 ? 112.480 102.894 107.040 1.00 53.65 ?  290 LEU C C     1 
ATOM   13359 O  O     . LEU C 2 311 ? 112.445 102.891 105.803 1.00 54.22 ?  290 LEU C O     1 
ATOM   13360 C  CB    . LEU C 2 311 ? 111.292 100.711 107.410 1.00 53.08 ?  290 LEU C CB    1 
ATOM   13361 C  CG    . LEU C 2 311 ? 110.580 99.702  108.315 1.00 53.33 ?  290 LEU C CG    1 
ATOM   13362 C  CD1   . LEU C 2 311 ? 110.234 98.443  107.534 1.00 53.79 ?  290 LEU C CD1   1 
ATOM   13363 C  CD2   . LEU C 2 311 ? 111.422 99.359  109.546 1.00 53.22 ?  290 LEU C CD2   1 
ATOM   13364 N  N     . LYS C 2 330 ? 140.048 109.492 114.965 1.00 57.38 ?  309 LYS C N     1 
ATOM   13365 C  CA    . LYS C 2 330 ? 141.247 110.290 114.736 1.00 58.57 ?  309 LYS C CA    1 
ATOM   13366 C  C     . LYS C 2 330 ? 141.962 109.858 113.462 1.00 57.73 ?  309 LYS C C     1 
ATOM   13367 O  O     . LYS C 2 330 ? 141.814 108.724 113.009 1.00 59.72 ?  309 LYS C O     1 
ATOM   13368 C  CB    . LYS C 2 330 ? 142.201 110.182 115.928 1.00 55.66 ?  309 LYS C CB    1 
ATOM   13369 C  CG    . LYS C 2 330 ? 141.901 111.143 117.065 1.00 56.05 ?  309 LYS C CG    1 
ATOM   13370 C  CD    . LYS C 2 330 ? 143.056 111.191 118.053 1.00 57.52 ?  309 LYS C CD    1 
ATOM   13371 C  CE    . LYS C 2 330 ? 142.753 112.114 119.221 1.00 58.27 ?  309 LYS C CE    1 
ATOM   13372 N  NZ    . LYS C 2 330 ? 141.981 111.423 120.290 1.00 57.81 1  309 LYS C NZ    1 
ATOM   13373 N  N     . ALA C 2 331 ? 142.740 110.770 112.887 1.00 46.74 ?  310 ALA C N     1 
ATOM   13374 C  CA    . ALA C 2 331 ? 143.576 110.452 111.743 1.00 47.69 ?  310 ALA C CA    1 
ATOM   13375 C  C     . ALA C 2 331 ? 144.923 109.924 112.219 1.00 44.34 ?  310 ALA C C     1 
ATOM   13376 O  O     . ALA C 2 331 ? 145.440 110.338 113.260 1.00 44.88 ?  310 ALA C O     1 
ATOM   13377 C  CB    . ALA C 2 331 ? 143.777 111.678 110.852 1.00 44.94 ?  310 ALA C CB    1 
ATOM   13378 N  N     . THR C 2 332 ? 145.480 108.993 111.449 1.00 40.86 ?  311 THR C N     1 
ATOM   13379 C  CA    . THR C 2 332 ? 146.735 108.353 111.821 1.00 38.81 ?  311 THR C CA    1 
ATOM   13380 C  C     . THR C 2 332 ? 147.850 109.380 111.946 1.00 36.15 ?  311 THR C C     1 
ATOM   13381 O  O     . THR C 2 332 ? 148.026 110.233 111.072 1.00 43.30 ?  311 THR C O     1 
ATOM   13382 C  CB    . THR C 2 332 ? 147.110 107.285 110.789 1.00 39.78 ?  311 THR C CB    1 
ATOM   13383 O  OG1   . THR C 2 332 ? 146.088 106.281 110.747 1.00 41.99 ?  311 THR C OG1   1 
ATOM   13384 C  CG2   . THR C 2 332 ? 148.439 106.638 111.146 1.00 37.37 ?  311 THR C CG2   1 
ATOM   13385 N  N     . VAL C 2 333 ? 148.600 109.294 113.039 1.00 29.00 ?  312 VAL C N     1 
ATOM   13386 C  CA    . VAL C 2 333 ? 149.689 110.230 113.298 1.00 27.73 ?  312 VAL C CA    1 
ATOM   13387 C  C     . VAL C 2 333 ? 150.981 109.644 112.745 1.00 34.73 ?  312 VAL C C     1 
ATOM   13388 O  O     . VAL C 2 333 ? 151.412 108.563 113.159 1.00 34.24 ?  312 VAL C O     1 
ATOM   13389 C  CB    . VAL C 2 333 ? 149.813 110.529 114.798 1.00 29.67 ?  312 VAL C CB    1 
ATOM   13390 C  CG1   . VAL C 2 333 ? 151.081 111.321 115.079 1.00 33.09 ?  312 VAL C CG1   1 
ATOM   13391 C  CG2   . VAL C 2 333 ? 148.588 111.281 115.290 1.00 33.00 ?  312 VAL C CG2   1 
ATOM   13392 N  N     . GLU C 2 334 ? 151.597 110.355 111.806 1.00 31.99 ?  313 GLU C N     1 
ATOM   13393 C  CA    . GLU C 2 334 ? 152.853 109.944 111.212 1.00 30.19 ?  313 GLU C CA    1 
ATOM   13394 C  C     . GLU C 2 334 ? 153.886 111.045 111.404 1.00 35.47 ?  313 GLU C C     1 
ATOM   13395 O  O     . GLU C 2 334 ? 153.619 112.203 111.051 1.00 39.91 ?  313 GLU C O     1 
ATOM   13396 C  CB    . GLU C 2 334 ? 152.677 109.637 109.716 1.00 31.98 ?  313 GLU C CB    1 
ATOM   13397 C  CG    . GLU C 2 334 ? 153.742 108.717 109.143 1.00 30.40 ?  313 GLU C CG    1 
ATOM   13398 C  CD    . GLU C 2 334 ? 153.741 108.692 107.628 1.00 36.69 ?  313 GLU C CD    1 
ATOM   13399 O  OE1   . GLU C 2 334 ? 152.645 108.631 107.034 1.00 35.22 ?  313 GLU C OE1   1 
ATOM   13400 O  OE2   . GLU C 2 334 ? 154.837 108.715 107.030 1.00 37.50 -1 313 GLU C OE2   1 
ATOM   13401 N  N     . PRO C 2 335 ? 155.054 110.741 111.963 1.00 33.23 ?  314 PRO C N     1 
ATOM   13402 C  CA    . PRO C 2 335 ? 156.031 111.796 112.247 1.00 32.48 ?  314 PRO C CA    1 
ATOM   13403 C  C     . PRO C 2 335 ? 156.557 112.445 110.977 1.00 32.75 ?  314 PRO C C     1 
ATOM   13404 O  O     . PRO C 2 335 ? 156.664 111.815 109.922 1.00 33.62 ?  314 PRO C O     1 
ATOM   13405 C  CB    . PRO C 2 335 ? 157.146 111.054 112.992 1.00 27.14 ?  314 PRO C CB    1 
ATOM   13406 C  CG    . PRO C 2 335 ? 157.038 109.648 112.508 1.00 33.25 ?  314 PRO C CG    1 
ATOM   13407 C  CD    . PRO C 2 335 ? 155.567 109.405 112.314 1.00 31.97 ?  314 PRO C CD    1 
ATOM   13408 N  N     . LEU C 2 336 ? 156.882 113.729 111.094 1.00 31.37 ?  315 LEU C N     1 
ATOM   13409 C  CA    . LEU C 2 336 ? 157.445 114.478 109.981 1.00 25.32 ?  315 LEU C CA    1 
ATOM   13410 C  C     . LEU C 2 336 ? 158.898 114.087 109.758 1.00 30.05 ?  315 LEU C C     1 
ATOM   13411 O  O     . LEU C 2 336 ? 159.677 113.965 110.707 1.00 28.04 ?  315 LEU C O     1 
ATOM   13412 C  CB    . LEU C 2 336 ? 157.352 115.980 110.247 1.00 24.68 ?  315 LEU C CB    1 
ATOM   13413 C  CG    . LEU C 2 336 ? 156.107 116.730 109.780 1.00 29.53 ?  315 LEU C CG    1 
ATOM   13414 C  CD1   . LEU C 2 336 ? 156.011 118.061 110.504 1.00 23.58 ?  315 LEU C CD1   1 
ATOM   13415 C  CD2   . LEU C 2 336 ? 156.130 116.936 108.277 1.00 23.76 ?  315 LEU C CD2   1 
ATOM   13416 N  N     . LYS C 2 337 ? 159.262 113.899 108.495 1.00 29.08 ?  316 LYS C N     1 
ATOM   13417 C  CA    . LYS C 2 337 ? 160.643 113.633 108.133 1.00 24.90 ?  316 LYS C CA    1 
ATOM   13418 C  C     . LYS C 2 337 ? 161.364 114.940 107.811 1.00 25.51 ?  316 LYS C C     1 
ATOM   13419 O  O     . LYS C 2 337 ? 160.752 115.994 107.635 1.00 33.13 ?  316 LYS C O     1 
ATOM   13420 C  CB    . LYS C 2 337 ? 160.716 112.677 106.943 1.00 29.23 ?  316 LYS C CB    1 
ATOM   13421 C  CG    . LYS C 2 337 ? 159.849 111.439 107.073 1.00 29.66 ?  316 LYS C CG    1 
ATOM   13422 C  CD    . LYS C 2 337 ? 160.308 110.351 106.115 1.00 30.93 ?  316 LYS C CD    1 
ATOM   13423 C  CE    . LYS C 2 337 ? 159.780 108.987 106.528 1.00 33.14 ?  316 LYS C CE    1 
ATOM   13424 N  NZ    . LYS C 2 337 ? 158.425 109.077 107.140 1.00 33.67 1  316 LYS C NZ    1 
ATOM   13425 N  N     . ASP C 2 338 ? 162.694 114.859 107.743 1.00 26.51 ?  317 ASP C N     1 
ATOM   13426 C  CA    . ASP C 2 338 ? 163.478 116.023 107.349 1.00 29.94 ?  317 ASP C CA    1 
ATOM   13427 C  C     . ASP C 2 338 ? 163.181 116.420 105.910 1.00 29.65 ?  317 ASP C C     1 
ATOM   13428 O  O     . ASP C 2 338 ? 163.083 117.610 105.593 1.00 24.94 ?  317 ASP C O     1 
ATOM   13429 C  CB    . ASP C 2 338 ? 164.968 115.742 107.535 1.00 32.12 ?  317 ASP C CB    1 
ATOM   13430 C  CG    . ASP C 2 338 ? 165.457 116.082 108.928 1.00 35.61 ?  317 ASP C CG    1 
ATOM   13431 O  OD1   . ASP C 2 338 ? 165.309 115.235 109.834 1.00 36.45 ?  317 ASP C OD1   1 
ATOM   13432 O  OD2   . ASP C 2 338 ? 165.987 117.196 109.120 1.00 32.88 -1 317 ASP C OD2   1 
ATOM   13433 N  N     . ASP C 2 339 ? 163.023 115.434 105.026 1.00 31.98 ?  318 ASP C N     1 
ATOM   13434 C  CA    . ASP C 2 339 ? 162.754 115.706 103.619 1.00 23.82 ?  318 ASP C CA    1 
ATOM   13435 C  C     . ASP C 2 339 ? 161.372 116.301 103.381 1.00 21.90 ?  318 ASP C C     1 
ATOM   13436 O  O     . ASP C 2 339 ? 161.113 116.791 102.276 1.00 29.62 ?  318 ASP C O     1 
ATOM   13437 C  CB    . ASP C 2 339 ? 162.910 114.422 102.800 1.00 24.61 ?  318 ASP C CB    1 
ATOM   13438 C  CG    . ASP C 2 339 ? 164.358 113.998 102.653 1.00 36.61 ?  318 ASP C CG    1 
ATOM   13439 O  OD1   . ASP C 2 339 ? 165.239 114.882 102.625 1.00 34.94 ?  318 ASP C OD1   1 
ATOM   13440 O  OD2   . ASP C 2 339 ? 164.615 112.778 102.566 1.00 37.02 -1 318 ASP C OD2   1 
ATOM   13441 N  N     . ASP C 2 340 ? 160.482 116.265 104.373 1.00 21.75 ?  319 ASP C N     1 
ATOM   13442 C  CA    . ASP C 2 340 ? 159.161 116.865 104.228 1.00 12.52 ?  319 ASP C CA    1 
ATOM   13443 C  C     . ASP C 2 340 ? 159.204 118.386 104.209 1.00 11.68 ?  319 ASP C C     1 
ATOM   13444 O  O     . ASP C 2 340 ? 158.226 119.009 103.782 1.00 29.94 ?  319 ASP C O     1 
ATOM   13445 C  CB    . ASP C 2 340 ? 158.246 116.396 105.358 1.00 15.38 ?  319 ASP C CB    1 
ATOM   13446 C  CG    . ASP C 2 340 ? 157.813 114.957 105.196 1.00 27.80 ?  319 ASP C CG    1 
ATOM   13447 O  OD1   . ASP C 2 340 ? 157.144 114.434 106.110 1.00 35.11 ?  319 ASP C OD1   1 
ATOM   13448 O  OD2   . ASP C 2 340 ? 158.139 114.348 104.155 1.00 32.85 -1 319 ASP C OD2   1 
ATOM   13449 N  N     . PHE C 2 341 ? 160.299 118.991 104.658 1.00 19.10 ?  320 PHE C N     1 
ATOM   13450 C  CA    . PHE C 2 341 ? 160.419 120.439 104.746 1.00 9.08  ?  320 PHE C CA    1 
ATOM   13451 C  C     . PHE C 2 341 ? 161.056 121.061 103.512 1.00 17.46 ?  320 PHE C C     1 
ATOM   13452 O  O     . PHE C 2 341 ? 161.205 122.285 103.462 1.00 21.47 ?  320 PHE C O     1 
ATOM   13453 C  CB    . PHE C 2 341 ? 161.225 120.817 105.990 1.00 14.57 ?  320 PHE C CB    1 
ATOM   13454 C  CG    . PHE C 2 341 ? 160.490 120.590 107.277 1.00 10.84 ?  320 PHE C CG    1 
ATOM   13455 C  CD1   . PHE C 2 341 ? 159.742 121.601 107.849 1.00 9.48  ?  320 PHE C CD1   1 
ATOM   13456 C  CD2   . PHE C 2 341 ? 160.541 119.361 107.911 1.00 12.36 ?  320 PHE C CD2   1 
ATOM   13457 C  CE1   . PHE C 2 341 ? 159.062 121.394 109.032 1.00 7.91  ?  320 PHE C CE1   1 
ATOM   13458 C  CE2   . PHE C 2 341 ? 159.862 119.148 109.092 1.00 13.16 ?  320 PHE C CE2   1 
ATOM   13459 C  CZ    . PHE C 2 341 ? 159.122 120.166 109.653 1.00 4.56  ?  320 PHE C CZ    1 
ATOM   13460 N  N     . TYR C 2 342 ? 161.433 120.258 102.522 1.00 9.53  ?  321 TYR C N     1 
ATOM   13461 C  CA    . TYR C 2 342 ? 162.007 120.762 101.285 1.00 17.23 ?  321 TYR C CA    1 
ATOM   13462 C  C     . TYR C 2 342 ? 161.192 120.262 100.102 1.00 16.10 ?  321 TYR C C     1 
ATOM   13463 O  O     . TYR C 2 342 ? 160.664 119.148 100.113 1.00 16.88 ?  321 TYR C O     1 
ATOM   13464 C  CB    . TYR C 2 342 ? 163.488 120.365 101.112 1.00 17.88 ?  321 TYR C CB    1 
ATOM   13465 C  CG    . TYR C 2 342 ? 164.333 120.472 102.364 1.00 13.83 ?  321 TYR C CG    1 
ATOM   13466 C  CD1   . TYR C 2 342 ? 164.228 119.544 103.392 1.00 18.12 ?  321 TYR C CD1   1 
ATOM   13467 C  CD2   . TYR C 2 342 ? 165.233 121.516 102.519 1.00 16.03 ?  321 TYR C CD2   1 
ATOM   13468 C  CE1   . TYR C 2 342 ? 165.002 119.652 104.531 1.00 15.48 ?  321 TYR C CE1   1 
ATOM   13469 C  CE2   . TYR C 2 342 ? 166.008 121.631 103.655 1.00 17.80 ?  321 TYR C CE2   1 
ATOM   13470 C  CZ    . TYR C 2 342 ? 165.888 120.697 104.658 1.00 19.62 ?  321 TYR C CZ    1 
ATOM   13471 O  OH    . TYR C 2 342 ? 166.660 120.807 105.792 1.00 28.71 ?  321 TYR C OH    1 
ATOM   13472 N  N     . PHE C 2 343 ? 161.097 121.109 99.083  1.00 7.71  ?  322 PHE C N     1 
ATOM   13473 C  CA    . PHE C 2 343 ? 160.242 120.845 97.934  1.00 20.35 ?  322 PHE C CA    1 
ATOM   13474 C  C     . PHE C 2 343 ? 160.966 121.161 96.630  1.00 25.47 ?  322 PHE C C     1 
ATOM   13475 O  O     . PHE C 2 343 ? 161.915 121.944 96.608  1.00 26.11 ?  322 PHE C O     1 
ATOM   13476 C  CB    . PHE C 2 343 ? 158.955 121.664 98.042  1.00 15.28 ?  322 PHE C CB    1 
ATOM   13477 C  CG    . PHE C 2 343 ? 158.207 121.444 99.324  1.00 13.74 ?  322 PHE C CG    1 
ATOM   13478 C  CD1   . PHE C 2 343 ? 157.345 120.372 99.464  1.00 17.31 ?  322 PHE C CD1   1 
ATOM   13479 C  CD2   . PHE C 2 343 ? 158.381 122.299 100.397 1.00 4.75  ?  322 PHE C CD2   1 
ATOM   13480 C  CE1   . PHE C 2 343 ? 156.663 120.165 100.645 1.00 16.31 ?  322 PHE C CE1   1 
ATOM   13481 C  CE2   . PHE C 2 343 ? 157.705 122.096 101.579 1.00 5.64  ?  322 PHE C CE2   1 
ATOM   13482 C  CZ    . PHE C 2 343 ? 156.843 121.028 101.703 1.00 10.19 ?  322 PHE C CZ    1 
ATOM   13483 N  N     . ASP D 2 37  ? 118.842 108.304 145.795 1.00 32.44 ?  16  ASP D N     1 
ATOM   13484 C  CA    . ASP D 2 37  ? 119.368 109.670 145.735 1.00 32.83 ?  16  ASP D CA    1 
ATOM   13485 C  C     . ASP D 2 37  ? 120.506 109.855 144.732 1.00 31.65 ?  16  ASP D C     1 
ATOM   13486 O  O     . ASP D 2 37  ? 120.950 110.986 144.515 1.00 32.65 ?  16  ASP D O     1 
ATOM   13487 C  CB    . ASP D 2 37  ? 119.888 110.114 147.111 1.00 33.73 ?  16  ASP D CB    1 
ATOM   13488 C  CG    . ASP D 2 37  ? 118.793 110.221 148.161 1.00 36.81 ?  16  ASP D CG    1 
ATOM   13489 O  OD1   . ASP D 2 37  ? 119.143 110.216 149.365 1.00 39.69 ?  16  ASP D OD1   1 
ATOM   13490 O  OD2   . ASP D 2 37  ? 117.597 110.304 147.798 1.00 39.67 -1 16  ASP D OD2   1 
ATOM   13491 N  N     . PHE D 2 38  ? 120.985 108.770 144.127 1.00 29.55 ?  17  PHE D N     1 
ATOM   13492 C  CA    . PHE D 2 38  ? 122.271 108.833 143.433 1.00 27.75 ?  17  PHE D CA    1 
ATOM   13493 C  C     . PHE D 2 38  ? 122.389 108.101 142.086 1.00 26.21 ?  17  PHE D C     1 
ATOM   13494 O  O     . PHE D 2 38  ? 123.292 108.397 141.311 1.00 25.93 ?  17  PHE D O     1 
ATOM   13495 C  CB    . PHE D 2 38  ? 123.393 108.376 144.393 1.00 27.37 ?  17  PHE D CB    1 
ATOM   13496 C  CG    . PHE D 2 38  ? 123.217 106.970 144.902 1.00 27.32 ?  17  PHE D CG    1 
ATOM   13497 C  CD1   . PHE D 2 38  ? 123.660 105.885 144.152 1.00 27.01 ?  17  PHE D CD1   1 
ATOM   13498 C  CD2   . PHE D 2 38  ? 122.608 106.728 146.127 1.00 28.02 ?  17  PHE D CD2   1 
ATOM   13499 C  CE1   . PHE D 2 38  ? 123.494 104.581 144.614 1.00 27.66 ?  17  PHE D CE1   1 
ATOM   13500 C  CE2   . PHE D 2 38  ? 122.434 105.430 146.590 1.00 27.68 ?  17  PHE D CE2   1 
ATOM   13501 C  CZ    . PHE D 2 38  ? 122.879 104.353 145.830 1.00 27.47 ?  17  PHE D CZ    1 
ATOM   13502 N  N     . THR D 2 39  ? 121.494 107.158 141.810 1.00 24.88 ?  18  THR D N     1 
ATOM   13503 C  CA    . THR D 2 39  ? 121.639 106.288 140.631 1.00 23.81 ?  18  THR D CA    1 
ATOM   13504 C  C     . THR D 2 39  ? 121.568 107.027 139.282 1.00 23.56 ?  18  THR D C     1 
ATOM   13505 O  O     . THR D 2 39  ? 122.351 106.754 138.373 1.00 23.02 ?  18  THR D O     1 
ATOM   13506 C  CB    . THR D 2 39  ? 120.681 105.074 140.695 1.00 23.40 ?  18  THR D CB    1 
ATOM   13507 O  OG1   . THR D 2 39  ? 121.222 104.100 141.597 1.00 23.77 ?  18  THR D OG1   1 
ATOM   13508 C  CG2   . THR D 2 39  ? 120.517 104.416 139.335 1.00 22.31 ?  18  THR D CG2   1 
ATOM   13509 N  N     . GLN D 2 40  ? 120.648 107.974 139.150 1.00 23.78 ?  19  GLN D N     1 
ATOM   13510 C  CA    . GLN D 2 40  ? 120.568 108.730 137.897 1.00 23.88 ?  19  GLN D CA    1 
ATOM   13511 C  C     . GLN D 2 40  ? 121.815 109.587 137.659 1.00 24.09 ?  19  GLN D C     1 
ATOM   13512 O  O     . GLN D 2 40  ? 122.323 109.648 136.548 1.00 23.15 ?  19  GLN D O     1 
ATOM   13513 C  CB    . GLN D 2 40  ? 119.284 109.558 137.822 1.00 24.53 ?  19  GLN D CB    1 
ATOM   13514 C  CG    . GLN D 2 40  ? 118.047 108.681 137.704 1.00 24.06 ?  19  GLN D CG    1 
ATOM   13515 C  CD    . GLN D 2 40  ? 116.836 109.419 137.182 1.00 25.83 ?  19  GLN D CD    1 
ATOM   13516 O  OE1   . GLN D 2 40  ? 116.948 110.536 136.680 1.00 25.90 ?  19  GLN D OE1   1 
ATOM   13517 N  NE2   . GLN D 2 40  ? 115.667 108.785 137.279 1.00 23.56 ?  19  GLN D NE2   1 
ATOM   13518 N  N     . MET D 2 41  ? 122.329 110.208 138.713 1.00 24.07 ?  20  MET D N     1 
ATOM   13519 C  CA    . MET D 2 41  ? 123.595 110.936 138.615 1.00 25.53 ?  20  MET D CA    1 
ATOM   13520 C  C     . MET D 2 41  ? 124.762 110.036 138.160 1.00 24.24 ?  20  MET D C     1 
ATOM   13521 O  O     . MET D 2 41  ? 125.557 110.430 137.302 1.00 23.16 ?  20  MET D O     1 
ATOM   13522 C  CB    . MET D 2 41  ? 123.914 111.615 139.951 1.00 26.79 ?  20  MET D CB    1 
ATOM   13523 C  CG    . MET D 2 41  ? 125.222 112.381 139.982 1.00 32.62 ?  20  MET D CG    1 
ATOM   13524 S  SD    . MET D 2 41  ? 125.632 112.837 141.683 1.00 44.01 ?  20  MET D SD    1 
ATOM   13525 C  CE    . MET D 2 41  ? 127.417 112.999 141.578 1.00 41.93 ?  20  MET D CE    1 
ATOM   13526 N  N     . PHE D 2 42  ? 124.856 108.828 138.720 1.00 23.31 ?  21  PHE D N     1 
ATOM   13527 C  CA    . PHE D 2 42  ? 125.917 107.905 138.319 1.00 23.44 ?  21  PHE D CA    1 
ATOM   13528 C  C     . PHE D 2 42  ? 125.702 107.361 136.921 1.00 23.55 ?  21  PHE D C     1 
ATOM   13529 O  O     . PHE D 2 42  ? 126.662 107.129 136.195 1.00 23.74 ?  21  PHE D O     1 
ATOM   13530 C  CB    . PHE D 2 42  ? 126.092 106.769 139.330 1.00 22.97 ?  21  PHE D CB    1 
ATOM   13531 C  CG    . PHE D 2 42  ? 126.998 107.132 140.454 1.00 23.86 ?  21  PHE D CG    1 
ATOM   13532 C  CD1   . PHE D 2 42  ? 128.349 106.797 140.411 1.00 24.55 ?  21  PHE D CD1   1 
ATOM   13533 C  CD2   . PHE D 2 42  ? 126.519 107.845 141.536 1.00 24.06 ?  21  PHE D CD2   1 
ATOM   13534 C  CE1   . PHE D 2 42  ? 129.204 107.154 141.455 1.00 25.78 ?  21  PHE D CE1   1 
ATOM   13535 C  CE2   . PHE D 2 42  ? 127.368 108.208 142.585 1.00 25.25 ?  21  PHE D CE2   1 
ATOM   13536 C  CZ    . PHE D 2 42  ? 128.704 107.869 142.543 1.00 25.79 ?  21  PHE D CZ    1 
ATOM   13537 N  N     . TYR D 2 43  ? 124.437 107.179 136.547 1.00 24.08 ?  22  TYR D N     1 
ATOM   13538 C  CA    . TYR D 2 43  ? 124.096 106.807 135.184 1.00 24.74 ?  22  TYR D CA    1 
ATOM   13539 C  C     . TYR D 2 43  ? 124.718 107.811 134.211 1.00 25.72 ?  22  TYR D C     1 
ATOM   13540 O  O     . TYR D 2 43  ? 125.397 107.426 133.255 1.00 25.56 ?  22  TYR D O     1 
ATOM   13541 C  CB    . TYR D 2 43  ? 122.574 106.731 134.973 1.00 24.90 ?  22  TYR D CB    1 
ATOM   13542 C  CG    . TYR D 2 43  ? 122.216 106.510 133.511 1.00 24.38 ?  22  TYR D CG    1 
ATOM   13543 C  CD1   . TYR D 2 43  ? 122.097 105.227 132.992 1.00 23.96 ?  22  TYR D CD1   1 
ATOM   13544 C  CD2   . TYR D 2 43  ? 122.054 107.592 132.640 1.00 24.73 ?  22  TYR D CD2   1 
ATOM   13545 C  CE1   . TYR D 2 43  ? 121.804 105.020 131.642 1.00 23.42 ?  22  TYR D CE1   1 
ATOM   13546 C  CE2   . TYR D 2 43  ? 121.747 107.401 131.291 1.00 26.65 ?  22  TYR D CE2   1 
ATOM   13547 C  CZ    . TYR D 2 43  ? 121.629 106.111 130.803 1.00 25.68 ?  22  TYR D CZ    1 
ATOM   13548 O  OH    . TYR D 2 43  ? 121.329 105.918 129.474 1.00 26.57 ?  22  TYR D OH    1 
ATOM   13549 N  N     . ASN D 2 44  ? 124.469 109.094 134.467 1.00 26.77 ?  23  ASN D N     1 
ATOM   13550 C  CA    . ASN D 2 44  ? 124.971 110.171 133.623 1.00 28.57 ?  23  ASN D CA    1 
ATOM   13551 C  C     . ASN D 2 44  ? 126.484 110.162 133.509 1.00 28.70 ?  23  ASN D C     1 
ATOM   13552 O  O     . ASN D 2 44  ? 127.022 110.165 132.399 1.00 28.99 ?  23  ASN D O     1 
ATOM   13553 C  CB    . ASN D 2 44  ? 124.454 111.525 134.117 1.00 29.62 ?  23  ASN D CB    1 
ATOM   13554 C  CG    . ASN D 2 44  ? 122.957 111.691 133.883 1.00 32.44 ?  23  ASN D CG    1 
ATOM   13555 O  OD1   . ASN D 2 44  ? 122.371 111.021 133.022 1.00 34.30 ?  23  ASN D OD1   1 
ATOM   13556 N  ND2   . ASN D 2 44  ? 122.329 112.581 134.648 1.00 35.17 ?  23  ASN D ND2   1 
ATOM   13557 N  N     . GLN D 2 45  ? 127.161 110.105 134.653 1.00 28.97 ?  24  GLN D N     1 
ATOM   13558 C  CA    . GLN D 2 45  ? 128.619 110.103 134.678 1.00 29.99 ?  24  GLN D CA    1 
ATOM   13559 C  C     . GLN D 2 45  ? 129.215 108.876 133.973 1.00 29.69 ?  24  GLN D C     1 
ATOM   13560 O  O     . GLN D 2 45  ? 130.209 108.993 133.259 1.00 30.01 ?  24  GLN D O     1 
ATOM   13561 C  CB    . GLN D 2 45  ? 129.145 110.225 136.114 1.00 30.27 ?  24  GLN D CB    1 
ATOM   13562 C  CG    . GLN D 2 45  ? 130.669 110.466 136.202 1.00 32.29 ?  24  GLN D CG    1 
ATOM   13563 C  CD    . GLN D 2 45  ? 131.109 111.778 135.565 1.00 35.95 ?  24  GLN D CD    1 
ATOM   13564 O  OE1   . GLN D 2 45  ? 130.346 112.746 135.507 1.00 36.72 ?  24  GLN D OE1   1 
ATOM   13565 N  NE2   . GLN D 2 45  ? 132.348 111.815 135.085 1.00 37.05 ?  24  GLN D NE2   1 
ATOM   13566 N  N     . ASN D 2 46  ? 128.590 107.713 134.154 1.00 28.93 ?  25  ASN D N     1 
ATOM   13567 C  CA    . ASN D 2 46  ? 129.035 106.499 133.490 1.00 28.70 ?  25  ASN D CA    1 
ATOM   13568 C  C     . ASN D 2 46  ? 128.940 106.563 131.971 1.00 29.05 ?  25  ASN D C     1 
ATOM   13569 O  O     . ASN D 2 46  ? 129.924 106.288 131.278 1.00 28.51 ?  25  ASN D O     1 
ATOM   13570 C  CB    . ASN D 2 46  ? 128.285 105.268 134.018 1.00 28.36 ?  25  ASN D CB    1 
ATOM   13571 C  CG    . ASN D 2 46  ? 128.953 104.665 135.235 1.00 28.45 ?  25  ASN D CG    1 
ATOM   13572 O  OD1   . ASN D 2 46  ? 129.719 103.712 135.112 1.00 28.03 ?  25  ASN D OD1   1 
ATOM   13573 N  ND2   . ASN D 2 46  ? 128.693 105.234 136.411 1.00 26.53 ?  25  ASN D ND2   1 
ATOM   13574 N  N     . VAL D 2 47  ? 127.772 106.949 131.457 1.00 29.66 ?  26  VAL D N     1 
ATOM   13575 C  CA    . VAL D 2 47  ? 127.550 106.931 130.011 1.00 31.15 ?  26  VAL D CA    1 
ATOM   13576 C  C     . VAL D 2 47  ? 128.339 108.031 129.305 1.00 32.39 ?  26  VAL D C     1 
ATOM   13577 O  O     . VAL D 2 47  ? 128.749 107.863 128.158 1.00 32.80 ?  26  VAL D O     1 
ATOM   13578 C  CB    . VAL D 2 47  ? 126.039 106.953 129.603 1.00 31.08 ?  26  VAL D CB    1 
ATOM   13579 C  CG1   . VAL D 2 47  ? 125.287 105.797 130.254 1.00 31.09 ?  26  VAL D CG1   1 
ATOM   13580 C  CG2   . VAL D 2 47  ? 125.375 108.300 129.924 1.00 30.81 ?  26  VAL D CG2   1 
ATOM   13581 N  N     . LYS D 2 48  ? 128.582 109.142 129.990 1.00 33.28 ?  27  LYS D N     1 
ATOM   13582 C  CA    . LYS D 2 48  ? 129.371 110.194 129.369 1.00 34.87 ?  27  LYS D CA    1 
ATOM   13583 C  C     . LYS D 2 48  ? 130.884 109.894 129.347 1.00 34.91 ?  27  LYS D C     1 
ATOM   13584 O  O     . LYS D 2 48  ? 131.640 110.567 128.651 1.00 34.92 ?  27  LYS D O     1 
ATOM   13585 C  CB    . LYS D 2 48  ? 129.035 111.572 129.958 1.00 35.45 ?  27  LYS D CB    1 
ATOM   13586 C  CG    . LYS D 2 48  ? 129.777 111.967 131.214 1.00 37.41 ?  27  LYS D CG    1 
ATOM   13587 C  CD    . LYS D 2 48  ? 129.635 113.480 131.447 1.00 40.91 ?  27  LYS D CD    1 
ATOM   13588 C  CE    . LYS D 2 48  ? 130.675 113.984 132.451 1.00 42.46 ?  27  LYS D CE    1 
ATOM   13589 N  NZ    . LYS D 2 48  ? 130.676 115.470 132.591 1.00 45.13 1  27  LYS D NZ    1 
ATOM   13590 N  N     . GLN D 2 49  ? 131.302 108.870 130.095 1.00 34.66 ?  28  GLN D N     1 
ATOM   13591 C  CA    . GLN D 2 49  ? 132.686 108.406 130.114 1.00 34.64 ?  28  GLN D CA    1 
ATOM   13592 C  C     . GLN D 2 49  ? 132.918 107.275 129.113 1.00 34.20 ?  28  GLN D C     1 
ATOM   13593 O  O     . GLN D 2 49  ? 133.990 106.668 129.112 1.00 34.53 ?  28  GLN D O     1 
ATOM   13594 C  CB    . GLN D 2 49  ? 133.083 107.920 131.523 1.00 34.89 ?  28  GLN D CB    1 
ATOM   13595 C  CG    . GLN D 2 49  ? 133.608 109.008 132.457 1.00 36.47 ?  28  GLN D CG    1 
ATOM   13596 C  CD    . GLN D 2 49  ? 133.806 108.532 133.898 1.00 38.37 ?  28  GLN D CD    1 
ATOM   13597 O  OE1   . GLN D 2 49  ? 133.654 109.314 134.837 1.00 40.68 ?  28  GLN D OE1   1 
ATOM   13598 N  NE2   . GLN D 2 49  ? 134.141 107.255 134.078 1.00 38.57 ?  28  GLN D NE2   1 
ATOM   13599 N  N     . PHE D 2 50  ? 131.925 106.981 128.272 1.00 33.42 ?  29  PHE D N     1 
ATOM   13600 C  CA    . PHE D 2 50  ? 132.037 105.858 127.342 1.00 32.57 ?  29  PHE D CA    1 
ATOM   13601 C  C     . PHE D 2 50  ? 133.197 106.083 126.371 1.00 32.60 ?  29  PHE D C     1 
ATOM   13602 O  O     . PHE D 2 50  ? 133.409 107.198 125.885 1.00 32.39 ?  29  PHE D O     1 
ATOM   13603 C  CB    . PHE D 2 50  ? 130.722 105.605 126.587 1.00 32.77 ?  29  PHE D CB    1 
ATOM   13604 C  CG    . PHE D 2 50  ? 130.778 104.427 125.634 1.00 32.24 ?  29  PHE D CG    1 
ATOM   13605 C  CD1   . PHE D 2 50  ? 130.738 103.121 126.112 1.00 31.50 ?  29  PHE D CD1   1 
ATOM   13606 C  CD2   . PHE D 2 50  ? 130.874 104.630 124.262 1.00 33.60 ?  29  PHE D CD2   1 
ATOM   13607 C  CE1   . PHE D 2 50  ? 130.792 102.040 125.246 1.00 33.02 ?  29  PHE D CE1   1 
ATOM   13608 C  CE2   . PHE D 2 50  ? 130.933 103.550 123.378 1.00 33.78 ?  29  PHE D CE2   1 
ATOM   13609 C  CZ    . PHE D 2 50  ? 130.884 102.255 123.869 1.00 33.13 ?  29  PHE D CZ    1 
ATOM   13610 N  N     . TRP D 2 51  ? 133.943 105.018 126.109 1.00 31.95 ?  30  TRP D N     1 
ATOM   13611 C  CA    . TRP D 2 51  ? 135.096 105.067 125.209 1.00 32.03 ?  30  TRP D CA    1 
ATOM   13612 C  C     . TRP D 2 51  ? 135.328 103.686 124.612 1.00 33.03 ?  30  TRP D C     1 
ATOM   13613 O  O     . TRP D 2 51  ? 134.744 102.698 125.064 1.00 32.54 ?  30  TRP D O     1 
ATOM   13614 C  CB    . TRP D 2 51  ? 136.351 105.574 125.938 1.00 31.19 ?  30  TRP D CB    1 
ATOM   13615 C  CG    . TRP D 2 51  ? 136.788 104.701 127.097 1.00 28.11 ?  30  TRP D CG    1 
ATOM   13616 C  CD1   . TRP D 2 51  ? 136.249 104.675 128.346 1.00 26.51 ?  30  TRP D CD1   1 
ATOM   13617 C  CD2   . TRP D 2 51  ? 137.846 103.729 127.096 1.00 25.93 ?  30  TRP D CD2   1 
ATOM   13618 N  NE1   . TRP D 2 51  ? 136.909 103.752 129.131 1.00 24.52 ?  30  TRP D NE1   1 
ATOM   13619 C  CE2   . TRP D 2 51  ? 137.890 103.157 128.388 1.00 24.42 ?  30  TRP D CE2   1 
ATOM   13620 C  CE3   . TRP D 2 51  ? 138.766 103.292 126.132 1.00 25.37 ?  30  TRP D CE3   1 
ATOM   13621 C  CZ2   . TRP D 2 51  ? 138.821 102.171 128.744 1.00 24.00 ?  30  TRP D CZ2   1 
ATOM   13622 C  CZ3   . TRP D 2 51  ? 139.687 102.305 126.484 1.00 24.99 ?  30  TRP D CZ3   1 
ATOM   13623 C  CH2   . TRP D 2 51  ? 139.705 101.756 127.779 1.00 23.72 ?  30  TRP D CH2   1 
ATOM   13624 N  N     . LEU D 2 52  ? 136.167 103.633 123.583 1.00 34.81 ?  31  LEU D N     1 
ATOM   13625 C  CA    . LEU D 2 52  ? 136.482 102.398 122.882 1.00 36.58 ?  31  LEU D CA    1 
ATOM   13626 C  C     . LEU D 2 52  ? 137.992 102.274 122.693 1.00 37.80 ?  31  LEU D C     1 
ATOM   13627 O  O     . LEU D 2 52  ? 138.672 103.282 122.528 1.00 37.92 ?  31  LEU D O     1 
ATOM   13628 C  CB    . LEU D 2 52  ? 135.761 102.350 121.525 1.00 36.95 ?  31  LEU D CB    1 
ATOM   13629 C  CG    . LEU D 2 52  ? 134.288 101.930 121.480 1.00 38.15 ?  31  LEU D CG    1 
ATOM   13630 C  CD1   . LEU D 2 52  ? 133.876 101.612 120.048 1.00 39.50 ?  31  LEU D CD1   1 
ATOM   13631 C  CD2   . LEU D 2 52  ? 134.010 100.724 122.371 1.00 37.94 ?  31  LEU D CD2   1 
ATOM   13632 N  N     . PRO D 2 53  ? 138.523 101.035 122.710 1.00 39.26 ?  32  PRO D N     1 
ATOM   13633 C  CA    . PRO D 2 53  ? 139.969 100.791 122.557 1.00 40.41 ?  32  PRO D CA    1 
ATOM   13634 C  C     . PRO D 2 53  ? 140.571 101.422 121.294 1.00 41.91 ?  32  PRO D C     1 
ATOM   13635 O  O     . PRO D 2 53  ? 141.639 102.040 121.358 1.00 42.52 ?  32  PRO D O     1 
ATOM   13636 C  CB    . PRO D 2 53  ? 140.058 99.264  122.461 1.00 40.42 ?  32  PRO D CB    1 
ATOM   13637 C  CG    . PRO D 2 53  ? 138.812 98.762  123.072 1.00 40.01 ?  32  PRO D CG    1 
ATOM   13638 C  CD    . PRO D 2 53  ? 137.759 99.778  122.803 1.00 39.30 ?  32  PRO D CD    1 
ATOM   13639 N  N     . GLU D 2 54  ? 139.874 101.281 120.171 1.00 43.27 ?  33  GLU D N     1 
ATOM   13640 C  CA    . GLU D 2 54  ? 140.318 101.784 118.860 1.00 45.17 ?  33  GLU D CA    1 
ATOM   13641 C  C     . GLU D 2 54  ? 140.694 103.274 118.821 1.00 45.57 ?  33  GLU D C     1 
ATOM   13642 O  O     . GLU D 2 54  ? 141.431 103.707 117.930 1.00 46.08 ?  33  GLU D O     1 
ATOM   13643 C  CB    . GLU D 2 54  ? 139.243 101.499 117.800 1.00 45.55 ?  33  GLU D CB    1 
ATOM   13644 C  CG    . GLU D 2 54  ? 139.258 100.077 117.234 1.00 48.19 ?  33  GLU D CG    1 
ATOM   13645 C  CD    . GLU D 2 54  ? 138.956 99.002  118.269 1.00 50.61 ?  33  GLU D CD    1 
ATOM   13646 O  OE1   . GLU D 2 54  ? 137.971 99.155  119.029 1.00 51.10 ?  33  GLU D OE1   1 
ATOM   13647 O  OE2   . GLU D 2 54  ? 139.714 98.004  118.321 1.00 52.64 -1 33  GLU D OE2   1 
ATOM   13648 N  N     . GLU D 2 55  ? 140.187 104.046 119.782 1.00 45.74 ?  34  GLU D N     1 
ATOM   13649 C  CA    . GLU D 2 55  ? 140.415 105.496 119.830 1.00 46.28 ?  34  GLU D CA    1 
ATOM   13650 C  C     . GLU D 2 55  ? 141.879 105.872 120.089 1.00 46.49 ?  34  GLU D C     1 
ATOM   13651 O  O     . GLU D 2 55  ? 142.346 106.921 119.636 1.00 46.73 ?  34  GLU D O     1 
ATOM   13652 C  CB    . GLU D 2 55  ? 139.508 106.156 120.874 1.00 46.17 ?  34  GLU D CB    1 
ATOM   13653 C  CG    . GLU D 2 55  ? 138.008 106.045 120.588 1.00 47.10 ?  34  GLU D CG    1 
ATOM   13654 C  CD    . GLU D 2 55  ? 137.162 106.772 121.632 1.00 48.43 ?  34  GLU D CD    1 
ATOM   13655 O  OE1   . GLU D 2 55  ? 137.280 108.012 121.742 1.00 49.62 ?  34  GLU D OE1   1 
ATOM   13656 O  OE2   . GLU D 2 55  ? 136.379 106.105 122.340 1.00 47.11 -1 34  GLU D OE2   1 
ATOM   13657 N  N     . ILE D 2 56  ? 142.594 105.019 120.822 1.00 46.23 ?  35  ILE D N     1 
ATOM   13658 C  CA    . ILE D 2 56  ? 144.007 105.242 121.113 1.00 46.25 ?  35  ILE D CA    1 
ATOM   13659 C  C     . ILE D 2 56  ? 144.859 104.343 120.218 1.00 46.30 ?  35  ILE D C     1 
ATOM   13660 O  O     . ILE D 2 56  ? 144.734 103.115 120.262 1.00 46.36 ?  35  ILE D O     1 
ATOM   13661 C  CB    . ILE D 2 56  ? 144.351 104.962 122.618 1.00 45.84 ?  35  ILE D CB    1 
ATOM   13662 C  CG1   . ILE D 2 56  ? 143.277 105.519 123.576 1.00 46.15 ?  35  ILE D CG1   1 
ATOM   13663 C  CG2   . ILE D 2 56  ? 145.769 105.455 122.969 1.00 45.72 ?  35  ILE D CG2   1 
ATOM   13664 C  CD1   . ILE D 2 56  ? 143.093 107.033 123.564 1.00 47.27 ?  35  ILE D CD1   1 
ATOM   13665 N  N     . ALA D 2 57  ? 145.712 104.952 119.400 1.00 46.51 ?  36  ALA D N     1 
ATOM   13666 C  CA    . ALA D 2 57  ? 146.672 104.200 118.587 1.00 46.56 ?  36  ALA D CA    1 
ATOM   13667 C  C     . ALA D 2 57  ? 147.828 103.732 119.476 1.00 46.08 ?  36  ALA D C     1 
ATOM   13668 O  O     . ALA D 2 57  ? 148.450 104.546 120.157 1.00 45.70 ?  36  ALA D O     1 
ATOM   13669 C  CB    . ALA D 2 57  ? 147.189 105.057 117.434 1.00 47.10 ?  36  ALA D CB    1 
ATOM   13670 N  N     . LEU D 2 58  ? 148.115 102.432 119.456 1.00 45.66 ?  37  LEU D N     1 
ATOM   13671 C  CA    . LEU D 2 58  ? 149.098 101.849 120.382 1.00 45.27 ?  37  LEU D CA    1 
ATOM   13672 C  C     . LEU D 2 58  ? 150.523 101.693 119.857 1.00 45.25 ?  37  LEU D C     1 
ATOM   13673 O  O     . LEU D 2 58  ? 151.468 101.592 120.647 1.00 44.82 ?  37  LEU D O     1 
ATOM   13674 C  CB    . LEU D 2 58  ? 148.600 100.504 120.909 1.00 45.05 ?  37  LEU D CB    1 
ATOM   13675 C  CG    . LEU D 2 58  ? 147.555 100.599 122.019 1.00 45.41 ?  37  LEU D CG    1 
ATOM   13676 C  CD1   . LEU D 2 58  ? 147.091 99.209  122.410 1.00 45.40 ?  37  LEU D CD1   1 
ATOM   13677 C  CD2   . LEU D 2 58  ? 148.111 101.347 123.229 1.00 44.70 ?  37  LEU D CD2   1 
ATOM   13678 N  N     . ASN D 2 59  ? 150.683 101.686 118.536 1.00 45.33 ?  38  ASN D N     1 
ATOM   13679 C  CA    . ASN D 2 59  ? 151.962 101.312 117.926 1.00 45.22 ?  38  ASN D CA    1 
ATOM   13680 C  C     . ASN D 2 59  ? 153.170 102.167 118.334 1.00 44.39 ?  38  ASN D C     1 
ATOM   13681 O  O     . ASN D 2 59  ? 154.292 101.653 118.421 1.00 44.33 ?  38  ASN D O     1 
ATOM   13682 C  CB    . ASN D 2 59  ? 151.829 101.250 116.407 1.00 46.22 ?  38  ASN D CB    1 
ATOM   13683 C  CG    . ASN D 2 59  ? 152.673 100.146 115.794 1.00 47.90 ?  38  ASN D CG    1 
ATOM   13684 O  OD1   . ASN D 2 59  ? 153.580 100.408 115.005 1.00 49.28 ?  38  ASN D OD1   1 
ATOM   13685 N  ND2   . ASN D 2 59  ? 152.374 98.897  116.157 1.00 49.18 ?  38  ASN D ND2   1 
ATOM   13686 N  N     . GLY D 2 60  ? 152.934 103.452 118.604 1.00 43.45 ?  39  GLY D N     1 
ATOM   13687 C  CA    . GLY D 2 60  ? 153.988 104.382 119.022 1.00 42.42 ?  39  GLY D CA    1 
ATOM   13688 C  C     . GLY D 2 60  ? 154.629 104.103 120.379 1.00 41.55 ?  39  GLY D C     1 
ATOM   13689 O  O     . GLY D 2 60  ? 155.617 104.745 120.750 1.00 41.29 ?  39  GLY D O     1 
ATOM   13690 N  N     . ASP D 2 61  ? 154.067 103.157 121.129 1.00 40.35 ?  40  ASP D N     1 
ATOM   13691 C  CA    . ASP D 2 61  ? 154.667 102.723 122.396 1.00 39.53 ?  40  ASP D CA    1 
ATOM   13692 C  C     . ASP D 2 61  ? 155.944 101.917 122.210 1.00 39.38 ?  40  ASP D C     1 
ATOM   13693 O  O     . ASP D 2 61  ? 156.781 101.854 123.108 1.00 38.90 ?  40  ASP D O     1 
ATOM   13694 C  CB    . ASP D 2 61  ? 153.673 101.902 123.203 1.00 38.93 ?  40  ASP D CB    1 
ATOM   13695 C  CG    . ASP D 2 61  ? 152.762 102.755 124.039 1.00 38.21 ?  40  ASP D CG    1 
ATOM   13696 O  OD1   . ASP D 2 61  ? 152.902 103.998 124.023 1.00 38.79 ?  40  ASP D OD1   1 
ATOM   13697 O  OD2   . ASP D 2 61  ? 151.906 102.175 124.726 1.00 38.02 -1 40  ASP D OD2   1 
ATOM   13698 N  N     . LEU D 2 62  ? 156.085 101.303 121.039 1.00 39.82 ?  41  LEU D N     1 
ATOM   13699 C  CA    . LEU D 2 62  ? 157.249 100.484 120.726 1.00 40.22 ?  41  LEU D CA    1 
ATOM   13700 C  C     . LEU D 2 62  ? 158.536 101.309 120.714 1.00 40.40 ?  41  LEU D C     1 
ATOM   13701 O  O     . LEU D 2 62  ? 159.629 100.759 120.859 1.00 40.91 ?  41  LEU D O     1 
ATOM   13702 C  CB    . LEU D 2 62  ? 157.041 99.759  119.393 1.00 40.52 ?  41  LEU D CB    1 
ATOM   13703 C  CG    . LEU D 2 62  ? 155.917 98.717  119.360 1.00 41.03 ?  41  LEU D CG    1 
ATOM   13704 C  CD1   . LEU D 2 62  ? 155.754 98.147  117.958 1.00 42.53 ?  41  LEU D CD1   1 
ATOM   13705 C  CD2   . LEU D 2 62  ? 156.155 97.599  120.384 1.00 41.89 ?  41  LEU D CD2   1 
ATOM   13706 N  N     . LEU D 2 63  ? 158.385 102.628 120.564 1.00 40.20 ?  42  LEU D N     1 
ATOM   13707 C  CA    . LEU D 2 63  ? 159.497 103.577 120.550 1.00 39.85 ?  42  LEU D CA    1 
ATOM   13708 C  C     . LEU D 2 63  ? 160.073 103.864 121.950 1.00 38.90 ?  42  LEU D C     1 
ATOM   13709 O  O     . LEU D 2 63  ? 161.176 104.411 122.076 1.00 39.48 ?  42  LEU D O     1 
ATOM   13710 C  CB    . LEU D 2 63  ? 159.047 104.880 119.869 1.00 40.50 ?  42  LEU D CB    1 
ATOM   13711 C  CG    . LEU D 2 63  ? 160.008 105.743 119.036 1.00 41.98 ?  42  LEU D CG    1 
ATOM   13712 C  CD1   . LEU D 2 63  ? 160.675 104.957 117.912 1.00 43.07 ?  42  LEU D CD1   1 
ATOM   13713 C  CD2   . LEU D 2 63  ? 159.250 106.919 118.446 1.00 43.17 ?  42  LEU D CD2   1 
ATOM   13714 N  N     . THR D 2 64  ? 159.337 103.513 123.001 1.00 37.28 ?  43  THR D N     1 
ATOM   13715 C  CA    . THR D 2 64  ? 159.887 103.602 124.363 1.00 35.53 ?  43  THR D CA    1 
ATOM   13716 C  C     . THR D 2 64  ? 160.053 102.230 125.004 1.00 34.57 ?  43  THR D C     1 
ATOM   13717 O  O     . THR D 2 64  ? 160.936 102.034 125.844 1.00 34.23 ?  43  THR D O     1 
ATOM   13718 C  CB    . THR D 2 64  ? 159.080 104.534 125.295 1.00 35.18 ?  43  THR D CB    1 
ATOM   13719 O  OG1   . THR D 2 64  ? 157.683 104.233 125.213 1.00 34.59 ?  43  THR D OG1   1 
ATOM   13720 C  CG2   . THR D 2 64  ? 159.303 105.973 124.921 1.00 35.48 ?  43  THR D CG2   1 
ATOM   13721 N  N     . TRP D 2 65  ? 159.206 101.287 124.591 1.00 33.62 ?  44  TRP D N     1 
ATOM   13722 C  CA    . TRP D 2 65  ? 159.249 99.899  125.080 1.00 32.87 ?  44  TRP D CA    1 
ATOM   13723 C  C     . TRP D 2 65  ? 160.616 99.248  124.832 1.00 33.46 ?  44  TRP D C     1 
ATOM   13724 O  O     . TRP D 2 65  ? 161.162 98.583  125.714 1.00 32.58 ?  44  TRP D O     1 
ATOM   13725 C  CB    . TRP D 2 65  ? 158.134 99.078  124.413 1.00 32.09 ?  44  TRP D CB    1 
ATOM   13726 C  CG    . TRP D 2 65  ? 158.113 97.621  124.782 1.00 30.42 ?  44  TRP D CG    1 
ATOM   13727 C  CD1   . TRP D 2 65  ? 158.498 96.573  123.993 1.00 29.35 ?  44  TRP D CD1   1 
ATOM   13728 C  CD2   . TRP D 2 65  ? 157.678 97.048  126.026 1.00 28.04 ?  44  TRP D CD2   1 
ATOM   13729 N  NE1   . TRP D 2 65  ? 158.331 95.385  124.666 1.00 28.44 ?  44  TRP D NE1   1 
ATOM   13730 C  CE2   . TRP D 2 65  ? 157.833 95.648  125.916 1.00 28.14 ?  44  TRP D CE2   1 
ATOM   13731 C  CE3   . TRP D 2 65  ? 157.182 97.581  127.223 1.00 27.11 ?  44  TRP D CE3   1 
ATOM   13732 C  CZ2   . TRP D 2 65  ? 157.502 94.768  126.956 1.00 27.21 ?  44  TRP D CZ2   1 
ATOM   13733 C  CZ3   . TRP D 2 65  ? 156.844 96.704  128.258 1.00 27.45 ?  44  TRP D CZ3   1 
ATOM   13734 C  CH2   . TRP D 2 65  ? 157.002 95.312  128.110 1.00 27.25 ?  44  TRP D CH2   1 
ATOM   13735 N  N     . LYS D 2 66  ? 161.151 99.458  123.631 1.00 34.52 ?  45  LYS D N     1 
ATOM   13736 C  CA    . LYS D 2 66  ? 162.453 98.930  123.234 1.00 36.41 ?  45  LYS D CA    1 
ATOM   13737 C  C     . LYS D 2 66  ? 163.612 99.422  124.099 1.00 36.26 ?  45  LYS D C     1 
ATOM   13738 O  O     . LYS D 2 66  ? 164.663 98.783  124.139 1.00 36.52 ?  45  LYS D O     1 
ATOM   13739 C  CB    . LYS D 2 66  ? 162.733 99.241  121.758 1.00 36.98 ?  45  LYS D CB    1 
ATOM   13740 C  CG    . LYS D 2 66  ? 162.513 98.056  120.821 1.00 40.03 ?  45  LYS D CG    1 
ATOM   13741 C  CD    . LYS D 2 66  ? 161.031 97.693  120.667 1.00 43.70 ?  45  LYS D CD    1 
ATOM   13742 C  CE    . LYS D 2 66  ? 160.839 96.539  119.679 1.00 45.57 ?  45  LYS D CE    1 
ATOM   13743 N  NZ    . LYS D 2 66  ? 161.307 96.871  118.301 1.00 46.59 1  45  LYS D NZ    1 
ATOM   13744 N  N     . TYR D 2 67  ? 163.412 100.538 124.795 1.00 36.26 ?  46  TYR D N     1 
ATOM   13745 C  CA    . TYR D 2 67  ? 164.471 101.106 125.636 1.00 36.90 ?  46  TYR D CA    1 
ATOM   13746 C  C     . TYR D 2 67  ? 164.408 100.708 127.113 1.00 36.28 ?  46  TYR D C     1 
ATOM   13747 O  O     . TYR D 2 67  ? 165.266 101.114 127.891 1.00 36.44 ?  46  TYR D O     1 
ATOM   13748 C  CB    . TYR D 2 67  ? 164.542 102.630 125.489 1.00 37.15 ?  46  TYR D CB    1 
ATOM   13749 C  CG    . TYR D 2 67  ? 164.758 103.092 124.067 1.00 39.40 ?  46  TYR D CG    1 
ATOM   13750 C  CD1   . TYR D 2 67  ? 165.686 102.455 123.239 1.00 41.26 ?  46  TYR D CD1   1 
ATOM   13751 C  CD2   . TYR D 2 67  ? 164.057 104.179 123.556 1.00 41.06 ?  46  TYR D CD2   1 
ATOM   13752 C  CE1   . TYR D 2 67  ? 165.889 102.874 121.925 1.00 43.03 ?  46  TYR D CE1   1 
ATOM   13753 C  CE2   . TYR D 2 67  ? 164.257 104.613 122.243 1.00 43.05 ?  46  TYR D CE2   1 
ATOM   13754 C  CZ    . TYR D 2 67  ? 165.173 103.959 121.434 1.00 43.80 ?  46  TYR D CZ    1 
ATOM   13755 O  OH    . TYR D 2 67  ? 165.366 104.388 120.134 1.00 45.18 ?  46  TYR D OH    1 
ATOM   13756 N  N     . LEU D 2 68  ? 163.399 99.931  127.501 1.00 35.71 ?  47  LEU D N     1 
ATOM   13757 C  CA    . LEU D 2 68  ? 163.315 99.446  128.880 1.00 34.92 ?  47  LEU D CA    1 
ATOM   13758 C  C     . LEU D 2 68  ? 164.197 98.210  129.076 1.00 34.32 ?  47  LEU D C     1 
ATOM   13759 O  O     . LEU D 2 68  ? 164.375 97.410  128.154 1.00 34.50 ?  47  LEU D O     1 
ATOM   13760 C  CB    . LEU D 2 68  ? 161.864 99.136  129.279 1.00 35.00 ?  47  LEU D CB    1 
ATOM   13761 C  CG    . LEU D 2 68  ? 160.774 100.200 129.067 1.00 35.82 ?  47  LEU D CG    1 
ATOM   13762 C  CD1   . LEU D 2 68  ? 159.428 99.668  129.538 1.00 35.95 ?  47  LEU D CD1   1 
ATOM   13763 C  CD2   . LEU D 2 68  ? 161.094 101.526 129.756 1.00 35.97 ?  47  LEU D CD2   1 
ATOM   13764 N  N     . GLY D 2 69  ? 164.744 98.063  130.282 1.00 33.50 ?  48  GLY D N     1 
ATOM   13765 C  CA    . GLY D 2 69  ? 165.469 96.857  130.671 1.00 32.41 ?  48  GLY D CA    1 
ATOM   13766 C  C     . GLY D 2 69  ? 164.565 95.636  130.770 1.00 32.15 ?  48  GLY D C     1 
ATOM   13767 O  O     . GLY D 2 69  ? 163.333 95.755  130.776 1.00 30.98 ?  48  GLY D O     1 
ATOM   13768 N  N     . LYS D 2 70  ? 165.183 94.460  130.859 1.00 32.14 ?  49  LYS D N     1 
ATOM   13769 C  CA    . LYS D 2 70  ? 164.448 93.204  130.971 1.00 32.25 ?  49  LYS D CA    1 
ATOM   13770 C  C     . LYS D 2 70  ? 163.558 93.154  132.211 1.00 31.24 ?  49  LYS D C     1 
ATOM   13771 O  O     . LYS D 2 70  ? 162.419 92.700  132.118 1.00 31.34 ?  49  LYS D O     1 
ATOM   13772 C  CB    . LYS D 2 70  ? 165.403 92.007  130.958 1.00 33.07 ?  49  LYS D CB    1 
ATOM   13773 C  CG    . LYS D 2 70  ? 166.202 91.871  129.671 1.00 35.74 ?  49  LYS D CG    1 
ATOM   13774 C  CD    . LYS D 2 70  ? 167.320 90.848  129.850 1.00 39.67 ?  49  LYS D CD    1 
ATOM   13775 C  CE    . LYS D 2 70  ? 168.326 90.922  128.712 1.00 40.96 ?  49  LYS D CE    1 
ATOM   13776 N  NZ    . LYS D 2 70  ? 169.542 90.144  129.056 1.00 42.55 1  49  LYS D NZ    1 
ATOM   13777 N  N     . ASN D 2 71  ? 164.067 93.625  133.354 1.00 29.92 ?  50  ASN D N     1 
ATOM   13778 C  CA    . ASN D 2 71  ? 163.287 93.642  134.597 1.00 29.37 ?  50  ASN D CA    1 
ATOM   13779 C  C     . ASN D 2 71  ? 162.069 94.553  134.492 1.00 28.35 ?  50  ASN D C     1 
ATOM   13780 O  O     . ASN D 2 71  ? 160.990 94.204  134.986 1.00 27.64 ?  50  ASN D O     1 
ATOM   13781 C  CB    . ASN D 2 71  ? 164.135 94.038  135.821 1.00 29.38 ?  50  ASN D CB    1 
ATOM   13782 C  CG    . ASN D 2 71  ? 165.050 92.915  136.304 1.00 31.22 ?  50  ASN D CG    1 
ATOM   13783 O  OD1   . ASN D 2 71  ? 164.737 91.729  136.174 1.00 33.03 ?  50  ASN D OD1   1 
ATOM   13784 N  ND2   . ASN D 2 71  ? 166.188 93.291  136.879 1.00 31.97 ?  50  ASN D ND2   1 
ATOM   13785 N  N     . GLU D 2 72  ? 162.243 95.706  133.841 1.00 27.72 ?  51  GLU D N     1 
ATOM   13786 C  CA    . GLU D 2 72  ? 161.131 96.645  133.624 1.00 27.70 ?  51  GLU D CA    1 
ATOM   13787 C  C     . GLU D 2 72  ? 160.054 96.041  132.719 1.00 27.62 ?  51  GLU D C     1 
ATOM   13788 O  O     . GLU D 2 72  ? 158.856 96.178  132.985 1.00 27.56 ?  51  GLU D O     1 
ATOM   13789 C  CB    . GLU D 2 72  ? 161.623 97.966  133.024 1.00 27.55 ?  51  GLU D CB    1 
ATOM   13790 C  CG    . GLU D 2 72  ? 162.650 98.723  133.876 1.00 28.77 ?  51  GLU D CG    1 
ATOM   13791 C  CD    . GLU D 2 72  ? 162.989 100.075 133.273 1.00 31.18 ?  51  GLU D CD    1 
ATOM   13792 O  OE1   . GLU D 2 72  ? 163.684 100.109 132.236 1.00 33.17 ?  51  GLU D OE1   1 
ATOM   13793 O  OE2   . GLU D 2 72  ? 162.552 101.101 133.832 1.00 31.66 -1 51  GLU D OE2   1 
ATOM   13794 N  N     . GLN D 2 73  ? 160.490 95.375  131.654 1.00 27.32 ?  52  GLN D N     1 
ATOM   13795 C  CA    . GLN D 2 73  ? 159.572 94.743  130.712 1.00 27.33 ?  52  GLN D CA    1 
ATOM   13796 C  C     . GLN D 2 73  ? 158.846 93.574  131.383 1.00 26.85 ?  52  GLN D C     1 
ATOM   13797 O  O     . GLN D 2 73  ? 157.636 93.404  131.206 1.00 26.24 ?  52  GLN D O     1 
ATOM   13798 C  CB    . GLN D 2 73  ? 160.312 94.282  129.462 1.00 27.65 ?  52  GLN D CB    1 
ATOM   13799 C  CG    . GLN D 2 73  ? 160.743 95.415  128.511 1.00 29.66 ?  52  GLN D CG    1 
ATOM   13800 C  CD    . GLN D 2 73  ? 161.306 94.903  127.186 1.00 32.60 ?  52  GLN D CD    1 
ATOM   13801 O  OE1   . GLN D 2 73  ? 161.733 93.756  127.080 1.00 34.76 ?  52  GLN D OE1   1 
ATOM   13802 N  NE2   . GLN D 2 73  ? 161.322 95.761  126.177 1.00 33.42 ?  52  GLN D NE2   1 
ATOM   13803 N  N     . ASP D 2 74  ? 159.589 92.807  132.178 1.00 26.26 ?  53  ASP D N     1 
ATOM   13804 C  CA    . ASP D 2 74  ? 159.053 91.671  132.937 1.00 26.50 ?  53  ASP D CA    1 
ATOM   13805 C  C     . ASP D 2 74  ? 158.011 92.124  133.949 1.00 25.81 ?  53  ASP D C     1 
ATOM   13806 O  O     . ASP D 2 74  ? 156.928 91.549  134.024 1.00 26.12 ?  53  ASP D O     1 
ATOM   13807 C  CB    . ASP D 2 74  ? 160.196 90.943  133.658 1.00 26.84 ?  53  ASP D CB    1 
ATOM   13808 C  CG    . ASP D 2 74  ? 159.750 89.657  134.354 1.00 29.50 ?  53  ASP D CG    1 
ATOM   13809 O  OD1   . ASP D 2 74  ? 159.312 88.707  133.670 1.00 32.08 ?  53  ASP D OD1   1 
ATOM   13810 O  OD2   . ASP D 2 74  ? 159.884 89.579  135.592 1.00 33.52 -1 53  ASP D OD2   1 
ATOM   13811 N  N     . THR D 2 75  ? 158.332 93.157  134.728 1.00 25.10 ?  54  THR D N     1 
ATOM   13812 C  CA    . THR D 2 75  ? 157.389 93.670  135.726 1.00 24.11 ?  54  THR D CA    1 
ATOM   13813 C  C     . THR D 2 75  ? 156.115 94.180  135.047 1.00 23.82 ?  54  THR D C     1 
ATOM   13814 O  O     . THR D 2 75  ? 155.007 93.841  135.464 1.00 23.81 ?  54  THR D O     1 
ATOM   13815 C  CB    . THR D 2 75  ? 158.027 94.760  136.610 1.00 23.80 ?  54  THR D CB    1 
ATOM   13816 O  OG1   . THR D 2 75  ? 159.114 94.185  137.348 1.00 24.62 ?  54  THR D OG1   1 
ATOM   13817 C  CG2   . THR D 2 75  ? 156.998 95.338  137.598 1.00 23.25 ?  54  THR D CG2   1 
ATOM   13818 N  N     . TYR D 2 76  ? 156.282 94.997  134.017 1.00 24.06 ?  55  TYR D N     1 
ATOM   13819 C  CA    . TYR D 2 76  ? 155.151 95.515  133.254 1.00 24.76 ?  55  TYR D CA    1 
ATOM   13820 C  C     . TYR D 2 76  ? 154.225 94.405  132.735 1.00 24.85 ?  55  TYR D C     1 
ATOM   13821 O  O     . TYR D 2 76  ? 153.006 94.479  132.915 1.00 24.83 ?  55  TYR D O     1 
ATOM   13822 C  CB    . TYR D 2 76  ? 155.628 96.383  132.090 1.00 24.78 ?  55  TYR D CB    1 
ATOM   13823 C  CG    . TYR D 2 76  ? 154.560 97.328  131.578 1.00 26.19 ?  55  TYR D CG    1 
ATOM   13824 C  CD1   . TYR D 2 76  ? 154.444 98.615  132.107 1.00 27.81 ?  55  TYR D CD1   1 
ATOM   13825 C  CD2   . TYR D 2 76  ? 153.659 96.939  130.582 1.00 28.03 ?  55  TYR D CD2   1 
ATOM   13826 C  CE1   . TYR D 2 76  ? 153.472 99.496  131.653 1.00 29.32 ?  55  TYR D CE1   1 
ATOM   13827 C  CE2   . TYR D 2 76  ? 152.671 97.820  130.117 1.00 29.01 ?  55  TYR D CE2   1 
ATOM   13828 C  CZ    . TYR D 2 76  ? 152.590 99.096  130.664 1.00 30.76 ?  55  TYR D CZ    1 
ATOM   13829 O  OH    . TYR D 2 76  ? 151.641 99.992  130.230 1.00 34.50 ?  55  TYR D OH    1 
ATOM   13830 N  N     . MET D 2 77  ? 154.806 93.391  132.095 1.00 25.76 ?  56  MET D N     1 
ATOM   13831 C  CA    . MET D 2 77  ? 154.036 92.248  131.593 1.00 26.81 ?  56  MET D CA    1 
ATOM   13832 C  C     . MET D 2 77  ? 153.246 91.559  132.710 1.00 26.23 ?  56  MET D C     1 
ATOM   13833 O  O     . MET D 2 77  ? 152.059 91.265  132.553 1.00 25.00 ?  56  MET D O     1 
ATOM   13834 C  CB    . MET D 2 77  ? 154.950 91.235  130.907 1.00 28.11 ?  56  MET D CB    1 
ATOM   13835 C  CG    . MET D 2 77  ? 155.557 91.699  129.577 1.00 32.52 ?  56  MET D CG    1 
ATOM   13836 S  SD    . MET D 2 77  ? 154.381 91.757  128.215 1.00 42.68 ?  56  MET D SD    1 
ATOM   13837 C  CE    . MET D 2 77  ? 153.657 93.387  128.393 1.00 38.97 ?  56  MET D CE    1 
ATOM   13838 N  N     . LYS D 2 78  ? 153.922 91.302  133.831 1.00 26.01 ?  57  LYS D N     1 
ATOM   13839 C  CA    . LYS D 2 78  ? 153.310 90.604  134.965 1.00 26.07 ?  57  LYS D CA    1 
ATOM   13840 C  C     . LYS D 2 78  ? 152.187 91.416  135.608 1.00 25.69 ?  57  LYS D C     1 
ATOM   13841 O  O     . LYS D 2 78  ? 151.147 90.864  135.987 1.00 25.58 ?  57  LYS D O     1 
ATOM   13842 C  CB    . LYS D 2 78  ? 154.365 90.223  136.012 1.00 26.08 ?  57  LYS D CB    1 
ATOM   13843 C  CG    . LYS D 2 78  ? 155.327 89.121  135.547 1.00 27.64 ?  57  LYS D CG    1 
ATOM   13844 C  CD    . LYS D 2 78  ? 156.455 88.904  136.549 1.00 29.47 ?  57  LYS D CD    1 
ATOM   13845 C  CE    . LYS D 2 78  ? 157.270 87.675  136.180 1.00 31.69 ?  57  LYS D CE    1 
ATOM   13846 N  NZ    . LYS D 2 78  ? 158.369 87.416  137.149 1.00 33.36 1  57  LYS D NZ    1 
ATOM   13847 N  N     . VAL D 2 79  ? 152.405 92.723  135.731 1.00 25.32 ?  58  VAL D N     1 
ATOM   13848 C  CA    . VAL D 2 79  ? 151.406 93.638  136.294 1.00 25.47 ?  58  VAL D CA    1 
ATOM   13849 C  C     . VAL D 2 79  ? 150.184 93.668  135.381 1.00 25.09 ?  58  VAL D C     1 
ATOM   13850 O  O     . VAL D 2 79  ? 149.044 93.542  135.836 1.00 24.46 ?  58  VAL D O     1 
ATOM   13851 C  CB    . VAL D 2 79  ? 152.009 95.061  136.462 1.00 25.83 ?  58  VAL D CB    1 
ATOM   13852 C  CG1   . VAL D 2 79  ? 150.943 96.130  136.397 1.00 27.35 ?  58  VAL D CG1   1 
ATOM   13853 C  CG2   . VAL D 2 79  ? 152.819 95.138  137.756 1.00 26.42 ?  58  VAL D CG2   1 
ATOM   13854 N  N     . LEU D 2 80  ? 150.447 93.787  134.082 1.00 25.27 ?  59  LEU D N     1 
ATOM   13855 C  CA    . LEU D 2 80  ? 149.398 93.872  133.090 1.00 25.55 ?  59  LEU D CA    1 
ATOM   13856 C  C     . LEU D 2 80  ? 148.531 92.615  133.123 1.00 24.94 ?  59  LEU D C     1 
ATOM   13857 O  O     . LEU D 2 80  ? 147.306 92.710  133.083 1.00 24.82 ?  59  LEU D O     1 
ATOM   13858 C  CB    . LEU D 2 80  ? 150.005 94.065  131.699 1.00 25.80 ?  59  LEU D CB    1 
ATOM   13859 C  CG    . LEU D 2 80  ? 149.644 95.263  130.814 1.00 28.76 ?  59  LEU D CG    1 
ATOM   13860 C  CD1   . LEU D 2 80  ? 149.730 94.821  129.352 1.00 30.25 ?  59  LEU D CD1   1 
ATOM   13861 C  CD2   . LEU D 2 80  ? 148.283 95.874  131.102 1.00 27.79 ?  59  LEU D CD2   1 
ATOM   13862 N  N     . ALA D 2 81  ? 149.174 91.449  133.201 1.00 24.86 ?  60  ALA D N     1 
ATOM   13863 C  CA    . ALA D 2 81  ? 148.459 90.165  133.250 1.00 24.60 ?  60  ALA D CA    1 
ATOM   13864 C  C     . ALA D 2 81  ? 147.638 90.053  134.531 1.00 23.80 ?  60  ALA D C     1 
ATOM   13865 O  O     . ALA D 2 81  ? 146.527 89.538  134.521 1.00 24.07 ?  60  ALA D O     1 
ATOM   13866 C  CB    . ALA D 2 81  ? 149.440 88.999  133.139 1.00 24.48 ?  60  ALA D CB    1 
ATOM   13867 N  N     . GLY D 2 82  ? 148.194 90.548  135.631 1.00 23.54 ?  61  GLY D N     1 
ATOM   13868 C  CA    . GLY D 2 82  ? 147.482 90.599  136.903 1.00 22.53 ?  61  GLY D CA    1 
ATOM   13869 C  C     . GLY D 2 82  ? 146.197 91.393  136.790 1.00 22.23 ?  61  GLY D C     1 
ATOM   13870 O  O     . GLY D 2 82  ? 145.133 90.927  137.197 1.00 21.27 ?  61  GLY D O     1 
ATOM   13871 N  N     . LEU D 2 83  ? 146.293 92.598  136.229 1.00 22.36 ?  62  LEU D N     1 
ATOM   13872 C  CA    . LEU D 2 83  ? 145.112 93.446  136.031 1.00 22.42 ?  62  LEU D CA    1 
ATOM   13873 C  C     . LEU D 2 83  ? 144.097 92.777  135.115 1.00 22.91 ?  62  LEU D C     1 
ATOM   13874 O  O     . LEU D 2 83  ? 142.891 92.795  135.394 1.00 22.99 ?  62  LEU D O     1 
ATOM   13875 C  CB    . LEU D 2 83  ? 145.501 94.815  135.457 1.00 22.19 ?  62  LEU D CB    1 
ATOM   13876 C  CG    . LEU D 2 83  ? 146.352 95.726  136.356 1.00 22.17 ?  62  LEU D CG    1 
ATOM   13877 C  CD1   . LEU D 2 83  ? 146.939 96.875  135.525 1.00 21.55 ?  62  LEU D CD1   1 
ATOM   13878 C  CD2   . LEU D 2 83  ? 145.507 96.257  137.500 1.00 22.42 ?  62  LEU D CD2   1 
ATOM   13879 N  N     . THR D 2 84  ? 144.590 92.171  134.039 1.00 23.39 ?  63  THR D N     1 
ATOM   13880 C  CA    . THR D 2 84  ? 143.721 91.521  133.061 1.00 24.42 ?  63  THR D CA    1 
ATOM   13881 C  C     . THR D 2 84  ? 142.908 90.398  133.710 1.00 24.55 ?  63  THR D C     1 
ATOM   13882 O  O     . THR D 2 84  ? 141.686 90.335  133.558 1.00 23.68 ?  63  THR D O     1 
ATOM   13883 C  CB    . THR D 2 84  ? 144.524 90.957  131.861 1.00 24.70 ?  63  THR D CB    1 
ATOM   13884 O  OG1   . THR D 2 84  ? 145.233 92.025  131.218 1.00 25.57 ?  63  THR D OG1   1 
ATOM   13885 C  CG2   . THR D 2 84  ? 143.586 90.322  130.848 1.00 25.36 ?  63  THR D CG2   1 
ATOM   13886 N  N     . LEU D 2 85  ? 143.609 89.530  134.431 1.00 25.38 ?  64  LEU D N     1 
ATOM   13887 C  CA    . LEU D 2 85  ? 142.987 88.391  135.093 1.00 26.44 ?  64  LEU D CA    1 
ATOM   13888 C  C     . LEU D 2 85  ? 141.946 88.821  136.131 1.00 25.96 ?  64  LEU D C     1 
ATOM   13889 O  O     . LEU D 2 85  ? 140.825 88.292  136.129 1.00 25.83 ?  64  LEU D O     1 
ATOM   13890 C  CB    . LEU D 2 85  ? 144.047 87.438  135.667 1.00 26.65 ?  64  LEU D CB    1 
ATOM   13891 C  CG    . LEU D 2 85  ? 144.718 86.578  134.578 1.00 29.62 ?  64  LEU D CG    1 
ATOM   13892 C  CD1   . LEU D 2 85  ? 146.086 86.080  135.006 1.00 31.57 ?  64  LEU D CD1   1 
ATOM   13893 C  CD2   . LEU D 2 85  ? 143.834 85.390  134.154 1.00 30.96 ?  64  LEU D CD2   1 
ATOM   13894 N  N     . LEU D 2 86  ? 142.281 89.801  136.974 1.00 25.63 ?  65  LEU D N     1 
ATOM   13895 C  CA    . LEU D 2 86  ? 141.310 90.305  137.948 1.00 25.59 ?  65  LEU D CA    1 
ATOM   13896 C  C     . LEU D 2 86  ? 140.096 90.972  137.305 1.00 25.60 ?  65  LEU D C     1 
ATOM   13897 O  O     . LEU D 2 86  ? 138.970 90.829  137.790 1.00 25.47 ?  65  LEU D O     1 
ATOM   13898 C  CB    . LEU D 2 86  ? 141.959 91.246  138.981 1.00 25.76 ?  65  LEU D CB    1 
ATOM   13899 C  CG    . LEU D 2 86  ? 142.926 90.593  139.978 1.00 26.71 ?  65  LEU D CG    1 
ATOM   13900 C  CD1   . LEU D 2 86  ? 143.749 91.636  140.728 1.00 28.01 ?  65  LEU D CD1   1 
ATOM   13901 C  CD2   . LEU D 2 86  ? 142.194 89.708  140.960 1.00 28.01 ?  65  LEU D CD2   1 
ATOM   13902 N  N     . ASP D 2 87  ? 140.319 91.709  136.223 1.00 25.49 ?  66  ASP D N     1 
ATOM   13903 C  CA    . ASP D 2 87  ? 139.233 92.433  135.584 1.00 25.83 ?  66  ASP D CA    1 
ATOM   13904 C  C     . ASP D 2 87  ? 138.245 91.493  134.878 1.00 26.20 ?  66  ASP D C     1 
ATOM   13905 O  O     . ASP D 2 87  ? 137.057 91.784  134.797 1.00 25.99 ?  66  ASP D O     1 
ATOM   13906 C  CB    . ASP D 2 87  ? 139.778 93.479  134.620 1.00 25.50 ?  66  ASP D CB    1 
ATOM   13907 C  CG    . ASP D 2 87  ? 138.887 94.685  134.530 1.00 25.76 ?  66  ASP D CG    1 
ATOM   13908 O  OD1   . ASP D 2 87  ? 138.182 94.975  135.526 1.00 26.91 ?  66  ASP D OD1   1 
ATOM   13909 O  OD2   . ASP D 2 87  ? 138.884 95.349  133.475 1.00 23.11 -1 66  ASP D OD2   1 
ATOM   13910 N  N     . THR D 2 88  ? 138.750 90.360  134.396 1.00 27.12 ?  67  THR D N     1 
ATOM   13911 C  CA    . THR D 2 88  ? 137.921 89.323  133.796 1.00 28.40 ?  67  THR D CA    1 
ATOM   13912 C  C     . THR D 2 88  ? 136.957 88.729  134.810 1.00 28.28 ?  67  THR D C     1 
ATOM   13913 O  O     . THR D 2 88  ? 135.791 88.501  134.496 1.00 28.10 ?  67  THR D O     1 
ATOM   13914 C  CB    . THR D 2 88  ? 138.778 88.207  133.169 1.00 29.04 ?  67  THR D CB    1 
ATOM   13915 O  OG1   . THR D 2 88  ? 139.621 88.780  132.166 1.00 31.00 ?  67  THR D OG1   1 
ATOM   13916 C  CG2   . THR D 2 88  ? 137.893 87.149  132.514 1.00 30.16 ?  67  THR D CG2   1 
ATOM   13917 N  N     . GLU D 2 89  ? 137.437 88.482  136.028 1.00 28.28 ?  68  GLU D N     1 
ATOM   13918 C  CA    . GLU D 2 89  ? 136.555 88.010  137.090 1.00 29.16 ?  68  GLU D CA    1 
ATOM   13919 C  C     . GLU D 2 89  ? 135.447 89.030  137.340 1.00 28.65 ?  68  GLU D C     1 
ATOM   13920 O  O     . GLU D 2 89  ? 134.294 88.661  137.516 1.00 28.44 ?  68  GLU D O     1 
ATOM   13921 C  CB    . GLU D 2 89  ? 137.325 87.737  138.390 1.00 29.32 ?  68  GLU D CB    1 
ATOM   13922 C  CG    . GLU D 2 89  ? 138.421 86.669  138.274 1.00 31.95 ?  68  GLU D CG    1 
ATOM   13923 C  CD    . GLU D 2 89  ? 137.896 85.275  137.945 1.00 35.19 ?  68  GLU D CD    1 
ATOM   13924 O  OE1   . GLU D 2 89  ? 136.681 85.011  138.095 1.00 35.47 ?  68  GLU D OE1   1 
ATOM   13925 O  OE2   . GLU D 2 89  ? 138.716 84.433  137.525 1.00 38.06 -1 68  GLU D OE2   1 
ATOM   13926 N  N     . GLN D 2 90  ? 135.801 90.313  137.334 1.00 28.45 ?  69  GLN D N     1 
ATOM   13927 C  CA    . GLN D 2 90  ? 134.819 91.368  137.587 1.00 28.47 ?  69  GLN D CA    1 
ATOM   13928 C  C     . GLN D 2 90  ? 133.762 91.446  136.476 1.00 28.97 ?  69  GLN D C     1 
ATOM   13929 O  O     . GLN D 2 90  ? 132.583 91.656  136.755 1.00 28.84 ?  69  GLN D O     1 
ATOM   13930 C  CB    . GLN D 2 90  ? 135.512 92.716  137.804 1.00 28.21 ?  69  GLN D CB    1 
ATOM   13931 C  CG    . GLN D 2 90  ? 134.643 93.777  138.477 1.00 27.75 ?  69  GLN D CG    1 
ATOM   13932 C  CD    . GLN D 2 90  ? 134.376 93.515  139.954 1.00 28.91 ?  69  GLN D CD    1 
ATOM   13933 O  OE1   . GLN D 2 90  ? 134.476 92.380  140.440 1.00 27.62 ?  69  GLN D OE1   1 
ATOM   13934 N  NE2   . GLN D 2 90  ? 134.007 94.574  140.677 1.00 28.23 ?  69  GLN D NE2   1 
ATOM   13935 N  N     . GLY D 2 91  ? 134.187 91.250  135.227 1.00 29.62 ?  70  GLY D N     1 
ATOM   13936 C  CA    . GLY D 2 91  ? 133.269 91.244  134.086 1.00 30.43 ?  70  GLY D CA    1 
ATOM   13937 C  C     . GLY D 2 91  ? 132.375 90.013  133.987 1.00 31.11 ?  70  GLY D C     1 
ATOM   13938 O  O     . GLY D 2 91  ? 131.189 90.114  133.656 1.00 30.77 ?  70  GLY D O     1 
ATOM   13939 N  N     . ASN D 2 92  ? 132.940 88.846  134.260 1.00 31.69 ?  71  ASN D N     1 
ATOM   13940 C  CA    . ASN D 2 92  ? 132.170 87.612  134.157 1.00 32.72 ?  71  ASN D CA    1 
ATOM   13941 C  C     . ASN D 2 92  ? 131.306 87.285  135.367 1.00 32.60 ?  71  ASN D C     1 
ATOM   13942 O  O     . ASN D 2 92  ? 130.261 86.647  135.217 1.00 33.12 ?  71  ASN D O     1 
ATOM   13943 C  CB    . ASN D 2 92  ? 133.081 86.439  133.824 1.00 33.68 ?  71  ASN D CB    1 
ATOM   13944 C  CG    . ASN D 2 92  ? 133.585 86.490  132.397 1.00 35.15 ?  71  ASN D CG    1 
ATOM   13945 O  OD1   . ASN D 2 92  ? 134.650 85.963  132.097 1.00 40.21 ?  71  ASN D OD1   1 
ATOM   13946 N  ND2   . ASN D 2 92  ? 132.826 87.136  131.510 1.00 36.91 ?  71  ASN D ND2   1 
ATOM   13947 N  N     . THR D 2 93  ? 131.729 87.739  136.547 1.00 31.76 ?  72  THR D N     1 
ATOM   13948 C  CA    . THR D 2 93  ? 131.058 87.380  137.791 1.00 31.47 ?  72  THR D CA    1 
ATOM   13949 C  C     . THR D 2 93  ? 130.684 88.577  138.661 1.00 30.62 ?  72  THR D C     1 
ATOM   13950 O  O     . THR D 2 93  ? 129.511 88.771  138.968 1.00 30.71 ?  72  THR D O     1 
ATOM   13951 C  CB    . THR D 2 93  ? 131.906 86.403  138.601 1.00 31.60 ?  72  THR D CB    1 
ATOM   13952 O  OG1   . THR D 2 93  ? 132.207 85.262  137.786 1.00 33.14 ?  72  THR D OG1   1 
ATOM   13953 C  CG2   . THR D 2 93  ? 131.165 85.954  139.850 1.00 31.89 ?  72  THR D CG2   1 
ATOM   13954 N  N     . GLY D 2 94  ? 131.680 89.372  139.048 1.00 29.61 ?  73  GLY D N     1 
ATOM   13955 C  CA    . GLY D 2 94  ? 131.488 90.462  140.006 1.00 28.47 ?  73  GLY D CA    1 
ATOM   13956 C  C     . GLY D 2 94  ? 130.359 91.424  139.698 1.00 27.90 ?  73  GLY D C     1 
ATOM   13957 O  O     . GLY D 2 94  ? 129.466 91.644  140.528 1.00 28.27 ?  73  GLY D O     1 
ATOM   13958 N  N     . MET D 2 95  ? 130.393 92.030  138.520 1.00 26.67 ?  74  MET D N     1 
ATOM   13959 C  CA    . MET D 2 95  ? 129.334 92.980  138.186 1.00 26.00 ?  74  MET D CA    1 
ATOM   13960 C  C     . MET D 2 95  ? 128.019 92.278  137.866 1.00 25.25 ?  74  MET D C     1 
ATOM   13961 O  O     . MET D 2 95  ? 126.978 92.727  138.326 1.00 24.97 ?  74  MET D O     1 
ATOM   13962 C  CB    . MET D 2 95  ? 129.734 93.946  137.064 1.00 26.00 ?  74  MET D CB    1 
ATOM   13963 C  CG    . MET D 2 95  ? 130.612 95.085  137.522 1.00 26.40 ?  74  MET D CG    1 
ATOM   13964 S  SD    . MET D 2 95  ? 129.841 96.160  138.758 1.00 28.10 ?  74  MET D SD    1 
ATOM   13965 C  CE    . MET D 2 95  ? 131.243 97.201  139.144 1.00 28.95 ?  74  MET D CE    1 
ATOM   13966 N  N     . PRO D 2 96  ? 128.057 91.188  137.076 1.00 24.98 ?  75  PRO D N     1 
ATOM   13967 C  CA    . PRO D 2 96  ? 126.751 90.570  136.783 1.00 24.59 ?  75  PRO D CA    1 
ATOM   13968 C  C     . PRO D 2 96  ? 126.055 89.968  138.001 1.00 23.90 ?  75  PRO D C     1 
ATOM   13969 O  O     . PRO D 2 96  ? 124.830 89.971  138.045 1.00 23.45 ?  75  PRO D O     1 
ATOM   13970 C  CB    . PRO D 2 96  ? 127.092 89.464  135.776 1.00 24.80 ?  75  PRO D CB    1 
ATOM   13971 C  CG    . PRO D 2 96  ? 128.373 89.930  135.123 1.00 25.75 ?  75  PRO D CG    1 
ATOM   13972 C  CD    . PRO D 2 96  ? 129.129 90.646  136.213 1.00 25.07 ?  75  PRO D CD    1 
ATOM   13973 N  N     . ILE D 2 97  ? 126.815 89.451  138.970 1.00 23.36 ?  76  ILE D N     1 
ATOM   13974 C  CA    . ILE D 2 97  ? 126.197 88.837  140.141 1.00 23.48 ?  76  ILE D CA    1 
ATOM   13975 C  C     . ILE D 2 97  ? 125.554 89.893  141.025 1.00 23.30 ?  76  ILE D C     1 
ATOM   13976 O  O     . ILE D 2 97  ? 124.486 89.660  141.588 1.00 23.45 ?  76  ILE D O     1 
ATOM   13977 C  CB    . ILE D 2 97  ? 127.178 87.934  140.941 1.00 23.96 ?  76  ILE D CB    1 
ATOM   13978 C  CG1   . ILE D 2 97  ? 126.416 86.865  141.717 1.00 24.71 ?  76  ILE D CG1   1 
ATOM   13979 C  CG2   . ILE D 2 97  ? 128.101 88.752  141.876 1.00 24.02 ?  76  ILE D CG2   1 
ATOM   13980 C  CD1   . ILE D 2 97  ? 127.205 85.538  141.829 1.00 29.17 ?  76  ILE D CD1   1 
ATOM   13981 N  N     . VAL D 2 98  ? 126.195 91.056  141.135 1.00 22.71 ?  77  VAL D N     1 
ATOM   13982 C  CA    . VAL D 2 98  ? 125.633 92.167  141.920 1.00 22.78 ?  77  VAL D CA    1 
ATOM   13983 C  C     . VAL D 2 98  ? 124.385 92.725  141.233 1.00 22.89 ?  77  VAL D C     1 
ATOM   13984 O  O     . VAL D 2 98  ? 123.373 92.984  141.884 1.00 23.72 ?  77  VAL D O     1 
ATOM   13985 C  CB    . VAL D 2 98  ? 126.696 93.264  142.204 1.00 22.49 ?  77  VAL D CB    1 
ATOM   13986 C  CG1   . VAL D 2 98  ? 126.062 94.526  142.819 1.00 21.91 ?  77  VAL D CG1   1 
ATOM   13987 C  CG2   . VAL D 2 98  ? 127.760 92.715  143.139 1.00 23.02 ?  77  VAL D CG2   1 
ATOM   13988 N  N     . ALA D 2 99  ? 124.444 92.873  139.910 1.00 23.19 ?  78  ALA D N     1 
ATOM   13989 C  CA    . ALA D 2 99  ? 123.277 93.327  139.139 1.00 23.05 ?  78  ALA D CA    1 
ATOM   13990 C  C     . ALA D 2 99  ? 122.089 92.380  139.333 1.00 23.52 ?  78  ALA D C     1 
ATOM   13991 O  O     . ALA D 2 99  ? 120.934 92.812  139.421 1.00 23.68 ?  78  ALA D O     1 
ATOM   13992 C  CB    . ALA D 2 99  ? 123.633 93.458  137.668 1.00 22.81 ?  78  ALA D CB    1 
ATOM   13993 N  N     . GLU D 2 100 ? 122.373 91.084  139.409 1.00 23.68 ?  79  GLU D N     1 
ATOM   13994 C  CA    . GLU D 2 100 ? 121.329 90.084  139.621 1.00 24.14 ?  79  GLU D CA    1 
ATOM   13995 C  C     . GLU D 2 100 ? 120.594 90.218  140.965 1.00 23.66 ?  79  GLU D C     1 
ATOM   13996 O  O     . GLU D 2 100 ? 119.368 90.089  141.025 1.00 22.94 ?  79  GLU D O     1 
ATOM   13997 C  CB    . GLU D 2 100 ? 121.927 88.683  139.483 1.00 24.47 ?  79  GLU D CB    1 
ATOM   13998 C  CG    . GLU D 2 100 ? 120.894 87.573  139.449 1.00 27.90 ?  79  GLU D CG    1 
ATOM   13999 C  CD    . GLU D 2 100 ? 121.522 86.191  139.491 1.00 32.30 ?  79  GLU D CD    1 
ATOM   14000 O  OE1   . GLU D 2 100 ? 122.687 86.041  139.060 1.00 32.88 ?  79  GLU D OE1   1 
ATOM   14001 O  OE2   . GLU D 2 100 ? 120.842 85.257  139.963 1.00 34.74 -1 79  GLU D OE2   1 
ATOM   14002 N  N     . HIS D 2 101 ? 121.340 90.466  142.040 1.00 23.62 ?  80  HIS D N     1 
ATOM   14003 C  CA    . HIS D 2 101 ? 120.751 90.506  143.391 1.00 23.99 ?  80  HIS D CA    1 
ATOM   14004 C  C     . HIS D 2 101 ? 120.251 91.874  143.876 1.00 24.35 ?  80  HIS D C     1 
ATOM   14005 O  O     . HIS D 2 101 ? 119.468 91.941  144.824 1.00 24.21 ?  80  HIS D O     1 
ATOM   14006 C  CB    . HIS D 2 101 ? 121.712 89.881  144.412 1.00 24.13 ?  80  HIS D CB    1 
ATOM   14007 C  CG    . HIS D 2 101 ? 121.937 88.414  144.195 1.00 24.76 ?  80  HIS D CG    1 
ATOM   14008 N  ND1   . HIS D 2 101 ? 121.199 87.443  144.841 1.00 25.68 ?  80  HIS D ND1   1 
ATOM   14009 C  CD2   . HIS D 2 101 ? 122.798 87.754  143.385 1.00 25.75 ?  80  HIS D CD2   1 
ATOM   14010 C  CE1   . HIS D 2 101 ? 121.602 86.249  144.441 1.00 26.21 ?  80  HIS D CE1   1 
ATOM   14011 N  NE2   . HIS D 2 101 ? 122.571 86.409  143.558 1.00 25.35 ?  80  HIS D NE2   1 
ATOM   14012 N  N     . VAL D 2 102 ? 120.706 92.957  143.247 1.00 24.50 ?  81  VAL D N     1 
ATOM   14013 C  CA    . VAL D 2 102 ? 120.245 94.299  143.599 1.00 25.50 ?  81  VAL D CA    1 
ATOM   14014 C  C     . VAL D 2 102 ? 118.836 94.541  143.035 1.00 26.14 ?  81  VAL D C     1 
ATOM   14015 O  O     . VAL D 2 102 ? 118.575 94.226  141.877 1.00 26.96 ?  81  VAL D O     1 
ATOM   14016 C  CB    . VAL D 2 102 ? 121.231 95.388  143.082 1.00 25.30 ?  81  VAL D CB    1 
ATOM   14017 C  CG1   . VAL D 2 102 ? 120.629 96.768  143.198 1.00 27.08 ?  81  VAL D CG1   1 
ATOM   14018 C  CG2   . VAL D 2 102 ? 122.532 95.336  143.867 1.00 25.41 ?  81  VAL D CG2   1 
ATOM   14019 N  N     . ASP D 2 103 ? 117.940 95.078  143.859 1.00 26.45 ?  82  ASP D N     1 
ATOM   14020 C  CA    . ASP D 2 103 ? 116.598 95.456  143.409 1.00 27.15 ?  82  ASP D CA    1 
ATOM   14021 C  C     . ASP D 2 103 ? 116.586 96.895  142.913 1.00 26.39 ?  82  ASP D C     1 
ATOM   14022 O  O     . ASP D 2 103 ? 117.241 97.772  143.491 1.00 26.40 ?  82  ASP D O     1 
ATOM   14023 C  CB    . ASP D 2 103 ? 115.569 95.299  144.534 1.00 27.72 ?  82  ASP D CB    1 
ATOM   14024 C  CG    . ASP D 2 103 ? 115.420 93.859  145.012 1.00 31.46 ?  82  ASP D CG    1 
ATOM   14025 O  OD1   . ASP D 2 103 ? 115.579 92.906  144.203 1.00 34.26 ?  82  ASP D OD1   1 
ATOM   14026 O  OD2   . ASP D 2 103 ? 115.130 93.677  146.217 1.00 35.52 -1 82  ASP D OD2   1 
ATOM   14027 N  N     . GLY D 2 104 ? 115.821 97.134  141.852 1.00 25.52 ?  83  GLY D N     1 
ATOM   14028 C  CA    . GLY D 2 104 ? 115.676 98.475  141.290 1.00 24.31 ?  83  GLY D CA    1 
ATOM   14029 C  C     . GLY D 2 104 ? 116.072 98.452  139.818 1.00 23.27 ?  83  GLY D C     1 
ATOM   14030 O  O     . GLY D 2 104 ? 117.178 98.041  139.471 1.00 22.38 ?  83  GLY D O     1 
ATOM   14031 N  N     . HIS D 2 105 ? 115.160 98.879  138.949 1.00 22.46 ?  84  HIS D N     1 
ATOM   14032 C  CA    . HIS D 2 105 ? 115.431 98.888  137.510 1.00 22.17 ?  84  HIS D CA    1 
ATOM   14033 C  C     . HIS D 2 105 ? 116.588 99.792  137.119 1.00 21.13 ?  84  HIS D C     1 
ATOM   14034 O  O     . HIS D 2 105 ? 117.383 99.437  136.252 1.00 20.91 ?  84  HIS D O     1 
ATOM   14035 C  CB    . HIS D 2 105 ? 114.169 99.273  136.724 1.00 22.07 ?  84  HIS D CB    1 
ATOM   14036 C  CG    . HIS D 2 105 ? 113.025 98.340  136.962 1.00 23.85 ?  84  HIS D CG    1 
ATOM   14037 N  ND1   . HIS D 2 105 ? 113.150 96.973  136.831 1.00 24.86 ?  84  HIS D ND1   1 
ATOM   14038 C  CD2   . HIS D 2 105 ? 111.752 98.568  137.357 1.00 25.19 ?  84  HIS D CD2   1 
ATOM   14039 C  CE1   . HIS D 2 105 ? 111.993 96.400  137.115 1.00 24.94 ?  84  HIS D CE1   1 
ATOM   14040 N  NE2   . HIS D 2 105 ? 111.132 97.346  137.443 1.00 26.41 ?  84  HIS D NE2   1 
ATOM   14041 N  N     . GLN D 2 106 ? 116.681 100.953 137.751 1.00 20.66 ?  85  GLN D N     1 
ATOM   14042 C  CA    . GLN D 2 106 ? 117.689 101.931 137.350 1.00 20.70 ?  85  GLN D CA    1 
ATOM   14043 C  C     . GLN D 2 106 ? 119.074 101.477 137.808 1.00 20.46 ?  85  GLN D C     1 
ATOM   14044 O  O     . GLN D 2 106 ? 120.050 101.635 137.076 1.00 20.72 ?  85  GLN D O     1 
ATOM   14045 C  CB    . GLN D 2 106 ? 117.316 103.347 137.821 1.00 20.60 ?  85  GLN D CB    1 
ATOM   14046 C  CG    . GLN D 2 106 ? 115.980 103.851 137.210 1.00 20.74 ?  85  GLN D CG    1 
ATOM   14047 C  CD    . GLN D 2 106 ? 115.471 105.170 137.804 1.00 22.11 ?  85  GLN D CD    1 
ATOM   14048 O  OE1   . GLN D 2 106 ? 116.247 106.003 138.258 1.00 22.88 ?  85  GLN D OE1   1 
ATOM   14049 N  NE2   . GLN D 2 106 ? 114.154 105.362 137.784 1.00 21.64 ?  85  GLN D NE2   1 
ATOM   14050 N  N     . ARG D 2 107 ? 119.141 100.867 138.994 1.00 20.17 ?  86  ARG D N     1 
ATOM   14051 C  CA    . ARG D 2 107 ? 120.394 100.310 139.506 1.00 20.29 ?  86  ARG D CA    1 
ATOM   14052 C  C     . ARG D 2 107 ? 120.870 99.161  138.632 1.00 20.07 ?  86  ARG D C     1 
ATOM   14053 O  O     . ARG D 2 107 ? 122.054 99.061  138.336 1.00 19.53 ?  86  ARG D O     1 
ATOM   14054 C  CB    . ARG D 2 107 ? 120.228 99.810  140.938 1.00 20.88 ?  86  ARG D CB    1 
ATOM   14055 C  CG    . ARG D 2 107 ? 119.784 100.878 141.882 1.00 22.56 ?  86  ARG D CG    1 
ATOM   14056 C  CD    . ARG D 2 107 ? 119.318 100.281 143.186 1.00 27.21 ?  86  ARG D CD    1 
ATOM   14057 N  NE    . ARG D 2 107 ? 119.405 101.333 144.180 1.00 31.70 ?  86  ARG D NE    1 
ATOM   14058 C  CZ    . ARG D 2 107 ? 119.466 101.145 145.482 1.00 32.23 ?  86  ARG D CZ    1 
ATOM   14059 N  NH1   . ARG D 2 107 ? 119.438 99.916  145.994 1.00 34.27 1  86  ARG D NH1   1 
ATOM   14060 N  NH2   . ARG D 2 107 ? 119.562 102.207 146.262 1.00 33.79 ?  86  ARG D NH2   1 
ATOM   14061 N  N     . LYS D 2 108 ? 119.945 98.286  138.236 1.00 19.61 ?  87  LYS D N     1 
ATOM   14062 C  CA    . LYS D 2 108 ? 120.300 97.182  137.344 1.00 19.92 ?  87  LYS D CA    1 
ATOM   14063 C  C     . LYS D 2 108 ? 120.859 97.689  136.011 1.00 20.08 ?  87  LYS D C     1 
ATOM   14064 O  O     . LYS D 2 108 ? 121.754 97.064  135.431 1.00 20.38 ?  87  LYS D O     1 
ATOM   14065 C  CB    . LYS D 2 108 ? 119.120 96.235  137.112 1.00 19.54 ?  87  LYS D CB    1 
ATOM   14066 C  CG    . LYS D 2 108 ? 118.690 95.462  138.344 1.00 20.55 ?  87  LYS D CG    1 
ATOM   14067 C  CD    . LYS D 2 108 ? 117.527 94.516  138.032 1.00 21.09 ?  87  LYS D CD    1 
ATOM   14068 C  CE    . LYS D 2 108 ? 117.108 93.700  139.249 1.00 22.98 ?  87  LYS D CE    1 
ATOM   14069 N  NZ    . LYS D 2 108 ? 118.141 92.645  139.577 1.00 22.30 1  87  LYS D NZ    1 
ATOM   14070 N  N     . ALA D 2 109 ? 120.329 98.811  135.524 1.00 19.72 ?  88  ALA D N     1 
ATOM   14071 C  CA    . ALA D 2 109 ? 120.795 99.379  134.265 1.00 19.83 ?  88  ALA D CA    1 
ATOM   14072 C  C     . ALA D 2 109 ? 122.219 99.924  134.392 1.00 19.84 ?  88  ALA D C     1 
ATOM   14073 O  O     . ALA D 2 109 ? 123.070 99.662  133.535 1.00 19.96 ?  88  ALA D O     1 
ATOM   14074 C  CB    . ALA D 2 109 ? 119.825 100.460 133.758 1.00 19.65 ?  88  ALA D CB    1 
ATOM   14075 N  N     . VAL D 2 110 ? 122.483 100.657 135.471 1.00 19.33 ?  89  VAL D N     1 
ATOM   14076 C  CA    . VAL D 2 110 ? 123.827 101.198 135.721 1.00 19.22 ?  89  VAL D CA    1 
ATOM   14077 C  C     . VAL D 2 110 ? 124.818 100.029 135.875 1.00 19.45 ?  89  VAL D C     1 
ATOM   14078 O  O     . VAL D 2 110 ? 125.850 99.977  135.191 1.00 18.97 ?  89  VAL D O     1 
ATOM   14079 C  CB    . VAL D 2 110 ? 123.825 102.171 136.935 1.00 19.01 ?  89  VAL D CB    1 
ATOM   14080 C  CG1   . VAL D 2 110 ? 125.266 102.602 137.336 1.00 19.90 ?  89  VAL D CG1   1 
ATOM   14081 C  CG2   . VAL D 2 110 ? 123.006 103.397 136.596 1.00 19.69 ?  89  VAL D CG2   1 
ATOM   14082 N  N     . LEU D 2 111 ? 124.461 99.058  136.716 1.00 19.27 ?  90  LEU D N     1 
ATOM   14083 C  CA    . LEU D 2 111 ? 125.300 97.870  136.890 1.00 19.96 ?  90  LEU D CA    1 
ATOM   14084 C  C     . LEU D 2 111 ? 125.561 97.109  135.584 1.00 20.30 ?  90  LEU D C     1 
ATOM   14085 O  O     . LEU D 2 111 ? 126.690 96.677  135.337 1.00 19.88 ?  90  LEU D O     1 
ATOM   14086 C  CB    . LEU D 2 111 ? 124.750 96.954  137.992 1.00 19.87 ?  90  LEU D CB    1 
ATOM   14087 C  CG    . LEU D 2 111 ? 124.828 97.576  139.388 1.00 20.24 ?  90  LEU D CG    1 
ATOM   14088 C  CD1   . LEU D 2 111 ? 123.975 96.829  140.425 1.00 21.85 ?  90  LEU D CD1   1 
ATOM   14089 C  CD2   . LEU D 2 111 ? 126.290 97.707  139.855 1.00 20.29 ?  90  LEU D CD2   1 
ATOM   14090 N  N     . ASN D 2 112 ? 124.532 96.970  134.743 1.00 20.92 ?  91  ASN D N     1 
ATOM   14091 C  CA    . ASN D 2 112 ? 124.710 96.396  133.389 1.00 20.70 ?  91  ASN D CA    1 
ATOM   14092 C  C     . ASN D 2 112 ? 125.697 97.174  132.537 1.00 20.57 ?  91  ASN D C     1 
ATOM   14093 O  O     . ASN D 2 112 ? 126.461 96.587  131.753 1.00 20.45 ?  91  ASN D O     1 
ATOM   14094 C  CB    . ASN D 2 112 ? 123.390 96.374  132.615 1.00 21.16 ?  91  ASN D CB    1 
ATOM   14095 C  CG    . ASN D 2 112 ? 122.669 95.044  132.706 1.00 21.98 ?  91  ASN D CG    1 
ATOM   14096 O  OD1   . ASN D 2 112 ? 123.085 94.130  133.425 1.00 25.37 ?  91  ASN D OD1   1 
ATOM   14097 N  ND2   . ASN D 2 112 ? 121.564 94.939  131.992 1.00 21.12 ?  91  ASN D ND2   1 
ATOM   14098 N  N     . PHE D 2 113 ? 125.618 98.499  132.625 1.00 19.70 ?  92  PHE D N     1 
ATOM   14099 C  CA    . PHE D 2 113 ? 126.535 99.346  131.892 1.00 20.02 ?  92  PHE D CA    1 
ATOM   14100 C  C     . PHE D 2 113 ? 127.981 99.114  132.357 1.00 19.97 ?  92  PHE D C     1 
ATOM   14101 O  O     . PHE D 2 113 ? 128.894 98.985  131.533 1.00 19.22 ?  92  PHE D O     1 
ATOM   14102 C  CB    . PHE D 2 113 ? 126.154 100.833 131.986 1.00 20.09 ?  92  PHE D CB    1 
ATOM   14103 C  CG    . PHE D 2 113 ? 126.979 101.698 131.099 1.00 20.54 ?  92  PHE D CG    1 
ATOM   14104 C  CD1   . PHE D 2 113 ? 126.584 101.944 129.783 1.00 20.14 ?  92  PHE D CD1   1 
ATOM   14105 C  CD2   . PHE D 2 113 ? 128.192 102.217 131.555 1.00 20.77 ?  92  PHE D CD2   1 
ATOM   14106 C  CE1   . PHE D 2 113 ? 127.375 102.723 128.942 1.00 20.54 ?  92  PHE D CE1   1 
ATOM   14107 C  CE2   . PHE D 2 113 ? 128.993 102.991 130.717 1.00 21.23 ?  92  PHE D CE2   1 
ATOM   14108 C  CZ    . PHE D 2 113 ? 128.578 103.239 129.402 1.00 20.92 ?  92  PHE D CZ    1 
ATOM   14109 N  N     . MET D 2 114 ? 128.176 99.052  133.671 1.00 19.67 ?  93  MET D N     1 
ATOM   14110 C  CA    . MET D 2 114 ? 129.493 98.769  134.227 1.00 20.55 ?  93  MET D CA    1 
ATOM   14111 C  C     . MET D 2 114 ? 130.018 97.396  133.804 1.00 20.82 ?  93  MET D C     1 
ATOM   14112 O  O     . MET D 2 114 ? 131.187 97.291  133.456 1.00 20.43 ?  93  MET D O     1 
ATOM   14113 C  CB    . MET D 2 114 ? 129.484 98.900  135.745 1.00 20.24 ?  93  MET D CB    1 
ATOM   14114 C  CG    . MET D 2 114 ? 129.034 100.281 136.177 1.00 22.05 ?  93  MET D CG    1 
ATOM   14115 S  SD    . MET D 2 114 ? 128.806 100.467 137.931 1.00 25.85 ?  93  MET D SD    1 
ATOM   14116 C  CE    . MET D 2 114 ? 129.006 102.251 138.067 1.00 27.57 ?  93  MET D CE    1 
ATOM   14117 N  N     . ALA D 2 115 ? 129.160 96.367  133.833 1.00 21.19 ?  94  ALA D N     1 
ATOM   14118 C  CA    . ALA D 2 115 ? 129.547 95.020  133.368 1.00 21.53 ?  94  ALA D CA    1 
ATOM   14119 C  C     . ALA D 2 115 ? 129.958 95.050  131.898 1.00 21.75 ?  94  ALA D C     1 
ATOM   14120 O  O     . ALA D 2 115 ? 130.964 94.447  131.524 1.00 22.18 ?  94  ALA D O     1 
ATOM   14121 C  CB    . ALA D 2 115 ? 128.424 94.003  133.599 1.00 21.32 ?  94  ALA D CB    1 
ATOM   14122 N  N     . MET D 2 116 ? 129.196 95.776  131.076 1.00 21.47 ?  95  MET D N     1 
ATOM   14123 C  CA    . MET D 2 116 ? 129.537 95.970  129.670 1.00 21.83 ?  95  MET D CA    1 
ATOM   14124 C  C     . MET D 2 116 ? 130.953 96.555  129.499 1.00 22.15 ?  95  MET D C     1 
ATOM   14125 O  O     . MET D 2 116 ? 131.732 96.063  128.686 1.00 22.09 ?  95  MET D O     1 
ATOM   14126 C  CB    . MET D 2 116 ? 128.489 96.854  128.975 1.00 21.72 ?  95  MET D CB    1 
ATOM   14127 C  CG    . MET D 2 116 ? 128.802 97.208  127.512 1.00 22.57 ?  95  MET D CG    1 
ATOM   14128 S  SD    . MET D 2 116 ? 130.012 98.539  127.301 1.00 22.75 ?  95  MET D SD    1 
ATOM   14129 C  CE    . MET D 2 116 ? 129.118 99.950  127.950 1.00 22.96 ?  95  MET D CE    1 
ATOM   14130 N  N     . MET D 2 117 ? 131.272 97.599  130.267 1.00 22.04 ?  96  MET D N     1 
ATOM   14131 C  CA    . MET D 2 117 ? 132.596 98.240  130.190 1.00 22.45 ?  96  MET D CA    1 
ATOM   14132 C  C     . MET D 2 117 ? 133.728 97.250  130.515 1.00 22.39 ?  96  MET D C     1 
ATOM   14133 O  O     . MET D 2 117 ? 134.771 97.257  129.860 1.00 21.88 ?  96  MET D O     1 
ATOM   14134 C  CB    . MET D 2 117 ? 132.669 99.482  131.102 1.00 22.00 ?  96  MET D CB    1 
ATOM   14135 C  CG    . MET D 2 117 ? 131.845 100.689 130.582 1.00 23.25 ?  96  MET D CG    1 
ATOM   14136 S  SD    . MET D 2 117 ? 132.333 101.251 128.934 1.00 24.28 ?  96  MET D SD    1 
ATOM   14137 C  CE    . MET D 2 117 ? 133.900 102.045 129.272 1.00 24.59 ?  96  MET D CE    1 
ATOM   14138 N  N     . GLU D 2 118 ? 133.507 96.388  131.507 1.00 22.66 ?  97  GLU D N     1 
ATOM   14139 C  CA    . GLU D 2 118 ? 134.495 95.361  131.860 1.00 23.52 ?  97  GLU D CA    1 
ATOM   14140 C  C     . GLU D 2 118 ? 134.762 94.419  130.698 1.00 24.25 ?  97  GLU D C     1 
ATOM   14141 O  O     . GLU D 2 118 ? 135.919 94.203  130.333 1.00 25.05 ?  97  GLU D O     1 
ATOM   14142 C  CB    . GLU D 2 118 ? 134.077 94.538  133.100 1.00 23.11 ?  97  GLU D CB    1 
ATOM   14143 C  CG    . GLU D 2 118 ? 133.515 95.330  134.288 1.00 23.08 ?  97  GLU D CG    1 
ATOM   14144 C  CD    . GLU D 2 118 ? 134.538 96.195  135.007 1.00 24.08 ?  97  GLU D CD    1 
ATOM   14145 O  OE1   . GLU D 2 118 ? 135.616 96.448  134.448 1.00 26.39 ?  97  GLU D OE1   1 
ATOM   14146 O  OE2   . GLU D 2 118 ? 134.250 96.651  136.134 1.00 27.52 -1 97  GLU D OE2   1 
ATOM   14147 N  N     . ASN D 2 119 ? 133.690 93.888  130.115 1.00 25.47 ?  98  ASN D N     1 
ATOM   14148 C  CA    . ASN D 2 119 ? 133.767 92.808  129.110 1.00 26.32 ?  98  ASN D CA    1 
ATOM   14149 C  C     . ASN D 2 119 ? 134.026 93.268  127.679 1.00 26.22 ?  98  ASN D C     1 
ATOM   14150 O  O     . ASN D 2 119 ? 134.753 92.599  126.916 1.00 26.54 ?  98  ASN D O     1 
ATOM   14151 C  CB    . ASN D 2 119 ? 132.484 91.957  129.141 1.00 26.72 ?  98  ASN D CB    1 
ATOM   14152 C  CG    . ASN D 2 119 ? 132.319 91.197  130.457 1.00 29.12 ?  98  ASN D CG    1 
ATOM   14153 O  OD1   . ASN D 2 119 ? 133.219 90.465  130.884 1.00 32.07 ?  98  ASN D OD1   1 
ATOM   14154 N  ND2   . ASN D 2 119 ? 131.183 91.393  131.116 1.00 29.12 ?  98  ASN D ND2   1 
ATOM   14155 N  N     . ALA D 2 120 ? 133.412 94.389  127.315 1.00 25.46 ?  99  ALA D N     1 
ATOM   14156 C  CA    . ALA D 2 120 ? 133.462 94.889  125.942 1.00 25.77 ?  99  ALA D CA    1 
ATOM   14157 C  C     . ALA D 2 120 ? 134.568 95.914  125.710 1.00 25.51 ?  99  ALA D C     1 
ATOM   14158 O  O     . ALA D 2 120 ? 135.058 96.047  124.585 1.00 26.64 ?  99  ALA D O     1 
ATOM   14159 C  CB    . ALA D 2 120 ? 132.101 95.474  125.530 1.00 25.75 ?  99  ALA D CB    1 
ATOM   14160 N  N     . VAL D 2 121 ? 134.953 96.640  126.753 1.00 24.40 ?  100 VAL D N     1 
ATOM   14161 C  CA    . VAL D 2 121 ? 135.892 97.743  126.581 1.00 24.15 ?  100 VAL D CA    1 
ATOM   14162 C  C     . VAL D 2 121 ? 137.233 97.460  127.262 1.00 23.94 ?  100 VAL D C     1 
ATOM   14163 O  O     . VAL D 2 121 ? 138.275 97.422  126.600 1.00 23.75 ?  100 VAL D O     1 
ATOM   14164 C  CB    . VAL D 2 121 ? 135.282 99.100  127.050 1.00 23.68 ?  100 VAL D CB    1 
ATOM   14165 C  CG1   . VAL D 2 121 ? 136.268 100.245 126.822 1.00 23.76 ?  100 VAL D CG1   1 
ATOM   14166 C  CG2   . VAL D 2 121 ? 133.976 99.377  126.299 1.00 23.99 ?  100 VAL D CG2   1 
ATOM   14167 N  N     . HIS D 2 122 ? 137.199 97.258  128.578 1.00 23.68 ?  101 HIS D N     1 
ATOM   14168 C  CA    . HIS D 2 122 ? 138.418 96.999  129.347 1.00 24.02 ?  101 HIS D CA    1 
ATOM   14169 C  C     . HIS D 2 122 ? 139.155 95.752  128.889 1.00 24.39 ?  101 HIS D C     1 
ATOM   14170 O  O     . HIS D 2 122 ? 140.367 95.797  128.695 1.00 24.71 ?  101 HIS D O     1 
ATOM   14171 C  CB    . HIS D 2 122 ? 138.140 96.927  130.854 1.00 23.20 ?  101 HIS D CB    1 
ATOM   14172 C  CG    . HIS D 2 122 ? 137.641 98.211  131.440 1.00 22.82 ?  101 HIS D CG    1 
ATOM   14173 N  ND1   . HIS D 2 122 ? 137.276 98.329  132.763 1.00 20.48 ?  101 HIS D ND1   1 
ATOM   14174 C  CD2   . HIS D 2 122 ? 137.420 99.425  130.879 1.00 21.03 ?  101 HIS D CD2   1 
ATOM   14175 C  CE1   . HIS D 2 122 ? 136.868 99.562  132.997 1.00 19.88 ?  101 HIS D CE1   1 
ATOM   14176 N  NE2   . HIS D 2 122 ? 136.947 100.250 131.870 1.00 21.62 ?  101 HIS D NE2   1 
ATOM   14177 N  N     . ALA D 2 123 ? 138.433 94.646  128.707 1.00 25.30 ?  102 ALA D N     1 
ATOM   14178 C  CA    . ALA D 2 123 ? 139.080 93.377  128.342 1.00 25.77 ?  102 ALA D CA    1 
ATOM   14179 C  C     . ALA D 2 123 ? 139.763 93.445  126.972 1.00 26.37 ?  102 ALA D C     1 
ATOM   14180 O  O     . ALA D 2 123 ? 140.862 92.907  126.786 1.00 25.87 ?  102 ALA D O     1 
ATOM   14181 C  CB    . ALA D 2 123 ? 138.079 92.215  128.396 1.00 26.43 ?  102 ALA D CB    1 
ATOM   14182 N  N     . LYS D 2 124 ? 139.106 94.110  126.021 1.00 26.51 ?  103 LYS D N     1 
ATOM   14183 C  CA    . LYS D 2 124 ? 139.664 94.302  124.691 1.00 27.22 ?  103 LYS D CA    1 
ATOM   14184 C  C     . LYS D 2 124 ? 140.886 95.230  124.746 1.00 26.63 ?  103 LYS D C     1 
ATOM   14185 O  O     . LYS D 2 124 ? 141.853 95.025  124.013 1.00 26.07 ?  103 LYS D O     1 
ATOM   14186 C  CB    . LYS D 2 124 ? 138.593 94.847  123.725 1.00 27.51 ?  103 LYS D CB    1 
ATOM   14187 C  CG    . LYS D 2 124 ? 139.087 95.176  122.299 1.00 30.58 ?  103 LYS D CG    1 
ATOM   14188 C  CD    . LYS D 2 124 ? 139.494 93.930  121.526 1.00 35.72 ?  103 LYS D CD    1 
ATOM   14189 C  CE    . LYS D 2 124 ? 140.014 94.260  120.125 1.00 37.33 ?  103 LYS D CE    1 
ATOM   14190 N  NZ    . LYS D 2 124 ? 138.928 94.827  119.283 1.00 40.73 1  103 LYS D NZ    1 
ATOM   14191 N  N     . SER D 2 125 ? 140.833 96.229  125.631 1.00 26.02 ?  104 SER D N     1 
ATOM   14192 C  CA    . SER D 2 125 ? 141.918 97.200  125.798 1.00 26.16 ?  104 SER D CA    1 
ATOM   14193 C  C     . SER D 2 125 ? 143.195 96.555  126.336 1.00 26.18 ?  104 SER D C     1 
ATOM   14194 O  O     . SER D 2 125 ? 144.293 96.847  125.846 1.00 26.06 ?  104 SER D O     1 
ATOM   14195 C  CB    . SER D 2 125 ? 141.491 98.351  126.712 1.00 26.10 ?  104 SER D CB    1 
ATOM   14196 O  OG    . SER D 2 125 ? 140.456 99.102  126.104 1.00 26.58 ?  104 SER D OG    1 
ATOM   14197 N  N     . TYR D 2 126 ? 143.045 95.687  127.334 1.00 25.68 ?  105 TYR D N     1 
ATOM   14198 C  CA    . TYR D 2 126 ? 144.181 94.949  127.900 1.00 26.12 ?  105 TYR D CA    1 
ATOM   14199 C  C     . TYR D 2 126 ? 144.796 94.015  126.852 1.00 26.38 ?  105 TYR D C     1 
ATOM   14200 O  O     . TYR D 2 126 ? 146.018 93.941  126.711 1.00 26.83 ?  105 TYR D O     1 
ATOM   14201 C  CB    . TYR D 2 126 ? 143.761 94.137  129.140 1.00 25.35 ?  105 TYR D CB    1 
ATOM   14202 C  CG    . TYR D 2 126 ? 143.617 94.940  130.419 1.00 25.46 ?  105 TYR D CG    1 
ATOM   14203 C  CD1   . TYR D 2 126 ? 144.674 95.716  130.898 1.00 25.41 ?  105 TYR D CD1   1 
ATOM   14204 C  CD2   . TYR D 2 126 ? 142.435 94.898  131.173 1.00 24.77 ?  105 TYR D CD2   1 
ATOM   14205 C  CE1   . TYR D 2 126 ? 144.556 96.455  132.073 1.00 25.89 ?  105 TYR D CE1   1 
ATOM   14206 C  CE2   . TYR D 2 126 ? 142.307 95.640  132.358 1.00 23.11 ?  105 TYR D CE2   1 
ATOM   14207 C  CZ    . TYR D 2 126 ? 143.377 96.401  132.806 1.00 25.38 ?  105 TYR D CZ    1 
ATOM   14208 O  OH    . TYR D 2 126 ? 143.287 97.140  133.966 1.00 23.31 ?  105 TYR D OH    1 
ATOM   14209 N  N     . SER D 2 127 ? 143.940 93.324  126.107 1.00 27.16 ?  106 SER D N     1 
ATOM   14210 C  CA    . SER D 2 127 ? 144.388 92.433  125.031 1.00 27.83 ?  106 SER D CA    1 
ATOM   14211 C  C     . SER D 2 127 ? 145.190 93.202  123.972 1.00 28.21 ?  106 SER D C     1 
ATOM   14212 O  O     . SER D 2 127 ? 146.278 92.764  123.578 1.00 28.30 ?  106 SER D O     1 
ATOM   14213 C  CB    . SER D 2 127 ? 143.189 91.702  124.403 1.00 28.37 ?  106 SER D CB    1 
ATOM   14214 O  OG    . SER D 2 127 ? 143.586 90.914  123.282 1.00 29.33 ?  106 SER D OG    1 
ATOM   14215 N  N     . ASN D 2 128 ? 144.651 94.344  123.533 1.00 28.27 ?  107 ASN D N     1 
ATOM   14216 C  CA    . ASN D 2 128 ? 145.325 95.250  122.589 1.00 28.79 ?  107 ASN D CA    1 
ATOM   14217 C  C     . ASN D 2 128 ? 146.709 95.700  123.046 1.00 28.53 ?  107 ASN D C     1 
ATOM   14218 O  O     . ASN D 2 128 ? 147.654 95.700  122.249 1.00 28.03 ?  107 ASN D O     1 
ATOM   14219 C  CB    . ASN D 2 128 ? 144.467 96.492  122.284 1.00 29.05 ?  107 ASN D CB    1 
ATOM   14220 C  CG    . ASN D 2 128 ? 143.227 96.168  121.445 1.00 30.48 ?  107 ASN D CG    1 
ATOM   14221 O  OD1   . ASN D 2 128 ? 143.088 95.068  120.916 1.00 32.19 ?  107 ASN D OD1   1 
ATOM   14222 N  ND2   . ASN D 2 128 ? 142.316 97.130  121.340 1.00 31.59 ?  107 ASN D ND2   1 
ATOM   14223 N  N     . ILE D 2 129 ? 146.824 96.107  124.312 1.00 28.21 ?  108 ILE D N     1 
ATOM   14224 C  CA    . ILE D 2 129 ? 148.131 96.485  124.868 1.00 28.76 ?  108 ILE D CA    1 
ATOM   14225 C  C     . ILE D 2 129 ? 149.123 95.312  124.780 1.00 29.83 ?  108 ILE D C     1 
ATOM   14226 O  O     . ILE D 2 129 ? 150.258 95.480  124.314 1.00 29.99 ?  108 ILE D O     1 
ATOM   14227 C  CB    . ILE D 2 129 ? 148.032 97.029  126.329 1.00 28.28 ?  108 ILE D CB    1 
ATOM   14228 C  CG1   . ILE D 2 129 ? 147.206 98.323  126.377 1.00 27.94 ?  108 ILE D CG1   1 
ATOM   14229 C  CG2   . ILE D 2 129 ? 149.432 97.287  126.904 1.00 27.52 ?  108 ILE D CG2   1 
ATOM   14230 C  CD1   . ILE D 2 129 ? 146.752 98.723  127.776 1.00 27.98 ?  108 ILE D CD1   1 
ATOM   14231 N  N     . PHE D 2 130 ? 148.695 94.133  125.223 1.00 30.86 ?  109 PHE D N     1 
ATOM   14232 C  CA    . PHE D 2 130 ? 149.533 92.939  125.159 1.00 32.76 ?  109 PHE D CA    1 
ATOM   14233 C  C     . PHE D 2 130 ? 150.016 92.612  123.743 1.00 34.37 ?  109 PHE D C     1 
ATOM   14234 O  O     . PHE D 2 130 ? 151.213 92.451  123.520 1.00 34.61 ?  109 PHE D O     1 
ATOM   14235 C  CB    . PHE D 2 130 ? 148.808 91.731  125.747 1.00 32.81 ?  109 PHE D CB    1 
ATOM   14236 C  CG    . PHE D 2 130 ? 149.138 91.465  127.188 1.00 33.84 ?  109 PHE D CG    1 
ATOM   14237 C  CD1   . PHE D 2 130 ? 150.410 91.034  127.555 1.00 34.61 ?  109 PHE D CD1   1 
ATOM   14238 C  CD2   . PHE D 2 130 ? 148.168 91.613  128.172 1.00 35.74 ?  109 PHE D CD2   1 
ATOM   14239 C  CE1   . PHE D 2 130 ? 150.722 90.773  128.889 1.00 36.99 ?  109 PHE D CE1   1 
ATOM   14240 C  CE2   . PHE D 2 130 ? 148.465 91.354  129.516 1.00 36.96 ?  109 PHE D CE2   1 
ATOM   14241 C  CZ    . PHE D 2 130 ? 149.745 90.933  129.876 1.00 36.91 ?  109 PHE D CZ    1 
ATOM   14242 N  N     . MET D 2 131 ? 149.077 92.535  122.799 1.00 35.90 ?  110 MET D N     1 
ATOM   14243 C  CA    . MET D 2 131 ? 149.374 92.190  121.407 1.00 37.94 ?  110 MET D CA    1 
ATOM   14244 C  C     . MET D 2 131 ? 150.330 93.180  120.756 1.00 38.05 ?  110 MET D C     1 
ATOM   14245 O  O     . MET D 2 131 ? 151.074 92.814  119.852 1.00 38.20 ?  110 MET D O     1 
ATOM   14246 C  CB    . MET D 2 131 ? 148.088 92.079  120.573 1.00 38.63 ?  110 MET D CB    1 
ATOM   14247 C  CG    . MET D 2 131 ? 147.184 90.890  120.940 1.00 42.34 ?  110 MET D CG    1 
ATOM   14248 S  SD    . MET D 2 131 ? 145.665 90.755  119.942 1.00 50.15 ?  110 MET D SD    1 
ATOM   14249 C  CE    . MET D 2 131 ? 144.696 92.166  120.493 1.00 48.14 ?  110 MET D CE    1 
ATOM   14250 N  N     . THR D 2 132 ? 150.306 94.430  121.218 1.00 38.12 ?  111 THR D N     1 
ATOM   14251 C  CA    . THR D 2 132 ? 151.208 95.458  120.701 1.00 38.79 ?  111 THR D CA    1 
ATOM   14252 C  C     . THR D 2 132 ? 152.653 95.272  121.199 1.00 38.81 ?  111 THR D C     1 
ATOM   14253 O  O     . THR D 2 132 ? 153.601 95.414  120.420 1.00 39.26 ?  111 THR D O     1 
ATOM   14254 C  CB    . THR D 2 132 ? 150.698 96.874  121.041 1.00 38.78 ?  111 THR D CB    1 
ATOM   14255 O  OG1   . THR D 2 132 ? 149.375 97.039  120.519 1.00 39.32 ?  111 THR D OG1   1 
ATOM   14256 C  CG2   . THR D 2 132 ? 151.595 97.944  120.428 1.00 39.75 ?  111 THR D CG2   1 
ATOM   14257 N  N     . LEU D 2 133 ? 152.804 94.941  122.483 1.00 38.34 ?  112 LEU D N     1 
ATOM   14258 C  CA    . LEU D 2 133 ? 154.111 94.907  123.147 1.00 38.36 ?  112 LEU D CA    1 
ATOM   14259 C  C     . LEU D 2 133 ? 154.831 93.559  123.104 1.00 38.94 ?  112 LEU D C     1 
ATOM   14260 O  O     . LEU D 2 133 ? 156.061 93.515  123.091 1.00 39.14 ?  112 LEU D O     1 
ATOM   14261 C  CB    . LEU D 2 133 ? 153.983 95.361  124.610 1.00 37.62 ?  112 LEU D CB    1 
ATOM   14262 C  CG    . LEU D 2 133 ? 153.344 96.722  124.900 1.00 36.50 ?  112 LEU D CG    1 
ATOM   14263 C  CD1   . LEU D 2 133 ? 153.082 96.880  126.402 1.00 35.80 ?  112 LEU D CD1   1 
ATOM   14264 C  CD2   . LEU D 2 133 ? 154.179 97.875  124.369 1.00 35.32 ?  112 LEU D CD2   1 
ATOM   14265 N  N     . ALA D 2 134 ? 154.085 92.461  123.097 1.00 39.41 ?  113 ALA D N     1 
ATOM   14266 C  CA    . ALA D 2 134 ? 154.723 91.140  123.126 1.00 40.33 ?  113 ALA D CA    1 
ATOM   14267 C  C     . ALA D 2 134 ? 154.268 90.241  121.981 1.00 41.05 ?  113 ALA D C     1 
ATOM   14268 O  O     . ALA D 2 134 ? 153.141 90.372  121.515 1.00 40.81 ?  113 ALA D O     1 
ATOM   14269 C  CB    . ALA D 2 134 ? 154.473 90.467  124.463 1.00 40.15 ?  113 ALA D CB    1 
ATOM   14270 N  N     . PRO D 2 135 ? 155.148 89.330  121.513 1.00 42.21 ?  114 PRO D N     1 
ATOM   14271 C  CA    . PRO D 2 135 ? 154.687 88.325  120.547 1.00 43.27 ?  114 PRO D CA    1 
ATOM   14272 C  C     . PRO D 2 135 ? 153.791 87.277  121.224 1.00 43.89 ?  114 PRO D C     1 
ATOM   14273 O  O     . PRO D 2 135 ? 153.840 87.121  122.447 1.00 43.31 ?  114 PRO D O     1 
ATOM   14274 C  CB    . PRO D 2 135 ? 155.986 87.686  120.050 1.00 43.69 ?  114 PRO D CB    1 
ATOM   14275 C  CG    . PRO D 2 135 ? 156.945 87.876  121.163 1.00 43.01 ?  114 PRO D CG    1 
ATOM   14276 C  CD    . PRO D 2 135 ? 156.584 89.180  121.819 1.00 42.16 ?  114 PRO D CD    1 
ATOM   14277 N  N     . THR D 2 136 ? 152.996 86.568  120.423 1.00 45.26 ?  115 THR D N     1 
ATOM   14278 C  CA    . THR D 2 136 ? 151.990 85.617  120.926 1.00 46.11 ?  115 THR D CA    1 
ATOM   14279 C  C     . THR D 2 136 ? 152.542 84.639  121.967 1.00 46.35 ?  115 THR D C     1 
ATOM   14280 O  O     . THR D 2 136 ? 151.921 84.435  123.016 1.00 46.25 ?  115 THR D O     1 
ATOM   14281 C  CB    . THR D 2 136 ? 151.292 84.849  119.770 1.00 46.59 ?  115 THR D CB    1 
ATOM   14282 O  OG1   . THR D 2 136 ? 150.769 85.789  118.826 1.00 47.80 ?  115 THR D OG1   1 
ATOM   14283 C  CG2   . THR D 2 136 ? 150.131 83.999  120.283 1.00 46.94 ?  115 THR D CG2   1 
ATOM   14284 N  N     . GLU D 2 137 ? 153.710 84.059  121.691 1.00 46.92 ?  116 GLU D N     1 
ATOM   14285 C  CA    . GLU D 2 137 ? 154.317 83.082  122.594 1.00 47.37 ?  116 GLU D CA    1 
ATOM   14286 C  C     . GLU D 2 137 ? 154.664 83.668  123.965 1.00 46.64 ?  116 GLU D C     1 
ATOM   14287 O  O     . GLU D 2 137 ? 154.492 82.995  124.983 1.00 46.89 ?  116 GLU D O     1 
ATOM   14288 C  CB    . GLU D 2 137 ? 155.547 82.419  121.956 1.00 48.04 ?  116 GLU D CB    1 
ATOM   14289 C  CG    . GLU D 2 137 ? 156.174 81.285  122.788 1.00 49.86 ?  116 GLU D CG    1 
ATOM   14290 C  CD    . GLU D 2 137 ? 155.324 80.007  122.852 1.00 52.40 ?  116 GLU D CD    1 
ATOM   14291 O  OE1   . GLU D 2 137 ? 154.131 80.077  123.222 1.00 52.97 ?  116 GLU D OE1   1 
ATOM   14292 O  OE2   . GLU D 2 137 ? 155.865 78.917  122.553 1.00 54.12 -1 116 GLU D OE2   1 
ATOM   14293 N  N     . THR D 2 138 ? 155.144 84.911  123.982 1.00 46.09 ?  117 THR D N     1 
ATOM   14294 C  CA    . THR D 2 138 ? 155.464 85.619  125.231 1.00 45.30 ?  117 THR D CA    1 
ATOM   14295 C  C     . THR D 2 138 ? 154.210 85.911  126.064 1.00 44.63 ?  117 THR D C     1 
ATOM   14296 O  O     . THR D 2 138 ? 154.230 85.781  127.292 1.00 44.51 ?  117 THR D O     1 
ATOM   14297 C  CB    . THR D 2 138 ? 156.234 86.933  124.956 1.00 45.20 ?  117 THR D CB    1 
ATOM   14298 O  OG1   . THR D 2 138 ? 157.419 86.643  124.207 1.00 45.69 ?  117 THR D OG1   1 
ATOM   14299 C  CG2   . THR D 2 138 ? 156.632 87.631  126.256 1.00 44.67 ?  117 THR D CG2   1 
ATOM   14300 N  N     . ILE D 2 139 ? 153.123 86.295  125.395 1.00 44.24 ?  118 ILE D N     1 
ATOM   14301 C  CA    . ILE D 2 139 ? 151.847 86.545  126.069 1.00 43.65 ?  118 ILE D CA    1 
ATOM   14302 C  C     . ILE D 2 139 ? 151.342 85.272  126.764 1.00 43.87 ?  118 ILE D C     1 
ATOM   14303 O  O     . ILE D 2 139 ? 150.993 85.300  127.948 1.00 43.36 ?  118 ILE D O     1 
ATOM   14304 C  CB    . ILE D 2 139 ? 150.791 87.129  125.095 1.00 43.68 ?  118 ILE D CB    1 
ATOM   14305 C  CG1   . ILE D 2 139 ? 151.209 88.539  124.648 1.00 43.30 ?  118 ILE D CG1   1 
ATOM   14306 C  CG2   . ILE D 2 139 ? 149.392 87.157  125.740 1.00 43.11 ?  118 ILE D CG2   1 
ATOM   14307 C  CD1   . ILE D 2 139 ? 150.491 89.063  123.411 1.00 43.41 ?  118 ILE D CD1   1 
ATOM   14308 N  N     . ASN D 2 140 ? 151.337 84.159  126.032 1.00 44.52 ?  119 ASN D N     1 
ATOM   14309 C  CA    . ASN D 2 140 ? 150.912 82.865  126.578 1.00 45.00 ?  119 ASN D CA    1 
ATOM   14310 C  C     . ASN D 2 140 ? 151.725 82.433  127.816 1.00 44.99 ?  119 ASN D C     1 
ATOM   14311 O  O     . ASN D 2 140 ? 151.159 81.917  128.787 1.00 44.61 ?  119 ASN D O     1 
ATOM   14312 C  CB    . ASN D 2 140 ? 150.937 81.778  125.488 1.00 45.74 ?  119 ASN D CB    1 
ATOM   14313 C  CG    . ASN D 2 140 ? 149.988 82.076  124.322 1.00 46.40 ?  119 ASN D CG    1 
ATOM   14314 O  OD1   . ASN D 2 140 ? 149.100 82.931  124.415 1.00 46.85 ?  119 ASN D OD1   1 
ATOM   14315 N  ND2   . ASN D 2 140 ? 150.173 81.357  123.217 1.00 48.16 ?  119 ASN D ND2   1 
ATOM   14316 N  N     . GLU D 2 141 ? 153.038 82.672  127.786 1.00 45.09 ?  120 GLU D N     1 
ATOM   14317 C  CA    . GLU D 2 141 ? 153.920 82.319  128.903 1.00 45.27 ?  120 GLU D CA    1 
ATOM   14318 C  C     . GLU D 2 141 ? 153.709 83.187  130.152 1.00 44.75 ?  120 GLU D C     1 
ATOM   14319 O  O     . GLU D 2 141 ? 153.697 82.674  131.276 1.00 44.37 ?  120 GLU D O     1 
ATOM   14320 C  CB    . GLU D 2 141 ? 155.388 82.357  128.476 1.00 45.75 ?  120 GLU D CB    1 
ATOM   14321 C  CG    . GLU D 2 141 ? 155.777 81.257  127.487 1.00 48.17 ?  120 GLU D CG    1 
ATOM   14322 C  CD    . GLU D 2 141 ? 157.248 81.276  127.124 1.00 50.15 ?  120 GLU D CD    1 
ATOM   14323 O  OE1   . GLU D 2 141 ? 158.097 81.320  128.039 1.00 50.90 ?  120 GLU D OE1   1 
ATOM   14324 O  OE2   . GLU D 2 141 ? 157.557 81.240  125.915 1.00 52.25 -1 120 GLU D OE2   1 
ATOM   14325 N  N     . VAL D 2 142 ? 153.560 84.496  129.948 1.00 44.31 ?  121 VAL D N     1 
ATOM   14326 C  CA    . VAL D 2 142 ? 153.284 85.429  131.042 1.00 43.91 ?  121 VAL D CA    1 
ATOM   14327 C  C     . VAL D 2 142 ? 151.970 85.067  131.741 1.00 43.71 ?  121 VAL D C     1 
ATOM   14328 O  O     . VAL D 2 142 ? 151.896 85.064  132.969 1.00 43.44 ?  121 VAL D O     1 
ATOM   14329 C  CB    . VAL D 2 142 ? 153.256 86.905  130.557 1.00 43.65 ?  121 VAL D CB    1 
ATOM   14330 C  CG1   . VAL D 2 142 ? 152.838 87.843  131.688 1.00 43.40 ?  121 VAL D CG1   1 
ATOM   14331 C  CG2   . VAL D 2 142 ? 154.625 87.315  130.023 1.00 43.96 ?  121 VAL D CG2   1 
ATOM   14332 N  N     . PHE D 2 143 ? 150.944 84.749  130.956 1.00 44.03 ?  122 PHE D N     1 
ATOM   14333 C  CA    . PHE D 2 143 ? 149.658 84.359  131.522 1.00 44.42 ?  122 PHE D CA    1 
ATOM   14334 C  C     . PHE D 2 143 ? 149.708 83.014  132.238 1.00 45.38 ?  122 PHE D C     1 
ATOM   14335 O  O     . PHE D 2 143 ? 149.052 82.840  133.262 1.00 45.50 ?  122 PHE D O     1 
ATOM   14336 C  CB    . PHE D 2 143 ? 148.539 84.414  130.480 1.00 44.27 ?  122 PHE D CB    1 
ATOM   14337 C  CG    . PHE D 2 143 ? 147.913 85.771  130.365 1.00 43.28 ?  122 PHE D CG    1 
ATOM   14338 C  CD1   . PHE D 2 143 ? 146.931 86.175  131.268 1.00 42.17 ?  122 PHE D CD1   1 
ATOM   14339 C  CD2   . PHE D 2 143 ? 148.328 86.661  129.383 1.00 42.76 ?  122 PHE D CD2   1 
ATOM   14340 C  CE1   . PHE D 2 143 ? 146.358 87.438  131.183 1.00 42.16 ?  122 PHE D CE1   1 
ATOM   14341 C  CE2   . PHE D 2 143 ? 147.762 87.927  129.289 1.00 42.77 ?  122 PHE D CE2   1 
ATOM   14342 C  CZ    . PHE D 2 143 ? 146.773 88.319  130.191 1.00 42.28 ?  122 PHE D CZ    1 
ATOM   14343 N  N     . GLU D 2 144 ? 150.503 82.084  131.716 1.00 46.18 ?  123 GLU D N     1 
ATOM   14344 C  CA    . GLU D 2 144 ? 150.776 80.825  132.410 1.00 47.19 ?  123 GLU D CA    1 
ATOM   14345 C  C     . GLU D 2 144 ? 151.429 81.074  133.778 1.00 46.99 ?  123 GLU D C     1 
ATOM   14346 O  O     . GLU D 2 144 ? 151.023 80.466  134.773 1.00 46.94 ?  123 GLU D O     1 
ATOM   14347 C  CB    . GLU D 2 144 ? 151.657 79.915  131.544 1.00 47.80 ?  123 GLU D CB    1 
ATOM   14348 C  CG    . GLU D 2 144 ? 151.894 78.506  132.098 1.00 49.54 ?  123 GLU D CG    1 
ATOM   14349 C  CD    . GLU D 2 144 ? 152.873 77.688  131.250 1.00 52.37 ?  123 GLU D CD    1 
ATOM   14350 O  OE1   . GLU D 2 144 ? 153.941 78.219  130.865 1.00 52.92 ?  123 GLU D OE1   1 
ATOM   14351 O  OE2   . GLU D 2 144 ? 152.578 76.505  130.974 1.00 53.55 -1 123 GLU D OE2   1 
ATOM   14352 N  N     . TRP D 2 145 ? 152.427 81.965  133.816 1.00 47.02 ?  124 TRP D N     1 
ATOM   14353 C  CA    . TRP D 2 145 ? 153.151 82.316  135.051 1.00 46.93 ?  124 TRP D CA    1 
ATOM   14354 C  C     . TRP D 2 145 ? 152.235 82.990  136.062 1.00 46.55 ?  124 TRP D C     1 
ATOM   14355 O  O     . TRP D 2 145 ? 152.167 82.575  137.215 1.00 46.42 ?  124 TRP D O     1 
ATOM   14356 C  CB    . TRP D 2 145 ? 154.344 83.238  134.753 1.00 47.07 ?  124 TRP D CB    1 
ATOM   14357 C  CG    . TRP D 2 145 ? 155.280 83.496  135.938 1.00 47.82 ?  124 TRP D CG    1 
ATOM   14358 C  CD1   . TRP D 2 145 ? 156.417 82.799  136.250 1.00 48.78 ?  124 TRP D CD1   1 
ATOM   14359 C  CD2   . TRP D 2 145 ? 155.163 84.530  136.937 1.00 47.80 ?  124 TRP D CD2   1 
ATOM   14360 N  NE1   . TRP D 2 145 ? 157.008 83.325  137.378 1.00 49.06 ?  124 TRP D NE1   1 
ATOM   14361 C  CE2   . TRP D 2 145 ? 156.260 84.385  137.822 1.00 48.24 ?  124 TRP D CE2   1 
ATOM   14362 C  CE3   . TRP D 2 145 ? 154.238 85.556  137.174 1.00 47.65 ?  124 TRP D CE3   1 
ATOM   14363 C  CZ2   . TRP D 2 145 ? 156.455 85.229  138.927 1.00 47.74 ?  124 TRP D CZ2   1 
ATOM   14364 C  CZ3   . TRP D 2 145 ? 154.431 86.397  138.273 1.00 46.92 ?  124 TRP D CZ3   1 
ATOM   14365 C  CH2   . TRP D 2 145 ? 155.535 86.225  139.135 1.00 47.88 ?  124 TRP D CH2   1 
ATOM   14366 N  N     . VAL D 2 146 ? 151.535 84.033  135.623 1.00 46.09 ?  125 VAL D N     1 
ATOM   14367 C  CA    . VAL D 2 146 ? 150.677 84.805  136.514 1.00 45.36 ?  125 VAL D CA    1 
ATOM   14368 C  C     . VAL D 2 146 ? 149.485 83.956  136.985 1.00 45.28 ?  125 VAL D C     1 
ATOM   14369 O  O     . VAL D 2 146 ? 149.025 84.100  138.123 1.00 45.29 ?  125 VAL D O     1 
ATOM   14370 C  CB    . VAL D 2 146 ? 150.293 86.180  135.876 1.00 45.33 ?  125 VAL D CB    1 
ATOM   14371 C  CG1   . VAL D 2 146 ? 149.288 86.924  136.715 1.00 44.97 ?  125 VAL D CG1   1 
ATOM   14372 C  CG2   . VAL D 2 146 ? 151.544 87.046  135.711 1.00 44.52 ?  125 VAL D CG2   1 
ATOM   14373 N  N     . LYS D 2 147 ? 149.027 83.041  136.130 1.00 44.98 ?  126 LYS D N     1 
ATOM   14374 C  CA    . LYS D 2 147 ? 147.963 82.096  136.495 1.00 44.65 ?  126 LYS D CA    1 
ATOM   14375 C  C     . LYS D 2 147 ? 148.374 81.139  137.626 1.00 44.06 ?  126 LYS D C     1 
ATOM   14376 O  O     . LYS D 2 147 ? 147.529 80.688  138.402 1.00 44.65 ?  126 LYS D O     1 
ATOM   14377 C  CB    . LYS D 2 147 ? 147.505 81.283  135.281 1.00 45.31 ?  126 LYS D CB    1 
ATOM   14378 C  CG    . LYS D 2 147 ? 145.993 81.173  135.157 1.00 46.54 ?  126 LYS D CG    1 
ATOM   14379 C  CD    . LYS D 2 147 ? 145.531 79.768  134.767 1.00 49.06 ?  126 LYS D CD    1 
ATOM   14380 C  CE    . LYS D 2 147 ? 145.333 78.883  136.005 1.00 50.46 ?  126 LYS D CE    1 
ATOM   14381 N  NZ    . LYS D 2 147 ? 144.339 77.790  135.782 1.00 51.33 1  126 LYS D NZ    1 
ATOM   14382 N  N     . GLN D 2 148 ? 149.666 80.834  137.712 1.00 42.58 ?  127 GLN D N     1 
ATOM   14383 C  CA    . GLN D 2 148 ? 150.194 79.950  138.750 1.00 41.39 ?  127 GLN D CA    1 
ATOM   14384 C  C     . GLN D 2 148 ? 150.701 80.717  139.978 1.00 39.56 ?  127 GLN D C     1 
ATOM   14385 O  O     . GLN D 2 148 ? 150.906 80.125  141.037 1.00 39.77 ?  127 GLN D O     1 
ATOM   14386 C  CB    . GLN D 2 148 ? 151.287 79.042  138.153 1.00 42.11 ?  127 GLN D CB    1 
ATOM   14387 C  CG    . GLN D 2 148 ? 152.452 78.686  139.072 1.00 44.08 ?  127 GLN D CG    1 
ATOM   14388 C  CD    . GLN D 2 148 ? 153.687 79.564  138.860 1.00 46.12 ?  127 GLN D CD    1 
ATOM   14389 O  OE1   . GLN D 2 148 ? 153.587 80.785  138.686 1.00 46.47 ?  127 GLN D OE1   1 
ATOM   14390 N  NE2   . GLN D 2 148 ? 154.864 78.938  138.891 1.00 45.69 ?  127 GLN D NE2   1 
ATOM   14391 N  N     . ASN D 2 149 ? 150.888 82.031  139.830 1.00 36.99 ?  128 ASN D N     1 
ATOM   14392 C  CA    . ASN D 2 149 ? 151.428 82.874  140.896 1.00 34.54 ?  128 ASN D CA    1 
ATOM   14393 C  C     . ASN D 2 149 ? 150.594 82.874  142.180 1.00 33.13 ?  128 ASN D C     1 
ATOM   14394 O  O     . ASN D 2 149 ? 149.399 83.160  142.157 1.00 32.62 ?  128 ASN D O     1 
ATOM   14395 C  CB    . ASN D 2 149 ? 151.623 84.310  140.405 1.00 34.24 ?  128 ASN D CB    1 
ATOM   14396 C  CG    . ASN D 2 149 ? 152.291 85.187  141.445 1.00 33.83 ?  128 ASN D CG    1 
ATOM   14397 O  OD1   . ASN D 2 149 ? 151.628 85.953  142.146 1.00 32.21 ?  128 ASN D OD1   1 
ATOM   14398 N  ND2   . ASN D 2 149 ? 153.609 85.052  141.573 1.00 33.26 ?  128 ASN D ND2   1 
ATOM   14399 N  N     . LYS D 2 150 ? 151.252 82.584  143.299 1.00 31.49 ?  129 LYS D N     1 
ATOM   14400 C  CA    . LYS D 2 150 ? 150.594 82.415  144.592 1.00 30.68 ?  129 LYS D CA    1 
ATOM   14401 C  C     . LYS D 2 150 ? 149.840 83.670  145.096 1.00 28.95 ?  129 LYS D C     1 
ATOM   14402 O  O     . LYS D 2 150 ? 148.730 83.560  145.629 1.00 27.90 ?  129 LYS D O     1 
ATOM   14403 C  CB    . LYS D 2 150 ? 151.637 81.928  145.609 1.00 31.17 ?  129 LYS D CB    1 
ATOM   14404 C  CG    . LYS D 2 150 ? 151.276 82.018  147.078 1.00 33.66 ?  129 LYS D CG    1 
ATOM   14405 C  CD    . LYS D 2 150 ? 152.456 81.513  147.923 1.00 38.08 ?  129 LYS D CD    1 
ATOM   14406 C  CE    . LYS D 2 150 ? 152.461 82.121  149.331 1.00 40.20 ?  129 LYS D CE    1 
ATOM   14407 N  NZ    . LYS D 2 150 ? 151.731 81.278  150.317 1.00 42.60 1  129 LYS D NZ    1 
ATOM   14408 N  N     . TYR D 2 151 ? 150.441 84.847  144.930 1.00 27.36 ?  130 TYR D N     1 
ATOM   14409 C  CA    . TYR D 2 151 ? 149.860 86.086  145.478 1.00 26.56 ?  130 TYR D CA    1 
ATOM   14410 C  C     . TYR D 2 151 ? 148.713 86.611  144.630 1.00 25.66 ?  130 TYR D C     1 
ATOM   14411 O  O     . TYR D 2 151 ? 147.726 87.111  145.178 1.00 25.61 ?  130 TYR D O     1 
ATOM   14412 C  CB    . TYR D 2 151 ? 150.939 87.163  145.715 1.00 26.32 ?  130 TYR D CB    1 
ATOM   14413 C  CG    . TYR D 2 151 ? 152.167 86.591  146.397 1.00 27.20 ?  130 TYR D CG    1 
ATOM   14414 C  CD1   . TYR D 2 151 ? 152.115 86.187  147.731 1.00 27.31 ?  130 TYR D CD1   1 
ATOM   14415 C  CD2   . TYR D 2 151 ? 153.358 86.402  145.696 1.00 27.22 ?  130 TYR D CD2   1 
ATOM   14416 C  CE1   . TYR D 2 151 ? 153.226 85.629  148.359 1.00 29.65 ?  130 TYR D CE1   1 
ATOM   14417 C  CE2   . TYR D 2 151 ? 154.483 85.841  146.319 1.00 28.75 ?  130 TYR D CE2   1 
ATOM   14418 C  CZ    . TYR D 2 151 ? 154.398 85.467  147.663 1.00 29.17 ?  130 TYR D CZ    1 
ATOM   14419 O  OH    . TYR D 2 151 ? 155.477 84.914  148.316 1.00 30.61 ?  130 TYR D OH    1 
ATOM   14420 N  N     . LEU D 2 152 ? 148.843 86.495  143.307 1.00 24.87 ?  131 LEU D N     1 
ATOM   14421 C  CA    . LEU D 2 152 ? 147.744 86.834  142.409 1.00 24.37 ?  131 LEU D CA    1 
ATOM   14422 C  C     . LEU D 2 152 ? 146.554 85.897  142.649 1.00 24.18 ?  131 LEU D C     1 
ATOM   14423 O  O     . LEU D 2 152 ? 145.432 86.363  142.847 1.00 23.16 ?  131 LEU D O     1 
ATOM   14424 C  CB    . LEU D 2 152 ? 148.154 86.814  140.932 1.00 24.45 ?  131 LEU D CB    1 
ATOM   14425 C  CG    . LEU D 2 152 ? 146.902 87.238  140.143 1.00 26.33 ?  131 LEU D CG    1 
ATOM   14426 C  CD1   . LEU D 2 152 ? 146.650 88.746  140.283 1.00 25.00 ?  131 LEU D CD1   1 
ATOM   14427 C  CD2   . LEU D 2 152 ? 146.905 86.803  138.707 1.00 29.15 ?  131 LEU D CD2   1 
ATOM   14428 N  N     . GLN D 2 153 ? 146.809 84.587  142.664 1.00 24.07 ?  132 GLN D N     1 
ATOM   14429 C  CA    . GLN D 2 153 ? 145.743 83.605  142.952 1.00 24.99 ?  132 GLN D CA    1 
ATOM   14430 C  C     . GLN D 2 153 ? 145.066 83.814  144.304 1.00 24.24 ?  132 GLN D C     1 
ATOM   14431 O  O     . GLN D 2 153 ? 143.827 83.760  144.407 1.00 23.75 ?  132 GLN D O     1 
ATOM   14432 C  CB    . GLN D 2 153 ? 146.245 82.158  142.807 1.00 25.84 ?  132 GLN D CB    1 
ATOM   14433 C  CG    . GLN D 2 153 ? 146.515 81.740  141.337 1.00 28.48 ?  132 GLN D CG    1 
ATOM   14434 C  CD    . GLN D 2 153 ? 145.272 81.805  140.436 1.00 30.95 ?  132 GLN D CD    1 
ATOM   14435 O  OE1   . GLN D 2 153 ? 144.164 81.511  140.870 1.00 31.78 ?  132 GLN D OE1   1 
ATOM   14436 N  NE2   . GLN D 2 153 ? 145.466 82.180  139.170 1.00 32.81 ?  132 GLN D NE2   1 
ATOM   14437 N  N     . LYS D 2 154 ? 145.854 84.065  145.346 1.00 24.00 ?  133 LYS D N     1 
ATOM   14438 C  CA    . LYS D 2 154 ? 145.250 84.254  146.665 1.00 24.43 ?  133 LYS D CA    1 
ATOM   14439 C  C     . LYS D 2 154 ? 144.169 85.343  146.631 1.00 23.40 ?  133 LYS D C     1 
ATOM   14440 O  O     . LYS D 2 154 ? 143.029 85.105  147.039 1.00 22.68 ?  133 LYS D O     1 
ATOM   14441 C  CB    . LYS D 2 154 ? 146.280 84.577  147.752 1.00 24.64 ?  133 LYS D CB    1 
ATOM   14442 C  CG    . LYS D 2 154 ? 145.603 84.729  149.126 1.00 28.01 ?  133 LYS D CG    1 
ATOM   14443 C  CD    . LYS D 2 154 ? 146.566 84.875  150.281 1.00 32.56 ?  133 LYS D CD    1 
ATOM   14444 C  CE    . LYS D 2 154 ? 147.304 83.587  150.550 1.00 34.45 ?  133 LYS D CE    1 
ATOM   14445 N  NZ    . LYS D 2 154 ? 148.259 83.757  151.690 1.00 36.11 1  133 LYS D NZ    1 
ATOM   14446 N  N     . LYS D 2 155 ? 144.523 86.532  146.143 1.00 23.07 ?  134 LYS D N     1 
ATOM   14447 C  CA    . LYS D 2 155 ? 143.544 87.615  146.083 1.00 22.70 ?  134 LYS D CA    1 
ATOM   14448 C  C     . LYS D 2 155 ? 142.418 87.333  145.089 1.00 21.96 ?  134 LYS D C     1 
ATOM   14449 O  O     . LYS D 2 155 ? 141.259 87.578  145.406 1.00 22.25 ?  134 LYS D O     1 
ATOM   14450 C  CB    . LYS D 2 155 ? 144.197 88.990  145.853 1.00 22.70 ?  134 LYS D CB    1 
ATOM   14451 C  CG    . LYS D 2 155 ? 144.900 89.195  144.527 1.00 23.62 ?  134 LYS D CG    1 
ATOM   14452 C  CD    . LYS D 2 155 ? 145.413 90.631  144.449 1.00 25.32 ?  134 LYS D CD    1 
ATOM   14453 C  CE    . LYS D 2 155 ? 146.730 90.689  143.680 1.00 27.09 ?  134 LYS D CE    1 
ATOM   14454 N  NZ    . LYS D 2 155 ? 147.194 92.100  143.541 1.00 26.65 1  134 LYS D NZ    1 
ATOM   14455 N  N     . ALA D 2 156 ? 142.732 86.794  143.910 1.00 21.76 ?  135 ALA D N     1 
ATOM   14456 C  CA    . ALA D 2 156 ? 141.672 86.514  142.924 1.00 21.83 ?  135 ALA D CA    1 
ATOM   14457 C  C     . ALA D 2 156 ? 140.617 85.556  143.504 1.00 22.30 ?  135 ALA D C     1 
ATOM   14458 O  O     . ALA D 2 156 ? 139.412 85.808  143.395 1.00 21.92 ?  135 ALA D O     1 
ATOM   14459 C  CB    . ALA D 2 156 ? 142.256 85.950  141.617 1.00 22.30 ?  135 ALA D CB    1 
ATOM   14460 N  N     . GLN D 2 157 ? 141.070 84.477  144.143 1.00 22.15 ?  136 GLN D N     1 
ATOM   14461 C  CA    . GLN D 2 157 ? 140.141 83.485  144.696 1.00 22.38 ?  136 GLN D CA    1 
ATOM   14462 C  C     . GLN D 2 157 ? 139.393 83.966  145.946 1.00 21.59 ?  136 GLN D C     1 
ATOM   14463 O  O     . GLN D 2 157 ? 138.252 83.565  146.174 1.00 21.44 ?  136 GLN D O     1 
ATOM   14464 C  CB    . GLN D 2 157 ? 140.837 82.137  144.958 1.00 22.94 ?  136 GLN D CB    1 
ATOM   14465 C  CG    . GLN D 2 157 ? 141.492 81.494  143.724 1.00 25.31 ?  136 GLN D CG    1 
ATOM   14466 C  CD    . GLN D 2 157 ? 140.607 81.508  142.474 1.00 28.02 ?  136 GLN D CD    1 
ATOM   14467 O  OE1   . GLN D 2 157 ? 139.392 81.300  142.540 1.00 27.14 ?  136 GLN D OE1   1 
ATOM   14468 N  NE2   . GLN D 2 157 ? 141.231 81.746  141.322 1.00 29.47 ?  136 GLN D NE2   1 
ATOM   14469 N  N     . MET D 2 158 ? 140.025 84.809  146.755 1.00 21.52 ?  137 MET D N     1 
ATOM   14470 C  CA    . MET D 2 158 ? 139.334 85.413  147.907 1.00 22.20 ?  137 MET D CA    1 
ATOM   14471 C  C     . MET D 2 158 ? 138.117 86.239  147.475 1.00 21.84 ?  137 MET D C     1 
ATOM   14472 O  O     . MET D 2 158 ? 137.042 86.135  148.071 1.00 21.91 ?  137 MET D O     1 
ATOM   14473 C  CB    . MET D 2 158 ? 140.282 86.284  148.732 1.00 22.52 ?  137 MET D CB    1 
ATOM   14474 C  CG    . MET D 2 158 ? 141.229 85.484  149.638 1.00 25.81 ?  137 MET D CG    1 
ATOM   14475 S  SD    . MET D 2 158 ? 142.355 86.527  150.605 1.00 31.19 ?  137 MET D SD    1 
ATOM   14476 C  CE    . MET D 2 158 ? 141.148 87.383  151.582 1.00 23.91 ?  137 MET D CE    1 
ATOM   14477 N  N     . ILE D 2 159 ? 138.302 87.050  146.436 1.00 21.41 ?  138 ILE D N     1 
ATOM   14478 C  CA    . ILE D 2 159 ? 137.242 87.907  145.912 1.00 21.51 ?  138 ILE D CA    1 
ATOM   14479 C  C     . ILE D 2 159 ? 136.121 87.057  145.294 1.00 21.77 ?  138 ILE D C     1 
ATOM   14480 O  O     . ILE D 2 159 ? 134.936 87.253  145.611 1.00 21.44 ?  138 ILE D O     1 
ATOM   14481 C  CB    . ILE D 2 159 ? 137.832 88.961  144.897 1.00 21.49 ?  138 ILE D CB    1 
ATOM   14482 C  CG1   . ILE D 2 159 ? 138.836 89.898  145.587 1.00 21.16 ?  138 ILE D CG1   1 
ATOM   14483 C  CG2   . ILE D 2 159 ? 136.730 89.764  144.194 1.00 22.34 ?  138 ILE D CG2   1 
ATOM   14484 C  CD1   . ILE D 2 159 ? 138.248 90.767  146.719 1.00 23.85 ?  138 ILE D CD1   1 
ATOM   14485 N  N     . VAL D 2 160 ? 136.509 86.111  144.431 1.00 21.96 ?  139 VAL D N     1 
ATOM   14486 C  CA    . VAL D 2 160 ? 135.578 85.215  143.729 1.00 22.59 ?  139 VAL D CA    1 
ATOM   14487 C  C     . VAL D 2 160 ? 134.779 84.367  144.728 1.00 22.36 ?  139 VAL D C     1 
ATOM   14488 O  O     . VAL D 2 160 ? 133.585 84.121  144.523 1.00 21.64 ?  139 VAL D O     1 
ATOM   14489 C  CB    . VAL D 2 160 ? 136.329 84.313  142.692 1.00 23.08 ?  139 VAL D CB    1 
ATOM   14490 C  CG1   . VAL D 2 160 ? 135.473 83.121  142.223 1.00 24.33 ?  139 VAL D CG1   1 
ATOM   14491 C  CG2   . VAL D 2 160 ? 136.783 85.145  141.482 1.00 22.87 ?  139 VAL D CG2   1 
ATOM   14492 N  N     . GLY D 2 161 ? 135.441 83.934  145.804 1.00 22.21 ?  140 GLY D N     1 
ATOM   14493 C  CA    . GLY D 2 161 ? 134.781 83.181  146.868 1.00 22.50 ?  140 GLY D CA    1 
ATOM   14494 C  C     . GLY D 2 161 ? 133.597 83.934  147.466 1.00 22.88 ?  140 GLY D C     1 
ATOM   14495 O  O     . GLY D 2 161 ? 132.528 83.349  147.688 1.00 23.54 ?  140 GLY D O     1 
ATOM   14496 N  N     . LEU D 2 162 ? 133.775 85.231  147.716 1.00 22.25 ?  141 LEU D N     1 
ATOM   14497 C  CA    . LEU D 2 162 ? 132.689 86.054  148.256 1.00 22.48 ?  141 LEU D CA    1 
ATOM   14498 C  C     . LEU D 2 162 ? 131.547 86.274  147.259 1.00 22.27 ?  141 LEU D C     1 
ATOM   14499 O  O     . LEU D 2 162 ? 130.385 86.323  147.665 1.00 22.31 ?  141 LEU D O     1 
ATOM   14500 C  CB    . LEU D 2 162 ? 133.209 87.382  148.842 1.00 22.07 ?  141 LEU D CB    1 
ATOM   14501 C  CG    . LEU D 2 162 ? 133.929 87.229  150.199 1.00 22.81 ?  141 LEU D CG    1 
ATOM   14502 C  CD1   . LEU D 2 162 ? 134.853 88.408  150.498 1.00 21.65 ?  141 LEU D CD1   1 
ATOM   14503 C  CD2   . LEU D 2 162 ? 132.963 86.959  151.359 1.00 23.35 ?  141 LEU D CD2   1 
ATOM   14504 N  N     . TYR D 2 163 ? 131.867 86.406  145.970 1.00 22.63 ?  142 TYR D N     1 
ATOM   14505 C  CA    . TYR D 2 163 ? 130.822 86.483  144.929 1.00 23.30 ?  142 TYR D CA    1 
ATOM   14506 C  C     . TYR D 2 163 ? 130.015 85.194  144.839 1.00 23.40 ?  142 TYR D C     1 
ATOM   14507 O  O     . TYR D 2 163 ? 128.807 85.232  144.662 1.00 23.75 ?  142 TYR D O     1 
ATOM   14508 C  CB    . TYR D 2 163 ? 131.408 86.740  143.548 1.00 23.22 ?  142 TYR D CB    1 
ATOM   14509 C  CG    . TYR D 2 163 ? 132.160 88.032  143.377 1.00 24.01 ?  142 TYR D CG    1 
ATOM   14510 C  CD1   . TYR D 2 163 ? 131.929 89.116  144.214 1.00 24.47 ?  142 TYR D CD1   1 
ATOM   14511 C  CD2   . TYR D 2 163 ? 133.100 88.165  142.360 1.00 24.62 ?  142 TYR D CD2   1 
ATOM   14512 C  CE1   . TYR D 2 163 ? 132.618 90.300  144.051 1.00 26.33 ?  142 TYR D CE1   1 
ATOM   14513 C  CE2   . TYR D 2 163 ? 133.790 89.353  142.178 1.00 26.07 ?  142 TYR D CE2   1 
ATOM   14514 C  CZ    . TYR D 2 163 ? 133.536 90.419  143.032 1.00 26.65 ?  142 TYR D CZ    1 
ATOM   14515 O  OH    . TYR D 2 163 ? 134.217 91.604  142.878 1.00 31.13 ?  142 TYR D OH    1 
ATOM   14516 N  N     . LYS D 2 164 ? 130.689 84.056  144.949 1.00 23.70 ?  143 LYS D N     1 
ATOM   14517 C  CA    . LYS D 2 164 ? 130.011 82.751  144.898 1.00 24.47 ?  143 LYS D CA    1 
ATOM   14518 C  C     . LYS D 2 164 ? 129.140 82.460  146.131 1.00 24.55 ?  143 LYS D C     1 
ATOM   14519 O  O     . LYS D 2 164 ? 128.274 81.584  146.094 1.00 24.49 ?  143 LYS D O     1 
ATOM   14520 C  CB    . LYS D 2 164 ? 131.041 81.635  144.710 1.00 24.98 ?  143 LYS D CB    1 
ATOM   14521 C  CG    . LYS D 2 164 ? 131.618 81.527  143.290 1.00 27.10 ?  143 LYS D CG    1 
ATOM   14522 C  CD    . LYS D 2 164 ? 132.531 80.314  143.196 1.00 30.75 ?  143 LYS D CD    1 
ATOM   14523 C  CE    . LYS D 2 164 ? 133.062 80.081  141.782 1.00 32.81 ?  143 LYS D CE    1 
ATOM   14524 N  NZ    . LYS D 2 164 ? 134.054 78.933  141.731 1.00 33.68 1  143 LYS D NZ    1 
ATOM   14525 N  N     . ALA D 2 165 ? 129.380 83.184  147.221 1.00 24.18 ?  144 ALA D N     1 
ATOM   14526 C  CA    . ALA D 2 165 ? 128.664 82.952  148.479 1.00 25.04 ?  144 ALA D CA    1 
ATOM   14527 C  C     . ALA D 2 165 ? 127.390 83.790  148.653 1.00 25.00 ?  144 ALA D C     1 
ATOM   14528 O  O     . ALA D 2 165 ? 126.690 83.647  149.666 1.00 25.50 ?  144 ALA D O     1 
ATOM   14529 C  CB    . ALA D 2 165 ? 129.604 83.153  149.680 1.00 25.02 ?  144 ALA D CB    1 
ATOM   14530 N  N     . ILE D 2 166 ? 127.086 84.660  147.686 1.00 24.60 ?  145 ILE D N     1 
ATOM   14531 C  CA    . ILE D 2 166 ? 125.850 85.442  147.736 1.00 24.40 ?  145 ILE D CA    1 
ATOM   14532 C  C     . ILE D 2 166 ? 124.646 84.492  147.667 1.00 25.75 ?  145 ILE D C     1 
ATOM   14533 O  O     . ILE D 2 166 ? 124.605 83.584  146.830 1.00 25.84 ?  145 ILE D O     1 
ATOM   14534 C  CB    . ILE D 2 166 ? 125.736 86.484  146.587 1.00 24.15 ?  145 ILE D CB    1 
ATOM   14535 C  CG1   . ILE D 2 166 ? 126.997 87.342  146.492 1.00 23.15 ?  145 ILE D CG1   1 
ATOM   14536 C  CG2   . ILE D 2 166 ? 124.506 87.369  146.790 1.00 22.72 ?  145 ILE D CG2   1 
ATOM   14537 C  CD1   . ILE D 2 166 ? 127.053 88.215  145.256 1.00 21.70 ?  145 ILE D CD1   1 
ATOM   14538 N  N     . GLN D 2 167 ? 123.695 84.688  148.571 1.00 26.52 ?  146 GLN D N     1 
ATOM   14539 C  CA    . GLN D 2 167 ? 122.473 83.895  148.578 1.00 28.77 ?  146 GLN D CA    1 
ATOM   14540 C  C     . GLN D 2 167 ? 121.271 84.761  148.220 1.00 29.20 ?  146 GLN D C     1 
ATOM   14541 O  O     . GLN D 2 167 ? 121.181 85.923  148.641 1.00 28.89 ?  146 GLN D O     1 
ATOM   14542 C  CB    . GLN D 2 167 ? 122.267 83.251  149.946 1.00 29.04 ?  146 GLN D CB    1 
ATOM   14543 C  CG    . GLN D 2 167 ? 123.335 82.233  150.296 1.00 31.87 ?  146 GLN D CG    1 
ATOM   14544 C  CD    . GLN D 2 167 ? 123.805 82.375  151.719 1.00 35.35 ?  146 GLN D CD    1 
ATOM   14545 O  OE1   . GLN D 2 167 ? 123.061 82.097  152.662 1.00 36.91 ?  146 GLN D OE1   1 
ATOM   14546 N  NE2   . GLN D 2 167 ? 125.053 82.809  151.888 1.00 36.19 ?  146 GLN D NE2   1 
ATOM   14547 N  N     . LYS D 2 168 ? 120.352 84.189  147.445 1.00 30.29 ?  147 LYS D N     1 
ATOM   14548 C  CA    . LYS D 2 168 ? 119.119 84.884  147.079 1.00 31.24 ?  147 LYS D CA    1 
ATOM   14549 C  C     . LYS D 2 168 ? 118.413 85.449  148.312 1.00 31.73 ?  147 LYS D C     1 
ATOM   14550 O  O     . LYS D 2 168 ? 118.314 84.770  149.334 1.00 31.46 ?  147 LYS D O     1 
ATOM   14551 C  CB    . LYS D 2 168 ? 118.188 83.955  146.306 1.00 31.92 ?  147 LYS D CB    1 
ATOM   14552 C  CG    . LYS D 2 168 ? 116.919 84.637  145.816 1.00 33.23 ?  147 LYS D CG    1 
ATOM   14553 C  CD    . LYS D 2 168 ? 116.141 83.753  144.855 1.00 36.06 ?  147 LYS D CD    1 
ATOM   14554 C  CE    . LYS D 2 168 ? 114.845 84.411  144.431 1.00 35.46 ?  147 LYS D CE    1 
ATOM   14555 N  NZ    . LYS D 2 168 ? 115.072 85.568  143.525 1.00 38.24 1  147 LYS D NZ    1 
ATOM   14556 N  N     . ASP D 2 169 ? 117.951 86.698  148.208 1.00 32.28 ?  148 ASP D N     1 
ATOM   14557 C  CA    . ASP D 2 169 ? 117.242 87.393  149.297 1.00 33.45 ?  148 ASP D CA    1 
ATOM   14558 C  C     . ASP D 2 169 ? 117.999 87.495  150.621 1.00 33.30 ?  148 ASP D C     1 
ATOM   14559 O  O     . ASP D 2 169 ? 117.384 87.628  151.681 1.00 34.32 ?  148 ASP D O     1 
ATOM   14560 C  CB    . ASP D 2 169 ? 115.874 86.744  149.566 1.00 34.63 ?  148 ASP D CB    1 
ATOM   14561 C  CG    . ASP D 2 169 ? 114.856 87.034  148.484 1.00 36.09 ?  148 ASP D CG    1 
ATOM   14562 O  OD1   . ASP D 2 169 ? 115.083 87.922  147.635 1.00 37.80 ?  148 ASP D OD1   1 
ATOM   14563 O  OD2   . ASP D 2 169 ? 113.807 86.358  148.498 1.00 40.47 -1 148 ASP D OD2   1 
ATOM   14564 N  N     . ASP D 2 170 ? 119.319 87.411  150.580 1.00 32.58 ?  149 ASP D N     1 
ATOM   14565 C  CA    . ASP D 2 170 ? 120.109 87.622  151.791 1.00 32.01 ?  149 ASP D CA    1 
ATOM   14566 C  C     . ASP D 2 170 ? 121.024 88.822  151.579 1.00 30.59 ?  149 ASP D C     1 
ATOM   14567 O  O     . ASP D 2 170 ? 122.042 88.728  150.892 1.00 29.11 ?  149 ASP D O     1 
ATOM   14568 C  CB    . ASP D 2 170 ? 120.891 86.363  152.174 1.00 32.93 ?  149 ASP D CB    1 
ATOM   14569 C  CG    . ASP D 2 170 ? 121.911 86.609  153.278 1.00 35.05 ?  149 ASP D CG    1 
ATOM   14570 O  OD1   . ASP D 2 170 ? 121.716 87.501  154.133 1.00 39.25 ?  149 ASP D OD1   1 
ATOM   14571 O  OD2   . ASP D 2 170 ? 122.916 85.887  153.303 1.00 39.22 -1 149 ASP D OD2   1 
ATOM   14572 N  N     . GLU D 2 171 ? 120.633 89.946  152.172 1.00 29.34 ?  150 GLU D N     1 
ATOM   14573 C  CA    . GLU D 2 171 ? 121.340 91.210  151.989 1.00 28.51 ?  150 GLU D CA    1 
ATOM   14574 C  C     . GLU D 2 171 ? 122.703 91.256  152.694 1.00 27.27 ?  150 GLU D C     1 
ATOM   14575 O  O     . GLU D 2 171 ? 123.564 92.030  152.307 1.00 26.62 ?  150 GLU D O     1 
ATOM   14576 C  CB    . GLU D 2 171 ? 120.454 92.391  152.406 1.00 29.09 ?  150 GLU D CB    1 
ATOM   14577 C  CG    . GLU D 2 171 ? 120.176 92.506  153.904 1.00 30.68 ?  150 GLU D CG    1 
ATOM   14578 C  CD    . GLU D 2 171 ? 119.151 93.582  154.224 1.00 33.92 ?  150 GLU D CD    1 
ATOM   14579 O  OE1   . GLU D 2 171 ? 118.688 94.269  153.281 1.00 36.31 ?  150 GLU D OE1   1 
ATOM   14580 O  OE2   . GLU D 2 171 ? 118.805 93.755  155.413 1.00 34.02 -1 150 GLU D OE2   1 
ATOM   14581 N  N     . ILE D 2 172 ? 122.899 90.414  153.707 1.00 26.19 ?  151 ILE D N     1 
ATOM   14582 C  CA    . ILE D 2 172 ? 124.188 90.339  154.397 1.00 25.49 ?  151 ILE D CA    1 
ATOM   14583 C  C     . ILE D 2 172 ? 125.263 89.767  153.468 1.00 24.61 ?  151 ILE D C     1 
ATOM   14584 O  O     . ILE D 2 172 ? 126.355 90.336  153.346 1.00 24.09 ?  151 ILE D O     1 
ATOM   14585 C  CB    . ILE D 2 172 ? 124.095 89.534  155.725 1.00 25.98 ?  151 ILE D CB    1 
ATOM   14586 C  CG1   . ILE D 2 172 ? 123.162 90.229  156.718 1.00 26.86 ?  151 ILE D CG1   1 
ATOM   14587 C  CG2   . ILE D 2 172 ? 125.488 89.292  156.364 1.00 26.50 ?  151 ILE D CG2   1 
ATOM   14588 C  CD1   . ILE D 2 172 ? 123.599 91.632  157.116 1.00 27.81 ?  151 ILE D CD1   1 
ATOM   14589 N  N     . SER D 2 173 ? 124.938 88.664  152.802 1.00 23.71 ?  152 SER D N     1 
ATOM   14590 C  CA    . SER D 2 173 ? 125.861 88.038  151.856 1.00 23.38 ?  152 SER D CA    1 
ATOM   14591 C  C     . SER D 2 173 ? 126.103 88.947  150.637 1.00 22.41 ?  152 SER D C     1 
ATOM   14592 O  O     . SER D 2 173 ? 127.204 88.981  150.081 1.00 21.43 ?  152 SER D O     1 
ATOM   14593 C  CB    . SER D 2 173 ? 125.361 86.650  151.434 1.00 23.90 ?  152 SER D CB    1 
ATOM   14594 O  OG    . SER D 2 173 ? 124.207 86.696  150.597 1.00 23.74 ?  152 SER D OG    1 
ATOM   14595 N  N     . LEU D 2 174 ? 125.078 89.695  150.242 1.00 21.63 ?  153 LEU D N     1 
ATOM   14596 C  CA    . LEU D 2 174 ? 125.233 90.660  149.150 1.00 20.75 ?  153 LEU D CA    1 
ATOM   14597 C  C     . LEU D 2 174 ? 126.200 91.766  149.568 1.00 20.96 ?  153 LEU D C     1 
ATOM   14598 O  O     . LEU D 2 174 ? 127.084 92.145  148.799 1.00 20.41 ?  153 LEU D O     1 
ATOM   14599 C  CB    . LEU D 2 174 ? 123.874 91.253  148.727 1.00 20.62 ?  153 LEU D CB    1 
ATOM   14600 C  CG    . LEU D 2 174 ? 123.902 92.316  147.608 1.00 19.55 ?  153 LEU D CG    1 
ATOM   14601 C  CD1   . LEU D 2 174 ? 124.646 91.793  146.373 1.00 20.44 ?  153 LEU D CD1   1 
ATOM   14602 C  CD2   . LEU D 2 174 ? 122.471 92.745  147.254 1.00 20.99 ?  153 LEU D CD2   1 
ATOM   14603 N  N     . PHE D 2 175 ? 126.032 92.277  150.787 1.00 21.07 ?  154 PHE D N     1 
ATOM   14604 C  CA    . PHE D 2 175 ? 126.907 93.327  151.304 1.00 21.32 ?  154 PHE D CA    1 
ATOM   14605 C  C     . PHE D 2 175 ? 128.375 92.880  151.314 1.00 21.08 ?  154 PHE D C     1 
ATOM   14606 O  O     . PHE D 2 175 ? 129.264 93.626  150.899 1.00 20.85 ?  154 PHE D O     1 
ATOM   14607 C  CB    . PHE D 2 175 ? 126.473 93.743  152.713 1.00 21.20 ?  154 PHE D CB    1 
ATOM   14608 C  CG    . PHE D 2 175 ? 127.468 94.614  153.422 1.00 22.46 ?  154 PHE D CG    1 
ATOM   14609 C  CD1   . PHE D 2 175 ? 127.392 96.002  153.316 1.00 21.21 ?  154 PHE D CD1   1 
ATOM   14610 C  CD2   . PHE D 2 175 ? 128.481 94.054  154.205 1.00 22.53 ?  154 PHE D CD2   1 
ATOM   14611 C  CE1   . PHE D 2 175 ? 128.295 96.813  153.973 1.00 22.11 ?  154 PHE D CE1   1 
ATOM   14612 C  CE2   . PHE D 2 175 ? 129.407 94.863  154.857 1.00 23.26 ?  154 PHE D CE2   1 
ATOM   14613 C  CZ    . PHE D 2 175 ? 129.313 96.247  154.747 1.00 22.08 ?  154 PHE D CZ    1 
ATOM   14614 N  N     . LYS D 2 176 ? 128.617 91.668  151.800 1.00 21.14 ?  155 LYS D N     1 
ATOM   14615 C  CA    . LYS D 2 176 ? 129.974 91.111  151.845 1.00 20.93 ?  155 LYS D CA    1 
ATOM   14616 C  C     . LYS D 2 176 ? 130.617 91.045  150.462 1.00 20.61 ?  155 LYS D C     1 
ATOM   14617 O  O     . LYS D 2 176 ? 131.795 91.380  150.296 1.00 20.62 ?  155 LYS D O     1 
ATOM   14618 C  CB    . LYS D 2 176 ? 129.946 89.735  152.492 1.00 21.27 ?  155 LYS D CB    1 
ATOM   14619 C  CG    . LYS D 2 176 ? 129.722 89.816  153.977 1.00 22.04 ?  155 LYS D CG    1 
ATOM   14620 C  CD    . LYS D 2 176 ? 129.587 88.449  154.626 1.00 25.24 ?  155 LYS D CD    1 
ATOM   14621 C  CE    . LYS D 2 176 ? 129.430 88.622  156.115 1.00 25.83 ?  155 LYS D CE    1 
ATOM   14622 N  NZ    . LYS D 2 176 ? 129.309 87.325  156.842 1.00 26.64 1  155 LYS D NZ    1 
ATOM   14623 N  N     . ALA D 2 177 ? 129.830 90.639  149.472 1.00 20.02 ?  156 ALA D N     1 
ATOM   14624 C  CA    . ALA D 2 177 ? 130.286 90.631  148.084 1.00 19.86 ?  156 ALA D CA    1 
ATOM   14625 C  C     . ALA D 2 177 ? 130.555 92.047  147.555 1.00 19.61 ?  156 ALA D C     1 
ATOM   14626 O  O     . ALA D 2 177 ? 131.473 92.262  146.761 1.00 19.69 ?  156 ALA D O     1 
ATOM   14627 C  CB    . ALA D 2 177 ? 129.271 89.941  147.233 1.00 19.99 ?  156 ALA D CB    1 
ATOM   14628 N  N     . MET D 2 178 ? 129.745 93.011  147.987 1.00 19.75 ?  157 MET D N     1 
ATOM   14629 C  CA    . MET D 2 178 ? 129.920 94.411  147.548 1.00 18.89 ?  157 MET D CA    1 
ATOM   14630 C  C     . MET D 2 178 ? 131.208 94.984  148.118 1.00 18.62 ?  157 MET D C     1 
ATOM   14631 O  O     . MET D 2 178 ? 131.929 95.715  147.430 1.00 18.10 ?  157 MET D O     1 
ATOM   14632 C  CB    . MET D 2 178 ? 128.728 95.267  147.967 1.00 18.82 ?  157 MET D CB    1 
ATOM   14633 C  CG    . MET D 2 178 ? 127.486 95.020  147.126 1.00 20.20 ?  157 MET D CG    1 
ATOM   14634 S  SD    . MET D 2 178 ? 126.097 95.954  147.783 1.00 23.78 ?  157 MET D SD    1 
ATOM   14635 C  CE    . MET D 2 178 ? 124.895 95.677  146.484 1.00 22.62 ?  157 MET D CE    1 
ATOM   14636 N  N     . VAL D 2 179 ? 131.499 94.622  149.369 1.00 18.34 ?  158 VAL D N     1 
ATOM   14637 C  CA    . VAL D 2 179 ? 132.751 94.993  150.010 1.00 18.75 ?  158 VAL D CA    1 
ATOM   14638 C  C     . VAL D 2 179 ? 133.932 94.441  149.222 1.00 18.86 ?  158 VAL D C     1 
ATOM   14639 O  O     . VAL D 2 179 ? 134.898 95.176  148.954 1.00 18.79 ?  158 VAL D O     1 
ATOM   14640 C  CB    . VAL D 2 179 ? 132.834 94.517  151.485 1.00 19.02 ?  158 VAL D CB    1 
ATOM   14641 C  CG1   . VAL D 2 179 ? 134.252 94.734  152.033 1.00 19.10 ?  158 VAL D CG1   1 
ATOM   14642 C  CG2   . VAL D 2 179 ? 131.793 95.243  152.350 1.00 18.94 ?  158 VAL D CG2   1 
ATOM   14643 N  N     . ALA D 2 180 ? 133.854 93.151  148.868 1.00 18.96 ?  159 ALA D N     1 
ATOM   14644 C  CA    . ALA D 2 180 ? 134.864 92.515  148.019 1.00 19.05 ?  159 ALA D CA    1 
ATOM   14645 C  C     . ALA D 2 180 ? 135.016 93.259  146.691 1.00 18.67 ?  159 ALA D C     1 
ATOM   14646 O  O     . ALA D 2 180 ? 136.140 93.536  146.254 1.00 17.72 ?  159 ALA D O     1 
ATOM   14647 C  CB    . ALA D 2 180 ? 134.521 91.034  147.776 1.00 19.43 ?  159 ALA D CB    1 
ATOM   14648 N  N     . SER D 2 181 ? 133.883 93.609  146.074 1.00 18.49 ?  160 SER D N     1 
ATOM   14649 C  CA    . SER D 2 181 ? 133.902 94.338  144.805 1.00 18.51 ?  160 SER D CA    1 
ATOM   14650 C  C     . SER D 2 181 ? 134.559 95.713  144.930 1.00 18.23 ?  160 SER D C     1 
ATOM   14651 O  O     . SER D 2 181 ? 135.395 96.079  144.115 1.00 18.18 ?  160 SER D O     1 
ATOM   14652 C  CB    . SER D 2 181 ? 132.491 94.490  144.230 1.00 18.51 ?  160 SER D CB    1 
ATOM   14653 O  OG    . SER D 2 181 ? 132.573 95.044  142.931 1.00 19.42 ?  160 SER D OG    1 
ATOM   14654 N  N     . VAL D 2 182 ? 134.181 96.468  145.960 1.00 18.43 ?  161 VAL D N     1 
ATOM   14655 C  CA    . VAL D 2 182 ? 134.809 97.768  146.213 1.00 18.09 ?  161 VAL D CA    1 
ATOM   14656 C  C     . VAL D 2 182 ? 136.315 97.618  146.459 1.00 18.41 ?  161 VAL D C     1 
ATOM   14657 O  O     . VAL D 2 182 ? 137.112 98.400  145.937 1.00 18.52 ?  161 VAL D O     1 
ATOM   14658 C  CB    . VAL D 2 182 ? 134.129 98.521  147.363 1.00 17.71 ?  161 VAL D CB    1 
ATOM   14659 C  CG1   . VAL D 2 182 ? 134.935 99.784  147.750 1.00 16.02 ?  161 VAL D CG1   1 
ATOM   14660 C  CG2   . VAL D 2 182 ? 132.702 98.907  146.945 1.00 17.78 ?  161 VAL D CG2   1 
ATOM   14661 N  N     . TYR D 2 183 ? 136.702 96.588  147.213 1.00 19.06 ?  162 TYR D N     1 
ATOM   14662 C  CA    . TYR D 2 183 ? 138.122 96.349  147.450 1.00 19.73 ?  162 TYR D CA    1 
ATOM   14663 C  C     . TYR D 2 183 ? 138.863 96.056  146.153 1.00 19.90 ?  162 TYR D C     1 
ATOM   14664 O  O     . TYR D 2 183 ? 139.999 96.474  145.997 1.00 20.73 ?  162 TYR D O     1 
ATOM   14665 C  CB    . TYR D 2 183 ? 138.376 95.244  148.492 1.00 19.84 ?  162 TYR D CB    1 
ATOM   14666 C  CG    . TYR D 2 183 ? 138.072 95.649  149.920 1.00 20.24 ?  162 TYR D CG    1 
ATOM   14667 C  CD1   . TYR D 2 183 ? 137.857 96.982  150.261 1.00 21.51 ?  162 TYR D CD1   1 
ATOM   14668 C  CD2   . TYR D 2 183 ? 138.020 94.693  150.942 1.00 20.45 ?  162 TYR D CD2   1 
ATOM   14669 C  CE1   . TYR D 2 183 ? 137.583 97.355  151.583 1.00 21.68 ?  162 TYR D CE1   1 
ATOM   14670 C  CE2   . TYR D 2 183 ? 137.768 95.059  152.270 1.00 19.97 ?  162 TYR D CE2   1 
ATOM   14671 C  CZ    . TYR D 2 183 ? 137.546 96.391  152.579 1.00 21.83 ?  162 TYR D CZ    1 
ATOM   14672 O  OH    . TYR D 2 183 ? 137.286 96.765  153.883 1.00 21.96 ?  162 TYR D OH    1 
ATOM   14673 N  N     . LEU D 2 184 ? 138.227 95.365  145.217 1.00 20.22 ?  163 LEU D N     1 
ATOM   14674 C  CA    . LEU D 2 184 ? 138.877 95.105  143.935 1.00 20.89 ?  163 LEU D CA    1 
ATOM   14675 C  C     . LEU D 2 184 ? 138.985 96.404  143.122 1.00 20.72 ?  163 LEU D C     1 
ATOM   14676 O  O     . LEU D 2 184 ? 140.078 96.788  142.716 1.00 21.07 ?  163 LEU D O     1 
ATOM   14677 C  CB    . LEU D 2 184 ? 138.172 93.973  143.161 1.00 21.16 ?  163 LEU D CB    1 
ATOM   14678 C  CG    . LEU D 2 184 ? 138.689 93.584  141.761 1.00 22.77 ?  163 LEU D CG    1 
ATOM   14679 C  CD1   . LEU D 2 184 ? 140.208 93.303  141.739 1.00 22.44 ?  163 LEU D CD1   1 
ATOM   14680 C  CD2   . LEU D 2 184 ? 137.927 92.392  141.203 1.00 24.75 ?  163 LEU D CD2   1 
ATOM   14681 N  N     . GLU D 2 185 ? 137.858 97.087  142.933 1.00 20.65 ?  164 GLU D N     1 
ATOM   14682 C  CA    . GLU D 2 185 ? 137.794 98.316  142.128 1.00 20.69 ?  164 GLU D CA    1 
ATOM   14683 C  C     . GLU D 2 185 ? 138.663 99.461  142.648 1.00 20.64 ?  164 GLU D C     1 
ATOM   14684 O  O     . GLU D 2 185 ? 139.281 100.193 141.860 1.00 20.25 ?  164 GLU D O     1 
ATOM   14685 C  CB    . GLU D 2 185 ? 136.345 98.818  142.037 1.00 21.03 ?  164 GLU D CB    1 
ATOM   14686 C  CG    . GLU D 2 185 ? 135.352 97.824  141.428 1.00 22.19 ?  164 GLU D CG    1 
ATOM   14687 C  CD    . GLU D 2 185 ? 135.330 97.828  139.902 1.00 24.19 ?  164 GLU D CD    1 
ATOM   14688 O  OE1   . GLU D 2 185 ? 136.138 98.521  139.259 1.00 27.97 ?  164 GLU D OE1   1 
ATOM   14689 O  OE2   . GLU D 2 185 ? 134.477 97.148  139.330 1.00 25.47 -1 164 GLU D OE2   1 
ATOM   14690 N  N     . SER D 2 186 ? 138.683 99.632  143.966 1.00 20.42 ?  165 SER D N     1 
ATOM   14691 C  CA    . SER D 2 186 ? 139.263 100.827 144.577 1.00 20.70 ?  165 SER D CA    1 
ATOM   14692 C  C     . SER D 2 186 ? 140.580 100.578 145.312 1.00 20.88 ?  165 SER D C     1 
ATOM   14693 O  O     . SER D 2 186 ? 141.159 101.509 145.871 1.00 21.21 ?  165 SER D O     1 
ATOM   14694 C  CB    . SER D 2 186 ? 138.257 101.484 145.539 1.00 21.25 ?  165 SER D CB    1 
ATOM   14695 O  OG    . SER D 2 186 ? 137.001 101.714 144.916 1.00 20.97 ?  165 SER D OG    1 
ATOM   14696 N  N     . PHE D 2 187 ? 141.067 99.337  145.312 1.00 20.94 ?  166 PHE D N     1 
ATOM   14697 C  CA    . PHE D 2 187 ? 142.217 99.009  146.142 1.00 21.19 ?  166 PHE D CA    1 
ATOM   14698 C  C     . PHE D 2 187 ? 143.147 97.995  145.476 1.00 21.22 ?  166 PHE D C     1 
ATOM   14699 O  O     . PHE D 2 187 ? 144.299 98.335  145.185 1.00 21.10 ?  166 PHE D O     1 
ATOM   14700 C  CB    . PHE D 2 187 ? 141.746 98.615  147.569 1.00 21.63 ?  166 PHE D CB    1 
ATOM   14701 C  CG    . PHE D 2 187 ? 142.736 97.811  148.372 1.00 24.05 ?  166 PHE D CG    1 
ATOM   14702 C  CD1   . PHE D 2 187 ? 144.007 98.307  148.659 1.00 25.52 ?  166 PHE D CD1   1 
ATOM   14703 C  CD2   . PHE D 2 187 ? 142.373 96.570  148.887 1.00 27.03 ?  166 PHE D CD2   1 
ATOM   14704 C  CE1   . PHE D 2 187 ? 144.902 97.567  149.421 1.00 26.73 ?  166 PHE D CE1   1 
ATOM   14705 C  CE2   . PHE D 2 187 ? 143.279 95.815  149.648 1.00 27.36 ?  166 PHE D CE2   1 
ATOM   14706 C  CZ    . PHE D 2 187 ? 144.538 96.318  149.908 1.00 27.87 ?  166 PHE D CZ    1 
ATOM   14707 N  N     . LEU D 2 188 ? 142.646 96.797  145.188 1.00 20.78 ?  167 LEU D N     1 
ATOM   14708 C  CA    . LEU D 2 188 ? 143.493 95.709  144.658 1.00 21.78 ?  167 LEU D CA    1 
ATOM   14709 C  C     . LEU D 2 188 ? 144.120 95.982  143.285 1.00 21.91 ?  167 LEU D C     1 
ATOM   14710 O  O     . LEU D 2 188 ? 145.224 95.513  143.011 1.00 22.87 ?  167 LEU D O     1 
ATOM   14711 C  CB    . LEU D 2 188 ? 142.726 94.388  144.614 1.00 22.32 ?  167 LEU D CB    1 
ATOM   14712 C  CG    . LEU D 2 188 ? 142.295 93.702  145.910 1.00 23.33 ?  167 LEU D CG    1 
ATOM   14713 C  CD1   . LEU D 2 188 ? 141.536 92.434  145.560 1.00 22.43 ?  167 LEU D CD1   1 
ATOM   14714 C  CD2   . LEU D 2 188 ? 143.476 93.388  146.837 1.00 25.71 ?  167 LEU D CD2   1 
ATOM   14715 N  N     . PHE D 2 189 ? 143.413 96.716  142.422 1.00 21.56 ?  168 PHE D N     1 
ATOM   14716 C  CA    . PHE D 2 189 ? 143.945 97.100  141.112 1.00 21.86 ?  168 PHE D CA    1 
ATOM   14717 C  C     . PHE D 2 189 ? 145.184 98.015  141.216 1.00 21.87 ?  168 PHE D C     1 
ATOM   14718 O  O     . PHE D 2 189 ? 145.994 98.085  140.288 1.00 21.79 ?  168 PHE D O     1 
ATOM   14719 C  CB    . PHE D 2 189 ? 142.885 97.843  140.279 1.00 21.79 ?  168 PHE D CB    1 
ATOM   14720 C  CG    . PHE D 2 189 ? 141.867 96.947  139.611 1.00 21.88 ?  168 PHE D CG    1 
ATOM   14721 C  CD1   . PHE D 2 189 ? 142.232 95.720  139.053 1.00 21.44 ?  168 PHE D CD1   1 
ATOM   14722 C  CD2   . PHE D 2 189 ? 140.538 97.360  139.511 1.00 22.82 ?  168 PHE D CD2   1 
ATOM   14723 C  CE1   . PHE D 2 189 ? 141.279 94.903  138.430 1.00 22.35 ?  168 PHE D CE1   1 
ATOM   14724 C  CE2   . PHE D 2 189 ? 139.577 96.561  138.892 1.00 22.08 ?  168 PHE D CE2   1 
ATOM   14725 C  CZ    . PHE D 2 189 ? 139.944 95.322  138.359 1.00 22.60 ?  168 PHE D CZ    1 
ATOM   14726 N  N     . TYR D 2 190 ? 145.318 98.731  142.328 1.00 21.91 ?  169 TYR D N     1 
ATOM   14727 C  CA    . TYR D 2 190 ? 146.281 99.841  142.377 1.00 22.52 ?  169 TYR D CA    1 
ATOM   14728 C  C     . TYR D 2 190 ? 147.751 99.448  142.540 1.00 22.75 ?  169 TYR D C     1 
ATOM   14729 O  O     . TYR D 2 190 ? 148.619 100.193 142.105 1.00 21.93 ?  169 TYR D O     1 
ATOM   14730 C  CB    . TYR D 2 190 ? 145.843 100.925 143.366 1.00 22.67 ?  169 TYR D CB    1 
ATOM   14731 C  CG    . TYR D 2 190 ? 144.717 101.755 142.783 1.00 24.77 ?  169 TYR D CG    1 
ATOM   14732 C  CD1   . TYR D 2 190 ? 143.413 101.254 142.716 1.00 25.65 ?  169 TYR D CD1   1 
ATOM   14733 C  CD2   . TYR D 2 190 ? 144.965 103.020 142.256 1.00 25.94 ?  169 TYR D CD2   1 
ATOM   14734 C  CE1   . TYR D 2 190 ? 142.381 102.008 142.148 1.00 26.62 ?  169 TYR D CE1   1 
ATOM   14735 C  CE2   . TYR D 2 190 ? 143.941 103.786 141.703 1.00 26.91 ?  169 TYR D CE2   1 
ATOM   14736 C  CZ    . TYR D 2 190 ? 142.658 103.276 141.649 1.00 27.39 ?  169 TYR D CZ    1 
ATOM   14737 O  OH    . TYR D 2 190 ? 141.658 104.049 141.090 1.00 27.50 ?  169 TYR D OH    1 
ATOM   14738 N  N     . SER D 2 191 ? 148.025 98.277  143.123 1.00 22.74 ?  170 SER D N     1 
ATOM   14739 C  CA    . SER D 2 191 ? 149.392 97.742  143.107 1.00 23.43 ?  170 SER D CA    1 
ATOM   14740 C  C     . SER D 2 191 ? 149.824 97.512  141.658 1.00 23.08 ?  170 SER D C     1 
ATOM   14741 O  O     . SER D 2 191 ? 150.995 97.603  141.332 1.00 23.67 ?  170 SER D O     1 
ATOM   14742 C  CB    . SER D 2 191 ? 149.514 96.442  143.918 1.00 23.39 ?  170 SER D CB    1 
ATOM   14743 O  OG    . SER D 2 191 ? 148.687 95.416  143.388 1.00 24.10 ?  170 SER D OG    1 
ATOM   14744 N  N     . GLY D 2 192 ? 148.853 97.254  140.791 1.00 22.82 ?  171 GLY D N     1 
ATOM   14745 C  CA    . GLY D 2 192 ? 149.095 97.074  139.365 1.00 22.08 ?  171 GLY D CA    1 
ATOM   14746 C  C     . GLY D 2 192 ? 149.140 98.378  138.586 1.00 22.12 ?  171 GLY D C     1 
ATOM   14747 O  O     . GLY D 2 192 ? 150.081 98.611  137.825 1.00 22.86 ?  171 GLY D O     1 
ATOM   14748 N  N     . PHE D 2 193 ? 148.133 99.230  138.774 1.00 21.48 ?  172 PHE D N     1 
ATOM   14749 C  CA    . PHE D 2 193 ? 148.068 100.535 138.090 1.00 21.06 ?  172 PHE D CA    1 
ATOM   14750 C  C     . PHE D 2 193 ? 149.323 101.377 138.318 1.00 21.13 ?  172 PHE D C     1 
ATOM   14751 O  O     . PHE D 2 193 ? 149.686 102.188 137.465 1.00 21.18 ?  172 PHE D O     1 
ATOM   14752 C  CB    . PHE D 2 193 ? 146.857 101.342 138.556 1.00 21.33 ?  172 PHE D CB    1 
ATOM   14753 C  CG    . PHE D 2 193 ? 145.527 100.826 138.061 1.00 20.93 ?  172 PHE D CG    1 
ATOM   14754 C  CD1   . PHE D 2 193 ? 145.411 100.161 136.840 1.00 20.88 ?  172 PHE D CD1   1 
ATOM   14755 C  CD2   . PHE D 2 193 ? 144.378 101.057 138.805 1.00 19.83 ?  172 PHE D CD2   1 
ATOM   14756 C  CE1   . PHE D 2 193 ? 144.163 99.708  136.394 1.00 22.31 ?  172 PHE D CE1   1 
ATOM   14757 C  CE2   . PHE D 2 193 ? 143.126 100.619 138.359 1.00 20.67 ?  172 PHE D CE2   1 
ATOM   14758 C  CZ    . PHE D 2 193 ? 143.020 99.944  137.152 1.00 21.00 ?  172 PHE D CZ    1 
ATOM   14759 N  N     . TYR D 2 194 ? 149.986 101.172 139.459 1.00 20.48 ?  173 TYR D N     1 
ATOM   14760 C  CA    . TYR D 2 194 ? 151.167 101.954 139.819 1.00 20.76 ?  173 TYR D CA    1 
ATOM   14761 C  C     . TYR D 2 194 ? 152.171 102.047 138.665 1.00 20.53 ?  173 TYR D C     1 
ATOM   14762 O  O     . TYR D 2 194 ? 152.628 103.134 138.296 1.00 19.89 ?  173 TYR D O     1 
ATOM   14763 C  CB    . TYR D 2 194 ? 151.856 101.380 141.083 1.00 20.94 ?  173 TYR D CB    1 
ATOM   14764 C  CG    . TYR D 2 194 ? 152.944 102.295 141.618 1.00 21.56 ?  173 TYR D CG    1 
ATOM   14765 C  CD1   . TYR D 2 194 ? 152.697 103.150 142.695 1.00 22.23 ?  173 TYR D CD1   1 
ATOM   14766 C  CD2   . TYR D 2 194 ? 154.215 102.323 141.032 1.00 22.00 ?  173 TYR D CD2   1 
ATOM   14767 C  CE1   . TYR D 2 194 ? 153.686 104.008 143.173 1.00 21.58 ?  173 TYR D CE1   1 
ATOM   14768 C  CE2   . TYR D 2 194 ? 155.203 103.166 141.505 1.00 20.52 ?  173 TYR D CE2   1 
ATOM   14769 C  CZ    . TYR D 2 194 ? 154.934 104.006 142.572 1.00 21.66 ?  173 TYR D CZ    1 
ATOM   14770 O  OH    . TYR D 2 194 ? 155.910 104.861 143.024 1.00 21.37 ?  173 TYR D OH    1 
ATOM   14771 N  N     . TYR D 2 195 ? 152.488 100.907 138.074 1.00 20.77 ?  174 TYR D N     1 
ATOM   14772 C  CA    . TYR D 2 195 ? 153.582 100.861 137.120 1.00 21.12 ?  174 TYR D CA    1 
ATOM   14773 C  C     . TYR D 2 195 ? 153.284 101.614 135.812 1.00 21.49 ?  174 TYR D C     1 
ATOM   14774 O  O     . TYR D 2 195 ? 154.089 102.460 135.410 1.00 21.60 ?  174 TYR D O     1 
ATOM   14775 C  CB    . TYR D 2 195 ? 154.042 99.416  136.907 1.00 21.23 ?  174 TYR D CB    1 
ATOM   14776 C  CG    . TYR D 2 195 ? 155.506 99.256  136.561 1.00 21.77 ?  174 TYR D CG    1 
ATOM   14777 C  CD1   . TYR D 2 195 ? 156.487 100.056 137.157 1.00 23.28 ?  174 TYR D CD1   1 
ATOM   14778 C  CD2   . TYR D 2 195 ? 155.913 98.283  135.651 1.00 22.87 ?  174 TYR D CD2   1 
ATOM   14779 C  CE1   . TYR D 2 195 ? 157.841 99.892  136.832 1.00 23.81 ?  174 TYR D CE1   1 
ATOM   14780 C  CE2   . TYR D 2 195 ? 157.258 98.109  135.332 1.00 24.09 ?  174 TYR D CE2   1 
ATOM   14781 C  CZ    . TYR D 2 195 ? 158.211 98.917  135.918 1.00 23.51 ?  174 TYR D CZ    1 
ATOM   14782 O  OH    . TYR D 2 195 ? 159.542 98.746  135.589 1.00 25.36 ?  174 TYR D OH    1 
ATOM   14783 N  N     . PRO D 2 196 ? 152.132 101.330 135.150 1.00 21.86 ?  175 PRO D N     1 
ATOM   14784 C  CA    . PRO D 2 196 ? 151.765 102.123 133.967 1.00 22.03 ?  175 PRO D CA    1 
ATOM   14785 C  C     . PRO D 2 196 ? 151.682 103.621 134.257 1.00 22.18 ?  175 PRO D C     1 
ATOM   14786 O  O     . PRO D 2 196 ? 152.093 104.421 133.413 1.00 23.00 ?  175 PRO D O     1 
ATOM   14787 C  CB    . PRO D 2 196 ? 150.376 101.594 133.585 1.00 21.50 ?  175 PRO D CB    1 
ATOM   14788 C  CG    . PRO D 2 196 ? 150.283 100.276 134.174 1.00 22.47 ?  175 PRO D CG    1 
ATOM   14789 C  CD    . PRO D 2 196 ? 151.254 100.157 135.311 1.00 20.91 ?  175 PRO D CD    1 
ATOM   14790 N  N     . LEU D 2 197 ? 151.172 103.997 135.431 1.00 21.70 ?  176 LEU D N     1 
ATOM   14791 C  CA    . LEU D 2 197 ? 151.126 105.411 135.831 1.00 22.40 ?  176 LEU D CA    1 
ATOM   14792 C  C     . LEU D 2 197 ? 152.521 106.006 136.038 1.00 22.58 ?  176 LEU D C     1 
ATOM   14793 O  O     . LEU D 2 197 ? 152.763 107.173 135.704 1.00 22.15 ?  176 LEU D O     1 
ATOM   14794 C  CB    . LEU D 2 197 ? 150.313 105.596 137.105 1.00 22.15 ?  176 LEU D CB    1 
ATOM   14795 C  CG    . LEU D 2 197 ? 148.790 105.418 137.058 1.00 23.08 ?  176 LEU D CG    1 
ATOM   14796 C  CD1   . LEU D 2 197 ? 148.279 105.295 138.484 1.00 21.62 ?  176 LEU D CD1   1 
ATOM   14797 C  CD2   . LEU D 2 197 ? 148.114 106.591 136.320 1.00 21.94 ?  176 LEU D CD2   1 
ATOM   14798 N  N     . TYR D 2 198 ? 153.419 105.192 136.599 1.00 22.76 ?  177 TYR D N     1 
ATOM   14799 C  CA    . TYR D 2 198 ? 154.825 105.552 136.791 1.00 23.23 ?  177 TYR D CA    1 
ATOM   14800 C  C     . TYR D 2 198 ? 155.509 105.838 135.453 1.00 23.91 ?  177 TYR D C     1 
ATOM   14801 O  O     . TYR D 2 198 ? 156.196 106.860 135.309 1.00 24.20 ?  177 TYR D O     1 
ATOM   14802 C  CB    . TYR D 2 198 ? 155.553 104.446 137.573 1.00 23.19 ?  177 TYR D CB    1 
ATOM   14803 C  CG    . TYR D 2 198 ? 157.015 104.706 137.882 1.00 23.52 ?  177 TYR D CG    1 
ATOM   14804 C  CD1   . TYR D 2 198 ? 157.393 105.717 138.754 1.00 24.85 ?  177 TYR D CD1   1 
ATOM   14805 C  CD2   . TYR D 2 198 ? 158.020 103.901 137.330 1.00 25.30 ?  177 TYR D CD2   1 
ATOM   14806 C  CE1   . TYR D 2 198 ? 158.737 105.948 139.057 1.00 26.05 ?  177 TYR D CE1   1 
ATOM   14807 C  CE2   . TYR D 2 198 ? 159.375 104.121 137.631 1.00 26.38 ?  177 TYR D CE2   1 
ATOM   14808 C  CZ    . TYR D 2 198 ? 159.716 105.145 138.495 1.00 26.68 ?  177 TYR D CZ    1 
ATOM   14809 O  OH    . TYR D 2 198 ? 161.036 105.381 138.810 1.00 30.01 ?  177 TYR D OH    1 
ATOM   14810 N  N     . PHE D 2 199 ? 155.320 104.958 134.470 1.00 24.84 ?  178 PHE D N     1 
ATOM   14811 C  CA    . PHE D 2 199 ? 155.834 105.232 133.124 1.00 25.81 ?  178 PHE D CA    1 
ATOM   14812 C  C     . PHE D 2 199 ? 155.174 106.437 132.465 1.00 26.23 ?  178 PHE D C     1 
ATOM   14813 O  O     . PHE D 2 199 ? 155.856 107.283 131.887 1.00 26.58 ?  178 PHE D O     1 
ATOM   14814 C  CB    . PHE D 2 199 ? 155.721 104.008 132.225 1.00 26.08 ?  178 PHE D CB    1 
ATOM   14815 C  CG    . PHE D 2 199 ? 156.749 102.955 132.515 1.00 28.71 ?  178 PHE D CG    1 
ATOM   14816 C  CD1   . PHE D 2 199 ? 158.083 103.297 132.690 1.00 32.03 ?  178 PHE D CD1   1 
ATOM   14817 C  CD2   . PHE D 2 199 ? 156.389 101.622 132.619 1.00 31.77 ?  178 PHE D CD2   1 
ATOM   14818 C  CE1   . PHE D 2 199 ? 159.052 102.322 132.974 1.00 32.29 ?  178 PHE D CE1   1 
ATOM   14819 C  CE2   . PHE D 2 199 ? 157.350 100.643 132.893 1.00 32.72 ?  178 PHE D CE2   1 
ATOM   14820 C  CZ    . PHE D 2 199 ? 158.682 101.002 133.069 1.00 31.91 ?  178 PHE D CZ    1 
ATOM   14821 N  N     . TYR D 2 200 ? 153.849 106.493 132.565 1.00 26.46 ?  179 TYR D N     1 
ATOM   14822 C  CA    . TYR D 2 200 ? 153.025 107.567 131.986 1.00 27.43 ?  179 TYR D CA    1 
ATOM   14823 C  C     . TYR D 2 200 ? 153.466 108.931 132.505 1.00 27.68 ?  179 TYR D C     1 
ATOM   14824 O  O     . TYR D 2 200 ? 153.522 109.899 131.748 1.00 28.71 ?  179 TYR D O     1 
ATOM   14825 C  CB    . TYR D 2 200 ? 151.571 107.309 132.365 1.00 27.27 ?  179 TYR D CB    1 
ATOM   14826 C  CG    . TYR D 2 200 ? 150.504 108.031 131.579 1.00 28.90 ?  179 TYR D CG    1 
ATOM   14827 C  CD1   . TYR D 2 200 ? 150.523 108.063 130.191 1.00 29.00 ?  179 TYR D CD1   1 
ATOM   14828 C  CD2   . TYR D 2 200 ? 149.427 108.626 132.242 1.00 30.14 ?  179 TYR D CD2   1 
ATOM   14829 C  CE1   . TYR D 2 200 ? 149.516 108.706 129.474 1.00 31.26 ?  179 TYR D CE1   1 
ATOM   14830 C  CE2   . TYR D 2 200 ? 148.413 109.259 131.541 1.00 31.86 ?  179 TYR D CE2   1 
ATOM   14831 C  CZ    . TYR D 2 200 ? 148.465 109.301 130.158 1.00 32.51 ?  179 TYR D CZ    1 
ATOM   14832 O  OH    . TYR D 2 200 ? 147.461 109.932 129.463 1.00 33.77 ?  179 TYR D OH    1 
ATOM   14833 N  N     . GLY D 2 201 ? 153.783 109.001 133.797 1.00 27.68 ?  180 GLY D N     1 
ATOM   14834 C  CA    . GLY D 2 201 ? 154.279 110.228 134.411 1.00 28.02 ?  180 GLY D CA    1 
ATOM   14835 C  C     . GLY D 2 201 ? 155.689 110.636 133.994 1.00 28.60 ?  180 GLY D C     1 
ATOM   14836 O  O     . GLY D 2 201 ? 156.094 111.763 134.245 1.00 28.44 ?  180 GLY D O     1 
ATOM   14837 N  N     . GLN D 2 202 ? 156.428 109.710 133.377 1.00 29.34 ?  181 GLN D N     1 
ATOM   14838 C  CA    . GLN D 2 202 ? 157.801 109.935 132.892 1.00 30.39 ?  181 GLN D CA    1 
ATOM   14839 C  C     . GLN D 2 202 ? 157.885 110.157 131.381 1.00 30.55 ?  181 GLN D C     1 
ATOM   14840 O  O     . GLN D 2 202 ? 158.979 110.371 130.850 1.00 31.23 ?  181 GLN D O     1 
ATOM   14841 C  CB    . GLN D 2 202 ? 158.667 108.700 133.150 1.00 30.31 ?  181 GLN D CB    1 
ATOM   14842 C  CG    . GLN D 2 202 ? 158.992 108.355 134.553 1.00 32.40 ?  181 GLN D CG    1 
ATOM   14843 C  CD    . GLN D 2 202 ? 159.844 107.104 134.602 1.00 33.85 ?  181 GLN D CD    1 
ATOM   14844 O  OE1   . GLN D 2 202 ? 159.371 106.026 134.953 1.00 33.94 ?  181 GLN D OE1   1 
ATOM   14845 N  NE2   . GLN D 2 202 ? 161.098 107.233 134.203 1.00 34.92 ?  181 GLN D NE2   1 
ATOM   14846 N  N     . GLY D 2 203 ? 156.764 110.035 130.681 1.00 30.57 ?  182 GLY D N     1 
ATOM   14847 C  CA    . GLY D 2 203 ? 156.760 110.161 129.222 1.00 30.83 ?  182 GLY D CA    1 
ATOM   14848 C  C     . GLY D 2 203 ? 157.010 108.856 128.482 1.00 30.80 ?  182 GLY D C     1 
ATOM   14849 O  O     . GLY D 2 203 ? 157.231 108.860 127.268 1.00 30.86 ?  182 GLY D O     1 
ATOM   14850 N  N     . LYS D 2 204 ? 156.968 107.739 129.209 1.00 30.14 ?  183 LYS D N     1 
ATOM   14851 C  CA    . LYS D 2 204 ? 157.157 106.414 128.611 1.00 30.35 ?  183 LYS D CA    1 
ATOM   14852 C  C     . LYS D 2 204 ? 155.836 105.662 128.467 1.00 29.52 ?  183 LYS D C     1 
ATOM   14853 O  O     . LYS D 2 204 ? 154.945 105.811 129.300 1.00 28.60 ?  183 LYS D O     1 
ATOM   14854 C  CB    . LYS D 2 204 ? 158.144 105.591 129.437 1.00 30.76 ?  183 LYS D CB    1 
ATOM   14855 C  CG    . LYS D 2 204 ? 159.567 106.159 129.434 1.00 32.95 ?  183 LYS D CG    1 
ATOM   14856 C  CD    . LYS D 2 204 ? 160.401 105.469 130.486 1.00 36.37 ?  183 LYS D CD    1 
ATOM   14857 C  CE    . LYS D 2 204 ? 161.825 105.994 130.524 1.00 38.47 ?  183 LYS D CE    1 
ATOM   14858 N  NZ    . LYS D 2 204 ? 162.493 105.446 131.742 1.00 40.21 1  183 LYS D NZ    1 
ATOM   14859 N  N     . LEU D 2 205 ? 155.726 104.849 127.413 1.00 29.47 ?  184 LEU D N     1 
ATOM   14860 C  CA    . LEU D 2 205 ? 154.515 104.062 127.128 1.00 29.06 ?  184 LEU D CA    1 
ATOM   14861 C  C     . LEU D 2 205 ? 153.231 104.893 127.334 1.00 28.96 ?  184 LEU D C     1 
ATOM   14862 O  O     . LEU D 2 205 ? 152.324 104.513 128.085 1.00 27.68 ?  184 LEU D O     1 
ATOM   14863 C  CB    . LEU D 2 205 ? 154.488 102.769 127.958 1.00 28.63 ?  184 LEU D CB    1 
ATOM   14864 C  CG    . LEU D 2 205 ? 155.680 101.808 127.833 1.00 29.00 ?  184 LEU D CG    1 
ATOM   14865 C  CD1   . LEU D 2 205 ? 155.510 100.624 128.789 1.00 28.90 ?  184 LEU D CD1   1 
ATOM   14866 C  CD2   . LEU D 2 205 ? 155.849 101.309 126.404 1.00 28.67 ?  184 LEU D CD2   1 
ATOM   14867 N  N     . MET D 2 206 ? 153.190 106.028 126.642 1.00 29.02 ?  185 MET D N     1 
ATOM   14868 C  CA    . MET D 2 206 ? 152.121 107.009 126.751 1.00 29.72 ?  185 MET D CA    1 
ATOM   14869 C  C     . MET D 2 206 ? 150.766 106.569 126.208 1.00 29.54 ?  185 MET D C     1 
ATOM   14870 O  O     . MET D 2 206 ? 149.736 106.984 126.733 1.00 29.47 ?  185 MET D O     1 
ATOM   14871 C  CB    . MET D 2 206 ? 152.549 108.317 126.074 1.00 30.69 ?  185 MET D CB    1 
ATOM   14872 C  CG    . MET D 2 206 ? 153.816 108.908 126.674 1.00 32.03 ?  185 MET D CG    1 
ATOM   14873 S  SD    . MET D 2 206 ? 153.618 109.237 128.434 1.00 36.63 ?  185 MET D SD    1 
ATOM   14874 C  CE    . MET D 2 206 ? 152.853 110.848 128.381 1.00 33.80 ?  185 MET D CE    1 
ATOM   14875 N  N     . GLN D 2 207 ? 150.766 105.760 125.150 1.00 29.56 ?  186 GLN D N     1 
ATOM   14876 C  CA    . GLN D 2 207 ? 149.518 105.299 124.530 1.00 29.17 ?  186 GLN D CA    1 
ATOM   14877 C  C     . GLN D 2 207 ? 148.821 104.277 125.423 1.00 28.26 ?  186 GLN D C     1 
ATOM   14878 O  O     . GLN D 2 207 ? 147.624 104.387 125.672 1.00 27.98 ?  186 GLN D O     1 
ATOM   14879 C  CB    . GLN D 2 207 ? 149.768 104.712 123.132 1.00 29.80 ?  186 GLN D CB    1 
ATOM   14880 C  CG    . GLN D 2 207 ? 150.515 105.639 122.175 1.00 31.75 ?  186 GLN D CG    1 
ATOM   14881 C  CD    . GLN D 2 207 ? 149.877 107.011 122.092 1.00 34.93 ?  186 GLN D CD    1 
ATOM   14882 O  OE1   . GLN D 2 207 ? 148.790 107.178 121.523 1.00 36.91 ?  186 GLN D OE1   1 
ATOM   14883 N  NE2   . GLN D 2 207 ? 150.545 108.002 122.670 1.00 36.09 ?  186 GLN D NE2   1 
ATOM   14884 N  N     . SER D 2 208 ? 149.570 103.286 125.905 0.50 27.75 ?  187 SER D N     1 
ATOM   14885 C  CA    . SER D 2 208 ? 149.009 102.291 126.811 0.50 27.12 ?  187 SER D CA    1 
ATOM   14886 C  C     . SER D 2 208 ? 148.699 102.911 128.170 0.50 26.72 ?  187 SER D C     1 
ATOM   14887 O  O     . SER D 2 208 ? 147.748 102.498 128.832 0.50 26.30 ?  187 SER D O     1 
ATOM   14888 C  CB    . SER D 2 208 ? 149.942 101.089 126.963 0.50 26.88 ?  187 SER D CB    1 
ATOM   14889 O  OG    . SER D 2 208 ? 151.244 101.509 127.304 0.50 26.59 ?  187 SER D OG    1 
ATOM   14890 N  N     . GLY D 2 209 ? 149.500 103.898 128.574 1.00 26.64 ?  188 GLY D N     1 
ATOM   14891 C  CA    . GLY D 2 209 ? 149.255 104.651 129.820 1.00 26.43 ?  188 GLY D CA    1 
ATOM   14892 C  C     . GLY D 2 209 ? 147.969 105.466 129.767 1.00 26.66 ?  188 GLY D C     1 
ATOM   14893 O  O     . GLY D 2 209 ? 147.263 105.601 130.767 1.00 26.57 ?  188 GLY D O     1 
ATOM   14894 N  N     . GLU D 2 210 ? 147.663 106.019 128.597 1.00 27.42 ?  189 GLU D N     1 
ATOM   14895 C  CA    . GLU D 2 210 ? 146.400 106.727 128.395 1.00 27.73 ?  189 GLU D CA    1 
ATOM   14896 C  C     . GLU D 2 210 ? 145.225 105.748 128.530 1.00 27.04 ?  189 GLU D C     1 
ATOM   14897 O  O     . GLU D 2 210 ? 144.244 106.034 129.217 1.00 26.57 ?  189 GLU D O     1 
ATOM   14898 C  CB    . GLU D 2 210 ? 146.377 107.447 127.034 1.00 28.28 ?  189 GLU D CB    1 
ATOM   14899 C  CG    . GLU D 2 210 ? 145.111 108.290 126.810 1.00 30.71 ?  189 GLU D CG    1 
ATOM   14900 C  CD    . GLU D 2 210 ? 145.179 109.216 125.597 1.00 35.43 ?  189 GLU D CD    1 
ATOM   14901 O  OE1   . GLU D 2 210 ? 146.141 109.126 124.793 1.00 36.89 ?  189 GLU D OE1   1 
ATOM   14902 O  OE2   . GLU D 2 210 ? 144.256 110.051 125.455 1.00 37.04 -1 189 GLU D OE2   1 
ATOM   14903 N  N     . ILE D 2 211 ? 145.340 104.591 127.885 1.00 26.80 ?  190 ILE D N     1 
ATOM   14904 C  CA    . ILE D 2 211 ? 144.340 103.536 128.023 1.00 26.92 ?  190 ILE D CA    1 
ATOM   14905 C  C     . ILE D 2 211 ? 144.153 103.144 129.483 1.00 26.45 ?  190 ILE D C     1 
ATOM   14906 O  O     . ILE D 2 211 ? 143.021 103.063 129.954 1.00 26.65 ?  190 ILE D O     1 
ATOM   14907 C  CB    . ILE D 2 211 ? 144.669 102.300 127.148 1.00 27.00 ?  190 ILE D CB    1 
ATOM   14908 C  CG1   . ILE D 2 211 ? 144.476 102.653 125.668 1.00 28.77 ?  190 ILE D CG1   1 
ATOM   14909 C  CG2   . ILE D 2 211 ? 143.779 101.106 127.531 1.00 26.82 ?  190 ILE D CG2   1 
ATOM   14910 C  CD1   . ILE D 2 211 ? 144.914 101.573 124.687 1.00 30.88 ?  190 ILE D CD1   1 
ATOM   14911 N  N     . ILE D 2 212 ? 145.255 102.930 130.207 1.00 26.49 ?  191 ILE D N     1 
ATOM   14912 C  CA    . ILE D 2 212 ? 145.168 102.504 131.604 1.00 25.73 ?  191 ILE D CA    1 
ATOM   14913 C  C     . ILE D 2 212 ? 144.480 103.573 132.456 1.00 25.48 ?  191 ILE D C     1 
ATOM   14914 O  O     . ILE D 2 212 ? 143.675 103.254 133.336 1.00 24.95 ?  191 ILE D O     1 
ATOM   14915 C  CB    . ILE D 2 212 ? 146.557 102.119 132.197 1.00 26.44 ?  191 ILE D CB    1 
ATOM   14916 C  CG1   . ILE D 2 212 ? 147.124 100.879 131.494 1.00 26.71 ?  191 ILE D CG1   1 
ATOM   14917 C  CG2   . ILE D 2 212 ? 146.471 101.898 133.723 1.00 26.01 ?  191 ILE D CG2   1 
ATOM   14918 C  CD1   . ILE D 2 212 ? 146.311 99.606  131.635 1.00 30.50 ?  191 ILE D CD1   1 
ATOM   14919 N  N     . ASN D 2 213 ? 144.782 104.836 132.171 1.00 24.79 ?  192 ASN D N     1 
ATOM   14920 C  CA    . ASN D 2 213 ? 144.163 105.944 132.884 1.00 24.80 ?  192 ASN D CA    1 
ATOM   14921 C  C     . ASN D 2 213 ? 142.635 106.000 132.680 1.00 24.44 ?  192 ASN D C     1 
ATOM   14922 O  O     . ASN D 2 213 ? 141.889 106.366 133.595 1.00 23.25 ?  192 ASN D O     1 
ATOM   14923 C  CB    . ASN D 2 213 ? 144.826 107.264 132.484 1.00 25.68 ?  192 ASN D CB    1 
ATOM   14924 C  CG    . ASN D 2 213 ? 144.962 108.226 133.649 1.00 27.89 ?  192 ASN D CG    1 
ATOM   14925 O  OD1   . ASN D 2 213 ? 145.104 107.819 134.799 1.00 31.05 ?  192 ASN D OD1   1 
ATOM   14926 N  ND2   . ASN D 2 213 ? 144.926 109.517 133.349 1.00 31.70 ?  192 ASN D ND2   1 
ATOM   14927 N  N     . LEU D 2 214 ? 142.176 105.622 131.486 1.00 23.60 ?  193 LEU D N     1 
ATOM   14928 C  CA    . LEU D 2 214 ? 140.742 105.594 131.196 1.00 23.84 ?  193 LEU D CA    1 
ATOM   14929 C  C     . LEU D 2 214 ? 140.081 104.442 131.932 1.00 23.48 ?  193 LEU D C     1 
ATOM   14930 O  O     . LEU D 2 214 ? 138.989 104.598 132.485 1.00 24.12 ?  193 LEU D O     1 
ATOM   14931 C  CB    . LEU D 2 214 ? 140.494 105.475 129.693 1.00 23.71 ?  193 LEU D CB    1 
ATOM   14932 C  CG    . LEU D 2 214 ? 140.773 106.743 128.875 1.00 25.29 ?  193 LEU D CG    1 
ATOM   14933 C  CD1   . LEU D 2 214 ? 140.633 106.456 127.379 1.00 25.41 ?  193 LEU D CD1   1 
ATOM   14934 C  CD2   . LEU D 2 214 ? 139.857 107.886 129.281 1.00 25.80 ?  193 LEU D CD2   1 
ATOM   14935 N  N     . ILE D 2 215 ? 140.757 103.293 131.941 1.00 22.89 ?  194 ILE D N     1 
ATOM   14936 C  CA    . ILE D 2 215 ? 140.287 102.121 132.665 1.00 22.25 ?  194 ILE D CA    1 
ATOM   14937 C  C     . ILE D 2 215 ? 140.182 102.460 134.148 1.00 22.55 ?  194 ILE D C     1 
ATOM   14938 O  O     . ILE D 2 215 ? 139.142 102.230 134.781 1.00 22.53 ?  194 ILE D O     1 
ATOM   14939 C  CB    . ILE D 2 215 ? 141.227 100.913 132.473 1.00 22.37 ?  194 ILE D CB    1 
ATOM   14940 C  CG1   . ILE D 2 215 ? 141.189 100.435 131.016 1.00 21.89 ?  194 ILE D CG1   1 
ATOM   14941 C  CG2   . ILE D 2 215 ? 140.863 99.783  133.457 1.00 20.25 ?  194 ILE D CG2   1 
ATOM   14942 C  CD1   . ILE D 2 215 ? 142.103 99.241  130.716 1.00 20.48 ?  194 ILE D CD1   1 
ATOM   14943 N  N     . LEU D 2 216 ? 141.257 103.023 134.694 1.00 22.35 ?  195 LEU D N     1 
ATOM   14944 C  CA    . LEU D 2 216 ? 141.316 103.354 136.115 1.00 22.51 ?  195 LEU D CA    1 
ATOM   14945 C  C     . LEU D 2 216 ? 140.184 104.317 136.487 1.00 22.30 ?  195 LEU D C     1 
ATOM   14946 O  O     . LEU D 2 216 ? 139.556 104.157 137.542 1.00 21.62 ?  195 LEU D O     1 
ATOM   14947 C  CB    . LEU D 2 216 ? 142.688 103.962 136.445 1.00 23.06 ?  195 LEU D CB    1 
ATOM   14948 C  CG    . LEU D 2 216 ? 143.055 104.537 137.822 1.00 23.98 ?  195 LEU D CG    1 
ATOM   14949 C  CD1   . LEU D 2 216 ? 144.554 104.673 137.888 1.00 24.44 ?  195 LEU D CD1   1 
ATOM   14950 C  CD2   . LEU D 2 216 ? 142.400 105.904 138.079 1.00 25.00 ?  195 LEU D CD2   1 
ATOM   14951 N  N     . ARG D 2 217 ? 139.938 105.310 135.625 1.00 21.64 ?  196 ARG D N     1 
ATOM   14952 C  CA    . ARG D 2 217 ? 138.851 106.272 135.839 1.00 22.49 ?  196 ARG D CA    1 
ATOM   14953 C  C     . ARG D 2 217 ? 137.471 105.571 135.900 1.00 21.56 ?  196 ARG D C     1 
ATOM   14954 O  O     . ARG D 2 217 ? 136.634 105.941 136.713 1.00 21.32 ?  196 ARG D O     1 
ATOM   14955 C  CB    . ARG D 2 217 ? 138.867 107.404 134.793 1.00 23.07 ?  196 ARG D CB    1 
ATOM   14956 C  CG    . ARG D 2 217 ? 137.856 108.537 135.075 1.00 25.64 ?  196 ARG D CG    1 
ATOM   14957 C  CD    . ARG D 2 217 ? 137.732 109.539 133.913 1.00 32.11 ?  196 ARG D CD    1 
ATOM   14958 N  NE    . ARG D 2 217 ? 137.315 108.895 132.660 1.00 35.06 ?  196 ARG D NE    1 
ATOM   14959 C  CZ    . ARG D 2 217 ? 136.925 109.542 131.567 1.00 37.65 ?  196 ARG D CZ    1 
ATOM   14960 N  NH1   . ARG D 2 217 ? 136.867 110.870 131.556 1.00 40.20 1  196 ARG D NH1   1 
ATOM   14961 N  NH2   . ARG D 2 217 ? 136.577 108.860 130.479 1.00 38.20 ?  196 ARG D NH2   1 
ATOM   14962 N  N     . ASP D 2 218 ? 137.246 104.566 135.051 1.00 21.34 ?  197 ASP D N     1 
ATOM   14963 C  CA    . ASP D 2 218 ? 136.042 103.727 135.152 1.00 21.09 ?  197 ASP D CA    1 
ATOM   14964 C  C     . ASP D 2 218 ? 135.999 102.940 136.478 1.00 20.65 ?  197 ASP D C     1 
ATOM   14965 O  O     . ASP D 2 218 ? 134.964 102.920 137.149 1.00 20.16 ?  197 ASP D O     1 
ATOM   14966 C  CB    . ASP D 2 218 ? 135.934 102.751 133.971 1.00 21.58 ?  197 ASP D CB    1 
ATOM   14967 C  CG    . ASP D 2 218 ? 135.693 103.451 132.634 1.00 22.60 ?  197 ASP D CG    1 
ATOM   14968 O  OD1   . ASP D 2 218 ? 135.176 104.592 132.612 1.00 24.72 ?  197 ASP D OD1   1 
ATOM   14969 O  OD2   . ASP D 2 218 ? 136.037 102.846 131.592 1.00 22.64 -1 197 ASP D OD2   1 
ATOM   14970 N  N     . GLU D 2 219 ? 137.101 102.293 136.860 1.00 20.59 ?  198 GLU D N     1 
ATOM   14971 C  CA    . GLU D 2 219 ? 137.097 101.489 138.103 1.00 20.66 ?  198 GLU D CA    1 
ATOM   14972 C  C     . GLU D 2 219 ? 136.830 102.355 139.338 1.00 20.45 ?  198 GLU D C     1 
ATOM   14973 O  O     . GLU D 2 219 ? 136.153 101.915 140.273 1.00 20.59 ?  198 GLU D O     1 
ATOM   14974 C  CB    . GLU D 2 219 ? 138.392 100.682 138.288 1.00 20.55 ?  198 GLU D CB    1 
ATOM   14975 C  CG    . GLU D 2 219 ? 138.960 99.985  137.013 1.00 21.99 ?  198 GLU D CG    1 
ATOM   14976 C  CD    . GLU D 2 219 ? 138.034 98.952  136.359 1.00 24.00 ?  198 GLU D CD    1 
ATOM   14977 O  OE1   . GLU D 2 219 ? 136.795 99.004  136.516 1.00 25.06 ?  198 GLU D OE1   1 
ATOM   14978 O  OE2   . GLU D 2 219 ? 138.552 98.080  135.641 1.00 24.49 -1 198 GLU D OE2   1 
ATOM   14979 N  N     . ALA D 2 220 ? 137.344 103.582 139.328 1.00 20.47 ?  199 ALA D N     1 
ATOM   14980 C  CA    . ALA D 2 220 ? 137.089 104.542 140.422 1.00 21.10 ?  199 ALA D CA    1 
ATOM   14981 C  C     . ALA D 2 220 ? 135.597 104.789 140.631 1.00 21.34 ?  199 ALA D C     1 
ATOM   14982 O  O     . ALA D 2 220 ? 135.096 104.616 141.741 1.00 21.19 ?  199 ALA D O     1 
ATOM   14983 C  CB    . ALA D 2 220 ? 137.836 105.858 140.194 1.00 21.09 ?  199 ALA D CB    1 
ATOM   14984 N  N     . ILE D 2 221 ? 134.888 105.163 139.564 1.00 21.31 ?  200 ILE D N     1 
ATOM   14985 C  CA    . ILE D 2 221 ? 133.440 105.338 139.655 1.00 21.80 ?  200 ILE D CA    1 
ATOM   14986 C  C     . ILE D 2 221 ? 132.680 104.031 139.968 1.00 20.90 ?  200 ILE D C     1 
ATOM   14987 O  O     . ILE D 2 221 ? 131.698 104.057 140.709 1.00 20.54 ?  200 ILE D O     1 
ATOM   14988 C  CB    . ILE D 2 221 ? 132.840 106.107 138.444 1.00 22.75 ?  200 ILE D CB    1 
ATOM   14989 C  CG1   . ILE D 2 221 ? 131.445 106.611 138.796 1.00 24.63 ?  200 ILE D CG1   1 
ATOM   14990 C  CG2   . ILE D 2 221 ? 132.768 105.232 137.195 1.00 23.38 ?  200 ILE D CG2   1 
ATOM   14991 C  CD1   . ILE D 2 221 ? 130.982 107.765 137.955 1.00 26.91 ?  200 ILE D CD1   1 
ATOM   14992 N  N     . HIS D 2 222 ? 133.149 102.892 139.446 1.00 20.31 ?  201 HIS D N     1 
ATOM   14993 C  CA    . HIS D 2 222 ? 132.543 101.605 139.799 1.00 20.25 ?  201 HIS D CA    1 
ATOM   14994 C  C     . HIS D 2 222 ? 132.622 101.379 141.307 1.00 20.51 ?  201 HIS D C     1 
ATOM   14995 O  O     . HIS D 2 222 ? 131.617 101.056 141.951 1.00 20.99 ?  201 HIS D O     1 
ATOM   14996 C  CB    . HIS D 2 222 ? 133.201 100.431 139.064 1.00 19.79 ?  201 HIS D CB    1 
ATOM   14997 C  CG    . HIS D 2 222 ? 133.081 100.482 137.572 1.00 19.25 ?  201 HIS D CG    1 
ATOM   14998 N  ND1   . HIS D 2 222 ? 133.747 99.595  136.753 1.00 18.35 ?  201 HIS D ND1   1 
ATOM   14999 C  CD2   . HIS D 2 222 ? 132.390 101.310 136.749 1.00 17.64 ?  201 HIS D CD2   1 
ATOM   15000 C  CE1   . HIS D 2 222 ? 133.463 99.862  135.490 1.00 18.28 ?  201 HIS D CE1   1 
ATOM   15001 N  NE2   . HIS D 2 222 ? 132.648 100.904 135.460 1.00 20.01 ?  201 HIS D NE2   1 
ATOM   15002 N  N     . GLY D 2 223 ? 133.817 101.573 141.869 1.00 20.33 ?  202 GLY D N     1 
ATOM   15003 C  CA    . GLY D 2 223 ? 134.039 101.439 143.315 1.00 19.94 ?  202 GLY D CA    1 
ATOM   15004 C  C     . GLY D 2 223 ? 133.165 102.362 144.156 1.00 19.80 ?  202 GLY D C     1 
ATOM   15005 O  O     . GLY D 2 223 ? 132.581 101.926 145.147 1.00 19.96 ?  202 GLY D O     1 
ATOM   15006 N  N     . VAL D 2 224 ? 133.046 103.628 143.751 1.00 19.49 ?  203 VAL D N     1 
ATOM   15007 C  CA    . VAL D 2 224 ? 132.194 104.588 144.472 1.00 18.88 ?  203 VAL D CA    1 
ATOM   15008 C  C     . VAL D 2 224 ? 130.716 104.173 144.444 1.00 18.55 ?  203 VAL D C     1 
ATOM   15009 O  O     . VAL D 2 224 ? 130.023 104.212 145.474 1.00 17.65 ?  203 VAL D O     1 
ATOM   15010 C  CB    . VAL D 2 224 ? 132.365 106.057 143.936 1.00 19.22 ?  203 VAL D CB    1 
ATOM   15011 C  CG1   . VAL D 2 224 ? 131.438 107.031 144.692 1.00 18.51 ?  203 VAL D CG1   1 
ATOM   15012 C  CG2   . VAL D 2 224 ? 133.832 106.518 144.062 1.00 19.69 ?  203 VAL D CG2   1 
ATOM   15013 N  N     . TYR D 2 225 ? 130.248 103.752 143.271 1.00 18.17 ?  204 TYR D N     1 
ATOM   15014 C  CA    . TYR D 2 225 ? 128.850 103.357 143.086 1.00 18.76 ?  204 TYR D CA    1 
ATOM   15015 C  C     . TYR D 2 225 ? 128.491 102.106 143.906 1.00 18.93 ?  204 TYR D C     1 
ATOM   15016 O  O     . TYR D 2 225 ? 127.521 102.107 144.676 1.00 18.77 ?  204 TYR D O     1 
ATOM   15017 C  CB    . TYR D 2 225 ? 128.524 103.139 141.595 1.00 18.96 ?  204 TYR D CB    1 
ATOM   15018 C  CG    . TYR D 2 225 ? 127.042 102.862 141.371 1.00 20.06 ?  204 TYR D CG    1 
ATOM   15019 C  CD1   . TYR D 2 225 ? 126.086 103.855 141.623 1.00 21.79 ?  204 TYR D CD1   1 
ATOM   15020 C  CD2   . TYR D 2 225 ? 126.596 101.607 140.946 1.00 19.51 ?  204 TYR D CD2   1 
ATOM   15021 C  CE1   . TYR D 2 225 ? 124.723 103.606 141.450 1.00 20.38 ?  204 TYR D CE1   1 
ATOM   15022 C  CE2   . TYR D 2 225 ? 125.219 101.349 140.763 1.00 19.38 ?  204 TYR D CE2   1 
ATOM   15023 C  CZ    . TYR D 2 225 ? 124.298 102.360 141.024 1.00 20.84 ?  204 TYR D CZ    1 
ATOM   15024 O  OH    . TYR D 2 225 ? 122.947 102.140 140.872 1.00 20.77 ?  204 TYR D OH    1 
ATOM   15025 N  N     . VAL D 2 226 ? 129.278 101.043 143.750 1.00 18.76 ?  205 VAL D N     1 
ATOM   15026 C  CA    . VAL D 2 226 ? 129.040 99.822  144.515 1.00 18.85 ?  205 VAL D CA    1 
ATOM   15027 C  C     . VAL D 2 226 ? 129.144 100.116 146.011 1.00 19.19 ?  205 VAL D C     1 
ATOM   15028 O  O     . VAL D 2 226 ? 128.381 99.559  146.803 1.00 19.87 ?  205 VAL D O     1 
ATOM   15029 C  CB    . VAL D 2 226 ? 129.979 98.686  144.092 1.00 19.28 ?  205 VAL D CB    1 
ATOM   15030 C  CG1   . VAL D 2 226 ? 129.750 97.422  144.964 1.00 18.22 ?  205 VAL D CG1   1 
ATOM   15031 C  CG2   . VAL D 2 226 ? 129.752 98.378  142.603 1.00 18.40 ?  205 VAL D CG2   1 
ATOM   15032 N  N     . GLY D 2 227 ? 130.063 101.010 146.381 1.00 18.53 ?  206 GLY D N     1 
ATOM   15033 C  CA    . GLY D 2 227 ? 130.185 101.478 147.775 1.00 18.74 ?  206 GLY D CA    1 
ATOM   15034 C  C     . GLY D 2 227 ? 128.911 102.080 148.342 1.00 19.17 ?  206 GLY D C     1 
ATOM   15035 O  O     . GLY D 2 227 ? 128.558 101.838 149.505 1.00 18.66 ?  206 GLY D O     1 
ATOM   15036 N  N     . LEU D 2 228 ? 128.226 102.884 147.531 1.00 19.00 ?  207 LEU D N     1 
ATOM   15037 C  CA    . LEU D 2 228 ? 126.961 103.487 147.958 1.00 19.73 ?  207 LEU D CA    1 
ATOM   15038 C  C     . LEU D 2 228 ? 125.872 102.421 148.132 1.00 19.76 ?  207 LEU D C     1 
ATOM   15039 O  O     . LEU D 2 228 ? 125.098 102.477 149.087 1.00 20.07 ?  207 LEU D O     1 
ATOM   15040 C  CB    . LEU D 2 228 ? 126.528 104.590 146.989 1.00 19.36 ?  207 LEU D CB    1 
ATOM   15041 C  CG    . LEU D 2 228 ? 127.398 105.857 147.002 1.00 20.50 ?  207 LEU D CG    1 
ATOM   15042 C  CD1   . LEU D 2 228 ? 127.047 106.758 145.832 1.00 19.87 ?  207 LEU D CD1   1 
ATOM   15043 C  CD2   . LEU D 2 228 ? 127.262 106.630 148.345 1.00 22.38 ?  207 LEU D CD2   1 
ATOM   15044 N  N     . LEU D 2 229 ? 125.841 101.432 147.238 1.00 19.27 ?  208 LEU D N     1 
ATOM   15045 C  CA    . LEU D 2 229 ? 124.910 100.297 147.380 1.00 19.47 ?  208 LEU D CA    1 
ATOM   15046 C  C     . LEU D 2 229 ? 125.173 99.466  148.642 1.00 19.67 ?  208 LEU D C     1 
ATOM   15047 O  O     . LEU D 2 229 ? 124.231 98.977  149.278 1.00 19.82 ?  208 LEU D O     1 
ATOM   15048 C  CB    . LEU D 2 229 ? 124.944 99.388  146.134 1.00 19.51 ?  208 LEU D CB    1 
ATOM   15049 C  CG    . LEU D 2 229 ? 124.558 99.967  144.763 1.00 19.48 ?  208 LEU D CG    1 
ATOM   15050 C  CD1   . LEU D 2 229 ? 124.817 98.930  143.655 1.00 20.14 ?  208 LEU D CD1   1 
ATOM   15051 C  CD2   . LEU D 2 229 ? 123.102 100.481 144.710 1.00 19.95 ?  208 LEU D CD2   1 
ATOM   15052 N  N     . ALA D 2 230 ? 126.446 99.298  149.000 1.00 19.43 ?  209 ALA D N     1 
ATOM   15053 C  CA    . ALA D 2 230 ? 126.819 98.608  150.243 1.00 20.29 ?  209 ALA D CA    1 
ATOM   15054 C  C     . ALA D 2 230 ? 126.404 99.396  151.487 1.00 21.17 ?  209 ALA D C     1 
ATOM   15055 O  O     . ALA D 2 230 ? 125.883 98.821  152.437 1.00 21.73 ?  209 ALA D O     1 
ATOM   15056 C  CB    . ALA D 2 230 ? 128.317 98.315  150.267 1.00 19.99 ?  209 ALA D CB    1 
ATOM   15057 N  N     . GLN D 2 231 ? 126.630 100.709 151.477 1.00 22.26 ?  210 GLN D N     1 
ATOM   15058 C  CA    . GLN D 2 231 ? 126.218 101.578 152.596 1.00 23.33 ?  210 GLN D CA    1 
ATOM   15059 C  C     . GLN D 2 231 ? 124.702 101.549 152.818 1.00 23.85 ?  210 GLN D C     1 
ATOM   15060 O  O     . GLN D 2 231 ? 124.241 101.587 153.955 1.00 24.91 ?  210 GLN D O     1 
ATOM   15061 C  CB    . GLN D 2 231 ? 126.669 103.025 152.371 1.00 23.49 ?  210 GLN D CB    1 
ATOM   15062 C  CG    . GLN D 2 231 ? 128.185 103.249 152.381 1.00 23.05 ?  210 GLN D CG    1 
ATOM   15063 C  CD    . GLN D 2 231 ? 128.546 104.711 152.124 1.00 24.65 ?  210 GLN D CD    1 
ATOM   15064 O  OE1   . GLN D 2 231 ? 128.020 105.606 152.784 1.00 25.85 ?  210 GLN D OE1   1 
ATOM   15065 N  NE2   . GLN D 2 231 ? 129.429 104.957 151.155 1.00 22.30 ?  210 GLN D NE2   1 
ATOM   15066 N  N     . GLU D 2 232 ? 123.936 101.501 151.732 1.00 24.36 ?  211 GLU D N     1 
ATOM   15067 C  CA    . GLU D 2 232 ? 122.486 101.341 151.818 1.00 24.83 ?  211 GLU D CA    1 
ATOM   15068 C  C     . GLU D 2 232 ? 122.093 100.094 152.617 1.00 24.34 ?  211 GLU D C     1 
ATOM   15069 O  O     . GLU D 2 232 ? 121.216 100.164 153.480 1.00 24.20 ?  211 GLU D O     1 
ATOM   15070 C  CB    . GLU D 2 232 ? 121.868 101.283 150.426 1.00 25.15 ?  211 GLU D CB    1 
ATOM   15071 C  CG    . GLU D 2 232 ? 120.365 101.383 150.419 1.00 28.55 ?  211 GLU D CG    1 
ATOM   15072 C  CD    . GLU D 2 232 ? 119.820 101.344 149.017 1.00 33.83 ?  211 GLU D CD    1 
ATOM   15073 O  OE1   . GLU D 2 232 ? 119.646 102.432 148.430 1.00 35.09 ?  211 GLU D OE1   1 
ATOM   15074 O  OE2   . GLU D 2 232 ? 119.609 100.230 148.489 1.00 35.51 -1 211 GLU D OE2   1 
ATOM   15075 N  N     . ILE D 2 233 ? 122.742 98.964  152.340 1.00 23.39 ?  212 ILE D N     1 
ATOM   15076 C  CA    . ILE D 2 233 ? 122.495 97.730  153.105 1.00 23.42 ?  212 ILE D CA    1 
ATOM   15077 C  C     . ILE D 2 233 ? 122.958 97.883  154.554 1.00 23.74 ?  212 ILE D C     1 
ATOM   15078 O  O     . ILE D 2 233 ? 122.215 97.579  155.487 1.00 24.61 ?  212 ILE D O     1 
ATOM   15079 C  CB    . ILE D 2 233 ? 123.142 96.483  152.444 1.00 22.81 ?  212 ILE D CB    1 
ATOM   15080 C  CG1   . ILE D 2 233 ? 122.476 96.185  151.093 1.00 22.94 ?  212 ILE D CG1   1 
ATOM   15081 C  CG2   . ILE D 2 233 ? 123.029 95.255  153.358 1.00 22.45 ?  212 ILE D CG2   1 
ATOM   15082 C  CD1   . ILE D 2 233 ? 123.266 95.199  150.205 1.00 22.21 ?  212 ILE D CD1   1 
ATOM   15083 N  N     . TYR D 2 234 ? 124.180 98.374  154.737 1.00 24.19 ?  213 TYR D N     1 
ATOM   15084 C  CA    . TYR D 2 234 ? 124.762 98.589  156.054 1.00 24.59 ?  213 TYR D CA    1 
ATOM   15085 C  C     . TYR D 2 234 ? 123.841 99.422  156.952 1.00 25.15 ?  213 TYR D C     1 
ATOM   15086 O  O     . TYR D 2 234 ? 123.668 99.099  158.130 1.00 24.94 ?  213 TYR D O     1 
ATOM   15087 C  CB    . TYR D 2 234 ? 126.121 99.280  155.911 1.00 24.41 ?  213 TYR D CB    1 
ATOM   15088 C  CG    . TYR D 2 234 ? 126.832 99.580  157.214 1.00 25.93 ?  213 TYR D CG    1 
ATOM   15089 C  CD1   . TYR D 2 234 ? 127.632 98.620  157.825 1.00 24.70 ?  213 TYR D CD1   1 
ATOM   15090 C  CD2   . TYR D 2 234 ? 126.711 100.833 157.829 1.00 26.11 ?  213 TYR D CD2   1 
ATOM   15091 C  CE1   . TYR D 2 234 ? 128.294 98.892  159.019 1.00 27.90 ?  213 TYR D CE1   1 
ATOM   15092 C  CE2   . TYR D 2 234 ? 127.374 101.113 159.017 1.00 27.70 ?  213 TYR D CE2   1 
ATOM   15093 C  CZ    . TYR D 2 234 ? 128.163 100.141 159.604 1.00 27.89 ?  213 TYR D CZ    1 
ATOM   15094 O  OH    . TYR D 2 234 ? 128.819 100.411 160.783 1.00 32.34 ?  213 TYR D OH    1 
ATOM   15095 N  N     . ASN D 2 235 ? 123.267 100.485 156.387 1.00 25.43 ?  214 ASN D N     1 
ATOM   15096 C  CA    . ASN D 2 235 ? 122.408 101.413 157.142 1.00 26.77 ?  214 ASN D CA    1 
ATOM   15097 C  C     . ASN D 2 235 ? 121.048 100.833 157.528 1.00 27.06 ?  214 ASN D C     1 
ATOM   15098 O  O     . ASN D 2 235 ? 120.332 101.408 158.342 1.00 27.42 ?  214 ASN D O     1 
ATOM   15099 C  CB    . ASN D 2 235 ? 122.188 102.716 156.371 1.00 26.80 ?  214 ASN D CB    1 
ATOM   15100 C  CG    . ASN D 2 235 ? 123.461 103.491 156.157 1.00 28.19 ?  214 ASN D CG    1 
ATOM   15101 O  OD1   . ASN D 2 235 ? 124.358 103.491 156.998 1.00 29.35 ?  214 ASN D OD1   1 
ATOM   15102 N  ND2   . ASN D 2 235 ? 123.544 104.170 155.025 1.00 30.84 ?  214 ASN D ND2   1 
ATOM   15103 N  N     . LYS D 2 236 ? 120.696 99.700  156.937 1.00 26.87 ?  215 LYS D N     1 
ATOM   15104 C  CA    . LYS D 2 236 ? 119.449 99.026  157.272 1.00 27.86 ?  215 LYS D CA    1 
ATOM   15105 C  C     . LYS D 2 236 ? 119.629 98.057  158.449 1.00 28.07 ?  215 LYS D C     1 
ATOM   15106 O  O     . LYS D 2 236 ? 118.667 97.437  158.900 1.00 28.22 ?  215 LYS D O     1 
ATOM   15107 C  CB    . LYS D 2 236 ? 118.895 98.289  156.051 1.00 27.52 ?  215 LYS D CB    1 
ATOM   15108 C  CG    . LYS D 2 236 ? 118.491 99.194  154.912 1.00 29.60 ?  215 LYS D CG    1 
ATOM   15109 C  CD    . LYS D 2 236 ? 117.428 98.555  154.034 1.00 34.24 ?  215 LYS D CD    1 
ATOM   15110 C  CE    . LYS D 2 236 ? 117.986 97.934  152.768 1.00 36.75 ?  215 LYS D CE    1 
ATOM   15111 N  NZ    . LYS D 2 236 ? 118.865 96.782  153.063 1.00 40.41 1  215 LYS D NZ    1 
ATOM   15112 N  N     . GLN D 2 237 ? 120.858 97.940  158.945 1.00 28.33 ?  216 GLN D N     1 
ATOM   15113 C  CA    . GLN D 2 237 ? 121.181 96.947  159.973 1.00 29.60 ?  216 GLN D CA    1 
ATOM   15114 C  C     . GLN D 2 237 ? 121.129 97.522  161.384 1.00 30.69 ?  216 GLN D C     1 
ATOM   15115 O  O     . GLN D 2 237 ? 121.235 98.738  161.573 1.00 30.85 ?  216 GLN D O     1 
ATOM   15116 C  CB    . GLN D 2 237 ? 122.572 96.325  159.724 1.00 29.08 ?  216 GLN D CB    1 
ATOM   15117 C  CG    . GLN D 2 237 ? 122.801 95.750  158.323 1.00 27.78 ?  216 GLN D CG    1 
ATOM   15118 C  CD    . GLN D 2 237 ? 121.690 94.819  157.863 1.00 28.38 ?  216 GLN D CD    1 
ATOM   15119 O  OE1   . GLN D 2 237 ? 121.308 93.890  158.573 1.00 29.30 ?  216 GLN D OE1   1 
ATOM   15120 N  NE2   . GLN D 2 237 ? 121.176 95.059  156.661 1.00 26.88 ?  216 GLN D NE2   1 
ATOM   15121 N  N     . THR D 2 238 ? 120.980 96.634  162.366 1.00 32.02 ?  217 THR D N     1 
ATOM   15122 C  CA    . THR D 2 238 ? 121.080 97.006  163.781 1.00 33.47 ?  217 THR D CA    1 
ATOM   15123 C  C     . THR D 2 238 ? 122.502 97.455  164.134 1.00 34.29 ?  217 THR D C     1 
ATOM   15124 O  O     . THR D 2 238 ? 123.442 97.288  163.339 1.00 33.78 ?  217 THR D O     1 
ATOM   15125 C  CB    . THR D 2 238 ? 120.679 95.825  164.708 1.00 34.00 ?  217 THR D CB    1 
ATOM   15126 O  OG1   . THR D 2 238 ? 121.627 94.756  164.568 1.00 34.33 ?  217 THR D OG1   1 
ATOM   15127 C  CG2   . THR D 2 238 ? 119.271 95.309  164.366 1.00 33.53 ?  217 THR D CG2   1 
ATOM   15128 N  N     . GLU D 2 239 ? 122.669 98.010  165.330 1.00 35.45 ?  218 GLU D N     1 
ATOM   15129 C  CA    . GLU D 2 239 ? 123.987 98.454  165.773 1.00 36.37 ?  218 GLU D CA    1 
ATOM   15130 C  C     . GLU D 2 239 ? 124.962 97.295  165.966 1.00 36.29 ?  218 GLU D C     1 
ATOM   15131 O  O     . GLU D 2 239 ? 126.138 97.409  165.609 1.00 36.18 ?  218 GLU D O     1 
ATOM   15132 C  CB    . GLU D 2 239 ? 123.889 99.320  167.032 1.00 37.27 ?  218 GLU D CB    1 
ATOM   15133 C  CG    . GLU D 2 239 ? 123.247 100.697 166.781 1.00 39.45 ?  218 GLU D CG    1 
ATOM   15134 C  CD    . GLU D 2 239 ? 123.959 101.508 165.700 1.00 41.22 ?  218 GLU D CD    1 
ATOM   15135 O  OE1   . GLU D 2 239 ? 125.207 101.591 165.724 1.00 42.62 ?  218 GLU D OE1   1 
ATOM   15136 O  OE2   . GLU D 2 239 ? 123.268 102.066 164.821 1.00 41.24 -1 218 GLU D OE2   1 
ATOM   15137 N  N     . GLU D 2 240 ? 124.472 96.181  166.507 1.00 36.66 ?  219 GLU D N     1 
ATOM   15138 C  CA    . GLU D 2 240 ? 125.308 94.994  166.694 1.00 37.01 ?  219 GLU D CA    1 
ATOM   15139 C  C     . GLU D 2 240 ? 125.718 94.395  165.348 1.00 35.85 ?  219 GLU D C     1 
ATOM   15140 O  O     . GLU D 2 240 ? 126.872 93.995  165.173 1.00 35.62 ?  219 GLU D O     1 
ATOM   15141 C  CB    . GLU D 2 240 ? 124.608 93.935  167.559 1.00 37.98 ?  219 GLU D CB    1 
ATOM   15142 C  CG    . GLU D 2 240 ? 125.497 92.719  167.863 1.00 40.87 ?  219 GLU D CG    1 
ATOM   15143 C  CD    . GLU D 2 240 ? 124.825 91.642  168.711 1.00 44.58 ?  219 GLU D CD    1 
ATOM   15144 O  OE1   . GLU D 2 240 ? 125.564 90.901  169.405 1.00 45.86 ?  219 GLU D OE1   1 
ATOM   15145 O  OE2   . GLU D 2 240 ? 123.575 91.527  168.685 1.00 45.75 -1 219 GLU D OE2   1 
ATOM   15146 N  N     . LYS D 2 241 ? 124.767 94.336  164.416 1.00 34.54 ?  220 LYS D N     1 
ATOM   15147 C  CA    . LYS D 2 241 ? 125.024 93.817  163.070 1.00 33.65 ?  220 LYS D CA    1 
ATOM   15148 C  C     . LYS D 2 241 ? 125.999 94.724  162.308 1.00 32.67 ?  220 LYS D C     1 
ATOM   15149 O  O     . LYS D 2 241 ? 126.857 94.225  161.584 1.00 32.05 ?  220 LYS D O     1 
ATOM   15150 C  CB    . LYS D 2 241 ? 123.716 93.632  162.293 1.00 33.30 ?  220 LYS D CB    1 
ATOM   15151 C  CG    . LYS D 2 241 ? 123.851 92.944  160.921 1.00 34.50 ?  220 LYS D CG    1 
ATOM   15152 C  CD    . LYS D 2 241 ? 124.425 91.524  161.015 1.00 36.30 ?  220 LYS D CD    1 
ATOM   15153 C  CE    . LYS D 2 241 ? 123.433 90.551  161.641 1.00 38.44 ?  220 LYS D CE    1 
ATOM   15154 N  NZ    . LYS D 2 241 ? 124.130 89.374  162.227 1.00 39.28 1  220 LYS D NZ    1 
ATOM   15155 N  N     . LYS D 2 242 ? 125.861 96.041  162.481 1.00 31.90 ?  221 LYS D N     1 
ATOM   15156 C  CA    . LYS D 2 242 ? 126.793 97.007  161.897 1.00 31.28 ?  221 LYS D CA    1 
ATOM   15157 C  C     . LYS D 2 242 ? 128.223 96.767  162.379 1.00 31.32 ?  221 LYS D C     1 
ATOM   15158 O  O     . LYS D 2 242 ? 129.136 96.686  161.568 1.00 30.72 ?  221 LYS D O     1 
ATOM   15159 C  CB    . LYS D 2 242 ? 126.376 98.452  162.208 1.00 31.38 ?  221 LYS D CB    1 
ATOM   15160 C  CG    . LYS D 2 242 ? 125.298 99.016  161.289 1.00 30.64 ?  221 LYS D CG    1 
ATOM   15161 C  CD    . LYS D 2 242 ? 124.969 100.456 161.680 1.00 32.51 ?  221 LYS D CD    1 
ATOM   15162 C  CE    . LYS D 2 242 ? 123.922 101.046 160.761 1.00 32.66 ?  221 LYS D CE    1 
ATOM   15163 N  NZ    . LYS D 2 242 ? 123.432 102.342 161.281 1.00 35.31 1  221 LYS D NZ    1 
ATOM   15164 N  N     . ALA D 2 243 ? 128.406 96.661  163.699 1.00 31.62 ?  222 ALA D N     1 
ATOM   15165 C  CA    . ALA D 2 243 ? 129.721 96.388  164.289 1.00 31.66 ?  222 ALA D CA    1 
ATOM   15166 C  C     . ALA D 2 243 ? 130.340 95.097  163.738 1.00 31.52 ?  222 ALA D C     1 
ATOM   15167 O  O     . ALA D 2 243 ? 131.554 95.012  163.537 1.00 31.41 ?  222 ALA D O     1 
ATOM   15168 C  CB    . ALA D 2 243 ? 129.621 96.337  165.818 1.00 31.89 ?  222 ALA D CB    1 
ATOM   15169 N  N     . GLU D 2 244 ? 129.482 94.114  163.480 1.00 31.35 ?  223 GLU D N     1 
ATOM   15170 C  CA    . GLU D 2 244 ? 129.870 92.823  162.934 1.00 31.54 ?  223 GLU D CA    1 
ATOM   15171 C  C     . GLU D 2 244 ? 130.299 92.935  161.453 1.00 30.63 ?  223 GLU D C     1 
ATOM   15172 O  O     . GLU D 2 244 ? 131.270 92.299  161.019 1.00 29.47 ?  223 GLU D O     1 
ATOM   15173 C  CB    . GLU D 2 244 ? 128.685 91.884  163.091 1.00 32.45 ?  223 GLU D CB    1 
ATOM   15174 C  CG    . GLU D 2 244 ? 128.944 90.425  162.882 1.00 35.31 ?  223 GLU D CG    1 
ATOM   15175 C  CD    . GLU D 2 244 ? 127.780 89.590  163.379 1.00 38.36 ?  223 GLU D CD    1 
ATOM   15176 O  OE1   . GLU D 2 244 ? 127.562 89.542  164.607 1.00 41.93 ?  223 GLU D OE1   1 
ATOM   15177 O  OE2   . GLU D 2 244 ? 127.073 88.989  162.546 1.00 39.37 -1 223 GLU D OE2   1 
ATOM   15178 N  N     . LEU D 2 245 ? 129.571 93.749  160.696 1.00 29.62 ?  224 LEU D N     1 
ATOM   15179 C  CA    . LEU D 2 245 ? 129.921 94.038  159.307 1.00 29.44 ?  224 LEU D CA    1 
ATOM   15180 C  C     . LEU D 2 245 ? 131.199 94.871  159.188 1.00 28.99 ?  224 LEU D C     1 
ATOM   15181 O  O     . LEU D 2 245 ? 131.970 94.676  158.253 1.00 28.63 ?  224 LEU D O     1 
ATOM   15182 C  CB    . LEU D 2 245 ? 128.755 94.724  158.588 1.00 29.06 ?  224 LEU D CB    1 
ATOM   15183 C  CG    . LEU D 2 245 ? 127.501 93.874  158.353 1.00 29.27 ?  224 LEU D CG    1 
ATOM   15184 C  CD1   . LEU D 2 245 ? 126.470 94.694  157.583 1.00 30.76 ?  224 LEU D CD1   1 
ATOM   15185 C  CD2   . LEU D 2 245 ? 127.816 92.587  157.598 1.00 28.11 ?  224 LEU D CD2   1 
ATOM   15186 N  N     . ARG D 2 246 ? 131.416 95.791  160.130 1.00 29.31 ?  225 ARG D N     1 
ATOM   15187 C  CA    . ARG D 2 246 ? 132.665 96.556  160.188 1.00 29.86 ?  225 ARG D CA    1 
ATOM   15188 C  C     . ARG D 2 246 ? 133.855 95.642  160.447 1.00 29.23 ?  225 ARG D C     1 
ATOM   15189 O  O     . ARG D 2 246 ? 134.890 95.776  159.809 1.00 28.95 ?  225 ARG D O     1 
ATOM   15190 C  CB    . ARG D 2 246 ? 132.633 97.635  161.276 1.00 30.56 ?  225 ARG D CB    1 
ATOM   15191 C  CG    . ARG D 2 246 ? 131.828 98.865  160.924 1.00 33.71 ?  225 ARG D CG    1 
ATOM   15192 C  CD    . ARG D 2 246 ? 132.247 100.096 161.750 1.00 37.42 ?  225 ARG D CD    1 
ATOM   15193 N  NE    . ARG D 2 246 ? 132.184 99.879  163.200 1.00 39.17 ?  225 ARG D NE    1 
ATOM   15194 C  CZ    . ARG D 2 246 ? 131.072 99.901  163.936 1.00 40.68 ?  225 ARG D CZ    1 
ATOM   15195 N  NH1   . ARG D 2 246 ? 129.883 100.117 163.378 1.00 40.28 1  225 ARG D NH1   1 
ATOM   15196 N  NH2   . ARG D 2 246 ? 131.149 99.691  165.246 1.00 41.65 ?  225 ARG D NH2   1 
ATOM   15197 N  N     . GLU D 2 247 ? 133.702 94.730  161.399 1.00 28.89 ?  226 GLU D N     1 
ATOM   15198 C  CA    . GLU D 2 247 ? 134.747 93.758  161.700 1.00 29.27 ?  226 GLU D CA    1 
ATOM   15199 C  C     . GLU D 2 247 ? 135.052 92.894  160.477 1.00 27.84 ?  226 GLU D C     1 
ATOM   15200 O  O     . GLU D 2 247 ? 136.223 92.651  160.178 1.00 27.37 ?  226 GLU D O     1 
ATOM   15201 C  CB    . GLU D 2 247 ? 134.375 92.891  162.916 1.00 30.21 ?  226 GLU D CB    1 
ATOM   15202 C  CG    . GLU D 2 247 ? 135.370 91.757  163.233 1.00 34.46 ?  226 GLU D CG    1 
ATOM   15203 C  CD    . GLU D 2 247 ? 136.782 92.261  163.518 1.00 40.77 ?  226 GLU D CD    1 
ATOM   15204 O  OE1   . GLU D 2 247 ? 136.960 93.002  164.514 1.00 44.03 ?  226 GLU D OE1   1 
ATOM   15205 O  OE2   . GLU D 2 247 ? 137.718 91.921  162.750 1.00 42.98 -1 226 GLU D OE2   1 
ATOM   15206 N  N     . PHE D 2 248 ? 134.007 92.450  159.773 1.00 26.73 ?  227 PHE D N     1 
ATOM   15207 C  CA    . PHE D 2 248 ? 134.175 91.708  158.517 1.00 26.15 ?  227 PHE D CA    1 
ATOM   15208 C  C     . PHE D 2 248 ? 135.022 92.489  157.509 1.00 25.33 ?  227 PHE D C     1 
ATOM   15209 O  O     . PHE D 2 248 ? 135.964 91.943  156.941 1.00 24.70 ?  227 PHE D O     1 
ATOM   15210 C  CB    . PHE D 2 248 ? 132.836 91.327  157.855 1.00 26.02 ?  227 PHE D CB    1 
ATOM   15211 C  CG    . PHE D 2 248 ? 132.982 90.905  156.393 1.00 25.61 ?  227 PHE D CG    1 
ATOM   15212 C  CD1   . PHE D 2 248 ? 133.290 89.590  156.060 1.00 26.51 ?  227 PHE D CD1   1 
ATOM   15213 C  CD2   . PHE D 2 248 ? 132.849 91.840  155.362 1.00 26.21 ?  227 PHE D CD2   1 
ATOM   15214 C  CE1   . PHE D 2 248 ? 133.451 89.199  154.731 1.00 26.16 ?  227 PHE D CE1   1 
ATOM   15215 C  CE2   . PHE D 2 248 ? 133.011 91.463  154.021 1.00 26.07 ?  227 PHE D CE2   1 
ATOM   15216 C  CZ    . PHE D 2 248 ? 133.316 90.134  153.710 1.00 25.82 ?  227 PHE D CZ    1 
ATOM   15217 N  N     . ALA D 2 249 ? 134.662 93.755  157.287 1.00 24.83 ?  228 ALA D N     1 
ATOM   15218 C  CA    . ALA D 2 249 ? 135.326 94.608  156.292 1.00 24.08 ?  228 ALA D CA    1 
ATOM   15219 C  C     . ALA D 2 249 ? 136.805 94.844  156.633 1.00 23.93 ?  228 ALA D C     1 
ATOM   15220 O  O     . ALA D 2 249 ? 137.669 94.776  155.757 1.00 22.51 ?  228 ALA D O     1 
ATOM   15221 C  CB    . ALA D 2 249 ? 134.589 95.947  156.174 1.00 24.18 ?  228 ALA D CB    1 
ATOM   15222 N  N     . ILE D 2 250 ? 137.082 95.127  157.906 1.00 24.20 ?  229 ILE D N     1 
ATOM   15223 C  CA    . ILE D 2 250 ? 138.451 95.376  158.359 1.00 24.86 ?  229 ILE D CA    1 
ATOM   15224 C  C     . ILE D 2 250 ? 139.289 94.094  158.301 1.00 24.68 ?  229 ILE D C     1 
ATOM   15225 O  O     . ILE D 2 250 ? 140.438 94.124  157.874 1.00 24.30 ?  229 ILE D O     1 
ATOM   15226 C  CB    . ILE D 2 250 ? 138.493 96.028  159.786 1.00 25.44 ?  229 ILE D CB    1 
ATOM   15227 C  CG1   . ILE D 2 250 ? 137.730 97.367  159.825 1.00 26.49 ?  229 ILE D CG1   1 
ATOM   15228 C  CG2   . ILE D 2 250 ? 139.933 96.214  160.283 1.00 27.13 ?  229 ILE D CG2   1 
ATOM   15229 C  CD1   . ILE D 2 250 ? 138.146 98.399  158.774 1.00 28.58 ?  229 ILE D CD1   1 
ATOM   15230 N  N     . ASP D 2 251 ? 138.707 92.972  158.727 1.00 24.90 ?  230 ASP D N     1 
ATOM   15231 C  CA    . ASP D 2 251 ? 139.376 91.677  158.671 1.00 25.04 ?  230 ASP D CA    1 
ATOM   15232 C  C     . ASP D 2 251 ? 139.729 91.304  157.219 1.00 24.25 ?  230 ASP D C     1 
ATOM   15233 O  O     . ASP D 2 251 ? 140.855 90.889  156.935 1.00 23.60 ?  230 ASP D O     1 
ATOM   15234 C  CB    . ASP D 2 251 ? 138.489 90.605  159.312 1.00 26.23 ?  230 ASP D CB    1 
ATOM   15235 C  CG    . ASP D 2 251 ? 139.056 89.209  159.177 1.00 28.91 ?  230 ASP D CG    1 
ATOM   15236 O  OD1   . ASP D 2 251 ? 140.098 88.910  159.799 1.00 32.03 ?  230 ASP D OD1   1 
ATOM   15237 O  OD2   . ASP D 2 251 ? 138.438 88.396  158.462 1.00 33.16 -1 230 ASP D OD2   1 
ATOM   15238 N  N     . LEU D 2 252 ? 138.761 91.448  156.317 1.00 23.43 ?  231 LEU D N     1 
ATOM   15239 C  CA    . LEU D 2 252 ? 138.998 91.209  154.896 1.00 22.79 ?  231 LEU D CA    1 
ATOM   15240 C  C     . LEU D 2 252 ? 140.096 92.130  154.355 1.00 22.71 ?  231 LEU D C     1 
ATOM   15241 O  O     . LEU D 2 252 ? 140.996 91.678  153.637 1.00 21.58 ?  231 LEU D O     1 
ATOM   15242 C  CB    . LEU D 2 252 ? 137.712 91.393  154.083 1.00 22.48 ?  231 LEU D CB    1 
ATOM   15243 C  CG    . LEU D 2 252 ? 137.844 91.160  152.566 1.00 21.05 ?  231 LEU D CG    1 
ATOM   15244 C  CD1   . LEU D 2 252 ? 138.368 89.743  152.244 1.00 22.94 ?  231 LEU D CD1   1 
ATOM   15245 C  CD2   . LEU D 2 252 ? 136.517 91.395  151.860 1.00 19.31 ?  231 LEU D CD2   1 
ATOM   15246 N  N     . LEU D 2 253 ? 140.013 93.416  154.699 1.00 22.90 ?  232 LEU D N     1 
ATOM   15247 C  CA    . LEU D 2 253 ? 141.026 94.382  154.249 1.00 23.78 ?  232 LEU D CA    1 
ATOM   15248 C  C     . LEU D 2 253 ? 142.429 93.957  154.699 1.00 23.75 ?  232 LEU D C     1 
ATOM   15249 O  O     . LEU D 2 253 ? 143.373 93.989  153.909 1.00 23.26 ?  232 LEU D O     1 
ATOM   15250 C  CB    . LEU D 2 253 ? 140.727 95.789  154.769 1.00 24.03 ?  232 LEU D CB    1 
ATOM   15251 C  CG    . LEU D 2 253 ? 141.857 96.809  154.541 1.00 26.46 ?  232 LEU D CG    1 
ATOM   15252 C  CD1   . LEU D 2 253 ? 141.941 97.175  153.078 1.00 26.52 ?  232 LEU D CD1   1 
ATOM   15253 C  CD2   . LEU D 2 253 ? 141.668 98.069  155.390 1.00 27.50 ?  232 LEU D CD2   1 
ATOM   15254 N  N     . ASN D 2 254 ? 142.550 93.588  155.975 1.00 24.63 ?  233 ASN D N     1 
ATOM   15255 C  CA    . ASN D 2 254 ? 143.813 93.095  156.530 1.00 25.49 ?  233 ASN D CA    1 
ATOM   15256 C  C     . ASN D 2 254 ? 144.394 91.891  155.774 1.00 24.94 ?  233 ASN D C     1 
ATOM   15257 O  O     . ASN D 2 254 ? 145.595 91.863  155.496 1.00 24.64 ?  233 ASN D O     1 
ATOM   15258 C  CB    . ASN D 2 254 ? 143.658 92.742  158.007 1.00 26.98 ?  233 ASN D CB    1 
ATOM   15259 C  CG    . ASN D 2 254 ? 143.854 93.936  158.914 1.00 29.94 ?  233 ASN D CG    1 
ATOM   15260 O  OD1   . ASN D 2 254 ? 144.739 94.772  158.689 1.00 34.55 ?  233 ASN D OD1   1 
ATOM   15261 N  ND2   . ASN D 2 254 ? 143.039 94.020  159.957 1.00 33.81 ?  233 ASN D ND2   1 
ATOM   15262 N  N     . GLN D 2 255 ? 143.549 90.907  155.462 1.00 24.08 ?  234 GLN D N     1 
ATOM   15263 C  CA    . GLN D 2 255 ? 144.003 89.719  154.734 1.00 24.35 ?  234 GLN D CA    1 
ATOM   15264 C  C     . GLN D 2 255 ? 144.522 90.114  153.364 1.00 23.26 ?  234 GLN D C     1 
ATOM   15265 O  O     . GLN D 2 255 ? 145.611 89.685  152.969 1.00 23.12 ?  234 GLN D O     1 
ATOM   15266 C  CB    . GLN D 2 255 ? 142.885 88.685  154.553 1.00 24.84 ?  234 GLN D CB    1 
ATOM   15267 C  CG    . GLN D 2 255 ? 142.475 87.928  155.796 1.00 27.45 ?  234 GLN D CG    1 
ATOM   15268 C  CD    . GLN D 2 255 ? 143.634 87.213  156.469 1.00 32.02 ?  234 GLN D CD    1 
ATOM   15269 O  OE1   . GLN D 2 255 ? 143.960 87.506  157.617 1.00 35.80 ?  234 GLN D OE1   1 
ATOM   15270 N  NE2   . GLN D 2 255 ? 144.260 86.270  155.761 1.00 32.12 ?  234 GLN D NE2   1 
ATOM   15271 N  N     . LEU D 2 256 ? 143.742 90.931  152.653 1.00 21.77 ?  235 LEU D N     1 
ATOM   15272 C  CA    . LEU D 2 256 ? 144.114 91.379  151.309 1.00 21.68 ?  235 LEU D CA    1 
ATOM   15273 C  C     . LEU D 2 256 ? 145.365 92.251  151.350 1.00 21.49 ?  235 LEU D C     1 
ATOM   15274 O  O     . LEU D 2 256 ? 146.240 92.119  150.501 1.00 20.89 ?  235 LEU D O     1 
ATOM   15275 C  CB    . LEU D 2 256 ? 142.965 92.146  150.625 1.00 20.49 ?  235 LEU D CB    1 
ATOM   15276 C  CG    . LEU D 2 256 ? 141.720 91.331  150.250 1.00 21.52 ?  235 LEU D CG    1 
ATOM   15277 C  CD1   . LEU D 2 256 ? 140.564 92.234  149.786 1.00 20.71 ?  235 LEU D CD1   1 
ATOM   15278 C  CD2   . LEU D 2 256 ? 142.027 90.292  149.180 1.00 20.74 ?  235 LEU D CD2   1 
ATOM   15279 N  N     . TYR D 2 257 ? 145.441 93.133  152.345 1.00 21.42 ?  236 TYR D N     1 
ATOM   15280 C  CA    . TYR D 2 257 ? 146.592 94.026  152.473 1.00 22.02 ?  236 TYR D CA    1 
ATOM   15281 C  C     . TYR D 2 257 ? 147.899 93.268  152.706 1.00 22.61 ?  236 TYR D C     1 
ATOM   15282 O  O     . TYR D 2 257 ? 148.920 93.584  152.094 1.00 22.19 ?  236 TYR D O     1 
ATOM   15283 C  CB    . TYR D 2 257 ? 146.364 95.065  153.565 1.00 22.06 ?  236 TYR D CB    1 
ATOM   15284 C  CG    . TYR D 2 257 ? 147.576 95.920  153.862 1.00 23.44 ?  236 TYR D CG    1 
ATOM   15285 C  CD1   . TYR D 2 257 ? 148.068 96.826  152.914 1.00 24.01 ?  236 TYR D CD1   1 
ATOM   15286 C  CD2   . TYR D 2 257 ? 148.224 95.829  155.091 1.00 25.22 ?  236 TYR D CD2   1 
ATOM   15287 C  CE1   . TYR D 2 257 ? 149.182 97.616  153.191 1.00 25.14 ?  236 TYR D CE1   1 
ATOM   15288 C  CE2   . TYR D 2 257 ? 149.343 96.606  155.374 1.00 26.71 ?  236 TYR D CE2   1 
ATOM   15289 C  CZ    . TYR D 2 257 ? 149.811 97.497  154.424 1.00 25.35 ?  236 TYR D CZ    1 
ATOM   15290 O  OH    . TYR D 2 257 ? 150.907 98.266  154.720 1.00 26.77 ?  236 TYR D OH    1 
ATOM   15291 N  N     . GLU D 2 258 ? 147.868 92.263  153.577 1.00 23.09 ?  237 GLU D N     1 
ATOM   15292 C  CA    . GLU D 2 258 ? 149.088 91.504  153.862 1.00 23.98 ?  237 GLU D CA    1 
ATOM   15293 C  C     . GLU D 2 258 ? 149.566 90.726  152.635 1.00 23.13 ?  237 GLU D C     1 
ATOM   15294 O  O     . GLU D 2 258 ? 150.764 90.652  152.377 1.00 23.02 ?  237 GLU D O     1 
ATOM   15295 C  CB    . GLU D 2 258 ? 148.917 90.597  155.089 1.00 25.20 ?  237 GLU D CB    1 
ATOM   15296 C  CG    . GLU D 2 258 ? 148.721 91.373  156.403 1.00 28.82 ?  237 GLU D CG    1 
ATOM   15297 C  CD    . GLU D 2 258 ? 149.975 92.108  156.896 1.00 34.48 ?  237 GLU D CD    1 
ATOM   15298 O  OE1   . GLU D 2 258 ? 151.116 91.656  156.614 1.00 37.75 ?  237 GLU D OE1   1 
ATOM   15299 O  OE2   . GLU D 2 258 ? 149.821 93.144  157.588 1.00 37.16 -1 237 GLU D OE2   1 
ATOM   15300 N  N     . ASN D 2 259 ? 148.628 90.184  151.870 1.00 22.12 ?  238 ASN D N     1 
ATOM   15301 C  CA    . ASN D 2 259 ? 148.948 89.557  150.587 1.00 22.35 ?  238 ASN D CA    1 
ATOM   15302 C  C     . ASN D 2 259 ? 149.449 90.562  149.515 1.00 22.11 ?  238 ASN D C     1 
ATOM   15303 O  O     . ASN D 2 259 ? 150.337 90.231  148.727 1.00 22.24 ?  238 ASN D O     1 
ATOM   15304 C  CB    . ASN D 2 259 ? 147.750 88.751  150.072 1.00 21.69 ?  238 ASN D CB    1 
ATOM   15305 C  CG    . ASN D 2 259 ? 148.046 88.037  148.765 1.00 23.38 ?  238 ASN D CG    1 
ATOM   15306 O  OD1   . ASN D 2 259 ? 148.789 87.045  148.732 1.00 23.95 ?  238 ASN D OD1   1 
ATOM   15307 N  ND2   . ASN D 2 259 ? 147.479 88.544  147.679 1.00 21.14 ?  238 ASN D ND2   1 
ATOM   15308 N  N     . GLU D 2 260 ? 148.884 91.775  149.498 1.00 21.95 ?  239 GLU D N     1 
ATOM   15309 C  CA    . GLU D 2 260 ? 149.351 92.851  148.599 1.00 22.50 ?  239 GLU D CA    1 
ATOM   15310 C  C     . GLU D 2 260 ? 150.810 93.226  148.853 1.00 22.03 ?  239 GLU D C     1 
ATOM   15311 O  O     . GLU D 2 260 ? 151.544 93.536  147.919 1.00 22.03 ?  239 GLU D O     1 
ATOM   15312 C  CB    . GLU D 2 260 ? 148.510 94.132  148.743 1.00 22.90 ?  239 GLU D CB    1 
ATOM   15313 C  CG    . GLU D 2 260 ? 147.200 94.181  147.940 1.00 25.84 ?  239 GLU D CG    1 
ATOM   15314 C  CD    . GLU D 2 260 ? 147.354 93.773  146.478 1.00 28.59 ?  239 GLU D CD    1 
ATOM   15315 O  OE1   . GLU D 2 260 ? 147.398 92.556  146.204 1.00 28.18 ?  239 GLU D OE1   1 
ATOM   15316 O  OE2   . GLU D 2 260 ? 147.390 94.667  145.600 1.00 30.32 -1 239 GLU D OE2   1 
ATOM   15317 N  N     . LEU D 2 261 ? 151.213 93.233  150.119 1.00 21.50 ?  240 LEU D N     1 
ATOM   15318 C  CA    . LEU D 2 261 ? 152.595 93.550  150.462 1.00 22.03 ?  240 LEU D CA    1 
ATOM   15319 C  C     . LEU D 2 261 ? 153.527 92.510  149.865 1.00 21.52 ?  240 LEU D C     1 
ATOM   15320 O  O     . LEU D 2 261 ? 154.559 92.862  149.292 1.00 21.44 ?  240 LEU D O     1 
ATOM   15321 C  CB    . LEU D 2 261 ? 152.798 93.640  151.972 1.00 21.57 ?  240 LEU D CB    1 
ATOM   15322 C  CG    . LEU D 2 261 ? 152.008 94.701  152.740 1.00 23.22 ?  240 LEU D CG    1 
ATOM   15323 C  CD1   . LEU D 2 261 ? 152.337 94.590  154.217 1.00 23.06 ?  240 LEU D CD1   1 
ATOM   15324 C  CD2   . LEU D 2 261 ? 152.314 96.106  152.220 1.00 23.52 ?  240 LEU D CD2   1 
ATOM   15325 N  N     . GLU D 2 262 ? 153.146 91.238  149.980 1.00 21.69 ?  241 GLU D N     1 
ATOM   15326 C  CA    . GLU D 2 262 ? 153.931 90.142  149.388 1.00 22.31 ?  241 GLU D CA    1 
ATOM   15327 C  C     . GLU D 2 262 ? 153.914 90.194  147.859 1.00 21.69 ?  241 GLU D C     1 
ATOM   15328 O  O     . GLU D 2 262 ? 154.947 90.007  147.211 1.00 21.75 ?  241 GLU D O     1 
ATOM   15329 C  CB    . GLU D 2 262 ? 153.418 88.778  149.860 1.00 22.46 ?  241 GLU D CB    1 
ATOM   15330 C  CG    . GLU D 2 262 ? 153.497 88.522  151.367 1.00 25.63 ?  241 GLU D CG    1 
ATOM   15331 C  CD    . GLU D 2 262 ? 153.056 87.105  151.709 1.00 29.83 ?  241 GLU D CD    1 
ATOM   15332 O  OE1   . GLU D 2 262 ? 151.834 86.850  151.757 1.00 33.22 ?  241 GLU D OE1   1 
ATOM   15333 O  OE2   . GLU D 2 262 ? 153.925 86.236  151.900 1.00 33.36 -1 241 GLU D OE2   1 
ATOM   15334 N  N     . TYR D 2 263 ? 152.734 90.427  147.287 1.00 21.42 ?  242 TYR D N     1 
ATOM   15335 C  CA    . TYR D 2 263 ? 152.569 90.591  145.838 1.00 21.04 ?  242 TYR D CA    1 
ATOM   15336 C  C     . TYR D 2 263 ? 153.487 91.710  145.328 1.00 21.15 ?  242 TYR D C     1 
ATOM   15337 O  O     . TYR D 2 263 ? 154.128 91.581  144.284 1.00 20.32 ?  242 TYR D O     1 
ATOM   15338 C  CB    . TYR D 2 263 ? 151.102 90.925  145.525 1.00 20.95 ?  242 TYR D CB    1 
ATOM   15339 C  CG    . TYR D 2 263 ? 150.791 91.224  144.070 1.00 21.86 ?  242 TYR D CG    1 
ATOM   15340 C  CD1   . TYR D 2 263 ? 150.615 90.190  143.149 1.00 23.53 ?  242 TYR D CD1   1 
ATOM   15341 C  CD2   . TYR D 2 263 ? 150.672 92.540  143.612 1.00 21.20 ?  242 TYR D CD2   1 
ATOM   15342 C  CE1   . TYR D 2 263 ? 150.327 90.456  141.819 1.00 23.34 ?  242 TYR D CE1   1 
ATOM   15343 C  CE2   . TYR D 2 263 ? 150.385 92.815  142.280 1.00 23.11 ?  242 TYR D CE2   1 
ATOM   15344 C  CZ    . TYR D 2 263 ? 150.220 91.767  141.389 1.00 23.27 ?  242 TYR D CZ    1 
ATOM   15345 O  OH    . TYR D 2 263 ? 149.934 92.034  140.067 1.00 27.07 ?  242 TYR D OH    1 
ATOM   15346 N  N     . THR D 2 264 ? 153.518 92.808  146.081 1.00 21.12 ?  243 THR D N     1 
ATOM   15347 C  CA    . THR D 2 264 ? 154.284 94.000  145.729 1.00 21.98 ?  243 THR D CA    1 
ATOM   15348 C  C     . THR D 2 264 ? 155.784 93.714  145.706 1.00 22.32 ?  243 THR D C     1 
ATOM   15349 O  O     . THR D 2 264 ? 156.451 94.011  144.717 1.00 21.78 ?  243 THR D O     1 
ATOM   15350 C  CB    . THR D 2 264 ? 153.945 95.173  146.677 1.00 21.68 ?  243 THR D CB    1 
ATOM   15351 O  OG1   . THR D 2 264 ? 152.582 95.554  146.471 1.00 23.29 ?  243 THR D OG1   1 
ATOM   15352 C  CG2   . THR D 2 264 ? 154.859 96.392  146.443 1.00 23.16 ?  243 THR D CG2   1 
ATOM   15353 N  N     . GLU D 2 265 ? 156.304 93.119  146.779 1.00 22.48 ?  244 GLU D N     1 
ATOM   15354 C  CA    . GLU D 2 265 ? 157.730 92.784  146.823 1.00 23.73 ?  244 GLU D CA    1 
ATOM   15355 C  C     . GLU D 2 265 ? 158.110 91.820  145.710 1.00 23.85 ?  244 GLU D C     1 
ATOM   15356 O  O     . GLU D 2 265 ? 159.153 91.983  145.091 1.00 24.40 ?  244 GLU D O     1 
ATOM   15357 C  CB    . GLU D 2 265 ? 158.116 92.209  148.177 1.00 23.19 ?  244 GLU D CB    1 
ATOM   15358 C  CG    . GLU D 2 265 ? 158.158 93.267  149.247 1.00 25.08 ?  244 GLU D CG    1 
ATOM   15359 C  CD    . GLU D 2 265 ? 158.369 92.700  150.636 1.00 27.30 ?  244 GLU D CD    1 
ATOM   15360 O  OE1   . GLU D 2 265 ? 158.688 91.502  150.763 1.00 27.77 ?  244 GLU D OE1   1 
ATOM   15361 O  OE2   . GLU D 2 265 ? 158.214 93.467  151.603 1.00 28.63 -1 244 GLU D OE2   1 
ATOM   15362 N  N     . ASP D 2 266 ? 157.237 90.848  145.445 1.00 24.13 ?  245 ASP D N     1 
ATOM   15363 C  CA    . ASP D 2 266 ? 157.456 89.836  144.407 1.00 25.22 ?  245 ASP D CA    1 
ATOM   15364 C  C     . ASP D 2 266 ? 157.654 90.454  143.005 1.00 24.84 ?  245 ASP D C     1 
ATOM   15365 O  O     . ASP D 2 266 ? 158.464 89.961  142.215 1.00 25.64 ?  245 ASP D O     1 
ATOM   15366 C  CB    . ASP D 2 266 ? 156.283 88.843  144.412 1.00 25.79 ?  245 ASP D CB    1 
ATOM   15367 C  CG    . ASP D 2 266 ? 156.485 87.672  143.460 1.00 27.71 ?  245 ASP D CG    1 
ATOM   15368 O  OD1   . ASP D 2 266 ? 157.505 86.976  143.581 1.00 31.57 ?  245 ASP D OD1   1 
ATOM   15369 O  OD2   . ASP D 2 266 ? 155.609 87.429  142.602 1.00 30.29 -1 245 ASP D OD2   1 
ATOM   15370 N  N     . LEU D 2 267 ? 156.933 91.534  142.715 1.00 24.07 ?  246 LEU D N     1 
ATOM   15371 C  CA    . LEU D 2 267 ? 156.976 92.175  141.398 1.00 23.98 ?  246 LEU D CA    1 
ATOM   15372 C  C     . LEU D 2 267 ? 157.926 93.369  141.300 1.00 22.83 ?  246 LEU D C     1 
ATOM   15373 O  O     . LEU D 2 267 ? 158.589 93.550  140.271 1.00 23.00 ?  246 LEU D O     1 
ATOM   15374 C  CB    . LEU D 2 267 ? 155.570 92.630  140.969 1.00 23.82 ?  246 LEU D CB    1 
ATOM   15375 C  CG    . LEU D 2 267 ? 154.562 91.522  140.632 1.00 26.05 ?  246 LEU D CG    1 
ATOM   15376 C  CD1   . LEU D 2 267 ? 153.335 92.103  139.983 1.00 26.74 ?  246 LEU D CD1   1 
ATOM   15377 C  CD2   . LEU D 2 267 ? 155.168 90.467  139.727 1.00 28.00 ?  246 LEU D CD2   1 
ATOM   15378 N  N     . TYR D 2 268 ? 157.980 94.174  142.362 1.00 21.68 ?  247 TYR D N     1 
ATOM   15379 C  CA    . TYR D 2 268 ? 158.637 95.484  142.307 1.00 20.95 ?  247 TYR D CA    1 
ATOM   15380 C  C     . TYR D 2 268 ? 160.039 95.585  142.922 1.00 21.43 ?  247 TYR D C     1 
ATOM   15381 O  O     . TYR D 2 268 ? 160.745 96.555  142.647 1.00 20.73 ?  247 TYR D O     1 
ATOM   15382 C  CB    . TYR D 2 268 ? 157.742 96.566  142.919 1.00 20.27 ?  247 TYR D CB    1 
ATOM   15383 C  CG    . TYR D 2 268 ? 156.520 96.918  142.092 1.00 19.54 ?  247 TYR D CG    1 
ATOM   15384 C  CD1   . TYR D 2 268 ? 155.264 96.421  142.426 1.00 18.52 ?  247 TYR D CD1   1 
ATOM   15385 C  CD2   . TYR D 2 268 ? 156.627 97.751  140.968 1.00 20.62 ?  247 TYR D CD2   1 
ATOM   15386 C  CE1   . TYR D 2 268 ? 154.114 96.756  141.665 1.00 18.33 ?  247 TYR D CE1   1 
ATOM   15387 C  CE2   . TYR D 2 268 ? 155.489 98.091  140.199 1.00 20.79 ?  247 TYR D CE2   1 
ATOM   15388 C  CZ    . TYR D 2 268 ? 154.245 97.595  140.564 1.00 20.23 ?  247 TYR D CZ    1 
ATOM   15389 O  OH    . TYR D 2 268 ? 153.143 97.934  139.805 1.00 20.50 ?  247 TYR D OH    1 
ATOM   15390 N  N     . ASP D 2 269 ? 160.444 94.622  143.757 1.00 21.65 ?  248 ASP D N     1 
ATOM   15391 C  CA    . ASP D 2 269 ? 161.823 94.637  144.258 1.00 22.30 ?  248 ASP D CA    1 
ATOM   15392 C  C     . ASP D 2 269 ? 162.871 94.660  143.119 1.00 22.54 ?  248 ASP D C     1 
ATOM   15393 O  O     . ASP D 2 269 ? 163.890 95.347  143.233 1.00 22.49 ?  248 ASP D O     1 
ATOM   15394 C  CB    . ASP D 2 269 ? 162.096 93.477  145.216 1.00 22.83 ?  248 ASP D CB    1 
ATOM   15395 C  CG    . ASP D 2 269 ? 161.599 93.752  146.632 1.00 23.55 ?  248 ASP D CG    1 
ATOM   15396 O  OD1   . ASP D 2 269 ? 161.183 94.893  146.918 1.00 24.95 ?  248 ASP D OD1   1 
ATOM   15397 O  OD2   . ASP D 2 269 ? 161.625 92.819  147.466 1.00 24.47 -1 248 ASP D OD2   1 
ATOM   15398 N  N     . GLN D 2 270 ? 162.615 93.926  142.035 1.00 22.79 ?  249 GLN D N     1 
ATOM   15399 C  CA    . GLN D 2 270 ? 163.562 93.848  140.916 1.00 23.41 ?  249 GLN D CA    1 
ATOM   15400 C  C     . GLN D 2 270 ? 163.734 95.170  140.161 1.00 22.83 ?  249 GLN D C     1 
ATOM   15401 O  O     . GLN D 2 270 ? 164.691 95.327  139.404 1.00 23.75 ?  249 GLN D O     1 
ATOM   15402 C  CB    . GLN D 2 270 ? 163.200 92.722  139.942 1.00 24.02 ?  249 GLN D CB    1 
ATOM   15403 C  CG    . GLN D 2 270 ? 161.923 92.965  139.117 1.00 25.40 ?  249 GLN D CG    1 
ATOM   15404 C  CD    . GLN D 2 270 ? 161.438 91.711  138.410 1.00 29.23 ?  249 GLN D CD    1 
ATOM   15405 O  OE1   . GLN D 2 270 ? 161.623 90.597  138.903 1.00 31.31 ?  249 GLN D OE1   1 
ATOM   15406 N  NE2   . GLN D 2 270 ? 160.801 91.886  137.254 1.00 30.04 ?  249 GLN D NE2   1 
ATOM   15407 N  N     . VAL D 2 271 ? 162.804 96.105  140.352 1.00 21.93 ?  250 VAL D N     1 
ATOM   15408 C  CA    . VAL D 2 271 ? 162.926 97.443  139.766 1.00 21.29 ?  250 VAL D CA    1 
ATOM   15409 C  C     . VAL D 2 271 ? 163.008 98.546  140.838 1.00 21.16 ?  250 VAL D C     1 
ATOM   15410 O  O     . VAL D 2 271 ? 162.896 99.735  140.526 1.00 21.54 ?  250 VAL D O     1 
ATOM   15411 C  CB    . VAL D 2 271 ? 161.788 97.722  138.731 1.00 21.62 ?  250 VAL D CB    1 
ATOM   15412 C  CG1   . VAL D 2 271 ? 161.906 96.773  137.540 1.00 21.36 ?  250 VAL D CG1   1 
ATOM   15413 C  CG2   . VAL D 2 271 ? 160.397 97.610  139.383 1.00 21.17 ?  250 VAL D CG2   1 
ATOM   15414 N  N     . GLY D 2 272 ? 163.179 98.138  142.101 1.00 20.92 ?  251 GLY D N     1 
ATOM   15415 C  CA    . GLY D 2 272 ? 163.461 99.058  143.222 1.00 20.61 ?  251 GLY D CA    1 
ATOM   15416 C  C     . GLY D 2 272 ? 162.351 100.006 143.673 1.00 20.77 ?  251 GLY D C     1 
ATOM   15417 O  O     . GLY D 2 272 ? 162.629 101.069 144.248 1.00 20.28 ?  251 GLY D O     1 
ATOM   15418 N  N     . LEU D 2 273 ? 161.099 99.621  143.442 1.00 19.85 ?  252 LEU D N     1 
ATOM   15419 C  CA    . LEU D 2 273 ? 159.987 100.547 143.665 1.00 20.09 ?  252 LEU D CA    1 
ATOM   15420 C  C     . LEU D 2 273 ? 159.049 100.215 144.829 1.00 19.88 ?  252 LEU D C     1 
ATOM   15421 O  O     . LEU D 2 273 ? 158.154 101.000 145.125 1.00 20.04 ?  252 LEU D O     1 
ATOM   15422 C  CB    . LEU D 2 273 ? 159.152 100.660 142.378 1.00 19.97 ?  252 LEU D CB    1 
ATOM   15423 C  CG    . LEU D 2 273 ? 159.873 101.146 141.129 1.00 20.26 ?  252 LEU D CG    1 
ATOM   15424 C  CD1   . LEU D 2 273 ? 158.850 101.285 140.024 1.00 18.98 ?  252 LEU D CD1   1 
ATOM   15425 C  CD2   . LEU D 2 273 ? 160.616 102.490 141.369 1.00 21.03 ?  252 LEU D CD2   1 
ATOM   15426 N  N     . SER D 2 274 ? 159.269 99.074  145.483 0.50 19.54 ?  253 SER D N     1 
ATOM   15427 C  CA    . SER D 2 274 ? 158.295 98.511  146.432 0.50 19.34 ?  253 SER D CA    1 
ATOM   15428 C  C     . SER D 2 274 ? 157.864 99.453  147.562 0.50 20.05 ?  253 SER D C     1 
ATOM   15429 O  O     . SER D 2 274 ? 156.682 99.505  147.901 0.50 20.31 ?  253 SER D O     1 
ATOM   15430 C  CB    . SER D 2 274 ? 158.790 97.175  147.004 0.50 18.97 ?  253 SER D CB    1 
ATOM   15431 O  OG    . SER D 2 274 ? 159.084 96.250  145.973 0.50 15.35 ?  253 SER D OG    1 
ATOM   15432 N  N     . HIS D 2 275 ? 158.817 100.180 148.144 1.00 20.77 ?  254 HIS D N     1 
ATOM   15433 C  CA    . HIS D 2 275 ? 158.511 101.159 149.207 1.00 21.18 ?  254 HIS D CA    1 
ATOM   15434 C  C     . HIS D 2 275 ? 157.416 102.153 148.784 1.00 21.50 ?  254 HIS D C     1 
ATOM   15435 O  O     . HIS D 2 275 ? 156.430 102.357 149.512 1.00 19.88 ?  254 HIS D O     1 
ATOM   15436 C  CB    . HIS D 2 275 ? 159.770 101.913 149.663 1.00 21.60 ?  254 HIS D CB    1 
ATOM   15437 C  CG    . HIS D 2 275 ? 159.487 103.006 150.650 1.00 22.43 ?  254 HIS D CG    1 
ATOM   15438 N  ND1   . HIS D 2 275 ? 159.451 102.794 152.013 1.00 22.77 ?  254 HIS D ND1   1 
ATOM   15439 C  CD2   . HIS D 2 275 ? 159.209 104.321 150.465 1.00 22.50 ?  254 HIS D CD2   1 
ATOM   15440 C  CE1   . HIS D 2 275 ? 159.169 103.932 152.624 1.00 24.05 ?  254 HIS D CE1   1 
ATOM   15441 N  NE2   . HIS D 2 275 ? 159.011 104.872 151.707 1.00 23.22 ?  254 HIS D NE2   1 
ATOM   15442 N  N     . ASP D 2 276 ? 157.589 102.750 147.603 1.00 22.34 ?  255 ASP D N     1 
ATOM   15443 C  CA    . ASP D 2 276 ? 156.629 103.725 147.092 1.00 23.19 ?  255 ASP D CA    1 
ATOM   15444 C  C     . ASP D 2 276 ? 155.309 103.086 146.684 1.00 22.17 ?  255 ASP D C     1 
ATOM   15445 O  O     . ASP D 2 276 ? 154.263 103.701 146.841 1.00 21.87 ?  255 ASP D O     1 
ATOM   15446 C  CB    . ASP D 2 276 ? 157.205 104.516 145.906 1.00 24.33 ?  255 ASP D CB    1 
ATOM   15447 C  CG    . ASP D 2 276 ? 157.990 105.757 146.338 1.00 27.58 ?  255 ASP D CG    1 
ATOM   15448 O  OD1   . ASP D 2 276 ? 157.748 106.293 147.442 1.00 31.10 ?  255 ASP D OD1   1 
ATOM   15449 O  OD2   . ASP D 2 276 ? 158.863 106.195 145.554 1.00 29.88 -1 255 ASP D OD2   1 
ATOM   15450 N  N     . VAL D 2 277 ? 155.361 101.876 146.129 1.00 21.21 ?  256 VAL D N     1 
ATOM   15451 C  CA    . VAL D 2 277 ? 154.133 101.154 145.777 1.00 20.51 ?  256 VAL D CA    1 
ATOM   15452 C  C     . VAL D 2 277 ? 153.285 100.865 147.021 1.00 20.32 ?  256 VAL D C     1 
ATOM   15453 O  O     . VAL D 2 277 ? 152.065 101.002 146.983 1.00 19.81 ?  256 VAL D O     1 
ATOM   15454 C  CB    . VAL D 2 277 ? 154.416 99.839  144.997 1.00 20.30 ?  256 VAL D CB    1 
ATOM   15455 C  CG1   . VAL D 2 277 ? 153.122 99.092  144.721 1.00 21.16 ?  256 VAL D CG1   1 
ATOM   15456 C  CG2   . VAL D 2 277 ? 155.126 100.140 143.690 1.00 19.06 ?  256 VAL D CG2   1 
ATOM   15457 N  N     . LYS D 2 278 ? 153.945 100.488 148.116 1.00 19.84 ?  257 LYS D N     1 
ATOM   15458 C  CA    . LYS D 2 278 ? 153.262 100.235 149.385 1.00 20.27 ?  257 LYS D CA    1 
ATOM   15459 C  C     . LYS D 2 278 ? 152.502 101.464 149.900 1.00 20.16 ?  257 LYS D C     1 
ATOM   15460 O  O     . LYS D 2 278 ? 151.376 101.325 150.371 1.00 19.88 ?  257 LYS D O     1 
ATOM   15461 C  CB    . LYS D 2 278 ? 154.231 99.694  150.440 1.00 20.20 ?  257 LYS D CB    1 
ATOM   15462 C  CG    . LYS D 2 278 ? 154.643 98.247  150.190 1.00 21.60 ?  257 LYS D CG    1 
ATOM   15463 C  CD    . LYS D 2 278 ? 155.803 97.824  151.082 1.00 21.53 ?  257 LYS D CD    1 
ATOM   15464 C  CE    . LYS D 2 278 ? 156.283 96.450  150.684 1.00 24.52 ?  257 LYS D CE    1 
ATOM   15465 N  NZ    . LYS D 2 278 ? 157.402 95.999  151.574 1.00 26.32 1  257 LYS D NZ    1 
ATOM   15466 N  N     . LYS D 2 279 ? 153.103 102.653 149.783 1.00 19.67 ?  258 LYS D N     1 
ATOM   15467 C  CA    . LYS D 2 279 ? 152.407 103.897 150.143 1.00 20.10 ?  258 LYS D CA    1 
ATOM   15468 C  C     . LYS D 2 279 ? 151.138 104.085 149.302 1.00 19.12 ?  258 LYS D C     1 
ATOM   15469 O  O     . LYS D 2 279 ? 150.103 104.500 149.827 1.00 18.59 ?  258 LYS D O     1 
ATOM   15470 C  CB    . LYS D 2 279 ? 153.321 105.130 150.005 1.00 20.54 ?  258 LYS D CB    1 
ATOM   15471 C  CG    . LYS D 2 279 ? 154.559 105.117 150.900 1.00 22.84 ?  258 LYS D CG    1 
ATOM   15472 C  CD    . LYS D 2 279 ? 155.110 106.537 151.165 1.00 24.16 ?  258 LYS D CD    1 
ATOM   15473 C  CE    . LYS D 2 279 ? 155.664 107.199 149.906 1.00 25.61 ?  258 LYS D CE    1 
ATOM   15474 N  NZ    . LYS D 2 279 ? 156.207 108.587 150.177 1.00 24.70 1  258 LYS D NZ    1 
ATOM   15475 N  N     . PHE D 2 280 ? 151.232 103.755 148.010 1.00 19.04 ?  259 PHE D N     1 
ATOM   15476 C  CA    . PHE D 2 280 ? 150.115 103.875 147.055 1.00 19.31 ?  259 PHE D CA    1 
ATOM   15477 C  C     . PHE D 2 280 ? 148.974 102.893 147.343 1.00 19.25 ?  259 PHE D C     1 
ATOM   15478 O  O     . PHE D 2 280 ? 147.793 103.237 147.210 1.00 19.71 ?  259 PHE D O     1 
ATOM   15479 C  CB    . PHE D 2 280 ? 150.628 103.667 145.630 1.00 19.04 ?  259 PHE D CB    1 
ATOM   15480 C  CG    . PHE D 2 280 ? 149.684 104.142 144.542 1.00 20.15 ?  259 PHE D CG    1 
ATOM   15481 C  CD1   . PHE D 2 280 ? 149.225 105.450 144.514 1.00 21.63 ?  259 PHE D CD1   1 
ATOM   15482 C  CD2   . PHE D 2 280 ? 149.304 103.274 143.515 1.00 19.95 ?  259 PHE D CD2   1 
ATOM   15483 C  CE1   . PHE D 2 280 ? 148.378 105.895 143.474 1.00 22.56 ?  259 PHE D CE1   1 
ATOM   15484 C  CE2   . PHE D 2 280 ? 148.470 103.697 142.482 1.00 20.29 ?  259 PHE D CE2   1 
ATOM   15485 C  CZ    . PHE D 2 280 ? 148.002 105.012 142.462 1.00 21.30 ?  259 PHE D CZ    1 
ATOM   15486 N  N     . ILE D 2 281 ? 149.325 101.667 147.719 1.00 19.36 ?  260 ILE D N     1 
ATOM   15487 C  CA    . ILE D 2 281 ? 148.339 100.686 148.181 1.00 19.45 ?  260 ILE D CA    1 
ATOM   15488 C  C     . ILE D 2 281 ? 147.535 101.187 149.400 1.00 19.61 ?  260 ILE D C     1 
ATOM   15489 O  O     . ILE D 2 281 ? 146.306 101.094 149.405 1.00 19.72 ?  260 ILE D O     1 
ATOM   15490 C  CB    . ILE D 2 281 ? 149.034 99.332  148.480 1.00 19.49 ?  260 ILE D CB    1 
ATOM   15491 C  CG1   . ILE D 2 281 ? 149.580 98.736  147.180 1.00 20.10 ?  260 ILE D CG1   1 
ATOM   15492 C  CG2   . ILE D 2 281 ? 148.111 98.346  149.230 1.00 20.53 ?  260 ILE D CG2   1 
ATOM   15493 C  CD1   . ILE D 2 281 ? 150.564 97.588  147.431 1.00 21.17 ?  260 ILE D CD1   1 
ATOM   15494 N  N     . ARG D 2 282 ? 148.223 101.722 150.412 1.00 19.75 ?  261 ARG D N     1 
ATOM   15495 C  CA    . ARG D 2 282 ? 147.556 102.183 151.646 1.00 20.34 ?  261 ARG D CA    1 
ATOM   15496 C  C     . ARG D 2 282 ? 146.643 103.375 151.388 1.00 21.18 ?  261 ARG D C     1 
ATOM   15497 O  O     . ARG D 2 282 ? 145.533 103.462 151.932 1.00 21.68 ?  261 ARG D O     1 
ATOM   15498 C  CB    . ARG D 2 282 ? 148.577 102.512 152.743 1.00 20.20 ?  261 ARG D CB    1 
ATOM   15499 C  CG    . ARG D 2 282 ? 149.261 101.291 153.332 1.00 20.57 ?  261 ARG D CG    1 
ATOM   15500 C  CD    . ARG D 2 282 ? 150.137 101.668 154.530 1.00 23.15 ?  261 ARG D CD    1 
ATOM   15501 N  NE    . ARG D 2 282 ? 151.377 102.351 154.158 1.00 23.46 ?  261 ARG D NE    1 
ATOM   15502 C  CZ    . ARG D 2 282 ? 152.523 101.737 153.868 1.00 22.84 ?  261 ARG D CZ    1 
ATOM   15503 N  NH1   . ARG D 2 282 ? 152.599 100.413 153.866 1.00 23.37 1  261 ARG D NH1   1 
ATOM   15504 N  NH2   . ARG D 2 282 ? 153.597 102.454 153.566 1.00 22.27 ?  261 ARG D NH2   1 
ATOM   15505 N  N     . TYR D 2 283 ? 147.131 104.300 150.568 1.00 21.46 ?  262 TYR D N     1 
ATOM   15506 C  CA    . TYR D 2 283 ? 146.361 105.470 150.153 1.00 22.97 ?  262 TYR D CA    1 
ATOM   15507 C  C     . TYR D 2 283 ? 145.061 105.033 149.442 1.00 22.12 ?  262 TYR D C     1 
ATOM   15508 O  O     . TYR D 2 283 ? 143.984 105.575 149.705 1.00 22.00 ?  262 TYR D O     1 
ATOM   15509 C  CB    . TYR D 2 283 ? 147.252 106.352 149.272 1.00 23.37 ?  262 TYR D CB    1 
ATOM   15510 C  CG    . TYR D 2 283 ? 146.560 107.424 148.463 1.00 27.31 ?  262 TYR D CG    1 
ATOM   15511 C  CD1   . TYR D 2 283 ? 146.313 108.684 149.007 1.00 30.79 ?  262 TYR D CD1   1 
ATOM   15512 C  CD2   . TYR D 2 283 ? 146.195 107.191 147.137 1.00 30.31 ?  262 TYR D CD2   1 
ATOM   15513 C  CE1   . TYR D 2 283 ? 145.677 109.685 148.253 1.00 33.18 ?  262 TYR D CE1   1 
ATOM   15514 C  CE2   . TYR D 2 283 ? 145.571 108.181 146.372 1.00 33.20 ?  262 TYR D CE2   1 
ATOM   15515 C  CZ    . TYR D 2 283 ? 145.322 109.426 146.938 1.00 34.74 ?  262 TYR D CZ    1 
ATOM   15516 O  OH    . TYR D 2 283 ? 144.713 110.405 146.177 1.00 37.63 ?  262 TYR D OH    1 
ATOM   15517 N  N     . ASN D 2 284 ? 145.152 104.021 148.583 1.00 21.63 ?  263 ASN D N     1 
ATOM   15518 C  CA    . ASN D 2 284 ? 143.971 103.532 147.877 1.00 21.41 ?  263 ASN D CA    1 
ATOM   15519 C  C     . ASN D 2 284 ? 143.063 102.650 148.740 1.00 20.86 ?  263 ASN D C     1 
ATOM   15520 O  O     . ASN D 2 284 ? 141.852 102.648 148.548 1.00 20.92 ?  263 ASN D O     1 
ATOM   15521 C  CB    . ASN D 2 284 ? 144.350 102.866 146.553 1.00 21.15 ?  263 ASN D CB    1 
ATOM   15522 C  CG    . ASN D 2 284 ? 144.736 103.887 145.491 1.00 22.59 ?  263 ASN D CG    1 
ATOM   15523 O  OD1   . ASN D 2 284 ? 143.880 104.605 144.966 1.00 22.35 ?  263 ASN D OD1   1 
ATOM   15524 N  ND2   . ASN D 2 284 ? 146.027 103.968 145.181 1.00 22.93 ?  263 ASN D ND2   1 
ATOM   15525 N  N     . ALA D 2 285 ? 143.646 101.918 149.688 1.00 20.92 ?  264 ALA D N     1 
ATOM   15526 C  CA    . ALA D 2 285 ? 142.864 101.213 150.718 1.00 20.77 ?  264 ALA D CA    1 
ATOM   15527 C  C     . ALA D 2 285 ? 141.961 102.174 151.499 1.00 21.13 ?  264 ALA D C     1 
ATOM   15528 O  O     . ALA D 2 285 ? 140.786 101.871 151.744 1.00 19.92 ?  264 ALA D O     1 
ATOM   15529 C  CB    . ALA D 2 285 ? 143.786 100.439 151.672 1.00 20.68 ?  264 ALA D CB    1 
ATOM   15530 N  N     . ASN D 2 286 ? 142.514 103.331 151.879 1.00 21.38 ?  265 ASN D N     1 
ATOM   15531 C  CA    . ASN D 2 286 ? 141.751 104.383 152.556 1.00 21.94 ?  265 ASN D CA    1 
ATOM   15532 C  C     . ASN D 2 286 ? 140.594 104.917 151.693 1.00 22.13 ?  265 ASN D C     1 
ATOM   15533 O  O     . ASN D 2 286 ? 139.512 105.179 152.204 1.00 21.95 ?  265 ASN D O     1 
ATOM   15534 C  CB    . ASN D 2 286 ? 142.662 105.541 152.968 1.00 22.22 ?  265 ASN D CB    1 
ATOM   15535 C  CG    . ASN D 2 286 ? 143.463 105.261 154.236 1.00 22.80 ?  265 ASN D CG    1 
ATOM   15536 O  OD1   . ASN D 2 286 ? 143.200 104.308 154.979 1.00 22.57 ?  265 ASN D OD1   1 
ATOM   15537 N  ND2   . ASN D 2 286 ? 144.459 106.104 154.482 1.00 23.91 ?  265 ASN D ND2   1 
ATOM   15538 N  N     . LYS D 2 287 ? 140.823 105.068 150.391 1.00 22.51 ?  266 LYS D N     1 
ATOM   15539 C  CA    . LYS D 2 287 ? 139.750 105.494 149.480 1.00 22.91 ?  266 LYS D CA    1 
ATOM   15540 C  C     . LYS D 2 287 ? 138.628 104.450 149.417 1.00 22.33 ?  266 LYS D C     1 
ATOM   15541 O  O     . LYS D 2 287 ? 137.456 104.805 149.438 1.00 22.24 ?  266 LYS D O     1 
ATOM   15542 C  CB    . LYS D 2 287 ? 140.292 105.788 148.074 1.00 23.65 ?  266 LYS D CB    1 
ATOM   15543 C  CG    . LYS D 2 287 ? 141.064 107.104 147.973 1.00 26.50 ?  266 LYS D CG    1 
ATOM   15544 C  CD    . LYS D 2 287 ? 141.561 107.334 146.534 1.00 31.30 ?  266 LYS D CD    1 
ATOM   15545 C  CE    . LYS D 2 287 ? 141.866 108.805 146.311 1.00 35.08 ?  266 LYS D CE    1 
ATOM   15546 N  NZ    . LYS D 2 287 ? 142.322 109.121 144.923 1.00 37.66 1  266 LYS D NZ    1 
ATOM   15547 N  N     . ALA D 2 288 ? 139.003 103.171 149.357 1.00 21.41 ?  267 ALA D N     1 
ATOM   15548 C  CA    . ALA D 2 288 ? 138.056 102.056 149.341 1.00 21.53 ?  267 ALA D CA    1 
ATOM   15549 C  C     . ALA D 2 288 ? 137.192 102.028 150.614 1.00 21.77 ?  267 ALA D C     1 
ATOM   15550 O  O     . ALA D 2 288 ? 135.963 101.853 150.553 1.00 21.59 ?  267 ALA D O     1 
ATOM   15551 C  CB    . ALA D 2 288 ? 138.801 100.726 149.155 1.00 21.33 ?  267 ALA D CB    1 
ATOM   15552 N  N     . LEU D 2 289 ? 137.832 102.225 151.759 1.00 21.71 ?  268 LEU D N     1 
ATOM   15553 C  CA    . LEU D 2 289 ? 137.104 102.328 153.018 1.00 22.36 ?  268 LEU D CA    1 
ATOM   15554 C  C     . LEU D 2 289 ? 136.149 103.513 153.004 1.00 23.01 ?  268 LEU D C     1 
ATOM   15555 O  O     . LEU D 2 289 ? 134.984 103.381 153.388 1.00 23.14 ?  268 LEU D O     1 
ATOM   15556 C  CB    . LEU D 2 289 ? 138.069 102.399 154.208 1.00 22.61 ?  268 LEU D CB    1 
ATOM   15557 C  CG    . LEU D 2 289 ? 138.833 101.095 154.521 1.00 21.22 ?  268 LEU D CG    1 
ATOM   15558 C  CD1   . LEU D 2 289 ? 139.974 101.354 155.493 1.00 20.77 ?  268 LEU D CD1   1 
ATOM   15559 C  CD2   . LEU D 2 289 ? 137.898 99.991  155.064 1.00 21.40 ?  268 LEU D CD2   1 
ATOM   15560 N  N     . MET D 2 290 ? 136.617 104.667 152.539 1.00 23.87 ?  269 MET D N     1 
ATOM   15561 C  CA    . MET D 2 290 ? 135.729 105.824 152.470 1.00 25.26 ?  269 MET D CA    1 
ATOM   15562 C  C     . MET D 2 290 ? 134.535 105.578 151.531 1.00 24.37 ?  269 MET D C     1 
ATOM   15563 O  O     . MET D 2 290 ? 133.423 105.985 151.851 1.00 23.97 ?  269 MET D O     1 
ATOM   15564 C  CB    . MET D 2 290 ? 136.503 107.104 152.170 1.00 25.94 ?  269 MET D CB    1 
ATOM   15565 C  CG    . MET D 2 290 ? 137.197 107.641 153.437 1.00 31.08 ?  269 MET D CG    1 
ATOM   15566 S  SD    . MET D 2 290 ? 138.169 109.143 153.181 1.00 41.28 ?  269 MET D SD    1 
ATOM   15567 C  CE    . MET D 2 290 ? 136.958 110.224 152.377 1.00 38.56 ?  269 MET D CE    1 
ATOM   15568 N  N     . ASN D 2 291 ? 134.755 104.872 150.418 1.00 23.66 ?  270 ASN D N     1 
ATOM   15569 C  CA    . ASN D 2 291 ? 133.642 104.436 149.541 1.00 23.17 ?  270 ASN D CA    1 
ATOM   15570 C  C     . ASN D 2 291 ? 132.568 103.607 150.252 1.00 23.22 ?  270 ASN D C     1 
ATOM   15571 O  O     . ASN D 2 291 ? 131.398 103.643 149.873 1.00 22.68 ?  270 ASN D O     1 
ATOM   15572 C  CB    . ASN D 2 291 ? 134.153 103.656 148.320 1.00 22.41 ?  270 ASN D CB    1 
ATOM   15573 C  CG    . ASN D 2 291 ? 134.901 104.531 147.340 1.00 21.93 ?  270 ASN D CG    1 
ATOM   15574 O  OD1   . ASN D 2 291 ? 134.846 105.763 147.419 1.00 20.94 ?  270 ASN D OD1   1 
ATOM   15575 N  ND2   . ASN D 2 291 ? 135.609 103.901 146.407 1.00 19.20 ?  270 ASN D ND2   1 
ATOM   15576 N  N     . LEU D 2 292 ? 132.987 102.864 151.275 1.00 23.53 ?  271 LEU D N     1 
ATOM   15577 C  CA    . LEU D 2 292 ? 132.086 102.031 152.076 1.00 24.21 ?  271 LEU D CA    1 
ATOM   15578 C  C     . LEU D 2 292 ? 131.578 102.765 153.321 1.00 25.14 ?  271 LEU D C     1 
ATOM   15579 O  O     . LEU D 2 292 ? 130.954 102.158 154.207 1.00 25.14 ?  271 LEU D O     1 
ATOM   15580 C  CB    . LEU D 2 292 ? 132.781 100.709 152.463 1.00 23.71 ?  271 LEU D CB    1 
ATOM   15581 C  CG    . LEU D 2 292 ? 133.168 99.750  151.328 1.00 23.37 ?  271 LEU D CG    1 
ATOM   15582 C  CD1   . LEU D 2 292 ? 134.181 98.709  151.811 1.00 23.28 ?  271 LEU D CD1   1 
ATOM   15583 C  CD2   . LEU D 2 292 ? 131.932 99.065  150.712 1.00 23.06 ?  271 LEU D CD2   1 
ATOM   15584 N  N     . GLY D 2 293 ? 131.838 104.072 153.377 1.00 25.82 ?  272 GLY D N     1 
ATOM   15585 C  CA    . GLY D 2 293 ? 131.409 104.908 154.493 1.00 27.13 ?  272 GLY D CA    1 
ATOM   15586 C  C     . GLY D 2 293 ? 132.163 104.668 155.785 1.00 27.99 ?  272 GLY D C     1 
ATOM   15587 O  O     . GLY D 2 293 ? 131.684 105.036 156.853 1.00 27.97 ?  272 GLY D O     1 
ATOM   15588 N  N     . PHE D 2 294 ? 133.344 104.049 155.689 1.00 28.02 ?  273 PHE D N     1 
ATOM   15589 C  CA    . PHE D 2 294 ? 134.182 103.765 156.861 1.00 28.75 ?  273 PHE D CA    1 
ATOM   15590 C  C     . PHE D 2 294 ? 135.348 104.753 156.998 1.00 29.00 ?  273 PHE D C     1 
ATOM   15591 O  O     . PHE D 2 294 ? 135.734 105.404 156.030 1.00 28.74 ?  273 PHE D O     1 
ATOM   15592 C  CB    . PHE D 2 294 ? 134.734 102.332 156.792 1.00 28.32 ?  273 PHE D CB    1 
ATOM   15593 C  CG    . PHE D 2 294 ? 133.678 101.265 156.869 1.00 28.66 ?  273 PHE D CG    1 
ATOM   15594 C  CD1   . PHE D 2 294 ? 132.614 101.376 157.764 1.00 30.23 ?  273 PHE D CD1   1 
ATOM   15595 C  CD2   . PHE D 2 294 ? 133.756 100.140 156.058 1.00 26.94 ?  273 PHE D CD2   1 
ATOM   15596 C  CE1   . PHE D 2 294 ? 131.631 100.382 157.837 1.00 31.04 ?  273 PHE D CE1   1 
ATOM   15597 C  CE2   . PHE D 2 294 ? 132.792 99.144  156.122 1.00 27.39 ?  273 PHE D CE2   1 
ATOM   15598 C  CZ    . PHE D 2 294 ? 131.728 99.256  157.010 1.00 29.80 ?  273 PHE D CZ    1 
ATOM   15599 N  N     . ASP D 2 295 ? 135.899 104.855 158.206 1.00 29.60 ?  274 ASP D N     1 
ATOM   15600 C  CA    . ASP D 2 295 ? 137.055 105.709 158.466 1.00 30.40 ?  274 ASP D CA    1 
ATOM   15601 C  C     . ASP D 2 295 ? 138.333 105.149 157.811 1.00 29.58 ?  274 ASP D C     1 
ATOM   15602 O  O     . ASP D 2 295 ? 138.456 103.937 157.627 1.00 28.68 ?  274 ASP D O     1 
ATOM   15603 C  CB    . ASP D 2 295 ? 137.282 105.873 159.975 1.00 31.44 ?  274 ASP D CB    1 
ATOM   15604 C  CG    . ASP D 2 295 ? 136.149 106.620 160.670 1.00 34.27 ?  274 ASP D CG    1 
ATOM   15605 O  OD1   . ASP D 2 295 ? 135.479 107.465 160.028 1.00 36.43 ?  274 ASP D OD1   1 
ATOM   15606 O  OD2   . ASP D 2 295 ? 135.937 106.357 161.874 1.00 38.03 -1 274 ASP D OD2   1 
ATOM   15607 N  N     . PRO D 2 296 ? 139.290 106.032 157.469 1.00 29.59 ?  275 PRO D N     1 
ATOM   15608 C  CA    . PRO D 2 296 ? 140.557 105.527 156.931 1.00 29.09 ?  275 PRO D CA    1 
ATOM   15609 C  C     . PRO D 2 296 ? 141.273 104.653 157.959 1.00 29.26 ?  275 PRO D C     1 
ATOM   15610 O  O     . PRO D 2 296 ? 141.190 104.908 159.161 1.00 29.36 ?  275 PRO D O     1 
ATOM   15611 C  CB    . PRO D 2 296 ? 141.366 106.800 156.652 1.00 29.49 ?  275 PRO D CB    1 
ATOM   15612 C  CG    . PRO D 2 296 ? 140.706 107.884 157.460 1.00 30.28 ?  275 PRO D CG    1 
ATOM   15613 C  CD    . PRO D 2 296 ? 139.261 107.506 157.545 1.00 29.63 ?  275 PRO D CD    1 
ATOM   15614 N  N     . TYR D 2 297 ? 141.951 103.618 157.487 1.00 28.97 ?  276 TYR D N     1 
ATOM   15615 C  CA    . TYR D 2 297 ? 142.640 102.680 158.366 1.00 29.63 ?  276 TYR D CA    1 
ATOM   15616 C  C     . TYR D 2 297 ? 144.110 103.079 158.571 1.00 29.55 ?  276 TYR D C     1 
ATOM   15617 O  O     . TYR D 2 297 ? 144.683 102.881 159.650 1.00 30.12 ?  276 TYR D O     1 
ATOM   15618 C  CB    . TYR D 2 297 ? 142.557 101.282 157.753 1.00 29.49 ?  276 TYR D CB    1 
ATOM   15619 C  CG    . TYR D 2 297 ? 142.936 100.152 158.672 1.00 31.19 ?  276 TYR D CG    1 
ATOM   15620 C  CD1   . TYR D 2 297 ? 142.199 99.897  159.834 1.00 31.93 ?  276 TYR D CD1   1 
ATOM   15621 C  CD2   . TYR D 2 297 ? 144.013 99.316  158.373 1.00 31.98 ?  276 TYR D CD2   1 
ATOM   15622 C  CE1   . TYR D 2 297 ? 142.535 98.851  160.683 1.00 33.86 ?  276 TYR D CE1   1 
ATOM   15623 C  CE2   . TYR D 2 297 ? 144.356 98.258  159.217 1.00 33.88 ?  276 TYR D CE2   1 
ATOM   15624 C  CZ    . TYR D 2 297 ? 143.605 98.035  160.365 1.00 34.42 ?  276 TYR D CZ    1 
ATOM   15625 O  OH    . TYR D 2 297 ? 143.928 97.005  161.211 1.00 37.63 ?  276 TYR D OH    1 
ATOM   15626 N  N     . PHE D 2 298 ? 144.701 103.636 157.520 1.00 29.10 ?  277 PHE D N     1 
ATOM   15627 C  CA    . PHE D 2 298 ? 146.125 103.951 157.472 1.00 28.97 ?  277 PHE D CA    1 
ATOM   15628 C  C     . PHE D 2 298 ? 146.356 105.460 157.612 1.00 29.77 ?  277 PHE D C     1 
ATOM   15629 O  O     . PHE D 2 298 ? 145.528 106.265 157.174 1.00 29.07 ?  277 PHE D O     1 
ATOM   15630 C  CB    . PHE D 2 298 ? 146.726 103.463 156.150 1.00 27.99 ?  277 PHE D CB    1 
ATOM   15631 C  CG    . PHE D 2 298 ? 146.623 101.971 155.939 1.00 27.61 ?  277 PHE D CG    1 
ATOM   15632 C  CD1   . PHE D 2 298 ? 145.736 101.446 155.008 1.00 25.91 ?  277 PHE D CD1   1 
ATOM   15633 C  CD2   . PHE D 2 298 ? 147.432 101.093 156.662 1.00 27.32 ?  277 PHE D CD2   1 
ATOM   15634 C  CE1   . PHE D 2 298 ? 145.647 100.079 154.809 1.00 26.65 ?  277 PHE D CE1   1 
ATOM   15635 C  CE2   . PHE D 2 298 ? 147.356 99.725  156.472 1.00 25.38 ?  277 PHE D CE2   1 
ATOM   15636 C  CZ    . PHE D 2 298 ? 146.460 99.211  155.554 1.00 26.20 ?  277 PHE D CZ    1 
ATOM   15637 N  N     . GLU D 2 299 ? 147.478 105.829 158.228 1.00 31.10 ?  278 GLU D N     1 
ATOM   15638 C  CA    . GLU D 2 299 ? 147.897 107.231 158.316 1.00 32.86 ?  278 GLU D CA    1 
ATOM   15639 C  C     . GLU D 2 299 ? 148.116 107.799 156.907 1.00 33.04 ?  278 GLU D C     1 
ATOM   15640 O  O     . GLU D 2 299 ? 148.473 107.065 155.981 1.00 32.23 ?  278 GLU D O     1 
ATOM   15641 C  CB    . GLU D 2 299 ? 149.174 107.367 159.163 1.00 33.45 ?  278 GLU D CB    1 
ATOM   15642 C  CG    . GLU D 2 299 ? 150.384 106.624 158.577 1.00 36.27 ?  278 GLU D CG    1 
ATOM   15643 C  CD    . GLU D 2 299 ? 151.691 106.855 159.322 1.00 40.47 ?  278 GLU D CD    1 
ATOM   15644 O  OE1   . GLU D 2 299 ? 151.692 106.890 160.574 1.00 41.72 ?  278 GLU D OE1   1 
ATOM   15645 O  OE2   . GLU D 2 299 ? 152.729 106.972 158.634 1.00 42.65 -1 278 GLU D OE2   1 
ATOM   15646 N  N     . GLU D 2 300 ? 147.892 109.103 156.763 1.00 34.09 ?  279 GLU D N     1 
ATOM   15647 C  CA    . GLU D 2 300 ? 148.080 109.802 155.499 1.00 35.06 ?  279 GLU D CA    1 
ATOM   15648 C  C     . GLU D 2 300 ? 149.561 109.824 155.120 1.00 34.97 ?  279 GLU D C     1 
ATOM   15649 O  O     . GLU D 2 300 ? 150.424 110.087 155.959 1.00 34.96 ?  279 GLU D O     1 
ATOM   15650 C  CB    . GLU D 2 300 ? 147.517 111.230 155.594 1.00 35.81 ?  279 GLU D CB    1 
ATOM   15651 C  CG    . GLU D 2 300 ? 147.490 111.988 154.265 1.00 38.58 ?  279 GLU D CG    1 
ATOM   15652 C  CD    . GLU D 2 300 ? 146.441 113.098 154.227 1.00 43.09 ?  279 GLU D CD    1 
ATOM   15653 O  OE1   . GLU D 2 300 ? 145.582 113.069 153.316 1.00 44.69 ?  279 GLU D OE1   1 
ATOM   15654 O  OE2   . GLU D 2 300 ? 146.468 113.989 155.106 1.00 44.94 -1 279 GLU D OE2   1 
ATOM   15655 N  N     . GLU D 2 301 ? 149.839 109.518 153.856 1.00 34.73 ?  280 GLU D N     1 
ATOM   15656 C  CA    . GLU D 2 301 ? 151.195 109.528 153.322 1.00 35.16 ?  280 GLU D CA    1 
ATOM   15657 C  C     . GLU D 2 301 ? 151.199 110.274 151.999 1.00 35.23 ?  280 GLU D C     1 
ATOM   15658 O  O     . GLU D 2 301 ? 150.184 110.314 151.297 1.00 34.92 ?  280 GLU D O     1 
ATOM   15659 C  CB    . GLU D 2 301 ? 151.695 108.094 153.099 1.00 35.10 ?  280 GLU D CB    1 
ATOM   15660 C  CG    . GLU D 2 301 ? 152.210 107.389 154.351 1.00 36.62 ?  280 GLU D CG    1 
ATOM   15661 C  CD    . GLU D 2 301 ? 152.439 105.893 154.139 1.00 37.59 ?  280 GLU D CD    1 
ATOM   15662 O  OE1   . GLU D 2 301 ? 151.488 105.182 153.751 1.00 38.10 ?  280 GLU D OE1   1 
ATOM   15663 O  OE2   . GLU D 2 301 ? 153.566 105.419 154.385 1.00 38.93 -1 280 GLU D OE2   1 
ATOM   15664 N  N     . ASP D 2 302 ? 152.336 110.866 151.656 1.00 35.60 ?  281 ASP D N     1 
ATOM   15665 C  CA    . ASP D 2 302 ? 152.477 111.504 150.352 1.00 35.96 ?  281 ASP D CA    1 
ATOM   15666 C  C     . ASP D 2 302 ? 152.756 110.425 149.314 1.00 35.01 ?  281 ASP D C     1 
ATOM   15667 O  O     . ASP D 2 302 ? 153.295 109.369 149.646 1.00 35.52 ?  281 ASP D O     1 
ATOM   15668 C  CB    . ASP D 2 302 ? 153.566 112.591 150.374 1.00 36.82 ?  281 ASP D CB    1 
ATOM   15669 C  CG    . ASP D 2 302 ? 154.975 112.040 150.663 1.00 39.01 ?  281 ASP D CG    1 
ATOM   15670 O  OD1   . ASP D 2 302 ? 155.124 110.930 151.232 1.00 40.83 ?  281 ASP D OD1   1 
ATOM   15671 O  OD2   . ASP D 2 302 ? 155.946 112.751 150.331 1.00 41.13 -1 281 ASP D OD2   1 
ATOM   15672 N  N     . ILE D 2 303 ? 152.358 110.663 148.072 1.00 33.94 ?  282 ILE D N     1 
ATOM   15673 C  CA    . ILE D 2 303 ? 152.567 109.682 147.010 1.00 33.00 ?  282 ILE D CA    1 
ATOM   15674 C  C     . ILE D 2 303 ? 153.691 110.097 146.052 1.00 31.59 ?  282 ILE D C     1 
ATOM   15675 O  O     . ILE D 2 303 ? 153.955 111.288 145.875 1.00 31.14 ?  282 ILE D O     1 
ATOM   15676 C  CB    . ILE D 2 303 ? 151.231 109.348 146.270 1.00 33.44 ?  282 ILE D CB    1 
ATOM   15677 C  CG1   . ILE D 2 303 ? 151.467 108.966 144.804 1.00 34.29 ?  282 ILE D CG1   1 
ATOM   15678 C  CG2   . ILE D 2 303 ? 150.247 110.500 146.392 1.00 35.47 ?  282 ILE D CG2   1 
ATOM   15679 C  CD1   . ILE D 2 303 ? 150.198 108.828 143.986 1.00 36.30 ?  282 ILE D CD1   1 
ATOM   15680 N  N     . ASN D 2 304 ? 154.361 109.107 145.462 1.00 29.53 ?  283 ASN D N     1 
ATOM   15681 C  CA    . ASN D 2 304 ? 155.394 109.356 144.461 1.00 28.49 ?  283 ASN D CA    1 
ATOM   15682 C  C     . ASN D 2 304 ? 154.934 110.398 143.419 1.00 27.87 ?  283 ASN D C     1 
ATOM   15683 O  O     . ASN D 2 304 ? 153.888 110.226 142.795 1.00 27.02 ?  283 ASN D O     1 
ATOM   15684 C  CB    . ASN D 2 304 ? 155.781 108.045 143.773 1.00 28.20 ?  283 ASN D CB    1 
ATOM   15685 C  CG    . ASN D 2 304 ? 156.910 108.222 142.792 1.00 28.17 ?  283 ASN D CG    1 
ATOM   15686 O  OD1   . ASN D 2 304 ? 156.687 108.577 141.639 1.00 29.01 ?  283 ASN D OD1   1 
ATOM   15687 N  ND2   . ASN D 2 304 ? 158.131 107.976 143.241 1.00 27.24 ?  283 ASN D ND2   1 
ATOM   15688 N  N     . PRO D 2 305 ? 155.709 111.489 143.243 1.00 28.00 ?  284 PRO D N     1 
ATOM   15689 C  CA    . PRO D 2 305 ? 155.279 112.583 142.357 1.00 27.58 ?  284 PRO D CA    1 
ATOM   15690 C  C     . PRO D 2 305 ? 155.198 112.210 140.875 1.00 27.01 ?  284 PRO D C     1 
ATOM   15691 O  O     . PRO D 2 305 ? 154.449 112.836 140.132 1.00 26.66 ?  284 PRO D O     1 
ATOM   15692 C  CB    . PRO D 2 305 ? 156.345 113.665 142.578 1.00 28.21 ?  284 PRO D CB    1 
ATOM   15693 C  CG    . PRO D 2 305 ? 157.505 112.972 143.143 1.00 28.80 ?  284 PRO D CG    1 
ATOM   15694 C  CD    . PRO D 2 305 ? 156.943 111.837 143.970 1.00 28.11 ?  284 PRO D CD    1 
ATOM   15695 N  N     . ILE D 2 306 ? 155.955 111.201 140.454 1.00 26.52 ?  285 ILE D N     1 
ATOM   15696 C  CA    . ILE D 2 306 ? 155.897 110.742 139.072 1.00 26.50 ?  285 ILE D CA    1 
ATOM   15697 C  C     . ILE D 2 306 ? 154.553 110.048 138.806 1.00 26.43 ?  285 ILE D C     1 
ATOM   15698 O  O     . ILE D 2 306 ? 153.864 110.343 137.820 1.00 26.00 ?  285 ILE D O     1 
ATOM   15699 C  CB    . ILE D 2 306 ? 157.105 109.840 138.712 1.00 26.88 ?  285 ILE D CB    1 
ATOM   15700 C  CG1   . ILE D 2 306 ? 158.414 110.630 138.890 1.00 26.98 ?  285 ILE D CG1   1 
ATOM   15701 C  CG2   . ILE D 2 306 ? 156.950 109.304 137.289 1.00 24.94 ?  285 ILE D CG2   1 
ATOM   15702 C  CD1   . ILE D 2 306 ? 159.673 109.817 138.754 1.00 26.65 ?  285 ILE D CD1   1 
ATOM   15703 N  N     . VAL D 2 307 ? 154.176 109.153 139.713 1.00 26.36 ?  286 VAL D N     1 
ATOM   15704 C  CA    . VAL D 2 307 ? 152.855 108.538 139.682 1.00 26.71 ?  286 VAL D CA    1 
ATOM   15705 C  C     . VAL D 2 307 ? 151.741 109.584 139.792 1.00 27.68 ?  286 VAL D C     1 
ATOM   15706 O  O     . VAL D 2 307 ? 150.755 109.498 139.059 1.00 27.92 ?  286 VAL D O     1 
ATOM   15707 C  CB    . VAL D 2 307 ? 152.721 107.414 140.745 1.00 26.37 ?  286 VAL D CB    1 
ATOM   15708 C  CG1   . VAL D 2 307 ? 151.266 106.938 140.885 1.00 25.48 ?  286 VAL D CG1   1 
ATOM   15709 C  CG2   . VAL D 2 307 ? 153.592 106.265 140.349 1.00 25.55 ?  286 VAL D CG2   1 
ATOM   15710 N  N     . LEU D 2 308 ? 151.905 110.584 140.663 1.00 28.80 ?  287 LEU D N     1 
ATOM   15711 C  CA    . LEU D 2 308 ? 150.933 111.688 140.727 1.00 30.07 ?  287 LEU D CA    1 
ATOM   15712 C  C     . LEU D 2 308 ? 150.786 112.421 139.389 1.00 30.38 ?  287 LEU D C     1 
ATOM   15713 O  O     . LEU D 2 308 ? 149.673 112.757 138.971 1.00 30.71 ?  287 LEU D O     1 
ATOM   15714 C  CB    . LEU D 2 308 ? 151.283 112.685 141.836 1.00 30.86 ?  287 LEU D CB    1 
ATOM   15715 C  CG    . LEU D 2 308 ? 150.787 112.321 143.239 1.00 32.62 ?  287 LEU D CG    1 
ATOM   15716 C  CD1   . LEU D 2 308 ? 151.365 113.264 144.273 1.00 33.97 ?  287 LEU D CD1   1 
ATOM   15717 C  CD2   . LEU D 2 308 ? 149.248 112.311 143.311 1.00 34.73 ?  287 LEU D CD2   1 
ATOM   15718 N  N     . ASN D 2 309 ? 151.905 112.657 138.713 1.00 30.81 ?  288 ASN D N     1 
ATOM   15719 C  CA    . ASN D 2 309 ? 151.871 113.304 137.406 1.00 31.25 ?  288 ASN D CA    1 
ATOM   15720 C  C     . ASN D 2 309 ? 151.145 112.444 136.369 1.00 31.83 ?  288 ASN D C     1 
ATOM   15721 O  O     . ASN D 2 309 ? 150.468 112.971 135.480 1.00 31.73 ?  288 ASN D O     1 
ATOM   15722 C  CB    . ASN D 2 309 ? 153.277 113.681 136.927 1.00 31.21 ?  288 ASN D CB    1 
ATOM   15723 C  CG    . ASN D 2 309 ? 153.248 114.530 135.666 1.00 31.41 ?  288 ASN D CG    1 
ATOM   15724 O  OD1   . ASN D 2 309 ? 152.452 115.469 135.557 1.00 31.88 ?  288 ASN D OD1   1 
ATOM   15725 N  ND2   . ASN D 2 309 ? 154.108 114.202 134.707 1.00 29.12 ?  288 ASN D ND2   1 
ATOM   15726 N  N     . GLY D 2 310 ? 151.287 111.125 136.496 1.00 32.04 ?  289 GLY D N     1 
ATOM   15727 C  CA    . GLY D 2 310 ? 150.534 110.179 135.680 1.00 33.04 ?  289 GLY D CA    1 
ATOM   15728 C  C     . GLY D 2 310 ? 149.041 110.251 135.978 1.00 33.85 ?  289 GLY D C     1 
ATOM   15729 O  O     . GLY D 2 310 ? 148.227 110.325 135.058 1.00 34.05 ?  289 GLY D O     1 
ATOM   15730 N  N     . LEU D 2 311 ? 148.690 110.233 137.263 1.00 34.33 ?  290 LEU D N     1 
ATOM   15731 C  CA    . LEU D 2 311 ? 147.294 110.274 137.707 1.00 35.77 ?  290 LEU D CA    1 
ATOM   15732 C  C     . LEU D 2 311 ? 146.563 111.545 137.287 1.00 37.01 ?  290 LEU D C     1 
ATOM   15733 O  O     . LEU D 2 311 ? 145.397 111.496 136.893 1.00 37.18 ?  290 LEU D O     1 
ATOM   15734 C  CB    . LEU D 2 311 ? 147.209 110.144 139.233 1.00 35.50 ?  290 LEU D CB    1 
ATOM   15735 C  CG    . LEU D 2 311 ? 147.082 108.785 139.915 1.00 35.45 ?  290 LEU D CG    1 
ATOM   15736 C  CD1   . LEU D 2 311 ? 147.212 108.969 141.435 1.00 35.28 ?  290 LEU D CD1   1 
ATOM   15737 C  CD2   . LEU D 2 311 ? 145.766 108.083 139.573 1.00 34.16 ?  290 LEU D CD2   1 
ATOM   15738 N  N     . LYS D 2 330 ? 118.670 117.512 150.014 1.00 61.72 ?  309 LYS D N     1 
ATOM   15739 C  CA    . LYS D 2 330 ? 117.396 116.803 150.031 1.00 61.83 ?  309 LYS D CA    1 
ATOM   15740 C  C     . LYS D 2 330 ? 117.084 116.280 151.426 1.00 62.21 ?  309 LYS D C     1 
ATOM   15741 O  O     . LYS D 2 330 ? 117.378 115.124 151.731 1.00 61.32 ?  309 LYS D O     1 
ATOM   15742 C  CB    . LYS D 2 330 ? 117.413 115.632 149.045 1.00 59.60 ?  309 LYS D CB    1 
ATOM   15743 C  CG    . LYS D 2 330 ? 117.965 115.953 147.670 1.00 60.95 ?  309 LYS D CG    1 
ATOM   15744 C  CD    . LYS D 2 330 ? 116.944 115.658 146.583 1.00 60.77 ?  309 LYS D CD    1 
ATOM   15745 C  CE    . LYS D 2 330 ? 117.328 116.318 145.269 1.00 61.40 ?  309 LYS D CE    1 
ATOM   15746 N  NZ    . LYS D 2 330 ? 116.470 117.494 144.961 1.00 62.04 1  309 LYS D NZ    1 
ATOM   15747 N  N     . ALA D 2 331 ? 116.502 117.115 152.286 1.00 57.72 ?  310 ALA D N     1 
ATOM   15748 C  CA    . ALA D 2 331 ? 116.145 116.641 153.615 1.00 58.04 ?  310 ALA D CA    1 
ATOM   15749 C  C     . ALA D 2 331 ? 114.816 115.896 153.626 1.00 58.14 ?  310 ALA D C     1 
ATOM   15750 O  O     . ALA D 2 331 ? 114.799 114.674 153.810 1.00 58.87 ?  310 ALA D O     1 
ATOM   15751 C  CB    . ALA D 2 331 ? 116.093 117.817 154.597 1.00 56.57 ?  310 ALA D CB    1 
ATOM   15752 N  N     . THR D 2 332 ? 113.703 116.606 153.429 1.00 46.15 ?  311 THR D N     1 
ATOM   15753 C  CA    . THR D 2 332 ? 112.408 116.004 153.125 1.00 42.78 ?  311 THR D CA    1 
ATOM   15754 C  C     . THR D 2 332 ? 111.411 117.072 152.684 1.00 42.27 ?  311 THR D C     1 
ATOM   15755 O  O     . THR D 2 332 ? 111.060 117.959 153.469 1.00 45.09 ?  311 THR D O     1 
ATOM   15756 C  CB    . THR D 2 332 ? 111.875 115.208 154.324 1.00 46.86 ?  311 THR D CB    1 
ATOM   15757 O  OG1   . THR D 2 332 ? 110.715 114.458 153.940 1.00 46.97 ?  311 THR D OG1   1 
ATOM   15758 C  CG2   . THR D 2 332 ? 111.571 116.114 155.500 1.00 43.65 ?  311 THR D CG2   1 
ATOM   15759 N  N     . VAL D 2 333 ? 110.946 117.001 151.438 1.00 39.49 ?  312 VAL D N     1 
ATOM   15760 C  CA    . VAL D 2 333 ? 109.960 117.952 150.937 1.00 35.97 ?  312 VAL D CA    1 
ATOM   15761 C  C     . VAL D 2 333 ? 108.633 117.730 151.651 1.00 40.19 ?  312 VAL D C     1 
ATOM   15762 O  O     . VAL D 2 333 ? 108.099 116.614 151.658 1.00 43.38 ?  312 VAL D O     1 
ATOM   15763 C  CB    . VAL D 2 333 ? 109.792 117.832 149.411 1.00 38.60 ?  312 VAL D CB    1 
ATOM   15764 C  CG1   . VAL D 2 333 ? 108.437 118.372 148.974 1.00 39.63 ?  312 VAL D CG1   1 
ATOM   15765 C  CG2   . VAL D 2 333 ? 110.916 118.561 148.694 1.00 39.03 ?  312 VAL D CG2   1 
ATOM   15766 N  N     . GLU D 2 334 ? 108.096 118.784 152.264 1.00 39.20 ?  313 GLU D N     1 
ATOM   15767 C  CA    . GLU D 2 334 ? 106.776 118.741 152.886 1.00 36.81 ?  313 GLU D CA    1 
ATOM   15768 C  C     . GLU D 2 334 ? 106.014 119.989 152.461 1.00 37.73 ?  313 GLU D C     1 
ATOM   15769 O  O     . GLU D 2 334 ? 106.564 121.106 152.546 1.00 40.12 ?  313 GLU D O     1 
ATOM   15770 C  CB    . GLU D 2 334 ? 106.867 118.648 154.410 1.00 34.61 ?  313 GLU D CB    1 
ATOM   15771 C  CG    . GLU D 2 334 ? 105.517 118.429 155.078 1.00 37.90 ?  313 GLU D CG    1 
ATOM   15772 C  CD    . GLU D 2 334 ? 105.606 118.311 156.585 1.00 39.43 ?  313 GLU D CD    1 
ATOM   15773 O  OE1   . GLU D 2 334 ? 106.732 118.280 157.116 1.00 37.54 ?  313 GLU D OE1   1 
ATOM   15774 O  OE2   . GLU D 2 334 ? 104.546 118.245 157.240 1.00 39.69 -1 313 GLU D OE2   1 
ATOM   15775 N  N     . PRO D 2 335 ? 104.774 119.863 151.997 1.00 38.18 ?  314 PRO D N     1 
ATOM   15776 C  CA    . PRO D 2 335 ? 104.030 121.043 151.548 1.00 40.62 ?  314 PRO D CA    1 
ATOM   15777 C  C     . PRO D 2 335 ? 103.615 121.934 152.708 1.00 40.02 ?  314 PRO D C     1 
ATOM   15778 O  O     . PRO D 2 335 ? 103.486 121.492 153.851 1.00 41.11 ?  314 PRO D O     1 
ATOM   15779 C  CB    . PRO D 2 335 ? 102.808 120.443 150.848 1.00 37.91 ?  314 PRO D CB    1 
ATOM   15780 C  CG    . PRO D 2 335 ? 102.616 119.126 151.522 1.00 34.58 ?  314 PRO D CG    1 
ATOM   15781 C  CD    . PRO D 2 335 ? 104.001 118.622 151.816 1.00 36.60 ?  314 PRO D CD    1 
ATOM   15782 N  N     . LEU D 2 336 ? 103.413 123.212 152.396 1.00 34.57 ?  315 LEU D N     1 
ATOM   15783 C  CA    . LEU D 2 336 ? 102.836 124.148 153.350 1.00 30.08 ?  315 LEU D CA    1 
ATOM   15784 C  C     . LEU D 2 336 ? 101.329 123.937 153.408 1.00 33.20 ?  315 LEU D C     1 
ATOM   15785 O  O     . LEU D 2 336 ? 100.631 124.109 152.404 1.00 37.22 ?  315 LEU D O     1 
ATOM   15786 C  CB    . LEU D 2 336 ? 103.159 125.587 152.947 1.00 28.04 ?  315 LEU D CB    1 
ATOM   15787 C  CG    . LEU D 2 336 ? 104.562 126.101 153.271 1.00 27.76 ?  315 LEU D CG    1 
ATOM   15788 C  CD1   . LEU D 2 336 ? 104.943 127.235 152.335 1.00 24.11 ?  315 LEU D CD1   1 
ATOM   15789 C  CD2   . LEU D 2 336 ? 104.640 126.551 154.718 1.00 29.08 ?  315 LEU D CD2   1 
ATOM   15790 N  N     . LYS D 2 337 ? 100.826 123.565 154.584 1.00 36.25 ?  316 LYS D N     1 
ATOM   15791 C  CA    . LYS D 2 337 ? 99.436  123.157 154.746 1.00 47.76 ?  316 LYS D CA    1 
ATOM   15792 C  C     . LYS D 2 337 ? 98.603  124.237 155.428 1.00 47.26 ?  316 LYS D C     1 
ATOM   15793 O  O     . LYS D 2 337 ? 97.700  123.928 156.208 1.00 51.37 ?  316 LYS D O     1 
ATOM   15794 C  CB    . LYS D 2 337 ? 99.349  121.847 155.528 1.00 44.37 ?  316 LYS D CB    1 
ATOM   15795 C  CG    . LYS D 2 337 ? 100.324 121.760 156.689 1.00 46.03 ?  316 LYS D CG    1 
ATOM   15796 C  CD    . LYS D 2 337 ? 100.816 120.338 156.897 1.00 46.40 ?  316 LYS D CD    1 
ATOM   15797 C  CE    . LYS D 2 337 ? 101.363 119.751 155.607 1.00 45.29 ?  316 LYS D CE    1 
ATOM   15798 N  NZ    . LYS D 2 337 ? 102.256 118.589 155.859 1.00 42.09 1  316 LYS D NZ    1 
ATOM   15799 N  N     . ASP D 2 338 ? 98.906  125.505 155.141 1.00 29.55 ?  317 ASP D N     1 
ATOM   15800 C  CA    . ASP D 2 338 ? 98.230  126.655 155.736 1.00 32.48 ?  317 ASP D CA    1 
ATOM   15801 C  C     . ASP D 2 338 ? 98.410  126.695 157.249 1.00 37.94 ?  317 ASP D C     1 
ATOM   15802 O  O     . ASP D 2 338 ? 98.908  125.737 157.851 1.00 40.84 ?  317 ASP D O     1 
ATOM   15803 C  CB    . ASP D 2 338 ? 96.742  126.661 155.374 1.00 36.01 ?  317 ASP D CB    1 
ATOM   15804 C  CG    . ASP D 2 338 ? 96.163  128.059 155.335 1.00 38.86 ?  317 ASP D CG    1 
ATOM   15805 O  OD1   . ASP D 2 338 ? 96.929  129.022 155.549 1.00 36.19 ?  317 ASP D OD1   1 
ATOM   15806 O  OD2   . ASP D 2 338 ? 94.945  128.195 155.092 1.00 34.94 -1 317 ASP D OD2   1 
ATOM   15807 N  N     . ASP D 2 339 ? 98.054  127.829 157.860 1.00 32.37 ?  318 ASP D N     1 
ATOM   15808 C  CA    . ASP D 2 339 ? 98.253  128.089 159.284 1.00 28.49 ?  318 ASP D CA    1 
ATOM   15809 C  C     . ASP D 2 339 ? 99.740  128.194 159.605 1.00 28.80 ?  318 ASP D C     1 
ATOM   15810 O  O     . ASP D 2 339 ? 100.118 128.487 160.743 1.00 36.28 ?  318 ASP D O     1 
ATOM   15811 C  CB    . ASP D 2 339 ? 97.584  127.018 160.150 1.00 30.55 ?  318 ASP D CB    1 
ATOM   15812 C  CG    . ASP D 2 339 ? 96.715  127.612 161.242 1.00 37.05 ?  318 ASP D CG    1 
ATOM   15813 O  OD1   . ASP D 2 339 ? 97.050  128.708 161.739 1.00 32.14 ?  318 ASP D OD1   1 
ATOM   15814 O  OD2   . ASP D 2 339 ? 95.696  126.985 161.603 1.00 39.30 -1 318 ASP D OD2   1 
ATOM   15815 N  N     . ASP D 2 340 ? 100.587 127.957 158.604 1.00 24.72 ?  319 ASP D N     1 
ATOM   15816 C  CA    . ASP D 2 340 ? 102.006 128.256 158.682 1.00 24.52 ?  319 ASP D CA    1 
ATOM   15817 C  C     . ASP D 2 340 ? 102.306 129.696 158.303 1.00 21.51 ?  319 ASP D C     1 
ATOM   15818 O  O     . ASP D 2 340 ? 103.431 130.160 158.516 1.00 32.71 ?  319 ASP D O     1 
ATOM   15819 C  CB    . ASP D 2 340 ? 102.796 127.310 157.772 1.00 23.05 ?  319 ASP D CB    1 
ATOM   15820 C  CG    . ASP D 2 340 ? 102.755 125.872 158.250 1.00 28.00 ?  319 ASP D CG    1 
ATOM   15821 O  OD1   . ASP D 2 340 ? 102.670 125.651 159.476 1.00 34.28 ?  319 ASP D OD1   1 
ATOM   15822 O  OD2   . ASP D 2 340 ? 102.808 124.960 157.399 1.00 31.08 -1 319 ASP D OD2   1 
ATOM   15823 N  N     . PHE D 2 341 ? 101.327 130.403 157.744 1.00 10.52 ?  320 PHE D N     1 
ATOM   15824 C  CA    . PHE D 2 341 ? 101.437 131.816 157.425 1.00 15.27 ?  320 PHE D CA    1 
ATOM   15825 C  C     . PHE D 2 341 ? 100.861 132.700 158.519 1.00 12.85 ?  320 PHE D C     1 
ATOM   15826 O  O     . PHE D 2 341 ? 100.858 133.925 158.373 1.00 22.40 ?  320 PHE D O     1 
ATOM   15827 C  CB    . PHE D 2 341 ? 100.727 132.112 156.100 1.00 21.01 ?  320 PHE D CB    1 
ATOM   15828 C  CG    . PHE D 2 341 ? 101.311 131.386 154.920 1.00 15.79 ?  320 PHE D CG    1 
ATOM   15829 C  CD1   . PHE D 2 341 ? 100.921 130.091 154.628 1.00 11.88 ?  320 PHE D CD1   1 
ATOM   15830 C  CD2   . PHE D 2 341 ? 102.239 132.000 154.100 1.00 9.87  ?  320 PHE D CD2   1 
ATOM   15831 C  CE1   . PHE D 2 341 ? 101.453 129.421 153.546 1.00 13.02 ?  320 PHE D CE1   1 
ATOM   15832 C  CE2   . PHE D 2 341 ? 102.773 131.334 153.016 1.00 10.78 ?  320 PHE D CE2   1 
ATOM   15833 C  CZ    . PHE D 2 341 ? 102.380 130.043 152.740 1.00 4.79  ?  320 PHE D CZ    1 
ATOM   15834 N  N     . TYR D 2 342 ? 100.374 132.106 159.605 1.00 12.46 ?  321 TYR D N     1 
ATOM   15835 C  CA    . TYR D 2 342 ? 99.763  132.836 160.704 1.00 17.95 ?  321 TYR D CA    1 
ATOM   15836 C  C     . TYR D 2 342 ? 100.479 132.475 161.995 1.00 22.41 ?  321 TYR D C     1 
ATOM   15837 O  O     . TYR D 2 342 ? 100.842 131.315 162.209 1.00 24.04 ?  321 TYR D O     1 
ATOM   15838 C  CB    . TYR D 2 342 ? 98.271  132.513 160.819 1.00 13.28 ?  321 TYR D CB    1 
ATOM   15839 C  CG    . TYR D 2 342 ? 97.468  132.924 159.608 1.00 11.63 ?  321 TYR D CG    1 
ATOM   15840 C  CD1   . TYR D 2 342 ? 97.003  134.225 159.466 1.00 16.81 ?  321 TYR D CD1   1 
ATOM   15841 C  CD2   . TYR D 2 342 ? 97.181  132.013 158.601 1.00 15.94 ?  321 TYR D CD2   1 
ATOM   15842 C  CE1   . TYR D 2 342 ? 96.271  134.604 158.358 1.00 20.80 ?  321 TYR D CE1   1 
ATOM   15843 C  CE2   . TYR D 2 342 ? 96.451  132.383 157.490 1.00 15.55 ?  321 TYR D CE2   1 
ATOM   15844 C  CZ    . TYR D 2 342 ? 95.998  133.679 157.373 1.00 24.69 ?  321 TYR D CZ    1 
ATOM   15845 O  OH    . TYR D 2 342 ? 95.268  134.054 156.268 1.00 21.45 ?  321 TYR D OH    1 
ATOM   15846 N  N     . PHE D 2 343 ? 100.686 133.472 162.847 1.00 12.93 ?  322 PHE D N     1 
ATOM   15847 C  CA    . PHE D 2 343 ? 101.426 133.273 164.088 1.00 18.66 ?  322 PHE D CA    1 
ATOM   15848 C  C     . PHE D 2 343 ? 100.746 133.985 165.252 1.00 24.79 ?  322 PHE D C     1 
ATOM   15849 O  O     . PHE D 2 343 ? 100.389 135.157 165.154 1.00 23.91 ?  322 PHE D O     1 
ATOM   15850 C  CB    . PHE D 2 343 ? 102.869 133.766 163.933 1.00 13.99 ?  322 PHE D CB    1 
ATOM   15851 C  CG    . PHE D 2 343 ? 103.519 133.342 162.647 1.00 14.21 ?  322 PHE D CG    1 
ATOM   15852 C  CD1   . PHE D 2 343 ? 103.435 134.135 161.516 1.00 13.48 ?  322 PHE D CD1   1 
ATOM   15853 C  CD2   . PHE D 2 343 ? 104.211 132.148 162.569 1.00 16.65 ?  322 PHE D CD2   1 
ATOM   15854 C  CE1   . PHE D 2 343 ? 104.027 133.742 160.333 1.00 9.34  ?  322 PHE D CE1   1 
ATOM   15855 C  CE2   . PHE D 2 343 ? 104.804 131.752 161.388 1.00 9.50  ?  322 PHE D CE2   1 
ATOM   15856 C  CZ    . PHE D 2 343 ? 104.711 132.551 160.271 1.00 5.03  ?  322 PHE D CZ    1 
HETATM 15857 P  PA    . TTP E 3 .   ? 146.030 144.525 134.253 1.00 19.37 ?  801 TTP A PA    1 
HETATM 15858 O  O1A   . TTP E 3 .   ? 144.590 144.958 134.164 1.00 21.91 -1 801 TTP A O1A   1 
HETATM 15859 O  O2A   . TTP E 3 .   ? 146.891 145.336 133.318 1.00 26.56 ?  801 TTP A O2A   1 
HETATM 15860 O  O3A   . TTP E 3 .   ? 146.543 144.574 135.775 1.00 35.02 ?  801 TTP A O3A   1 
HETATM 15861 P  PB    . TTP E 3 .   ? 147.619 145.658 136.275 1.00 29.77 ?  801 TTP A PB    1 
HETATM 15862 O  O1B   . TTP E 3 .   ? 147.274 146.104 137.672 1.00 33.96 -1 801 TTP A O1B   1 
HETATM 15863 O  O2B   . TTP E 3 .   ? 147.727 146.850 135.360 1.00 25.37 ?  801 TTP A O2B   1 
HETATM 15864 O  O3B   . TTP E 3 .   ? 148.956 144.765 136.267 1.00 28.38 ?  801 TTP A O3B   1 
HETATM 15865 P  PG    . TTP E 3 .   ? 150.291 145.232 135.501 1.00 32.16 ?  801 TTP A PG    1 
HETATM 15866 O  O1G   . TTP E 3 .   ? 149.948 145.740 134.122 1.00 33.52 ?  801 TTP A O1G   1 
HETATM 15867 O  O2G   . TTP E 3 .   ? 151.215 144.048 135.378 1.00 23.47 -1 801 TTP A O2G   1 
HETATM 15868 O  O3G   . TTP E 3 .   ? 150.980 146.323 136.281 1.00 34.78 ?  801 TTP A O3G   1 
HETATM 15869 O  "O5'" . TTP E 3 .   ? 146.179 142.965 133.917 1.00 18.77 ?  801 TTP A "O5'" 1 
HETATM 15870 C  "C5'" . TTP E 3 .   ? 147.099 142.576 132.904 1.00 25.04 ?  801 TTP A "C5'" 1 
HETATM 15871 C  "C4'" . TTP E 3 .   ? 146.913 141.107 132.569 1.00 26.93 ?  801 TTP A "C4'" 1 
HETATM 15872 O  "O4'" . TTP E 3 .   ? 146.615 140.371 133.754 1.00 30.38 ?  801 TTP A "O4'" 1 
HETATM 15873 C  "C3'" . TTP E 3 .   ? 145.746 140.913 131.621 1.00 25.75 ?  801 TTP A "C3'" 1 
HETATM 15874 O  "O3'" . TTP E 3 .   ? 146.221 140.584 130.313 1.00 30.86 ?  801 TTP A "O3'" 1 
HETATM 15875 C  "C2'" . TTP E 3 .   ? 144.950 139.757 132.186 1.00 28.56 ?  801 TTP A "C2'" 1 
HETATM 15876 C  "C1'" . TTP E 3 .   ? 145.642 139.363 133.482 1.00 25.58 ?  801 TTP A "C1'" 1 
HETATM 15877 N  N1    . TTP E 3 .   ? 144.668 139.300 134.570 1.00 26.58 ?  801 TTP A N1    1 
HETATM 15878 C  C2    . TTP E 3 .   ? 144.126 138.053 134.948 1.00 30.61 ?  801 TTP A C2    1 
HETATM 15879 O  O2    . TTP E 3 .   ? 144.493 137.021 134.348 1.00 27.38 ?  801 TTP A O2    1 
HETATM 15880 N  N3    . TTP E 3 .   ? 143.234 137.949 135.940 1.00 28.52 ?  801 TTP A N3    1 
HETATM 15881 C  C4    . TTP E 3 .   ? 142.827 139.036 136.598 1.00 31.97 ?  801 TTP A C4    1 
HETATM 15882 O  O4    . TTP E 3 .   ? 141.994 138.942 137.522 1.00 33.14 ?  801 TTP A O4    1 
HETATM 15883 C  C5    . TTP E 3 .   ? 143.378 140.357 136.218 1.00 26.42 ?  801 TTP A C5    1 
HETATM 15884 C  C5M   . TTP E 3 .   ? 142.946 141.604 136.937 1.00 26.94 ?  801 TTP A C5M   1 
HETATM 15885 C  C6    . TTP E 3 .   ? 144.302 140.426 135.187 1.00 25.12 ?  801 TTP A C6    1 
HETATM 15886 MG MG    . MG  F 4 .   ? 148.123 146.923 132.922 1.00 24.14 ?  802 MG  A MG    1 
HETATM 15887 P  PG    . ATP G 5 .   ? 108.480 131.902 78.418  1.00 73.57 ?  803 ATP A PG    1 
HETATM 15888 O  O1G   . ATP G 5 .   ? 108.906 132.810 77.315  1.00 63.77 ?  803 ATP A O1G   1 
HETATM 15889 O  O2G   . ATP G 5 .   ? 107.996 130.532 77.935  1.00 64.13 -1 803 ATP A O2G   1 
HETATM 15890 O  O3G   . ATP G 5 .   ? 109.549 131.705 79.498  1.00 61.47 ?  803 ATP A O3G   1 
HETATM 15891 P  PB    . ATP G 5 .   ? 106.906 133.344 80.522  1.00 71.75 ?  803 ATP A PB    1 
HETATM 15892 O  O1B   . ATP G 5 .   ? 107.673 134.605 80.582  1.00 63.94 -1 803 ATP A O1B   1 
HETATM 15893 O  O2B   . ATP G 5 .   ? 105.388 133.499 80.604  1.00 62.90 ?  803 ATP A O2B   1 
HETATM 15894 O  O3B   . ATP G 5 .   ? 107.228 132.518 79.202  1.00 66.82 ?  803 ATP A O3B   1 
HETATM 15895 P  PA    . ATP G 5 .   ? 106.637 131.222 82.574  1.00 70.68 ?  803 ATP A PA    1 
HETATM 15896 O  O1A   . ATP G 5 .   ? 107.328 129.920 82.488  1.00 64.00 -1 803 ATP A O1A   1 
HETATM 15897 O  O2A   . ATP G 5 .   ? 105.161 131.187 82.181  1.00 62.49 ?  803 ATP A O2A   1 
HETATM 15898 O  O3A   . ATP G 5 .   ? 107.345 132.323 81.663  1.00 63.22 ?  803 ATP A O3A   1 
HETATM 15899 O  "O5'" . ATP G 5 .   ? 106.751 131.846 84.020  1.00 62.47 ?  803 ATP A "O5'" 1 
HETATM 15900 C  "C5'" . ATP G 5 .   ? 105.839 132.873 84.464  1.00 61.67 ?  803 ATP A "C5'" 1 
HETATM 15901 C  "C4'" . ATP G 5 .   ? 106.530 133.730 85.493  1.00 61.88 ?  803 ATP A "C4'" 1 
HETATM 15902 O  "O4'" . ATP G 5 .   ? 107.059 132.893 86.544  1.00 63.84 ?  803 ATP A "O4'" 1 
HETATM 15903 C  "C3'" . ATP G 5 .   ? 107.723 134.526 84.981  1.00 60.84 ?  803 ATP A "C3'" 1 
HETATM 15904 O  "O3'" . ATP G 5 .   ? 107.309 135.777 84.442  1.00 63.01 ?  803 ATP A "O3'" 1 
HETATM 15905 C  "C2'" . ATP G 5 .   ? 108.558 134.711 86.248  1.00 62.28 ?  803 ATP A "C2'" 1 
HETATM 15906 O  "O2'" . ATP G 5 .   ? 108.087 135.800 87.034  1.00 61.13 ?  803 ATP A "O2'" 1 
HETATM 15907 C  "C1'" . ATP G 5 .   ? 108.319 133.383 86.972  1.00 61.93 ?  803 ATP A "C1'" 1 
HETATM 15908 N  N9    . ATP G 5 .   ? 109.327 132.364 86.700  1.00 60.22 ?  803 ATP A N9    1 
HETATM 15909 C  C8    . ATP G 5 .   ? 109.123 131.127 86.147  1.00 60.42 ?  803 ATP A C8    1 
HETATM 15910 N  N7    . ATP G 5 .   ? 110.214 130.412 86.017  1.00 60.85 ?  803 ATP A N7    1 
HETATM 15911 C  C5    . ATP G 5 .   ? 111.207 131.235 86.522  1.00 61.63 ?  803 ATP A C5    1 
HETATM 15912 C  C6    . ATP G 5 .   ? 112.597 131.067 86.673  1.00 58.03 ?  803 ATP A C6    1 
HETATM 15913 N  N6    . ATP G 5 .   ? 113.257 129.962 86.311  1.00 57.72 ?  803 ATP A N6    1 
HETATM 15914 N  N1    . ATP G 5 .   ? 113.298 132.085 87.217  1.00 58.44 ?  803 ATP A N1    1 
HETATM 15915 C  C2    . ATP G 5 .   ? 112.648 133.195 87.576  1.00 58.37 ?  803 ATP A C2    1 
HETATM 15916 N  N3    . ATP G 5 .   ? 111.345 133.465 87.487  1.00 61.94 ?  803 ATP A N3    1 
HETATM 15917 C  C4    . ATP G 5 .   ? 110.675 132.442 86.949  1.00 62.47 ?  803 ATP A C4    1 
HETATM 15918 O  O1B   . DGI H 6 .   ? 104.008 148.916 84.089  1.00 65.79 ?  804 DGI A O1B   1 
HETATM 15919 P  PB    . DGI H 6 .   ? 104.084 150.395 84.396  1.00 74.95 ?  804 DGI A PB    1 
HETATM 15920 O  O2B   . DGI H 6 .   ? 102.728 151.072 84.386  1.00 66.56 -1 804 DGI A O2B   1 
HETATM 15921 O  O3B   . DGI H 6 .   ? 105.109 151.124 83.553  1.00 66.82 ?  804 DGI A O3B   1 
HETATM 15922 O  O3A   . DGI H 6 .   ? 104.617 150.441 85.932  1.00 67.64 ?  804 DGI A O3A   1 
HETATM 15923 P  PA    . DGI H 6 .   ? 104.557 149.620 87.304  1.00 72.66 ?  804 DGI A PA    1 
HETATM 15924 O  O1A   . DGI H 6 .   ? 104.670 150.563 88.436  1.00 65.42 -1 804 DGI A O1A   1 
HETATM 15925 O  O2A   . DGI H 6 .   ? 103.409 148.684 87.254  1.00 66.08 ?  804 DGI A O2A   1 
HETATM 15926 O  "O5'" . DGI H 6 .   ? 105.916 148.788 87.228  1.00 64.30 ?  804 DGI A "O5'" 1 
HETATM 15927 C  "C5'" . DGI H 6 .   ? 107.154 149.463 86.924  1.00 63.95 ?  804 DGI A "C5'" 1 
HETATM 15928 C  "C4'" . DGI H 6 .   ? 108.306 148.532 87.205  1.00 63.55 ?  804 DGI A "C4'" 1 
HETATM 15929 O  "O4'" . DGI H 6 .   ? 108.265 148.113 88.588  1.00 62.06 ?  804 DGI A "O4'" 1 
HETATM 15930 C  "C3'" . DGI H 6 .   ? 108.326 147.253 86.360  1.00 64.87 ?  804 DGI A "C3'" 1 
HETATM 15931 O  "O3'" . DGI H 6 .   ? 109.632 147.028 85.830  1.00 62.86 ?  804 DGI A "O3'" 1 
HETATM 15932 C  "C2'" . DGI H 6 .   ? 107.954 146.160 87.355  1.00 62.93 ?  804 DGI A "C2'" 1 
HETATM 15933 C  "C1'" . DGI H 6 .   ? 108.482 146.720 88.661  1.00 59.66 ?  804 DGI A "C1'" 1 
HETATM 15934 N  N9    . DGI H 6 .   ? 107.794 146.209 89.862  1.00 62.34 ?  804 DGI A N9    1 
HETATM 15935 C  C8    . DGI H 6 .   ? 108.368 145.618 90.954  1.00 63.25 ?  804 DGI A C8    1 
HETATM 15936 N  N7    . DGI H 6 .   ? 107.497 145.250 91.862  1.00 62.94 ?  804 DGI A N7    1 
HETATM 15937 C  C5    . DGI H 6 .   ? 106.272 145.622 91.335  1.00 64.85 ?  804 DGI A C5    1 
HETATM 15938 C  C4    . DGI H 6 .   ? 106.439 146.215 90.102  1.00 64.28 ?  804 DGI A C4    1 
HETATM 15939 N  N3    . DGI H 6 .   ? 105.493 146.710 89.282  1.00 64.32 ?  804 DGI A N3    1 
HETATM 15940 C  C2    . DGI H 6 .   ? 104.266 146.580 89.778  1.00 62.71 ?  804 DGI A C2    1 
HETATM 15941 N  N2    . DGI H 6 .   ? 103.220 147.027 89.080  1.00 63.01 ?  804 DGI A N2    1 
HETATM 15942 N  N1    . DGI H 6 .   ? 104.000 146.005 90.991  1.00 63.42 ?  804 DGI A N1    1 
HETATM 15943 C  C6    . DGI H 6 .   ? 104.949 145.489 91.853  1.00 64.23 ?  804 DGI A C6    1 
HETATM 15944 O  O6    . DGI H 6 .   ? 104.616 144.986 92.925  1.00 64.17 ?  804 DGI A O6    1 
HETATM 15945 P  PA    . TTP I 3 .   ? 119.387 146.246 124.269 1.00 22.87 ?  801 TTP B PA    1 
HETATM 15946 O  O1A   . TTP I 3 .   ? 120.760 145.803 123.837 1.00 21.90 -1 801 TTP B O1A   1 
HETATM 15947 O  O2A   . TTP I 3 .   ? 119.424 147.652 124.811 1.00 27.07 ?  801 TTP B O2A   1 
HETATM 15948 O  O3A   . TTP I 3 .   ? 118.325 146.136 123.067 1.00 36.80 ?  801 TTP B O3A   1 
HETATM 15949 P  PB    . TTP I 3 .   ? 118.239 147.227 121.890 1.00 32.44 ?  801 TTP B PB    1 
HETATM 15950 O  O1B   . TTP I 3 .   ? 119.070 146.805 120.706 1.00 35.04 -1 801 TTP B O1B   1 
HETATM 15951 O  O2B   . TTP I 3 .   ? 118.643 148.601 122.355 1.00 28.12 ?  801 TTP B O2B   1 
HETATM 15952 O  O3B   . TTP I 3 .   ? 116.676 147.189 121.526 1.00 37.21 ?  801 TTP B O3B   1 
HETATM 15953 P  PG    . TTP I 3 .   ? 115.577 147.432 122.677 1.00 30.08 ?  801 TTP B PG    1 
HETATM 15954 O  O1G   . TTP I 3 .   ? 115.152 146.097 123.229 1.00 20.36 ?  801 TTP B O1G   1 
HETATM 15955 O  O2G   . TTP I 3 .   ? 114.368 148.125 122.103 1.00 33.83 -1 801 TTP B O2G   1 
HETATM 15956 O  O3G   . TTP I 3 .   ? 116.171 148.268 123.784 1.00 27.09 ?  801 TTP B O3G   1 
HETATM 15957 O  "O5'" . TTP I 3 .   ? 118.767 145.236 125.352 1.00 24.10 ?  801 TTP B "O5'" 1 
HETATM 15958 C  "C5'" . TTP I 3 .   ? 118.053 144.085 124.914 1.00 22.09 ?  801 TTP B "C5'" 1 
HETATM 15959 C  "C4'" . TTP I 3 .   ? 117.991 143.070 126.043 1.00 23.21 ?  801 TTP B "C4'" 1 
HETATM 15960 O  "O4'" . TTP I 3 .   ? 118.095 141.770 125.465 1.00 35.77 ?  801 TTP B "O4'" 1 
HETATM 15961 C  "C3'" . TTP I 3 .   ? 119.156 143.251 126.996 1.00 25.49 ?  801 TTP B "C3'" 1 
HETATM 15962 O  "O3'" . TTP I 3 .   ? 118.675 143.384 128.335 1.00 27.76 ?  801 TTP B "O3'" 1 
HETATM 15963 C  "C2'" . TTP I 3 .   ? 119.996 141.999 126.881 1.00 25.02 ?  801 TTP B "C2'" 1 
HETATM 15964 C  "C1'" . TTP I 3 .   ? 119.216 141.053 125.983 1.00 28.60 ?  801 TTP B "C1'" 1 
HETATM 15965 N  N1    . TTP I 3 .   ? 120.053 140.603 124.872 1.00 27.06 ?  801 TTP B N1    1 
HETATM 15966 C  C2    . TTP I 3 .   ? 120.227 139.221 124.641 1.00 29.68 ?  801 TTP B C2    1 
HETATM 15967 O  O2    . TTP I 3 .   ? 119.662 138.399 125.392 1.00 27.86 ?  801 TTP B O2    1 
HETATM 15968 N  N3    . TTP I 3 .   ? 120.985 138.773 123.633 1.00 27.67 ?  801 TTP B N3    1 
HETATM 15969 C  C4    . TTP I 3 .   ? 121.599 139.631 122.815 1.00 32.29 ?  801 TTP B C4    1 
HETATM 15970 O  O4    . TTP I 3 .   ? 122.305 139.212 121.875 1.00 35.26 ?  801 TTP B O4    1 
HETATM 15971 C  C5    . TTP I 3 .   ? 121.431 141.086 123.038 1.00 27.29 ?  801 TTP B C5    1 
HETATM 15972 C  C5M   . TTP I 3 .   ? 122.106 142.085 122.138 1.00 27.10 ?  801 TTP B C5M   1 
HETATM 15973 C  C6    . TTP I 3 .   ? 120.640 141.512 124.089 1.00 25.61 ?  801 TTP B C6    1 
HETATM 15974 MG MG    . MG  J 4 .   ? 117.570 149.041 125.153 1.00 27.32 ?  802 MG  B MG    1 
HETATM 15975 P  PG    . ATP K 5 .   ? 155.724 139.548 179.254 1.00 78.28 ?  803 ATP B PG    1 
HETATM 15976 O  O1G   . ATP K 5 .   ? 155.506 140.062 180.637 1.00 64.48 ?  803 ATP B O1G   1 
HETATM 15977 O  O2G   . ATP K 5 .   ? 154.429 139.360 178.458 1.00 66.98 -1 803 ATP B O2G   1 
HETATM 15978 O  O3G   . ATP K 5 .   ? 156.699 140.394 178.429 1.00 64.37 ?  803 ATP B O3G   1 
HETATM 15979 P  PB    . ATP K 5 .   ? 157.769 137.401 179.654 1.00 74.62 ?  803 ATP B PB    1 
HETATM 15980 O  O1B   . ATP K 5 .   ? 158.881 137.933 178.843 1.00 63.94 -1 803 ATP B O1B   1 
HETATM 15981 O  O2B   . ATP K 5 .   ? 157.941 137.501 181.169 1.00 65.48 ?  803 ATP B O2B   1 
HETATM 15982 O  O3B   . ATP K 5 .   ? 156.387 138.095 179.292 1.00 67.90 ?  803 ATP B O3B   1 
HETATM 15983 P  PA    . ATP K 5 .   ? 156.718 135.073 178.162 1.00 74.99 ?  803 ATP B PA    1 
HETATM 15984 O  O1A   . ATP K 5 .   ? 155.388 134.610 178.606 1.00 65.28 -1 803 ATP B O1A   1 
HETATM 15985 O  O2A   . ATP K 5 .   ? 157.668 133.969 177.701 1.00 66.62 ?  803 ATP B O2A   1 
HETATM 15986 O  O3A   . ATP K 5 .   ? 157.462 135.877 179.314 1.00 66.93 ?  803 ATP B O3A   1 
HETATM 15987 O  "O5'" . ATP K 5 .   ? 156.598 136.140 177.005 1.00 63.34 ?  803 ATP B "O5'" 1 
HETATM 15988 C  "C5'" . ATP K 5 .   ? 157.625 136.274 176.001 1.00 62.23 ?  803 ATP B "C5'" 1 
HETATM 15989 C  "C4'" . ATP K 5 .   ? 157.106 137.144 174.886 1.00 64.37 ?  803 ATP B "C4'" 1 
HETATM 15990 O  "O4'" . ATP K 5 .   ? 156.361 136.337 173.949 1.00 66.78 ?  803 ATP B "O4'" 1 
HETATM 15991 C  "C3'" . ATP K 5 .   ? 156.144 138.246 175.313 1.00 61.93 ?  803 ATP B "C3'" 1 
HETATM 15992 O  "O3'" . ATP K 5 .   ? 156.849 139.420 175.695 1.00 65.20 ?  803 ATP B "O3'" 1 
HETATM 15993 C  "C2'" . ATP K 5 .   ? 155.323 138.472 174.043 1.00 61.89 ?  803 ATP B "C2'" 1 
HETATM 15994 O  "O2'" . ATP K 5 .   ? 155.992 139.332 173.129 1.00 64.23 ?  803 ATP B "O2'" 1 
HETATM 15995 C  "C1'" . ATP K 5 .   ? 155.232 137.053 173.474 1.00 63.64 ?  803 ATP B "C1'" 1 
HETATM 15996 N  N9    . ATP K 5 .   ? 154.028 136.327 173.861 1.00 61.39 ?  803 ATP B N9    1 
HETATM 15997 C  C8    . ATP K 5 .   ? 153.953 135.172 174.596 1.00 60.31 ?  803 ATP B C8    1 
HETATM 15998 N  N7    . ATP K 5 .   ? 152.731 134.737 174.789 1.00 61.85 ?  803 ATP B N7    1 
HETATM 15999 C  C5    . ATP K 5 .   ? 151.944 135.671 174.133 1.00 64.90 ?  803 ATP B C5    1 
HETATM 16000 C  C6    . ATP K 5 .   ? 150.552 135.788 173.959 1.00 60.15 ?  803 ATP B C6    1 
HETATM 16001 N  N6    . ATP K 5 .   ? 149.664 134.920 174.455 1.00 59.38 ?  803 ATP B N6    1 
HETATM 16002 N  N1    . ATP K 5 .   ? 150.093 136.840 173.249 1.00 59.56 ?  803 ATP B N1    1 
HETATM 16003 C  C2    . ATP K 5 .   ? 150.972 137.714 172.754 1.00 58.45 ?  803 ATP B C2    1 
HETATM 16004 N  N3    . ATP K 5 .   ? 152.303 137.707 172.850 1.00 61.55 ?  803 ATP B N3    1 
HETATM 16005 C  C4    . ATP K 5 .   ? 152.730 136.656 173.555 1.00 64.32 ?  803 ATP B C4    1 
HETATM 16006 O  O1B   . DGI L 6 .   ? 162.598 154.780 173.057 1.00 62.73 -1 804 DGI B O1B   1 
HETATM 16007 P  PB    . DGI L 6 .   ? 162.878 153.311 172.808 1.00 78.16 ?  804 DGI B PB    1 
HETATM 16008 O  O2B   . DGI L 6 .   ? 164.327 153.032 172.480 1.00 66.34 ?  804 DGI B O2B   1 
HETATM 16009 O  O3B   . DGI L 6 .   ? 162.335 152.418 173.903 1.00 63.38 ?  804 DGI B O3B   1 
HETATM 16010 O  O3A   . DGI L 6 .   ? 162.089 152.907 171.442 1.00 65.58 ?  804 DGI B O3A   1 
HETATM 16011 P  PA    . DGI L 6 .   ? 162.133 151.861 170.233 1.00 72.25 ?  804 DGI B PA    1 
HETATM 16012 O  O1A   . DGI L 6 .   ? 163.036 150.745 170.601 1.00 65.11 ?  804 DGI B O1A   1 
HETATM 16013 O  O2A   . DGI L 6 .   ? 162.368 152.594 168.972 1.00 63.88 -1 804 DGI B O2A   1 
HETATM 16014 O  "O5'" . DGI L 6 .   ? 160.626 151.336 170.217 1.00 64.69 ?  804 DGI B "O5'" 1 
HETATM 16015 C  "C5'" . DGI L 6 .   ? 159.538 152.282 170.258 1.00 61.37 ?  804 DGI B "C5'" 1 
HETATM 16016 C  "C4'" . DGI L 6 .   ? 158.230 151.538 170.156 1.00 62.25 ?  804 DGI B "C4'" 1 
HETATM 16017 O  "O4'" . DGI L 6 .   ? 158.178 150.817 168.905 1.00 62.79 ?  804 DGI B "O4'" 1 
HETATM 16018 C  "C3'" . DGI L 6 .   ? 157.977 150.514 171.267 1.00 63.26 ?  804 DGI B "C3'" 1 
HETATM 16019 O  "O3'" . DGI L 6 .   ? 156.664 150.675 171.802 1.00 62.44 ?  804 DGI B "O3'" 1 
HETATM 16020 C  "C2'" . DGI L 6 .   ? 158.109 149.172 170.555 1.00 58.79 ?  804 DGI B "C2'" 1 
HETATM 16021 C  "C1'" . DGI L 6 .   ? 157.689 149.515 169.139 1.00 58.08 ?  804 DGI B "C1'" 1 
HETATM 16022 N  N9    . DGI L 6 .   ? 158.247 148.621 168.105 1.00 59.64 ?  804 DGI B N9    1 
HETATM 16023 C  C8    . DGI L 6 .   ? 157.553 147.953 167.133 1.00 62.54 ?  804 DGI B C8    1 
HETATM 16024 N  N7    . DGI L 6 .   ? 158.319 147.228 166.353 1.00 61.46 ?  804 DGI B N7    1 
HETATM 16025 C  C5    . DGI L 6 .   ? 159.598 147.431 166.843 1.00 64.08 ?  804 DGI B C5    1 
HETATM 16026 C  C4    . DGI L 6 .   ? 159.569 148.288 167.922 1.00 62.76 ?  804 DGI B C4    1 
HETATM 16027 N  N3    . DGI L 6 .   ? 160.605 148.725 168.665 1.00 63.02 ?  804 DGI B N3    1 
HETATM 16028 C  C2    . DGI L 6 .   ? 161.772 148.231 168.258 1.00 61.32 ?  804 DGI B C2    1 
HETATM 16029 N  N2    . DGI L 6 .   ? 162.892 148.569 168.902 1.00 62.38 ?  804 DGI B N2    1 
HETATM 16030 N  N1    . DGI L 6 .   ? 161.899 147.374 167.198 1.00 60.59 ?  804 DGI B N1    1 
HETATM 16031 C  C6    . DGI L 6 .   ? 160.857 146.911 166.419 1.00 62.82 ?  804 DGI B C6    1 
HETATM 16032 O  O6    . DGI L 6 .   ? 161.068 146.141 165.482 1.00 61.55 ?  804 DGI B O6    1 
HETATM 16033 MN MN    . MN  M 7 .   ? 117.111 93.364  121.975 0.85 25.05 ?  401 MN  C MN    1 
HETATM 16034 MN MN    . MN  N 7 .   ? 115.659 96.580  123.203 0.85 26.37 ?  402 MN  C MN    1 
HETATM 16035 MN MN    . MN  O 7 .   ? 135.220 97.860  137.252 1.00 22.51 ?  401 MN  D MN    1 
HETATM 16036 MN MN    . MN  P 7 .   ? 137.560 96.844  134.288 1.00 24.72 ?  402 MN  D MN    1 
# 
